data_9I2S
# 
_entry.id   9I2S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9I2S         pdb_00009i2s 10.2210/pdb9i2s/pdb 
WWPDB D_1292144857 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9I2S 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rficner@gwdg.de 
_pdbx_contact_author.name_first         Ficner 
_pdbx_contact_author.name_last          Ficner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1739-6086 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Neumann, P.' 1 0000-0003-0129-8112 
'Ficner, R.'  2 0000-0002-1739-6086 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? ?  ? ? primary 'To Be Published'                                ?      0353 ?         ? ? ?  ? ?   ?   
'Velvet domain of the transcriptional regulator VeA'                                                         ?    ? ? ?        ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861 877 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix' 2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Neumann, P.'       1  0000-0003-0129-8112 
primary 'Ficner, R.'        2  0000-0002-1739-6086 
1       'Liebschner, D.'    3  0000-0003-3921-3209 
1       'Afonine, P.V.'     4  0000-0002-5052-991X 
1       'Baker, M.L.'       5  ?                   
1       'Bunkoczi, G.'      6  ?                   
1       'Chen, V.B.'        7  0000-0003-2492-979X 
1       'Croll, T.I.'       8  ?                   
1       'Hintze, B.'        9  0000-0002-4871-2096 
1       'Hung, L.W.'        10 0000-0001-6690-8458 
1       'Jain, S.'          11 ?                   
1       'McCoy, A.J.'       12 ?                   
1       'Moriarty, N.W.'    13 0000-0001-8857-9464 
1       'Oeffner, R.D.'     14 0000-0003-3107-2202 
1       'Poon, B.K.'        15 0000-0001-9633-6067 
1       'Prisant, M.G.'     16 ?                   
1       'Read, R.J.'        17 0000-0001-8273-0047 
1       'Richardson, J.S.'  18 0000-0002-3311-2944 
1       'Richardson, D.C.'  19 ?                   
1       'Sammito, M.D.'     20 0000-0002-8346-9247 
1       'Sobolev, O.V.'     21 0000-0002-0623-3214 
1       'Stockwell, D.H.'   22 ?                   
1       'Terwilliger, T.C.' 23 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  24 ?                   
1       'Videau, L.L.'      25 ?                   
1       'Williams, C.J.'    26 ?                   
1       'Adams, P.D.'       27 0000-0001-9333-8219 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Developmental and secondary metabolism regulator veA' 24714.033 4  ? ? ? 'Velvet domain residues 1 to 224' 
2 water   nat water                                                  18.015    44 ? ? ? ?                                 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Velvet complex subunit A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNK
TDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQI
KDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNK
TDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQI
KDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQG
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LEU n 
1 5   ALA n 
1 6   ALA n 
1 7   PRO n 
1 8   PRO n 
1 9   PRO n 
1 10  PRO n 
1 11  LEU n 
1 12  GLY n 
1 13  GLU n 
1 14  SER n 
1 15  GLY n 
1 16  ASN n 
1 17  SER n 
1 18  ASN n 
1 19  SER n 
1 20  VAL n 
1 21  SER n 
1 22  ARG n 
1 23  ILE n 
1 24  THR n 
1 25  ARG n 
1 26  GLU n 
1 27  GLY n 
1 28  LYS n 
1 29  LYS n 
1 30  ILE n 
1 31  THR n 
1 32  TYR n 
1 33  LYS n 
1 34  LEU n 
1 35  ASN n 
1 36  ILE n 
1 37  MET n 
1 38  GLN n 
1 39  GLN n 
1 40  PRO n 
1 41  LYS n 
1 42  ARG n 
1 43  ALA n 
1 44  ARG n 
1 45  ALA n 
1 46  CYS n 
1 47  GLY n 
1 48  GLN n 
1 49  GLY n 
1 50  SER n 
1 51  LYS n 
1 52  SER n 
1 53  HIS n 
1 54  THR n 
1 55  ASP n 
1 56  ARG n 
1 57  ARG n 
1 58  PRO n 
1 59  VAL n 
1 60  ASP n 
1 61  PRO n 
1 62  PRO n 
1 63  PRO n 
1 64  VAL n 
1 65  ILE n 
1 66  GLU n 
1 67  LEU n 
1 68  ASN n 
1 69  ILE n 
1 70  PHE n 
1 71  GLU n 
1 72  SER n 
1 73  ASP n 
1 74  PRO n 
1 75  HIS n 
1 76  ASP n 
1 77  ASP n 
1 78  SER n 
1 79  ASN n 
1 80  LYS n 
1 81  THR n 
1 82  ASP n 
1 83  ILE n 
1 84  THR n 
1 85  PHE n 
1 86  VAL n 
1 87  TYR n 
1 88  ASN n 
1 89  ALA n 
1 90  ASN n 
1 91  PHE n 
1 92  PHE n 
1 93  LEU n 
1 94  PHE n 
1 95  ALA n 
1 96  THR n 
1 97  LEU n 
1 98  GLU n 
1 99  PRO n 
1 100 GLU n 
1 101 ARG n 
1 102 PRO n 
1 103 ILE n 
1 104 ALA n 
1 105 THR n 
1 106 GLY n 
1 107 LYS n 
1 108 LEU n 
1 109 MET n 
1 110 THR n 
1 111 ASN n 
1 112 GLN n 
1 113 GLY n 
1 114 SER n 
1 115 PRO n 
1 116 VAL n 
1 117 LEU n 
1 118 THR n 
1 119 GLY n 
1 120 VAL n 
1 121 PRO n 
1 122 VAL n 
1 123 ALA n 
1 124 GLY n 
1 125 VAL n 
1 126 ALA n 
1 127 TYR n 
1 128 LEU n 
1 129 ASP n 
1 130 LYS n 
1 131 PRO n 
1 132 ASN n 
1 133 ARG n 
1 134 ALA n 
1 135 GLY n 
1 136 TYR n 
1 137 PHE n 
1 138 ILE n 
1 139 PHE n 
1 140 PRO n 
1 141 ASP n 
1 142 LEU n 
1 143 SER n 
1 144 VAL n 
1 145 ARG n 
1 146 ASN n 
1 147 GLU n 
1 148 GLY n 
1 149 SER n 
1 150 TYR n 
1 151 ARG n 
1 152 PHE n 
1 153 SER n 
1 154 PHE n 
1 155 HIS n 
1 156 LEU n 
1 157 PHE n 
1 158 GLU n 
1 159 GLN n 
1 160 ILE n 
1 161 LYS n 
1 162 ASP n 
1 163 PRO n 
1 164 LYS n 
1 165 ASP n 
1 166 ALA n 
1 167 THR n 
1 168 GLU n 
1 169 GLY n 
1 170 THR n 
1 171 GLN n 
1 172 PRO n 
1 173 MET n 
1 174 PRO n 
1 175 SER n 
1 176 PRO n 
1 177 VAL n 
1 178 PRO n 
1 179 GLY n 
1 180 LYS n 
1 181 LEU n 
1 182 SER n 
1 183 SER n 
1 184 PRO n 
1 185 GLN n 
1 186 GLU n 
1 187 PHE n 
1 188 LEU n 
1 189 GLU n 
1 190 PHE n 
1 191 ARG n 
1 192 LEU n 
1 193 GLU n 
1 194 VAL n 
1 195 ILE n 
1 196 SER n 
1 197 ASN n 
1 198 PRO n 
1 199 PHE n 
1 200 ILE n 
1 201 VAL n 
1 202 TYR n 
1 203 SER n 
1 204 ALA n 
1 205 LYS n 
1 206 LYS n 
1 207 PHE n 
1 208 PRO n 
1 209 GLY n 
1 210 LEU n 
1 211 THR n 
1 212 THR n 
1 213 SER n 
1 214 THR n 
1 215 PRO n 
1 216 ILE n 
1 217 SER n 
1 218 ARG n 
1 219 MET n 
1 220 ILE n 
1 221 ALA n 
1 222 GLU n 
1 223 GLN n 
1 224 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   224 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'veA, ANIA_01052' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aspergillus nidulans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     162425 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   PRO 8   8   ?   ?   ?   A . n 
A 1 9   PRO 9   9   ?   ?   ?   A . n 
A 1 10  PRO 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  GLY 12  12  ?   ?   ?   A . n 
A 1 13  GLU 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  MET 37  37  37  MET MET A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  HIS 75  75  75  HIS HIS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 PRO 102 102 ?   ?   ?   A . n 
A 1 103 ILE 103 103 ?   ?   ?   A . n 
A 1 104 ALA 104 104 ?   ?   ?   A . n 
A 1 105 THR 105 105 ?   ?   ?   A . n 
A 1 106 GLY 106 106 ?   ?   ?   A . n 
A 1 107 LYS 107 107 ?   ?   ?   A . n 
A 1 108 LEU 108 108 ?   ?   ?   A . n 
A 1 109 MET 109 109 ?   ?   ?   A . n 
A 1 110 THR 110 110 ?   ?   ?   A . n 
A 1 111 ASN 111 111 ?   ?   ?   A . n 
A 1 112 GLN 112 112 ?   ?   ?   A . n 
A 1 113 GLY 113 113 ?   ?   ?   A . n 
A 1 114 SER 114 114 ?   ?   ?   A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 GLU 168 168 ?   ?   ?   A . n 
A 1 169 GLY 169 169 ?   ?   ?   A . n 
A 1 170 THR 170 170 ?   ?   ?   A . n 
A 1 171 GLN 171 171 ?   ?   ?   A . n 
A 1 172 PRO 172 172 ?   ?   ?   A . n 
A 1 173 MET 173 173 ?   ?   ?   A . n 
A 1 174 PRO 174 174 ?   ?   ?   A . n 
A 1 175 SER 175 175 ?   ?   ?   A . n 
A 1 176 PRO 176 176 ?   ?   ?   A . n 
A 1 177 VAL 177 177 ?   ?   ?   A . n 
A 1 178 PRO 178 178 ?   ?   ?   A . n 
A 1 179 GLY 179 179 ?   ?   ?   A . n 
A 1 180 LYS 180 180 ?   ?   ?   A . n 
A 1 181 LEU 181 181 ?   ?   ?   A . n 
A 1 182 SER 182 182 ?   ?   ?   A . n 
A 1 183 SER 183 183 ?   ?   ?   A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 SER 213 213 ?   ?   ?   A . n 
A 1 214 THR 214 214 ?   ?   ?   A . n 
A 1 215 PRO 215 215 ?   ?   ?   A . n 
A 1 216 ILE 216 216 ?   ?   ?   A . n 
A 1 217 SER 217 217 ?   ?   ?   A . n 
A 1 218 ARG 218 218 ?   ?   ?   A . n 
A 1 219 MET 219 219 ?   ?   ?   A . n 
A 1 220 ILE 220 220 ?   ?   ?   A . n 
A 1 221 ALA 221 221 ?   ?   ?   A . n 
A 1 222 GLU 222 222 ?   ?   ?   A . n 
A 1 223 GLN 223 223 ?   ?   ?   A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   LEU 4   4   ?   ?   ?   B . n 
B 1 5   ALA 5   5   ?   ?   ?   B . n 
B 1 6   ALA 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   ?   ?   ?   B . n 
B 1 8   PRO 8   8   ?   ?   ?   B . n 
B 1 9   PRO 9   9   ?   ?   ?   B . n 
B 1 10  PRO 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  GLY 12  12  ?   ?   ?   B . n 
B 1 13  GLU 13  13  ?   ?   ?   B . n 
B 1 14  SER 14  14  ?   ?   ?   B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  THR 31  31  31  THR THR B . n 
B 1 32  TYR 32  32  32  TYR TYR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  MET 37  37  37  MET MET B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLN 39  39  39  GLN GLN B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  ARG 42  42  42  ARG ARG B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  CYS 46  46  46  CYS CYS B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  GLY 49  49  ?   ?   ?   B . n 
B 1 50  SER 50  50  ?   ?   ?   B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  HIS 53  53  53  HIS HIS B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ASP 55  55  55  ASP ASP B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  ASP 60  60  60  ASP ASP B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  HIS 75  75  75  HIS HIS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  SER 78  78  78  SER SER B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  PHE 85  85  85  PHE PHE B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ARG 101 101 101 ARG ARG B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 ILE 103 103 ?   ?   ?   B . n 
B 1 104 ALA 104 104 ?   ?   ?   B . n 
B 1 105 THR 105 105 ?   ?   ?   B . n 
B 1 106 GLY 106 106 ?   ?   ?   B . n 
B 1 107 LYS 107 107 ?   ?   ?   B . n 
B 1 108 LEU 108 108 ?   ?   ?   B . n 
B 1 109 MET 109 109 ?   ?   ?   B . n 
B 1 110 THR 110 110 ?   ?   ?   B . n 
B 1 111 ASN 111 111 ?   ?   ?   B . n 
B 1 112 GLN 112 112 ?   ?   ?   B . n 
B 1 113 GLY 113 113 ?   ?   ?   B . n 
B 1 114 SER 114 114 114 SER SER B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 VAL 116 116 116 VAL VAL B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 TYR 127 127 127 TYR TYR B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LYS 130 130 130 LYS LYS B . n 
B 1 131 PRO 131 131 131 PRO PRO B . n 
B 1 132 ASN 132 132 132 ASN ASN B . n 
B 1 133 ARG 133 133 133 ARG ARG B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 TYR 136 136 136 TYR TYR B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 PHE 139 139 139 PHE PHE B . n 
B 1 140 PRO 140 140 140 PRO PRO B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 SER 143 143 143 SER SER B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ARG 145 145 145 ARG ARG B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 GLY 148 148 148 GLY GLY B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 ARG 151 151 151 ARG ARG B . n 
B 1 152 PHE 152 152 152 PHE PHE B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 PHE 154 154 154 PHE PHE B . n 
B 1 155 HIS 155 155 155 HIS HIS B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 PHE 157 157 157 PHE PHE B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 LYS 161 161 161 LYS LYS B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 PRO 163 163 163 PRO PRO B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 ASP 165 165 165 ASP ASP B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 THR 167 167 167 THR THR B . n 
B 1 168 GLU 168 168 ?   ?   ?   B . n 
B 1 169 GLY 169 169 ?   ?   ?   B . n 
B 1 170 THR 170 170 ?   ?   ?   B . n 
B 1 171 GLN 171 171 ?   ?   ?   B . n 
B 1 172 PRO 172 172 ?   ?   ?   B . n 
B 1 173 MET 173 173 ?   ?   ?   B . n 
B 1 174 PRO 174 174 ?   ?   ?   B . n 
B 1 175 SER 175 175 ?   ?   ?   B . n 
B 1 176 PRO 176 176 ?   ?   ?   B . n 
B 1 177 VAL 177 177 ?   ?   ?   B . n 
B 1 178 PRO 178 178 ?   ?   ?   B . n 
B 1 179 GLY 179 179 ?   ?   ?   B . n 
B 1 180 LYS 180 180 ?   ?   ?   B . n 
B 1 181 LEU 181 181 ?   ?   ?   B . n 
B 1 182 SER 182 182 ?   ?   ?   B . n 
B 1 183 SER 183 183 ?   ?   ?   B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 PHE 187 187 187 PHE PHE B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 PHE 190 190 190 PHE PHE B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 GLU 193 193 193 GLU GLU B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 ILE 195 195 195 ILE ILE B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 TYR 202 202 202 TYR TYR B . n 
B 1 203 SER 203 203 203 SER SER B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LYS 206 206 206 LYS LYS B . n 
B 1 207 PHE 207 207 207 PHE PHE B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 THR 211 211 211 THR THR B . n 
B 1 212 THR 212 212 212 THR THR B . n 
B 1 213 SER 213 213 ?   ?   ?   B . n 
B 1 214 THR 214 214 ?   ?   ?   B . n 
B 1 215 PRO 215 215 ?   ?   ?   B . n 
B 1 216 ILE 216 216 ?   ?   ?   B . n 
B 1 217 SER 217 217 ?   ?   ?   B . n 
B 1 218 ARG 218 218 ?   ?   ?   B . n 
B 1 219 MET 219 219 ?   ?   ?   B . n 
B 1 220 ILE 220 220 ?   ?   ?   B . n 
B 1 221 ALA 221 221 ?   ?   ?   B . n 
B 1 222 GLU 222 222 ?   ?   ?   B . n 
B 1 223 GLN 223 223 ?   ?   ?   B . n 
B 1 224 GLY 224 224 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   ?   ?   ?   C . n 
C 1 3   THR 3   3   ?   ?   ?   C . n 
C 1 4   LEU 4   4   ?   ?   ?   C . n 
C 1 5   ALA 5   5   ?   ?   ?   C . n 
C 1 6   ALA 6   6   ?   ?   ?   C . n 
C 1 7   PRO 7   7   ?   ?   ?   C . n 
C 1 8   PRO 8   8   ?   ?   ?   C . n 
C 1 9   PRO 9   9   ?   ?   ?   C . n 
C 1 10  PRO 10  10  ?   ?   ?   C . n 
C 1 11  LEU 11  11  ?   ?   ?   C . n 
C 1 12  GLY 12  12  ?   ?   ?   C . n 
C 1 13  GLU 13  13  ?   ?   ?   C . n 
C 1 14  SER 14  14  ?   ?   ?   C . n 
C 1 15  GLY 15  15  15  GLY GLY C . n 
C 1 16  ASN 16  16  16  ASN ASN C . n 
C 1 17  SER 17  17  17  SER SER C . n 
C 1 18  ASN 18  18  18  ASN ASN C . n 
C 1 19  SER 19  19  19  SER SER C . n 
C 1 20  VAL 20  20  20  VAL VAL C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  ARG 22  22  22  ARG ARG C . n 
C 1 23  ILE 23  23  23  ILE ILE C . n 
C 1 24  THR 24  24  24  THR THR C . n 
C 1 25  ARG 25  25  25  ARG ARG C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  LYS 28  28  28  LYS LYS C . n 
C 1 29  LYS 29  29  29  LYS LYS C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  THR 31  31  31  THR THR C . n 
C 1 32  TYR 32  32  32  TYR TYR C . n 
C 1 33  LYS 33  33  33  LYS LYS C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  ASN 35  35  35  ASN ASN C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  MET 37  37  37  MET MET C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  GLN 39  39  39  GLN GLN C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  LYS 41  41  41  LYS LYS C . n 
C 1 42  ARG 42  42  42  ARG ARG C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  ARG 44  44  44  ARG ARG C . n 
C 1 45  ALA 45  45  45  ALA ALA C . n 
C 1 46  CYS 46  46  46  CYS CYS C . n 
C 1 47  GLY 47  47  47  GLY GLY C . n 
C 1 48  GLN 48  48  48  GLN GLN C . n 
C 1 49  GLY 49  49  49  GLY GLY C . n 
C 1 50  SER 50  50  50  SER SER C . n 
C 1 51  LYS 51  51  51  LYS LYS C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  HIS 53  53  53  HIS HIS C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ASP 55  55  55  ASP ASP C . n 
C 1 56  ARG 56  56  56  ARG ARG C . n 
C 1 57  ARG 57  57  57  ARG ARG C . n 
C 1 58  PRO 58  58  58  PRO PRO C . n 
C 1 59  VAL 59  59  59  VAL VAL C . n 
C 1 60  ASP 60  60  60  ASP ASP C . n 
C 1 61  PRO 61  61  61  PRO PRO C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  PRO 63  63  63  PRO PRO C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  ILE 65  65  65  ILE ILE C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  ASN 68  68  68  ASN ASN C . n 
C 1 69  ILE 69  69  69  ILE ILE C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  GLU 71  71  71  GLU GLU C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  ASP 73  73  73  ASP ASP C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  HIS 75  75  75  HIS HIS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  ASP 77  77  77  ASP ASP C . n 
C 1 78  SER 78  78  78  SER SER C . n 
C 1 79  ASN 79  79  79  ASN ASN C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  THR 81  81  81  THR THR C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  ILE 83  83  83  ILE ILE C . n 
C 1 84  THR 84  84  84  THR THR C . n 
C 1 85  PHE 85  85  85  PHE PHE C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  TYR 87  87  87  TYR TYR C . n 
C 1 88  ASN 88  88  88  ASN ASN C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  PHE 91  91  91  PHE PHE C . n 
C 1 92  PHE 92  92  92  PHE PHE C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  PHE 94  94  94  PHE PHE C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  THR 96  96  96  THR THR C . n 
C 1 97  LEU 97  97  97  LEU LEU C . n 
C 1 98  GLU 98  98  98  GLU GLU C . n 
C 1 99  PRO 99  99  99  PRO PRO C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ARG 101 101 101 ARG ARG C . n 
C 1 102 PRO 102 102 102 PRO PRO C . n 
C 1 103 ILE 103 103 103 ILE ILE C . n 
C 1 104 ALA 104 104 ?   ?   ?   C . n 
C 1 105 THR 105 105 ?   ?   ?   C . n 
C 1 106 GLY 106 106 ?   ?   ?   C . n 
C 1 107 LYS 107 107 ?   ?   ?   C . n 
C 1 108 LEU 108 108 ?   ?   ?   C . n 
C 1 109 MET 109 109 ?   ?   ?   C . n 
C 1 110 THR 110 110 ?   ?   ?   C . n 
C 1 111 ASN 111 111 ?   ?   ?   C . n 
C 1 112 GLN 112 112 ?   ?   ?   C . n 
C 1 113 GLY 113 113 113 GLY GLY C . n 
C 1 114 SER 114 114 114 SER SER C . n 
C 1 115 PRO 115 115 115 PRO PRO C . n 
C 1 116 VAL 116 116 116 VAL VAL C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 THR 118 118 118 THR THR C . n 
C 1 119 GLY 119 119 119 GLY GLY C . n 
C 1 120 VAL 120 120 120 VAL VAL C . n 
C 1 121 PRO 121 121 121 PRO PRO C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 GLY 124 124 124 GLY GLY C . n 
C 1 125 VAL 125 125 125 VAL VAL C . n 
C 1 126 ALA 126 126 126 ALA ALA C . n 
C 1 127 TYR 127 127 127 TYR TYR C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 ASP 129 129 129 ASP ASP C . n 
C 1 130 LYS 130 130 130 LYS LYS C . n 
C 1 131 PRO 131 131 131 PRO PRO C . n 
C 1 132 ASN 132 132 132 ASN ASN C . n 
C 1 133 ARG 133 133 133 ARG ARG C . n 
C 1 134 ALA 134 134 134 ALA ALA C . n 
C 1 135 GLY 135 135 135 GLY GLY C . n 
C 1 136 TYR 136 136 136 TYR TYR C . n 
C 1 137 PHE 137 137 137 PHE PHE C . n 
C 1 138 ILE 138 138 138 ILE ILE C . n 
C 1 139 PHE 139 139 139 PHE PHE C . n 
C 1 140 PRO 140 140 140 PRO PRO C . n 
C 1 141 ASP 141 141 141 ASP ASP C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 SER 143 143 143 SER SER C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 ARG 145 145 145 ARG ARG C . n 
C 1 146 ASN 146 146 146 ASN ASN C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 GLY 148 148 148 GLY GLY C . n 
C 1 149 SER 149 149 149 SER SER C . n 
C 1 150 TYR 150 150 150 TYR TYR C . n 
C 1 151 ARG 151 151 151 ARG ARG C . n 
C 1 152 PHE 152 152 152 PHE PHE C . n 
C 1 153 SER 153 153 153 SER SER C . n 
C 1 154 PHE 154 154 154 PHE PHE C . n 
C 1 155 HIS 155 155 155 HIS HIS C . n 
C 1 156 LEU 156 156 156 LEU LEU C . n 
C 1 157 PHE 157 157 157 PHE PHE C . n 
C 1 158 GLU 158 158 158 GLU GLU C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 ILE 160 160 160 ILE ILE C . n 
C 1 161 LYS 161 161 161 LYS LYS C . n 
C 1 162 ASP 162 162 162 ASP ASP C . n 
C 1 163 PRO 163 163 163 PRO PRO C . n 
C 1 164 LYS 164 164 164 LYS LYS C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 ALA 166 166 166 ALA ALA C . n 
C 1 167 THR 167 167 167 THR THR C . n 
C 1 168 GLU 168 168 ?   ?   ?   C . n 
C 1 169 GLY 169 169 ?   ?   ?   C . n 
C 1 170 THR 170 170 ?   ?   ?   C . n 
C 1 171 GLN 171 171 ?   ?   ?   C . n 
C 1 172 PRO 172 172 ?   ?   ?   C . n 
C 1 173 MET 173 173 ?   ?   ?   C . n 
C 1 174 PRO 174 174 ?   ?   ?   C . n 
C 1 175 SER 175 175 ?   ?   ?   C . n 
C 1 176 PRO 176 176 ?   ?   ?   C . n 
C 1 177 VAL 177 177 ?   ?   ?   C . n 
C 1 178 PRO 178 178 ?   ?   ?   C . n 
C 1 179 GLY 179 179 ?   ?   ?   C . n 
C 1 180 LYS 180 180 ?   ?   ?   C . n 
C 1 181 LEU 181 181 ?   ?   ?   C . n 
C 1 182 SER 182 182 ?   ?   ?   C . n 
C 1 183 SER 183 183 ?   ?   ?   C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLN 185 185 185 GLN GLN C . n 
C 1 186 GLU 186 186 186 GLU GLU C . n 
C 1 187 PHE 187 187 187 PHE PHE C . n 
C 1 188 LEU 188 188 188 LEU LEU C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 PHE 190 190 190 PHE PHE C . n 
C 1 191 ARG 191 191 191 ARG ARG C . n 
C 1 192 LEU 192 192 192 LEU LEU C . n 
C 1 193 GLU 193 193 193 GLU GLU C . n 
C 1 194 VAL 194 194 194 VAL VAL C . n 
C 1 195 ILE 195 195 195 ILE ILE C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 ASN 197 197 197 ASN ASN C . n 
C 1 198 PRO 198 198 198 PRO PRO C . n 
C 1 199 PHE 199 199 199 PHE PHE C . n 
C 1 200 ILE 200 200 200 ILE ILE C . n 
C 1 201 VAL 201 201 201 VAL VAL C . n 
C 1 202 TYR 202 202 202 TYR TYR C . n 
C 1 203 SER 203 203 203 SER SER C . n 
C 1 204 ALA 204 204 204 ALA ALA C . n 
C 1 205 LYS 205 205 205 LYS LYS C . n 
C 1 206 LYS 206 206 206 LYS LYS C . n 
C 1 207 PHE 207 207 207 PHE PHE C . n 
C 1 208 PRO 208 208 208 PRO PRO C . n 
C 1 209 GLY 209 209 209 GLY GLY C . n 
C 1 210 LEU 210 210 210 LEU LEU C . n 
C 1 211 THR 211 211 211 THR THR C . n 
C 1 212 THR 212 212 212 THR THR C . n 
C 1 213 SER 213 213 ?   ?   ?   C . n 
C 1 214 THR 214 214 ?   ?   ?   C . n 
C 1 215 PRO 215 215 ?   ?   ?   C . n 
C 1 216 ILE 216 216 ?   ?   ?   C . n 
C 1 217 SER 217 217 ?   ?   ?   C . n 
C 1 218 ARG 218 218 ?   ?   ?   C . n 
C 1 219 MET 219 219 ?   ?   ?   C . n 
C 1 220 ILE 220 220 ?   ?   ?   C . n 
C 1 221 ALA 221 221 ?   ?   ?   C . n 
C 1 222 GLU 222 222 ?   ?   ?   C . n 
C 1 223 GLN 223 223 ?   ?   ?   C . n 
C 1 224 GLY 224 224 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ALA 2   2   ?   ?   ?   D . n 
D 1 3   THR 3   3   ?   ?   ?   D . n 
D 1 4   LEU 4   4   ?   ?   ?   D . n 
D 1 5   ALA 5   5   ?   ?   ?   D . n 
D 1 6   ALA 6   6   ?   ?   ?   D . n 
D 1 7   PRO 7   7   ?   ?   ?   D . n 
D 1 8   PRO 8   8   ?   ?   ?   D . n 
D 1 9   PRO 9   9   ?   ?   ?   D . n 
D 1 10  PRO 10  10  ?   ?   ?   D . n 
D 1 11  LEU 11  11  ?   ?   ?   D . n 
D 1 12  GLY 12  12  ?   ?   ?   D . n 
D 1 13  GLU 13  13  ?   ?   ?   D . n 
D 1 14  SER 14  14  ?   ?   ?   D . n 
D 1 15  GLY 15  15  15  GLY GLY D . n 
D 1 16  ASN 16  16  16  ASN ASN D . n 
D 1 17  SER 17  17  17  SER SER D . n 
D 1 18  ASN 18  18  18  ASN ASN D . n 
D 1 19  SER 19  19  19  SER SER D . n 
D 1 20  VAL 20  20  20  VAL VAL D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  ARG 22  22  22  ARG ARG D . n 
D 1 23  ILE 23  23  23  ILE ILE D . n 
D 1 24  THR 24  24  24  THR THR D . n 
D 1 25  ARG 25  25  25  ARG ARG D . n 
D 1 26  GLU 26  26  26  GLU GLU D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  LYS 28  28  28  LYS LYS D . n 
D 1 29  LYS 29  29  29  LYS LYS D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  THR 31  31  31  THR THR D . n 
D 1 32  TYR 32  32  32  TYR TYR D . n 
D 1 33  LYS 33  33  33  LYS LYS D . n 
D 1 34  LEU 34  34  34  LEU LEU D . n 
D 1 35  ASN 35  35  35  ASN ASN D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  MET 37  37  37  MET MET D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  GLN 39  39  39  GLN GLN D . n 
D 1 40  PRO 40  40  40  PRO PRO D . n 
D 1 41  LYS 41  41  41  LYS LYS D . n 
D 1 42  ARG 42  42  42  ARG ARG D . n 
D 1 43  ALA 43  43  43  ALA ALA D . n 
D 1 44  ARG 44  44  44  ARG ARG D . n 
D 1 45  ALA 45  45  45  ALA ALA D . n 
D 1 46  CYS 46  46  46  CYS CYS D . n 
D 1 47  GLY 47  47  47  GLY GLY D . n 
D 1 48  GLN 48  48  48  GLN GLN D . n 
D 1 49  GLY 49  49  49  GLY GLY D . n 
D 1 50  SER 50  50  50  SER SER D . n 
D 1 51  LYS 51  51  51  LYS LYS D . n 
D 1 52  SER 52  52  52  SER SER D . n 
D 1 53  HIS 53  53  53  HIS HIS D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ASP 55  55  55  ASP ASP D . n 
D 1 56  ARG 56  56  56  ARG ARG D . n 
D 1 57  ARG 57  57  57  ARG ARG D . n 
D 1 58  PRO 58  58  58  PRO PRO D . n 
D 1 59  VAL 59  59  59  VAL VAL D . n 
D 1 60  ASP 60  60  60  ASP ASP D . n 
D 1 61  PRO 61  61  61  PRO PRO D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  PRO 63  63  63  PRO PRO D . n 
D 1 64  VAL 64  64  64  VAL VAL D . n 
D 1 65  ILE 65  65  65  ILE ILE D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  ASN 68  68  68  ASN ASN D . n 
D 1 69  ILE 69  69  69  ILE ILE D . n 
D 1 70  PHE 70  70  70  PHE PHE D . n 
D 1 71  GLU 71  71  71  GLU GLU D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  ASP 73  73  73  ASP ASP D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  HIS 75  75  75  HIS HIS D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  ASP 77  77  77  ASP ASP D . n 
D 1 78  SER 78  78  78  SER SER D . n 
D 1 79  ASN 79  79  79  ASN ASN D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  THR 81  81  81  THR THR D . n 
D 1 82  ASP 82  82  82  ASP ASP D . n 
D 1 83  ILE 83  83  83  ILE ILE D . n 
D 1 84  THR 84  84  84  THR THR D . n 
D 1 85  PHE 85  85  85  PHE PHE D . n 
D 1 86  VAL 86  86  86  VAL VAL D . n 
D 1 87  TYR 87  87  87  TYR TYR D . n 
D 1 88  ASN 88  88  88  ASN ASN D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASN 90  90  90  ASN ASN D . n 
D 1 91  PHE 91  91  91  PHE PHE D . n 
D 1 92  PHE 92  92  92  PHE PHE D . n 
D 1 93  LEU 93  93  93  LEU LEU D . n 
D 1 94  PHE 94  94  94  PHE PHE D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  THR 96  96  96  THR THR D . n 
D 1 97  LEU 97  97  97  LEU LEU D . n 
D 1 98  GLU 98  98  98  GLU GLU D . n 
D 1 99  PRO 99  99  99  PRO PRO D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ARG 101 101 101 ARG ARG D . n 
D 1 102 PRO 102 102 102 PRO PRO D . n 
D 1 103 ILE 103 103 103 ILE ILE D . n 
D 1 104 ALA 104 104 ?   ?   ?   D . n 
D 1 105 THR 105 105 ?   ?   ?   D . n 
D 1 106 GLY 106 106 ?   ?   ?   D . n 
D 1 107 LYS 107 107 ?   ?   ?   D . n 
D 1 108 LEU 108 108 ?   ?   ?   D . n 
D 1 109 MET 109 109 ?   ?   ?   D . n 
D 1 110 THR 110 110 ?   ?   ?   D . n 
D 1 111 ASN 111 111 ?   ?   ?   D . n 
D 1 112 GLN 112 112 ?   ?   ?   D . n 
D 1 113 GLY 113 113 ?   ?   ?   D . n 
D 1 114 SER 114 114 ?   ?   ?   D . n 
D 1 115 PRO 115 115 115 PRO PRO D . n 
D 1 116 VAL 116 116 116 VAL VAL D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 THR 118 118 118 THR THR D . n 
D 1 119 GLY 119 119 119 GLY GLY D . n 
D 1 120 VAL 120 120 120 VAL VAL D . n 
D 1 121 PRO 121 121 121 PRO PRO D . n 
D 1 122 VAL 122 122 122 VAL VAL D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 GLY 124 124 124 GLY GLY D . n 
D 1 125 VAL 125 125 125 VAL VAL D . n 
D 1 126 ALA 126 126 126 ALA ALA D . n 
D 1 127 TYR 127 127 127 TYR TYR D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 ASP 129 129 129 ASP ASP D . n 
D 1 130 LYS 130 130 130 LYS LYS D . n 
D 1 131 PRO 131 131 131 PRO PRO D . n 
D 1 132 ASN 132 132 132 ASN ASN D . n 
D 1 133 ARG 133 133 133 ARG ARG D . n 
D 1 134 ALA 134 134 134 ALA ALA D . n 
D 1 135 GLY 135 135 135 GLY GLY D . n 
D 1 136 TYR 136 136 136 TYR TYR D . n 
D 1 137 PHE 137 137 137 PHE PHE D . n 
D 1 138 ILE 138 138 138 ILE ILE D . n 
D 1 139 PHE 139 139 139 PHE PHE D . n 
D 1 140 PRO 140 140 140 PRO PRO D . n 
D 1 141 ASP 141 141 141 ASP ASP D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 SER 143 143 143 SER SER D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 ARG 145 145 145 ARG ARG D . n 
D 1 146 ASN 146 146 146 ASN ASN D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 GLY 148 148 148 GLY GLY D . n 
D 1 149 SER 149 149 149 SER SER D . n 
D 1 150 TYR 150 150 150 TYR TYR D . n 
D 1 151 ARG 151 151 151 ARG ARG D . n 
D 1 152 PHE 152 152 152 PHE PHE D . n 
D 1 153 SER 153 153 153 SER SER D . n 
D 1 154 PHE 154 154 154 PHE PHE D . n 
D 1 155 HIS 155 155 155 HIS HIS D . n 
D 1 156 LEU 156 156 156 LEU LEU D . n 
D 1 157 PHE 157 157 157 PHE PHE D . n 
D 1 158 GLU 158 158 158 GLU GLU D . n 
D 1 159 GLN 159 159 159 GLN GLN D . n 
D 1 160 ILE 160 160 160 ILE ILE D . n 
D 1 161 LYS 161 161 161 LYS LYS D . n 
D 1 162 ASP 162 162 162 ASP ASP D . n 
D 1 163 PRO 163 163 163 PRO PRO D . n 
D 1 164 LYS 164 164 164 LYS LYS D . n 
D 1 165 ASP 165 165 165 ASP ASP D . n 
D 1 166 ALA 166 166 166 ALA ALA D . n 
D 1 167 THR 167 167 167 THR THR D . n 
D 1 168 GLU 168 168 ?   ?   ?   D . n 
D 1 169 GLY 169 169 ?   ?   ?   D . n 
D 1 170 THR 170 170 ?   ?   ?   D . n 
D 1 171 GLN 171 171 ?   ?   ?   D . n 
D 1 172 PRO 172 172 ?   ?   ?   D . n 
D 1 173 MET 173 173 ?   ?   ?   D . n 
D 1 174 PRO 174 174 ?   ?   ?   D . n 
D 1 175 SER 175 175 ?   ?   ?   D . n 
D 1 176 PRO 176 176 ?   ?   ?   D . n 
D 1 177 VAL 177 177 ?   ?   ?   D . n 
D 1 178 PRO 178 178 ?   ?   ?   D . n 
D 1 179 GLY 179 179 ?   ?   ?   D . n 
D 1 180 LYS 180 180 ?   ?   ?   D . n 
D 1 181 LEU 181 181 ?   ?   ?   D . n 
D 1 182 SER 182 182 ?   ?   ?   D . n 
D 1 183 SER 183 183 ?   ?   ?   D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLN 185 185 185 GLN GLN D . n 
D 1 186 GLU 186 186 186 GLU GLU D . n 
D 1 187 PHE 187 187 187 PHE PHE D . n 
D 1 188 LEU 188 188 188 LEU LEU D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 PHE 190 190 190 PHE PHE D . n 
D 1 191 ARG 191 191 191 ARG ARG D . n 
D 1 192 LEU 192 192 192 LEU LEU D . n 
D 1 193 GLU 193 193 193 GLU GLU D . n 
D 1 194 VAL 194 194 194 VAL VAL D . n 
D 1 195 ILE 195 195 195 ILE ILE D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 ASN 197 197 197 ASN ASN D . n 
D 1 198 PRO 198 198 198 PRO PRO D . n 
D 1 199 PHE 199 199 199 PHE PHE D . n 
D 1 200 ILE 200 200 200 ILE ILE D . n 
D 1 201 VAL 201 201 201 VAL VAL D . n 
D 1 202 TYR 202 202 202 TYR TYR D . n 
D 1 203 SER 203 203 203 SER SER D . n 
D 1 204 ALA 204 204 204 ALA ALA D . n 
D 1 205 LYS 205 205 205 LYS LYS D . n 
D 1 206 LYS 206 206 206 LYS LYS D . n 
D 1 207 PHE 207 207 207 PHE PHE D . n 
D 1 208 PRO 208 208 208 PRO PRO D . n 
D 1 209 GLY 209 209 209 GLY GLY D . n 
D 1 210 LEU 210 210 210 LEU LEU D . n 
D 1 211 THR 211 211 211 THR THR D . n 
D 1 212 THR 212 212 212 THR THR D . n 
D 1 213 SER 213 213 ?   ?   ?   D . n 
D 1 214 THR 214 214 ?   ?   ?   D . n 
D 1 215 PRO 215 215 ?   ?   ?   D . n 
D 1 216 ILE 216 216 ?   ?   ?   D . n 
D 1 217 SER 217 217 ?   ?   ?   D . n 
D 1 218 ARG 218 218 ?   ?   ?   D . n 
D 1 219 MET 219 219 ?   ?   ?   D . n 
D 1 220 ILE 220 220 ?   ?   ?   D . n 
D 1 221 ALA 221 221 ?   ?   ?   D . n 
D 1 222 GLU 222 222 ?   ?   ?   D . n 
D 1 223 GLN 223 223 ?   ?   ?   D . n 
D 1 224 GLY 224 224 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HOH 1  301 114 HOH HOH A . 
E 2 HOH 2  302 547 HOH HOH A . 
E 2 HOH 3  303 639 HOH HOH A . 
E 2 HOH 4  304 44  HOH HOH A . 
E 2 HOH 5  305 341 HOH HOH A . 
E 2 HOH 6  306 635 HOH HOH A . 
E 2 HOH 7  307 631 HOH HOH A . 
E 2 HOH 8  308 209 HOH HOH A . 
E 2 HOH 9  309 465 HOH HOH A . 
E 2 HOH 10 310 640 HOH HOH A . 
E 2 HOH 11 311 142 HOH HOH A . 
E 2 HOH 12 312 636 HOH HOH A . 
E 2 HOH 13 313 638 HOH HOH A . 
E 2 HOH 14 314 637 HOH HOH A . 
F 2 HOH 1  301 33  HOH HOH B . 
F 2 HOH 2  302 627 HOH HOH B . 
F 2 HOH 3  303 628 HOH HOH B . 
F 2 HOH 4  304 131 HOH HOH B . 
F 2 HOH 5  305 632 HOH HOH B . 
F 2 HOH 6  306 331 HOH HOH B . 
F 2 HOH 7  307 295 HOH HOH B . 
F 2 HOH 8  308 70  HOH HOH B . 
F 2 HOH 9  309 380 HOH HOH B . 
F 2 HOH 10 310 43  HOH HOH B . 
G 2 HOH 1  301 622 HOH HOH C . 
G 2 HOH 2  302 287 HOH HOH C . 
G 2 HOH 3  303 60  HOH HOH C . 
G 2 HOH 4  304 51  HOH HOH C . 
G 2 HOH 5  305 626 HOH HOH C . 
G 2 HOH 6  306 467 HOH HOH C . 
G 2 HOH 7  307 629 HOH HOH C . 
G 2 HOH 8  308 641 HOH HOH C . 
G 2 HOH 9  309 630 HOH HOH C . 
G 2 HOH 10 310 621 HOH HOH C . 
G 2 HOH 11 311 625 HOH HOH C . 
G 2 HOH 12 312 459 HOH HOH C . 
G 2 HOH 13 313 634 HOH HOH C . 
G 2 HOH 14 314 458 HOH HOH C . 
H 2 HOH 1  301 563 HOH HOH D . 
H 2 HOH 2  302 18  HOH HOH D . 
H 2 HOH 3  303 633 HOH HOH D . 
H 2 HOH 4  304 623 HOH HOH D . 
H 2 HOH 5  305 624 HOH HOH D . 
H 2 HOH 6  306 620 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? 'Paul D. Adams' pdadams@lbl.gov ? ? ? ? Python/C++ https://www.phenix-online.org/ ? PHENIX ? ? program 
1.21_5207 1 
? 'data scaling'   ? ? ?               ?               ? ? ? ? ?          ?                              ? XSCALE ? ? ?       . 2 
? 'data reduction' ? ? ?               ?               ? ? ? ? ?          ?                              ? XDS    ? ? ?       . 3 
? phasing          ? ? ?               ?               ? ? ? ? ?          ?                              ? PHASER ? ? ?       . 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I2S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     106.040 
_cell.length_a_esd                 ? 
_cell.length_b                     156.080 
_cell.length_b_esd                 ? 
_cell.length_c                     52.730 
_cell.length_c_esd                 ? 
_cell.volume                       872719.645 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9I2S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9I2S 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.27 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;25% PEG 3350
200 mM (NH4)2SO4
100 mM BisTris/HCl
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-08-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          71.49 
_reflns.entry_id                                       9I2S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               47.21 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     34384 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.18 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.93 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.047 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.041 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.40  2.5  ? ? ? ? ? ? 3879  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.078 ? ? 1 1 0.492 ? ? ? ? 1.821 ? ? ? ? ? ? ? ? ? 
2.50  2.6  ? ? ? ? ? ? 3305  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.246 ? ? 2 1 0.7   ? ? ? ? 1.088 ? ? ? ? ? ? ? ? ? 
2.60  2.8  ? ? ? ? ? ? 5344  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.788 ? ? 3 1 0.831 ? ? ? ? 0.685 ? ? ? ? ? ? ? ? ? 
2.80  8.0  ? ? ? ? ? ? 20830 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039 ? ? 4 1 1.0   ? ? ? ? 0.034 ? ? ? ? ? ? ? ? ? 
8.00  14.0 ? ? ? ? ? ? 826   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.011 ? ? 5 1 1.0   ? ? ? ? 0.009 ? ? ? ? ? ? ? ? ? 
14.00 17.0 ? ? ? ? ? ? 92    ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.009 ? ? 6 1 1.0   ? ? ? ? 0.008 ? ? ? ? ? ? ? ? ? 
17.00 50.0 ? ? ? ? ? ? 108   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.009 ? ? 7 1 1.0   ? ? ? ? 0.007 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               102.05 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9I2S 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             47.21 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     34361 
_refine.ls_number_reflns_R_free                  1719 
_refine.ls_number_reflns_R_work                  32642 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.95 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2209 
_refine.ls_R_factor_R_free                       0.2529 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2192 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.1270 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4735 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        47.21 
_refine_hist.number_atoms_solvent             44 
_refine_hist.number_atoms_total               5519 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5475 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0039 ? 5629 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7007 ? 7618 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0480 ? 817  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0059 ? 1005 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 4.5766 ? 740  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.47  . . 140 2651 97.93 . . . . 0.4106 . . . . . . . . . . . 0.4778 
'X-RAY DIFFRACTION' 2.47 2.55  . . 140 2660 98.14 . . . . 0.4050 . . . . . . . . . . . 0.4562 
'X-RAY DIFFRACTION' 2.55 2.64  . . 143 2705 97.43 . . . . 0.3964 . . . . . . . . . . . 0.4539 
'X-RAY DIFFRACTION' 2.64 2.75  . . 140 2672 98.12 . . . . 0.3429 . . . . . . . . . . . 0.3919 
'X-RAY DIFFRACTION' 2.75 2.87  . . 141 2685 98.50 . . . . 0.3277 . . . . . . . . . . . 0.3708 
'X-RAY DIFFRACTION' 2.87 3.02  . . 142 2705 98.31 . . . . 0.3066 . . . . . . . . . . . 0.3492 
'X-RAY DIFFRACTION' 3.02 3.21  . . 143 2713 98.14 . . . . 0.2817 . . . . . . . . . . . 0.3457 
'X-RAY DIFFRACTION' 3.21 3.46  . . 143 2705 97.84 . . . . 0.2219 . . . . . . . . . . . 0.2523 
'X-RAY DIFFRACTION' 3.46 3.81  . . 145 2758 98.71 . . . . 0.2090 . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 3.81 4.36  . . 144 2736 97.93 . . . . 0.1891 . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 4.36 5.49  . . 146 2782 98.39 . . . . 0.1581 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 5.49 47.21 . . 152 2870 96.15 . . . . 0.2010 . . . . . . . . . . . 0.2249 
# 
_struct.entry_id                     9I2S 
_struct.title                        'Velvet domain of the transcriptional regulator VeA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9I2S 
_struct_keywords.text            'Sexual development, secondary metabolism, regulator, veA, velvet family, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    VEA_EMENI 
_struct_ref.pdbx_db_accession          C8VTV4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNK
TDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQI
KDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9I2S A 1 ? 224 ? C8VTV4 1 ? 224 ? 1 224 
2 1 9I2S B 1 ? 224 ? C8VTV4 1 ? 224 ? 1 224 
3 1 9I2S C 1 ? 224 ? C8VTV4 1 ? 224 ? 1 224 
4 1 9I2S D 1 ? 224 ? C8VTV4 1 ? 224 ? 1 224 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1720  ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  18660 ? 
2 'ABSA (A^2)' 1820  ? 
2 MORE         -11   ? 
2 'SSA (A^2)'  18740 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F 
2 1 C,D,G,H 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 50  ? THR A 54  ? SER A 50  THR A 54  5 ? 5 
HELX_P HELX_P2  AA2 ASP A 162 ? ALA A 166 ? ASP A 162 ALA A 166 5 ? 5 
HELX_P HELX_P3  AA3 PHE A 207 ? THR A 212 ? PHE A 207 THR A 212 1 ? 6 
HELX_P HELX_P4  AA4 HIS B 53  ? ARG B 57  ? HIS B 53  ARG B 57  5 ? 5 
HELX_P HELX_P5  AA5 ASP B 162 ? ALA B 166 ? ASP B 162 ALA B 166 5 ? 5 
HELX_P HELX_P6  AA6 HIS C 53  ? ARG C 57  ? HIS C 53  ARG C 57  5 ? 5 
HELX_P HELX_P7  AA7 ASP C 162 ? ALA C 166 ? ASP C 162 ALA C 166 5 ? 5 
HELX_P HELX_P8  AA8 SER D 50  ? THR D 54  ? SER D 50  THR D 54  5 ? 5 
HELX_P HELX_P9  AA9 ASP D 162 ? ALA D 166 ? ASP D 162 ALA D 166 5 ? 5 
HELX_P HELX_P10 AB1 PHE D 207 ? THR D 212 ? PHE D 207 THR D 212 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 60  A . ? ASP 60  A PRO 61  A ? PRO 61  A 1 -4.80  
2 LYS 130 A . ? LYS 130 A PRO 131 A ? PRO 131 A 1 1.55   
3 ASP 60  B . ? ASP 60  B PRO 61  B ? PRO 61  B 1 -5.59  
4 LYS 130 B . ? LYS 130 B PRO 131 B ? PRO 131 B 1 3.34   
5 ASP 60  C . ? ASP 60  C PRO 61  C ? PRO 61  C 1 -11.95 
6 LYS 130 C . ? LYS 130 C PRO 131 C ? PRO 131 C 1 0.00   
7 ASP 60  D . ? ASP 60  D PRO 61  D ? PRO 61  D 1 -2.80  
8 LYS 130 D . ? LYS 130 D PRO 131 D ? PRO 131 D 1 4.86   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 5 ? 
AC1 ? 4 ? 
AC2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 17  ? ILE A 23  ? SER A 17  ILE A 23  
AA1 2 LYS A 29  ? GLN A 38  ? LYS A 29  GLN A 38  
AA1 3 VAL A 64  ? SER A 72  ? VAL A 64  SER A 72  
AA1 4 LYS A 80  ? ASP A 82  ? LYS A 80  ASP A 82  
AA2 1 SER A 17  ? ILE A 23  ? SER A 17  ILE A 23  
AA2 2 LYS A 29  ? GLN A 38  ? LYS A 29  GLN A 38  
AA2 3 VAL A 64  ? SER A 72  ? VAL A 64  SER A 72  
AA2 4 ALA A 134 ? ILE A 138 ? ALA A 134 ILE A 138 
AA2 5 ALA A 126 ? LEU A 128 ? ALA A 126 LEU A 128 
AA3 1 ARG A 42  ? ARG A 44  ? ARG A 42  ARG A 44  
AA3 2 PHE A 199 ? TYR A 202 ? PHE A 199 TYR A 202 
AA3 3 GLY A 148 ? ILE A 160 ? GLY A 148 ILE A 160 
AA3 4 ALA A 89  ? PRO A 99  ? ALA A 89  PRO A 99  
AA3 5 VAL A 122 ? GLY A 124 ? VAL A 122 GLY A 124 
AA4 1 ARG A 42  ? ARG A 44  ? ARG A 42  ARG A 44  
AA4 2 PHE A 199 ? TYR A 202 ? PHE A 199 TYR A 202 
AA4 3 GLY A 148 ? ILE A 160 ? GLY A 148 ILE A 160 
AA4 4 GLU A 189 ? ILE A 195 ? GLU A 189 ILE A 195 
AA5 1 LEU A 117 ? GLY A 119 ? LEU A 117 GLY A 119 
AA5 2 LEU A 142 ? VAL A 144 ? LEU A 142 VAL A 144 
AA6 1 SER B 17  ? ILE B 23  ? SER B 17  ILE B 23  
AA6 2 LYS B 29  ? GLN B 38  ? LYS B 29  GLN B 38  
AA6 3 VAL B 64  ? SER B 72  ? VAL B 64  SER B 72  
AA6 4 THR B 81  ? ASP B 82  ? THR B 81  ASP B 82  
AA7 1 SER B 17  ? ILE B 23  ? SER B 17  ILE B 23  
AA7 2 LYS B 29  ? GLN B 38  ? LYS B 29  GLN B 38  
AA7 3 VAL B 64  ? SER B 72  ? VAL B 64  SER B 72  
AA7 4 ALA B 134 ? ILE B 138 ? ALA B 134 ILE B 138 
AA7 5 ALA B 126 ? LEU B 128 ? ALA B 126 LEU B 128 
AA8 1 ARG B 42  ? ARG B 44  ? ARG B 42  ARG B 44  
AA8 2 PHE B 199 ? TYR B 202 ? PHE B 199 TYR B 202 
AA8 3 GLY B 148 ? ILE B 160 ? GLY B 148 ILE B 160 
AA8 4 ALA B 89  ? PRO B 99  ? ALA B 89  PRO B 99  
AA8 5 VAL B 122 ? GLY B 124 ? VAL B 122 GLY B 124 
AA9 1 ARG B 42  ? ARG B 44  ? ARG B 42  ARG B 44  
AA9 2 PHE B 199 ? TYR B 202 ? PHE B 199 TYR B 202 
AA9 3 GLY B 148 ? ILE B 160 ? GLY B 148 ILE B 160 
AA9 4 LEU B 188 ? ILE B 195 ? LEU B 188 ILE B 195 
AB1 1 LEU B 117 ? GLY B 119 ? LEU B 117 GLY B 119 
AB1 2 LEU B 142 ? VAL B 144 ? LEU B 142 VAL B 144 
AB2 1 SER C 17  ? ILE C 23  ? SER C 17  ILE C 23  
AB2 2 LYS C 29  ? GLN C 38  ? LYS C 29  GLN C 38  
AB2 3 VAL C 64  ? ASP C 73  ? VAL C 64  ASP C 73  
AB2 4 ASP C 76  ? ASP C 82  ? ASP C 76  ASP C 82  
AB3 1 SER C 17  ? ILE C 23  ? SER C 17  ILE C 23  
AB3 2 LYS C 29  ? GLN C 38  ? LYS C 29  GLN C 38  
AB3 3 VAL C 64  ? ASP C 73  ? VAL C 64  ASP C 73  
AB3 4 ALA C 134 ? ILE C 138 ? ALA C 134 ILE C 138 
AB3 5 ALA C 126 ? LEU C 128 ? ALA C 126 LEU C 128 
AB4 1 ARG C 42  ? ARG C 44  ? ARG C 42  ARG C 44  
AB4 2 PHE C 199 ? TYR C 202 ? PHE C 199 TYR C 202 
AB4 3 GLY C 148 ? ILE C 160 ? GLY C 148 ILE C 160 
AB4 4 ALA C 89  ? PRO C 99  ? ALA C 89  PRO C 99  
AB4 5 VAL C 122 ? GLY C 124 ? VAL C 122 GLY C 124 
AB5 1 ARG C 42  ? ARG C 44  ? ARG C 42  ARG C 44  
AB5 2 PHE C 199 ? TYR C 202 ? PHE C 199 TYR C 202 
AB5 3 GLY C 148 ? ILE C 160 ? GLY C 148 ILE C 160 
AB5 4 GLU C 189 ? ILE C 195 ? GLU C 189 ILE C 195 
AB6 1 LEU C 117 ? GLY C 119 ? LEU C 117 GLY C 119 
AB6 2 LEU C 142 ? VAL C 144 ? LEU C 142 VAL C 144 
AB7 1 SER D 17  ? ILE D 23  ? SER D 17  ILE D 23  
AB7 2 LYS D 29  ? GLN D 38  ? LYS D 29  GLN D 38  
AB7 3 VAL D 64  ? SER D 72  ? VAL D 64  SER D 72  
AB7 4 THR D 81  ? ASP D 82  ? THR D 81  ASP D 82  
AB8 1 SER D 17  ? ILE D 23  ? SER D 17  ILE D 23  
AB8 2 LYS D 29  ? GLN D 38  ? LYS D 29  GLN D 38  
AB8 3 VAL D 64  ? SER D 72  ? VAL D 64  SER D 72  
AB8 4 ALA D 134 ? ILE D 138 ? ALA D 134 ILE D 138 
AB8 5 ALA D 126 ? LEU D 128 ? ALA D 126 LEU D 128 
AB9 1 ARG D 42  ? ARG D 44  ? ARG D 42  ARG D 44  
AB9 2 PHE D 199 ? TYR D 202 ? PHE D 199 TYR D 202 
AB9 3 GLY D 148 ? ILE D 160 ? GLY D 148 ILE D 160 
AB9 4 ALA D 89  ? PRO D 99  ? ALA D 89  PRO D 99  
AB9 5 VAL D 122 ? GLY D 124 ? VAL D 122 GLY D 124 
AC1 1 ARG D 42  ? ARG D 44  ? ARG D 42  ARG D 44  
AC1 2 PHE D 199 ? TYR D 202 ? PHE D 199 TYR D 202 
AC1 3 GLY D 148 ? ILE D 160 ? GLY D 148 ILE D 160 
AC1 4 GLU D 189 ? ILE D 195 ? GLU D 189 ILE D 195 
AC2 1 LEU D 117 ? GLY D 119 ? LEU D 117 GLY D 119 
AC2 2 LEU D 142 ? VAL D 144 ? LEU D 142 VAL D 144 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 18  ? N ASN A 18  O LEU A 34  ? O LEU A 34  
AA1 2 3 N ASN A 35  ? N ASN A 35  O GLU A 66  ? O GLU A 66  
AA1 3 4 N GLU A 71  ? N GLU A 71  O THR A 81  ? O THR A 81  
AA2 1 2 N ASN A 18  ? N ASN A 18  O LEU A 34  ? O LEU A 34  
AA2 2 3 N ASN A 35  ? N ASN A 35  O GLU A 66  ? O GLU A 66  
AA2 3 4 N LEU A 67  ? N LEU A 67  O GLY A 135 ? O GLY A 135 
AA2 4 5 O ALA A 134 ? O ALA A 134 N LEU A 128 ? N LEU A 128 
AA3 1 2 N ALA A 43  ? N ALA A 43  O TYR A 202 ? O TYR A 202 
AA3 2 3 O VAL A 201 ? O VAL A 201 N GLY A 148 ? N GLY A 148 
AA3 3 4 O PHE A 157 ? O PHE A 157 N PHE A 92  ? N PHE A 92  
AA3 4 5 N LEU A 93  ? N LEU A 93  O ALA A 123 ? O ALA A 123 
AA4 1 2 N ALA A 43  ? N ALA A 43  O TYR A 202 ? O TYR A 202 
AA4 2 3 O VAL A 201 ? O VAL A 201 N GLY A 148 ? N GLY A 148 
AA4 3 4 N GLU A 158 ? N GLU A 158 O GLU A 189 ? O GLU A 189 
AA5 1 2 N THR A 118 ? N THR A 118 O SER A 143 ? O SER A 143 
AA6 1 2 N VAL B 20  ? N VAL B 20  O TYR B 32  ? O TYR B 32  
AA6 2 3 N LYS B 29  ? N LYS B 29  O SER B 72  ? O SER B 72  
AA6 3 4 N GLU B 71  ? N GLU B 71  O THR B 81  ? O THR B 81  
AA7 1 2 N VAL B 20  ? N VAL B 20  O TYR B 32  ? O TYR B 32  
AA7 2 3 N LYS B 29  ? N LYS B 29  O SER B 72  ? O SER B 72  
AA7 3 4 N ILE B 65  ? N ILE B 65  O PHE B 137 ? O PHE B 137 
AA7 4 5 O ALA B 134 ? O ALA B 134 N LEU B 128 ? N LEU B 128 
AA8 1 2 N ALA B 43  ? N ALA B 43  O TYR B 202 ? O TYR B 202 
AA8 2 3 O VAL B 201 ? O VAL B 201 N GLY B 148 ? N GLY B 148 
AA8 3 4 O ARG B 151 ? O ARG B 151 N GLU B 98  ? N GLU B 98  
AA8 4 5 N LEU B 93  ? N LEU B 93  O ALA B 123 ? O ALA B 123 
AA9 1 2 N ALA B 43  ? N ALA B 43  O TYR B 202 ? O TYR B 202 
AA9 2 3 O VAL B 201 ? O VAL B 201 N GLY B 148 ? N GLY B 148 
AA9 3 4 N GLU B 158 ? N GLU B 158 O GLU B 189 ? O GLU B 189 
AB1 1 2 N THR B 118 ? N THR B 118 O SER B 143 ? O SER B 143 
AB2 1 2 N ARG C 22  ? N ARG C 22  O ILE C 30  ? O ILE C 30  
AB2 2 3 N ASN C 35  ? N ASN C 35  O GLU C 66  ? O GLU C 66  
AB2 3 4 N GLU C 71  ? N GLU C 71  O THR C 81  ? O THR C 81  
AB3 1 2 N ARG C 22  ? N ARG C 22  O ILE C 30  ? O ILE C 30  
AB3 2 3 N ASN C 35  ? N ASN C 35  O GLU C 66  ? O GLU C 66  
AB3 3 4 N LEU C 67  ? N LEU C 67  O GLY C 135 ? O GLY C 135 
AB3 4 5 O ALA C 134 ? O ALA C 134 N LEU C 128 ? N LEU C 128 
AB4 1 2 N ALA C 43  ? N ALA C 43  O TYR C 202 ? O TYR C 202 
AB4 2 3 O VAL C 201 ? O VAL C 201 N GLY C 148 ? N GLY C 148 
AB4 3 4 O HIS C 155 ? O HIS C 155 N PHE C 94  ? N PHE C 94  
AB4 4 5 N LEU C 93  ? N LEU C 93  O ALA C 123 ? O ALA C 123 
AB5 1 2 N ALA C 43  ? N ALA C 43  O TYR C 202 ? O TYR C 202 
AB5 2 3 O VAL C 201 ? O VAL C 201 N GLY C 148 ? N GLY C 148 
AB5 3 4 N GLU C 158 ? N GLU C 158 O GLU C 189 ? O GLU C 189 
AB6 1 2 N THR C 118 ? N THR C 118 O SER C 143 ? O SER C 143 
AB7 1 2 N ARG D 22  ? N ARG D 22  O ILE D 30  ? O ILE D 30  
AB7 2 3 N ASN D 35  ? N ASN D 35  O GLU D 66  ? O GLU D 66  
AB7 3 4 N GLU D 71  ? N GLU D 71  O THR D 81  ? O THR D 81  
AB8 1 2 N ARG D 22  ? N ARG D 22  O ILE D 30  ? O ILE D 30  
AB8 2 3 N ASN D 35  ? N ASN D 35  O GLU D 66  ? O GLU D 66  
AB8 3 4 N LEU D 67  ? N LEU D 67  O GLY D 135 ? O GLY D 135 
AB8 4 5 O ALA D 134 ? O ALA D 134 N LEU D 128 ? N LEU D 128 
AB9 1 2 N ALA D 43  ? N ALA D 43  O TYR D 202 ? O TYR D 202 
AB9 2 3 O VAL D 201 ? O VAL D 201 N GLY D 148 ? N GLY D 148 
AB9 3 4 O HIS D 155 ? O HIS D 155 N PHE D 94  ? N PHE D 94  
AB9 4 5 N LEU D 93  ? N LEU D 93  O ALA D 123 ? O ALA D 123 
AC1 1 2 N ALA D 43  ? N ALA D 43  O TYR D 202 ? O TYR D 202 
AC1 2 3 O VAL D 201 ? O VAL D 201 N GLY D 148 ? N GLY D 148 
AC1 3 4 N GLU D 158 ? N GLU D 158 O GLU D 189 ? O GLU D 189 
AC2 1 2 N THR D 118 ? N THR D 118 O SER D 143 ? O SER D 143 
# 
_pdbx_entry_details.entry_id                   9I2S 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 210 ? ? -90.53  -60.54 
2 1 ARG C 101 ? ? -163.54 79.05  
3 1 LEU C 210 ? ? -104.91 -67.98 
4 1 PRO D 102 ? ? -60.70  0.25   
5 1 GLN D 185 ? ? -103.73 40.73  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -22.9425957614 12.7796958565  -21.8184752641  0.579961177761 ? 0.0353630838413   ? 0.033429575053 
? 0.655386861859 ? -0.0478949768644  ? 0.524785773683 ? 9.14645344078 ? -0.52438248348  ? -4.59488172504  ? 5.5660824938  ? 
-0.919026126762  ? 4.30372287572  ? 0.166867626328   ? 0.569489022641   ? 0.15256185888    ? 0.367580961702   ? -0.144048928226  ? 
0.046682129964  ? -0.107884954701   ? -0.26831871116   ? -0.0314808129826 ? 
2  'X-RAY DIFFRACTION' ? refined -17.8686585806 13.5249504617  -26.6476060916  0.699535486679 ? 0.0562453197172   ? 
0.0532650504487   ? 0.648333189039 ? -0.00810569791525 ? 0.518891926744 ? 6.12086130242 ? 1.59052714706   ? -2.42522780677  ? 
4.85156486055 ? -0.378729366961  ? 3.10643816913  ? 0.159168490521   ? 0.234339955787   ? 0.613541773756   ? -0.0351280791033 ? 
0.108333229081   ? 0.0382704050285 ? -0.373339315967   ? 0.157778780628   ? -0.265983387249  ? 
3  'X-RAY DIFFRACTION' ? refined -23.2982456004 7.2470868054   -26.0571806083  0.652530304182 ? 0.0878748037336   ? 
0.0765263203047   ? 0.710955478215 ? 0.0330212559963   ? 0.416112355928 ? 2.84286345808 ? -2.12585456897  ? -1.37143746454  ? 
4.79891396304 ? 2.60814673368    ? 1.30071448661  ? 0.240539155688   ? 0.115761366719   ? 0.2644895704     ? -0.287796721006  ? 
0.0261826037835  ? 0.0708334667203 ? -0.122997217      ? 0.26700424882    ? -0.0438004650377 ? 
4  'X-RAY DIFFRACTION' ? refined -33.9060866681 10.7174023926  -11.4956822171  0.704420511239 ? 0.0406948344497   ? 0.111674543693 
? 0.586727104527 ? 0.0276630832664   ? 0.741659695218 ? 6.84280912903 ? 0.620147527458  ? -4.24649951414  ? 3.62260433126 ? 
-0.248367976934  ? 3.46763399215  ? 0.182331910704   ? -0.288194040719  ? -0.460155384526  ? 0.604811068221   ? -0.255152654537  ? 
0.953436920535  ? 0.141922365583    ? 0.0363779244846  ? 0.0601519578423  ? 
5  'X-RAY DIFFRACTION' ? refined -37.5906651006 -8.13773919631 -29.108859482   0.805581555063 ? 0.0386087021136   ? 
-0.367737639867   ? 0.731067278265 ? -0.173501285971   ? 1.25927954239  ? 7.80687032397 ? -1.35076879592  ? -1.19435719156  ? 
1.2460898395  ? 2.17550714015    ? 3.90970854612  ? 0.438680024546   ? -0.378736831675  ? -1.18405874836   ? -0.81121385607   ? 
-0.20917374874   ? 2.48463103372   ? 0.678099407556    ? -0.85359442003   ? 0.252760063011   ? 
6  'X-RAY DIFFRACTION' ? refined -8.34556337132 -13.7927624656 -14.6512629697  0.977234832287 ? 0.0732474622782   ? 
-0.148098883425   ? 1.21911635929  ? 0.0589069955423   ? 1.05325100992  ? 3.40230913767 ? 1.57848053501   ? 1.64927302749   ? 
3.85262027377 ? 1.11598521512    ? 3.44710123533  ? -0.267018662234  ? 0.810629095601   ? -0.426307218258  ? -0.0421565298963 ? 
0.535127551203   ? -2.06233510241  ? 0.84467598134     ? 2.09208370769    ? 0.292219046711   ? 
7  'X-RAY DIFFRACTION' ? refined -31.8241856012 -10.260296939  -30.0680588455  0.958961578766 ? 0.10215112788     ? -0.26152322794 
? 0.621728664189 ? -0.0760136302421  ? 0.687295834144 ? 5.14610323408 ? -3.0084154189   ? 1.4847025936    ? 5.91453969241 ? 
-1.80569386132   ? 2.93734535109  ? 0.430560522647   ? 0.492049283119   ? -0.698998226369  ? -1.33265444858   ? -0.0831300872668 ? 
0.863131736765  ? 0.31355388882     ? -0.143955531223  ? -0.238593892788  ? 
8  'X-RAY DIFFRACTION' ? refined -16.8293189441 -3.72209995712 -16.8172853946  0.835465991243 ? 0.183432192138    ? 
-0.0307968968253  ? 0.443746653927 ? -0.0791223679721  ? 0.603617211765 ? 5.17838740992 ? 0.142206542781  ? 0.61398894266   ? 
3.82024564481 ? 0.142053852332   ? 4.4187700878   ? -0.291050438978  ? 0.56055239377    ? 0.601356379123   ? 0.74008133248    ? 
-0.246833515329  ? -0.154160683338 ? -0.426832436385   ? 0.764529425867   ? 0.269667207667   ? 
9  'X-RAY DIFFRACTION' ? refined -22.5678617028 -10.1990555971 -25.4685131382  0.786111951237 ? 0.0640149464765   ? 
-0.00312875951932 ? 0.620345453249 ? -0.0294493671505  ? 0.592722083003 ? 3.80201334177 ? -2.01056685155  ? 1.75707802602   ? 
6.20972920041 ? -1.56613884589   ? 6.61255826926  ? 0.405472865926   ? 0.502553264572   ? -0.124949048726  ? -0.719825211097  ? 
-0.39029371254   ? 0.241628799291  ? 0.526273871091    ? -0.13361861361   ? -0.26595616946   ? 
10 'X-RAY DIFFRACTION' ? refined -33.1973666693 4.30550089951  -40.0340172295  2.41709923012  ? 0.411629939645    ? 
-0.389669925747   ? 1.86239380654  ? -0.112295696273   ? 1.25557748889  ? 7.40159519753 ? 0.153950447474  ? -0.201268400872 ? 
4.15355384167 ? 2.03704616705    ? 3.29703171887  ? 1.96098465307    ? 2.71770851294    ? 0.164703818652   ? -1.7785605938    ? 
-0.98363374361   ? 0.99255954274   ? 1.27983907067     ? -0.0337313900992 ? -0.9562192711    ? 
11 'X-RAY DIFFRACTION' ? refined -15.2559436065 -10.2706678633 -13.8545291495  0.775370462717 ? 0.0823848599211   ? 
-0.0890072485457  ? 0.700652628566 ? -0.0668187235678  ? 0.613920662722 ? 2.71840800903 ? -0.58679569641  ? 2.60497068189   ? 
5.3742963096  ? -2.06142175491   ? 3.11905307435  ? 0.235724380049   ? -0.550999601282  ? 0.203312313996   ? 0.536776092164   ? 
-0.101447562668  ? -0.767807068685 ? -0.00706812312237 ? -0.138780392902  ? 0.176514079224   ? 
12 'X-RAY DIFFRACTION' ? refined -54.7051877235 46.9441510002  -13.4922023576  0.896151502898 ? 0.0329307005285   ? 
-0.0943423395972  ? 0.810090220092 ? -0.058410219369   ? 0.71100466636  ? 1.07688202933 ? 0.0970842435652 ? 0.223253253545  ? 
7.0453232839  ? 6.3096221912     ? 9.32835978616  ? -0.182937057093  ? 0.280540548459   ? 0.621060190705   ? -0.751159197493  ? 
-0.134222830749  ? 0.750799361538  ? -0.686145499538   ? 0.479414828257   ? 0.270364072015   ? 
13 'X-RAY DIFFRACTION' ? refined -41.7047095885 52.8827676185  16.9040031977   0.948887597474 ? -0.0146198980187  ? 
0.0114726429156   ? 1.05748097418  ? -0.197161409594   ? 1.264235994    ? 2.54651413071 ? -0.301048253978 ? -0.297255562228 ? 
1.91388877555 ? -0.0243156088654 ? 0.226718583457 ? -0.0455034332158 ? -1.32407964947   ? -0.834605263616  ? 1.05012376846    ? 
0.314987939855   ? -0.22082738077  ? 0.491746151258    ? 0.195887671086   ? -0.239712013387  ? 
14 'X-RAY DIFFRACTION' ? refined -52.3670756541 53.2193192205  0.484467934366  0.711718912894 ? 0.0558016292232   ? 
-0.122044687282   ? 0.618929561762 ? -0.0754083419632  ? 0.79845483912  ? 4.48352851443 ? 0.351950605347  ? -1.18313684199  ? 
2.83656436908 ? -0.392286236041  ? 4.31302692785  ? -0.0653100329748 ? -0.195466196543  ? 0.117951496565   ? -0.131030893925  ? 
0.0114436085261  ? 0.902668426767  ? -0.379277774183   ? -0.139961693839  ? -0.272463453947  ? 
15 'X-RAY DIFFRACTION' ? refined -57.2697478264 47.4739862534  -11.0962315409  0.783271265873 ? -0.037913397984   ? 
-0.151725008884   ? 0.78814156745  ? -0.0592907902184  ? 0.638848142555 ? 1.70759756017 ? 0.670102442184  ? 1.97366572609   ? 
4.80593553536 ? -1.10205189469   ? 6.18375824639  ? 0.12074000746    ? 0.478566476411   ? -0.370449125208  ? -1.08386392454   ? 
0.317530626258   ? 0.564982464959  ? 0.119212503587    ? -0.215542786006  ? -0.231444991854  ? 
16 'X-RAY DIFFRACTION' ? refined -43.4979411198 42.5399934503  8.65963668924   0.717325655512 ? -0.0427156682319  ? 0.060714759431 
? 0.82732051351  ? -0.0431619873546  ? 0.951958464151 ? 1.46488318715 ? 0.877002457022  ? -1.0719989563   ? 4.19184704504 ? 
1.3277444879     ? 5.45593914211  ? 0.672676789118   ? -0.288599195683  ? -0.278973931042  ? 0.0856964209249  ? -0.137691914021  ? 
-0.551219000337 ? -0.42288233778    ? 0.761174014626   ? -0.573895507812  ? 
17 'X-RAY DIFFRACTION' ? refined -55.7715620182 46.5390792587  -0.864039832042 0.496561823309 ? -0.00248775839369 ? 
-0.0900325537031  ? 0.651265714953 ? -0.0823995132384  ? 0.642519201683 ? 2.6303471324  ? -0.296750951133 ? 1.90561827571   ? 
5.47349998216 ? -0.635300778591  ? 7.55076268645  ? -0.102770732588  ? -0.0823342999898 ? 0.00332461041551 ? -0.239509191718  ? 
0.0345285659495  ? 0.647646786618  ? 0.0289917061111   ? -0.73042474581   ? -0.0775970816073 ? 
18 'X-RAY DIFFRACTION' ? refined -41.88241771   49.6853329548  10.1312164529   0.600345716701 ? 0.0488993005762   ? 
0.0108871159395   ? 0.651537066777 ? -0.0421819459575  ? 0.862058197376 ? 4.24618560331 ? 1.67167974962   ? 3.67018498847   ? 
3.52718977549 ? 0.426196485168   ? 5.50682929606  ? -0.18716008575   ? 0.189444784071   ? 0.112853122831   ? 0.117075455293   ? 
0.0663884271972  ? -0.255863304996 ? -0.294048882637   ? 0.63317378066    ? 0.0414480213668  ? 
19 'X-RAY DIFFRACTION' ? refined -55.431569727  28.1915316043  14.6004129334   1.11530569696  ? -0.101365977011   ? 0.470821623335 
? 0.906298890367 ? 0.0242829911953   ? 0.918648901278 ? 2.21762620659 ? 0.931045537825  ? 3.15926430338   ? 2.03346858394 ? 
1.23470019196    ? 4.4278549808   ? -0.262925057279  ? -1.2041723039    ? -0.265223647384  ? 1.40073615962    ? -0.162569159417  ? 
0.535175058571  ? 0.668704820512    ? 0.0773914885623  ? 0.243108605451   ? 
20 'X-RAY DIFFRACTION' ? refined -38.8218865809 27.8156343009  -12.7751519341  1.22878326718  ? 0.197908695806    ? 0.199018461304 
? 0.916560143812 ? 0.0598137363067   ? 1.08385664549  ? 4.960461918   ? 1.80591191812   ? -0.616151173093 ? 4.05157967059 ? 
1.66281740987    ? 3.46782469288  ? 0.238230981474   ? 1.19268254157    ? 0.442986964457   ? -0.999897667064  ? 0.798287128969   ? 
0.67615393533   ? -0.402468273059   ? -1.25914055912   ? -0.0413486130229 ? 
21 'X-RAY DIFFRACTION' ? refined -50.6521949785 23.5094211052  0.571308813965  0.692980207494 ? -0.112399640765   ? 0.209160025424 
? 0.644913168363 ? 0.00452010688178  ? 0.902791886672 ? 5.58080158683 ? -0.150659362932 ? 1.16050654656   ? 4.96098152929 ? 
0.674916873372   ? 5.12284390134  ? 0.145859775331   ? -0.60792418249   ? -0.68043708879   ? 0.186343224298   ? -0.575341660205  ? 
0.381570244707  ? 0.970597571791    ? 0.404813764977   ? 0.174877590471   ? 
22 'X-RAY DIFFRACTION' ? refined -62.3515326895 23.2226799872  18.9780116762   0.778870228193 ? -0.253978539825   ? 1.25200878114 
? 1.1600664254   ? 0.293747777245    ? 1.64709136495  ? 1.77889160499 ? 0.704911394033  ? -0.612089351449 ? 3.17940757191 ? 
-0.391820514504  ? 0.202948460087 ? -0.370276698413  ? -0.452037402645  ? -1.14700223738   ? 0.969485835946   ? -0.313465139128  ? 
0.267075400908  ? 0.638262299003    ? -0.192861005819  ? -2.27105334363   ? 
23 'X-RAY DIFFRACTION' ? refined -50.4456907132 28.5613083077  0.0349681944523 0.559495666934 ? 0.0516708390894   ? 
0.0692029588761   ? 0.695633982766 ? -0.125136988591   ? 0.621964404865 ? 4.11096765082 ? -2.19688599269  ? 0.275305354573  ? 
6.80997358691 ? -0.384023357094  ? 4.47367710242  ? -0.255003614621  ? -0.188492919312  ? -0.419968646084  ? -0.0950777551295 ? 
0.0159537557036  ? 0.705204158083  ? 0.746628610517    ? -0.19539619259   ? 0.0992577373743  ? 
24 'X-RAY DIFFRACTION' ? refined -47.9015069943 29.7927761696  -1.5785959419   0.422223866317 ? -0.0128200654581  ? 
0.0336296949191   ? 0.611315921454 ? -0.0187381280223  ? 0.644702063751 ? 3.35725245675 ? -0.650909637013 ? -0.666825186287 ? 
7.17974434841 ? 2.12148649095    ? 5.7514492287   ? -0.186552190216  ? -0.0459290133893 ? -0.487387199986  ? -0.0615801337539 ? 
-0.139797597544  ? 0.45957413538   ? 0.00939037594512  ? -0.131850235903  ? 0.108895419508   ? 
25 'X-RAY DIFFRACTION' ? refined -54.7723491166 33.78351111    5.56125534717   0.676323506086 ? -0.0763101728771  ? 0.126348600319 
? 0.866984204767 ? -0.0818708318197  ? 0.881460506366 ? 3.4651494526  ? 1.28854408834   ? -0.773335438956 ? 6.36406927421 ? 
-0.522081353162  ? 4.65802952884  ? -0.378055571067  ? -0.323345715594  ? -0.0992165179562 ? 0.87974840166    ? 0.0245226438958  ? 
1.05634877144   ? 0.214735890901    ? -0.806024012465  ? 0.133814893765   ? 
26 'X-RAY DIFFRACTION' ? refined -29.0275542639 25.7851395796  -24.3243748964  1.57125017682  ? 0.233542908315    ? 0.317743787052 
? 1.08967616792  ? 0.0468580710558   ? 1.30616429529  ? 1.89290302448 ? -1.62690970586  ? -3.21753268062  ? 3.8015566559  ? 
1.77106540369    ? 5.85806211623  ? 0.634248631348   ? 1.20996138519    ? -0.600486055369  ? -1.90500152202   ? 0.63677247601    ? 
0.416339471481  ? -0.49021651848    ? -0.307203207711  ? 0.0277038834686  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 15  ? A 58  A 72  ? ? 
;chain 'A' and (resid   15  through   72 )
;
2  'X-RAY DIFFRACTION' 2  A 59  A 73  ? A 106 A 133 ? ? 
;chain 'A' and (resid   73  through  133 )
;
3  'X-RAY DIFFRACTION' 3  A 107 A 134 ? A 145 A 188 ? ? 
;chain 'A' and (resid  134  through  188 )
;
4  'X-RAY DIFFRACTION' 4  A 146 A 189 ? A 169 A 212 ? ? 
;chain 'A' and (resid  189  through  212 )
;
5  'X-RAY DIFFRACTION' 5  B 1   B 15  ? B 24  B 38  ? ? 
;chain 'B' and (resid   15  through   38 )
;
6  'X-RAY DIFFRACTION' 6  B 25  B 39  ? B 40  B 56  ? ? 
;chain 'B' and (resid   39  through   56 )
;
7  'X-RAY DIFFRACTION' 7  B 41  B 57  ? B 83  B 99  ? ? 
;chain 'B' and (resid   57  through   99 )
;
8  'X-RAY DIFFRACTION' 8  B 84  B 100 ? B 97  B 124 ? ? 
;chain 'B' and (resid  100  through  124 )
;
9  'X-RAY DIFFRACTION' 9  B 98  B 125 ? B 133 B 160 ? ? 
;chain 'B' and (resid  125  through  160 )
;
10 'X-RAY DIFFRACTION' 10 B 134 B 161 ? B 144 B 187 ? ? 
;chain 'B' and (resid  161  through  187 )
;
11 'X-RAY DIFFRACTION' 11 B 145 B 188 ? B 169 B 212 ? ? 
;chain 'B' and (resid  188  through  212 )
;
12 'X-RAY DIFFRACTION' 12 C 1   C 15  ? C 24  C 38  ? ? 
;chain 'C' and (resid   15  through   38 )
;
13 'X-RAY DIFFRACTION' 13 C 25  C 39  ? C 39  C 53  ? ? 
;chain 'C' and (resid   39  through   53 )
;
14 'X-RAY DIFFRACTION' 14 C 40  C 54  ? C 59  C 73  ? ? 
;chain 'C' and (resid   54  through   73 )
;
15 'X-RAY DIFFRACTION' 15 C 60  C 74  ? C 85  C 99  ? ? 
;chain 'C' and (resid   74  through   99 )
;
16 'X-RAY DIFFRACTION' 16 C 86  C 100 ? C 101 C 124 ? ? 
;chain 'C' and (resid  100  through  124 )
;
17 'X-RAY DIFFRACTION' 17 C 102 C 125 ? C 148 C 187 ? ? 
;chain 'C' and (resid  125  through  187 )
;
18 'X-RAY DIFFRACTION' 18 C 149 C 188 ? C 173 C 212 ? ? 
;chain 'C' and (resid  188  through  212 )
;
19 'X-RAY DIFFRACTION' 19 D 1   D 15  ? D 24  D 38  ? ? 
;chain 'D' and (resid   15  through   38 )
;
20 'X-RAY DIFFRACTION' 20 D 25  D 39  ? D 39  D 53  ? ? 
;chain 'D' and (resid   39  through   53 )
;
21 'X-RAY DIFFRACTION' 21 D 40  D 54  ? D 59  D 73  ? ? 
;chain 'D' and (resid   54  through   73 )
;
22 'X-RAY DIFFRACTION' 22 D 60  D 74  ? D 74  D 88  ? ? 
;chain 'D' and (resid   74  through   88 )
;
23 'X-RAY DIFFRACTION' 23 D 75  D 89  ? D 108 D 133 ? ? 
;chain 'D' and (resid   89  through  133 )
;
24 'X-RAY DIFFRACTION' 24 D 109 D 134 ? D 135 D 160 ? ? 
;chain 'D' and (resid  134  through  160 )
;
25 'X-RAY DIFFRACTION' 25 D 136 D 161 ? D 161 D 202 ? ? 
;chain 'D' and (resid  161  through  202 )
;
26 'X-RAY DIFFRACTION' 26 D 162 D 203 ? D 171 D 212 ? ? 
;chain 'D' and (resid  203  through  212 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ALA 2   ? A ALA 2   
3   1 Y 1 A THR 3   ? A THR 3   
4   1 Y 1 A LEU 4   ? A LEU 4   
5   1 Y 1 A ALA 5   ? A ALA 5   
6   1 Y 1 A ALA 6   ? A ALA 6   
7   1 Y 1 A PRO 7   ? A PRO 7   
8   1 Y 1 A PRO 8   ? A PRO 8   
9   1 Y 1 A PRO 9   ? A PRO 9   
10  1 Y 1 A PRO 10  ? A PRO 10  
11  1 Y 1 A LEU 11  ? A LEU 11  
12  1 Y 1 A GLY 12  ? A GLY 12  
13  1 Y 1 A GLU 13  ? A GLU 13  
14  1 Y 1 A SER 14  ? A SER 14  
15  1 Y 1 A PRO 102 ? A PRO 102 
16  1 Y 1 A ILE 103 ? A ILE 103 
17  1 Y 1 A ALA 104 ? A ALA 104 
18  1 Y 1 A THR 105 ? A THR 105 
19  1 Y 1 A GLY 106 ? A GLY 106 
20  1 Y 1 A LYS 107 ? A LYS 107 
21  1 Y 1 A LEU 108 ? A LEU 108 
22  1 Y 1 A MET 109 ? A MET 109 
23  1 Y 1 A THR 110 ? A THR 110 
24  1 Y 1 A ASN 111 ? A ASN 111 
25  1 Y 1 A GLN 112 ? A GLN 112 
26  1 Y 1 A GLY 113 ? A GLY 113 
27  1 Y 1 A SER 114 ? A SER 114 
28  1 Y 1 A GLU 168 ? A GLU 168 
29  1 Y 1 A GLY 169 ? A GLY 169 
30  1 Y 1 A THR 170 ? A THR 170 
31  1 Y 1 A GLN 171 ? A GLN 171 
32  1 Y 1 A PRO 172 ? A PRO 172 
33  1 Y 1 A MET 173 ? A MET 173 
34  1 Y 1 A PRO 174 ? A PRO 174 
35  1 Y 1 A SER 175 ? A SER 175 
36  1 Y 1 A PRO 176 ? A PRO 176 
37  1 Y 1 A VAL 177 ? A VAL 177 
38  1 Y 1 A PRO 178 ? A PRO 178 
39  1 Y 1 A GLY 179 ? A GLY 179 
40  1 Y 1 A LYS 180 ? A LYS 180 
41  1 Y 1 A LEU 181 ? A LEU 181 
42  1 Y 1 A SER 182 ? A SER 182 
43  1 Y 1 A SER 183 ? A SER 183 
44  1 Y 1 A SER 213 ? A SER 213 
45  1 Y 1 A THR 214 ? A THR 214 
46  1 Y 1 A PRO 215 ? A PRO 215 
47  1 Y 1 A ILE 216 ? A ILE 216 
48  1 Y 1 A SER 217 ? A SER 217 
49  1 Y 1 A ARG 218 ? A ARG 218 
50  1 Y 1 A MET 219 ? A MET 219 
51  1 Y 1 A ILE 220 ? A ILE 220 
52  1 Y 1 A ALA 221 ? A ALA 221 
53  1 Y 1 A GLU 222 ? A GLU 222 
54  1 Y 1 A GLN 223 ? A GLN 223 
55  1 Y 1 A GLY 224 ? A GLY 224 
56  1 Y 1 B MET 1   ? B MET 1   
57  1 Y 1 B ALA 2   ? B ALA 2   
58  1 Y 1 B THR 3   ? B THR 3   
59  1 Y 1 B LEU 4   ? B LEU 4   
60  1 Y 1 B ALA 5   ? B ALA 5   
61  1 Y 1 B ALA 6   ? B ALA 6   
62  1 Y 1 B PRO 7   ? B PRO 7   
63  1 Y 1 B PRO 8   ? B PRO 8   
64  1 Y 1 B PRO 9   ? B PRO 9   
65  1 Y 1 B PRO 10  ? B PRO 10  
66  1 Y 1 B LEU 11  ? B LEU 11  
67  1 Y 1 B GLY 12  ? B GLY 12  
68  1 Y 1 B GLU 13  ? B GLU 13  
69  1 Y 1 B SER 14  ? B SER 14  
70  1 Y 1 B GLY 49  ? B GLY 49  
71  1 Y 1 B SER 50  ? B SER 50  
72  1 Y 1 B ILE 103 ? B ILE 103 
73  1 Y 1 B ALA 104 ? B ALA 104 
74  1 Y 1 B THR 105 ? B THR 105 
75  1 Y 1 B GLY 106 ? B GLY 106 
76  1 Y 1 B LYS 107 ? B LYS 107 
77  1 Y 1 B LEU 108 ? B LEU 108 
78  1 Y 1 B MET 109 ? B MET 109 
79  1 Y 1 B THR 110 ? B THR 110 
80  1 Y 1 B ASN 111 ? B ASN 111 
81  1 Y 1 B GLN 112 ? B GLN 112 
82  1 Y 1 B GLY 113 ? B GLY 113 
83  1 Y 1 B GLU 168 ? B GLU 168 
84  1 Y 1 B GLY 169 ? B GLY 169 
85  1 Y 1 B THR 170 ? B THR 170 
86  1 Y 1 B GLN 171 ? B GLN 171 
87  1 Y 1 B PRO 172 ? B PRO 172 
88  1 Y 1 B MET 173 ? B MET 173 
89  1 Y 1 B PRO 174 ? B PRO 174 
90  1 Y 1 B SER 175 ? B SER 175 
91  1 Y 1 B PRO 176 ? B PRO 176 
92  1 Y 1 B VAL 177 ? B VAL 177 
93  1 Y 1 B PRO 178 ? B PRO 178 
94  1 Y 1 B GLY 179 ? B GLY 179 
95  1 Y 1 B LYS 180 ? B LYS 180 
96  1 Y 1 B LEU 181 ? B LEU 181 
97  1 Y 1 B SER 182 ? B SER 182 
98  1 Y 1 B SER 183 ? B SER 183 
99  1 Y 1 B SER 213 ? B SER 213 
100 1 Y 1 B THR 214 ? B THR 214 
101 1 Y 1 B PRO 215 ? B PRO 215 
102 1 Y 1 B ILE 216 ? B ILE 216 
103 1 Y 1 B SER 217 ? B SER 217 
104 1 Y 1 B ARG 218 ? B ARG 218 
105 1 Y 1 B MET 219 ? B MET 219 
106 1 Y 1 B ILE 220 ? B ILE 220 
107 1 Y 1 B ALA 221 ? B ALA 221 
108 1 Y 1 B GLU 222 ? B GLU 222 
109 1 Y 1 B GLN 223 ? B GLN 223 
110 1 Y 1 B GLY 224 ? B GLY 224 
111 1 Y 1 C MET 1   ? C MET 1   
112 1 Y 1 C ALA 2   ? C ALA 2   
113 1 Y 1 C THR 3   ? C THR 3   
114 1 Y 1 C LEU 4   ? C LEU 4   
115 1 Y 1 C ALA 5   ? C ALA 5   
116 1 Y 1 C ALA 6   ? C ALA 6   
117 1 Y 1 C PRO 7   ? C PRO 7   
118 1 Y 1 C PRO 8   ? C PRO 8   
119 1 Y 1 C PRO 9   ? C PRO 9   
120 1 Y 1 C PRO 10  ? C PRO 10  
121 1 Y 1 C LEU 11  ? C LEU 11  
122 1 Y 1 C GLY 12  ? C GLY 12  
123 1 Y 1 C GLU 13  ? C GLU 13  
124 1 Y 1 C SER 14  ? C SER 14  
125 1 Y 1 C ALA 104 ? C ALA 104 
126 1 Y 1 C THR 105 ? C THR 105 
127 1 Y 1 C GLY 106 ? C GLY 106 
128 1 Y 1 C LYS 107 ? C LYS 107 
129 1 Y 1 C LEU 108 ? C LEU 108 
130 1 Y 1 C MET 109 ? C MET 109 
131 1 Y 1 C THR 110 ? C THR 110 
132 1 Y 1 C ASN 111 ? C ASN 111 
133 1 Y 1 C GLN 112 ? C GLN 112 
134 1 Y 1 C GLU 168 ? C GLU 168 
135 1 Y 1 C GLY 169 ? C GLY 169 
136 1 Y 1 C THR 170 ? C THR 170 
137 1 Y 1 C GLN 171 ? C GLN 171 
138 1 Y 1 C PRO 172 ? C PRO 172 
139 1 Y 1 C MET 173 ? C MET 173 
140 1 Y 1 C PRO 174 ? C PRO 174 
141 1 Y 1 C SER 175 ? C SER 175 
142 1 Y 1 C PRO 176 ? C PRO 176 
143 1 Y 1 C VAL 177 ? C VAL 177 
144 1 Y 1 C PRO 178 ? C PRO 178 
145 1 Y 1 C GLY 179 ? C GLY 179 
146 1 Y 1 C LYS 180 ? C LYS 180 
147 1 Y 1 C LEU 181 ? C LEU 181 
148 1 Y 1 C SER 182 ? C SER 182 
149 1 Y 1 C SER 183 ? C SER 183 
150 1 Y 1 C SER 213 ? C SER 213 
151 1 Y 1 C THR 214 ? C THR 214 
152 1 Y 1 C PRO 215 ? C PRO 215 
153 1 Y 1 C ILE 216 ? C ILE 216 
154 1 Y 1 C SER 217 ? C SER 217 
155 1 Y 1 C ARG 218 ? C ARG 218 
156 1 Y 1 C MET 219 ? C MET 219 
157 1 Y 1 C ILE 220 ? C ILE 220 
158 1 Y 1 C ALA 221 ? C ALA 221 
159 1 Y 1 C GLU 222 ? C GLU 222 
160 1 Y 1 C GLN 223 ? C GLN 223 
161 1 Y 1 C GLY 224 ? C GLY 224 
162 1 Y 1 D MET 1   ? D MET 1   
163 1 Y 1 D ALA 2   ? D ALA 2   
164 1 Y 1 D THR 3   ? D THR 3   
165 1 Y 1 D LEU 4   ? D LEU 4   
166 1 Y 1 D ALA 5   ? D ALA 5   
167 1 Y 1 D ALA 6   ? D ALA 6   
168 1 Y 1 D PRO 7   ? D PRO 7   
169 1 Y 1 D PRO 8   ? D PRO 8   
170 1 Y 1 D PRO 9   ? D PRO 9   
171 1 Y 1 D PRO 10  ? D PRO 10  
172 1 Y 1 D LEU 11  ? D LEU 11  
173 1 Y 1 D GLY 12  ? D GLY 12  
174 1 Y 1 D GLU 13  ? D GLU 13  
175 1 Y 1 D SER 14  ? D SER 14  
176 1 Y 1 D ALA 104 ? D ALA 104 
177 1 Y 1 D THR 105 ? D THR 105 
178 1 Y 1 D GLY 106 ? D GLY 106 
179 1 Y 1 D LYS 107 ? D LYS 107 
180 1 Y 1 D LEU 108 ? D LEU 108 
181 1 Y 1 D MET 109 ? D MET 109 
182 1 Y 1 D THR 110 ? D THR 110 
183 1 Y 1 D ASN 111 ? D ASN 111 
184 1 Y 1 D GLN 112 ? D GLN 112 
185 1 Y 1 D GLY 113 ? D GLY 113 
186 1 Y 1 D SER 114 ? D SER 114 
187 1 Y 1 D GLU 168 ? D GLU 168 
188 1 Y 1 D GLY 169 ? D GLY 169 
189 1 Y 1 D THR 170 ? D THR 170 
190 1 Y 1 D GLN 171 ? D GLN 171 
191 1 Y 1 D PRO 172 ? D PRO 172 
192 1 Y 1 D MET 173 ? D MET 173 
193 1 Y 1 D PRO 174 ? D PRO 174 
194 1 Y 1 D SER 175 ? D SER 175 
195 1 Y 1 D PRO 176 ? D PRO 176 
196 1 Y 1 D VAL 177 ? D VAL 177 
197 1 Y 1 D PRO 178 ? D PRO 178 
198 1 Y 1 D GLY 179 ? D GLY 179 
199 1 Y 1 D LYS 180 ? D LYS 180 
200 1 Y 1 D LEU 181 ? D LEU 181 
201 1 Y 1 D SER 182 ? D SER 182 
202 1 Y 1 D SER 183 ? D SER 183 
203 1 Y 1 D SER 213 ? D SER 213 
204 1 Y 1 D THR 214 ? D THR 214 
205 1 Y 1 D PRO 215 ? D PRO 215 
206 1 Y 1 D ILE 216 ? D ILE 216 
207 1 Y 1 D SER 217 ? D SER 217 
208 1 Y 1 D ARG 218 ? D ARG 218 
209 1 Y 1 D MET 219 ? D MET 219 
210 1 Y 1 D ILE 220 ? D ILE 220 
211 1 Y 1 D ALA 221 ? D ALA 221 
212 1 Y 1 D GLU 222 ? D GLU 222 
213 1 Y 1 D GLN 223 ? D GLN 223 
214 1 Y 1 D GLY 224 ? D GLY 224 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TYR N    N N N 321 
TYR CA   C N S 322 
TYR C    C N N 323 
TYR O    O N N 324 
TYR CB   C N N 325 
TYR CG   C Y N 326 
TYR CD1  C Y N 327 
TYR CD2  C Y N 328 
TYR CE1  C Y N 329 
TYR CE2  C Y N 330 
TYR CZ   C Y N 331 
TYR OH   O N N 332 
TYR OXT  O N N 333 
TYR H    H N N 334 
TYR H2   H N N 335 
TYR HA   H N N 336 
TYR HB2  H N N 337 
TYR HB3  H N N 338 
TYR HD1  H N N 339 
TYR HD2  H N N 340 
TYR HE1  H N N 341 
TYR HE2  H N N 342 
TYR HH   H N N 343 
TYR HXT  H N N 344 
VAL N    N N N 345 
VAL CA   C N S 346 
VAL C    C N N 347 
VAL O    O N N 348 
VAL CB   C N N 349 
VAL CG1  C N N 350 
VAL CG2  C N N 351 
VAL OXT  O N N 352 
VAL H    H N N 353 
VAL H2   H N N 354 
VAL HA   H N N 355 
VAL HB   H N N 356 
VAL HG11 H N N 357 
VAL HG12 H N N 358 
VAL HG13 H N N 359 
VAL HG21 H N N 360 
VAL HG22 H N N 361 
VAL HG23 H N N 362 
VAL HXT  H N N 363 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TYR N   CA   sing N N 306 
TYR N   H    sing N N 307 
TYR N   H2   sing N N 308 
TYR CA  C    sing N N 309 
TYR CA  CB   sing N N 310 
TYR CA  HA   sing N N 311 
TYR C   O    doub N N 312 
TYR C   OXT  sing N N 313 
TYR CB  CG   sing N N 314 
TYR CB  HB2  sing N N 315 
TYR CB  HB3  sing N N 316 
TYR CG  CD1  doub Y N 317 
TYR CG  CD2  sing Y N 318 
TYR CD1 CE1  sing Y N 319 
TYR CD1 HD1  sing N N 320 
TYR CD2 CE2  doub Y N 321 
TYR CD2 HD2  sing N N 322 
TYR CE1 CZ   doub Y N 323 
TYR CE1 HE1  sing N N 324 
TYR CE2 CZ   sing Y N 325 
TYR CE2 HE2  sing N N 326 
TYR CZ  OH   sing N N 327 
TYR OH  HH   sing N N 328 
TYR OXT HXT  sing N N 329 
VAL N   CA   sing N N 330 
VAL N   H    sing N N 331 
VAL N   H2   sing N N 332 
VAL CA  C    sing N N 333 
VAL CA  CB   sing N N 334 
VAL CA  HA   sing N N 335 
VAL C   O    doub N N 336 
VAL C   OXT  sing N N 337 
VAL CB  CG1  sing N N 338 
VAL CB  CG2  sing N N 339 
VAL CB  HB   sing N N 340 
VAL CG1 HG11 sing N N 341 
VAL CG1 HG12 sing N N 342 
VAL CG1 HG13 sing N N 343 
VAL CG2 HG21 sing N N 344 
VAL CG2 HG22 sing N N 345 
VAL CG2 HG23 sing N N 346 
VAL OXT HXT  sing N N 347 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4n6q 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9I2S 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009430 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006407 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.018965 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 15  ? -14.64616 16.56573  -10.93591 1.000 102.46819 ? 15  GLY A N   1 
ATOM   2    C CA  . GLY A 1 15  ? -15.12863 15.23599  -11.26352 1.000 113.24706 ? 15  GLY A CA  1 
ATOM   3    C C   . GLY A 1 15  ? -16.16372 15.23572  -12.37096 1.000 111.37487 ? 15  GLY A C   1 
ATOM   4    O O   . GLY A 1 15  ? -16.96147 14.30557  -12.49799 1.000 106.03100 ? 15  GLY A O   1 
ATOM   5    N N   . ASN A 1 16  ? -16.14815 16.29271  -13.17647 1.000 101.97415 ? 16  ASN A N   1 
ATOM   6    C CA  . ASN A 1 16  ? -17.09759 16.46105  -14.26588 1.000 86.51038  ? 16  ASN A CA  1 
ATOM   7    C C   . ASN A 1 16  ? -16.57932 15.93081  -15.59657 1.000 77.65781  ? 16  ASN A C   1 
ATOM   8    O O   . ASN A 1 16  ? -17.32598 15.94129  -16.58170 1.000 70.90479  ? 16  ASN A O   1 
ATOM   9    C CB  . ASN A 1 16  ? -17.46710 17.94311  -14.40885 1.000 102.57188 ? 16  ASN A CB  1 
ATOM   10   C CG  . ASN A 1 16  ? -16.24560 18.84008  -14.54058 1.000 115.46581 ? 16  ASN A CG  1 
ATOM   11   O OD1 . ASN A 1 16  ? -15.32885 18.79154  -13.71601 1.000 108.25245 ? 16  ASN A OD1 1 
ATOM   12   N ND2 . ASN A 1 16  ? -16.23109 19.66929  -15.57986 1.000 114.14212 ? 16  ASN A ND2 1 
ATOM   13   N N   . SER A 1 17  ? -15.33560 15.45492  -15.65325 1.000 79.59382  ? 17  SER A N   1 
ATOM   14   C CA  . SER A 1 17  ? -14.69943 15.15767  -16.92782 1.000 81.98960  ? 17  SER A CA  1 
ATOM   15   C C   . SER A 1 17  ? -13.88507 13.87582  -16.82941 1.000 70.90663  ? 17  SER A C   1 
ATOM   16   O O   . SER A 1 17  ? -13.51451 13.42402  -15.74386 1.000 71.98949  ? 17  SER A O   1 
ATOM   17   C CB  . SER A 1 17  ? -13.80046 16.31983  -17.40058 1.000 74.89143  ? 17  SER A CB  1 
ATOM   18   O OG  . SER A 1 17  ? -12.46243 16.18717  -16.94802 1.000 84.42488  ? 17  SER A OG  1 
ATOM   19   N N   . ASN A 1 18  ? -13.63271 13.28332  -17.99299 1.000 69.70946  ? 18  ASN A N   1 
ATOM   20   C CA  . ASN A 1 18  ? -12.75950 12.12747  -18.11245 1.000 68.30987  ? 18  ASN A CA  1 
ATOM   21   C C   . ASN A 1 18  ? -12.18026 12.10931  -19.51598 1.000 65.29869  ? 18  ASN A C   1 
ATOM   22   O O   . ASN A 1 18  ? -12.83111 12.53454  -20.47384 1.000 66.48163  ? 18  ASN A O   1 
ATOM   23   C CB  . ASN A 1 18  ? -13.51219 10.82328  -17.83044 1.000 64.77490  ? 18  ASN A CB  1 
ATOM   24   C CG  . ASN A 1 18  ? -12.58956 9.63127   -17.72315 1.000 69.34632  ? 18  ASN A CG  1 
ATOM   25   O OD1 . ASN A 1 18  ? -11.48089 9.73214   -17.19568 1.000 65.55474  ? 18  ASN A OD1 1 
ATOM   26   N ND2 . ASN A 1 18  ? -13.04671 8.48699   -18.21975 1.000 60.04574  ? 18  ASN A ND2 1 
ATOM   27   N N   . SER A 1 19  ? -10.94987 11.61937  -19.63355 1.000 74.70407  ? 19  SER A N   1 
ATOM   28   C CA  . SER A 1 19  ? -10.27755 11.60330  -20.92211 1.000 79.92942  ? 19  SER A CA  1 
ATOM   29   C C   . SER A 1 19  ? -9.59574  10.26355  -21.15620 1.000 81.49488  ? 19  SER A C   1 
ATOM   30   O O   . SER A 1 19  ? -9.15581  9.59887   -20.21442 1.000 73.87373  ? 19  SER A O   1 
ATOM   31   C CB  . SER A 1 19  ? -9.24710  12.72986  -21.02917 1.000 76.53728  ? 19  SER A CB  1 
ATOM   32   O OG  . SER A 1 19  ? -8.41940  12.75318  -19.88221 1.000 108.20885 ? 19  SER A OG  1 
ATOM   33   N N   . VAL A 1 20  ? -9.51576  9.87245   -22.42921 1.000 72.81019  ? 20  VAL A N   1 
ATOM   34   C CA  . VAL A 1 20  ? -8.81820  8.66116   -22.82773 1.000 67.22122  ? 20  VAL A CA  1 
ATOM   35   C C   . VAL A 1 20  ? -7.95193  8.99265   -24.03744 1.000 68.16212  ? 20  VAL A C   1 
ATOM   36   O O   . VAL A 1 20  ? -8.18033  9.97622   -24.74307 1.000 80.67538  ? 20  VAL A O   1 
ATOM   37   C CB  . VAL A 1 20  ? -9.78943  7.50211   -23.14760 1.000 65.30161  ? 20  VAL A CB  1 
ATOM   38   C CG1 . VAL A 1 20  ? -10.24326 7.56877   -24.59919 1.000 74.19181  ? 20  VAL A CG1 1 
ATOM   39   C CG2 . VAL A 1 20  ? -9.13986  6.15876   -22.84407 1.000 70.49663  ? 20  VAL A CG2 1 
ATOM   40   N N   . SER A 1 21  ? -6.94806  8.15159   -24.27601 1.000 81.76752  ? 21  SER A N   1 
ATOM   41   C CA  . SER A 1 21  ? -6.02746  8.35226   -25.38495 1.000 80.42039  ? 21  SER A CA  1 
ATOM   42   C C   . SER A 1 21  ? -5.78929  7.02490   -26.08928 1.000 85.73827  ? 21  SER A C   1 
ATOM   43   O O   . SER A 1 21  ? -5.81055  5.95795   -25.46860 1.000 81.50710  ? 21  SER A O   1 
ATOM   44   C CB  . SER A 1 21  ? -4.69295  8.96063   -24.92598 1.000 85.26542  ? 21  SER A CB  1 
ATOM   45   O OG  . SER A 1 21  ? -4.33196  8.50744   -23.63368 1.000 96.04801  ? 21  SER A OG  1 
ATOM   46   N N   . ARG A 1 22  ? -5.57060  7.10565   -27.39710 1.000 86.19297  ? 22  ARG A N   1 
ATOM   47   C CA  . ARG A 1 22  ? -5.23891  5.94605   -28.21053 1.000 86.35524  ? 22  ARG A CA  1 
ATOM   48   C C   . ARG A 1 22  ? -4.29691  6.38647   -29.32475 1.000 88.76670  ? 22  ARG A C   1 
ATOM   49   O O   . ARG A 1 22  ? -4.08686  7.58102   -29.55440 1.000 85.10622  ? 22  ARG A O   1 
ATOM   50   C CB  . ARG A 1 22  ? -6.50147  5.28358   -28.77077 1.000 75.95499  ? 22  ARG A CB  1 
ATOM   51   C CG  . ARG A 1 22  ? -6.86420  5.82014   -30.13188 1.000 85.54827  ? 22  ARG A CG  1 
ATOM   52   C CD  . ARG A 1 22  ? -8.21352  5.36919   -30.62421 1.000 82.58998  ? 22  ARG A CD  1 
ATOM   53   N NE  . ARG A 1 22  ? -8.72595  6.32905   -31.59195 1.000 82.75502  ? 22  ARG A NE  1 
ATOM   54   C CZ  . ARG A 1 22  ? -8.94191  6.05806   -32.87027 1.000 92.82960  ? 22  ARG A CZ  1 
ATOM   55   N NH1 . ARG A 1 22  ? -8.73613  4.84883   -33.36398 1.000 91.88988  ? 22  ARG A NH1 1 
ATOM   56   N NH2 . ARG A 1 22  ? -9.37630  7.02432   -33.67362 1.000 99.90112  ? 22  ARG A NH2 1 
ATOM   57   N N   . ILE A 1 23  ? -3.72780  5.40752   -30.02347 1.000 85.17863  ? 23  ILE A N   1 
ATOM   58   C CA  . ILE A 1 23  ? -2.73749  5.66774   -31.05892 1.000 89.07902  ? 23  ILE A CA  1 
ATOM   59   C C   . ILE A 1 23  ? -3.21709  5.00907   -32.34577 1.000 89.66339  ? 23  ILE A C   1 
ATOM   60   O O   . ILE A 1 23  ? -3.57120  3.82540   -32.34721 1.000 96.84979  ? 23  ILE A O   1 
ATOM   61   C CB  . ILE A 1 23  ? -1.34603  5.14375   -30.65582 1.000 104.23133 ? 23  ILE A CB  1 
ATOM   62   C CG1 . ILE A 1 23  ? -0.63918  6.15544   -29.75252 1.000 103.68089 ? 23  ILE A CG1 1 
ATOM   63   C CG2 . ILE A 1 23  ? -0.49927  4.88100   -31.88495 1.000 99.18704  ? 23  ILE A CG2 1 
ATOM   64   C CD1 . ILE A 1 23  ? 0.19698   5.51664   -28.66282 1.000 92.61568  ? 23  ILE A CD1 1 
ATOM   65   N N   . THR A 1 24  ? -3.24210  5.77634   -33.43102 1.000 97.21408  ? 24  THR A N   1 
ATOM   66   C CA  . THR A 1 24  ? -3.74485  5.29520   -34.70748 1.000 103.15138 ? 24  THR A CA  1 
ATOM   67   C C   . THR A 1 24  ? -2.63346  4.60624   -35.49119 1.000 111.71365 ? 24  THR A C   1 
ATOM   68   O O   . THR A 1 24  ? -1.46632  4.59743   -35.09554 1.000 111.52855 ? 24  THR A O   1 
ATOM   69   C CB  . THR A 1 24  ? -4.32610  6.43346   -35.53967 1.000 102.09911 ? 24  THR A CB  1 
ATOM   70   O OG1 . THR A 1 24  ? -3.31187  7.41318   -35.76598 1.000 110.72965 ? 24  THR A OG1 1 
ATOM   71   C CG2 . THR A 1 24  ? -5.48170  7.08280   -34.80378 1.000 97.69111  ? 24  THR A CG2 1 
ATOM   72   N N   . ARG A 1 25  ? -3.01332  4.03442   -36.63450 1.000 108.95530 ? 25  ARG A N   1 
ATOM   73   C CA  . ARG A 1 25  ? -2.04747  3.31405   -37.45334 1.000 110.51617 ? 25  ARG A CA  1 
ATOM   74   C C   . ARG A 1 25  ? -0.97650  4.24291   -38.01042 1.000 121.59206 ? 25  ARG A C   1 
ATOM   75   O O   . ARG A 1 25  ? 0.17163   3.82194   -38.19326 1.000 133.41503 ? 25  ARG A O   1 
ATOM   76   C CB  . ARG A 1 25  ? -2.77667  2.59540   -38.58562 1.000 126.90042 ? 25  ARG A CB  1 
ATOM   77   C CG  . ARG A 1 25  ? -3.72009  1.51508   -38.09244 1.000 136.25799 ? 25  ARG A CG  1 
ATOM   78   C CD  . ARG A 1 25  ? -4.51305  0.89633   -39.22593 1.000 144.26371 ? 25  ARG A CD  1 
ATOM   79   N NE  . ARG A 1 25  ? -5.37689  -0.17529  -38.74533 1.000 154.77796 ? 25  ARG A NE  1 
ATOM   80   C CZ  . ARG A 1 25  ? -6.45278  -0.61605  -39.38275 1.000 164.50829 ? 25  ARG A CZ  1 
ATOM   81   N NH1 . ARG A 1 25  ? -6.81649  -0.11648  -40.55262 1.000 167.77227 ? 25  ARG A NH1 1 
ATOM   82   N NH2 . ARG A 1 25  ? -7.17921  -1.58637  -38.83486 1.000 165.85359 ? 25  ARG A NH2 1 
ATOM   83   N N   . GLU A 1 26  ? -1.32492  5.49790   -38.28735 1.000 126.46738 ? 26  GLU A N   1 
ATOM   84   C CA  . GLU A 1 26  ? -0.36916  6.47461   -38.79522 1.000 127.87008 ? 26  GLU A CA  1 
ATOM   85   C C   . GLU A 1 26  ? 0.55178   7.02966   -37.71049 1.000 121.68943 ? 26  GLU A C   1 
ATOM   86   O O   . GLU A 1 26  ? 1.29942   7.97573   -37.98291 1.000 107.75311 ? 26  GLU A O   1 
ATOM   87   C CB  . GLU A 1 26  ? -1.11309  7.62896   -39.47352 1.000 141.25521 ? 26  GLU A CB  1 
ATOM   88   C CG  . GLU A 1 26  ? -2.19074  7.19353   -40.45410 1.000 149.94566 ? 26  GLU A CG  1 
ATOM   89   C CD  . GLU A 1 26  ? -2.24074  8.06919   -41.69302 1.000 162.93131 ? 26  GLU A CD  1 
ATOM   90   O OE1 . GLU A 1 26  ? -1.45392  7.82361   -42.63264 1.000 163.93277 ? 26  GLU A OE1 1 
ATOM   91   O OE2 . GLU A 1 26  ? -3.06750  9.00536   -41.72520 1.000 162.38018 ? 26  GLU A OE2 1 
ATOM   92   N N   . GLY A 1 27  ? 0.52503   6.46087   -36.50459 1.000 115.64676 ? 27  GLY A N   1 
ATOM   93   C CA  . GLY A 1 27  ? 1.29781   6.95355   -35.38101 1.000 115.18437 ? 27  GLY A CA  1 
ATOM   94   C C   . GLY A 1 27  ? 0.67401   8.11655   -34.63728 1.000 123.74271 ? 27  GLY A C   1 
ATOM   95   O O   . GLY A 1 27  ? 1.27036   8.60372   -33.66714 1.000 117.97719 ? 27  GLY A O   1 
ATOM   96   N N   . LYS A 1 28  ? -0.50868  8.56198   -35.05282 1.000 109.17088 ? 28  LYS A N   1 
ATOM   97   C CA  . LYS A 1 28  ? -1.17515  9.70634   -34.44621 1.000 110.89338 ? 28  LYS A CA  1 
ATOM   98   C C   . LYS A 1 28  ? -1.70127  9.33669   -33.06276 1.000 98.58329  ? 28  LYS A C   1 
ATOM   99   O O   . LYS A 1 28  ? -2.24049  8.24770   -32.85853 1.000 98.07690  ? 28  LYS A O   1 
ATOM   100  C CB  . LYS A 1 28  ? -2.31579  10.17613  -35.34864 1.000 113.81931 ? 28  LYS A CB  1 
ATOM   101  C CG  . LYS A 1 28  ? -1.88221  11.00697  -36.54769 1.000 115.12530 ? 28  LYS A CG  1 
ATOM   102  C CD  . LYS A 1 28  ? -3.02353  11.12469  -37.55562 1.000 128.79032 ? 28  LYS A CD  1 
ATOM   103  C CE  . LYS A 1 28  ? -3.61301  12.52027  -37.60591 1.000 122.41507 ? 28  LYS A CE  1 
ATOM   104  N NZ  . LYS A 1 28  ? -3.78045  13.03900  -38.99327 1.000 123.80525 ? 28  LYS A NZ  1 
ATOM   105  N N   . LYS A 1 29  ? -1.54451  10.24645  -32.10760 1.000 105.90036 ? 29  LYS A N   1 
ATOM   106  C CA  . LYS A 1 29  ? -2.07879  10.06573  -30.76107 1.000 93.31264  ? 29  LYS A CA  1 
ATOM   107  C C   . LYS A 1 29  ? -3.34177  10.90748  -30.61697 1.000 87.39760  ? 29  LYS A C   1 
ATOM   108  O O   . LYS A 1 29  ? -3.28026  12.14072  -30.61439 1.000 90.86228  ? 29  LYS A O   1 
ATOM   109  C CB  . LYS A 1 29  ? -1.05145  10.45370  -29.70257 1.000 91.40543  ? 29  LYS A CB  1 
ATOM   110  C CG  . LYS A 1 29  ? -1.56758  10.31511  -28.28149 1.000 78.27897  ? 29  LYS A CG  1 
ATOM   111  C CD  . LYS A 1 29  ? -0.56981  10.87870  -27.29234 1.000 106.06335 ? 29  LYS A CD  1 
ATOM   112  C CE  . LYS A 1 29  ? -0.80234  10.34471  -25.89170 1.000 112.68358 ? 29  LYS A CE  1 
ATOM   113  N NZ  . LYS A 1 29  ? -0.14502  11.21608  -24.87582 1.000 122.30518 ? 29  LYS A NZ  1 
ATOM   114  N N   . ILE A 1 30  ? -4.48110  10.23380  -30.48120 1.000 82.45647  ? 30  ILE A N   1 
ATOM   115  C CA  . ILE A 1 30  ? -5.79419  10.86518  -30.40970 1.000 76.04465  ? 30  ILE A CA  1 
ATOM   116  C C   . ILE A 1 30  ? -6.28294  10.78079  -28.97133 1.000 82.75975  ? 30  ILE A C   1 
ATOM   117  O O   . ILE A 1 30  ? -6.27498  9.70284   -28.36485 1.000 83.96778  ? 30  ILE A O   1 
ATOM   118  C CB  . ILE A 1 30  ? -6.80262  10.21577  -31.37657 1.000 64.48845  ? 30  ILE A CB  1 
ATOM   119  C CG1 . ILE A 1 30  ? -6.38624  10.39072  -32.84330 1.000 77.24024  ? 30  ILE A CG1 1 
ATOM   120  C CG2 . ILE A 1 30  ? -8.20252  10.77223  -31.14967 1.000 67.25232  ? 30  ILE A CG2 1 
ATOM   121  C CD1 . ILE A 1 30  ? -5.53432  11.61129  -33.13717 1.000 88.42363  ? 30  ILE A CD1 1 
ATOM   122  N N   . THR A 1 31  ? -6.69227  11.92179  -28.42562 1.000 80.61847  ? 31  THR A N   1 
ATOM   123  C CA  . THR A 1 31  ? -7.23239  12.01837  -27.07711 1.000 77.99639  ? 31  THR A CA  1 
ATOM   124  C C   . THR A 1 31  ? -8.69732  12.43082  -27.14387 1.000 69.74514  ? 31  THR A C   1 
ATOM   125  O O   . THR A 1 31  ? -9.04647  13.39436  -27.83500 1.000 72.78004  ? 31  THR A O   1 
ATOM   126  C CB  . THR A 1 31  ? -6.43605  13.02834  -26.23992 1.000 84.17613  ? 31  THR A CB  1 
ATOM   127  O OG1 . THR A 1 31  ? -5.03945  12.94057  -26.56166 1.000 86.81887  ? 31  THR A OG1 1 
ATOM   128  C CG2 . THR A 1 31  ? -6.62955  12.77736  -24.75479 1.000 77.27599  ? 31  THR A CG2 1 
ATOM   129  N N   . TYR A 1 32  ? -9.54739  11.68506  -26.44103 1.000 62.15417  ? 32  TYR A N   1 
ATOM   130  C CA  . TYR A 1 32  ? -10.96616 11.98889  -26.30641 1.000 59.95248  ? 32  TYR A CA  1 
ATOM   131  C C   . TYR A 1 32  ? -11.21889 12.53989  -24.91391 1.000 69.14547  ? 32  TYR A C   1 
ATOM   132  O O   . TYR A 1 32  ? -10.77270 11.95501  -23.92411 1.000 72.49919  ? 32  TYR A O   1 
ATOM   133  C CB  . TYR A 1 32  ? -11.83686 10.74207  -26.53539 1.000 61.04303  ? 32  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 32  ? -11.59270 10.04455  -27.85431 1.000 60.16042  ? 32  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 32  ? -10.54887 9.14174   -28.01008 1.000 60.81220  ? 32  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 32  ? -12.41527 10.28809  -28.94571 1.000 65.10002  ? 32  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 32  ? -10.32319 8.51484   -29.22321 1.000 64.68370  ? 32  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 32  ? -12.20217 9.66213   -30.15811 1.000 69.10707  ? 32  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 32  ? -11.15483 8.77537   -30.29240 1.000 65.41020  ? 32  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 32  ? -10.93893 8.15400   -31.50378 1.000 66.93113  ? 32  TYR A OH  1 
ATOM   141  N N   . LYS A 1 33  ? -11.91812 13.66965  -24.84173 1.000 61.23766  ? 33  LYS A N   1 
ATOM   142  C CA  . LYS A 1 33  ? -12.24621 14.29337  -23.57050 1.000 65.16411  ? 33  LYS A CA  1 
ATOM   143  C C   . LYS A 1 33  ? -13.75235 14.49051  -23.50083 1.000 67.68615  ? 33  LYS A C   1 
ATOM   144  O O   . LYS A 1 33  ? -14.34947 15.06321  -24.41655 1.000 73.18276  ? 33  LYS A O   1 
ATOM   145  C CB  . LYS A 1 33  ? -11.50951 15.62352  -23.39901 1.000 72.83045  ? 33  LYS A CB  1 
ATOM   146  C CG  . LYS A 1 33  ? -11.78090 16.34155  -22.08234 1.000 76.00403  ? 33  LYS A CG  1 
ATOM   147  C CD  . LYS A 1 33  ? -11.19350 17.75438  -22.11144 1.000 87.67718  ? 33  LYS A CD  1 
ATOM   148  C CE  . LYS A 1 33  ? -11.75742 18.64056  -21.00531 1.000 90.64380  ? 33  LYS A CE  1 
ATOM   149  N NZ  . LYS A 1 33  ? -10.69537 19.10517  -20.06071 1.000 95.13188  ? 33  LYS A NZ  1 
ATOM   150  N N   . LEU A 1 34  ? -14.36019 14.00272  -22.42485 1.000 69.53551  ? 34  LEU A N   1 
ATOM   151  C CA  . LEU A 1 34  ? -15.78789 14.14528  -22.17511 1.000 60.75323  ? 34  LEU A CA  1 
ATOM   152  C C   . LEU A 1 34  ? -15.95870 15.00785  -20.93904 1.000 58.51258  ? 34  LEU A C   1 
ATOM   153  O O   . LEU A 1 34  ? -15.29800 14.77454  -19.92254 1.000 67.58890  ? 34  LEU A O   1 
ATOM   154  C CB  . LEU A 1 34  ? -16.46965 12.79059  -21.95681 1.000 53.60258  ? 34  LEU A CB  1 
ATOM   155  C CG  . LEU A 1 34  ? -16.81595 11.93269  -23.16452 1.000 63.47488  ? 34  LEU A CG  1 
ATOM   156  C CD1 . LEU A 1 34  ? -17.51297 10.65453  -22.72214 1.000 47.43346  ? 34  LEU A CD1 1 
ATOM   157  C CD2 . LEU A 1 34  ? -17.69815 12.73178  -24.09581 1.000 60.42169  ? 34  LEU A CD2 1 
ATOM   158  N N   . ASN A 1 35  ? -16.85171 15.98726  -21.02124 1.000 59.92127  ? 35  ASN A N   1 
ATOM   159  C CA  . ASN A 1 35  ? -17.07913 16.91458  -19.92272 1.000 57.11325  ? 35  ASN A CA  1 
ATOM   160  C C   . ASN A 1 35  ? -18.57014 17.14057  -19.76061 1.000 65.48812  ? 35  ASN A C   1 
ATOM   161  O O   . ASN A 1 35  ? -19.24636 17.52765  -20.71810 1.000 57.18338  ? 35  ASN A O   1 
ATOM   162  C CB  . ASN A 1 35  ? -16.36751 18.24460  -20.18908 1.000 79.18246  ? 35  ASN A CB  1 
ATOM   163  C CG  . ASN A 1 35  ? -15.88103 18.91289  -18.92560 1.000 86.85481  ? 35  ASN A CG  1 
ATOM   164  O OD1 . ASN A 1 35  ? -16.06197 18.39603  -17.82530 1.000 93.59185  ? 35  ASN A OD1 1 
ATOM   165  N ND2 . ASN A 1 35  ? -15.25516 20.07382  -19.07758 1.000 101.71212 ? 35  ASN A ND2 1 
ATOM   166  N N   . ILE A 1 36  ? -19.08153 16.86852  -18.56397 1.000 64.75984  ? 36  ILE A N   1 
ATOM   167  C CA  . ILE A 1 36  ? -20.48392 17.11407  -18.25215 1.000 61.93064  ? 36  ILE A CA  1 
ATOM   168  C C   . ILE A 1 36  ? -20.63783 18.58751  -17.89459 1.000 71.52108  ? 36  ILE A C   1 
ATOM   169  O O   . ILE A 1 36  ? -20.12716 19.03654  -16.86620 1.000 77.89509  ? 36  ILE A O   1 
ATOM   170  C CB  . ILE A 1 36  ? -20.96839 16.22493  -17.10492 1.000 63.30689  ? 36  ILE A CB  1 
ATOM   171  C CG1 . ILE A 1 36  ? -20.68859 14.75736  -17.40929 1.000 64.93524  ? 36  ILE A CG1 1 
ATOM   172  C CG2 . ILE A 1 36  ? -22.44656 16.48715  -16.81248 1.000 66.67293  ? 36  ILE A CG2 1 
ATOM   173  C CD1 . ILE A 1 36  ? -21.23157 13.83589  -16.36629 1.000 54.12273  ? 36  ILE A CD1 1 
ATOM   174  N N   . MET A 1 37  ? -21.32638 19.34768  -18.74078 1.000 66.07148  ? 37  MET A N   1 
ATOM   175  C CA  . MET A 1 37  ? -21.51352 20.75995  -18.43755 1.000 72.89766  ? 37  MET A CA  1 
ATOM   176  C C   . MET A 1 37  ? -22.82755 21.04679  -17.73210 1.000 78.57427  ? 37  MET A C   1 
ATOM   177  O O   . MET A 1 37  ? -22.89548 21.98901  -16.93659 1.000 86.69740  ? 37  MET A O   1 
ATOM   178  C CB  . MET A 1 37  ? -21.43223 21.61192  -19.70099 1.000 82.55475  ? 37  MET A CB  1 
ATOM   179  C CG  . MET A 1 37  ? -20.63173 21.00080  -20.80138 1.000 70.61232  ? 37  MET A CG  1 
ATOM   180  S SD  . MET A 1 37  ? -18.93752 21.48751  -20.48157 1.000 94.32054  ? 37  MET A SD  1 
ATOM   181  C CE  . MET A 1 37  ? -18.76845 22.86551  -21.60100 1.000 103.79846 ? 37  MET A CE  1 
ATOM   182  N N   . GLN A 1 38  ? -23.86299 20.24867  -17.98367 1.000 70.73237  ? 38  GLN A N   1 
ATOM   183  C CA  . GLN A 1 38  ? -25.15970 20.39937  -17.32711 1.000 65.33710  ? 38  GLN A CA  1 
ATOM   184  C C   . GLN A 1 38  ? -25.50618 19.09195  -16.62004 1.000 69.01101  ? 38  GLN A C   1 
ATOM   185  O O   . GLN A 1 38  ? -25.83123 18.09135  -17.26878 1.000 58.82909  ? 38  GLN A O   1 
ATOM   186  C CB  . GLN A 1 38  ? -26.23783 20.79849  -18.32640 1.000 68.50004  ? 38  GLN A CB  1 
ATOM   187  C CG  . GLN A 1 38  ? -27.60286 21.03312  -17.70292 1.000 71.24849  ? 38  GLN A CG  1 
ATOM   188  C CD  . GLN A 1 38  ? -28.37354 22.11234  -18.42677 1.000 76.57501  ? 38  GLN A CD  1 
ATOM   189  O OE1 . GLN A 1 38  ? -28.41683 23.26330  -17.99059 1.000 90.09729  ? 38  GLN A OE1 1 
ATOM   190  N NE2 . GLN A 1 38  ? -28.98370 21.74731  -19.54906 1.000 77.02590  ? 38  GLN A NE2 1 
ATOM   191  N N   . GLN A 1 39  ? -25.36275 19.08715  -15.29643 1.000 72.38127  ? 39  GLN A N   1 
ATOM   192  C CA  . GLN A 1 39  ? -25.65976 17.93254  -14.46755 1.000 74.49536  ? 39  GLN A CA  1 
ATOM   193  C C   . GLN A 1 39  ? -27.16323 17.82522  -14.20893 1.000 77.47611  ? 39  GLN A C   1 
ATOM   194  O O   . GLN A 1 39  ? -27.86472 18.83760  -14.13417 1.000 80.65251  ? 39  GLN A O   1 
ATOM   195  C CB  . GLN A 1 39  ? -24.92855 18.03940  -13.13330 1.000 75.57732  ? 39  GLN A CB  1 
ATOM   196  C CG  . GLN A 1 39  ? -23.41662 17.92271  -13.23683 1.000 89.70713  ? 39  GLN A CG  1 
ATOM   197  C CD  . GLN A 1 39  ? -22.91879 16.51452  -13.00815 1.000 80.63734  ? 39  GLN A CD  1 
ATOM   198  O OE1 . GLN A 1 39  ? -23.68481 15.62481  -12.63558 1.000 78.16226  ? 39  GLN A OE1 1 
ATOM   199  N NE2 . GLN A 1 39  ? -21.62453 16.30631  -13.21861 1.000 74.34120  ? 39  GLN A NE2 1 
ATOM   200  N N   . PRO A 1 40  ? -27.67678 16.60938  -14.05208 1.000 85.04729  ? 40  PRO A N   1 
ATOM   201  C CA  . PRO A 1 40  ? -29.05078 16.44912  -13.56397 1.000 71.45585  ? 40  PRO A CA  1 
ATOM   202  C C   . PRO A 1 40  ? -29.14511 16.79436  -12.08762 1.000 75.31879  ? 40  PRO A C   1 
ATOM   203  O O   . PRO A 1 40  ? -28.18672 16.63335  -11.32748 1.000 78.43576  ? 40  PRO A O   1 
ATOM   204  C CB  . PRO A 1 40  ? -29.33492 14.96432  -13.80311 1.000 85.40628  ? 40  PRO A CB  1 
ATOM   205  C CG  . PRO A 1 40  ? -27.97964 14.31757  -13.71819 1.000 73.62104  ? 40  PRO A CG  1 
ATOM   206  C CD  . PRO A 1 40  ? -27.01782 15.31606  -14.30931 1.000 75.86640  ? 40  PRO A CD  1 
ATOM   207  N N   . LYS A 1 41  ? -30.31619 17.26655  -11.67459 1.000 64.29989  ? 41  LYS A N   1 
ATOM   208  C CA  . LYS A 1 41  ? -30.49477 17.58942  -10.26388 1.000 81.31456  ? 41  LYS A CA  1 
ATOM   209  C C   . LYS A 1 41  ? -31.65206 16.84538  -9.61692  1.000 84.33816  ? 41  LYS A C   1 
ATOM   210  O O   . LYS A 1 41  ? -31.54962 16.44015  -8.45550  1.000 86.58135  ? 41  LYS A O   1 
ATOM   211  C CB  . LYS A 1 41  ? -30.72082 19.10049  -10.10652 1.000 78.50585  ? 41  LYS A CB  1 
ATOM   212  C CG  . LYS A 1 41  ? -29.90187 19.93626  -11.06942 1.000 95.72241  ? 41  LYS A CG  1 
ATOM   213  C CD  . LYS A 1 41  ? -28.85117 20.81147  -10.42535 1.000 103.42624 ? 41  LYS A CD  1 
ATOM   214  C CE  . LYS A 1 41  ? -27.99260 21.43071  -11.52472 1.000 109.92673 ? 41  LYS A CE  1 
ATOM   215  N NZ  . LYS A 1 41  ? -26.53065 21.35206  -11.25244 1.000 102.57898 ? 41  LYS A NZ  1 
ATOM   216  N N   . ARG A 1 42  ? -32.74996 16.64500  -10.34076 1.000 75.02663  ? 42  ARG A N   1 
ATOM   217  C CA  . ARG A 1 42  ? -33.98634 16.15274  -9.74988  1.000 71.25927  ? 42  ARG A CA  1 
ATOM   218  C C   . ARG A 1 42  ? -34.83207 15.51557  -10.83905 1.000 86.46308  ? 42  ARG A C   1 
ATOM   219  O O   . ARG A 1 42  ? -34.70141 15.83744  -12.02262 1.000 80.58968  ? 42  ARG A O   1 
ATOM   220  C CB  . ARG A 1 42  ? -34.79065 17.27787  -9.09185  1.000 92.84059  ? 42  ARG A CB  1 
ATOM   221  C CG  . ARG A 1 42  ? -34.96193 18.48293  -10.01537 1.000 92.65020  ? 42  ARG A CG  1 
ATOM   222  C CD  . ARG A 1 42  ? -35.47388 19.72333  -9.31159  1.000 93.93102  ? 42  ARG A CD  1 
ATOM   223  N NE  . ARG A 1 42  ? -36.23578 19.43429  -8.10282  1.000 98.82895  ? 42  ARG A NE  1 
ATOM   224  C CZ  . ARG A 1 42  ? -37.50432 19.04707  -8.09386  1.000 106.47270 ? 42  ARG A CZ  1 
ATOM   225  N NH1 . ARG A 1 42  ? -38.16799 18.82943  -9.21830  1.000 114.56229 ? 42  ARG A NH1 1 
ATOM   226  N NH2 . ARG A 1 42  ? -38.12425 18.87466  -6.92909  1.000 91.27483  ? 42  ARG A NH2 1 
ATOM   227  N N   . ALA A 1 43  ? -35.72889 14.63194  -10.41418 1.000 83.02059  ? 43  ALA A N   1 
ATOM   228  C CA  . ALA A 1 43  ? -36.70410 14.03894  -11.31464 1.000 85.43485  ? 43  ALA A CA  1 
ATOM   229  C C   . ALA A 1 43  ? -37.84765 13.50329  -10.47132 1.000 82.32092  ? 43  ALA A C   1 
ATOM   230  O O   . ALA A 1 43  ? -37.66457 13.17627  -9.29655  1.000 78.94799  ? 43  ALA A O   1 
ATOM   231  C CB  . ALA A 1 43  ? -36.09341 12.92019  -12.16713 1.000 88.47890  ? 43  ALA A CB  1 
ATOM   232  N N   . ARG A 1 44  ? -39.02785 13.42161  -11.07501 1.000 81.01510  ? 44  ARG A N   1 
ATOM   233  C CA  . ARG A 1 44  ? -40.19338 12.86192  -10.40697 1.000 91.82198  ? 44  ARG A CA  1 
ATOM   234  C C   . ARG A 1 44  ? -40.39140 11.44787  -10.93577 1.000 89.79062  ? 44  ARG A C   1 
ATOM   235  O O   . ARG A 1 44  ? -40.49167 11.24673  -12.15150 1.000 85.38500  ? 44  ARG A O   1 
ATOM   236  C CB  . ARG A 1 44  ? -41.44750 13.71226  -10.61739 1.000 76.55186  ? 44  ARG A CB  1 
ATOM   237  C CG  . ARG A 1 44  ? -42.66508 13.13820  -9.89594  1.000 89.73068  ? 44  ARG A CG  1 
ATOM   238  C CD  . ARG A 1 44  ? -43.92744 13.97247  -10.04879 1.000 103.50567 ? 44  ARG A CD  1 
ATOM   239  N NE  . ARG A 1 44  ? -44.65158 13.67593  -11.27858 1.000 117.30219 ? 44  ARG A NE  1 
ATOM   240  C CZ  . ARG A 1 44  ? -44.72962 14.49342  -12.31931 1.000 125.59526 ? 44  ARG A CZ  1 
ATOM   241  N NH1 . ARG A 1 44  ? -44.12840 15.67184  -12.31907 1.000 123.59345 ? 44  ARG A NH1 1 
ATOM   242  N NH2 . ARG A 1 44  ? -45.43263 14.12142  -13.38546 1.000 130.05130 ? 44  ARG A NH2 1 
ATOM   243  N N   . ALA A 1 45  ? -40.42554 10.47611  -10.02903 1.000 87.94530  ? 45  ALA A N   1 
ATOM   244  C CA  . ALA A 1 45  ? -40.59968 9.08547   -10.42612 1.000 91.05641  ? 45  ALA A CA  1 
ATOM   245  C C   . ALA A 1 45  ? -41.89314 8.92377   -11.21418 1.000 101.45896 ? 45  ALA A C   1 
ATOM   246  O O   . ALA A 1 45  ? -42.97624 9.26412   -10.72765 1.000 117.90922 ? 45  ALA A O   1 
ATOM   247  C CB  . ALA A 1 45  ? -40.60387 8.18655   -9.19211  1.000 96.33732  ? 45  ALA A CB  1 
ATOM   248  N N   . CYS A 1 46  ? -41.77325 8.40742   -12.43602 1.000 92.83412  ? 46  CYS A N   1 
ATOM   249  C CA  . CYS A 1 46  ? -42.89611 8.29210   -13.35684 1.000 99.33859  ? 46  CYS A CA  1 
ATOM   250  C C   . CYS A 1 46  ? -43.72418 7.02960   -13.15268 1.000 122.21209 ? 46  CYS A C   1 
ATOM   251  O O   . CYS A 1 46  ? -44.83875 6.95099   -13.68052 1.000 138.98420 ? 46  CYS A O   1 
ATOM   252  C CB  . CYS A 1 46  ? -42.39590 8.34298   -14.80546 1.000 101.86733 ? 46  CYS A CB  1 
ATOM   253  S SG  . CYS A 1 46  ? -41.05674 7.19464   -15.17802 1.000 97.41681  ? 46  CYS A SG  1 
ATOM   254  N N   . GLY A 1 47  ? -43.22054 6.05245   -12.40035 1.000 113.65588 ? 47  GLY A N   1 
ATOM   255  C CA  . GLY A 1 47  ? -43.95049 4.81401   -12.19819 1.000 120.37517 ? 47  GLY A CA  1 
ATOM   256  C C   . GLY A 1 47  ? -44.10443 4.02206   -13.48803 1.000 145.11754 ? 47  GLY A C   1 
ATOM   257  O O   . GLY A 1 47  ? -43.34401 4.18676   -14.44330 1.000 145.99284 ? 47  GLY A O   1 
ATOM   258  N N   . GLN A 1 48  ? -45.16239 3.21646   -13.55061 1.000 159.51920 ? 48  GLN A N   1 
ATOM   259  C CA  . GLN A 1 48  ? -45.46447 2.41443   -14.73002 1.000 164.65139 ? 48  GLN A CA  1 
ATOM   260  C C   . GLN A 1 48  ? -46.90702 2.65461   -15.15356 1.000 182.08435 ? 48  GLN A C   1 
ATOM   261  O O   . GLN A 1 48  ? -47.63784 3.43773   -14.53937 1.000 185.89875 ? 48  GLN A O   1 
ATOM   262  C CB  . GLN A 1 48  ? -45.20710 0.92256   -14.47608 1.000 161.62426 ? 48  GLN A CB  1 
ATOM   263  C CG  . GLN A 1 48  ? -43.74504 0.57558   -14.23735 1.000 157.76426 ? 48  GLN A CG  1 
ATOM   264  C CD  . GLN A 1 48  ? -43.41284 0.39611   -12.76972 1.000 157.89907 ? 48  GLN A CD  1 
ATOM   265  O OE1 . GLN A 1 48  ? -44.24291 0.65035   -11.89631 1.000 145.43586 ? 48  GLN A OE1 1 
ATOM   266  N NE2 . GLN A 1 48  ? -42.18764 -0.03669  -12.49035 1.000 150.50775 ? 48  GLN A NE2 1 
ATOM   267  N N   . GLY A 1 49  ? -47.31948 1.96778   -16.21074 1.000 197.04354 ? 49  GLY A N   1 
ATOM   268  C CA  . GLY A 1 49  ? -48.67734 2.06988   -16.70384 1.000 205.91245 ? 49  GLY A CA  1 
ATOM   269  C C   . GLY A 1 49  ? -48.73865 2.88263   -17.98682 1.000 215.44755 ? 49  GLY A C   1 
ATOM   270  O O   . GLY A 1 49  ? -47.72993 3.35015   -18.51867 1.000 216.52339 ? 49  GLY A O   1 
ATOM   271  N N   . SER A 1 50  ? -49.96825 3.03181   -18.48267 1.000 211.75232 ? 50  SER A N   1 
ATOM   272  C CA  . SER A 1 50  ? -50.19553 3.77818   -19.71646 1.000 214.38621 ? 50  SER A CA  1 
ATOM   273  C C   . SER A 1 50  ? -49.91058 5.26704   -19.54806 1.000 218.39221 ? 50  SER A C   1 
ATOM   274  O O   . SER A 1 50  ? -49.47114 5.91916   -20.50236 1.000 220.63265 ? 50  SER A O   1 
ATOM   275  C CB  . SER A 1 50  ? -51.62886 3.56083   -20.20394 1.000 198.95954 ? 50  SER A CB  1 
ATOM   276  O OG  . SER A 1 50  ? -52.52479 4.46807   -19.58704 1.000 191.39187 ? 50  SER A OG  1 
ATOM   277  N N   . LYS A 1 51  ? -50.14816 5.82533   -18.35856 1.000 209.28110 ? 51  LYS A N   1 
ATOM   278  C CA  . LYS A 1 51  ? -49.81503 7.22787   -18.13239 1.000 203.95070 ? 51  LYS A CA  1 
ATOM   279  C C   . LYS A 1 51  ? -48.31393 7.45305   -17.99658 1.000 217.47782 ? 51  LYS A C   1 
ATOM   280  O O   . LYS A 1 51  ? -47.84595 8.57158   -18.23441 1.000 218.82506 ? 51  LYS A O   1 
ATOM   281  C CB  . LYS A 1 51  ? -50.52996 7.74377   -16.88243 1.000 187.16000 ? 51  LYS A CB  1 
ATOM   282  C CG  . LYS A 1 51  ? -51.73126 8.61896   -17.18037 1.000 174.89048 ? 51  LYS A CG  1 
ATOM   283  C CD  . LYS A 1 51  ? -52.88068 7.78279   -17.71029 1.000 165.67879 ? 51  LYS A CD  1 
ATOM   284  C CE  . LYS A 1 51  ? -54.06252 8.64916   -18.09837 1.000 170.67498 ? 51  LYS A CE  1 
ATOM   285  N NZ  . LYS A 1 51  ? -55.21660 7.82748   -18.55691 1.000 175.35391 ? 51  LYS A NZ  1 
ATOM   286  N N   . SER A 1 52  ? -47.55423 6.42455   -17.61060 1.000 242.64430 ? 52  SER A N   1 
ATOM   287  C CA  . SER A 1 52  ? -46.11520 6.57083   -17.41420 1.000 258.21579 ? 52  SER A CA  1 
ATOM   288  C C   . SER A 1 52  ? -45.36847 6.83090   -18.71642 1.000 267.41888 ? 52  SER A C   1 
ATOM   289  O O   . SER A 1 52  ? -44.23587 7.32436   -18.67868 1.000 240.67038 ? 52  SER A O   1 
ATOM   290  C CB  . SER A 1 52  ? -45.54103 5.32518   -16.74208 1.000 240.62036 ? 52  SER A CB  1 
ATOM   291  O OG  . SER A 1 52  ? -45.58828 4.20567   -17.61133 1.000 226.71281 ? 52  SER A OG  1 
ATOM   292  N N   . HIS A 1 53  ? -45.96856 6.50554   -19.85961 1.000 256.36978 ? 53  HIS A N   1 
ATOM   293  C CA  . HIS A 1 53  ? -45.35502 6.72934   -21.16063 1.000 248.57478 ? 53  HIS A CA  1 
ATOM   294  C C   . HIS A 1 53  ? -45.88152 7.97151   -21.86712 1.000 245.81784 ? 53  HIS A C   1 
ATOM   295  O O   . HIS A 1 53  ? -45.39947 8.29575   -22.95695 1.000 243.72960 ? 53  HIS A O   1 
ATOM   296  C CB  . HIS A 1 53  ? -45.56404 5.50240   -22.05661 1.000 248.49989 ? 53  HIS A CB  1 
ATOM   297  C CG  . HIS A 1 53  ? -45.01448 4.23275   -21.48316 1.000 239.85058 ? 53  HIS A CG  1 
ATOM   298  N ND1 . HIS A 1 53  ? -45.81643 3.17389   -21.11426 1.000 229.40831 ? 53  HIS A ND1 1 
ATOM   299  C CD2 . HIS A 1 53  ? -43.74254 3.85084   -21.21861 1.000 223.53169 ? 53  HIS A CD2 1 
ATOM   300  C CE1 . HIS A 1 53  ? -45.06264 2.19556   -20.64526 1.000 217.52811 ? 53  HIS A CE1 1 
ATOM   301  N NE2 . HIS A 1 53  ? -43.80029 2.58082   -20.69782 1.000 220.10161 ? 53  HIS A NE2 1 
ATOM   302  N N   . THR A 1 54  ? -46.85483 8.67362   -21.28306 1.000 244.39095 ? 54  THR A N   1 
ATOM   303  C CA  . THR A 1 54  ? -47.39980 9.86314   -21.92094 1.000 240.46794 ? 54  THR A CA  1 
ATOM   304  C C   . THR A 1 54  ? -47.62664 11.02942  -20.96743 1.000 238.08344 ? 54  THR A C   1 
ATOM   305  O O   . THR A 1 54  ? -48.02470 12.10344  -21.42990 1.000 241.67759 ? 54  THR A O   1 
ATOM   306  C CB  . THR A 1 54  ? -48.72787 9.53066   -22.62744 1.000 238.23929 ? 54  THR A CB  1 
ATOM   307  O OG1 . THR A 1 54  ? -49.44165 8.54380   -21.87193 1.000 232.89972 ? 54  THR A OG1 1 
ATOM   308  C CG2 . THR A 1 54  ? -48.47430 9.00136   -24.03298 1.000 233.28759 ? 54  THR A CG2 1 
ATOM   309  N N   . ASP A 1 55  ? -47.39599 10.86479  -19.66639 1.000 230.88085 ? 55  ASP A N   1 
ATOM   310  C CA  . ASP A 1 55  ? -47.64276 11.93067  -18.69750 1.000 217.98839 ? 55  ASP A CA  1 
ATOM   311  C C   . ASP A 1 55  ? -46.48728 12.02680  -17.70286 1.000 203.13141 ? 55  ASP A C   1 
ATOM   312  O O   . ASP A 1 55  ? -46.68753 12.10656  -16.49019 1.000 201.62351 ? 55  ASP A O   1 
ATOM   313  C CB  . ASP A 1 55  ? -48.96989 11.69834  -17.97510 1.000 210.61511 ? 55  ASP A CB  1 
ATOM   314  C CG  . ASP A 1 55  ? -49.54033 12.96787  -17.37351 1.000 209.42116 ? 55  ASP A CG  1 
ATOM   315  O OD1 . ASP A 1 55  ? -48.85799 14.01237  -17.42140 1.000 210.53122 ? 55  ASP A OD1 1 
ATOM   316  O OD2 . ASP A 1 55  ? -50.67248 12.91873  -16.84814 1.000 204.35191 ? 55  ASP A OD2 1 
ATOM   317  N N   . ARG A 1 56  ? -45.25459 12.02519  -18.20356 1.000 191.51608 ? 56  ARG A N   1 
ATOM   318  C CA  . ARG A 1 56  ? -44.08989 12.00218  -17.33143 1.000 167.48780 ? 56  ARG A CA  1 
ATOM   319  C C   . ARG A 1 56  ? -43.35696 13.33829  -17.35041 1.000 148.46273 ? 56  ARG A C   1 
ATOM   320  O O   . ARG A 1 56  ? -43.53641 14.16583  -18.24887 1.000 138.41737 ? 56  ARG A O   1 
ATOM   321  C CB  . ARG A 1 56  ? -43.12980 10.87105  -17.72285 1.000 160.29342 ? 56  ARG A CB  1 
ATOM   322  C CG  . ARG A 1 56  ? -42.63661 10.90106  -19.16371 1.000 153.11532 ? 56  ARG A CG  1 
ATOM   323  C CD  . ARG A 1 56  ? -41.85120 9.63092   -19.47134 1.000 156.61602 ? 56  ARG A CD  1 
ATOM   324  N NE  . ARG A 1 56  ? -41.68994 9.38080   -20.89963 1.000 159.32766 ? 56  ARG A NE  1 
ATOM   325  C CZ  . ARG A 1 56  ? -40.52018 9.24040   -21.51023 1.000 126.33388 ? 56  ARG A CZ  1 
ATOM   326  N NH1 . ARG A 1 56  ? -39.37769 9.34873   -20.85104 1.000 103.27392 ? 56  ARG A NH1 1 
ATOM   327  N NH2 . ARG A 1 56  ? -40.49552 8.98533   -22.81558 1.000 114.85257 ? 56  ARG A NH2 1 
ATOM   328  N N   . ARG A 1 57  ? -42.52535 13.53609  -16.32847 1.000 133.02935 ? 57  ARG A N   1 
ATOM   329  C CA  . ARG A 1 57  ? -41.66246 14.70668  -16.22235 1.000 101.42409 ? 57  ARG A CA  1 
ATOM   330  C C   . ARG A 1 57  ? -40.20580 14.27013  -16.32268 1.000 101.70732 ? 57  ARG A C   1 
ATOM   331  O O   . ARG A 1 57  ? -39.68666 13.65031  -15.37987 1.000 80.50193  ? 57  ARG A O   1 
ATOM   332  C CB  . ARG A 1 57  ? -41.92358 15.43688  -14.90462 1.000 99.92863  ? 57  ARG A CB  1 
ATOM   333  C CG  . ARG A 1 57  ? -41.18058 16.74405  -14.73970 1.000 110.18220 ? 57  ARG A CG  1 
ATOM   334  C CD  . ARG A 1 57  ? -41.42371 17.33011  -13.35806 1.000 107.69873 ? 57  ARG A CD  1 
ATOM   335  N NE  . ARG A 1 57  ? -42.32164 18.47796  -13.41858 1.000 119.83537 ? 57  ARG A NE  1 
ATOM   336  C CZ  . ARG A 1 57  ? -42.08042 19.65266  -12.85113 1.000 120.47034 ? 57  ARG A CZ  1 
ATOM   337  N NH1 . ARG A 1 57  ? -40.97464 19.87241  -12.16054 1.000 127.08159 ? 57  ARG A NH1 1 
ATOM   338  N NH2 . ARG A 1 57  ? -42.97237 20.63146  -12.97834 1.000 101.18378 ? 57  ARG A NH2 1 
ATOM   339  N N   . PRO A 1 58  ? -39.51077 14.54982  -17.42292 1.000 91.05669  ? 58  PRO A N   1 
ATOM   340  C CA  . PRO A 1 58  ? -38.15898 14.00357  -17.60557 1.000 86.17313  ? 58  PRO A CA  1 
ATOM   341  C C   . PRO A 1 58  ? -37.14970 14.65881  -16.67049 1.000 82.62236  ? 58  PRO A C   1 
ATOM   342  O O   . PRO A 1 58  ? -37.43905 15.62740  -15.96531 1.000 85.47552  ? 58  PRO A O   1 
ATOM   343  C CB  . PRO A 1 58  ? -37.83499 14.30192  -19.07353 1.000 78.93373  ? 58  PRO A CB  1 
ATOM   344  C CG  . PRO A 1 58  ? -38.77770 15.38203  -19.48490 1.000 85.20886  ? 58  PRO A CG  1 
ATOM   345  C CD  . PRO A 1 58  ? -39.93011 15.43008  -18.52660 1.000 89.40450  ? 58  PRO A CD  1 
ATOM   346  N N   . VAL A 1 59  ? -35.93695 14.09352  -16.67093 1.000 76.73208  ? 59  VAL A N   1 
ATOM   347  C CA  . VAL A 1 59  ? -34.87158 14.59053  -15.80699 1.000 73.75809  ? 59  VAL A CA  1 
ATOM   348  C C   . VAL A 1 59  ? -34.54247 16.02717  -16.18465 1.000 75.95893  ? 59  VAL A C   1 
ATOM   349  O O   . VAL A 1 59  ? -34.30276 16.33847  -17.35750 1.000 75.61093  ? 59  VAL A O   1 
ATOM   350  C CB  . VAL A 1 59  ? -33.63693 13.68564  -15.91989 1.000 76.30347  ? 59  VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 59  ? -32.41741 14.38753  -15.36900 1.000 71.05051  ? 59  VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 59  ? -33.87548 12.36175  -15.20671 1.000 73.01485  ? 59  VAL A CG2 1 
ATOM   353  N N   . ASP A 1 60  ? -34.49727 16.90785  -15.18675 1.000 83.31227  ? 60  ASP A N   1 
ATOM   354  C CA  . ASP A 1 60  ? -34.26166 18.31865  -15.44965 1.000 87.86277  ? 60  ASP A CA  1 
ATOM   355  C C   . ASP A 1 60  ? -33.17540 18.87189  -14.53712 1.000 85.32271  ? 60  ASP A C   1 
ATOM   356  O O   . ASP A 1 60  ? -33.11510 18.51591  -13.35391 1.000 94.52647  ? 60  ASP A O   1 
ATOM   357  C CB  . ASP A 1 60  ? -35.55208 19.12339  -15.27983 1.000 88.63238  ? 60  ASP A CB  1 
ATOM   358  C CG  . ASP A 1 60  ? -35.43072 20.52307  -15.82406 1.000 99.95147  ? 60  ASP A CG  1 
ATOM   359  O OD1 . ASP A 1 60  ? -35.51093 20.68223  -17.05961 1.000 103.30113 ? 60  ASP A OD1 1 
ATOM   360  O OD2 . ASP A 1 60  ? -35.26715 21.46286  -15.01885 1.000 117.93016 ? 60  ASP A OD2 1 
ATOM   361  N N   . PRO A 1 61  ? -32.28674 19.72618  -15.05844 1.000 81.79887  ? 61  PRO A N   1 
ATOM   362  C CA  . PRO A 1 61  ? -32.14730 20.15131  -16.45622 1.000 79.30825  ? 61  PRO A CA  1 
ATOM   363  C C   . PRO A 1 61  ? -31.57584 19.01669  -17.28654 1.000 82.29248  ? 61  PRO A C   1 
ATOM   364  O O   . PRO A 1 61  ? -30.90838 18.13975  -16.74800 1.000 75.34278  ? 61  PRO A O   1 
ATOM   365  C CB  . PRO A 1 61  ? -31.20649 21.35612  -16.35168 1.000 76.13667  ? 61  PRO A CB  1 
ATOM   366  C CG  . PRO A 1 61  ? -30.33881 21.02627  -15.18132 1.000 79.00199  ? 61  PRO A CG  1 
ATOM   367  C CD  . PRO A 1 61  ? -31.27767 20.37162  -14.19983 1.000 83.47860  ? 61  PRO A CD  1 
ATOM   368  N N   . PRO A 1 62  ? -31.84409 18.99956  -18.58746 1.000 77.84090  ? 62  PRO A N   1 
ATOM   369  C CA  . PRO A 1 62  ? -31.36806 17.90355  -19.42945 1.000 57.00189  ? 62  PRO A CA  1 
ATOM   370  C C   . PRO A 1 62  ? -29.85534 17.81246  -19.39456 1.000 73.91922  ? 62  PRO A C   1 
ATOM   371  O O   . PRO A 1 62  ? -29.15954 18.82954  -19.53474 1.000 70.32528  ? 62  PRO A O   1 
ATOM   372  C CB  . PRO A 1 62  ? -31.86761 18.28796  -20.83076 1.000 65.67087  ? 62  PRO A CB  1 
ATOM   373  C CG  . PRO A 1 62  ? -32.08714 19.77072  -20.75797 1.000 76.30937  ? 62  PRO A CG  1 
ATOM   374  C CD  . PRO A 1 62  ? -32.57946 20.01185  -19.36401 1.000 66.81364  ? 62  PRO A CD  1 
ATOM   375  N N   . PRO A 1 63  ? -29.30901 16.61407  -19.18727 1.000 74.85734  ? 63  PRO A N   1 
ATOM   376  C CA  . PRO A 1 63  ? -27.85139 16.47593  -19.15201 1.000 57.24772  ? 63  PRO A CA  1 
ATOM   377  C C   . PRO A 1 63  ? -27.24875 16.85420  -20.49376 1.000 58.08508  ? 63  PRO A C   1 
ATOM   378  O O   . PRO A 1 63  ? -27.77351 16.50994  -21.55528 1.000 58.05441  ? 63  PRO A O   1 
ATOM   379  C CB  . PRO A 1 63  ? -27.64372 14.99005  -18.83076 1.000 53.52025  ? 63  PRO A CB  1 
ATOM   380  C CG  . PRO A 1 63  ? -28.90433 14.58722  -18.12724 1.000 70.95896  ? 63  PRO A CG  1 
ATOM   381  C CD  . PRO A 1 63  ? -29.99145 15.36364  -18.81263 1.000 63.35862  ? 63  PRO A CD  1 
ATOM   382  N N   . VAL A 1 64  ? -26.12362 17.55948  -20.42927 1.000 58.26956  ? 64  VAL A N   1 
ATOM   383  C CA  . VAL A 1 64  ? -25.39489 18.02069  -21.60252 1.000 51.56150  ? 64  VAL A CA  1 
ATOM   384  C C   . VAL A 1 64  ? -23.93989 17.63263  -21.42325 1.000 56.85526  ? 64  VAL A C   1 
ATOM   385  O O   . VAL A 1 64  ? -23.33820 17.92562  -20.38436 1.000 62.75999  ? 64  VAL A O   1 
ATOM   386  C CB  . VAL A 1 64  ? -25.53106 19.54233  -21.80290 1.000 62.26215  ? 64  VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 64  ? -24.56582 20.02363  -22.87916 1.000 62.30263  ? 64  VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 64  ? -26.97047 19.91127  -22.13736 1.000 55.85579  ? 64  VAL A CG2 1 
ATOM   389  N N   . ILE A 1 65  ? -23.38264 16.95122  -22.41557 1.000 51.86431  ? 65  ILE A N   1 
ATOM   390  C CA  . ILE A 1 65  ? -22.01279 16.47139  -22.34325 1.000 58.09926  ? 65  ILE A CA  1 
ATOM   391  C C   . ILE A 1 65  ? -21.25586 16.98731  -23.55260 1.000 56.16013  ? 65  ILE A C   1 
ATOM   392  O O   . ILE A 1 65  ? -21.73016 16.87647  -24.68892 1.000 56.57840  ? 65  ILE A O   1 
ATOM   393  C CB  . ILE A 1 65  ? -21.93315 14.93708  -22.25066 1.000 61.12795  ? 65  ILE A CB  1 
ATOM   394  C CG1 . ILE A 1 65  ? -22.54611 14.45358  -20.93303 1.000 53.97043  ? 65  ILE A CG1 1 
ATOM   395  C CG2 . ILE A 1 65  ? -20.49046 14.50417  -22.29836 1.000 47.55644  ? 65  ILE A CG2 1 
ATOM   396  C CD1 . ILE A 1 65  ? -24.03444 14.17389  -21.00380 1.000 56.21349  ? 65  ILE A CD1 1 
ATOM   397  N N   . GLU A 1 66  ? -20.10575 17.59113  -23.29317 1.000 54.93059  ? 66  GLU A N   1 
ATOM   398  C CA  . GLU A 1 66  ? -19.22692 18.13112  -24.31414 1.000 68.11732  ? 66  GLU A CA  1 
ATOM   399  C C   . GLU A 1 66  ? -18.12579 17.13698  -24.64487 1.000 62.83990  ? 66  GLU A C   1 
ATOM   400  O O   . GLU A 1 66  ? -17.58760 16.46911  -23.75810 1.000 62.19129  ? 66  GLU A O   1 
ATOM   401  C CB  . GLU A 1 66  ? -18.61113 19.45203  -23.85437 1.000 56.77549  ? 66  GLU A CB  1 
ATOM   402  C CG  . GLU A 1 66  ? -17.87168 20.16925  -24.95428 1.000 81.75563  ? 66  GLU A CG  1 
ATOM   403  C CD  . GLU A 1 66  ? -17.32209 21.51023  -24.52907 1.000 83.64063  ? 66  GLU A CD  1 
ATOM   404  O OE1 . GLU A 1 66  ? -18.10257 22.48161  -24.48076 1.000 101.01911 ? 66  GLU A OE1 1 
ATOM   405  O OE2 . GLU A 1 66  ? -16.11174 21.59016  -24.23227 1.000 97.14796  ? 66  GLU A OE2 1 
ATOM   406  N N   . LEU A 1 67  ? -17.81966 17.02613  -25.93380 1.000 58.03544  ? 67  LEU A N   1 
ATOM   407  C CA  . LEU A 1 67  ? -16.79397 16.12569  -26.43420 1.000 64.31973  ? 67  LEU A CA  1 
ATOM   408  C C   . LEU A 1 67  ? -15.75270 16.93397  -27.19314 1.000 67.14066  ? 67  LEU A C   1 
ATOM   409  O O   . LEU A 1 67  ? -16.09566 17.77537  -28.02931 1.000 71.01089  ? 67  LEU A O   1 
ATOM   410  C CB  . LEU A 1 67  ? -17.39875 15.04875  -27.34177 1.000 59.96932  ? 67  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 67  ? -16.46012 14.27296  -28.27017 1.000 59.63102  ? 67  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 67  ? -15.35237 13.57493  -27.48267 1.000 60.53816  ? 67  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 67  ? -17.23658 13.26907  -29.10290 1.000 67.07548  ? 67  LEU A CD2 1 
ATOM   414  N N   . ASN A 1 68  ? -14.48800 16.67234  -26.89883 1.000 60.86751  ? 68  ASN A N   1 
ATOM   415  C CA  . ASN A 1 68  ? -13.36945 17.26945  -27.60378 1.000 63.85698  ? 68  ASN A CA  1 
ATOM   416  C C   . ASN A 1 68  ? -12.38317 16.17230  -27.98133 1.000 70.23978  ? 68  ASN A C   1 
ATOM   417  O O   . ASN A 1 68  ? -12.20170 15.19696  -27.24621 1.000 68.16320  ? 68  ASN A O   1 
ATOM   418  C CB  . ASN A 1 68  ? -12.69789 18.34184  -26.74954 1.000 73.03410  ? 68  ASN A CB  1 
ATOM   419  C CG  . ASN A 1 68  ? -13.55852 19.57533  -26.59868 1.000 83.37941  ? 68  ASN A CG  1 
ATOM   420  O OD1 . ASN A 1 68  ? -13.56584 20.44696  -27.46752 1.000 72.19225  ? 68  ASN A OD1 1 
ATOM   421  N ND2 . ASN A 1 68  ? -14.30423 19.65004  -25.50101 1.000 83.68651  ? 68  ASN A ND2 1 
ATOM   422  N N   . ILE A 1 69  ? -11.74126 16.34791  -29.13391 1.000 72.92659  ? 69  ILE A N   1 
ATOM   423  C CA  . ILE A 1 69  ? -10.77504 15.39549  -29.66778 1.000 74.09773  ? 69  ILE A CA  1 
ATOM   424  C C   . ILE A 1 69  ? -9.48195  16.14939  -29.93617 1.000 71.12054  ? 69  ILE A C   1 
ATOM   425  O O   . ILE A 1 69  ? -9.50047  17.22575  -30.54248 1.000 81.53964  ? 69  ILE A O   1 
ATOM   426  C CB  . ILE A 1 69  ? -11.28315 14.71595  -30.95490 1.000 70.20588  ? 69  ILE A CB  1 
ATOM   427  C CG1 . ILE A 1 69  ? -12.53014 13.88524  -30.66980 1.000 67.86743  ? 69  ILE A CG1 1 
ATOM   428  C CG2 . ILE A 1 69  ? -10.21862 13.79355  -31.52809 1.000 76.07392  ? 69  ILE A CG2 1 
ATOM   429  C CD1 . ILE A 1 69  ? -13.52598 13.90328  -31.80236 1.000 72.15558  ? 69  ILE A CD1 1 
ATOM   430  N N   . PHE A 1 70  ? -8.36140  15.57333  -29.50977 1.000 79.34559  ? 70  PHE A N   1 
ATOM   431  C CA  . PHE A 1 70  ? -7.06705  16.23320  -29.58166 1.000 79.56824  ? 70  PHE A CA  1 
ATOM   432  C C   . PHE A 1 70  ? -6.05386  15.36573  -30.31410 1.000 90.72572  ? 70  PHE A C   1 
ATOM   433  O O   . PHE A 1 70  ? -5.91965  14.17142  -30.02824 1.000 86.21079  ? 70  PHE A O   1 
ATOM   434  C CB  . PHE A 1 70  ? -6.56034  16.56574  -28.17266 1.000 82.04153  ? 70  PHE A CB  1 
ATOM   435  C CG  . PHE A 1 70  ? -7.43546  17.53471  -27.43036 1.000 81.38975  ? 70  PHE A CG  1 
ATOM   436  C CD1 . PHE A 1 70  ? -7.25634  18.90324  -27.58126 1.000 86.40990  ? 70  PHE A CD1 1 
ATOM   437  C CD2 . PHE A 1 70  ? -8.45407  17.08310  -26.60550 1.000 71.04592  ? 70  PHE A CD2 1 
ATOM   438  C CE1 . PHE A 1 70  ? -8.06511  19.80436  -26.90725 1.000 76.50741  ? 70  PHE A CE1 1 
ATOM   439  C CE2 . PHE A 1 70  ? -9.26782  17.97675  -25.92801 1.000 67.62839  ? 70  PHE A CE2 1 
ATOM   440  C CZ  . PHE A 1 70  ? -9.07103  19.34292  -26.08013 1.000 64.55251  ? 70  PHE A CZ  1 
ATOM   441  N N   . GLU A 1 71  ? -5.36025  15.97964  -31.26996 1.000 89.83801  ? 71  GLU A N   1 
ATOM   442  C CA  . GLU A 1 71  ? -4.16525  15.41919  -31.88188 1.000 84.71138  ? 71  GLU A CA  1 
ATOM   443  C C   . GLU A 1 71  ? -2.93304  15.87665  -31.11545 1.000 91.25853  ? 71  GLU A C   1 
ATOM   444  O O   . GLU A 1 71  ? -2.75894  17.07398  -30.86354 1.000 89.92973  ? 71  GLU A O   1 
ATOM   445  C CB  . GLU A 1 71  ? -4.06241  15.89796  -33.32798 1.000 96.16870  ? 71  GLU A CB  1 
ATOM   446  C CG  . GLU A 1 71  ? -2.89779  15.35523  -34.10962 1.000 98.97072  ? 71  GLU A CG  1 
ATOM   447  C CD  . GLU A 1 71  ? -3.22808  15.15657  -35.56735 1.000 113.52335 ? 71  GLU A CD  1 
ATOM   448  O OE1 . GLU A 1 71  ? -4.41750  15.27362  -35.93458 1.000 112.81344 ? 71  GLU A OE1 1 
ATOM   449  O OE2 . GLU A 1 71  ? -2.28382  14.93993  -36.35613 1.000 116.01147 ? 71  GLU A OE2 1 
ATOM   450  N N   . SER A 1 72  ? -2.07072  14.93083  -30.76812 1.000 99.39484  ? 72  SER A N   1 
ATOM   451  C CA  . SER A 1 72  ? -0.79969  15.22873  -30.12368 1.000 102.72974 ? 72  SER A CA  1 
ATOM   452  C C   . SER A 1 72  ? 0.33311   14.97217  -31.10602 1.000 112.08901 ? 72  SER A C   1 
ATOM   453  O O   . SER A 1 72  ? 0.50912   13.83969  -31.56917 1.000 122.68518 ? 72  SER A O   1 
ATOM   454  C CB  . SER A 1 72  ? -0.61930  14.38808  -28.86140 1.000 96.28913  ? 72  SER A CB  1 
ATOM   455  O OG  . SER A 1 72  ? -1.72352  14.56317  -27.99405 1.000 112.23529 ? 72  SER A OG  1 
ATOM   456  N N   . ASP A 1 73  ? 1.09251   16.01541  -31.42231 1.000 116.06377 ? 73  ASP A N   1 
ATOM   457  C CA  . ASP A 1 73  ? 2.26107   15.83819  -32.27008 1.000 128.09891 ? 73  ASP A CA  1 
ATOM   458  C C   . ASP A 1 73  ? 3.28964   14.97805  -31.53868 1.000 130.59386 ? 73  ASP A C   1 
ATOM   459  O O   . ASP A 1 73  ? 3.50872   15.16066  -30.33660 1.000 121.42312 ? 73  ASP A O   1 
ATOM   460  C CB  . ASP A 1 73  ? 2.87046   17.18193  -32.66796 1.000 137.62943 ? 73  ASP A CB  1 
ATOM   461  C CG  . ASP A 1 73  ? 2.89282   18.17022  -31.52756 1.000 134.67058 ? 73  ASP A CG  1 
ATOM   462  O OD1 . ASP A 1 73  ? 2.30362   17.85761  -30.47120 1.000 121.87974 ? 73  ASP A OD1 1 
ATOM   463  O OD2 . ASP A 1 73  ? 3.51236   19.24635  -31.68398 1.000 108.52653 ? 73  ASP A OD2 1 
ATOM   464  N N   . PRO A 1 74  ? 3.91931   14.02361  -32.22817 1.000 144.83224 ? 74  PRO A N   1 
ATOM   465  C CA  . PRO A 1 74  ? 4.77713   13.05341  -31.52328 1.000 150.03587 ? 74  PRO A CA  1 
ATOM   466  C C   . PRO A 1 74  ? 5.95884   13.68140  -30.80824 1.000 150.18850 ? 74  PRO A C   1 
ATOM   467  O O   . PRO A 1 74  ? 6.39798   13.14765  -29.78134 1.000 140.82758 ? 74  PRO A O   1 
ATOM   468  C CB  . PRO A 1 74  ? 5.24287   12.10335  -32.63811 1.000 149.43679 ? 74  PRO A CB  1 
ATOM   469  C CG  . PRO A 1 74  ? 4.46579   12.46287  -33.86158 1.000 148.76804 ? 74  PRO A CG  1 
ATOM   470  C CD  . PRO A 1 74  ? 3.91380   13.83451  -33.68749 1.000 144.41027 ? 74  PRO A CD  1 
ATOM   471  N N   . HIS A 1 75  ? 6.48380   14.80093  -31.30751 1.000 162.20095 ? 75  HIS A N   1 
ATOM   472  C CA  . HIS A 1 75  ? 7.66216   15.40141  -30.69068 1.000 184.56747 ? 75  HIS A CA  1 
ATOM   473  C C   . HIS A 1 75  ? 7.33242   15.95420  -29.30953 1.000 170.14115 ? 75  HIS A C   1 
ATOM   474  O O   . HIS A 1 75  ? 7.88181   15.50314  -28.29768 1.000 188.95288 ? 75  HIS A O   1 
ATOM   475  C CB  . HIS A 1 75  ? 8.22914   16.49979  -31.59293 1.000 182.92599 ? 75  HIS A CB  1 
ATOM   476  C CG  . HIS A 1 75  ? 7.96408   16.28387  -33.04994 1.000 185.11593 ? 75  HIS A CG  1 
ATOM   477  N ND1 . HIS A 1 75  ? 6.88456   16.84046  -33.70163 1.000 185.62758 ? 75  HIS A ND1 1 
ATOM   478  C CD2 . HIS A 1 75  ? 8.64451   15.57815  -33.98390 1.000 184.81301 ? 75  HIS A CD2 1 
ATOM   479  C CE1 . HIS A 1 75  ? 6.90861   16.48261  -34.97312 1.000 191.46135 ? 75  HIS A CE1 1 
ATOM   480  N NE2 . HIS A 1 75  ? 7.96665   15.71685  -35.17051 1.000 189.29587 ? 75  HIS A NE2 1 
ATOM   481  N N   . ASP A 1 76  ? 6.43430   16.93050  -29.24641 1.000 135.43083 ? 76  ASP A N   1 
ATOM   482  C CA  . ASP A 1 76  ? 6.14736   17.65811  -28.01856 1.000 114.68658 ? 76  ASP A CA  1 
ATOM   483  C C   . ASP A 1 76  ? 4.71703   17.32999  -27.60531 1.000 122.96888 ? 76  ASP A C   1 
ATOM   484  O O   . ASP A 1 76  ? 3.76966   17.67618  -28.31616 1.000 128.01523 ? 76  ASP A O   1 
ATOM   485  C CB  . ASP A 1 76  ? 6.34325   19.16038  -28.24665 1.000 99.81172  ? 76  ASP A CB  1 
ATOM   486  C CG  . ASP A 1 76  ? 6.07654   20.00443  -27.00605 1.000 111.29621 ? 76  ASP A CG  1 
ATOM   487  O OD1 . ASP A 1 76  ? 5.36482   19.55614  -26.08695 1.000 110.08047 ? 76  ASP A OD1 1 
ATOM   488  O OD2 . ASP A 1 76  ? 6.59412   21.14261  -26.95581 1.000 113.22618 ? 76  ASP A OD2 1 
ATOM   489  N N   . ASP A 1 77  ? 4.56047   16.67589  -26.45434 1.000 111.53529 ? 77  ASP A N   1 
ATOM   490  C CA  . ASP A 1 77  ? 3.23583   16.33260  -25.95013 1.000 113.27011 ? 77  ASP A CA  1 
ATOM   491  C C   . ASP A 1 77  ? 2.60814   17.42917  -25.10009 1.000 116.42724 ? 77  ASP A C   1 
ATOM   492  O O   . ASP A 1 77  ? 1.44300   17.29283  -24.70962 1.000 113.93716 ? 77  ASP A O   1 
ATOM   493  C CB  . ASP A 1 77  ? 3.28358   15.03258  -25.14154 1.000 101.69596 ? 77  ASP A CB  1 
ATOM   494  C CG  . ASP A 1 77  ? 2.92444   13.81968  -25.97290 1.000 126.25909 ? 77  ASP A CG  1 
ATOM   495  O OD1 . ASP A 1 77  ? 2.96641   13.91660  -27.21779 1.000 128.16095 ? 77  ASP A OD1 1 
ATOM   496  O OD2 . ASP A 1 77  ? 2.59019   12.77157  -25.38246 1.000 146.81787 ? 77  ASP A OD2 1 
ATOM   497  N N   . SER A 1 78  ? 3.33780   18.50871  -24.80596 1.000 110.78391 ? 78  SER A N   1 
ATOM   498  C CA  . SER A 1 78  ? 2.70499   19.66261  -24.18132 1.000 103.27496 ? 78  SER A CA  1 
ATOM   499  C C   . SER A 1 78  ? 1.81663   20.42411  -25.15274 1.000 109.68240 ? 78  SER A C   1 
ATOM   500  O O   . SER A 1 78  ? 1.03589   21.27312  -24.71343 1.000 111.72824 ? 78  SER A O   1 
ATOM   501  C CB  . SER A 1 78  ? 3.76745   20.61663  -23.62000 1.000 101.06440 ? 78  SER A CB  1 
ATOM   502  O OG  . SER A 1 78  ? 4.39236   20.10066  -22.45741 1.000 94.60924  ? 78  SER A OG  1 
ATOM   503  N N   . ASN A 1 79  ? 1.89148   20.11713  -26.44548 1.000 107.34815 ? 79  ASN A N   1 
ATOM   504  C CA  . ASN A 1 79  ? 1.10103   20.77948  -27.47302 1.000 108.47081 ? 79  ASN A CA  1 
ATOM   505  C C   . ASN A 1 79  ? 0.04783   19.81641  -27.99782 1.000 107.40748 ? 79  ASN A C   1 
ATOM   506  O O   . ASN A 1 79  ? 0.36135   18.67031  -28.33687 1.000 108.52977 ? 79  ASN A O   1 
ATOM   507  C CB  . ASN A 1 79  ? 1.98902   21.27236  -28.61684 1.000 101.90496 ? 79  ASN A CB  1 
ATOM   508  C CG  . ASN A 1 79  ? 2.93734   22.37303  -28.18430 1.000 118.62928 ? 79  ASN A CG  1 
ATOM   509  O OD1 . ASN A 1 79  ? 2.93847   22.78815  -27.02385 1.000 115.83190 ? 79  ASN A OD1 1 
ATOM   510  N ND2 . ASN A 1 79  ? 3.74908   22.85528  -29.11841 1.000 110.71069 ? 79  ASN A ND2 1 
ATOM   511  N N   . LYS A 1 80  ? -1.19567  20.28248  -28.05740 1.000 103.71907 ? 80  LYS A N   1 
ATOM   512  C CA  . LYS A 1 80  ? -2.29555  19.50951  -28.60483 1.000 96.46121  ? 80  LYS A CA  1 
ATOM   513  C C   . LYS A 1 80  ? -3.07640  20.38582  -29.57284 1.000 98.18227  ? 80  LYS A C   1 
ATOM   514  O O   . LYS A 1 80  ? -3.06477  21.61576  -29.47561 1.000 113.90274 ? 80  LYS A O   1 
ATOM   515  C CB  . LYS A 1 80  ? -3.21928  18.99022  -27.49182 1.000 96.23858  ? 80  LYS A CB  1 
ATOM   516  C CG  . LYS A 1 80  ? -2.48129  18.28228  -26.36067 1.000 108.61907 ? 80  LYS A CG  1 
ATOM   517  C CD  . LYS A 1 80  ? -3.18101  17.01133  -25.90993 1.000 108.70494 ? 80  LYS A CD  1 
ATOM   518  C CE  . LYS A 1 80  ? -2.18590  16.03808  -25.28950 1.000 117.56112 ? 80  LYS A CE  1 
ATOM   519  N NZ  . LYS A 1 80  ? -2.68205  15.45903  -24.00779 1.000 115.36774 ? 80  LYS A NZ  1 
ATOM   520  N N   . THR A 1 81  ? -3.75833  19.74108  -30.51463 1.000 86.73962  ? 81  THR A N   1 
ATOM   521  C CA  . THR A 1 81  ? -4.59203  20.43282  -31.48924 1.000 85.88308  ? 81  THR A CA  1 
ATOM   522  C C   . THR A 1 81  ? -5.99770  19.85759  -31.43314 1.000 84.38068  ? 81  THR A C   1 
ATOM   523  O O   . THR A 1 81  ? -6.18438  18.65229  -31.62812 1.000 82.85968  ? 81  THR A O   1 
ATOM   524  C CB  . THR A 1 81  ? -4.01974  20.30046  -32.90134 1.000 90.34897  ? 81  THR A CB  1 
ATOM   525  O OG1 . THR A 1 81  ? -2.67874  20.80387  -32.92434 1.000 86.47338  ? 81  THR A OG1 1 
ATOM   526  C CG2 . THR A 1 81  ? -4.87084  21.08616  -33.89033 1.000 94.91996  ? 81  THR A CG2 1 
ATOM   527  N N   . ASP A 1 82  ? -6.98110  20.71551  -31.17650 1.000 77.36257  ? 82  ASP A N   1 
ATOM   528  C CA  . ASP A 1 82  ? -8.37344  20.28103  -31.14943 1.000 79.96651  ? 82  ASP A CA  1 
ATOM   529  C C   . ASP A 1 82  ? -8.82790  20.02429  -32.58159 1.000 82.29576  ? 82  ASP A C   1 
ATOM   530  O O   . ASP A 1 82  ? -8.97964  20.96082  -33.37209 1.000 76.22635  ? 82  ASP A O   1 
ATOM   531  C CB  . ASP A 1 82  ? -9.24660  21.32701  -30.46404 1.000 77.04690  ? 82  ASP A CB  1 
ATOM   532  C CG  . ASP A 1 82  ? -10.57735 20.76416  -30.00469 1.000 83.48757  ? 82  ASP A CG  1 
ATOM   533  O OD1 . ASP A 1 82  ? -11.24778 20.10445  -30.82211 1.000 78.64462  ? 82  ASP A OD1 1 
ATOM   534  O OD2 . ASP A 1 82  ? -10.95462 20.97998  -28.83210 1.000 83.21862  ? 82  ASP A OD2 1 
ATOM   535  N N   . ILE A 1 83  ? -9.06250  18.75637  -32.91427 1.000 72.40512  ? 83  ILE A N   1 
ATOM   536  C CA  . ILE A 1 83  ? -9.44635  18.37944  -34.26895 1.000 74.95895  ? 83  ILE A CA  1 
ATOM   537  C C   . ILE A 1 83  ? -10.88920 17.90161  -34.28105 1.000 70.07857  ? 83  ILE A C   1 
ATOM   538  O O   . ILE A 1 83  ? -11.28814 17.11798  -35.14765 1.000 76.28108  ? 83  ILE A O   1 
ATOM   539  C CB  . ILE A 1 83  ? -8.49929  17.30515  -34.83304 1.000 79.92754  ? 83  ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 83  ? -8.27570  16.19532  -33.80219 1.000 73.01771  ? 83  ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 83  ? -7.17576  17.93210  -35.24009 1.000 86.78944  ? 83  ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 83  ? -8.22744  14.81306  -34.39939 1.000 80.79252  ? 83  ILE A CD1 1 
ATOM   543  N N   . THR A 1 84  ? -11.68189 18.38674  -33.32392 1.000 67.12552  ? 84  THR A N   1 
ATOM   544  C CA  . THR A 1 84  ? -13.06749 17.94690  -33.20986 1.000 70.24996  ? 84  THR A CA  1 
ATOM   545  C C   . THR A 1 84  ? -13.85084 18.27931  -34.47068 1.000 78.30407  ? 84  THR A C   1 
ATOM   546  O O   . THR A 1 84  ? -14.67884 17.48189  -34.92668 1.000 82.90342  ? 84  THR A O   1 
ATOM   547  C CB  . THR A 1 84  ? -13.73010 18.59391  -31.99531 1.000 63.52605  ? 84  THR A CB  1 
ATOM   548  O OG1 . THR A 1 84  ? -12.87386 18.47043  -30.85097 1.000 71.30996  ? 84  THR A OG1 1 
ATOM   549  C CG2 . THR A 1 84  ? -15.07511 17.94265  -31.70982 1.000 68.63847  ? 84  THR A CG2 1 
ATOM   550  N N   . PHE A 1 85  ? -13.61936 19.46303  -35.03346 1.000 80.58286  ? 85  PHE A N   1 
ATOM   551  C CA  . PHE A 1 85  ? -14.28865 19.88153  -36.25586 1.000 84.92347  ? 85  PHE A CA  1 
ATOM   552  C C   . PHE A 1 85  ? -13.60523 19.36183  -37.51531 1.000 84.74662  ? 85  PHE A C   1 
ATOM   553  O O   . PHE A 1 85  ? -14.12459 19.57370  -38.61630 1.000 86.16454  ? 85  PHE A O   1 
ATOM   554  C CB  . PHE A 1 85  ? -14.37016 21.40763  -36.27052 1.000 93.38884  ? 85  PHE A CB  1 
ATOM   555  C CG  . PHE A 1 85  ? -15.43183 21.94867  -35.35913 1.000 91.44732  ? 85  PHE A CG  1 
ATOM   556  C CD1 . PHE A 1 85  ? -15.19921 22.02886  -33.99570 1.000 78.62630  ? 85  PHE A CD1 1 
ATOM   557  C CD2 . PHE A 1 85  ? -16.65569 22.36593  -35.85160 1.000 102.17496 ? 85  PHE A CD2 1 
ATOM   558  C CE1 . PHE A 1 85  ? -16.16309 22.51342  -33.13957 1.000 93.83264  ? 85  PHE A CE1 1 
ATOM   559  C CE2 . PHE A 1 85  ? -17.62696 22.85802  -34.99788 1.000 106.06813 ? 85  PHE A CE2 1 
ATOM   560  C CZ  . PHE A 1 85  ? -17.37868 22.93181  -33.63959 1.000 100.53554 ? 85  PHE A CZ  1 
ATOM   561  N N   . VAL A 1 86  ? -12.46334 18.69100  -37.37834 1.000 93.86537  ? 86  VAL A N   1 
ATOM   562  C CA  . VAL A 1 86  ? -11.76421 18.07817  -38.49746 1.000 87.31150  ? 86  VAL A CA  1 
ATOM   563  C C   . VAL A 1 86  ? -11.93062 16.56147  -38.49610 1.000 94.62548  ? 86  VAL A C   1 
ATOM   564  O O   . VAL A 1 86  ? -12.15336 15.95624  -39.54686 1.000 97.45328  ? 86  VAL A O   1 
ATOM   565  C CB  . VAL A 1 86  ? -10.27039 18.47636  -38.48456 1.000 84.34362  ? 86  VAL A CB  1 
ATOM   566  C CG1 . VAL A 1 86  ? -9.40768  17.41075  -39.14367 1.000 91.62589  ? 86  VAL A CG1 1 
ATOM   567  C CG2 . VAL A 1 86  ? -10.08010 19.81180  -39.17654 1.000 86.80059  ? 86  VAL A CG2 1 
ATOM   568  N N   . TYR A 1 87  ? -11.85255 15.94066  -37.31798 1.000 81.92719  ? 87  TYR A N   1 
ATOM   569  C CA  . TYR A 1 87  ? -11.98063 14.49456  -37.18614 1.000 82.06650  ? 87  TYR A CA  1 
ATOM   570  C C   . TYR A 1 87  ? -13.31767 14.02851  -37.74744 1.000 84.53877  ? 87  TYR A C   1 
ATOM   571  O O   . TYR A 1 87  ? -14.37562 14.55836  -37.39485 1.000 96.60415  ? 87  TYR A O   1 
ATOM   572  C CB  . TYR A 1 87  ? -11.83914 14.10861  -35.71356 1.000 83.21900  ? 87  TYR A CB  1 
ATOM   573  C CG  . TYR A 1 87  ? -11.62183 12.64267  -35.42995 1.000 81.27255  ? 87  TYR A CG  1 
ATOM   574  C CD1 . TYR A 1 87  ? -12.69641 11.78327  -35.25993 1.000 77.58561  ? 87  TYR A CD1 1 
ATOM   575  C CD2 . TYR A 1 87  ? -10.34068 12.12173  -35.31406 1.000 86.91630  ? 87  TYR A CD2 1 
ATOM   576  C CE1 . TYR A 1 87  ? -12.50076 10.44914  -34.98781 1.000 85.05098  ? 87  TYR A CE1 1 
ATOM   577  C CE2 . TYR A 1 87  ? -10.13533 10.78488  -35.04534 1.000 85.53336  ? 87  TYR A CE2 1 
ATOM   578  C CZ  . TYR A 1 87  ? -11.21865 9.95449   -34.88435 1.000 81.19657  ? 87  TYR A CZ  1 
ATOM   579  O OH  . TYR A 1 87  ? -11.02105 8.62368   -34.61543 1.000 90.02154  ? 87  TYR A OH  1 
ATOM   580  N N   . ASN A 1 88  ? -13.26984 13.02593  -38.61247 1.000 85.95726  ? 88  ASN A N   1 
ATOM   581  C CA  . ASN A 1 88  ? -14.43492 12.60629  -39.38001 1.000 101.20139 ? 88  ASN A CA  1 
ATOM   582  C C   . ASN A 1 88  ? -14.84874 11.20548  -38.92411 1.000 94.55618  ? 88  ASN A C   1 
ATOM   583  O O   . ASN A 1 88  ? -14.32224 10.19758  -39.39960 1.000 96.27002  ? 88  ASN A O   1 
ATOM   584  C CB  . ASN A 1 88  ? -14.11147 12.64070  -40.87251 1.000 112.36168 ? 88  ASN A CB  1 
ATOM   585  C CG  . ASN A 1 88  ? -15.27018 12.19277  -41.72812 1.000 125.02516 ? 88  ASN A CG  1 
ATOM   586  O OD1 . ASN A 1 88  ? -16.42800 12.35348  -41.34586 1.000 120.97053 ? 88  ASN A OD1 1 
ATOM   587  N ND2 . ASN A 1 88  ? -14.96849 11.61069  -42.88446 1.000 124.94670 ? 88  ASN A ND2 1 
ATOM   588  N N   . ALA A 1 89  ? -15.79986 11.15325  -37.99397 1.000 83.84032  ? 89  ALA A N   1 
ATOM   589  C CA  . ALA A 1 89  ? -16.35171 9.89191   -37.52124 1.000 83.75691  ? 89  ALA A CA  1 
ATOM   590  C C   . ALA A 1 89  ? -17.71342 10.16353  -36.89986 1.000 84.87287  ? 89  ALA A C   1 
ATOM   591  O O   . ALA A 1 89  ? -18.02398 11.29714  -36.52524 1.000 85.15242  ? 89  ALA A O   1 
ATOM   592  C CB  . ALA A 1 89  ? -15.42215 9.22772   -36.50172 1.000 77.54250  ? 89  ALA A CB  1 
ATOM   593  N N   . ASN A 1 90  ? -18.52316 9.10992   -36.78507 1.000 79.19084  ? 90  ASN A N   1 
ATOM   594  C CA  . ASN A 1 90  ? -19.80686 9.21122   -36.10187 1.000 72.35059  ? 90  ASN A CA  1 
ATOM   595  C C   . ASN A 1 90  ? -19.60184 9.00362   -34.60992 1.000 74.27746  ? 90  ASN A C   1 
ATOM   596  O O   . ASN A 1 90  ? -18.75342 8.20916   -34.19589 1.000 73.01985  ? 90  ASN A O   1 
ATOM   597  C CB  . ASN A 1 90  ? -20.80909 8.18845   -36.63259 1.000 71.37263  ? 90  ASN A CB  1 
ATOM   598  C CG  . ASN A 1 90  ? -21.12161 8.39217   -38.09426 1.000 102.27085 ? 90  ASN A CG  1 
ATOM   599  O OD1 . ASN A 1 90  ? -20.87364 7.51127   -38.91749 1.000 111.08161 ? 90  ASN A OD1 1 
ATOM   600  N ND2 . ASN A 1 90  ? -21.63847 9.56900   -38.43431 1.000 106.91346 ? 90  ASN A ND2 1 
ATOM   601  N N   . PHE A 1 91  ? -20.37375 9.72479   -33.80303 1.000 60.68443  ? 91  PHE A N   1 
ATOM   602  C CA  . PHE A 1 91  ? -20.26776 9.62822   -32.35496 1.000 51.53288  ? 91  PHE A CA  1 
ATOM   603  C C   . PHE A 1 91  ? -21.65334 9.48895   -31.74300 1.000 56.96118  ? 91  PHE A C   1 
ATOM   604  O O   . PHE A 1 91  ? -22.59107 10.18120  -32.14979 1.000 74.25198  ? 91  PHE A O   1 
ATOM   605  C CB  . PHE A 1 91  ? -19.56433 10.84691  -31.76212 1.000 60.04764  ? 91  PHE A CB  1 
ATOM   606  C CG  . PHE A 1 91  ? -18.07519 10.84176  -31.94972 1.000 66.97037  ? 91  PHE A CG  1 
ATOM   607  C CD1 . PHE A 1 91  ? -17.26181 10.05415  -31.15161 1.000 69.25667  ? 91  PHE A CD1 1 
ATOM   608  C CD2 . PHE A 1 91  ? -17.48760 11.64797  -32.91058 1.000 69.57587  ? 91  PHE A CD2 1 
ATOM   609  C CE1 . PHE A 1 91  ? -15.89157 10.05752  -31.32060 1.000 71.42164  ? 91  PHE A CE1 1 
ATOM   610  C CE2 . PHE A 1 91  ? -16.12011 11.65861  -33.08345 1.000 69.65793  ? 91  PHE A CE2 1 
ATOM   611  C CZ  . PHE A 1 91  ? -15.31994 10.86040  -32.28723 1.000 76.52524  ? 91  PHE A CZ  1 
ATOM   612  N N   . PHE A 1 92  ? -21.78372 8.59010   -30.77109 1.000 58.57923  ? 92  PHE A N   1 
ATOM   613  C CA  . PHE A 1 92  ? -23.02590 8.43158   -30.03291 1.000 56.16657  ? 92  PHE A CA  1 
ATOM   614  C C   . PHE A 1 92  ? -22.69180 8.38416   -28.55225 1.000 57.89433  ? 92  PHE A C   1 
ATOM   615  O O   . PHE A 1 92  ? -21.63190 7.89057   -28.15824 1.000 60.97495  ? 92  PHE A O   1 
ATOM   616  C CB  . PHE A 1 92  ? -23.78308 7.15872   -30.45719 1.000 64.58699  ? 92  PHE A CB  1 
ATOM   617  C CG  . PHE A 1 92  ? -23.96616 7.03445   -31.94482 1.000 66.14691  ? 92  PHE A CG  1 
ATOM   618  C CD1 . PHE A 1 92  ? -23.00161 6.41568   -32.72536 1.000 65.83803  ? 92  PHE A CD1 1 
ATOM   619  C CD2 . PHE A 1 92  ? -25.09381 7.54384   -32.56325 1.000 71.79522  ? 92  PHE A CD2 1 
ATOM   620  C CE1 . PHE A 1 92  ? -23.16070 6.30944   -34.09344 1.000 75.67911  ? 92  PHE A CE1 1 
ATOM   621  C CE2 . PHE A 1 92  ? -25.25914 7.43996   -33.93355 1.000 77.71863  ? 92  PHE A CE2 1 
ATOM   622  C CZ  . PHE A 1 92  ? -24.29228 6.82357   -34.69795 1.000 74.12092  ? 92  PHE A CZ  1 
ATOM   623  N N   . LEU A 1 93  ? -23.61296 8.87894   -27.73181 1.000 61.04582  ? 93  LEU A N   1 
ATOM   624  C CA  . LEU A 1 93  ? -23.46686 8.85377   -26.28394 1.000 50.82055  ? 93  LEU A CA  1 
ATOM   625  C C   . LEU A 1 93  ? -24.67273 8.16689   -25.67114 1.000 57.44767  ? 93  LEU A C   1 
ATOM   626  O O   . LEU A 1 93  ? -25.81564 8.56022   -25.92694 1.000 63.20143  ? 93  LEU A O   1 
ATOM   627  C CB  . LEU A 1 93  ? -23.30275 10.26677  -25.71944 1.000 47.42988  ? 93  LEU A CB  1 
ATOM   628  C CG  . LEU A 1 93  ? -22.62620 10.32653  -24.35469 1.000 55.12601  ? 93  LEU A CG  1 
ATOM   629  C CD1 . LEU A 1 93  ? -21.16803 9.88954   -24.44036 1.000 46.38949  ? 93  LEU A CD1 1 
ATOM   630  C CD2 . LEU A 1 93  ? -22.75201 11.73042  -23.77703 1.000 50.58622  ? 93  LEU A CD2 1 
ATOM   631  N N   . PHE A 1 94  ? -24.40569 7.15538   -24.85451 1.000 55.92155  ? 94  PHE A N   1 
ATOM   632  C CA  . PHE A 1 94  ? -25.42043 6.29413   -24.27267 1.000 47.42515  ? 94  PHE A CA  1 
ATOM   633  C C   . PHE A 1 94  ? -25.43995 6.47496   -22.76254 1.000 57.76581  ? 94  PHE A C   1 
ATOM   634  O O   . PHE A 1 94  ? -24.38797 6.46420   -22.11379 1.000 57.75400  ? 94  PHE A O   1 
ATOM   635  C CB  . PHE A 1 94  ? -25.13917 4.83052   -24.64357 1.000 58.79539  ? 94  PHE A CB  1 
ATOM   636  C CG  . PHE A 1 94  ? -26.05838 3.83824   -23.99175 1.000 58.67364  ? 94  PHE A CG  1 
ATOM   637  C CD1 . PHE A 1 94  ? -27.43313 3.94310   -24.13319 1.000 63.17100  ? 94  PHE A CD1 1 
ATOM   638  C CD2 . PHE A 1 94  ? -25.54328 2.78080   -23.25821 1.000 61.99119  ? 94  PHE A CD2 1 
ATOM   639  C CE1 . PHE A 1 94  ? -28.27882 3.01920   -23.54479 1.000 70.54554  ? 94  PHE A CE1 1 
ATOM   640  C CE2 . PHE A 1 94  ? -26.38470 1.84941   -22.67199 1.000 65.73020  ? 94  PHE A CE2 1 
ATOM   641  C CZ  . PHE A 1 94  ? -27.75258 1.97105   -22.81265 1.000 67.91597  ? 94  PHE A CZ  1 
ATOM   642  N N   . ALA A 1 95  ? -26.64010 6.58835   -22.20346 1.000 55.23727  ? 95  ALA A N   1 
ATOM   643  C CA  . ALA A 1 95  ? -26.83465 6.86816   -20.78818 1.000 55.02902  ? 95  ALA A CA  1 
ATOM   644  C C   . ALA A 1 95  ? -27.32770 5.60924   -20.08183 1.000 61.23067  ? 95  ALA A C   1 
ATOM   645  O O   . ALA A 1 95  ? -28.24059 4.93391   -20.56466 1.000 59.59798  ? 95  ALA A O   1 
ATOM   646  C CB  . ALA A 1 95  ? -27.82456 8.01818   -20.58555 1.000 49.39679  ? 95  ALA A CB  1 
ATOM   647  N N   . THR A 1 96  ? -26.70920 5.29730   -18.94623 1.000 54.83125  ? 96  THR A N   1 
ATOM   648  C CA  . THR A 1 96  ? -27.14227 4.23668   -18.05147 1.000 62.81523  ? 96  THR A CA  1 
ATOM   649  C C   . THR A 1 96  ? -27.32955 4.83418   -16.66710 1.000 61.36445  ? 96  THR A C   1 
ATOM   650  O O   . THR A 1 96  ? -26.72425 5.84909   -16.31651 1.000 64.79937  ? 96  THR A O   1 
ATOM   651  C CB  . THR A 1 96  ? -26.15023 3.04617   -17.97593 1.000 56.95611  ? 96  THR A CB  1 
ATOM   652  O OG1 . THR A 1 96  ? -24.84908 3.50130   -17.58841 1.000 67.08515  ? 96  THR A OG1 1 
ATOM   653  C CG2 . THR A 1 96  ? -26.05531 2.33176   -19.30924 1.000 49.74956  ? 96  THR A CG2 1 
ATOM   654  N N   . LEU A 1 97  ? -28.17261 4.18130   -15.87733 1.000 64.84227  ? 97  LEU A N   1 
ATOM   655  C CA  . LEU A 1 97  ? -28.54238 4.65051   -14.55184 1.000 64.17652  ? 97  LEU A CA  1 
ATOM   656  C C   . LEU A 1 97  ? -27.91535 3.71267   -13.53824 1.000 70.50910  ? 97  LEU A C   1 
ATOM   657  O O   . LEU A 1 97  ? -28.22829 2.51919   -13.51373 1.000 74.16987  ? 97  LEU A O   1 
ATOM   658  C CB  . LEU A 1 97  ? -30.06069 4.66752   -14.38836 1.000 62.98658  ? 97  LEU A CB  1 
ATOM   659  C CG  . LEU A 1 97  ? -30.64123 5.50438   -13.25333 1.000 66.11144  ? 97  LEU A CG  1 
ATOM   660  C CD1 . LEU A 1 97  ? -30.45428 6.98309   -13.50653 1.000 67.46755  ? 97  LEU A CD1 1 
ATOM   661  C CD2 . LEU A 1 97  ? -32.10610 5.16441   -13.08331 1.000 72.90315  ? 97  LEU A CD2 1 
ATOM   662  N N   . GLU A 1 98  ? -27.03427 4.25477   -12.70564 1.000 76.16983  ? 98  GLU A N   1 
ATOM   663  C CA  . GLU A 1 98  ? -26.33436 3.44484   -11.71955 1.000 80.71344  ? 98  GLU A CA  1 
ATOM   664  C C   . GLU A 1 98  ? -26.83151 3.77392   -10.32300 1.000 76.84888  ? 98  GLU A C   1 
ATOM   665  O O   . GLU A 1 98  ? -26.65519 4.91131   -9.85848  1.000 82.78804  ? 98  GLU A O   1 
ATOM   666  C CB  . GLU A 1 98  ? -24.82445 3.68067   -11.81715 1.000 85.75965  ? 98  GLU A CB  1 
ATOM   667  C CG  . GLU A 1 98  ? -24.30341 3.83343   -13.24902 1.000 93.47057  ? 98  GLU A CG  1 
ATOM   668  C CD  . GLU A 1 98  ? -24.34030 2.54278   -14.06501 1.000 121.88616 ? 98  GLU A CD  1 
ATOM   669  O OE1 . GLU A 1 98  ? -24.77932 1.49262   -13.54271 1.000 117.02995 ? 98  GLU A OE1 1 
ATOM   670  O OE2 . GLU A 1 98  ? -23.95467 2.59079   -15.25449 1.000 103.88465 ? 98  GLU A OE2 1 
ATOM   671  N N   . PRO A 1 99  ? -27.47237 2.83550   -9.63462  1.000 90.64658  ? 99  PRO A N   1 
ATOM   672  C CA  . PRO A 1 99  ? -27.88783 3.09218   -8.25287  1.000 88.44023  ? 99  PRO A CA  1 
ATOM   673  C C   . PRO A 1 99  ? -26.71034 3.47058   -7.36929  1.000 95.97211  ? 99  PRO A C   1 
ATOM   674  O O   . PRO A 1 99  ? -25.62702 2.88822   -7.45448  1.000 100.21020 ? 99  PRO A O   1 
ATOM   675  C CB  . PRO A 1 99  ? -28.50805 1.75853   -7.83388  1.000 82.58624  ? 99  PRO A CB  1 
ATOM   676  C CG  . PRO A 1 99  ? -29.02174 1.21007   -9.13473  1.000 84.15617  ? 99  PRO A CG  1 
ATOM   677  C CD  . PRO A 1 99  ? -27.93258 1.51380   -10.10624 1.000 93.08664  ? 99  PRO A CD  1 
ATOM   678  N N   . GLU A 1 100 ? -26.93408 4.46551   -6.51363  1.000 105.88462 ? 100 GLU A N   1 
ATOM   679  C CA  . GLU A 1 100 ? -25.90243 4.85866   -5.56658  1.000 116.18814 ? 100 GLU A CA  1 
ATOM   680  C C   . GLU A 1 100 ? -25.93327 4.00047   -4.31275  1.000 126.46226 ? 100 GLU A C   1 
ATOM   681  O O   . GLU A 1 100 ? -24.94476 3.97116   -3.57311  1.000 134.26392 ? 100 GLU A O   1 
ATOM   682  C CB  . GLU A 1 100 ? -26.05340 6.33262   -5.18455  1.000 122.32052 ? 100 GLU A CB  1 
ATOM   683  C CG  . GLU A 1 100 ? -25.23219 7.29685   -6.04130  1.000 119.54314 ? 100 GLU A CG  1 
ATOM   684  C CD  . GLU A 1 100 ? -23.75485 7.33836   -5.66658  1.000 134.19041 ? 100 GLU A CD  1 
ATOM   685  O OE1 . GLU A 1 100 ? -23.06788 6.29956   -5.79199  1.000 131.15679 ? 100 GLU A OE1 1 
ATOM   686  O OE2 . GLU A 1 100 ? -23.27896 8.41265   -5.24110  1.000 118.76726 ? 100 GLU A OE2 1 
ATOM   687  N N   . ARG A 1 101 ? -27.03622 3.29541   -4.07768  1.000 130.13196 ? 101 ARG A N   1 
ATOM   688  C CA  . ARG A 1 101 ? -27.19249 2.38863   -2.94634  1.000 138.48069 ? 101 ARG A CA  1 
ATOM   689  C C   . ARG A 1 101 ? -28.13654 1.24649   -3.31018  1.000 131.18721 ? 101 ARG A C   1 
ATOM   690  O O   . ARG A 1 101 ? -29.35131 1.35182   -3.14409  1.000 127.53113 ? 101 ARG A O   1 
ATOM   691  C CB  . ARG A 1 101 ? -27.71529 3.13370   -1.71518  1.000 149.68492 ? 101 ARG A CB  1 
ATOM   692  C CG  . ARG A 1 101 ? -27.60132 2.33873   -0.42776  1.000 158.43209 ? 101 ARG A CG  1 
ATOM   693  C CD  . ARG A 1 101 ? -28.20016 3.09138   0.74617   1.000 166.14699 ? 101 ARG A CD  1 
ATOM   694  N NE  . ARG A 1 101 ? -28.19225 2.29522   1.96930   1.000 174.91527 ? 101 ARG A NE  1 
ATOM   695  C CZ  . ARG A 1 101 ? -27.10191 1.89553   2.61013   1.000 176.72377 ? 101 ARG A CZ  1 
ATOM   696  N NH1 . ARG A 1 101 ? -25.89602 2.30738   2.25173   1.000 174.26407 ? 101 ARG A NH1 1 
ATOM   697  N NH2 . ARG A 1 101 ? -27.22879 1.09921   3.66717   1.000 172.67843 ? 101 ARG A NH2 1 
ATOM   698  N N   . PRO A 1 115 ? -37.88284 -1.22247  -17.22734 1.000 117.72224 ? 115 PRO A N   1 
ATOM   699  C CA  . PRO A 1 115 ? -36.56120 -0.69743  -16.87040 1.000 121.19437 ? 115 PRO A CA  1 
ATOM   700  C C   . PRO A 1 115 ? -36.65196 0.58161   -16.04050 1.000 111.72420 ? 115 PRO A C   1 
ATOM   701  O O   . PRO A 1 115 ? -37.61050 1.33413   -16.19544 1.000 112.61733 ? 115 PRO A O   1 
ATOM   702  C CB  . PRO A 1 115 ? -35.92200 -0.41519  -18.24268 1.000 97.90663  ? 115 PRO A CB  1 
ATOM   703  C CG  . PRO A 1 115 ? -36.88386 -1.06307  -19.29672 1.000 108.82921 ? 115 PRO A CG  1 
ATOM   704  C CD  . PRO A 1 115 ? -37.84840 -1.90748  -18.52408 1.000 100.72952 ? 115 PRO A CD  1 
ATOM   705  N N   . VAL A 1 116 ? -35.65705 0.81516   -15.17944 1.000 105.19320 ? 116 VAL A N   1 
ATOM   706  C CA  . VAL A 1 116 ? -35.66691 1.99629   -14.31931 1.000 98.36240  ? 116 VAL A CA  1 
ATOM   707  C C   . VAL A 1 116 ? -35.52352 3.27477   -15.13750 1.000 85.22029  ? 116 VAL A C   1 
ATOM   708  O O   . VAL A 1 116 ? -36.16931 4.28788   -14.84846 1.000 94.90390  ? 116 VAL A O   1 
ATOM   709  C CB  . VAL A 1 116 ? -34.58120 1.88817   -13.23688 1.000 89.94874  ? 116 VAL A CB  1 
ATOM   710  C CG1 . VAL A 1 116 ? -34.92371 2.81575   -12.07474 1.000 97.66326  ? 116 VAL A CG1 1 
ATOM   711  C CG2 . VAL A 1 116 ? -34.44643 0.44626   -12.76489 1.000 101.64082 ? 116 VAL A CG2 1 
ATOM   712  N N   . LEU A 1 117 ? -34.67876 3.25435   -16.16285 1.000 79.77623  ? 117 LEU A N   1 
ATOM   713  C CA  . LEU A 1 117 ? -34.49734 4.39348   -17.05260 1.000 73.50108  ? 117 LEU A CA  1 
ATOM   714  C C   . LEU A 1 117 ? -35.35661 4.21342   -18.29677 1.000 84.37727  ? 117 LEU A C   1 
ATOM   715  O O   . LEU A 1 117 ? -35.20521 3.22819   -19.02699 1.000 92.92582  ? 117 LEU A O   1 
ATOM   716  C CB  . LEU A 1 117 ? -33.02362 4.54513   -17.43048 1.000 69.69034  ? 117 LEU A CB  1 
ATOM   717  C CG  . LEU A 1 117 ? -32.65758 5.82290   -18.19208 1.000 65.19283  ? 117 LEU A CG  1 
ATOM   718  C CD1 . LEU A 1 117 ? -32.95007 7.06768   -17.37274 1.000 72.73046  ? 117 LEU A CD1 1 
ATOM   719  C CD2 . LEU A 1 117 ? -31.19539 5.79105   -18.60569 1.000 70.08547  ? 117 LEU A CD2 1 
ATOM   720  N N   . THR A 1 118 ? -36.23789 5.17728   -18.54622 1.000 84.34750  ? 118 THR A N   1 
ATOM   721  C CA  . THR A 1 118 ? -37.10546 5.15029   -19.70900 1.000 87.05453  ? 118 THR A CA  1 
ATOM   722  C C   . THR A 1 118 ? -36.88921 6.40644   -20.54048 1.000 81.82562  ? 118 THR A C   1 
ATOM   723  O O   . THR A 1 118 ? -36.39721 7.42826   -20.05436 1.000 82.94187  ? 118 THR A O   1 
ATOM   724  C CB  . THR A 1 118 ? -38.58768 5.05546   -19.30238 1.000 97.43658  ? 118 THR A CB  1 
ATOM   725  O OG1 . THR A 1 118 ? -38.71631 4.25558   -18.12100 1.000 108.63368 ? 118 THR A OG1 1 
ATOM   726  C CG2 . THR A 1 118 ? -39.41143 4.41658   -20.41595 1.000 115.74415 ? 118 THR A CG2 1 
ATOM   727  N N   . GLY A 1 119 ? -37.27745 6.31925   -21.80519 1.000 78.80875  ? 119 GLY A N   1 
ATOM   728  C CA  . GLY A 1 119 ? -37.06485 7.40104   -22.73734 1.000 62.07057  ? 119 GLY A CA  1 
ATOM   729  C C   . GLY A 1 119 ? -36.08036 7.05281   -23.82715 1.000 71.86105  ? 119 GLY A C   1 
ATOM   730  O O   . GLY A 1 119 ? -35.97178 5.89491   -24.24162 1.000 83.59917  ? 119 GLY A O   1 
ATOM   731  N N   . VAL A 1 120 ? -35.35188 8.05844   -24.29400 1.000 77.98187  ? 120 VAL A N   1 
ATOM   732  C CA  . VAL A 1 120 ? -34.34744 7.87485   -25.33299 1.000 67.95007  ? 120 VAL A CA  1 
ATOM   733  C C   . VAL A 1 120 ? -32.98266 8.04031   -24.68166 1.000 69.77713  ? 120 VAL A C   1 
ATOM   734  O O   . VAL A 1 120 ? -32.57325 9.17199   -24.38915 1.000 65.75847  ? 120 VAL A O   1 
ATOM   735  C CB  . VAL A 1 120 ? -34.55342 8.86562   -26.48624 1.000 64.18415  ? 120 VAL A CB  1 
ATOM   736  C CG1 . VAL A 1 120 ? -33.42994 8.73746   -27.50917 1.000 62.09913  ? 120 VAL A CG1 1 
ATOM   737  C CG2 . VAL A 1 120 ? -35.91818 8.64761   -27.12191 1.000 63.51173  ? 120 VAL A CG2 1 
ATOM   738  N N   . PRO A 1 121 ? -32.26120 6.95444   -24.41496 1.000 70.61999  ? 121 PRO A N   1 
ATOM   739  C CA  . PRO A 1 121 ? -30.96074 7.05865   -23.74224 1.000 53.79174  ? 121 PRO A CA  1 
ATOM   740  C C   . PRO A 1 121 ? -29.75931 7.20877   -24.66685 1.000 55.66775  ? 121 PRO A C   1 
ATOM   741  O O   . PRO A 1 121 ? -28.62713 7.14495   -24.17800 1.000 61.53951  ? 121 PRO A O   1 
ATOM   742  C CB  . PRO A 1 121 ? -30.89462 5.72621   -22.98652 1.000 64.27231  ? 121 PRO A CB  1 
ATOM   743  C CG  . PRO A 1 121 ? -31.60880 4.76357   -23.89599 1.000 53.14829  ? 121 PRO A CG  1 
ATOM   744  C CD  . PRO A 1 121 ? -32.69246 5.55520   -24.58418 1.000 61.73798  ? 121 PRO A CD  1 
ATOM   745  N N   . VAL A 1 122 ? -29.96306 7.41889   -25.96740 1.000 54.35518  ? 122 VAL A N   1 
ATOM   746  C CA  . VAL A 1 122 ? -28.87759 7.57472   -26.93195 1.000 60.10029  ? 122 VAL A CA  1 
ATOM   747  C C   . VAL A 1 122 ? -28.98482 8.95029   -27.58128 1.000 66.81663  ? 122 VAL A C   1 
ATOM   748  O O   . VAL A 1 122 ? -30.04185 9.31141   -28.11079 1.000 69.44371  ? 122 VAL A O   1 
ATOM   749  C CB  . VAL A 1 122 ? -28.89688 6.47118   -28.00282 1.000 66.52303  ? 122 VAL A CB  1 
ATOM   750  C CG1 . VAL A 1 122 ? -27.80803 6.73157   -29.02109 1.000 63.37001  ? 122 VAL A CG1 1 
ATOM   751  C CG2 . VAL A 1 122 ? -28.74109 5.09741   -27.36524 1.000 68.22119  ? 122 VAL A CG2 1 
ATOM   752  N N   . ALA A 1 123 ? -27.89163 9.70501   -27.56304 1.000 65.15105  ? 123 ALA A N   1 
ATOM   753  C CA  . ALA A 1 123 ? -27.85064 11.03013  -28.16531 1.000 60.56377  ? 123 ALA A CA  1 
ATOM   754  C C   . ALA A 1 123 ? -26.77530 11.08252  -29.23976 1.000 58.05783  ? 123 ALA A C   1 
ATOM   755  O O   . ALA A 1 123 ? -25.65033 10.61833  -29.02953 1.000 64.95787  ? 123 ALA A O   1 
ATOM   756  C CB  . ALA A 1 123 ? -27.58007 12.11772  -27.11544 1.000 55.85772  ? 123 ALA A CB  1 
ATOM   757  N N   . GLY A 1 124 ? -27.11991 11.66642  -30.38544 1.000 58.70259  ? 124 GLY A N   1 
ATOM   758  C CA  . GLY A 1 124 ? -26.12355 11.95303  -31.39424 1.000 58.17479  ? 124 GLY A CA  1 
ATOM   759  C C   . GLY A 1 124 ? -25.37682 13.23492  -31.07366 1.000 61.05904  ? 124 GLY A C   1 
ATOM   760  O O   . GLY A 1 124 ? -25.71628 13.96887  -30.14725 1.000 69.29486  ? 124 GLY A O   1 
ATOM   761  N N   . VAL A 1 125 ? -24.33054 13.50170  -31.84116 1.000 67.58308  ? 125 VAL A N   1 
ATOM   762  C CA  . VAL A 1 125 ? -23.48405 14.66300  -31.58327 1.000 69.64132  ? 125 VAL A CA  1 
ATOM   763  C C   . VAL A 1 125 ? -23.98033 15.86184  -32.38015 1.000 68.46365  ? 125 VAL A C   1 
ATOM   764  O O   . VAL A 1 125 ? -24.46064 15.73354  -33.51365 1.000 69.05597  ? 125 VAL A O   1 
ATOM   765  C CB  . VAL A 1 125 ? -22.00521 14.35431  -31.89610 1.000 65.69224  ? 125 VAL A CB  1 
ATOM   766  C CG1 . VAL A 1 125 ? -21.76626 14.29871  -33.39167 1.000 66.57898  ? 125 VAL A CG1 1 
ATOM   767  C CG2 . VAL A 1 125 ? -21.09571 15.40363  -31.25073 1.000 55.08900  ? 125 VAL A CG2 1 
ATOM   768  N N   . ALA A 1 126 ? -23.87892 17.03974  -31.77341 1.000 69.33833  ? 126 ALA A N   1 
ATOM   769  C CA  . ALA A 1 126 ? -24.15569 18.29321  -32.45952 1.000 63.39535  ? 126 ALA A CA  1 
ATOM   770  C C   . ALA A 1 126 ? -22.94917 19.19279  -32.28290 1.000 63.57789  ? 126 ALA A C   1 
ATOM   771  O O   . ALA A 1 126 ? -22.47899 19.39221  -31.15791 1.000 68.47464  ? 126 ALA A O   1 
ATOM   772  C CB  . ALA A 1 126 ? -25.41764 18.97705  -31.92365 1.000 65.25911  ? 126 ALA A CB  1 
ATOM   773  N N   . TYR A 1 127 ? -22.40307 19.66227  -33.39410 1.000 66.09134  ? 127 TYR A N   1 
ATOM   774  C CA  . TYR A 1 127 ? -21.19418 20.46712  -33.37182 1.000 75.03204  ? 127 TYR A CA  1 
ATOM   775  C C   . TYR A 1 127 ? -21.60077 21.93103  -33.25749 1.000 81.45200  ? 127 TYR A C   1 
ATOM   776  O O   . TYR A 1 127 ? -22.34531 22.43912  -34.10261 1.000 89.70825  ? 127 TYR A O   1 
ATOM   777  C CB  . TYR A 1 127 ? -20.35735 20.21119  -34.62245 1.000 67.06371  ? 127 TYR A CB  1 
ATOM   778  C CG  . TYR A 1 127 ? -19.80578 18.80789  -34.66337 1.000 76.62796  ? 127 TYR A CG  1 
ATOM   779  C CD1 . TYR A 1 127 ? -18.69096 18.46046  -33.90807 1.000 74.60061  ? 127 TYR A CD1 1 
ATOM   780  C CD2 . TYR A 1 127 ? -20.41287 17.82216  -35.43079 1.000 64.40627  ? 127 TYR A CD2 1 
ATOM   781  C CE1 . TYR A 1 127 ? -18.18585 17.17759  -33.92899 1.000 78.77712  ? 127 TYR A CE1 1 
ATOM   782  C CE2 . TYR A 1 127 ? -19.91341 16.53378  -35.45900 1.000 69.76423  ? 127 TYR A CE2 1 
ATOM   783  C CZ  . TYR A 1 127 ? -18.79881 16.21712  -34.70466 1.000 79.71023  ? 127 TYR A CZ  1 
ATOM   784  O OH  . TYR A 1 127 ? -18.29162 14.93643  -34.72267 1.000 73.60258  ? 127 TYR A OH  1 
ATOM   785  N N   . LEU A 1 128 ? -21.13457 22.59680  -32.20526 1.000 80.40169  ? 128 LEU A N   1 
ATOM   786  C CA  . LEU A 1 128 ? -21.46787 23.98826  -31.95254 1.000 88.59930  ? 128 LEU A CA  1 
ATOM   787  C C   . LEU A 1 128 ? -20.20554 24.75597  -31.60154 1.000 90.53786  ? 128 LEU A C   1 
ATOM   788  O O   . LEU A 1 128 ? -19.21630 24.19077  -31.12866 1.000 84.56690  ? 128 LEU A O   1 
ATOM   789  C CB  . LEU A 1 128 ? -22.49464 24.16050  -30.81904 1.000 84.30818  ? 128 LEU A CB  1 
ATOM   790  C CG  . LEU A 1 128 ? -23.59842 23.13035  -30.59470 1.000 86.06731  ? 128 LEU A CG  1 
ATOM   791  C CD1 . LEU A 1 128 ? -24.32995 23.42247  -29.29029 1.000 70.71059  ? 128 LEU A CD1 1 
ATOM   792  C CD2 . LEU A 1 128 ? -24.56781 23.14749  -31.76049 1.000 96.01593  ? 128 LEU A CD2 1 
ATOM   793  N N   . ASP A 1 129 ? -20.26905 26.06923  -31.80880 1.000 89.92296  ? 129 ASP A N   1 
ATOM   794  C CA  . ASP A 1 129 ? -19.12949 26.93762  -31.56379 1.000 97.98214  ? 129 ASP A CA  1 
ATOM   795  C C   . ASP A 1 129 ? -19.19984 27.60304  -30.20144 1.000 88.29807  ? 129 ASP A C   1 
ATOM   796  O O   . ASP A 1 129 ? -18.16730 28.04331  -29.68672 1.000 95.63274  ? 129 ASP A O   1 
ATOM   797  C CB  . ASP A 1 129 ? -19.04316 28.02500  -32.64394 1.000 105.08019 ? 129 ASP A CB  1 
ATOM   798  C CG  . ASP A 1 129 ? -18.79539 27.45726  -34.02987 1.000 124.27394 ? 129 ASP A CG  1 
ATOM   799  O OD1 . ASP A 1 129 ? -17.74158 26.81634  -34.23652 1.000 127.54269 ? 129 ASP A OD1 1 
ATOM   800  O OD2 . ASP A 1 129 ? -19.65044 27.66590  -34.91734 1.000 127.89209 ? 129 ASP A OD2 1 
ATOM   801  N N   . LYS A 1 130 ? -20.39058 27.68470  -29.61656 1.000 87.62604  ? 130 LYS A N   1 
ATOM   802  C CA  . LYS A 1 130 ? -20.60090 28.32415  -28.33649 1.000 96.54980  ? 130 LYS A CA  1 
ATOM   803  C C   . LYS A 1 130 ? -21.28331 27.34899  -27.38756 1.000 95.71923  ? 130 LYS A C   1 
ATOM   804  O O   . LYS A 1 130 ? -22.15116 26.57700  -27.81282 1.000 95.14955  ? 130 LYS A O   1 
ATOM   805  C CB  . LYS A 1 130 ? -21.46209 29.58508  -28.50235 1.000 97.88796  ? 130 LYS A CB  1 
ATOM   806  C CG  . LYS A 1 130 ? -20.72943 30.75092  -29.14919 1.000 91.08705  ? 130 LYS A CG  1 
ATOM   807  C CD  . LYS A 1 130 ? -21.64275 31.95329  -29.33270 1.000 142.40149 ? 130 LYS A CD  1 
ATOM   808  C CE  . LYS A 1 130 ? -23.04602 31.52559  -29.74257 1.000 146.67090 ? 130 LYS A CE  1 
ATOM   809  N NZ  . LYS A 1 130 ? -24.10298 32.30072  -29.03511 1.000 140.99536 ? 130 LYS A NZ  1 
ATOM   810  N N   . PRO A 1 131 ? -20.91624 27.35420  -26.09960 1.000 96.59943  ? 131 PRO A N   1 
ATOM   811  C CA  . PRO A 1 131 ? -19.92758 28.22922  -25.45240 1.000 88.92426  ? 131 PRO A CA  1 
ATOM   812  C C   . PRO A 1 131 ? -18.48853 27.85038  -25.80096 1.000 83.95283  ? 131 PRO A C   1 
ATOM   813  O O   . PRO A 1 131 ? -17.57487 28.64417  -25.60396 1.000 98.03748  ? 131 PRO A O   1 
ATOM   814  C CB  . PRO A 1 131 ? -20.22838 28.02952  -23.96142 1.000 78.77428  ? 131 PRO A CB  1 
ATOM   815  C CG  . PRO A 1 131 ? -20.72435 26.61453  -23.88388 1.000 94.09314  ? 131 PRO A CG  1 
ATOM   816  C CD  . PRO A 1 131 ? -21.54324 26.43125  -25.13654 1.000 85.72109  ? 131 PRO A CD  1 
ATOM   817  N N   . ASN A 1 132 ? -18.26890 26.65800  -26.35615 1.000 90.41759  ? 132 ASN A N   1 
ATOM   818  C CA  . ASN A 1 132 ? -16.95240 26.23369  -26.80900 1.000 76.87225  ? 132 ASN A CA  1 
ATOM   819  C C   . ASN A 1 132 ? -17.07323 25.50738  -28.13720 1.000 81.69701  ? 132 ASN A C   1 
ATOM   820  O O   . ASN A 1 132 ? -18.12043 24.93761  -28.45504 1.000 85.94254  ? 132 ASN A O   1 
ATOM   821  C CB  . ASN A 1 132 ? -16.28731 25.27164  -25.81214 1.000 71.88818  ? 132 ASN A CB  1 
ATOM   822  C CG  . ASN A 1 132 ? -16.03625 25.89618  -24.45722 1.000 96.24251  ? 132 ASN A CG  1 
ATOM   823  O OD1 . ASN A 1 132 ? -15.78519 27.09492  -24.34346 1.000 92.15259  ? 132 ASN A OD1 1 
ATOM   824  N ND2 . ASN A 1 132 ? -16.10377 25.07609  -23.41326 1.000 97.35318  ? 132 ASN A ND2 1 
ATOM   825  N N   . ARG A 1 133 ? -15.99448 25.54128  -28.91809 1.000 82.27422  ? 133 ARG A N   1 
ATOM   826  C CA  . ARG A 1 133 ? -15.96065 24.82418  -30.19034 1.000 89.03172  ? 133 ARG A CA  1 
ATOM   827  C C   . ARG A 1 133 ? -15.79213 23.35251  -29.84456 1.000 80.02242  ? 133 ARG A C   1 
ATOM   828  O O   . ARG A 1 133 ? -14.69352 22.91146  -29.49988 1.000 85.05596  ? 133 ARG A O   1 
ATOM   829  C CB  . ARG A 1 133 ? -14.82226 25.31070  -31.08215 1.000 82.17092  ? 133 ARG A CB  1 
ATOM   830  C CG  . ARG A 1 133 ? -14.62078 26.80121  -31.12312 1.000 89.86393  ? 133 ARG A CG  1 
ATOM   831  C CD  . ARG A 1 133 ? -14.89626 27.31380  -32.52078 1.000 104.93713 ? 133 ARG A CD  1 
ATOM   832  N NE  . ARG A 1 133 ? -14.77945 28.76225  -32.60682 1.000 109.91216 ? 133 ARG A NE  1 
ATOM   833  C CZ  . ARG A 1 133 ? -15.20695 29.47817  -33.63633 1.000 125.15017 ? 133 ARG A CZ  1 
ATOM   834  N NH1 . ARG A 1 133 ? -15.78400 28.90583  -34.68086 1.000 106.59057 ? 133 ARG A NH1 1 
ATOM   835  N NH2 . ARG A 1 133 ? -15.07837 30.80228  -33.60478 1.000 144.81189 ? 133 ARG A NH2 1 
ATOM   836  N N   . ALA A 1 134 ? -16.86401 22.58006  -29.94616 1.000 88.15273  ? 134 ALA A N   1 
ATOM   837  C CA  . ALA A 1 134 ? -16.80258 21.16925  -29.57540 1.000 87.89290  ? 134 ALA A CA  1 
ATOM   838  C C   . ALA A 1 134 ? -18.04728 20.46528  -30.10201 1.000 82.06175  ? 134 ALA A C   1 
ATOM   839  O O   . ALA A 1 134 ? -18.86853 21.05890  -30.81264 1.000 79.43050  ? 134 ALA A O   1 
ATOM   840  C CB  . ALA A 1 134 ? -16.67050 21.00907  -28.06073 1.000 81.74537  ? 134 ALA A CB  1 
ATOM   841  N N   . GLY A 1 135 ? -18.18399 19.19451  -29.73293 1.000 75.04587  ? 135 GLY A N   1 
ATOM   842  C CA  . GLY A 1 135 ? -19.38936 18.43076  -29.96950 1.000 61.79696  ? 135 GLY A CA  1 
ATOM   843  C C   . GLY A 1 135 ? -20.19211 18.36636  -28.68486 1.000 63.82376  ? 135 GLY A C   1 
ATOM   844  O O   . GLY A 1 135 ? -19.64028 18.42124  -27.58972 1.000 75.02360  ? 135 GLY A O   1 
ATOM   845  N N   . TYR A 1 136 ? -21.50660 18.24344  -28.82666 1.000 59.53190  ? 136 TYR A N   1 
ATOM   846  C CA  . TYR A 1 136 ? -22.41054 18.32733  -27.69082 1.000 64.25018  ? 136 TYR A CA  1 
ATOM   847  C C   . TYR A 1 136 ? -23.46196 17.23691  -27.79061 1.000 62.18846  ? 136 TYR A C   1 
ATOM   848  O O   . TYR A 1 136 ? -23.98339 16.96407  -28.87637 1.000 55.82573  ? 136 TYR A O   1 
ATOM   849  C CB  . TYR A 1 136 ? -23.09198 19.70057  -27.62234 1.000 67.73655  ? 136 TYR A CB  1 
ATOM   850  C CG  . TYR A 1 136 ? -22.16879 20.82796  -27.22508 1.000 66.03460  ? 136 TYR A CG  1 
ATOM   851  C CD1 . TYR A 1 136 ? -21.95433 21.13088  -25.88628 1.000 67.10849  ? 136 TYR A CD1 1 
ATOM   852  C CD2 . TYR A 1 136 ? -21.48839 21.56918  -28.18228 1.000 68.25363  ? 136 TYR A CD2 1 
ATOM   853  C CE1 . TYR A 1 136 ? -21.10425 22.15646  -25.51017 1.000 77.42742  ? 136 TYR A CE1 1 
ATOM   854  C CE2 . TYR A 1 136 ? -20.63365 22.59486  -27.81778 1.000 75.61222  ? 136 TYR A CE2 1 
ATOM   855  C CZ  . TYR A 1 136 ? -20.44574 22.88527  -26.48070 1.000 79.28205  ? 136 TYR A CZ  1 
ATOM   856  O OH  . TYR A 1 136 ? -19.59759 23.90663  -26.11381 1.000 77.66235  ? 136 TYR A OH  1 
ATOM   857  N N   . PHE A 1 137 ? -23.75850 16.61406  -26.64920 1.000 53.34578  ? 137 PHE A N   1 
ATOM   858  C CA  . PHE A 1 137 ? -24.83212 15.63827  -26.53131 1.000 53.48548  ? 137 PHE A CA  1 
ATOM   859  C C   . PHE A 1 137 ? -25.82131 16.11927  -25.48156 1.000 54.92708  ? 137 PHE A C   1 
ATOM   860  O O   . PHE A 1 137 ? -25.41743 16.51507  -24.38277 1.000 64.55510  ? 137 PHE A O   1 
ATOM   861  C CB  . PHE A 1 137 ? -24.29758 14.25493  -26.13455 1.000 58.12571  ? 137 PHE A CB  1 
ATOM   862  C CG  . PHE A 1 137 ? -23.20088 13.74447  -27.01984 1.000 51.26538  ? 137 PHE A CG  1 
ATOM   863  C CD1 . PHE A 1 137 ? -21.88049 14.06099  -26.75525 1.000 53.63495  ? 137 PHE A CD1 1 
ATOM   864  C CD2 . PHE A 1 137 ? -23.48713 12.94467  -28.11240 1.000 58.85617  ? 137 PHE A CD2 1 
ATOM   865  C CE1 . PHE A 1 137 ? -20.86515 13.59121  -27.56181 1.000 57.65823  ? 137 PHE A CE1 1 
ATOM   866  C CE2 . PHE A 1 137 ? -22.47422 12.47151  -28.92398 1.000 60.07132  ? 137 PHE A CE2 1 
ATOM   867  C CZ  . PHE A 1 137 ? -21.16146 12.79786  -28.64818 1.000 58.75815  ? 137 PHE A CZ  1 
ATOM   868  N N   . ILE A 1 138 ? -27.11213 16.07221  -25.81274 1.000 61.56870  ? 138 ILE A N   1 
ATOM   869  C CA  . ILE A 1 138 ? -28.17644 16.50581  -24.91374 1.000 64.41033  ? 138 ILE A CA  1 
ATOM   870  C C   . ILE A 1 138 ? -29.15945 15.35635  -24.72655 1.000 59.68217  ? 138 ILE A C   1 
ATOM   871  O O   . ILE A 1 138 ? -29.51005 14.65976  -25.68565 1.000 57.57737  ? 138 ILE A O   1 
ATOM   872  C CB  . ILE A 1 138 ? -28.89758 17.76755  -25.44261 1.000 56.50972  ? 138 ILE A CB  1 
ATOM   873  C CG1 . ILE A 1 138 ? -29.99515 18.22474  -24.47509 1.000 55.75885  ? 138 ILE A CG1 1 
ATOM   874  C CG2 . ILE A 1 138 ? -29.49030 17.52831  -26.83540 1.000 53.36385  ? 138 ILE A CG2 1 
ATOM   875  C CD1 . ILE A 1 138 ? -30.05530 19.75862  -24.24892 1.000 62.00946  ? 138 ILE A CD1 1 
ATOM   876  N N   . PHE A 1 139 ? -29.61618 15.16981  -23.48790 1.000 55.19608  ? 139 PHE A N   1 
ATOM   877  C CA  . PHE A 1 139 ? -30.55825 14.11107  -23.13339 1.000 55.74320  ? 139 PHE A CA  1 
ATOM   878  C C   . PHE A 1 139 ? -31.81952 14.73986  -22.55624 1.000 62.70077  ? 139 PHE A C   1 
ATOM   879  O O   . PHE A 1 139 ? -31.94772 14.88190  -21.32872 1.000 64.88355  ? 139 PHE A O   1 
ATOM   880  C CB  . PHE A 1 139 ? -29.93898 13.13626  -22.13357 1.000 60.06858  ? 139 PHE A CB  1 
ATOM   881  C CG  . PHE A 1 139 ? -28.76479 12.37372  -22.67178 1.000 61.15815  ? 139 PHE A CG  1 
ATOM   882  C CD1 . PHE A 1 139 ? -27.48311 12.88986  -22.56688 1.000 59.68738  ? 139 PHE A CD1 1 
ATOM   883  C CD2 . PHE A 1 139 ? -28.93978 11.14204  -23.28506 1.000 63.84721  ? 139 PHE A CD2 1 
ATOM   884  C CE1 . PHE A 1 139 ? -26.39602 12.18972  -23.05561 1.000 61.25981  ? 139 PHE A CE1 1 
ATOM   885  C CE2 . PHE A 1 139 ? -27.85653 10.43836  -23.77763 1.000 62.86004  ? 139 PHE A CE2 1 
ATOM   886  C CZ  . PHE A 1 139 ? -26.58308 10.96454  -23.66234 1.000 61.62464  ? 139 PHE A CZ  1 
ATOM   887  N N   . PRO A 1 140 ? -32.79109 15.11082  -23.39297 1.000 66.33960  ? 140 PRO A N   1 
ATOM   888  C CA  . PRO A 1 140 ? -33.96988 15.81452  -22.88024 1.000 70.62620  ? 140 PRO A CA  1 
ATOM   889  C C   . PRO A 1 140 ? -35.10830 14.90208  -22.45901 1.000 77.34402  ? 140 PRO A C   1 
ATOM   890  O O   . PRO A 1 140 ? -36.10038 15.40269  -21.90962 1.000 81.71551  ? 140 PRO A O   1 
ATOM   891  C CB  . PRO A 1 140 ? -34.38456 16.67842  -24.07701 1.000 60.20089  ? 140 PRO A CB  1 
ATOM   892  C CG  . PRO A 1 140 ? -34.00104 15.85733  -25.25717 1.000 65.66129  ? 140 PRO A CG  1 
ATOM   893  C CD  . PRO A 1 140 ? -32.71865 15.15588  -24.86517 1.000 67.28351  ? 140 PRO A CD  1 
ATOM   894  N N   . ASP A 1 141 ? -35.01164 13.59902  -22.71143 1.000 65.36137  ? 141 ASP A N   1 
ATOM   895  C CA  . ASP A 1 141 ? -36.13838 12.68908  -22.54391 1.000 77.94429  ? 141 ASP A CA  1 
ATOM   896  C C   . ASP A 1 141 ? -35.70664 11.47233  -21.71378 1.000 79.88200  ? 141 ASP A C   1 
ATOM   897  O O   . ASP A 1 141 ? -35.85149 10.32064  -22.12577 1.000 75.27106  ? 141 ASP A O   1 
ATOM   898  C CB  . ASP A 1 141 ? -36.68239 12.29124  -23.91933 1.000 81.42196  ? 141 ASP A CB  1 
ATOM   899  C CG  . ASP A 1 141 ? -37.88582 11.35069  -23.84597 1.000 109.50141 ? 141 ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 141 ? -38.33127 11.00549  -22.72874 1.000 103.32396 ? 141 ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 141 ? -38.37015 10.93141  -24.92227 1.000 102.66348 ? 141 ASP A OD2 1 
ATOM   902  N N   . LEU A 1 142 ? -35.10337 11.71071  -20.55239 1.000 72.68459  ? 142 LEU A N   1 
ATOM   903  C CA  . LEU A 1 142 ? -34.74186 10.64512  -19.62372 1.000 68.65804  ? 142 LEU A CA  1 
ATOM   904  C C   . LEU A 1 142 ? -35.70133 10.65331  -18.44412 1.000 77.15782  ? 142 LEU A C   1 
ATOM   905  O O   . LEU A 1 142 ? -35.93217 11.70483  -17.83893 1.000 83.07977  ? 142 LEU A O   1 
ATOM   906  C CB  . LEU A 1 142 ? -33.30661 10.79776  -19.12038 1.000 69.83516  ? 142 LEU A CB  1 
ATOM   907  C CG  . LEU A 1 142 ? -32.19054 10.89664  -20.14991 1.000 62.23791  ? 142 LEU A CG  1 
ATOM   908  C CD1 . LEU A 1 142 ? -30.86553 10.98979  -19.42870 1.000 71.73917  ? 142 LEU A CD1 1 
ATOM   909  C CD2 . LEU A 1 142 ? -32.21842 9.67754   -21.05786 1.000 67.54181  ? 142 LEU A CD2 1 
ATOM   910  N N   . SER A 1 143 ? -36.24539 9.48889   -18.10862 1.000 72.73589  ? 143 SER A N   1 
ATOM   911  C CA  . SER A 1 143 ? -37.14712 9.36631   -16.97457 1.000 75.34682  ? 143 SER A CA  1 
ATOM   912  C C   . SER A 1 143 ? -36.71669 8.19941   -16.10064 1.000 77.55717  ? 143 SER A C   1 
ATOM   913  O O   . SER A 1 143 ? -36.23938 7.17727   -16.60355 1.000 78.26415  ? 143 SER A O   1 
ATOM   914  C CB  . SER A 1 143 ? -38.59706 9.18192   -17.43302 1.000 93.06834  ? 143 SER A CB  1 
ATOM   915  O OG  . SER A 1 143 ? -38.84202 9.91736   -18.61799 1.000 102.38544 ? 143 SER A OG  1 
ATOM   916  N N   . VAL A 1 144 ? -36.88089 8.36459   -14.79124 1.000 67.82952  ? 144 VAL A N   1 
ATOM   917  C CA  . VAL A 1 144 ? -36.53607 7.35066   -13.80353 1.000 68.24654  ? 144 VAL A CA  1 
ATOM   918  C C   . VAL A 1 144 ? -37.83195 6.81282   -13.21591 1.000 80.62030  ? 144 VAL A C   1 
ATOM   919  O O   . VAL A 1 144 ? -38.72588 7.58589   -12.85100 1.000 82.13395  ? 144 VAL A O   1 
ATOM   920  C CB  . VAL A 1 144 ? -35.60747 7.91362   -12.71430 1.000 68.92741  ? 144 VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 144 ? -35.14271 6.81071   -11.79556 1.000 71.11488  ? 144 VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 144 ? -34.39207 8.56607   -13.36154 1.000 67.38111  ? 144 VAL A CG2 1 
ATOM   923  N N   . ARG A 1 145 ? -37.93077 5.48664   -13.12616 1.000 81.25710  ? 145 ARG A N   1 
ATOM   924  C CA  . ARG A 1 145 ? -39.17799 4.85360   -12.71840 1.000 83.46027  ? 145 ARG A CA  1 
ATOM   925  C C   . ARG A 1 145 ? -39.41443 4.95966   -11.21940 1.000 87.38570  ? 145 ARG A C   1 
ATOM   926  O O   . ARG A 1 145 ? -40.54632 5.19858   -10.78387 1.000 87.38048  ? 145 ARG A O   1 
ATOM   927  C CB  . ARG A 1 145 ? -39.16185 3.38476   -13.13978 1.000 98.11306  ? 145 ARG A CB  1 
ATOM   928  C CG  . ARG A 1 145 ? -39.41806 3.15474   -14.61289 1.000 113.27952 ? 145 ARG A CG  1 
ATOM   929  C CD  . ARG A 1 145 ? -40.84655 2.73134   -14.84456 1.000 125.93114 ? 145 ARG A CD  1 
ATOM   930  N NE  . ARG A 1 145 ? -41.02100 1.94917   -16.06230 1.000 135.42001 ? 145 ARG A NE  1 
ATOM   931  C CZ  . ARG A 1 145 ? -41.62140 2.39670   -17.15648 1.000 145.55669 ? 145 ARG A CZ  1 
ATOM   932  N NH1 . ARG A 1 145 ? -42.14115 3.61274   -17.21149 1.000 157.51251 ? 145 ARG A NH1 1 
ATOM   933  N NH2 . ARG A 1 145 ? -41.71086 1.60153   -18.21859 1.000 141.64757 ? 145 ARG A NH2 1 
ATOM   934  N N   . ASN A 1 146 ? -38.36007 4.83813   -10.42038 1.000 83.60361  ? 146 ASN A N   1 
ATOM   935  C CA  . ASN A 1 146 ? -38.50502 4.72110   -8.98037  1.000 76.48922  ? 146 ASN A CA  1 
ATOM   936  C C   . ASN A 1 146 ? -37.63155 5.73775   -8.26489  1.000 77.35800  ? 146 ASN A C   1 
ATOM   937  O O   . ASN A 1 146 ? -36.58347 6.14761   -8.77072  1.000 83.98060  ? 146 ASN A O   1 
ATOM   938  C CB  . ASN A 1 146 ? -38.13674 3.30620   -8.51752  1.000 86.54528  ? 146 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 146 ? -38.85651 2.23111   -9.30846  1.000 87.65151  ? 146 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 146 ? -40.08448 2.20024   -9.36048  1.000 89.11041  ? 146 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 146 ? -38.08954 1.33981   -9.93148  1.000 83.05774  ? 146 ASN A ND2 1 
ATOM   942  N N   . GLU A 1 147 ? -38.08374 6.14659   -7.08207  1.000 78.90635  ? 147 GLU A N   1 
ATOM   943  C CA  . GLU A 1 147 ? -37.37152 7.15883   -6.32212  1.000 88.24954  ? 147 GLU A CA  1 
ATOM   944  C C   . GLU A 1 147 ? -36.06523 6.59246   -5.77332  1.000 89.77907  ? 147 GLU A C   1 
ATOM   945  O O   . GLU A 1 147 ? -35.87860 5.37810   -5.65691  1.000 102.76408 ? 147 GLU A O   1 
ATOM   946  C CB  . GLU A 1 147 ? -38.23995 7.69130   -5.18013  1.000 88.67200  ? 147 GLU A CB  1 
ATOM   947  C CG  . GLU A 1 147 ? -38.72487 6.63439   -4.21413  1.000 98.16913  ? 147 GLU A CG  1 
ATOM   948  C CD  . GLU A 1 147 ? -40.19347 6.30609   -4.40590  1.000 130.71599 ? 147 GLU A CD  1 
ATOM   949  O OE1 . GLU A 1 147 ? -40.57153 5.91205   -5.53117  1.000 126.40596 ? 147 GLU A OE1 1 
ATOM   950  O OE2 . GLU A 1 147 ? -40.96727 6.43867   -3.43222  1.000 128.80329 ? 147 GLU A OE2 1 
ATOM   951  N N   . GLY A 1 148 ? -35.15903 7.49202   -5.43366  1.000 91.33632  ? 148 GLY A N   1 
ATOM   952  C CA  . GLY A 1 148 ? -33.89792 7.12076   -4.83271  1.000 73.30872  ? 148 GLY A CA  1 
ATOM   953  C C   . GLY A 1 148 ? -32.79978 8.06565   -5.27818  1.000 85.97823  ? 148 GLY A C   1 
ATOM   954  O O   . GLY A 1 148 ? -33.06255 9.14591   -5.79857  1.000 92.82565  ? 148 GLY A O   1 
ATOM   955  N N   . SER A 1 149 ? -31.56635 7.61535   -5.07711  1.000 70.75300  ? 149 SER A N   1 
ATOM   956  C CA  . SER A 1 149 ? -30.36964 8.35803   -5.44516  1.000 84.35979  ? 149 SER A CA  1 
ATOM   957  C C   . SER A 1 149 ? -29.62664 7.59760   -6.53008  1.000 89.12270  ? 149 SER A C   1 
ATOM   958  O O   . SER A 1 149 ? -29.33930 6.40658   -6.37098  1.000 89.07480  ? 149 SER A O   1 
ATOM   959  C CB  . SER A 1 149 ? -29.45916 8.58108   -4.23604  1.000 93.20833  ? 149 SER A CB  1 
ATOM   960  O OG  . SER A 1 149 ? -28.86689 7.36251   -3.82257  1.000 126.50622 ? 149 SER A OG  1 
ATOM   961  N N   . TYR A 1 150 ? -29.29552 8.28793   -7.61685  1.000 85.27643  ? 150 TYR A N   1 
ATOM   962  C CA  . TYR A 1 150 ? -28.71225 7.63743   -8.77636  1.000 73.45883  ? 150 TYR A CA  1 
ATOM   963  C C   . TYR A 1 150 ? -27.55909 8.47347   -9.30196  1.000 76.90906  ? 150 TYR A C   1 
ATOM   964  O O   . TYR A 1 150 ? -27.39887 9.64710   -8.95988  1.000 84.94161  ? 150 TYR A O   1 
ATOM   965  C CB  . TYR A 1 150 ? -29.73720 7.44046   -9.90046  1.000 68.28882  ? 150 TYR A CB  1 
ATOM   966  C CG  . TYR A 1 150 ? -30.94015 6.61457   -9.51782  1.000 80.17207  ? 150 TYR A CG  1 
ATOM   967  C CD1 . TYR A 1 150 ? -32.07029 7.21222   -8.97681  1.000 68.52147  ? 150 TYR A CD1 1 
ATOM   968  C CD2 . TYR A 1 150 ? -30.95009 5.23569   -9.70332  1.000 72.08978  ? 150 TYR A CD2 1 
ATOM   969  C CE1 . TYR A 1 150 ? -33.17702 6.46277   -8.62785  1.000 77.43188  ? 150 TYR A CE1 1 
ATOM   970  C CE2 . TYR A 1 150 ? -32.05344 4.47888   -9.35790  1.000 74.80185  ? 150 TYR A CE2 1 
ATOM   971  C CZ  . TYR A 1 150 ? -33.16348 5.09669   -8.81880  1.000 78.33001  ? 150 TYR A CZ  1 
ATOM   972  O OH  . TYR A 1 150 ? -34.26609 4.34829   -8.47177  1.000 89.84007  ? 150 TYR A OH  1 
ATOM   973  N N   . ARG A 1 151 ? -26.75425 7.83869   -10.14200 1.000 75.74312  ? 151 ARG A N   1 
ATOM   974  C CA  . ARG A 1 151 ? -25.74409 8.50756   -10.93896 1.000 64.39160  ? 151 ARG A CA  1 
ATOM   975  C C   . ARG A 1 151 ? -25.97711 8.14863   -12.39505 1.000 64.81139  ? 151 ARG A C   1 
ATOM   976  O O   . ARG A 1 151 ? -26.50763 7.08061   -12.71247 1.000 73.50242  ? 151 ARG A O   1 
ATOM   977  C CB  . ARG A 1 151 ? -24.32243 8.09197   -10.53772 1.000 70.76308  ? 151 ARG A CB  1 
ATOM   978  C CG  . ARG A 1 151 ? -23.81068 8.71886   -9.25891  1.000 81.24952  ? 151 ARG A CG  1 
ATOM   979  C CD  . ARG A 1 151 ? -22.39229 8.25091   -8.97696  1.000 93.93201  ? 151 ARG A CD  1 
ATOM   980  N NE  . ARG A 1 151 ? -21.86615 8.79862   -7.73273  1.000 96.93267  ? 151 ARG A NE  1 
ATOM   981  C CZ  . ARG A 1 151 ? -21.17694 9.92666   -7.63913  1.000 92.57002  ? 151 ARG A CZ  1 
ATOM   982  N NH1 . ARG A 1 151 ? -20.91948 10.67017  -8.70256  1.000 88.11491  ? 151 ARG A NH1 1 
ATOM   983  N NH2 . ARG A 1 151 ? -20.73274 10.31742  -6.44852  1.000 98.26495  ? 151 ARG A NH2 1 
ATOM   984  N N   . PHE A 1 152 ? -25.57726 9.04558   -13.27790 1.000 59.61630  ? 152 PHE A N   1 
ATOM   985  C CA  . PHE A 1 152 ? -25.62396 8.78061   -14.70303 1.000 56.57807  ? 152 PHE A CA  1 
ATOM   986  C C   . PHE A 1 152 ? -24.23123 8.41220   -15.17499 1.000 59.37666  ? 152 PHE A C   1 
ATOM   987  O O   . PHE A 1 152 ? -23.23774 9.01938   -14.76647 1.000 65.13332  ? 152 PHE A O   1 
ATOM   988  C CB  . PHE A 1 152 ? -26.14367 9.98010   -15.48960 1.000 64.70002  ? 152 PHE A CB  1 
ATOM   989  C CG  . PHE A 1 152 ? -27.62443 9.96212   -15.71115 1.000 70.11091  ? 152 PHE A CG  1 
ATOM   990  C CD1 . PHE A 1 152 ? -28.24449 8.83403   -16.21938 1.000 68.84775  ? 152 PHE A CD1 1 
ATOM   991  C CD2 . PHE A 1 152 ? -28.39700 11.07323  -15.41414 1.000 58.71688  ? 152 PHE A CD2 1 
ATOM   992  C CE1 . PHE A 1 152 ? -29.61094 8.81117   -16.42498 1.000 74.00146  ? 152 PHE A CE1 1 
ATOM   993  C CE2 . PHE A 1 152 ? -29.75990 11.05882  -15.61963 1.000 70.72169  ? 152 PHE A CE2 1 
ATOM   994  C CZ  . PHE A 1 152 ? -30.36886 9.92560   -16.12356 1.000 83.57125  ? 152 PHE A CZ  1 
ATOM   995  N N   . SER A 1 153 ? -24.17043 7.37738   -15.99442 1.000 55.60166  ? 153 SER A N   1 
ATOM   996  C CA  . SER A 1 153 ? -22.96267 6.96846   -16.68545 1.000 51.22832  ? 153 SER A CA  1 
ATOM   997  C C   . SER A 1 153 ? -23.20062 7.17699   -18.17055 1.000 58.33183  ? 153 SER A C   1 
ATOM   998  O O   . SER A 1 153 ? -24.20771 6.70496   -18.70895 1.000 57.20440  ? 153 SER A O   1 
ATOM   999  C CB  . SER A 1 153 ? -22.62325 5.50993   -16.37440 1.000 72.32190  ? 153 SER A CB  1 
ATOM   1000 O OG  . SER A 1 153 ? -21.30765 5.18805   -16.78195 1.000 75.08555  ? 153 SER A OG  1 
ATOM   1001 N N   . PHE A 1 154 ? -22.33826 7.96722   -18.80056 1.000 54.25366  ? 154 PHE A N   1 
ATOM   1002 C CA  . PHE A 1 154 ? -22.43014 8.26629   -20.22157 1.000 49.30378  ? 154 PHE A CA  1 
ATOM   1003 C C   . PHE A 1 154 ? -21.28052 7.56914   -20.93498 1.000 57.30252  ? 154 PHE A C   1 
ATOM   1004 O O   . PHE A 1 154 ? -20.11009 7.82697   -20.63139 1.000 64.45278  ? 154 PHE A O   1 
ATOM   1005 C CB  . PHE A 1 154 ? -22.40223 9.77839   -20.44920 1.000 60.46853  ? 154 PHE A CB  1 
ATOM   1006 C CG  . PHE A 1 154 ? -23.50072 10.51001  -19.72722 1.000 52.59061  ? 154 PHE A CG  1 
ATOM   1007 C CD1 . PHE A 1 154 ? -24.79502 10.51167  -20.22791 1.000 50.33984  ? 154 PHE A CD1 1 
ATOM   1008 C CD2 . PHE A 1 154 ? -23.25485 11.13988  -18.51965 1.000 52.64808  ? 154 PHE A CD2 1 
ATOM   1009 C CE1 . PHE A 1 154 ? -25.81183 11.16110  -19.56038 1.000 54.66209  ? 154 PHE A CE1 1 
ATOM   1010 C CE2 . PHE A 1 154 ? -24.27078 11.79355  -17.84193 1.000 51.59230  ? 154 PHE A CE2 1 
ATOM   1011 C CZ  . PHE A 1 154 ? -25.54724 11.80756  -18.36225 1.000 53.64467  ? 154 PHE A CZ  1 
ATOM   1012 N N   . HIS A 1 155 ? -21.61608 6.68963   -21.87639 1.000 52.74605  ? 155 HIS A N   1 
ATOM   1013 C CA  . HIS A 1 155 ? -20.64014 5.89104   -22.60298 1.000 55.90125  ? 155 HIS A CA  1 
ATOM   1014 C C   . HIS A 1 155 ? -20.55323 6.39171   -24.03525 1.000 60.25475  ? 155 HIS A C   1 
ATOM   1015 O O   . HIS A 1 155 ? -21.57232 6.48000   -24.72714 1.000 63.27061  ? 155 HIS A O   1 
ATOM   1016 C CB  . HIS A 1 155 ? -21.02637 4.40841   -22.56225 1.000 56.30177  ? 155 HIS A CB  1 
ATOM   1017 C CG  . HIS A 1 155 ? -21.56812 3.96632   -21.23689 1.000 46.77273  ? 155 HIS A CG  1 
ATOM   1018 N ND1 . HIS A 1 155 ? -20.76136 3.50623   -20.21743 1.000 61.09568  ? 155 HIS A ND1 1 
ATOM   1019 C CD2 . HIS A 1 155 ? -22.83115 3.95838   -20.74759 1.000 59.58353  ? 155 HIS A CD2 1 
ATOM   1020 C CE1 . HIS A 1 155 ? -21.50585 3.20800   -19.16703 1.000 51.80212  ? 155 HIS A CE1 1 
ATOM   1021 N NE2 . HIS A 1 155 ? -22.76546 3.47579   -19.46177 1.000 63.24931  ? 155 HIS A NE2 1 
ATOM   1022 N N   . LEU A 1 156 ? -19.33594 6.66755   -24.49449 1.000 57.63246  ? 156 LEU A N   1 
ATOM   1023 C CA  . LEU A 1 156 ? -19.12490 7.19610   -25.83082 1.000 53.99402  ? 156 LEU A CA  1 
ATOM   1024 C C   . LEU A 1 156 ? -18.79379 6.07003   -26.79548 1.000 58.92874  ? 156 LEU A C   1 
ATOM   1025 O O   . LEU A 1 156 ? -17.90823 5.25376   -26.52757 1.000 66.58818  ? 156 LEU A O   1 
ATOM   1026 C CB  . LEU A 1 156 ? -17.99827 8.22986   -25.83075 1.000 59.93819  ? 156 LEU A CB  1 
ATOM   1027 C CG  . LEU A 1 156 ? -17.70053 8.82230   -27.20890 1.000 60.29410  ? 156 LEU A CG  1 
ATOM   1028 C CD1 . LEU A 1 156 ? -18.88821 9.64393   -27.68105 1.000 56.53560  ? 156 LEU A CD1 1 
ATOM   1029 C CD2 . LEU A 1 156 ? -16.43531 9.65989   -27.18923 1.000 62.95742  ? 156 LEU A CD2 1 
ATOM   1030 N N   . PHE A 1 157 ? -19.49685 6.04140   -27.92067 1.000 63.51456  ? 157 PHE A N   1 
ATOM   1031 C CA  . PHE A 1 157 ? -19.24252 5.09297   -28.99354 1.000 60.93314  ? 157 PHE A CA  1 
ATOM   1032 C C   . PHE A 1 157 ? -18.79465 5.83832   -30.24067 1.000 64.14014  ? 157 PHE A C   1 
ATOM   1033 O O   . PHE A 1 157 ? -19.41005 6.83783   -30.62858 1.000 69.27019  ? 157 PHE A O   1 
ATOM   1034 C CB  . PHE A 1 157 ? -20.48530 4.26099   -29.29038 1.000 58.07523  ? 157 PHE A CB  1 
ATOM   1035 C CG  . PHE A 1 157 ? -20.90663 3.39242   -28.15447 1.000 60.21686  ? 157 PHE A CG  1 
ATOM   1036 C CD1 . PHE A 1 157 ? -20.13366 2.30738   -27.76950 1.000 68.29267  ? 157 PHE A CD1 1 
ATOM   1037 C CD2 . PHE A 1 157 ? -22.06289 3.67183   -27.45435 1.000 56.01287  ? 157 PHE A CD2 1 
ATOM   1038 C CE1 . PHE A 1 157 ? -20.52551 1.50559   -26.72064 1.000 63.09995  ? 157 PHE A CE1 1 
ATOM   1039 C CE2 . PHE A 1 157 ? -22.45761 2.87968   -26.40640 1.000 60.08483  ? 157 PHE A CE2 1 
ATOM   1040 C CZ  . PHE A 1 157 ? -21.69090 1.79629   -26.03535 1.000 61.73270  ? 157 PHE A CZ  1 
ATOM   1041 N N   . GLU A 1 158 ? -17.73431 5.34838   -30.86644 1.000 67.42570  ? 158 GLU A N   1 
ATOM   1042 C CA  . GLU A 1 158 ? -17.20217 5.93064   -32.08598 1.000 63.21826  ? 158 GLU A CA  1 
ATOM   1043 C C   . GLU A 1 158 ? -17.37954 4.97576   -33.25802 1.000 75.35893  ? 158 GLU A C   1 
ATOM   1044 O O   . GLU A 1 158 ? -17.15893 3.76787   -33.12954 1.000 80.74793  ? 158 GLU A O   1 
ATOM   1045 C CB  . GLU A 1 158 ? -15.72107 6.28947   -31.93160 1.000 73.33850  ? 158 GLU A CB  1 
ATOM   1046 C CG  . GLU A 1 158 ? -15.09017 6.84744   -33.20289 1.000 61.69853  ? 158 GLU A CG  1 
ATOM   1047 C CD  . GLU A 1 158 ? -13.62949 7.20756   -33.01993 1.000 76.33181  ? 158 GLU A CD  1 
ATOM   1048 O OE1 . GLU A 1 158 ? -13.14414 7.13120   -31.87501 1.000 83.29663  ? 158 GLU A OE1 1 
ATOM   1049 O OE2 . GLU A 1 158 ? -12.96550 7.56463   -34.01469 1.000 80.04316  ? 158 GLU A OE2 1 
ATOM   1050 N N   . GLN A 1 159 ? -17.80179 5.52428   -34.39133 1.000 82.63981  ? 159 GLN A N   1 
ATOM   1051 C CA  . GLN A 1 159 ? -17.98897 4.77655   -35.62938 1.000 69.18979  ? 159 GLN A CA  1 
ATOM   1052 C C   . GLN A 1 159 ? -17.07731 5.40390   -36.67498 1.000 93.35360  ? 159 GLN A C   1 
ATOM   1053 O O   . GLN A 1 159 ? -17.34374 6.51121   -37.15655 1.000 98.62633  ? 159 GLN A O   1 
ATOM   1054 C CB  . GLN A 1 159 ? -19.44774 4.80026   -36.07641 1.000 88.89804  ? 159 GLN A CB  1 
ATOM   1055 C CG  . GLN A 1 159 ? -20.04000 3.44217   -36.38539 1.000 92.66416  ? 159 GLN A CG  1 
ATOM   1056 C CD  . GLN A 1 159 ? -21.43109 3.54220   -36.96510 1.000 109.78915 ? 159 GLN A CD  1 
ATOM   1057 O OE1 . GLN A 1 159 ? -22.06064 4.60893   -36.91366 1.000 107.75567 ? 159 GLN A OE1 1 
ATOM   1058 N NE2 . GLN A 1 159 ? -21.89548 2.45148   -37.59001 1.000 124.39955 ? 159 GLN A NE2 1 
ATOM   1059 N N   . ILE A 1 160 ? -16.00847 4.69499   -37.02680 1.000 113.52797 ? 160 ILE A N   1 
ATOM   1060 C CA  . ILE A 1 160 ? -14.93000 5.26349   -37.82527 1.000 112.93740 ? 160 ILE A CA  1 
ATOM   1061 C C   . ILE A 1 160 ? -15.24441 5.08483   -39.30233 1.000 119.47046 ? 160 ILE A C   1 
ATOM   1062 O O   . ILE A 1 160 ? -15.73973 4.03438   -39.72908 1.000 117.56292 ? 160 ILE A O   1 
ATOM   1063 C CB  . ILE A 1 160 ? -13.58473 4.60954   -37.45062 1.000 125.63171 ? 160 ILE A CB  1 
ATOM   1064 C CG1 . ILE A 1 160 ? -13.06852 5.17284   -36.12381 1.000 118.34778 ? 160 ILE A CG1 1 
ATOM   1065 C CG2 . ILE A 1 160 ? -12.55417 4.80608   -38.54592 1.000 132.26647 ? 160 ILE A CG2 1 
ATOM   1066 C CD1 . ILE A 1 160 ? -11.57911 4.95511   -35.88936 1.000 117.39636 ? 160 ILE A CD1 1 
ATOM   1067 N N   . LYS A 1 161 ? -14.96312 6.12752   -40.08771 1.000 121.19289 ? 161 LYS A N   1 
ATOM   1068 C CA  . LYS A 1 161 ? -15.13948 6.09302   -41.53162 1.000 137.30716 ? 161 LYS A CA  1 
ATOM   1069 C C   . LYS A 1 161 ? -13.84184 6.20060   -42.32382 1.000 142.72037 ? 161 LYS A C   1 
ATOM   1070 O O   . LYS A 1 161 ? -13.83943 5.87213   -43.51471 1.000 132.25849 ? 161 LYS A O   1 
ATOM   1071 C CB  . LYS A 1 161 ? -16.13175 7.17853   -41.97945 1.000 117.38254 ? 161 LYS A CB  1 
ATOM   1072 C CG  . LYS A 1 161 ? -17.18569 7.49666   -40.92231 1.000 103.49928 ? 161 LYS A CG  1 
ATOM   1073 C CD  . LYS A 1 161 ? -18.30764 8.36382   -41.47636 1.000 117.20998 ? 161 LYS A CD  1 
ATOM   1074 C CE  . LYS A 1 161 ? -17.86729 9.78018   -41.74953 1.000 112.23755 ? 161 LYS A CE  1 
ATOM   1075 N NZ  . LYS A 1 161 ? -18.88074 10.78237  -41.30140 1.000 106.67190 ? 161 LYS A NZ  1 
ATOM   1076 N N   . ASP A 1 162 ? -12.74463 6.63489   -41.70285 1.000 153.21771 ? 162 ASP A N   1 
ATOM   1077 C CA  . ASP A 1 162 ? -11.44847 6.65209   -42.36936 1.000 161.06742 ? 162 ASP A CA  1 
ATOM   1078 C C   . ASP A 1 162 ? -10.54040 5.59365   -41.76527 1.000 160.81060 ? 162 ASP A C   1 
ATOM   1079 O O   . ASP A 1 162 ? -10.25860 5.64018   -40.55854 1.000 153.39234 ? 162 ASP A O   1 
ATOM   1080 C CB  . ASP A 1 162 ? -10.80508 8.03310   -42.24613 1.000 167.79210 ? 162 ASP A CB  1 
ATOM   1081 C CG  . ASP A 1 162 ? -11.13638 8.93958   -43.41525 1.000 176.50072 ? 162 ASP A CG  1 
ATOM   1082 O OD1 . ASP A 1 162 ? -11.89211 8.50731   -44.31042 1.000 183.27640 ? 162 ASP A OD1 1 
ATOM   1083 O OD2 . ASP A 1 162 ? -10.64318 10.08715  -43.43672 1.000 176.16686 ? 162 ASP A OD2 1 
ATOM   1084 N N   . PRO A 1 163 ? -10.06065 4.63402   -42.56177 1.000 171.47891 ? 163 PRO A N   1 
ATOM   1085 C CA  . PRO A 1 163 ? -9.29567  3.51108   -41.98950 1.000 169.92814 ? 163 PRO A CA  1 
ATOM   1086 C C   . PRO A 1 163 ? -8.00030  3.92597   -41.31146 1.000 162.36269 ? 163 PRO A C   1 
ATOM   1087 O O   . PRO A 1 163 ? -7.50100  3.18105   -40.45749 1.000 148.23173 ? 163 PRO A O   1 
ATOM   1088 C CB  . PRO A 1 163 ? -9.02392  2.60892   -43.20400 1.000 174.21471 ? 163 PRO A CB  1 
ATOM   1089 C CG  . PRO A 1 163 ? -9.91311  3.12127   -44.30856 1.000 170.81644 ? 163 PRO A CG  1 
ATOM   1090 C CD  . PRO A 1 163 ? -10.15787 4.56329   -44.02802 1.000 167.25422 ? 163 PRO A CD  1 
ATOM   1091 N N   . LYS A 1 164 ? -7.43686  5.08367   -41.66866 1.000 160.51350 ? 164 LYS A N   1 
ATOM   1092 C CA  . LYS A 1 164 ? -6.23370  5.56719   -40.99874 1.000 154.05014 ? 164 LYS A CA  1 
ATOM   1093 C C   . LYS A 1 164 ? -6.48601  5.84291   -39.52303 1.000 149.22501 ? 164 LYS A C   1 
ATOM   1094 O O   . LYS A 1 164 ? -5.58081  5.68562   -38.69451 1.000 134.64698 ? 164 LYS A O   1 
ATOM   1095 C CB  . LYS A 1 164 ? -5.72649  6.82972   -41.69512 1.000 161.37266 ? 164 LYS A CB  1 
ATOM   1096 C CG  . LYS A 1 164 ? -6.83721  7.78430   -42.11574 1.000 159.72338 ? 164 LYS A CG  1 
ATOM   1097 C CD  . LYS A 1 164 ? -6.36610  9.22917   -42.11274 1.000 159.37799 ? 164 LYS A CD  1 
ATOM   1098 C CE  . LYS A 1 164 ? -7.53019  10.18636  -42.31186 1.000 159.63332 ? 164 LYS A CE  1 
ATOM   1099 N NZ  . LYS A 1 164 ? -7.18145  11.58039  -41.92061 1.000 165.38761 ? 164 LYS A NZ  1 
ATOM   1100 N N   . ASP A 1 165 ? -7.71042  6.24165   -39.17614 1.000 141.61816 ? 165 ASP A N   1 
ATOM   1101 C CA  . ASP A 1 165 ? -8.04994  6.57091   -37.79987 1.000 122.91091 ? 165 ASP A CA  1 
ATOM   1102 C C   . ASP A 1 165 ? -8.13990  5.34612   -36.90256 1.000 111.68974 ? 165 ASP A C   1 
ATOM   1103 O O   . ASP A 1 165 ? -8.27122  5.50713   -35.68557 1.000 100.01481 ? 165 ASP A O   1 
ATOM   1104 C CB  . ASP A 1 165 ? -9.37644  7.33137   -37.76082 1.000 125.25079 ? 165 ASP A CB  1 
ATOM   1105 C CG  . ASP A 1 165 ? -9.31104  8.65452   -38.49582 1.000 125.35996 ? 165 ASP A CG  1 
ATOM   1106 O OD1 . ASP A 1 165 ? -8.19050  9.17137   -38.69429 1.000 116.04797 ? 165 ASP A OD1 1 
ATOM   1107 O OD2 . ASP A 1 165 ? -10.38178 9.17506   -38.87652 1.000 125.58833 ? 165 ASP A OD2 1 
ATOM   1108 N N   . ALA A 1 166 ? -8.08145  4.14062   -37.46357 1.000 111.32036 ? 166 ALA A N   1 
ATOM   1109 C CA  . ALA A 1 166 ? -8.21895  2.93759   -36.65590 1.000 111.47909 ? 166 ALA A CA  1 
ATOM   1110 C C   . ALA A 1 166 ? -7.07903  2.82986   -35.64966 1.000 111.26844 ? 166 ALA A C   1 
ATOM   1111 O O   . ALA A 1 166 ? -5.98470  3.36262   -35.85295 1.000 110.49559 ? 166 ALA A O   1 
ATOM   1112 C CB  . ALA A 1 166 ? -8.25441  1.69676   -37.54745 1.000 118.31090 ? 166 ALA A CB  1 
ATOM   1113 N N   . THR A 1 167 ? -7.34953  2.13120   -34.55216 1.000 98.97052  ? 167 THR A N   1 
ATOM   1114 C CA  . THR A 1 167 ? -6.37462  1.97314   -33.48162 1.000 90.74603  ? 167 THR A CA  1 
ATOM   1115 C C   . THR A 1 167 ? -5.15959  1.17405   -33.95269 1.000 107.00474 ? 167 THR A C   1 
ATOM   1116 O O   . THR A 1 167 ? -5.25497  -0.01872  -34.24645 1.000 117.17442 ? 167 THR A O   1 
ATOM   1117 C CB  . THR A 1 167 ? -6.99935  1.28307   -32.24911 1.000 89.69112  ? 167 THR A CB  1 
ATOM   1118 O OG1 . THR A 1 167 ? -8.20663  1.96152   -31.87333 1.000 92.81817  ? 167 THR A OG1 1 
ATOM   1119 C CG2 . THR A 1 167 ? -6.03186  1.31081   -31.07844 1.000 88.32175  ? 167 THR A CG2 1 
ATOM   1120 N N   . PRO A 1 184 ? -22.64542 -7.08320  -40.63929 1.000 194.10002 ? 184 PRO A N   1 
ATOM   1121 C CA  . PRO A 1 184 ? -22.45232 -5.63251  -40.67122 1.000 188.19456 ? 184 PRO A CA  1 
ATOM   1122 C C   . PRO A 1 184 ? -21.03600 -5.23640  -41.07112 1.000 183.57122 ? 184 PRO A C   1 
ATOM   1123 O O   . PRO A 1 184 ? -20.06958 -5.69390  -40.46145 1.000 190.72840 ? 184 PRO A O   1 
ATOM   1124 C CB  . PRO A 1 184 ? -22.74769 -5.20683  -39.22670 1.000 182.72110 ? 184 PRO A CB  1 
ATOM   1125 C CG  . PRO A 1 184 ? -23.47826 -6.38402  -38.58590 1.000 182.13262 ? 184 PRO A CG  1 
ATOM   1126 C CD  . PRO A 1 184 ? -23.62709 -7.46947  -39.61562 1.000 183.26428 ? 184 PRO A CD  1 
ATOM   1127 N N   . GLN A 1 185 ? -20.92169 -4.38767  -42.08784 1.000 173.95637 ? 185 GLN A N   1 
ATOM   1128 C CA  . GLN A 1 185 ? -19.63184 -3.89175  -42.54501 1.000 169.68204 ? 185 GLN A CA  1 
ATOM   1129 C C   . GLN A 1 185 ? -19.20911 -2.61570  -41.83110 1.000 165.57592 ? 185 GLN A C   1 
ATOM   1130 O O   . GLN A 1 185 ? -18.17258 -2.04033  -42.17895 1.000 160.75518 ? 185 GLN A O   1 
ATOM   1131 C CB  . GLN A 1 185 ? -19.65550 -3.66463  -44.05939 1.000 167.70725 ? 185 GLN A CB  1 
ATOM   1132 C CG  . GLN A 1 185 ? -19.93754 -4.92749  -44.85855 1.000 169.34395 ? 185 GLN A CG  1 
ATOM   1133 C CD  . GLN A 1 185 ? -20.06363 -4.66408  -46.34459 1.000 169.52764 ? 185 GLN A CD  1 
ATOM   1134 O OE1 . GLN A 1 185 ? -20.00683 -3.51841  -46.79042 1.000 173.14890 ? 185 GLN A OE1 1 
ATOM   1135 N NE2 . GLN A 1 185 ? -20.23302 -5.72775  -47.12187 1.000 172.00773 ? 185 GLN A NE2 1 
ATOM   1136 N N   . GLU A 1 186 ? -19.98449 -2.16214  -40.85146 1.000 159.32602 ? 186 GLU A N   1 
ATOM   1137 C CA  . GLU A 1 186 ? -19.61472 -1.04178  -40.00402 1.000 150.98226 ? 186 GLU A CA  1 
ATOM   1138 C C   . GLU A 1 186 ? -19.35321 -1.54465  -38.59145 1.000 140.93529 ? 186 GLU A C   1 
ATOM   1139 O O   . GLU A 1 186 ? -19.99103 -2.49274  -38.12399 1.000 144.30119 ? 186 GLU A O   1 
ATOM   1140 C CB  . GLU A 1 186 ? -20.71708 0.01919   -39.98653 1.000 149.76933 ? 186 GLU A CB  1 
ATOM   1141 C CG  . GLU A 1 186 ? -20.49708 1.15515   -40.96561 1.000 156.05400 ? 186 GLU A CG  1 
ATOM   1142 C CD  . GLU A 1 186 ? -21.79077 1.84051   -41.35044 1.000 159.03007 ? 186 GLU A CD  1 
ATOM   1143 O OE1 . GLU A 1 186 ? -22.80428 1.13281   -41.53362 1.000 151.86630 ? 186 GLU A OE1 1 
ATOM   1144 O OE2 . GLU A 1 186 ? -21.79595 3.08427   -41.46516 1.000 165.42938 ? 186 GLU A OE2 1 
ATOM   1145 N N   . PHE A 1 187 ? -18.40847 -0.90045  -37.91345 1.000 123.17647 ? 187 PHE A N   1 
ATOM   1146 C CA  . PHE A 1 187 ? -18.02413 -1.28105  -36.56452 1.000 111.84806 ? 187 PHE A CA  1 
ATOM   1147 C C   . PHE A 1 187 ? -18.29690 -0.13931  -35.59615 1.000 103.81473 ? 187 PHE A C   1 
ATOM   1148 O O   . PHE A 1 187 ? -18.22642 1.03689   -35.95785 1.000 106.83316 ? 187 PHE A O   1 
ATOM   1149 C CB  . PHE A 1 187 ? -16.53988 -1.66617  -36.49250 1.000 116.10562 ? 187 PHE A CB  1 
ATOM   1150 C CG  . PHE A 1 187 ? -16.25505 -3.08671  -36.89433 1.000 139.00240 ? 187 PHE A CG  1 
ATOM   1151 C CD1 . PHE A 1 187 ? -17.13370 -3.78669  -37.70510 1.000 150.76838 ? 187 PHE A CD1 1 
ATOM   1152 C CD2 . PHE A 1 187 ? -15.09885 -3.71931  -36.46686 1.000 145.19066 ? 187 PHE A CD2 1 
ATOM   1153 C CE1 . PHE A 1 187 ? -16.86829 -5.09166  -38.07908 1.000 158.55735 ? 187 PHE A CE1 1 
ATOM   1154 C CE2 . PHE A 1 187 ? -14.82720 -5.02463  -36.83714 1.000 154.86156 ? 187 PHE A CE2 1 
ATOM   1155 C CZ  . PHE A 1 187 ? -15.71354 -5.71141  -37.64407 1.000 159.40039 ? 187 PHE A CZ  1 
ATOM   1156 N N   . LEU A 1 188 ? -18.59655 -0.50481  -34.35563 1.000 80.81402  ? 188 LEU A N   1 
ATOM   1157 C CA  . LEU A 1 188 ? -18.84379 0.43594   -33.27528 1.000 73.56433  ? 188 LEU A CA  1 
ATOM   1158 C C   . LEU A 1 188 ? -17.81495 0.19554   -32.18178 1.000 77.73539  ? 188 LEU A C   1 
ATOM   1159 O O   . LEU A 1 188 ? -17.66758 -0.93506  -31.70799 1.000 86.68273  ? 188 LEU A O   1 
ATOM   1160 C CB  . LEU A 1 188 ? -20.26026 0.26572   -32.72202 1.000 76.97921  ? 188 LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 188 ? -20.86935 1.41046   -31.91833 1.000 74.71472  ? 188 LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 188 ? -21.26028 2.58075   -32.82053 1.000 76.48923  ? 188 LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 188 ? -22.06302 0.89274   -31.12700 1.000 75.13921  ? 188 LEU A CD2 1 
ATOM   1164 N N   . GLU A 1 189 ? -17.11579 1.25253   -31.77134 1.000 83.88701  ? 189 GLU A N   1 
ATOM   1165 C CA  . GLU A 1 189 ? -16.05400 1.14049   -30.77804 1.000 75.22941  ? 189 GLU A CA  1 
ATOM   1166 C C   . GLU A 1 189 ? -16.37958 1.98484   -29.55934 1.000 69.15983  ? 189 GLU A C   1 
ATOM   1167 O O   . GLU A 1 189 ? -16.61406 3.19223   -29.67893 1.000 74.10362  ? 189 GLU A O   1 
ATOM   1168 C CB  . GLU A 1 189 ? -14.69934 1.56249   -31.34810 1.000 63.57146  ? 189 GLU A CB  1 
ATOM   1169 C CG  . GLU A 1 189 ? -14.05398 0.53809   -32.25272 1.000 78.00205  ? 189 GLU A CG  1 
ATOM   1170 C CD  . GLU A 1 189 ? -12.55042 0.71700   -32.33052 1.000 106.63609 ? 189 GLU A CD  1 
ATOM   1171 O OE1 . GLU A 1 189 ? -12.09295 1.71012   -32.93428 1.000 108.76922 ? 189 GLU A OE1 1 
ATOM   1172 O OE2 . GLU A 1 189 ? -11.82369 -0.13240  -31.77295 1.000 123.51973 ? 189 GLU A OE2 1 
ATOM   1173 N N   . PHE A 1 190 ? -16.38407 1.34995   -28.39218 1.000 60.82150  ? 190 PHE A N   1 
ATOM   1174 C CA  . PHE A 1 190 ? -16.45088 2.09129   -27.14518 1.000 63.16843  ? 190 PHE A CA  1 
ATOM   1175 C C   . PHE A 1 190 ? -15.14117 2.83699   -26.93784 1.000 70.92004  ? 190 PHE A C   1 
ATOM   1176 O O   . PHE A 1 190 ? -14.05849 2.29486   -27.17618 1.000 68.46178  ? 190 PHE A O   1 
ATOM   1177 C CB  . PHE A 1 190 ? -16.73754 1.15533   -25.97301 1.000 69.04795  ? 190 PHE A CB  1 
ATOM   1178 C CG  . PHE A 1 190 ? -16.67165 1.82884   -24.63561 1.000 63.86490  ? 190 PHE A CG  1 
ATOM   1179 C CD1 . PHE A 1 190 ? -17.73144 2.59515   -24.17742 1.000 56.30340  ? 190 PHE A CD1 1 
ATOM   1180 C CD2 . PHE A 1 190 ? -15.55119 1.68354   -23.82841 1.000 62.35138  ? 190 PHE A CD2 1 
ATOM   1181 C CE1 . PHE A 1 190 ? -17.66810 3.22852   -22.94016 1.000 62.34469  ? 190 PHE A CE1 1 
ATOM   1182 C CE2 . PHE A 1 190 ? -15.48237 2.30476   -22.59109 1.000 59.34800  ? 190 PHE A CE2 1 
ATOM   1183 C CZ  . PHE A 1 190 ? -16.54293 3.07881   -22.14635 1.000 58.42719  ? 190 PHE A CZ  1 
ATOM   1184 N N   . ARG A 1 191 ? -15.24251 4.09461   -26.50574 1.000 60.21940  ? 191 ARG A N   1 
ATOM   1185 C CA  . ARG A 1 191 ? -14.06949 4.93021   -26.29512 1.000 62.77695  ? 191 ARG A CA  1 
ATOM   1186 C C   . ARG A 1 191 ? -13.81300 5.21851   -24.82225 1.000 64.13239  ? 191 ARG A C   1 
ATOM   1187 O O   . ARG A 1 191 ? -12.73805 4.88808   -24.31440 1.000 64.08629  ? 191 ARG A O   1 
ATOM   1188 C CB  . ARG A 1 191 ? -14.22606 6.24589   -27.07475 1.000 64.22200  ? 191 ARG A CB  1 
ATOM   1189 C CG  . ARG A 1 191 ? -14.04923 6.08932   -28.57443 1.000 66.95655  ? 191 ARG A CG  1 
ATOM   1190 C CD  . ARG A 1 191 ? -12.60699 5.75638   -28.90380 1.000 66.81934  ? 191 ARG A CD  1 
ATOM   1191 N NE  . ARG A 1 191 ? -12.43443 5.36418   -30.29730 1.000 64.16500  ? 191 ARG A NE  1 
ATOM   1192 C CZ  . ARG A 1 191 ? -11.92847 4.20463   -30.69472 1.000 78.92655  ? 191 ARG A CZ  1 
ATOM   1193 N NH1 . ARG A 1 191 ? -11.52698 3.28906   -29.82460 1.000 76.51048  ? 191 ARG A NH1 1 
ATOM   1194 N NH2 . ARG A 1 191 ? -11.80962 3.96223   -31.99787 1.000 88.05221  ? 191 ARG A NH2 1 
ATOM   1195 N N   . LEU A 1 192 ? -14.77191 5.80555   -24.11183 1.000 59.66955  ? 192 LEU A N   1 
ATOM   1196 C CA  . LEU A 1 192 ? -14.56342 6.13001   -22.70646 1.000 58.41067  ? 192 LEU A CA  1 
ATOM   1197 C C   . LEU A 1 192 ? -15.91330 6.40504   -22.06195 1.000 57.79938  ? 192 LEU A C   1 
ATOM   1198 O O   . LEU A 1 192 ? -16.95606 6.40785   -22.72205 1.000 56.59747  ? 192 LEU A O   1 
ATOM   1199 C CB  . LEU A 1 192 ? -13.63260 7.33674   -22.54113 1.000 60.64246  ? 192 LEU A CB  1 
ATOM   1200 C CG  . LEU A 1 192 ? -14.23276 8.73157   -22.76499 1.000 52.31578  ? 192 LEU A CG  1 
ATOM   1201 C CD1 . LEU A 1 192 ? -13.50881 9.74400   -21.88465 1.000 63.26688  ? 192 LEU A CD1 1 
ATOM   1202 C CD2 . LEU A 1 192 ? -14.21421 9.14587   -24.22247 1.000 57.19603  ? 192 LEU A CD2 1 
ATOM   1203 N N   . GLU A 1 193 ? -15.86749 6.74403   -20.78075 1.000 65.96115  ? 193 GLU A N   1 
ATOM   1204 C CA  . GLU A 1 193 ? -17.05971 6.87652   -19.96333 1.000 68.57198  ? 193 GLU A CA  1 
ATOM   1205 C C   . GLU A 1 193 ? -16.88885 8.03945   -18.99710 1.000 61.07544  ? 193 GLU A C   1 
ATOM   1206 O O   . GLU A 1 193 ? -15.78040 8.30107   -18.52133 1.000 63.46533  ? 193 GLU A O   1 
ATOM   1207 C CB  . GLU A 1 193 ? -17.30640 5.56087   -19.21237 1.000 57.90406  ? 193 GLU A CB  1 
ATOM   1208 C CG  . GLU A 1 193 ? -18.35150 5.57633   -18.12204 1.000 59.94930  ? 193 GLU A CG  1 
ATOM   1209 C CD  . GLU A 1 193 ? -18.12368 4.44783   -17.12154 1.000 85.19923  ? 193 GLU A CD  1 
ATOM   1210 O OE1 . GLU A 1 193 ? -16.97445 3.96439   -17.03199 1.000 90.46311  ? 193 GLU A OE1 1 
ATOM   1211 O OE2 . GLU A 1 193 ? -19.08297 4.04208   -16.42891 1.000 86.23895  ? 193 GLU A OE2 1 
ATOM   1212 N N   . VAL A 1 194 ? -17.98213 8.74968   -18.72813 1.000 55.64489  ? 194 VAL A N   1 
ATOM   1213 C CA  . VAL A 1 194 ? -17.98281 9.84294   -17.76468 1.000 58.97519  ? 194 VAL A CA  1 
ATOM   1214 C C   . VAL A 1 194 ? -19.13119 9.61844   -16.78953 1.000 60.16843  ? 194 VAL A C   1 
ATOM   1215 O O   . VAL A 1 194 ? -20.22008 9.18365   -17.18013 1.000 65.60735  ? 194 VAL A O   1 
ATOM   1216 C CB  . VAL A 1 194 ? -18.07364 11.22703  -18.45485 1.000 64.14738  ? 194 VAL A CB  1 
ATOM   1217 C CG1 . VAL A 1 194 ? -19.47115 11.50772  -18.97430 1.000 56.49447  ? 194 VAL A CG1 1 
ATOM   1218 C CG2 . VAL A 1 194 ? -17.63519 12.32629  -17.50137 1.000 64.23079  ? 194 VAL A CG2 1 
ATOM   1219 N N   . ILE A 1 195 ? -18.87424 9.89534   -15.51428 1.000 70.09217  ? 195 ILE A N   1 
ATOM   1220 C CA  . ILE A 1 195 ? -19.79132 9.59744   -14.41912 1.000 62.81171  ? 195 ILE A CA  1 
ATOM   1221 C C   . ILE A 1 195 ? -20.37561 10.90737  -13.91583 1.000 75.82844  ? 195 ILE A C   1 
ATOM   1222 O O   . ILE A 1 195 ? -19.63240 11.84498  -13.60216 1.000 81.32910  ? 195 ILE A O   1 
ATOM   1223 C CB  . ILE A 1 195 ? -19.09565 8.83909   -13.27539 1.000 69.94173  ? 195 ILE A CB  1 
ATOM   1224 C CG1 . ILE A 1 195 ? -18.72765 7.41344   -13.68727 1.000 77.01582  ? 195 ILE A CG1 1 
ATOM   1225 C CG2 . ILE A 1 195 ? -20.00547 8.77622   -12.06562 1.000 76.99810  ? 195 ILE A CG2 1 
ATOM   1226 C CD1 . ILE A 1 195 ? -19.64779 6.81793   -14.70397 1.000 79.85214  ? 195 ILE A CD1 1 
ATOM   1227 N N   . SER A 1 196 ? -21.69874 10.96612  -13.81996 1.000 68.15205  ? 196 SER A N   1 
ATOM   1228 C CA  . SER A 1 196 ? -22.35133 12.17703  -13.36382 1.000 64.51899  ? 196 SER A CA  1 
ATOM   1229 C C   . SER A 1 196 ? -22.30454 12.26429  -11.84344 1.000 72.64467  ? 196 SER A C   1 
ATOM   1230 O O   . SER A 1 196 ? -21.99384 11.30128  -11.13832 1.000 70.82831  ? 196 SER A O   1 
ATOM   1231 C CB  . SER A 1 196 ? -23.80120 12.23511  -13.83752 1.000 65.71426  ? 196 SER A CB  1 
ATOM   1232 O OG  . SER A 1 196 ? -24.63990 11.47995  -12.98348 1.000 68.83428  ? 196 SER A OG  1 
ATOM   1233 N N   . ASN A 1 197 ? -22.59299 13.45902  -11.34899 1.000 77.22108  ? 197 ASN A N   1 
ATOM   1234 C CA  . ASN A 1 197 ? -22.81455 13.66102  -9.93045  1.000 82.06775  ? 197 ASN A CA  1 
ATOM   1235 C C   . ASN A 1 197 ? -24.15419 13.05242  -9.52115  1.000 77.75020  ? 197 ASN A C   1 
ATOM   1236 O O   . ASN A 1 197 ? -25.04949 12.88704  -10.35543 1.000 69.55139  ? 197 ASN A O   1 
ATOM   1237 C CB  . ASN A 1 197 ? -22.79842 15.14971  -9.60118  1.000 72.19711  ? 197 ASN A CB  1 
ATOM   1238 C CG  . ASN A 1 197 ? -21.40892 15.73661  -9.65600  1.000 86.44617  ? 197 ASN A CG  1 
ATOM   1239 O OD1 . ASN A 1 197 ? -20.42104 15.05834  -9.35776  1.000 71.76860  ? 197 ASN A OD1 1 
ATOM   1240 N ND2 . ASN A 1 197 ? -21.31858 16.99776  -10.05794 1.000 88.76170  ? 197 ASN A ND2 1 
ATOM   1241 N N   . PRO A 1 198 ? -24.29713 12.66067  -8.25465  1.000 70.19914  ? 198 PRO A N   1 
ATOM   1242 C CA  . PRO A 1 198 ? -25.55970 12.05845  -7.81438  1.000 68.73906  ? 198 PRO A CA  1 
ATOM   1243 C C   . PRO A 1 198 ? -26.71561 13.03863  -7.92431  1.000 75.36957  ? 198 PRO A C   1 
ATOM   1244 O O   . PRO A 1 198 ? -26.56680 14.24382  -7.71099  1.000 82.83485  ? 198 PRO A O   1 
ATOM   1245 C CB  . PRO A 1 198 ? -25.29105 11.67909  -6.35202  1.000 71.27391  ? 198 PRO A CB  1 
ATOM   1246 C CG  . PRO A 1 198 ? -23.81414 11.75721  -6.17396  1.000 74.19696  ? 198 PRO A CG  1 
ATOM   1247 C CD  . PRO A 1 198 ? -23.31201 12.75072  -7.16420  1.000 73.20990  ? 198 PRO A CD  1 
ATOM   1248 N N   . PHE A 1 199 ? -27.88224 12.49705  -8.26280  1.000 74.28567  ? 199 PHE A N   1 
ATOM   1249 C CA  . PHE A 1 199 ? -29.11304 13.26662  -8.32468  1.000 73.31549  ? 199 PHE A CA  1 
ATOM   1250 C C   . PHE A 1 199 ? -30.22366 12.44555  -7.68752  1.000 82.70896  ? 199 PHE A C   1 
ATOM   1251 O O   . PHE A 1 199 ? -30.14215 11.21837  -7.59302  1.000 89.56264  ? 199 PHE A O   1 
ATOM   1252 C CB  . PHE A 1 199 ? -29.48088 13.66029  -9.76026  1.000 73.12558  ? 199 PHE A CB  1 
ATOM   1253 C CG  . PHE A 1 199 ? -29.91011 12.50842  -10.61706 1.000 81.53344  ? 199 PHE A CG  1 
ATOM   1254 C CD1 . PHE A 1 199 ? -28.98487 11.59118  -11.08730 1.000 73.10605  ? 199 PHE A CD1 1 
ATOM   1255 C CD2 . PHE A 1 199 ? -31.24576 12.33666  -10.94451 1.000 78.35030  ? 199 PHE A CD2 1 
ATOM   1256 C CE1 . PHE A 1 199 ? -29.38294 10.53379  -11.87785 1.000 72.11090  ? 199 PHE A CE1 1 
ATOM   1257 C CE2 . PHE A 1 199 ? -31.65191 11.27678  -11.73153 1.000 78.59140  ? 199 PHE A CE2 1 
ATOM   1258 C CZ  . PHE A 1 199 ? -30.72095 10.37298  -12.19788 1.000 72.69675  ? 199 PHE A CZ  1 
ATOM   1259 N N   . ILE A 1 200 ? -31.26583 13.14074  -7.24211  1.000 77.66077  ? 200 ILE A N   1 
ATOM   1260 C CA  . ILE A 1 200 ? -32.31207 12.55844  -6.41022  1.000 90.69480  ? 200 ILE A CA  1 
ATOM   1261 C C   . ILE A 1 200 ? -33.60276 12.50132  -7.20961  1.000 85.38077  ? 200 ILE A C   1 
ATOM   1262 O O   . ILE A 1 200 ? -34.05613 13.51683  -7.75111  1.000 80.09535  ? 200 ILE A O   1 
ATOM   1263 C CB  . ILE A 1 200 ? -32.52407 13.35206  -5.10658  1.000 83.03097  ? 200 ILE A CB  1 
ATOM   1264 C CG1 . ILE A 1 200 ? -31.21253 13.92720  -4.54950  1.000 97.66630  ? 200 ILE A CG1 1 
ATOM   1265 C CG2 . ILE A 1 200 ? -33.19065 12.47256  -4.05907  1.000 89.74424  ? 200 ILE A CG2 1 
ATOM   1266 C CD1 . ILE A 1 200 ? -30.06926 12.92331  -4.40045  1.000 85.72679  ? 200 ILE A CD1 1 
ATOM   1267 N N   . VAL A 1 201 ? -34.20398 11.31806  -7.25588  1.000 86.99152  ? 201 VAL A N   1 
ATOM   1268 C CA  . VAL A 1 201 ? -35.55157 11.13415  -7.77312  1.000 85.55649  ? 201 VAL A CA  1 
ATOM   1269 C C   . VAL A 1 201 ? -36.49677 11.06038  -6.58443  1.000 91.69088  ? 201 VAL A C   1 
ATOM   1270 O O   . VAL A 1 201 ? -36.32488 10.21843  -5.69399  1.000 81.53108  ? 201 VAL A O   1 
ATOM   1271 C CB  . VAL A 1 201 ? -35.65672 9.86641   -8.63381  1.000 81.44891  ? 201 VAL A CB  1 
ATOM   1272 C CG1 . VAL A 1 201 ? -37.06166 9.73240   -9.20603  1.000 77.27100  ? 201 VAL A CG1 1 
ATOM   1273 C CG2 . VAL A 1 201 ? -34.60995 9.88623   -9.73910  1.000 75.76982  ? 201 VAL A CG2 1 
ATOM   1274 N N   . TYR A 1 202 ? -37.47468 11.95867  -6.55286  1.000 80.81852  ? 202 TYR A N   1 
ATOM   1275 C CA  . TYR A 1 202 ? -38.41862 12.05221  -5.45274  1.000 78.68829  ? 202 TYR A CA  1 
ATOM   1276 C C   . TYR A 1 202 ? -39.75771 11.49015  -5.90429  1.000 81.63751  ? 202 TYR A C   1 
ATOM   1277 O O   . TYR A 1 202 ? -40.00012 11.26891  -7.09426  1.000 81.13881  ? 202 TYR A O   1 
ATOM   1278 C CB  . TYR A 1 202 ? -38.58642 13.50670  -4.99021  1.000 86.57700  ? 202 TYR A CB  1 
ATOM   1279 C CG  . TYR A 1 202 ? -39.03777 14.41936  -6.10442  1.000 77.46470  ? 202 TYR A CG  1 
ATOM   1280 C CD1 . TYR A 1 202 ? -40.38627 14.53839  -6.42323  1.000 78.96555  ? 202 TYR A CD1 1 
ATOM   1281 C CD2 . TYR A 1 202 ? -38.12055 15.13630  -6.85817  1.000 86.02940  ? 202 TYR A CD2 1 
ATOM   1282 C CE1 . TYR A 1 202 ? -40.80713 15.34735  -7.44817  1.000 90.41323  ? 202 TYR A CE1 1 
ATOM   1283 C CE2 . TYR A 1 202 ? -38.53415 15.94975  -7.89103  1.000 80.33290  ? 202 TYR A CE2 1 
ATOM   1284 C CZ  . TYR A 1 202 ? -39.87945 16.05668  -8.17893  1.000 90.34225  ? 202 TYR A CZ  1 
ATOM   1285 O OH  . TYR A 1 202 ? -40.30585 16.86904  -9.20453  1.000 94.26628  ? 202 TYR A OH  1 
ATOM   1286 N N   . SER A 1 203 ? -40.63386 11.25865  -4.93599  1.000 89.01025  ? 203 SER A N   1 
ATOM   1287 C CA  . SER A 1 203 ? -42.00708 10.86452  -5.20693  1.000 103.75583 ? 203 SER A CA  1 
ATOM   1288 C C   . SER A 1 203 ? -42.93725 11.91501  -4.62387  1.000 102.58623 ? 203 SER A C   1 
ATOM   1289 O O   . SER A 1 203 ? -42.78738 12.30735  -3.46227  1.000 104.33959 ? 203 SER A O   1 
ATOM   1290 C CB  . SER A 1 203 ? -42.32104 9.47495   -4.64059  1.000 93.07333  ? 203 SER A CB  1 
ATOM   1291 O OG  . SER A 1 203 ? -41.81782 9.32514   -3.32629  1.000 114.43390 ? 203 SER A OG  1 
ATOM   1292 N N   . ALA A 1 204 ? -43.87873 12.38057  -5.43473  1.000 122.26888 ? 204 ALA A N   1 
ATOM   1293 C CA  . ALA A 1 204 ? -44.89364 13.30424  -4.95563  1.000 123.43737 ? 204 ALA A CA  1 
ATOM   1294 C C   . ALA A 1 204 ? -45.91005 12.52327  -4.13432  1.000 118.08233 ? 204 ALA A C   1 
ATOM   1295 O O   . ALA A 1 204 ? -46.44191 11.50713  -4.59379  1.000 129.06291 ? 204 ALA A O   1 
ATOM   1296 C CB  . ALA A 1 204 ? -45.57182 14.02011  -6.12299  1.000 108.38362 ? 204 ALA A CB  1 
ATOM   1297 N N   . LYS A 1 205 ? -46.15914 12.98227  -2.91016  1.000 108.86677 ? 205 LYS A N   1 
ATOM   1298 C CA  . LYS A 1 205 ? -47.11166 12.29882  -2.04815  1.000 106.06644 ? 205 LYS A CA  1 
ATOM   1299 C C   . LYS A 1 205 ? -48.49902 12.34163  -2.67245  1.000 102.81732 ? 205 LYS A C   1 
ATOM   1300 O O   . LYS A 1 205 ? -48.82956 13.23863  -3.45231  1.000 114.76464 ? 205 LYS A O   1 
ATOM   1301 C CB  . LYS A 1 205 ? -47.14288 12.94187  -0.66119  1.000 104.56034 ? 205 LYS A CB  1 
ATOM   1302 C CG  . LYS A 1 205 ? -45.88864 12.71771  0.16525   1.000 108.74216 ? 205 LYS A CG  1 
ATOM   1303 C CD  . LYS A 1 205 ? -45.92170 13.54678  1.44237   1.000 101.61152 ? 205 LYS A CD  1 
ATOM   1304 C CE  . LYS A 1 205 ? -44.66388 13.34202  2.26992   1.000 116.64176 ? 205 LYS A CE  1 
ATOM   1305 N NZ  . LYS A 1 205 ? -43.84104 12.20973  1.75850   1.000 136.07843 ? 205 LYS A NZ  1 
ATOM   1306 N N   . LYS A 1 206 ? -49.31066 11.34883  -2.33556  1.000 118.91612 ? 206 LYS A N   1 
ATOM   1307 C CA  . LYS A 1 206 ? -50.63561 11.20917  -2.91605  1.000 120.24452 ? 206 LYS A CA  1 
ATOM   1308 C C   . LYS A 1 206 ? -51.67731 11.82879  -1.99798  1.000 117.79948 ? 206 LYS A C   1 
ATOM   1309 O O   . LYS A 1 206 ? -51.71132 11.54247  -0.79621  1.000 108.22675 ? 206 LYS A O   1 
ATOM   1310 C CB  . LYS A 1 206 ? -50.96042 9.73699   -3.17592  1.000 113.77112 ? 206 LYS A CB  1 
ATOM   1311 C CG  . LYS A 1 206 ? -50.04565 9.08337   -4.20251  1.000 114.06758 ? 206 LYS A CG  1 
ATOM   1312 C CD  . LYS A 1 206 ? -50.83001 8.21013   -5.16654  1.000 124.98273 ? 206 LYS A CD  1 
ATOM   1313 C CE  . LYS A 1 206 ? -49.94337 7.68822   -6.28668  1.000 126.03771 ? 206 LYS A CE  1 
ATOM   1314 N NZ  . LYS A 1 206 ? -50.60134 6.58164   -7.04039  1.000 135.59417 ? 206 LYS A NZ  1 
ATOM   1315 N N   . PHE A 1 207 ? -52.51483 12.68476  -2.57445  1.000 109.79367 ? 207 PHE A N   1 
ATOM   1316 C CA  . PHE A 1 207 ? -53.65151 13.28752  -1.88484  1.000 118.80057 ? 207 PHE A CA  1 
ATOM   1317 C C   . PHE A 1 207 ? -54.84310 13.09107  -2.81202  1.000 137.85214 ? 207 PHE A C   1 
ATOM   1318 O O   . PHE A 1 207 ? -55.00622 13.85156  -3.78270  1.000 134.95443 ? 207 PHE A O   1 
ATOM   1319 C CB  . PHE A 1 207 ? -53.40522 14.75851  -1.58197  1.000 124.31171 ? 207 PHE A CB  1 
ATOM   1320 C CG  . PHE A 1 207 ? -52.27148 15.00040  -0.62033  1.000 114.89235 ? 207 PHE A CG  1 
ATOM   1321 C CD1 . PHE A 1 207 ? -52.47726 14.94270  0.74809   1.000 105.60776 ? 207 PHE A CD1 1 
ATOM   1322 C CD2 . PHE A 1 207 ? -50.99731 15.28736  -1.08937  1.000 98.07426  ? 207 PHE A CD2 1 
ATOM   1323 C CE1 . PHE A 1 207 ? -51.43438 15.17314  1.63044   1.000 100.96695 ? 207 PHE A CE1 1 
ATOM   1324 C CE2 . PHE A 1 207 ? -49.95116 15.51474  -0.21203  1.000 89.49579  ? 207 PHE A CE2 1 
ATOM   1325 C CZ  . PHE A 1 207 ? -50.17016 15.45827  1.14779   1.000 92.26506  ? 207 PHE A CZ  1 
ATOM   1326 N N   . PRO A 1 208 ? -55.69127 12.08437  -2.55410  1.000 146.39917 ? 208 PRO A N   1 
ATOM   1327 C CA  . PRO A 1 208 ? -56.69797 11.67869  -3.54954  1.000 148.72726 ? 208 PRO A CA  1 
ATOM   1328 C C   . PRO A 1 208 ? -57.65341 12.78950  -3.95929  1.000 142.93324 ? 208 PRO A C   1 
ATOM   1329 O O   . PRO A 1 208 ? -57.72189 13.14482  -5.14008  1.000 152.60913 ? 208 PRO A O   1 
ATOM   1330 C CB  . PRO A 1 208 ? -57.45064 10.53579  -2.85054  1.000 151.03999 ? 208 PRO A CB  1 
ATOM   1331 C CG  . PRO A 1 208 ? -57.03487 10.58006  -1.41613  1.000 146.09861 ? 208 PRO A CG  1 
ATOM   1332 C CD  . PRO A 1 208 ? -55.69253 11.21777  -1.36474  1.000 132.30741 ? 208 PRO A CD  1 
ATOM   1333 N N   . GLY A 1 209 ? -58.38645 13.35395  -3.00347  1.000 119.85357 ? 209 GLY A N   1 
ATOM   1334 C CA  . GLY A 1 209 ? -59.35387 14.38085  -3.34374  1.000 121.88746 ? 209 GLY A CA  1 
ATOM   1335 C C   . GLY A 1 209 ? -58.74494 15.71660  -3.70781  1.000 144.41678 ? 209 GLY A C   1 
ATOM   1336 O O   . GLY A 1 209 ? -59.46549 16.59436  -4.19630  1.000 148.69397 ? 209 GLY A O   1 
ATOM   1337 N N   . LEU A 1 210 ? -57.44146 15.88576  -3.48834  1.000 145.08058 ? 210 LEU A N   1 
ATOM   1338 C CA  . LEU A 1 210 ? -56.75563 17.14556  -3.75343  1.000 137.09826 ? 210 LEU A CA  1 
ATOM   1339 C C   . LEU A 1 210 ? -56.18867 17.22750  -5.16903  1.000 144.24406 ? 210 LEU A C   1 
ATOM   1340 O O   . LEU A 1 210 ? -56.57234 18.10328  -5.95082  1.000 149.18115 ? 210 LEU A O   1 
ATOM   1341 C CB  . LEU A 1 210 ? -55.61707 17.32411  -2.74698  1.000 129.33941 ? 210 LEU A CB  1 
ATOM   1342 C CG  . LEU A 1 210 ? -55.62049 18.52203  -1.80664  1.000 131.73644 ? 210 LEU A CG  1 
ATOM   1343 C CD1 . LEU A 1 210 ? -54.26952 18.58117  -1.11180  1.000 117.48242 ? 210 LEU A CD1 1 
ATOM   1344 C CD2 . LEU A 1 210 ? -55.93851 19.81338  -2.54021  1.000 126.49992 ? 210 LEU A CD2 1 
ATOM   1345 N N   . THR A 1 211 ? -55.28124 16.31031  -5.51215  1.000 137.57551 ? 211 THR A N   1 
ATOM   1346 C CA  . THR A 1 211 ? -54.68426 16.31475  -6.84378  1.000 138.31872 ? 211 THR A CA  1 
ATOM   1347 C C   . THR A 1 211 ? -55.67692 15.90407  -7.92353  1.000 168.37041 ? 211 THR A C   1 
ATOM   1348 O O   . THR A 1 211 ? -55.56759 16.36992  -9.06408  1.000 168.51084 ? 211 THR A O   1 
ATOM   1349 C CB  . THR A 1 211 ? -53.46218 15.39565  -6.87318  1.000 148.22395 ? 211 THR A CB  1 
ATOM   1350 O OG1 . THR A 1 211 ? -53.71588 14.22993  -6.07728  1.000 151.62761 ? 211 THR A OG1 1 
ATOM   1351 C CG2 . THR A 1 211 ? -52.23931 16.12078  -6.32722  1.000 112.74972 ? 211 THR A CG2 1 
ATOM   1352 N N   . THR A 1 212 ? -56.64121 15.04910  -7.58810  1.000 201.88866 ? 212 THR A N   1 
ATOM   1353 C CA  . THR A 1 212 ? -57.68599 14.62313  -8.52060  1.000 208.69983 ? 212 THR A CA  1 
ATOM   1354 C C   . THR A 1 212 ? -57.10707 14.07966  -9.82561  1.000 207.07884 ? 212 THR A C   1 
ATOM   1355 O O   . THR A 1 212 ? -57.41664 12.96166  -10.23618 1.000 219.11242 ? 212 THR A O   1 
ATOM   1356 C CB  . THR A 1 212 ? -58.65641 15.77978  -8.85009  1.000 211.03321 ? 212 THR A CB  1 
ATOM   1357 O OG1 . THR A 1 212 ? -59.29770 16.23052  -7.65018  1.000 192.77403 ? 212 THR A OG1 1 
ATOM   1358 C CG2 . THR A 1 212 ? -59.71291 15.32454  -9.84574  1.000 221.97461 ? 212 THR A CG2 1 
ATOM   1359 N N   . GLY B 1 15  ? -35.14491 -15.97175 -16.28246 1.000 126.00351 ? 15  GLY B N   1 
ATOM   1360 C CA  . GLY B 1 15  ? -34.12623 -15.20023 -15.59297 1.000 122.58614 ? 15  GLY B CA  1 
ATOM   1361 C C   . GLY B 1 15  ? -32.93780 -14.86054 -16.47094 1.000 123.09697 ? 15  GLY B C   1 
ATOM   1362 O O   . GLY B 1 15  ? -32.26953 -13.84379 -16.27317 1.000 115.64109 ? 15  GLY B O   1 
ATOM   1363 N N   . ASN B 1 16  ? -32.67441 -15.72176 -17.44914 1.000 126.08998 ? 16  ASN B N   1 
ATOM   1364 C CA  . ASN B 1 16  ? -31.58169 -15.53222 -18.39104 1.000 109.98110 ? 16  ASN B CA  1 
ATOM   1365 C C   . ASN B 1 16  ? -32.00233 -14.78641 -19.65255 1.000 103.46365 ? 16  ASN B C   1 
ATOM   1366 O O   . ASN B 1 16  ? -31.19907 -14.67998 -20.58420 1.000 108.18443 ? 16  ASN B O   1 
ATOM   1367 C CB  . ASN B 1 16  ? -30.97131 -16.88602 -18.77033 1.000 115.84517 ? 16  ASN B CB  1 
ATOM   1368 C CG  . ASN B 1 16  ? -32.01507 -17.98561 -18.90192 1.000 143.83053 ? 16  ASN B CG  1 
ATOM   1369 O OD1 . ASN B 1 16  ? -33.21205 -17.74946 -18.72892 1.000 142.90102 ? 16  ASN B OD1 1 
ATOM   1370 N ND2 . ASN B 1 16  ? -31.56143 -19.19802 -19.20669 1.000 140.25964 ? 16  ASN B ND2 1 
ATOM   1371 N N   . SER B 1 17  ? -33.23620 -14.28295 -19.71746 1.000 99.11438  ? 17  SER B N   1 
ATOM   1372 C CA  . SER B 1 17  ? -33.74190 -13.67081 -20.93878 1.000 91.63163  ? 17  SER B CA  1 
ATOM   1373 C C   . SER B 1 17  ? -34.50967 -12.39115 -20.61561 1.000 89.10408  ? 17  SER B C   1 
ATOM   1374 O O   . SER B 1 17  ? -34.85627 -12.11656 -19.46302 1.000 84.31391  ? 17  SER B O   1 
ATOM   1375 C CB  . SER B 1 17  ? -34.61372 -14.66331 -21.72102 1.000 82.69447  ? 17  SER B CB  1 
ATOM   1376 O OG  . SER B 1 17  ? -35.98571 -14.48767 -21.43506 1.000 96.11487  ? 17  SER B OG  1 
ATOM   1377 N N   . ASN B 1 18  ? -34.75373 -11.59312 -21.65653 1.000 76.47030  ? 18  ASN B N   1 
ATOM   1378 C CA  . ASN B 1 18  ? -35.58459 -10.39766 -21.56625 1.000 74.16955  ? 18  ASN B CA  1 
ATOM   1379 C C   . ASN B 1 18  ? -36.12960 -10.04795 -22.94567 1.000 73.63490  ? 18  ASN B C   1 
ATOM   1380 O O   . ASN B 1 18  ? -35.47201 -10.28782 -23.96113 1.000 79.91171  ? 18  ASN B O   1 
ATOM   1381 C CB  . ASN B 1 18  ? -34.80308 -9.21239  -20.99006 1.000 77.39094  ? 18  ASN B CB  1 
ATOM   1382 C CG  . ASN B 1 18  ? -35.70699 -8.07443  -20.55239 1.000 83.86826  ? 18  ASN B CG  1 
ATOM   1383 O OD1 . ASN B 1 18  ? -36.81680 -8.29220  -20.06724 1.000 85.76824  ? 18  ASN B OD1 1 
ATOM   1384 N ND2 . ASN B 1 18  ? -35.23471 -6.84792  -20.73390 1.000 81.02192  ? 18  ASN B ND2 1 
ATOM   1385 N N   . SER B 1 19  ? -37.33913 -9.48780  -22.97370 1.000 98.64457  ? 19  SER B N   1 
ATOM   1386 C CA  . SER B 1 19  ? -38.02906 -9.19537  -24.22207 1.000 94.89828  ? 19  SER B CA  1 
ATOM   1387 C C   . SER B 1 19  ? -38.58568 -7.78010  -24.17630 1.000 84.33939  ? 19  SER B C   1 
ATOM   1388 O O   . SER B 1 19  ? -38.97504 -7.28347  -23.11658 1.000 91.64287  ? 19  SER B O   1 
ATOM   1389 C CB  . SER B 1 19  ? -39.17036 -10.18442 -24.49122 1.000 92.40192  ? 19  SER B CB  1 
ATOM   1390 O OG  . SER B 1 19  ? -38.69230 -11.34264 -25.14828 1.000 109.07974 ? 19  SER B OG  1 
ATOM   1391 N N   . VAL B 1 20  ? -38.65657 -7.15122  -25.34645 1.000 81.88879  ? 20  VAL B N   1 
ATOM   1392 C CA  . VAL B 1 20  ? -39.21532 -5.80947  -25.48599 1.000 80.38687  ? 20  VAL B CA  1 
ATOM   1393 C C   . VAL B 1 20  ? -39.91470 -5.71749  -26.83391 1.000 84.08708  ? 20  VAL B C   1 
ATOM   1394 O O   . VAL B 1 20  ? -39.38868 -6.17288  -27.85346 1.000 88.11479  ? 20  VAL B O   1 
ATOM   1395 C CB  . VAL B 1 20  ? -38.12062 -4.72895  -25.33777 1.000 73.83371  ? 20  VAL B CB  1 
ATOM   1396 C CG1 . VAL B 1 20  ? -38.48606 -3.48252  -26.11715 1.000 77.27007  ? 20  VAL B CG1 1 
ATOM   1397 C CG2 . VAL B 1 20  ? -37.92144 -4.37140  -23.87047 1.000 88.26454  ? 20  VAL B CG2 1 
ATOM   1398 N N   . SER B 1 21  ? -41.10857 -5.13427  -26.83461 1.000 79.44695  ? 21  SER B N   1 
ATOM   1399 C CA  . SER B 1 21  ? -41.91553 -5.01613  -28.03755 1.000 101.11892 ? 21  SER B CA  1 
ATOM   1400 C C   . SER B 1 21  ? -42.06010 -3.55595  -28.44849 1.000 98.94994  ? 21  SER B C   1 
ATOM   1401 O O   . SER B 1 21  ? -42.10023 -2.65506  -27.60575 1.000 92.17156  ? 21  SER B O   1 
ATOM   1402 C CB  . SER B 1 21  ? -43.30295 -5.62876  -27.82468 1.000 96.03557  ? 21  SER B CB  1 
ATOM   1403 O OG  . SER B 1 21  ? -43.23463 -6.76584  -26.97949 1.000 115.98704 ? 21  SER B OG  1 
ATOM   1404 N N   . ARG B 1 22  ? -42.11759 -3.33192  -29.75931 1.000 95.90314  ? 22  ARG B N   1 
ATOM   1405 C CA  . ARG B 1 22  ? -42.33854 -2.01054  -30.32470 1.000 99.33857  ? 22  ARG B CA  1 
ATOM   1406 C C   . ARG B 1 22  ? -43.23120 -2.16716  -31.54870 1.000 112.09956 ? 22  ARG B C   1 
ATOM   1407 O O   . ARG B 1 22  ? -43.50120 -3.28143  -32.00623 1.000 115.89396 ? 22  ARG B O   1 
ATOM   1408 C CB  . ARG B 1 22  ? -41.02026 -1.30569  -30.67735 1.000 105.14200 ? 22  ARG B CB  1 
ATOM   1409 C CG  . ARG B 1 22  ? -40.49831 -1.59856  -32.07062 1.000 105.73028 ? 22  ARG B CG  1 
ATOM   1410 C CD  . ARG B 1 22  ? -39.35530 -0.66443  -32.42653 1.000 96.71087  ? 22  ARG B CD  1 
ATOM   1411 N NE  . ARG B 1 22  ? -38.46459 -1.23866  -33.42674 1.000 91.50992  ? 22  ARG B NE  1 
ATOM   1412 C CZ  . ARG B 1 22  ? -38.71071 -1.24130  -34.73029 1.000 106.16544 ? 22  ARG B CZ  1 
ATOM   1413 N NH1 . ARG B 1 22  ? -39.81620 -0.71151  -35.22660 1.000 109.90763 ? 22  ARG B NH1 1 
ATOM   1414 N NH2 . ARG B 1 22  ? -37.82129 -1.78126  -35.55783 1.000 119.45075 ? 22  ARG B NH2 1 
ATOM   1415 N N   . ILE B 1 23  ? -43.69535 -1.04171  -32.08555 1.000 115.81392 ? 23  ILE B N   1 
ATOM   1416 C CA  . ILE B 1 23  ? -44.54509 -1.03539  -33.27008 1.000 120.25516 ? 23  ILE B CA  1 
ATOM   1417 C C   . ILE B 1 23  ? -43.90340 -0.14279  -34.32011 1.000 126.61547 ? 23  ILE B C   1 
ATOM   1418 O O   . ILE B 1 23  ? -43.54512 1.00479   -34.03134 1.000 124.49446 ? 23  ILE B O   1 
ATOM   1419 C CB  . ILE B 1 23  ? -45.97170 -0.56016  -32.94477 1.000 106.41502 ? 23  ILE B CB  1 
ATOM   1420 C CG1 . ILE B 1 23  ? -46.52500 -1.32299  -31.73789 1.000 117.23619 ? 23  ILE B CG1 1 
ATOM   1421 C CG2 . ILE B 1 23  ? -46.86907 -0.74206  -34.15376 1.000 131.96984 ? 23  ILE B CG2 1 
ATOM   1422 C CD1 . ILE B 1 23  ? -48.03116 -1.26771  -31.61013 1.000 113.02799 ? 23  ILE B CD1 1 
ATOM   1423 N N   . THR B 1 24  ? -43.75149 -0.67089  -35.53165 1.000 126.43879 ? 24  THR B N   1 
ATOM   1424 C CA  . THR B 1 24  ? -43.13572 0.09662   -36.59993 1.000 140.12456 ? 24  THR B CA  1 
ATOM   1425 C C   . THR B 1 24  ? -44.17855 0.98311   -37.27794 1.000 145.53686 ? 24  THR B C   1 
ATOM   1426 O O   . THR B 1 24  ? -45.34852 1.02734   -36.88787 1.000 152.98823 ? 24  THR B O   1 
ATOM   1427 C CB  . THR B 1 24  ? -42.46129 -0.83232  -37.60771 1.000 145.13343 ? 24  THR B CB  1 
ATOM   1428 O OG1 . THR B 1 24  ? -42.08949 -0.08634  -38.77299 1.000 154.09789 ? 24  THR B OG1 1 
ATOM   1429 C CG2 . THR B 1 24  ? -43.40684 -1.94565  -38.01950 1.000 149.07630 ? 24  THR B CG2 1 
ATOM   1430 N N   . ARG B 1 25  ? -43.74479 1.70360   -38.31499 1.000 146.68127 ? 25  ARG B N   1 
ATOM   1431 C CA  . ARG B 1 25  ? -44.64148 2.63197   -38.99586 1.000 152.27271 ? 25  ARG B CA  1 
ATOM   1432 C C   . ARG B 1 25  ? -45.73407 1.89040   -39.75641 1.000 157.61226 ? 25  ARG B C   1 
ATOM   1433 O O   . ARG B 1 25  ? -46.83474 2.42411   -39.93967 1.000 144.62557 ? 25  ARG B O   1 
ATOM   1434 C CB  . ARG B 1 25  ? -43.84169 3.54156   -39.92997 1.000 140.56225 ? 25  ARG B CB  1 
ATOM   1435 C CG  . ARG B 1 25  ? -42.95625 4.52996   -39.18562 1.000 145.94029 ? 25  ARG B CG  1 
ATOM   1436 C CD  . ARG B 1 25  ? -42.08318 5.35230   -40.11850 1.000 155.09985 ? 25  ARG B CD  1 
ATOM   1437 N NE  . ARG B 1 25  ? -41.34179 6.37302   -39.38554 1.000 170.36592 ? 25  ARG B NE  1 
ATOM   1438 C CZ  . ARG B 1 25  ? -40.27749 7.01212   -39.85252 1.000 169.24860 ? 25  ARG B CZ  1 
ATOM   1439 N NH1 . ARG B 1 25  ? -39.79947 6.76772   -41.06154 1.000 178.13338 ? 25  ARG B NH1 1 
ATOM   1440 N NH2 . ARG B 1 25  ? -39.67761 7.91978   -39.08689 1.000 157.40286 ? 25  ARG B NH2 1 
ATOM   1441 N N   . GLU B 1 26  ? -45.44908 0.66251   -40.19810 1.000 161.72027 ? 26  GLU B N   1 
ATOM   1442 C CA  . GLU B 1 26  ? -46.40018 -0.14445  -40.95297 1.000 156.03394 ? 26  GLU B CA  1 
ATOM   1443 C C   . GLU B 1 26  ? -47.50542 -0.72657  -40.08377 1.000 158.19008 ? 26  GLU B C   1 
ATOM   1444 O O   . GLU B 1 26  ? -48.44577 -1.31724  -40.62522 1.000 147.85117 ? 26  GLU B O   1 
ATOM   1445 C CB  . GLU B 1 26  ? -45.67734 -1.29118  -41.66029 1.000 157.35656 ? 26  GLU B CB  1 
ATOM   1446 C CG  . GLU B 1 26  ? -44.96667 -0.90089  -42.93835 1.000 169.21325 ? 26  GLU B CG  1 
ATOM   1447 C CD  . GLU B 1 26  ? -43.59248 -1.53118  -43.03562 1.000 181.53857 ? 26  GLU B CD  1 
ATOM   1448 O OE1 . GLU B 1 26  ? -42.63495 -0.95526  -42.47994 1.000 181.32958 ? 26  GLU B OE1 1 
ATOM   1449 O OE2 . GLU B 1 26  ? -43.46879 -2.60161  -43.66825 1.000 185.20649 ? 26  GLU B OE2 1 
ATOM   1450 N N   . GLY B 1 27  ? -47.41550 -0.58665  -38.76331 1.000 180.41978 ? 27  GLY B N   1 
ATOM   1451 C CA  . GLY B 1 27  ? -48.36925 -1.20006  -37.86714 1.000 178.96139 ? 27  GLY B CA  1 
ATOM   1452 C C   . GLY B 1 27  ? -47.98594 -2.58348  -37.39250 1.000 192.04452 ? 27  GLY B C   1 
ATOM   1453 O O   . GLY B 1 27  ? -48.70139 -3.15551  -36.55968 1.000 198.34063 ? 27  GLY B O   1 
ATOM   1454 N N   . LYS B 1 28  ? -46.88497 -3.13902  -37.89217 1.000 171.68725 ? 28  LYS B N   1 
ATOM   1455 C CA  . LYS B 1 28  ? -46.42473 -4.43747  -37.42528 1.000 161.07375 ? 28  LYS B CA  1 
ATOM   1456 C C   . LYS B 1 28  ? -45.81706 -4.31198  -36.03567 1.000 144.04670 ? 28  LYS B C   1 
ATOM   1457 O O   . LYS B 1 28  ? -45.16689 -3.31534  -35.70884 1.000 143.18325 ? 28  LYS B O   1 
ATOM   1458 C CB  . LYS B 1 28  ? -45.39424 -5.02919  -38.38691 1.000 164.53323 ? 28  LYS B CB  1 
ATOM   1459 C CG  . LYS B 1 28  ? -45.84846 -5.13831  -39.83163 1.000 173.12566 ? 28  LYS B CG  1 
ATOM   1460 C CD  . LYS B 1 28  ? -44.69021 -5.56388  -40.72240 1.000 171.99454 ? 28  LYS B CD  1 
ATOM   1461 C CE  . LYS B 1 28  ? -44.97496 -5.28795  -42.18773 1.000 175.94408 ? 28  LYS B CE  1 
ATOM   1462 N NZ  . LYS B 1 28  ? -43.74467 -5.41944  -43.01765 1.000 179.07384 ? 28  LYS B NZ  1 
ATOM   1463 N N   . LYS B 1 29  ? -46.04167 -5.32980  -35.21323 1.000 127.33251 ? 29  LYS B N   1 
ATOM   1464 C CA  . LYS B 1 29  ? -45.42062 -5.41410  -33.90134 1.000 123.61334 ? 29  LYS B CA  1 
ATOM   1465 C C   . LYS B 1 29  ? -44.13332 -6.21874  -34.01528 1.000 123.13294 ? 29  LYS B C   1 
ATOM   1466 O O   . LYS B 1 29  ? -44.13005 -7.32775  -34.55932 1.000 123.92035 ? 29  LYS B O   1 
ATOM   1467 C CB  . LYS B 1 29  ? -46.37562 -6.05334  -32.89381 1.000 119.63469 ? 29  LYS B CB  1 
ATOM   1468 C CG  . LYS B 1 29  ? -45.69490 -6.73046  -31.71910 1.000 112.57287 ? 29  LYS B CG  1 
ATOM   1469 C CD  . LYS B 1 29  ? -46.52255 -6.57154  -30.45738 1.000 113.17115 ? 29  LYS B CD  1 
ATOM   1470 C CE  . LYS B 1 29  ? -45.97324 -7.41351  -29.32367 1.000 117.13025 ? 29  LYS B CE  1 
ATOM   1471 N NZ  . LYS B 1 29  ? -46.92926 -7.48548  -28.18589 1.000 130.30460 ? 29  LYS B NZ  1 
ATOM   1472 N N   . ILE B 1 30  ? -43.04237 -5.65355  -33.50695 1.000 113.83686 ? 30  ILE B N   1 
ATOM   1473 C CA  . ILE B 1 30  ? -41.72721 -6.28033  -33.55044 1.000 109.94838 ? 30  ILE B CA  1 
ATOM   1474 C C   . ILE B 1 30  ? -41.25433 -6.52166  -32.12459 1.000 96.00865  ? 30  ILE B C   1 
ATOM   1475 O O   . ILE B 1 30  ? -41.22037 -5.59087  -31.31010 1.000 99.92954  ? 30  ILE B O   1 
ATOM   1476 C CB  . ILE B 1 30  ? -40.72207 -5.40889  -34.32457 1.000 105.91219 ? 30  ILE B CB  1 
ATOM   1477 C CG1 . ILE B 1 30  ? -41.22828 -5.17073  -35.75026 1.000 104.72566 ? 30  ILE B CG1 1 
ATOM   1478 C CG2 . ILE B 1 30  ? -39.34259 -6.04759  -34.31826 1.000 91.57089  ? 30  ILE B CG2 1 
ATOM   1479 C CD1 . ILE B 1 30  ? -40.13660 -4.93335  -36.76515 1.000 116.72353 ? 30  ILE B CD1 1 
ATOM   1480 N N   . THR B 1 31  ? -40.89034 -7.76695  -31.82605 1.000 97.23118  ? 31  THR B N   1 
ATOM   1481 C CA  . THR B 1 31  ? -40.41793 -8.15183  -30.50281 1.000 90.98818  ? 31  THR B CA  1 
ATOM   1482 C C   . THR B 1 31  ? -38.95835 -8.57672  -30.58404 1.000 89.57144  ? 31  THR B C   1 
ATOM   1483 O O   . THR B 1 31  ? -38.59049 -9.38984  -31.43959 1.000 95.27791  ? 31  THR B O   1 
ATOM   1484 C CB  . THR B 1 31  ? -41.26159 -9.29614  -29.93183 1.000 92.31532  ? 31  THR B CB  1 
ATOM   1485 O OG1 . THR B 1 31  ? -42.55917 -8.80550  -29.57058 1.000 106.40281 ? 31  THR B OG1 1 
ATOM   1486 C CG2 . THR B 1 31  ? -40.59054 -9.90962  -28.70726 1.000 86.89807  ? 31  THR B CG2 1 
ATOM   1487 N N   . TYR B 1 32  ? -38.13610 -8.01385  -29.69988 1.000 79.49670  ? 32  TYR B N   1 
ATOM   1488 C CA  . TYR B 1 32  ? -36.73089 -8.37205  -29.56048 1.000 76.32852  ? 32  TYR B CA  1 
ATOM   1489 C C   . TYR B 1 32  ? -36.56533 -9.21435  -28.30544 1.000 73.09162  ? 32  TYR B C   1 
ATOM   1490 O O   . TYR B 1 32  ? -36.99045 -8.80364  -27.22144 1.000 84.00933  ? 32  TYR B O   1 
ATOM   1491 C CB  . TYR B 1 32  ? -35.84791 -7.12367  -29.47137 1.000 82.01426  ? 32  TYR B CB  1 
ATOM   1492 C CG  . TYR B 1 32  ? -36.05446 -6.12841  -30.59238 1.000 72.84593  ? 32  TYR B CG  1 
ATOM   1493 C CD1 . TYR B 1 32  ? -37.13299 -5.25128  -30.58811 1.000 74.38191  ? 32  TYR B CD1 1 
ATOM   1494 C CD2 . TYR B 1 32  ? -35.16343 -6.06632  -31.65533 1.000 77.78126  ? 32  TYR B CD2 1 
ATOM   1495 C CE1 . TYR B 1 32  ? -37.31902 -4.34538  -31.61609 1.000 84.30824  ? 32  TYR B CE1 1 
ATOM   1496 C CE2 . TYR B 1 32  ? -35.34007 -5.16729  -32.68212 1.000 84.68148  ? 32  TYR B CE2 1 
ATOM   1497 C CZ  . TYR B 1 32  ? -36.41529 -4.30779  -32.65869 1.000 86.61802  ? 32  TYR B CZ  1 
ATOM   1498 O OH  . TYR B 1 32  ? -36.57872 -3.41390  -33.68943 1.000 86.88842  ? 32  TYR B OH  1 
ATOM   1499 N N   . LYS B 1 33  ? -35.93876 -10.37802 -28.44534 1.000 87.95295  ? 33  LYS B N   1 
ATOM   1500 C CA  . LYS B 1 33  ? -35.68375 -11.25857 -27.31443 1.000 83.27635  ? 33  LYS B CA  1 
ATOM   1501 C C   . LYS B 1 33  ? -34.18816 -11.50104 -27.19118 1.000 76.03723  ? 33  LYS B C   1 
ATOM   1502 O O   . LYS B 1 33  ? -33.54916 -11.95708 -28.14483 1.000 81.76513  ? 33  LYS B O   1 
ATOM   1503 C CB  . LYS B 1 33  ? -36.44129 -12.57960 -27.46244 1.000 92.74700  ? 33  LYS B CB  1 
ATOM   1504 C CG  . LYS B 1 33  ? -36.55946 -13.36361 -26.16344 1.000 97.61984  ? 33  LYS B CG  1 
ATOM   1505 C CD  . LYS B 1 33  ? -36.52675 -14.86375 -26.38914 1.000 112.17398 ? 33  LYS B CD  1 
ATOM   1506 C CE  . LYS B 1 33  ? -37.30698 -15.58433 -25.30090 1.000 124.17108 ? 33  LYS B CE  1 
ATOM   1507 N NZ  . LYS B 1 33  ? -37.05484 -17.04885 -25.30212 1.000 127.39997 ? 33  LYS B NZ  1 
ATOM   1508 N N   . LEU B 1 34  ? -33.63530 -11.19073 -26.02085 1.000 75.52212  ? 34  LEU B N   1 
ATOM   1509 C CA  . LEU B 1 34  ? -32.23992 -11.46152 -25.69937 1.000 72.72030  ? 34  LEU B CA  1 
ATOM   1510 C C   . LEU B 1 34  ? -32.22437 -12.57028 -24.66186 1.000 76.50726  ? 34  LEU B C   1 
ATOM   1511 O O   . LEU B 1 34  ? -32.98140 -12.51546 -23.68679 1.000 75.11848  ? 34  LEU B O   1 
ATOM   1512 C CB  . LEU B 1 34  ? -31.53321 -10.22347 -25.14342 1.000 70.22433  ? 34  LEU B CB  1 
ATOM   1513 C CG  . LEU B 1 34  ? -31.08913 -9.11936  -26.09338 1.000 70.71015  ? 34  LEU B CG  1 
ATOM   1514 C CD1 . LEU B 1 34  ? -30.51440 -7.99120  -25.28096 1.000 62.40070  ? 34  LEU B CD1 1 
ATOM   1515 C CD2 . LEU B 1 34  ? -30.05988 -9.64554  -27.07073 1.000 65.69305  ? 34  LEU B CD2 1 
ATOM   1516 N N   . ASN B 1 35  ? -31.39343 -13.58488 -24.87616 1.000 68.46757  ? 35  ASN B N   1 
ATOM   1517 C CA  . ASN B 1 35  ? -31.26667 -14.63656 -23.87849 1.000 80.37851  ? 35  ASN B CA  1 
ATOM   1518 C C   . ASN B 1 35  ? -29.81568 -15.08630 -23.83857 1.000 69.47687  ? 35  ASN B C   1 
ATOM   1519 O O   . ASN B 1 35  ? -29.16063 -15.20566 -24.87954 1.000 67.50691  ? 35  ASN B O   1 
ATOM   1520 C CB  . ASN B 1 35  ? -32.26357 -15.78489 -24.17411 1.000 78.88040  ? 35  ASN B CB  1 
ATOM   1521 C CG  . ASN B 1 35  ? -31.95650 -17.10953 -23.45638 1.000 88.47853  ? 35  ASN B CG  1 
ATOM   1522 O OD1 . ASN B 1 35  ? -30.83840 -17.40792 -23.02038 1.000 106.88764 ? 35  ASN B OD1 1 
ATOM   1523 N ND2 . ASN B 1 35  ? -33.02636 -17.86045 -23.22543 1.000 113.72293 ? 35  ASN B ND2 1 
ATOM   1524 N N   . ILE B 1 36  ? -29.30878 -15.27698 -22.62559 1.000 74.57481  ? 36  ILE B N   1 
ATOM   1525 C CA  . ILE B 1 36  ? -27.90885 -15.61182 -22.39524 1.000 68.15100  ? 36  ILE B CA  1 
ATOM   1526 C C   . ILE B 1 36  ? -27.76644 -17.12542 -22.50580 1.000 72.35088  ? 36  ILE B C   1 
ATOM   1527 O O   . ILE B 1 36  ? -28.42901 -17.87490 -21.78051 1.000 82.52154  ? 36  ILE B O   1 
ATOM   1528 C CB  . ILE B 1 36  ? -27.44132 -15.10994 -21.02234 1.000 77.11335  ? 36  ILE B CB  1 
ATOM   1529 C CG1 . ILE B 1 36  ? -27.67894 -13.60150 -20.89923 1.000 73.39716  ? 36  ILE B CG1 1 
ATOM   1530 C CG2 . ILE B 1 36  ? -25.98469 -15.47499 -20.77760 1.000 66.35124  ? 36  ILE B CG2 1 
ATOM   1531 C CD1 . ILE B 1 36  ? -27.70048 -13.10893 -19.47593 1.000 63.46115  ? 36  ILE B CD1 1 
ATOM   1532 N N   . MET B 1 37  ? -26.89794 -17.57333 -23.41199 1.000 81.60504  ? 37  MET B N   1 
ATOM   1533 C CA  . MET B 1 37  ? -26.55851 -18.98751 -23.56385 1.000 83.32356  ? 37  MET B CA  1 
ATOM   1534 C C   . MET B 1 37  ? -25.40943 -19.44353 -22.68233 1.000 76.70222  ? 37  MET B C   1 
ATOM   1535 O O   . MET B 1 37  ? -25.39660 -20.60254 -22.25035 1.000 93.46326  ? 37  MET B O   1 
ATOM   1536 C CB  . MET B 1 37  ? -26.24488 -19.31595 -25.02477 1.000 74.29277  ? 37  MET B CB  1 
ATOM   1537 C CG  . MET B 1 37  ? -27.28748 -18.80068 -25.97960 1.000 78.97098  ? 37  MET B CG  1 
ATOM   1538 S SD  . MET B 1 37  ? -28.88737 -19.11145 -25.20777 1.000 98.52669  ? 37  MET B SD  1 
ATOM   1539 C CE  . MET B 1 37  ? -29.80387 -19.85123 -26.54563 1.000 117.41432 ? 37  MET B CE  1 
ATOM   1540 N N   . GLN B 1 38  ? -24.45368 -18.56788 -22.39761 1.000 75.33827  ? 38  GLN B N   1 
ATOM   1541 C CA  . GLN B 1 38  ? -23.26994 -18.92274 -21.62107 1.000 80.62695  ? 38  GLN B CA  1 
ATOM   1542 C C   . GLN B 1 38  ? -23.02885 -17.81545 -20.60793 1.000 67.10184  ? 38  GLN B C   1 
ATOM   1543 O O   . GLN B 1 38  ? -22.67335 -16.69413 -20.98103 1.000 62.11081  ? 38  GLN B O   1 
ATOM   1544 C CB  . GLN B 1 38  ? -22.04940 -19.11410 -22.51984 1.000 67.32470  ? 38  GLN B CB  1 
ATOM   1545 C CG  . GLN B 1 38  ? -20.79097 -19.47413 -21.76695 1.000 67.33157  ? 38  GLN B CG  1 
ATOM   1546 C CD  . GLN B 1 38  ? -19.90248 -20.39416 -22.56074 1.000 79.01902  ? 38  GLN B CD  1 
ATOM   1547 O OE1 . GLN B 1 38  ? -19.95852 -21.61583 -22.40644 1.000 85.95118  ? 38  GLN B OE1 1 
ATOM   1548 N NE2 . GLN B 1 38  ? -19.08516 -19.81650 -23.43459 1.000 71.79648  ? 38  GLN B NE2 1 
ATOM   1549 N N   . GLN B 1 39  ? -23.28724 -18.11347 -19.34108 1.000 67.66499  ? 39  GLN B N   1 
ATOM   1550 C CA  . GLN B 1 39  ? -23.06433 -17.11602 -18.31555 1.000 78.82660  ? 39  GLN B CA  1 
ATOM   1551 C C   . GLN B 1 39  ? -21.57790 -17.02561 -17.97911 1.000 82.11516  ? 39  GLN B C   1 
ATOM   1552 O O   . GLN B 1 39  ? -20.85211 -18.02048 -18.05762 1.000 83.80073  ? 39  GLN B O   1 
ATOM   1553 C CB  . GLN B 1 39  ? -23.85270 -17.46202 -17.06020 1.000 79.63320  ? 39  GLN B CB  1 
ATOM   1554 C CG  . GLN B 1 39  ? -25.34802 -17.46009 -17.28044 1.000 76.13334  ? 39  GLN B CG  1 
ATOM   1555 C CD  . GLN B 1 39  ? -25.96891 -16.11044 -17.02116 1.000 88.19346  ? 39  GLN B CD  1 
ATOM   1556 O OE1 . GLN B 1 39  ? -25.32258 -15.20428 -16.48563 1.000 81.11136  ? 39  GLN B OE1 1 
ATOM   1557 N NE2 . GLN B 1 39  ? -27.23512 -15.96565 -17.39628 1.000 93.34591  ? 39  GLN B NE2 1 
ATOM   1558 N N   . PRO B 1 40  ? -21.10084 -15.83988 -17.61694 1.000 79.17203  ? 40  PRO B N   1 
ATOM   1559 C CA  . PRO B 1 40  ? -19.75058 -15.73276 -17.06033 1.000 70.67643  ? 40  PRO B CA  1 
ATOM   1560 C C   . PRO B 1 40  ? -19.66358 -16.37305 -15.68957 1.000 77.01749  ? 40  PRO B C   1 
ATOM   1561 O O   . PRO B 1 40  ? -20.61179 -16.34878 -14.90093 1.000 82.56606  ? 40  PRO B O   1 
ATOM   1562 C CB  . PRO B 1 40  ? -19.52689 -14.22096 -16.96758 1.000 80.08298  ? 40  PRO B CB  1 
ATOM   1563 C CG  . PRO B 1 40  ? -20.89169 -13.64755 -16.86520 1.000 82.01525  ? 40  PRO B CG  1 
ATOM   1564 C CD  . PRO B 1 40  ? -21.77410 -14.53355 -17.69852 1.000 83.57229  ? 40  PRO B CD  1 
ATOM   1565 N N   . LYS B 1 41  ? -18.50690 -16.96347 -15.41187 1.000 71.41742  ? 41  LYS B N   1 
ATOM   1566 C CA  . LYS B 1 41  ? -18.32160 -17.66914 -14.15415 1.000 72.81013  ? 41  LYS B CA  1 
ATOM   1567 C C   . LYS B 1 41  ? -17.22168 -17.07420 -13.29291 1.000 76.70891  ? 41  LYS B C   1 
ATOM   1568 O O   . LYS B 1 41  ? -17.45376 -16.76863 -12.11761 1.000 82.06707  ? 41  LYS B O   1 
ATOM   1569 C CB  . LYS B 1 41  ? -18.04190 -19.15483 -14.42848 1.000 80.50564  ? 41  LYS B CB  1 
ATOM   1570 C CG  . LYS B 1 41  ? -19.29402 -19.95624 -14.75403 1.000 82.60573  ? 41  LYS B CG  1 
ATOM   1571 C CD  . LYS B 1 41  ? -20.37525 -19.68788 -13.71293 1.000 98.63026  ? 41  LYS B CD  1 
ATOM   1572 C CE  . LYS B 1 41  ? -21.32555 -20.86819 -13.54839 1.000 101.08771 ? 41  LYS B CE  1 
ATOM   1573 N NZ  . LYS B 1 41  ? -21.26108 -21.82428 -14.68689 1.000 117.03308 ? 41  LYS B NZ  1 
ATOM   1574 N N   . ARG B 1 42  ? -16.01854 -16.92332 -13.83693 1.000 72.51585  ? 42  ARG B N   1 
ATOM   1575 C CA  . ARG B 1 42  ? -14.87559 -16.48708 -13.05429 1.000 65.44795  ? 42  ARG B CA  1 
ATOM   1576 C C   . ARG B 1 42  ? -13.94774 -15.60637 -13.87585 1.000 77.36754  ? 42  ARG B C   1 
ATOM   1577 O O   . ARG B 1 42  ? -13.95588 -15.62560 -15.10783 1.000 72.78863  ? 42  ARG B O   1 
ATOM   1578 C CB  . ARG B 1 42  ? -14.08861 -17.67686 -12.52392 1.000 83.09740  ? 42  ARG B CB  1 
ATOM   1579 C CG  . ARG B 1 42  ? -14.86487 -18.63451 -11.64127 1.000 102.97691 ? 42  ARG B CG  1 
ATOM   1580 C CD  . ARG B 1 42  ? -15.05957 -18.11042 -10.23874 1.000 102.28262 ? 42  ARG B CD  1 
ATOM   1581 N NE  . ARG B 1 42  ? -15.31612 -19.20039 -9.30357  1.000 101.35584 ? 42  ARG B NE  1 
ATOM   1582 C CZ  . ARG B 1 42  ? -16.48749 -19.46817 -8.74588  1.000 82.32329  ? 42  ARG B CZ  1 
ATOM   1583 N NH1 . ARG B 1 42  ? -17.56682 -18.75848 -9.02923  1.000 89.83294  ? 42  ARG B NH1 1 
ATOM   1584 N NH2 . ARG B 1 42  ? -16.56979 -20.45549 -7.85935  1.000 90.47500  ? 42  ARG B NH2 1 
ATOM   1585 N N   . ALA B 1 43  ? -13.13167 -14.83981 -13.16469 1.000 68.93555  ? 43  ALA B N   1 
ATOM   1586 C CA  . ALA B 1 43  ? -12.06832 -14.07315 -13.78863 1.000 78.53245  ? 43  ALA B CA  1 
ATOM   1587 C C   . ALA B 1 43  ? -11.01940 -13.78771 -12.73131 1.000 75.77647  ? 43  ALA B C   1 
ATOM   1588 O O   . ALA B 1 43  ? -11.31426 -13.75877 -11.53427 1.000 74.44649  ? 43  ALA B O   1 
ATOM   1589 C CB  . ALA B 1 43  ? -12.57563 -12.76318 -14.40163 1.000 78.89470  ? 43  ALA B CB  1 
ATOM   1590 N N   . ARG B 1 44  ? -9.79282  -13.58990 -13.18440 1.000 78.92461  ? 44  ARG B N   1 
ATOM   1591 C CA  . ARG B 1 44  ? -8.69354  -13.24346 -12.30103 1.000 82.06366  ? 44  ARG B CA  1 
ATOM   1592 C C   . ARG B 1 44  ? -8.44543  -11.75152 -12.46056 1.000 83.43332  ? 44  ARG B C   1 
ATOM   1593 O O   . ARG B 1 44  ? -8.29354  -11.26283 -13.58605 1.000 83.96369  ? 44  ARG B O   1 
ATOM   1594 C CB  . ARG B 1 44  ? -7.44729  -14.06013 -12.64371 1.000 87.94755  ? 44  ARG B CB  1 
ATOM   1595 C CG  . ARG B 1 44  ? -6.25484  -13.85952 -11.72943 1.000 91.89272  ? 44  ARG B CG  1 
ATOM   1596 C CD  . ARG B 1 44  ? -4.99680  -14.37386 -12.41055 1.000 99.42723  ? 44  ARG B CD  1 
ATOM   1597 N NE  . ARG B 1 44  ? -3.98772  -14.85577 -11.47338 1.000 111.51389 ? 44  ARG B NE  1 
ATOM   1598 C CZ  . ARG B 1 44  ? -2.76914  -15.24404 -11.82639 1.000 113.89351 ? 44  ARG B CZ  1 
ATOM   1599 N NH1 . ARG B 1 44  ? -2.37305  -15.21722 -13.08837 1.000 133.41224 ? 44  ARG B NH1 1 
ATOM   1600 N NH2 . ARG B 1 44  ? -1.92529  -15.66729 -10.89077 1.000 130.28024 ? 44  ARG B NH2 1 
ATOM   1601 N N   . ALA B 1 45  ? -8.45767  -11.02806 -11.34319 1.000 80.45245  ? 45  ALA B N   1 
ATOM   1602 C CA  . ALA B 1 45  ? -8.29426  -9.58299  -11.39419 1.000 79.58976  ? 45  ALA B CA  1 
ATOM   1603 C C   . ALA B 1 45  ? -7.01151  -9.21737  -12.12580 1.000 84.47108  ? 45  ALA B C   1 
ATOM   1604 O O   . ALA B 1 45  ? -5.93347  -9.72783  -11.81040 1.000 94.58635  ? 45  ALA B O   1 
ATOM   1605 C CB  . ALA B 1 45  ? -8.28694  -9.00514  -9.98017  1.000 78.61346  ? 45  ALA B CB  1 
ATOM   1606 N N   . CYS B 1 46  ? -7.13782  -8.33949  -13.12056 1.000 84.05866  ? 46  CYS B N   1 
ATOM   1607 C CA  . CYS B 1 46  ? -6.00336  -7.98658  -13.96253 1.000 98.73322  ? 46  CYS B CA  1 
ATOM   1608 C C   . CYS B 1 46  ? -5.12279  -6.90913  -13.34360 1.000 115.33958 ? 46  CYS B C   1 
ATOM   1609 O O   . CYS B 1 46  ? -3.98409  -6.73098  -13.79036 1.000 138.31387 ? 46  CYS B O   1 
ATOM   1610 C CB  . CYS B 1 46  ? -6.48685  -7.54494  -15.34811 1.000 95.28293  ? 46  CYS B CB  1 
ATOM   1611 S SG  . CYS B 1 46  ? -7.64558  -6.16161  -15.35863 1.000 109.22091 ? 46  CYS B SG  1 
ATOM   1612 N N   . GLY B 1 47  ? -5.60854  -6.20478  -12.32375 1.000 97.18206  ? 47  GLY B N   1 
ATOM   1613 C CA  . GLY B 1 47  ? -4.80703  -5.15594  -11.72251 1.000 129.19618 ? 47  GLY B CA  1 
ATOM   1614 C C   . GLY B 1 47  ? -4.50678  -4.03829  -12.70622 1.000 148.22785 ? 47  GLY B C   1 
ATOM   1615 O O   . GLY B 1 47  ? -5.24545  -3.79537  -13.66687 1.000 143.60930 ? 47  GLY B O   1 
ATOM   1616 N N   . GLN B 1 48  ? -3.39361  -3.35112  -12.47085 1.000 160.32716 ? 48  GLN B N   1 
ATOM   1617 C CA  . GLN B 1 48  ? -3.00459  -2.23191  -13.32276 1.000 166.11701 ? 48  GLN B CA  1 
ATOM   1618 C C   . GLN B 1 48  ? -1.69415  -2.52422  -14.04462 1.000 165.57023 ? 48  GLN B C   1 
ATOM   1619 O O   . GLN B 1 48  ? -1.35224  -3.68226  -14.28346 1.000 166.38559 ? 48  GLN B O   1 
ATOM   1620 C CB  . GLN B 1 48  ? -2.87017  -0.94682  -12.50068 1.000 168.80670 ? 48  GLN B CB  1 
ATOM   1621 C CG  . GLN B 1 48  ? -4.18790  -0.25834  -12.17059 1.000 163.58005 ? 48  GLN B CG  1 
ATOM   1622 C CD  . GLN B 1 48  ? -4.81417  -0.77001  -10.88491 1.000 161.37337 ? 48  GLN B CD  1 
ATOM   1623 O OE1 . GLN B 1 48  ? -4.58525  -1.90853  -10.47557 1.000 158.21051 ? 48  GLN B OE1 1 
ATOM   1624 N NE2 . GLN B 1 48  ? -5.59935  0.08036   -10.23258 1.000 156.92147 ? 48  GLN B NE2 1 
ATOM   1625 N N   . LYS B 1 51  ? 0.95904   -14.13457 -11.27927 1.000 136.99963 ? 51  LYS B N   1 
ATOM   1626 C CA  . LYS B 1 51  ? 0.30504   -13.13403 -12.11528 1.000 146.84526 ? 51  LYS B CA  1 
ATOM   1627 C C   . LYS B 1 51  ? 0.91033   -13.04826 -13.51328 1.000 150.95641 ? 51  LYS B C   1 
ATOM   1628 O O   . LYS B 1 51  ? 0.80733   -12.01657 -14.17786 1.000 148.52556 ? 51  LYS B O   1 
ATOM   1629 C CB  . LYS B 1 51  ? 0.35692   -11.75983 -11.44765 1.000 142.36513 ? 51  LYS B CB  1 
ATOM   1630 C CG  . LYS B 1 51  ? -0.31088  -11.70644 -10.08736 1.000 138.73402 ? 51  LYS B CG  1 
ATOM   1631 C CD  . LYS B 1 51  ? -0.41039  -10.27264 -9.59902  1.000 136.11932 ? 51  LYS B CD  1 
ATOM   1632 C CE  . LYS B 1 51  ? -1.16296  -10.17839 -8.28172  1.000 139.75983 ? 51  LYS B CE  1 
ATOM   1633 N NZ  . LYS B 1 51  ? -1.46214  -8.76502  -7.90731  1.000 147.86969 ? 51  LYS B NZ  1 
ATOM   1634 N N   . SER B 1 52  ? 1.53971   -14.13255 -13.96149 1.000 155.49209 ? 52  SER B N   1 
ATOM   1635 C CA  . SER B 1 52  ? 2.09027   -14.19826 -15.30712 1.000 156.93126 ? 52  SER B CA  1 
ATOM   1636 C C   . SER B 1 52  ? 1.17498   -14.95895 -16.24913 1.000 152.65531 ? 52  SER B C   1 
ATOM   1637 O O   . SER B 1 52  ? 1.54430   -15.21850 -17.39901 1.000 154.87436 ? 52  SER B O   1 
ATOM   1638 C CB  . SER B 1 52  ? 3.47215   -14.84969 -15.28256 1.000 149.95052 ? 52  SER B CB  1 
ATOM   1639 O OG  . SER B 1 52  ? 4.05472   -14.83337 -16.57206 1.000 154.32264 ? 52  SER B OG  1 
ATOM   1640 N N   . HIS B 1 53  ? -0.00597  -15.32074 -15.77421 1.000 130.94681 ? 53  HIS B N   1 
ATOM   1641 C CA  . HIS B 1 53  ? -1.00660  -16.05184 -16.53852 1.000 131.12637 ? 53  HIS B CA  1 
ATOM   1642 C C   . HIS B 1 53  ? -2.00673  -15.01139 -17.02424 1.000 123.84891 ? 53  HIS B C   1 
ATOM   1643 O O   . HIS B 1 53  ? -2.94479  -14.65383 -16.30677 1.000 110.67747 ? 53  HIS B O   1 
ATOM   1644 C CB  . HIS B 1 53  ? -1.64278  -17.14397 -15.68859 1.000 120.95140 ? 53  HIS B CB  1 
ATOM   1645 C CG  . HIS B 1 53  ? -0.65412  -18.13654 -15.16174 1.000 127.79572 ? 53  HIS B CG  1 
ATOM   1646 N ND1 . HIS B 1 53  ? 0.42433   -18.57023 -15.90251 1.000 138.36506 ? 53  HIS B ND1 1 
ATOM   1647 C CD2 . HIS B 1 53  ? -0.56357  -18.76271 -13.96463 1.000 129.75909 ? 53  HIS B CD2 1 
ATOM   1648 C CE1 . HIS B 1 53  ? 1.12686   -19.43388 -15.19169 1.000 137.13855 ? 53  HIS B CE1 1 
ATOM   1649 N NE2 . HIS B 1 53  ? 0.54977   -19.56727 -14.01111 1.000 133.41927 ? 53  HIS B NE2 1 
ATOM   1650 N N   . THR B 1 54  ? -1.80987  -14.53124 -18.25118 1.000 118.13386 ? 54  THR B N   1 
ATOM   1651 C CA  . THR B 1 54  ? -2.62075  -13.44008 -18.77077 1.000 115.12334 ? 54  THR B CA  1 
ATOM   1652 C C   . THR B 1 54  ? -3.89718  -13.92751 -19.43331 1.000 117.57476 ? 54  THR B C   1 
ATOM   1653 O O   . THR B 1 54  ? -4.85867  -13.15482 -19.53148 1.000 104.48170 ? 54  THR B O   1 
ATOM   1654 C CB  . THR B 1 54  ? -1.81455  -12.59155 -19.76231 1.000 117.94366 ? 54  THR B CB  1 
ATOM   1655 O OG1 . THR B 1 54  ? -1.46214  -13.37747 -20.90826 1.000 122.38789 ? 54  THR B OG1 1 
ATOM   1656 C CG2 . THR B 1 54  ? -0.55009  -12.07612 -19.10448 1.000 122.35132 ? 54  THR B CG2 1 
ATOM   1657 N N   . ASP B 1 55  ? -3.94158  -15.18557 -19.87110 1.000 116.71522 ? 55  ASP B N   1 
ATOM   1658 C CA  . ASP B 1 55  ? -5.17812  -15.71924 -20.42261 1.000 107.84159 ? 55  ASP B CA  1 
ATOM   1659 C C   . ASP B 1 55  ? -6.13284  -16.14254 -19.31856 1.000 102.43707 ? 55  ASP B C   1 
ATOM   1660 O O   . ASP B 1 55  ? -7.24172  -16.60023 -19.60916 1.000 109.98214 ? 55  ASP B O   1 
ATOM   1661 C CB  . ASP B 1 55  ? -4.89841  -16.90095 -21.35202 1.000 111.90880 ? 55  ASP B CB  1 
ATOM   1662 C CG  . ASP B 1 55  ? -5.86369  -16.95763 -22.52135 1.000 109.64281 ? 55  ASP B CG  1 
ATOM   1663 O OD1 . ASP B 1 55  ? -7.08429  -17.05282 -22.28873 1.000 117.75864 ? 55  ASP B OD1 1 
ATOM   1664 O OD2 . ASP B 1 55  ? -5.40505  -16.90695 -23.67809 1.000 123.92933 ? 55  ASP B OD2 1 
ATOM   1665 N N   . ARG B 1 56  ? -5.71886  -15.98423 -18.06251 1.000 102.37614 ? 56  ARG B N   1 
ATOM   1666 C CA  . ARG B 1 56  ? -6.53249  -16.28200 -16.89678 1.000 98.05977  ? 56  ARG B CA  1 
ATOM   1667 C C   . ARG B 1 56  ? -7.34928  -15.07482 -16.46165 1.000 92.62151  ? 56  ARG B C   1 
ATOM   1668 O O   . ARG B 1 56  ? -8.19166  -15.19720 -15.56706 1.000 88.61563  ? 56  ARG B O   1 
ATOM   1669 C CB  . ARG B 1 56  ? -5.63932  -16.74800 -15.74065 1.000 101.35924 ? 56  ARG B CB  1 
ATOM   1670 C CG  . ARG B 1 56  ? -5.08664  -18.15819 -15.90608 1.000 106.17470 ? 56  ARG B CG  1 
ATOM   1671 C CD  . ARG B 1 56  ? -5.41964  -19.04347 -14.71338 1.000 109.42185 ? 56  ARG B CD  1 
ATOM   1672 N NE  . ARG B 1 56  ? -4.22971  -19.55975 -14.04354 1.000 116.28507 ? 56  ARG B NE  1 
ATOM   1673 C CZ  . ARG B 1 56  ? -3.66196  -20.72958 -14.31096 1.000 115.99052 ? 56  ARG B CZ  1 
ATOM   1674 N NH1 . ARG B 1 56  ? -4.14748  -21.53854 -15.23712 1.000 116.20521 ? 56  ARG B NH1 1 
ATOM   1675 N NH2 . ARG B 1 56  ? -2.58383  -21.10141 -13.62611 1.000 121.22863 ? 56  ARG B NH2 1 
ATOM   1676 N N   . ARG B 1 57  ? -7.12437  -13.92219 -17.09033 1.000 96.47096  ? 57  ARG B N   1 
ATOM   1677 C CA  . ARG B 1 57  ? -7.76754  -12.65684 -16.75849 1.000 93.16384  ? 57  ARG B CA  1 
ATOM   1678 C C   . ARG B 1 57  ? -9.08636  -12.49006 -17.51265 1.000 78.13132  ? 57  ARG B C   1 
ATOM   1679 O O   . ARG B 1 57  ? -10.08058 -12.09820 -16.88637 1.000 71.90924  ? 57  ARG B O   1 
ATOM   1680 C CB  . ARG B 1 57  ? -6.82672  -11.47914 -17.04253 1.000 95.39317  ? 57  ARG B CB  1 
ATOM   1681 C CG  . ARG B 1 57  ? -5.73414  -11.28058 -16.00689 1.000 90.41238  ? 57  ARG B CG  1 
ATOM   1682 C CD  . ARG B 1 57  ? -4.57818  -10.48034 -16.57990 1.000 113.49141 ? 57  ARG B CD  1 
ATOM   1683 N NE  . ARG B 1 57  ? -3.65425  -10.02913 -15.54603 1.000 125.90212 ? 57  ARG B NE  1 
ATOM   1684 C CZ  . ARG B 1 57  ? -2.66367  -10.76092 -15.05503 1.000 137.08973 ? 57  ARG B CZ  1 
ATOM   1685 N NH1 . ARG B 1 57  ? -2.43552  -11.99189 -15.48295 1.000 132.92195 ? 57  ARG B NH1 1 
ATOM   1686 N NH2 . ARG B 1 57  ? -1.87793  -10.24223 -14.11579 1.000 146.92015 ? 57  ARG B NH2 1 
ATOM   1687 N N   . PRO B 1 58  ? -9.15496  -12.73658 -18.83041 1.000 79.65683  ? 58  PRO B N   1 
ATOM   1688 C CA  . PRO B 1 58  ? -10.44422 -12.59501 -19.52065 1.000 75.20219  ? 58  PRO B CA  1 
ATOM   1689 C C   . PRO B 1 58  ? -11.52225 -13.39952 -18.80841 1.000 78.01629  ? 58  PRO B C   1 
ATOM   1690 O O   . PRO B 1 58  ? -11.27735 -14.50464 -18.31857 1.000 77.98240  ? 58  PRO B O   1 
ATOM   1691 C CB  . PRO B 1 58  ? -10.17397 -13.14390 -20.92756 1.000 63.22273  ? 58  PRO B CB  1 
ATOM   1692 C CG  . PRO B 1 58  ? -8.71839  -13.41524 -21.01666 1.000 73.15153  ? 58  PRO B CG  1 
ATOM   1693 C CD  . PRO B 1 58  ? -8.04841  -12.93159 -19.78594 1.000 73.34429  ? 58  PRO B CD  1 
ATOM   1694 N N   . VAL B 1 59  ? -12.73039 -12.83735 -18.75827 1.000 70.99721  ? 59  VAL B N   1 
ATOM   1695 C CA  . VAL B 1 59  ? -13.82271 -13.51599 -18.07851 1.000 67.50590  ? 59  VAL B CA  1 
ATOM   1696 C C   . VAL B 1 59  ? -14.13063 -14.81732 -18.79849 1.000 71.33770  ? 59  VAL B C   1 
ATOM   1697 O O   . VAL B 1 59  ? -14.29376 -14.84931 -20.02484 1.000 67.24384  ? 59  VAL B O   1 
ATOM   1698 C CB  . VAL B 1 59  ? -15.05118 -12.60330 -18.00098 1.000 75.86354  ? 59  VAL B CB  1 
ATOM   1699 C CG1 . VAL B 1 59  ? -16.26457 -13.40890 -17.62855 1.000 74.23392  ? 59  VAL B CG1 1 
ATOM   1700 C CG2 . VAL B 1 59  ? -14.81542 -11.51400 -16.98663 1.000 71.98942  ? 59  VAL B CG2 1 
ATOM   1701 N N   . ASP B 1 60  ? -14.21138 -15.90129 -18.02978 1.000 75.77454  ? 60  ASP B N   1 
ATOM   1702 C CA  . ASP B 1 60  ? -14.34969 -17.24916 -18.54719 1.000 69.22625  ? 60  ASP B CA  1 
ATOM   1703 C C   . ASP B 1 60  ? -15.54352 -17.94688 -17.91210 1.000 72.98756  ? 60  ASP B C   1 
ATOM   1704 O O   . ASP B 1 60  ? -15.80128 -17.77674 -16.71396 1.000 80.45006  ? 60  ASP B O   1 
ATOM   1705 C CB  . ASP B 1 60  ? -13.07567 -18.06059 -18.28456 1.000 76.46193  ? 60  ASP B CB  1 
ATOM   1706 C CG  . ASP B 1 60  ? -12.85227 -19.13617 -19.31871 1.000 77.35724  ? 60  ASP B CG  1 
ATOM   1707 O OD1 . ASP B 1 60  ? -12.53956 -18.78723 -20.47330 1.000 81.14593  ? 60  ASP B OD1 1 
ATOM   1708 O OD2 . ASP B 1 60  ? -12.95609 -20.33054 -18.97316 1.000 85.63614  ? 60  ASP B OD2 1 
ATOM   1709 N N   . PRO B 1 61  ? -16.32843 -18.68705 -18.70138 1.000 70.56629  ? 61  PRO B N   1 
ATOM   1710 C CA  . PRO B 1 61  ? -16.25966 -18.83812 -20.16094 1.000 78.09426  ? 61  PRO B CA  1 
ATOM   1711 C C   . PRO B 1 61  ? -16.76769 -17.55728 -20.81088 1.000 72.01665  ? 61  PRO B C   1 
ATOM   1712 O O   . PRO B 1 61  ? -17.51185 -16.81854 -20.17139 1.000 74.09353  ? 61  PRO B O   1 
ATOM   1713 C CB  . PRO B 1 61  ? -17.15195 -20.05674 -20.42298 1.000 69.49083  ? 61  PRO B CB  1 
ATOM   1714 C CG  . PRO B 1 61  ? -18.16534 -19.99065 -19.32889 1.000 66.73112  ? 61  PRO B CG  1 
ATOM   1715 C CD  . PRO B 1 61  ? -17.39165 -19.52583 -18.12444 1.000 68.34980  ? 61  PRO B CD  1 
ATOM   1716 N N   . PRO B 1 62  ? -16.37942 -17.24420 -22.04377 1.000 72.86310  ? 62  PRO B N   1 
ATOM   1717 C CA  . PRO B 1 62  ? -16.81580 -15.98707 -22.65927 1.000 57.97330  ? 62  PRO B CA  1 
ATOM   1718 C C   . PRO B 1 62  ? -18.32623 -15.93762 -22.78318 1.000 62.00953  ? 62  PRO B C   1 
ATOM   1719 O O   . PRO B 1 62  ? -18.95095 -16.85826 -23.33085 1.000 70.36571  ? 62  PRO B O   1 
ATOM   1720 C CB  . PRO B 1 62  ? -16.14715 -16.01624 -24.04236 1.000 63.33587  ? 62  PRO B CB  1 
ATOM   1721 C CG  . PRO B 1 62  ? -15.89106 -17.47071 -24.30242 1.000 63.34392  ? 62  PRO B CG  1 
ATOM   1722 C CD  . PRO B 1 62  ? -15.55498 -18.04786 -22.96070 1.000 62.69750  ? 62  PRO B CD  1 
ATOM   1723 N N   . PRO B 1 63  ? -18.94527 -14.87497 -22.27829 1.000 71.87680  ? 63  PRO B N   1 
ATOM   1724 C CA  . PRO B 1 63  ? -20.40796 -14.77797 -22.31506 1.000 63.73026  ? 63  PRO B CA  1 
ATOM   1725 C C   . PRO B 1 63  ? -20.92486 -14.78351 -23.74357 1.000 67.92813  ? 63  PRO B C   1 
ATOM   1726 O O   . PRO B 1 63  ? -20.35001 -14.16226 -24.64063 1.000 69.05262  ? 63  PRO B O   1 
ATOM   1727 C CB  . PRO B 1 63  ? -20.69584 -13.45381 -21.60032 1.000 63.02433  ? 63  PRO B CB  1 
ATOM   1728 C CG  . PRO B 1 63  ? -19.49721 -13.23895 -20.73320 1.000 65.20855  ? 63  PRO B CG  1 
ATOM   1729 C CD  . PRO B 1 63  ? -18.33961 -13.76624 -21.52475 1.000 57.18152  ? 63  PRO B CD  1 
ATOM   1730 N N   . VAL B 1 64  ? -22.02637 -15.49875 -23.94297 1.000 70.09976  ? 64  VAL B N   1 
ATOM   1731 C CA  . VAL B 1 64  ? -22.66412 -15.63205 -25.24387 1.000 69.27161  ? 64  VAL B CA  1 
ATOM   1732 C C   . VAL B 1 64  ? -24.13890 -15.31332 -25.07374 1.000 66.66038  ? 64  VAL B C   1 
ATOM   1733 O O   . VAL B 1 64  ? -24.80883 -15.87084 -24.19794 1.000 68.89694  ? 64  VAL B O   1 
ATOM   1734 C CB  . VAL B 1 64  ? -22.48111 -17.04426 -25.83310 1.000 74.46363  ? 64  VAL B CB  1 
ATOM   1735 C CG1 . VAL B 1 64  ? -23.35149 -17.21443 -27.06166 1.000 66.72873  ? 64  VAL B CG1 1 
ATOM   1736 C CG2 . VAL B 1 64  ? -21.02036 -17.29584 -26.17043 1.000 61.29873  ? 64  VAL B CG2 1 
ATOM   1737 N N   . ILE B 1 65  ? -24.63235 -14.40687 -25.90806 1.000 64.99639  ? 65  ILE B N   1 
ATOM   1738 C CA  . ILE B 1 65  ? -26.00595 -13.93016 -25.87400 1.000 68.37546  ? 65  ILE B CA  1 
ATOM   1739 C C   . ILE B 1 65  ? -26.59318 -14.13518 -27.25733 1.000 70.14360  ? 65  ILE B C   1 
ATOM   1740 O O   . ILE B 1 65  ? -25.95840 -13.78698 -28.25978 1.000 71.58111  ? 65  ILE B O   1 
ATOM   1741 C CB  . ILE B 1 65  ? -26.09989 -12.43704 -25.48438 1.000 57.28014  ? 65  ILE B CB  1 
ATOM   1742 C CG1 . ILE B 1 65  ? -25.58291 -12.16711 -24.06401 1.000 60.88159  ? 65  ILE B CG1 1 
ATOM   1743 C CG2 . ILE B 1 65  ? -27.52801 -11.93433 -25.63175 1.000 68.23242  ? 65  ILE B CG2 1 
ATOM   1744 C CD1 . ILE B 1 65  ? -24.06708 -12.13557 -23.92282 1.000 50.91123  ? 65  ILE B CD1 1 
ATOM   1745 N N   . GLU B 1 66  ? -27.78714 -14.71564 -27.31766 1.000 63.09433  ? 66  GLU B N   1 
ATOM   1746 C CA  . GLU B 1 66  ? -28.47966 -14.89555 -28.58179 1.000 73.57301  ? 66  GLU B CA  1 
ATOM   1747 C C   . GLU B 1 66  ? -29.64293 -13.91776 -28.67835 1.000 67.94725  ? 66  GLU B C   1 
ATOM   1748 O O   . GLU B 1 66  ? -30.26211 -13.56276 -27.67007 1.000 72.17243  ? 66  GLU B O   1 
ATOM   1749 C CB  . GLU B 1 66  ? -28.98443 -16.33298 -28.78005 1.000 72.89597  ? 66  GLU B CB  1 
ATOM   1750 C CG  . GLU B 1 66  ? -30.46530 -16.55713 -28.49823 1.000 92.52151  ? 66  GLU B CG  1 
ATOM   1751 C CD  . GLU B 1 66  ? -30.93337 -17.95348 -28.89414 1.000 103.26944 ? 66  GLU B CD  1 
ATOM   1752 O OE1 . GLU B 1 66  ? -30.13499 -18.71031 -29.48743 1.000 98.71895  ? 66  GLU B OE1 1 
ATOM   1753 O OE2 . GLU B 1 66  ? -32.10070 -18.29998 -28.61237 1.000 114.45105 ? 66  GLU B OE2 1 
ATOM   1754 N N   . LEU B 1 67  ? -29.86678 -13.41432 -29.88413 1.000 68.61713  ? 67  LEU B N   1 
ATOM   1755 C CA  . LEU B 1 67  ? -30.92046 -12.45509 -30.16722 1.000 76.96402  ? 67  LEU B CA  1 
ATOM   1756 C C   . LEU B 1 67  ? -31.89633 -13.06715 -31.16029 1.000 73.20621  ? 67  LEU B C   1 
ATOM   1757 O O   . LEU B 1 67  ? -31.48534 -13.68708 -32.14544 1.000 82.01447  ? 67  LEU B O   1 
ATOM   1758 C CB  . LEU B 1 67  ? -30.34778 -11.14649 -30.72914 1.000 82.46911  ? 67  LEU B CB  1 
ATOM   1759 C CG  . LEU B 1 67  ? -31.32279 -10.13482 -31.34283 1.000 61.42401  ? 67  LEU B CG  1 
ATOM   1760 C CD1 . LEU B 1 67  ? -32.36280 -9.67041  -30.34209 1.000 60.12632  ? 67  LEU B CD1 1 
ATOM   1761 C CD2 . LEU B 1 67  ? -30.55490 -8.96246  -31.90502 1.000 75.74295  ? 67  LEU B CD2 1 
ATOM   1762 N N   . ASN B 1 68  ? -33.18722 -12.89094 -30.89977 1.000 76.60635  ? 68  ASN B N   1 
ATOM   1763 C CA  . ASN B 1 68  ? -34.22802 -13.29811 -31.83048 1.000 77.39081  ? 68  ASN B CA  1 
ATOM   1764 C C   . ASN B 1 68  ? -35.19459 -12.13927 -32.01516 1.000 85.70386  ? 68  ASN B C   1 
ATOM   1765 O O   . ASN B 1 68  ? -35.46429 -11.39044 -31.07318 1.000 89.57093  ? 68  ASN B O   1 
ATOM   1766 C CB  . ASN B 1 68  ? -34.98626 -14.53212 -31.33645 1.000 87.17715  ? 68  ASN B CB  1 
ATOM   1767 C CG  . ASN B 1 68  ? -34.16905 -15.79860 -31.44848 1.000 95.15272  ? 68  ASN B CG  1 
ATOM   1768 O OD1 . ASN B 1 68  ? -34.09316 -16.40737 -32.51521 1.000 89.07800  ? 68  ASN B OD1 1 
ATOM   1769 N ND2 . ASN B 1 68  ? -33.55688 -16.20867 -30.34326 1.000 79.83012  ? 68  ASN B ND2 1 
ATOM   1770 N N   . ILE B 1 69  ? -35.71663 -12.00013 -33.22994 1.000 90.62649  ? 69  ILE B N   1 
ATOM   1771 C CA  . ILE B 1 69  ? -36.65921 -10.94461 -33.57242 1.000 99.10781  ? 69  ILE B CA  1 
ATOM   1772 C C   . ILE B 1 69  ? -37.92887 -11.59978 -34.09125 1.000 108.67590 ? 69  ILE B C   1 
ATOM   1773 O O   . ILE B 1 69  ? -37.86897 -12.47000 -34.96791 1.000 112.93065 ? 69  ILE B O   1 
ATOM   1774 C CB  . ILE B 1 69  ? -36.08045 -9.98369  -34.62690 1.000 103.33640 ? 69  ILE B CB  1 
ATOM   1775 C CG1 . ILE B 1 69  ? -34.85990 -9.24926  -34.07801 1.000 93.51310  ? 69  ILE B CG1 1 
ATOM   1776 C CG2 . ILE B 1 69  ? -37.13111 -8.97286  -35.05870 1.000 100.00406 ? 69  ILE B CG2 1 
ATOM   1777 C CD1 . ILE B 1 69  ? -33.69966 -9.22077  -35.04609 1.000 94.65119  ? 69  ILE B CD1 1 
ATOM   1778 N N   . PHE B 1 70  ? -39.07247 -11.17193 -33.56472 1.000 110.17034 ? 70  PHE B N   1 
ATOM   1779 C CA  . PHE B 1 70  ? -40.36307 -11.77101 -33.87110 1.000 102.17940 ? 70  PHE B CA  1 
ATOM   1780 C C   . PHE B 1 70  ? -41.30120 -10.70428 -34.41842 1.000 112.72052 ? 70  PHE B C   1 
ATOM   1781 O O   . PHE B 1 70  ? -41.32784 -9.57115  -33.92704 1.000 118.12321 ? 70  PHE B O   1 
ATOM   1782 C CB  . PHE B 1 70  ? -40.98464 -12.43655 -32.62919 1.000 109.00161 ? 70  PHE B CB  1 
ATOM   1783 C CG  . PHE B 1 70  ? -40.13943 -13.53301 -32.02119 1.000 123.46201 ? 70  PHE B CG  1 
ATOM   1784 C CD1 . PHE B 1 70  ? -39.15837 -14.17617 -32.76033 1.000 122.02075 ? 70  PHE B CD1 1 
ATOM   1785 C CD2 . PHE B 1 70  ? -40.32186 -13.91027 -30.70129 1.000 136.03706 ? 70  PHE B CD2 1 
ATOM   1786 C CE1 . PHE B 1 70  ? -38.38508 -15.17896 -32.20038 1.000 116.39821 ? 70  PHE B CE1 1 
ATOM   1787 C CE2 . PHE B 1 70  ? -39.54882 -14.91172 -30.13461 1.000 136.71667 ? 70  PHE B CE2 1 
ATOM   1788 C CZ  . PHE B 1 70  ? -38.57986 -15.54575 -30.88658 1.000 115.03352 ? 70  PHE B CZ  1 
ATOM   1789 N N   . GLU B 1 71  ? -42.06926 -11.07425 -35.43733 1.000 120.88363 ? 71  GLU B N   1 
ATOM   1790 C CA  . GLU B 1 71  ? -43.04354 -10.19258 -36.06535 1.000 112.30034 ? 71  GLU B CA  1 
ATOM   1791 C C   . GLU B 1 71  ? -44.44801 -10.66808 -35.72962 1.000 125.74107 ? 71  GLU B C   1 
ATOM   1792 O O   . GLU B 1 71  ? -44.73238 -11.86894 -35.78473 1.000 136.32986 ? 71  GLU B O   1 
ATOM   1793 C CB  . GLU B 1 71  ? -42.85191 -10.14697 -37.58357 1.000 112.86441 ? 71  GLU B CB  1 
ATOM   1794 C CG  . GLU B 1 71  ? -43.85654 -9.27860  -38.32961 1.000 120.43827 ? 71  GLU B CG  1 
ATOM   1795 C CD  . GLU B 1 71  ? -44.23716 -9.85919  -39.68400 1.000 148.36146 ? 71  GLU B CD  1 
ATOM   1796 O OE1 . GLU B 1 71  ? -43.32760 -10.08317 -40.51142 1.000 148.40742 ? 71  GLU B OE1 1 
ATOM   1797 O OE2 . GLU B 1 71  ? -45.44192 -10.09838 -39.92037 1.000 153.46190 ? 71  GLU B OE2 1 
ATOM   1798 N N   . SER B 1 72  ? -45.31287 -9.72892  -35.36341 1.000 132.40267 ? 72  SER B N   1 
ATOM   1799 C CA  . SER B 1 72  ? -46.72370 -10.00471 -35.14420 1.000 144.07199 ? 72  SER B CA  1 
ATOM   1800 C C   . SER B 1 72  ? -47.53360 -8.98449  -35.92777 1.000 162.18778 ? 72  SER B C   1 
ATOM   1801 O O   . SER B 1 72  ? -47.32363 -7.77655  -35.77825 1.000 163.95518 ? 72  SER B O   1 
ATOM   1802 C CB  . SER B 1 72  ? -47.06901 -9.94180  -33.65273 1.000 141.77370 ? 72  SER B CB  1 
ATOM   1803 O OG  . SER B 1 72  ? -48.44883 -9.69879  -33.45707 1.000 158.02394 ? 72  SER B OG  1 
ATOM   1804 N N   . ASP B 1 73  ? -48.45323 -9.46752  -36.76055 1.000 215.11805 ? 73  ASP B N   1 
ATOM   1805 C CA  . ASP B 1 73  ? -49.26373 -8.56369  -37.55780 1.000 214.48083 ? 73  ASP B CA  1 
ATOM   1806 C C   . ASP B 1 73  ? -50.31333 -7.88258  -36.68019 1.000 213.49994 ? 73  ASP B C   1 
ATOM   1807 O O   . ASP B 1 73  ? -50.74818 -8.44422  -35.67222 1.000 216.44308 ? 73  ASP B O   1 
ATOM   1808 C CB  . ASP B 1 73  ? -49.94009 -9.31462  -38.70523 1.000 225.92711 ? 73  ASP B CB  1 
ATOM   1809 C CG  . ASP B 1 73  ? -50.46932 -10.67635 -38.28829 1.000 236.49353 ? 73  ASP B CG  1 
ATOM   1810 O OD1 . ASP B 1 73  ? -49.99080 -11.21797 -37.27009 1.000 234.97244 ? 73  ASP B OD1 1 
ATOM   1811 O OD2 . ASP B 1 73  ? -51.36292 -11.20738 -38.98351 1.000 234.79954 ? 73  ASP B OD2 1 
ATOM   1812 N N   . PRO B 1 74  ? -50.72856 -6.66327  -37.03556 1.000 224.25775 ? 74  PRO B N   1 
ATOM   1813 C CA  . PRO B 1 74  ? -51.79451 -6.00548  -36.25747 1.000 225.21708 ? 74  PRO B CA  1 
ATOM   1814 C C   . PRO B 1 74  ? -53.09188 -6.79307  -36.23538 1.000 221.61100 ? 74  PRO B C   1 
ATOM   1815 O O   . PRO B 1 74  ? -53.86385 -6.67919  -35.27476 1.000 219.07054 ? 74  PRO B O   1 
ATOM   1816 C CB  . PRO B 1 74  ? -51.97731 -4.64750  -36.95339 1.000 224.79863 ? 74  PRO B CB  1 
ATOM   1817 C CG  . PRO B 1 74  ? -51.11221 -4.65266  -38.15657 1.000 220.17587 ? 74  PRO B CG  1 
ATOM   1818 C CD  . PRO B 1 74  ? -50.20554 -5.83186  -38.13271 1.000 221.57140 ? 74  PRO B CD  1 
ATOM   1819 N N   . HIS B 1 75  ? -53.35426 -7.58638  -37.27605 1.000 224.36327 ? 75  HIS B N   1 
ATOM   1820 C CA  . HIS B 1 75  ? -54.56319 -8.40299  -37.31932 1.000 226.67385 ? 75  HIS B CA  1 
ATOM   1821 C C   . HIS B 1 75  ? -54.52517 -9.52278  -36.28400 1.000 225.88478 ? 75  HIS B C   1 
ATOM   1822 O O   . HIS B 1 75  ? -55.55305 -9.85179  -35.68016 1.000 222.70071 ? 75  HIS B O   1 
ATOM   1823 C CB  . HIS B 1 75  ? -54.75043 -8.96725  -38.72786 1.000 219.49687 ? 75  HIS B CB  1 
ATOM   1824 C CG  . HIS B 1 75  ? -54.51742 -7.96095  -39.81306 1.000 219.02795 ? 75  HIS B CG  1 
ATOM   1825 N ND1 . HIS B 1 75  ? -53.30232 -7.81937  -40.44849 1.000 218.34552 ? 75  HIS B ND1 1 
ATOM   1826 C CD2 . HIS B 1 75  ? -55.34028 -7.03890  -40.36690 1.000 206.27285 ? 75  HIS B CD2 1 
ATOM   1827 C CE1 . HIS B 1 75  ? -53.38808 -6.85765  -41.35025 1.000 203.26123 ? 75  HIS B CE1 1 
ATOM   1828 N NE2 . HIS B 1 75  ? -54.61418 -6.36758  -41.32076 1.000 195.40342 ? 75  HIS B NE2 1 
ATOM   1829 N N   . ASP B 1 76  ? -53.35447 -10.12142 -36.06849 1.000 228.32311 ? 76  ASP B N   1 
ATOM   1830 C CA  . ASP B 1 76  ? -53.17328 -11.20582 -35.10194 1.000 225.63406 ? 76  ASP B CA  1 
ATOM   1831 C C   . ASP B 1 76  ? -51.99753 -10.85350 -34.19401 1.000 216.66935 ? 76  ASP B C   1 
ATOM   1832 O O   . ASP B 1 76  ? -50.83677 -11.01813 -34.58068 1.000 220.68233 ? 76  ASP B O   1 
ATOM   1833 C CB  . ASP B 1 76  ? -52.94774 -12.53920 -35.81119 1.000 225.40300 ? 76  ASP B CB  1 
ATOM   1834 C CG  . ASP B 1 76  ? -52.97132 -13.72126 -34.85915 1.000 213.24375 ? 76  ASP B CG  1 
ATOM   1835 O OD1 . ASP B 1 76  ? -53.30114 -13.52885 -33.66974 1.000 207.15367 ? 76  ASP B OD1 1 
ATOM   1836 O OD2 . ASP B 1 76  ? -52.65945 -14.84625 -35.30290 1.000 216.87076 ? 76  ASP B OD2 1 
ATOM   1837 N N   . ASP B 1 77  ? -52.29548 -10.38845 -32.98270 1.000 199.14462 ? 77  ASP B N   1 
ATOM   1838 C CA  . ASP B 1 77  ? -51.26579 -9.99858  -32.02811 1.000 186.66008 ? 77  ASP B CA  1 
ATOM   1839 C C   . ASP B 1 77  ? -50.87639 -11.12202 -31.07491 1.000 182.54807 ? 77  ASP B C   1 
ATOM   1840 O O   . ASP B 1 77  ? -50.07186 -10.89064 -30.16633 1.000 176.22830 ? 77  ASP B O   1 
ATOM   1841 C CB  . ASP B 1 77  ? -51.72519 -8.77898  -31.21777 1.000 173.85669 ? 77  ASP B CB  1 
ATOM   1842 C CG  . ASP B 1 77  ? -51.56845 -7.47420  -31.97849 1.000 160.40420 ? 77  ASP B CG  1 
ATOM   1843 O OD1 . ASP B 1 77  ? -51.06933 -7.49996  -33.12133 1.000 165.82758 ? 77  ASP B OD1 1 
ATOM   1844 O OD2 . ASP B 1 77  ? -51.94170 -6.41811  -31.42778 1.000 152.83694 ? 77  ASP B OD2 1 
ATOM   1845 N N   . SER B 1 78  ? -51.42174 -12.32541 -31.25260 1.000 199.21265 ? 78  SER B N   1 
ATOM   1846 C CA  . SER B 1 78  ? -51.14173 -13.43650 -30.35360 1.000 209.26108 ? 78  SER B CA  1 
ATOM   1847 C C   . SER B 1 78  ? -50.10753 -14.41498 -30.90102 1.000 211.20616 ? 78  SER B C   1 
ATOM   1848 O O   . SER B 1 78  ? -49.65672 -15.29238 -30.15687 1.000 208.88435 ? 78  SER B O   1 
ATOM   1849 C CB  . SER B 1 78  ? -52.43783 -14.19563 -30.03777 1.000 208.78638 ? 78  SER B CB  1 
ATOM   1850 O OG  . SER B 1 78  ? -53.24797 -13.47004 -29.12876 1.000 203.49488 ? 78  SER B OG  1 
ATOM   1851 N N   . ASN B 1 79  ? -49.72347 -14.29238 -32.16941 1.000 213.74638 ? 79  ASN B N   1 
ATOM   1852 C CA  . ASN B 1 79  ? -48.76661 -15.19202 -32.79711 1.000 197.59505 ? 79  ASN B CA  1 
ATOM   1853 C C   . ASN B 1 79  ? -47.53302 -14.42514 -33.25515 1.000 180.92831 ? 79  ASN B C   1 
ATOM   1854 O O   . ASN B 1 79  ? -47.60916 -13.24094 -33.59516 1.000 201.36207 ? 79  ASN B O   1 
ATOM   1855 C CB  . ASN B 1 79  ? -49.39004 -15.92127 -33.99227 1.000 206.77092 ? 79  ASN B CB  1 
ATOM   1856 C CG  . ASN B 1 79  ? -50.43251 -16.93939 -33.57644 1.000 204.13830 ? 79  ASN B CG  1 
ATOM   1857 O OD1 . ASN B 1 79  ? -50.69528 -17.13223 -32.38882 1.000 205.33227 ? 79  ASN B OD1 1 
ATOM   1858 N ND2 . ASN B 1 79  ? -51.03664 -17.59605 -34.55845 1.000 199.02147 ? 79  ASN B ND2 1 
ATOM   1859 N N   . LYS B 1 80  ? -46.39123 -15.11152 -33.25972 1.000 163.15985 ? 80  LYS B N   1 
ATOM   1860 C CA  . LYS B 1 80  ? -45.10442 -14.49228 -33.54146 1.000 152.30979 ? 80  LYS B CA  1 
ATOM   1861 C C   . LYS B 1 80  ? -44.42912 -15.24921 -34.67483 1.000 128.40790 ? 80  LYS B C   1 
ATOM   1862 O O   . LYS B 1 80  ? -44.68466 -16.43703 -34.88662 1.000 136.28400 ? 80  LYS B O   1 
ATOM   1863 C CB  . LYS B 1 80  ? -44.18946 -14.47390 -32.30626 1.000 147.63021 ? 80  LYS B CB  1 
ATOM   1864 C CG  . LYS B 1 80  ? -44.87031 -14.00689 -31.03267 1.000 152.62238 ? 80  LYS B CG  1 
ATOM   1865 C CD  . LYS B 1 80  ? -44.42827 -14.83385 -29.83844 1.000 156.97453 ? 80  LYS B CD  1 
ATOM   1866 C CE  . LYS B 1 80  ? -45.50503 -14.86515 -28.76628 1.000 168.00436 ? 80  LYS B CE  1 
ATOM   1867 N NZ  . LYS B 1 80  ? -45.36418 -16.05089 -27.87796 1.000 163.68098 ? 80  LYS B NZ  1 
ATOM   1868 N N   . THR B 1 81  ? -43.55467 -14.55296 -35.39742 1.000 125.76948 ? 81  THR B N   1 
ATOM   1869 C CA  . THR B 1 81  ? -42.84236 -15.14018 -36.52665 1.000 112.07609 ? 81  THR B CA  1 
ATOM   1870 C C   . THR B 1 81  ? -41.39771 -14.66896 -36.51046 1.000 119.46632 ? 81  THR B C   1 
ATOM   1871 O O   . THR B 1 81  ? -41.13912 -13.46303 -36.55903 1.000 120.26859 ? 81  THR B O   1 
ATOM   1872 C CB  . THR B 1 81  ? -43.50253 -14.76717 -37.85590 1.000 129.25334 ? 81  THR B CB  1 
ATOM   1873 O OG1 . THR B 1 81  ? -44.92538 -14.91504 -37.74798 1.000 132.89598 ? 81  THR B OG1 1 
ATOM   1874 C CG2 . THR B 1 81  ? -42.98034 -15.66524 -38.96747 1.000 126.76186 ? 81  THR B CG2 1 
ATOM   1875 N N   . ASP B 1 82  ? -40.46292 -15.61352 -36.43641 1.000 117.39507 ? 82  ASP B N   1 
ATOM   1876 C CA  . ASP B 1 82  ? -39.05118 -15.26461 -36.34918 1.000 110.17104 ? 82  ASP B CA  1 
ATOM   1877 C C   . ASP B 1 82  ? -38.59135 -14.64901 -37.66498 1.000 121.61612 ? 82  ASP B C   1 
ATOM   1878 O O   . ASP B 1 82  ? -38.77138 -15.23752 -38.73564 1.000 119.09714 ? 82  ASP B O   1 
ATOM   1879 C CB  . ASP B 1 82  ? -38.21735 -16.49857 -36.01111 1.000 92.01934  ? 82  ASP B CB  1 
ATOM   1880 C CG  . ASP B 1 82  ? -36.86592 -16.14762 -35.41978 1.000 109.19145 ? 82  ASP B CG  1 
ATOM   1881 O OD1 . ASP B 1 82  ? -36.13778 -15.33742 -36.03016 1.000 117.18843 ? 82  ASP B OD1 1 
ATOM   1882 O OD2 . ASP B 1 82  ? -36.53293 -16.67662 -34.33847 1.000 108.12837 ? 82  ASP B OD2 1 
ATOM   1883 N N   . ILE B 1 83  ? -37.98749 -13.46359 -37.58179 1.000 114.39609 ? 83  ILE B N   1 
ATOM   1884 C CA  . ILE B 1 83  ? -37.48945 -12.77069 -38.76478 1.000 119.94124 ? 83  ILE B CA  1 
ATOM   1885 C C   . ILE B 1 83  ? -36.02163 -12.41252 -38.58810 1.000 121.57721 ? 83  ILE B C   1 
ATOM   1886 O O   . ILE B 1 83  ? -35.54093 -11.44243 -39.18414 1.000 129.44468 ? 83  ILE B O   1 
ATOM   1887 C CB  . ILE B 1 83  ? -38.30246 -11.49661 -39.05386 1.000 123.85752 ? 83  ILE B CB  1 
ATOM   1888 C CG1 . ILE B 1 83  ? -38.72637 -10.83169 -37.74427 1.000 114.35082 ? 83  ILE B CG1 1 
ATOM   1889 C CG2 . ILE B 1 83  ? -39.52036 -11.82728 -39.89879 1.000 128.85360 ? 83  ILE B CG2 1 
ATOM   1890 C CD1 . ILE B 1 83  ? -39.46813 -9.53732  -37.93522 1.000 125.19460 ? 83  ILE B CD1 1 
ATOM   1891 N N   . THR B 1 84  ? -35.30345 -13.17732 -37.76132 1.000 118.55360 ? 84  THR B N   1 
ATOM   1892 C CA  . THR B 1 84  ? -33.96640 -12.75904 -37.35108 1.000 114.34240 ? 84  THR B CA  1 
ATOM   1893 C C   . THR B 1 84  ? -33.04438 -12.60785 -38.55568 1.000 118.68763 ? 84  THR B C   1 
ATOM   1894 O O   . THR B 1 84  ? -32.25356 -11.65998 -38.62712 1.000 124.71580 ? 84  THR B O   1 
ATOM   1895 C CB  . THR B 1 84  ? -33.38675 -13.76000 -36.35197 1.000 110.12449 ? 84  THR B CB  1 
ATOM   1896 O OG1 . THR B 1 84  ? -34.22289 -13.80825 -35.18983 1.000 107.27563 ? 84  THR B OG1 1 
ATOM   1897 C CG2 . THR B 1 84  ? -31.98512 -13.34136 -35.92852 1.000 103.74556 ? 84  THR B CG2 1 
ATOM   1898 N N   . PHE B 1 85  ? -33.13402 -13.52623 -39.51587 1.000 119.70587 ? 85  PHE B N   1 
ATOM   1899 C CA  . PHE B 1 85  ? -32.32661 -13.42400 -40.72368 1.000 114.00363 ? 85  PHE B CA  1 
ATOM   1900 C C   . PHE B 1 85  ? -32.91956 -12.47527 -41.75746 1.000 126.80424 ? 85  PHE B C   1 
ATOM   1901 O O   . PHE B 1 85  ? -32.21453 -12.09873 -42.69996 1.000 130.09025 ? 85  PHE B O   1 
ATOM   1902 C CB  . PHE B 1 85  ? -32.13113 -14.80826 -41.34829 1.000 115.93754 ? 85  PHE B CB  1 
ATOM   1903 C CG  . PHE B 1 85  ? -31.18956 -15.69655 -40.58255 1.000 133.28918 ? 85  PHE B CG  1 
ATOM   1904 C CD1 . PHE B 1 85  ? -31.45406 -16.05400 -39.27069 1.000 131.86867 ? 85  PHE B CD1 1 
ATOM   1905 C CD2 . PHE B 1 85  ? -30.04691 -16.19419 -41.18880 1.000 130.17638 ? 85  PHE B CD2 1 
ATOM   1906 C CE1 . PHE B 1 85  ? -30.58732 -16.87011 -38.57167 1.000 124.33296 ? 85  PHE B CE1 1 
ATOM   1907 C CE2 . PHE B 1 85  ? -29.17938 -17.01595 -40.49707 1.000 116.73407 ? 85  PHE B CE2 1 
ATOM   1908 C CZ  . PHE B 1 85  ? -29.45027 -17.35467 -39.18708 1.000 121.68718 ? 85  PHE B CZ  1 
ATOM   1909 N N   . VAL B 1 86  ? -34.18687 -12.09248 -41.61458 1.000 139.28884 ? 86  VAL B N   1 
ATOM   1910 C CA  . VAL B 1 86  ? -34.84352 -11.23037 -42.59589 1.000 135.23406 ? 86  VAL B CA  1 
ATOM   1911 C C   . VAL B 1 86  ? -34.70613 -9.75570  -42.22980 1.000 131.73260 ? 86  VAL B C   1 
ATOM   1912 O O   . VAL B 1 86  ? -34.57553 -8.90203  -43.11072 1.000 128.42939 ? 86  VAL B O   1 
ATOM   1913 C CB  . VAL B 1 86  ? -36.32284 -11.63860 -42.74374 1.000 132.67769 ? 86  VAL B CB  1 
ATOM   1914 C CG1 . VAL B 1 86  ? -36.87436 -11.16120 -44.07860 1.000 147.95494 ? 86  VAL B CG1 1 
ATOM   1915 C CG2 . VAL B 1 86  ? -36.47512 -13.14623 -42.60379 1.000 140.71947 ? 86  VAL B CG2 1 
ATOM   1916 N N   . TYR B 1 87  ? -34.75413 -9.44437  -40.93542 1.000 130.50237 ? 87  TYR B N   1 
ATOM   1917 C CA  . TYR B 1 87  ? -34.66863 -8.06841  -40.45858 1.000 104.68772 ? 87  TYR B CA  1 
ATOM   1918 C C   . TYR B 1 87  ? -33.34535 -7.43375  -40.87413 1.000 121.77646 ? 87  TYR B C   1 
ATOM   1919 O O   . TYR B 1 87  ? -32.27259 -7.87972  -40.45534 1.000 132.42149 ? 87  TYR B O   1 
ATOM   1920 C CB  . TYR B 1 87  ? -34.83123 -8.05419  -38.94143 1.000 106.91116 ? 87  TYR B CB  1 
ATOM   1921 C CG  . TYR B 1 87  ? -35.14401 -6.70304  -38.35562 1.000 111.16307 ? 87  TYR B CG  1 
ATOM   1922 C CD1 . TYR B 1 87  ? -36.45819 -6.27624  -38.21836 1.000 114.58481 ? 87  TYR B CD1 1 
ATOM   1923 C CD2 . TYR B 1 87  ? -34.13190 -5.86838  -37.90722 1.000 109.53574 ? 87  TYR B CD2 1 
ATOM   1924 C CE1 . TYR B 1 87  ? -36.75542 -5.04665  -37.67449 1.000 106.65291 ? 87  TYR B CE1 1 
ATOM   1925 C CE2 . TYR B 1 87  ? -34.41896 -4.63653  -37.35978 1.000 109.61686 ? 87  TYR B CE2 1 
ATOM   1926 C CZ  . TYR B 1 87  ? -35.73264 -4.23030  -37.24391 1.000 114.04491 ? 87  TYR B CZ  1 
ATOM   1927 O OH  . TYR B 1 87  ? -36.02270 -3.00087  -36.69882 1.000 100.16031 ? 87  TYR B OH  1 
ATOM   1928 N N   . ASN B 1 88  ? -33.42309 -6.38200  -41.68889 1.000 138.13804 ? 88  ASN B N   1 
ATOM   1929 C CA  . ASN B 1 88  ? -32.24179 -5.76471  -42.29379 1.000 144.48400 ? 88  ASN B CA  1 
ATOM   1930 C C   . ASN B 1 88  ? -31.80583 -4.57631  -41.43817 1.000 145.30204 ? 88  ASN B C   1 
ATOM   1931 O O   . ASN B 1 88  ? -32.25966 -3.44542  -41.62572 1.000 148.06887 ? 88  ASN B O   1 
ATOM   1932 C CB  . ASN B 1 88  ? -32.53948 -5.36192  -43.73865 1.000 154.80538 ? 88  ASN B CB  1 
ATOM   1933 C CG  . ASN B 1 88  ? -31.64899 -4.23394  -44.23978 1.000 169.38552 ? 88  ASN B CG  1 
ATOM   1934 O OD1 . ASN B 1 88  ? -32.09072 -3.09226  -44.38005 1.000 184.31198 ? 88  ASN B OD1 1 
ATOM   1935 N ND2 . ASN B 1 88  ? -30.38941 -4.55214  -44.51374 1.000 170.80449 ? 88  ASN B ND2 1 
ATOM   1936 N N   . ALA B 1 89  ? -30.95616 -4.85247  -40.44953 1.000 129.56109 ? 89  ALA B N   1 
ATOM   1937 C CA  . ALA B 1 89  ? -30.38842 -3.79715  -39.62253 1.000 124.05409 ? 89  ALA B CA  1 
ATOM   1938 C C   . ALA B 1 89  ? -29.14378 -4.32298  -38.92451 1.000 105.21004 ? 89  ALA B C   1 
ATOM   1939 O O   . ALA B 1 89  ? -29.01661 -5.52582  -38.67958 1.000 107.80257 ? 89  ALA B O   1 
ATOM   1940 C CB  . ALA B 1 89  ? -31.39536 -3.28399  -38.58647 1.000 121.13618 ? 89  ALA B CB  1 
ATOM   1941 N N   . ASN B 1 90  ? -28.23129 -3.40892  -38.60366 1.000 99.96306  ? 90  ASN B N   1 
ATOM   1942 C CA  . ASN B 1 90  ? -27.04374 -3.77051  -37.84540 1.000 98.56562  ? 90  ASN B CA  1 
ATOM   1943 C C   . ASN B 1 90  ? -27.37537 -3.81907  -36.36153 1.000 88.74833  ? 90  ASN B C   1 
ATOM   1944 O O   . ASN B 1 90  ? -28.24004 -3.08725  -35.87182 1.000 90.11347  ? 90  ASN B O   1 
ATOM   1945 C CB  . ASN B 1 90  ? -25.90129 -2.78184  -38.09097 1.000 104.54902 ? 90  ASN B CB  1 
ATOM   1946 C CG  . ASN B 1 90  ? -25.43229 -2.77254  -39.53138 1.000 130.88730 ? 90  ASN B CG  1 
ATOM   1947 O OD1 . ASN B 1 90  ? -25.72816 -3.68905  -40.29631 1.000 141.77172 ? 90  ASN B OD1 1 
ATOM   1948 N ND2 . ASN B 1 90  ? -24.70227 -1.72896  -39.91126 1.000 136.42395 ? 90  ASN B ND2 1 
ATOM   1949 N N   . PHE B 1 91  ? -26.68448 -4.69624  -35.64506 1.000 86.08431  ? 91  PHE B N   1 
ATOM   1950 C CA  . PHE B 1 91  ? -26.90746 -4.85688  -34.21911 1.000 78.40466  ? 91  PHE B CA  1 
ATOM   1951 C C   . PHE B 1 91  ? -25.57334 -4.84761  -33.49702 1.000 62.14670  ? 91  PHE B C   1 
ATOM   1952 O O   . PHE B 1 91  ? -24.57722 -5.36898  -34.00558 1.000 79.15546  ? 91  PHE B O   1 
ATOM   1953 C CB  . PHE B 1 91  ? -27.65816 -6.15493  -33.89823 1.000 75.71456  ? 91  PHE B CB  1 
ATOM   1954 C CG  . PHE B 1 91  ? -29.13251 -6.08594  -34.17334 1.000 86.12998  ? 91  PHE B CG  1 
ATOM   1955 C CD1 . PHE B 1 91  ? -29.97179 -5.35061  -33.35284 1.000 81.61119  ? 91  PHE B CD1 1 
ATOM   1956 C CD2 . PHE B 1 91  ? -29.68292 -6.77642  -35.24109 1.000 86.79754  ? 91  PHE B CD2 1 
ATOM   1957 C CE1 . PHE B 1 91  ? -31.33169 -5.28733  -33.60355 1.000 82.79965  ? 91  PHE B CE1 1 
ATOM   1958 C CE2 . PHE B 1 91  ? -31.04095 -6.72183  -35.49414 1.000 86.13611  ? 91  PHE B CE2 1 
ATOM   1959 C CZ  . PHE B 1 91  ? -31.86633 -5.97702  -34.67405 1.000 89.92151  ? 91  PHE B CZ  1 
ATOM   1960 N N   . PHE B 1 92  ? -25.55175 -4.23062  -32.32597 1.000 67.17950  ? 92  PHE B N   1 
ATOM   1961 C CA  . PHE B 1 92  ? -24.37829 -4.24649  -31.47405 1.000 60.24685  ? 92  PHE B CA  1 
ATOM   1962 C C   . PHE B 1 92  ? -24.83176 -4.55977  -30.05652 1.000 65.89650  ? 92  PHE B C   1 
ATOM   1963 O O   . PHE B 1 92  ? -25.93148 -4.18326  -29.64363 1.000 69.27763  ? 92  PHE B O   1 
ATOM   1964 C CB  . PHE B 1 92  ? -23.62206 -2.91107  -31.53636 1.000 71.35992  ? 92  PHE B CB  1 
ATOM   1965 C CG  . PHE B 1 92  ? -23.22849 -2.50436  -32.93218 1.000 71.18165  ? 92  PHE B CG  1 
ATOM   1966 C CD1 . PHE B 1 92  ? -22.05507 -2.97260  -33.50498 1.000 69.25119  ? 92  PHE B CD1 1 
ATOM   1967 C CD2 . PHE B 1 92  ? -24.03118 -1.64962  -33.66943 1.000 77.99994  ? 92  PHE B CD2 1 
ATOM   1968 C CE1 . PHE B 1 92  ? -21.69515 -2.60014  -34.79212 1.000 77.04949  ? 92  PHE B CE1 1 
ATOM   1969 C CE2 . PHE B 1 92  ? -23.67450 -1.27039  -34.95333 1.000 86.19735  ? 92  PHE B CE2 1 
ATOM   1970 C CZ  . PHE B 1 92  ? -22.50562 -1.74669  -35.51472 1.000 85.91184  ? 92  PHE B CZ  1 
ATOM   1971 N N   . LEU B 1 93  ? -23.97394 -5.23312  -29.30176 1.000 57.20100  ? 93  LEU B N   1 
ATOM   1972 C CA  . LEU B 1 93  ? -24.25844 -5.53250  -27.90857 1.000 61.31958  ? 93  LEU B CA  1 
ATOM   1973 C C   . LEU B 1 93  ? -23.13103 -4.98145  -27.05763 1.000 61.95528  ? 93  LEU B C   1 
ATOM   1974 O O   . LEU B 1 93  ? -21.95735 -5.29535  -27.29049 1.000 67.02315  ? 93  LEU B O   1 
ATOM   1975 C CB  . LEU B 1 93  ? -24.43318 -7.03954  -27.68509 1.000 64.70585  ? 93  LEU B CB  1 
ATOM   1976 C CG  . LEU B 1 93  ? -25.23106 -7.42446  -26.43668 1.000 59.86122  ? 93  LEU B CG  1 
ATOM   1977 C CD1 . LEU B 1 93  ? -26.67241 -6.93604  -26.53302 1.000 64.34752  ? 93  LEU B CD1 1 
ATOM   1978 C CD2 . LEU B 1 93  ? -25.19742 -8.92495  -26.23382 1.000 63.74841  ? 93  LEU B CD2 1 
ATOM   1979 N N   . PHE B 1 94  ? -23.49549 -4.18125  -26.06339 1.000 50.71001  ? 94  PHE B N   1 
ATOM   1980 C CA  . PHE B 1 94  ? -22.54250 -3.45910  -25.23746 1.000 61.47857  ? 94  PHE B CA  1 
ATOM   1981 C C   . PHE B 1 94  ? -22.59334 -3.99243  -23.81776 1.000 63.66069  ? 94  PHE B C   1 
ATOM   1982 O O   . PHE B 1 94  ? -23.67631 -4.10739  -23.23267 1.000 67.74605  ? 94  PHE B O   1 
ATOM   1983 C CB  . PHE B 1 94  ? -22.84906 -1.95742  -25.26970 1.000 63.11995  ? 94  PHE B CB  1 
ATOM   1984 C CG  . PHE B 1 94  ? -21.93978 -1.12211  -24.41376 1.000 61.04334  ? 94  PHE B CG  1 
ATOM   1985 C CD1 . PHE B 1 94  ? -20.56466 -1.18346  -24.56766 1.000 53.52967  ? 94  PHE B CD1 1 
ATOM   1986 C CD2 . PHE B 1 94  ? -22.47034 -0.23405  -23.48643 1.000 62.32628  ? 94  PHE B CD2 1 
ATOM   1987 C CE1 . PHE B 1 94  ? -19.73034 -0.40174  -23.79182 1.000 57.97038  ? 94  PHE B CE1 1 
ATOM   1988 C CE2 . PHE B 1 94  ? -21.64213 0.56569   -22.71366 1.000 66.07427  ? 94  PHE B CE2 1 
ATOM   1989 C CZ  . PHE B 1 94  ? -20.27010 0.47828   -22.86359 1.000 74.66436  ? 94  PHE B CZ  1 
ATOM   1990 N N   . ALA B 1 95  ? -21.42184 -4.27972  -23.25925 1.000 57.10661  ? 95  ALA B N   1 
ATOM   1991 C CA  . ALA B 1 95  ? -21.30356 -4.87581  -21.93743 1.000 48.87821  ? 95  ALA B CA  1 
ATOM   1992 C C   . ALA B 1 95  ? -20.90223 -3.79907  -20.93772 1.000 64.44741  ? 95  ALA B C   1 
ATOM   1993 O O   . ALA B 1 95  ? -19.97049 -3.02723  -21.18636 1.000 70.53407  ? 95  ALA B O   1 
ATOM   1994 C CB  . ALA B 1 95  ? -20.28347 -6.01255  -21.93943 1.000 56.56426  ? 95  ALA B CB  1 
ATOM   1995 N N   . THR B 1 96  ? -21.60828 -3.75437  -19.81285 1.000 59.43806  ? 96  THR B N   1 
ATOM   1996 C CA  . THR B 1 96  ? -21.26562 -2.90075  -18.68791 1.000 58.29284  ? 96  THR B CA  1 
ATOM   1997 C C   . THR B 1 96  ? -21.15578 -3.76297  -17.44138 1.000 69.36361  ? 96  THR B C   1 
ATOM   1998 O O   . THR B 1 96  ? -21.79830 -4.80991  -17.33152 1.000 59.21673  ? 96  THR B O   1 
ATOM   1999 C CB  . THR B 1 96  ? -22.30420 -1.76442  -18.45676 1.000 56.34383  ? 96  THR B CB  1 
ATOM   2000 O OG1 . THR B 1 96  ? -23.63083 -2.30427  -18.37524 1.000 65.86438  ? 96  THR B OG1 1 
ATOM   2001 C CG2 . THR B 1 96  ? -22.24423 -0.72742  -19.56027 1.000 58.47249  ? 96  THR B CG2 1 
ATOM   2002 N N   . LEU B 1 97  ? -20.30735 -3.33110  -16.51637 1.000 70.05992  ? 97  LEU B N   1 
ATOM   2003 C CA  . LEU B 1 97  ? -20.01051 -4.10081  -15.31966 1.000 68.85136  ? 97  LEU B CA  1 
ATOM   2004 C C   . LEU B 1 97  ? -20.79461 -3.51441  -14.15736 1.000 78.74005  ? 97  LEU B C   1 
ATOM   2005 O O   . LEU B 1 97  ? -20.65938 -2.32441  -13.85344 1.000 85.69630  ? 97  LEU B O   1 
ATOM   2006 C CB  . LEU B 1 97  ? -18.51437 -4.05311  -15.01294 1.000 59.35309  ? 97  LEU B CB  1 
ATOM   2007 C CG  . LEU B 1 97  ? -18.01361 -5.03031  -13.95325 1.000 72.70320  ? 97  LEU B CG  1 
ATOM   2008 C CD1 . LEU B 1 97  ? -18.25450 -6.48136  -14.39542 1.000 58.34978  ? 97  LEU B CD1 1 
ATOM   2009 C CD2 . LEU B 1 97  ? -16.55243 -4.76018  -13.64327 1.000 63.86655  ? 97  LEU B CD2 1 
ATOM   2010 N N   . GLU B 1 98  ? -21.58865 -4.34934  -13.49033 1.000 81.83455  ? 98  GLU B N   1 
ATOM   2011 C CA  . GLU B 1 98  ? -22.39372 -3.85873  -12.38437 1.000 85.48600  ? 98  GLU B CA  1 
ATOM   2012 C C   . GLU B 1 98  ? -21.91206 -4.49079  -11.09106 1.000 80.20808  ? 98  GLU B C   1 
ATOM   2013 O O   . GLU B 1 98  ? -21.94750 -5.72209  -10.95652 1.000 78.52050  ? 98  GLU B O   1 
ATOM   2014 C CB  . GLU B 1 98  ? -23.87760 -4.16075  -12.60809 1.000 73.71941  ? 98  GLU B CB  1 
ATOM   2015 C CG  . GLU B 1 98  ? -24.42660 -3.70317  -13.96002 1.000 71.66024  ? 98  GLU B CG  1 
ATOM   2016 C CD  . GLU B 1 98  ? -24.27007 -2.20122  -14.19330 1.000 114.45879 ? 98  GLU B CD  1 
ATOM   2017 O OE1 . GLU B 1 98  ? -24.73727 -1.39987  -13.35178 1.000 116.24132 ? 98  GLU B OE1 1 
ATOM   2018 O OE2 . GLU B 1 98  ? -23.67656 -1.82197  -15.22754 1.000 106.67564 ? 98  GLU B OE2 1 
ATOM   2019 N N   . PRO B 1 99  ? -21.43316 -3.70338  -10.13486 1.000 88.93810  ? 99  PRO B N   1 
ATOM   2020 C CA  . PRO B 1 99  ? -21.04528 -4.26981  -8.83787  1.000 89.07828  ? 99  PRO B CA  1 
ATOM   2021 C C   . PRO B 1 99  ? -22.23944 -4.86913  -8.11194  1.000 109.40792 ? 99  PRO B C   1 
ATOM   2022 O O   . PRO B 1 99  ? -23.27146 -4.21675  -7.93078  1.000 117.12170 ? 99  PRO B O   1 
ATOM   2023 C CB  . PRO B 1 99  ? -20.46265 -3.06388  -8.09935  1.000 93.72441  ? 99  PRO B CB  1 
ATOM   2024 C CG  . PRO B 1 99  ? -19.98569 -2.18195  -9.22391  1.000 90.50784  ? 99  PRO B CG  1 
ATOM   2025 C CD  . PRO B 1 99  ? -21.07639 -2.27676  -10.22977 1.000 93.90230  ? 99  PRO B CD  1 
ATOM   2026 N N   . GLU B 1 100 ? -22.09432 -6.12582  -7.69145  1.000 104.75806 ? 100 GLU B N   1 
ATOM   2027 C CA  . GLU B 1 100 ? -23.19580 -6.78015  -6.99964  1.000 108.85600 ? 100 GLU B CA  1 
ATOM   2028 C C   . GLU B 1 100 ? -23.40840 -6.19200  -5.60968  1.000 128.95516 ? 100 GLU B C   1 
ATOM   2029 O O   . GLU B 1 100 ? -24.48699 -6.36069  -5.02987  1.000 136.25694 ? 100 GLU B O   1 
ATOM   2030 C CB  . GLU B 1 100 ? -22.93150 -8.28695  -6.93560  1.000 105.74048 ? 100 GLU B CB  1 
ATOM   2031 C CG  . GLU B 1 100 ? -23.77349 -9.05321  -5.93553  1.000 124.32914 ? 100 GLU B CG  1 
ATOM   2032 C CD  . GLU B 1 100 ? -24.45018 -10.24610 -6.55864  1.000 118.14339 ? 100 GLU B CD  1 
ATOM   2033 O OE1 . GLU B 1 100 ? -25.17502 -10.05199 -7.55892  1.000 118.17446 ? 100 GLU B OE1 1 
ATOM   2034 O OE2 . GLU B 1 100 ? -24.25206 -11.37351 -6.05605  1.000 119.10695 ? 100 GLU B OE2 1 
ATOM   2035 N N   . ARG B 1 101 ? -22.42888 -5.44643  -5.09916  1.000 147.24968 ? 101 ARG B N   1 
ATOM   2036 C CA  . ARG B 1 101 ? -22.48172 -4.82442  -3.77457  1.000 163.31438 ? 101 ARG B CA  1 
ATOM   2037 C C   . ARG B 1 101 ? -22.15385 -3.34022  -3.90081  1.000 163.70141 ? 101 ARG B C   1 
ATOM   2038 O O   . ARG B 1 101 ? -21.07888 -2.88981  -3.48481  1.000 160.90719 ? 101 ARG B O   1 
ATOM   2039 C CB  . ARG B 1 101 ? -21.52412 -5.51865  -2.80473  1.000 173.73467 ? 101 ARG B CB  1 
ATOM   2040 C CG  . ARG B 1 101 ? -21.88983 -6.95948  -2.47595  1.000 176.35502 ? 101 ARG B CG  1 
ATOM   2041 C CD  . ARG B 1 101 ? -22.83886 -7.01595  -1.28707  1.000 189.94888 ? 101 ARG B CD  1 
ATOM   2042 N NE  . ARG B 1 101 ? -22.22358 -6.47950  -0.07825  1.000 195.80521 ? 101 ARG B NE  1 
ATOM   2043 C CZ  . ARG B 1 101 ? -22.00228 -7.17970  1.02601   1.000 192.37054 ? 101 ARG B CZ  1 
ATOM   2044 N NH1 . ARG B 1 101 ? -22.33460 -8.45679  1.11257   1.000 177.53062 ? 101 ARG B NH1 1 
ATOM   2045 N NH2 . ARG B 1 101 ? -21.43275 -6.58310  2.06976   1.000 196.10634 ? 101 ARG B NH2 1 
ATOM   2046 N N   . PRO B 1 102 ? -23.06311 -2.54403  -4.48185  1.000 150.12704 ? 102 PRO B N   1 
ATOM   2047 C CA  . PRO B 1 102 ? -22.77806 -1.12031  -4.68129  1.000 135.75385 ? 102 PRO B CA  1 
ATOM   2048 C C   . PRO B 1 102 ? -23.26944 -0.25058  -3.53114  1.000 131.40280 ? 102 PRO B C   1 
ATOM   2049 O O   . PRO B 1 102 ? -24.34331 0.33752   -3.64980  1.000 144.60572 ? 102 PRO B O   1 
ATOM   2050 C CB  . PRO B 1 102 ? -23.54295 -0.80040  -5.96432  1.000 137.57472 ? 102 PRO B CB  1 
ATOM   2051 C CG  . PRO B 1 102 ? -24.71053 -1.79554  -5.97025  1.000 142.57388 ? 102 PRO B CG  1 
ATOM   2052 C CD  . PRO B 1 102 ? -24.39394 -2.91082  -4.99720  1.000 142.33722 ? 102 PRO B CD  1 
ATOM   2053 N N   . SER B 1 114 ? -8.95557  5.58927   -15.13693 1.000 94.01124  ? 114 SER B N   1 
ATOM   2054 C CA  . SER B 1 114 ? -8.69193  4.15611   -15.01966 1.000 128.69658 ? 114 SER B CA  1 
ATOM   2055 C C   . SER B 1 114 ? -9.97622  3.34569   -14.83001 1.000 121.95434 ? 114 SER B C   1 
ATOM   2056 O O   . SER B 1 114 ? -10.58656 3.36132   -13.75831 1.000 117.34050 ? 114 SER B O   1 
ATOM   2057 C CB  . SER B 1 114 ? -7.72006  3.88778   -13.86951 1.000 121.39257 ? 114 SER B CB  1 
ATOM   2058 O OG  . SER B 1 114 ? -8.27978  4.26828   -12.62599 1.000 133.36047 ? 114 SER B OG  1 
ATOM   2059 N N   . PRO B 1 115 ? -10.37512 2.62550   -15.87198 1.000 118.96322 ? 115 PRO B N   1 
ATOM   2060 C CA  . PRO B 1 115 ? -11.63778 1.88075   -15.82956 1.000 120.16184 ? 115 PRO B CA  1 
ATOM   2061 C C   . PRO B 1 115 ? -11.50861 0.54260   -15.11331 1.000 99.15412  ? 115 PRO B C   1 
ATOM   2062 O O   . PRO B 1 115 ? -10.42827 -0.03805  -14.98961 1.000 100.38523 ? 115 PRO B O   1 
ATOM   2063 C CB  . PRO B 1 115 ? -11.95842 1.69594   -17.31307 1.000 107.09744 ? 115 PRO B CB  1 
ATOM   2064 C CG  . PRO B 1 115 ? -10.60130 1.55980   -17.94596 1.000 118.26600 ? 115 PRO B CG  1 
ATOM   2065 C CD  . PRO B 1 115 ? -9.67391  2.46194   -17.16310 1.000 112.69561 ? 115 PRO B CD  1 
ATOM   2066 N N   . VAL B 1 116 ? -12.65291 0.05287   -14.64496 1.000 90.26523  ? 116 VAL B N   1 
ATOM   2067 C CA  . VAL B 1 116 ? -12.68408 -1.24483  -13.98116 1.000 90.34450  ? 116 VAL B CA  1 
ATOM   2068 C C   . VAL B 1 116 ? -12.84729 -2.36398  -14.99564 1.000 82.92790  ? 116 VAL B C   1 
ATOM   2069 O O   . VAL B 1 116 ? -12.20896 -3.41210  -14.87698 1.000 79.70496  ? 116 VAL B O   1 
ATOM   2070 C CB  . VAL B 1 116 ? -13.80450 -1.27672  -12.92689 1.000 75.72707  ? 116 VAL B CB  1 
ATOM   2071 C CG1 . VAL B 1 116 ? -13.75349 -2.58811  -12.14829 1.000 90.28691  ? 116 VAL B CG1 1 
ATOM   2072 C CG2 . VAL B 1 116 ? -13.68805 -0.07909  -12.00608 1.000 86.86962  ? 116 VAL B CG2 1 
ATOM   2073 N N   . LEU B 1 117 ? -13.68695 -2.16332  -16.00533 1.000 77.05440  ? 117 LEU B N   1 
ATOM   2074 C CA  . LEU B 1 117 ? -13.84344 -3.14408  -17.06696 1.000 77.34476  ? 117 LEU B CA  1 
ATOM   2075 C C   . LEU B 1 117 ? -12.89931 -2.75842  -18.19530 1.000 75.17293  ? 117 LEU B C   1 
ATOM   2076 O O   . LEU B 1 117 ? -12.85892 -1.59441  -18.60393 1.000 81.96477  ? 117 LEU B O   1 
ATOM   2077 C CB  . LEU B 1 117 ? -15.28336 -3.19796  -17.57428 1.000 67.93434  ? 117 LEU B CB  1 
ATOM   2078 C CG  . LEU B 1 117 ? -15.59100 -4.36093  -18.52609 1.000 71.71794  ? 117 LEU B CG  1 
ATOM   2079 C CD1 . LEU B 1 117 ? -15.49531 -5.71626  -17.82643 1.000 65.16101  ? 117 LEU B CD1 1 
ATOM   2080 C CD2 . LEU B 1 117 ? -16.95164 -4.17202  -19.19634 1.000 64.28110  ? 117 LEU B CD2 1 
ATOM   2081 N N   . THR B 1 118 ? -12.15057 -3.73195  -18.70247 1.000 75.39551  ? 118 THR B N   1 
ATOM   2082 C CA  . THR B 1 118 ? -11.19087 -3.48338  -19.76625 1.000 70.84864  ? 118 THR B CA  1 
ATOM   2083 C C   . THR B 1 118 ? -11.38229 -4.51208  -20.86928 1.000 70.58825  ? 118 THR B C   1 
ATOM   2084 O O   . THR B 1 118 ? -11.92854 -5.59606  -20.65042 1.000 80.80079  ? 118 THR B O   1 
ATOM   2085 C CB  . THR B 1 118 ? -9.73755  -3.49698  -19.25250 1.000 70.26445  ? 118 THR B CB  1 
ATOM   2086 O OG1 . THR B 1 118 ? -9.50612  -4.65964  -18.44598 1.000 86.31212  ? 118 THR B OG1 1 
ATOM   2087 C CG2 . THR B 1 118 ? -9.45886  -2.25330  -18.42693 1.000 80.41110  ? 118 THR B CG2 1 
ATOM   2088 N N   . GLY B 1 119 ? -10.92172 -4.15837  -22.06895 1.000 70.08474  ? 119 GLY B N   1 
ATOM   2089 C CA  . GLY B 1 119 ? -11.02360 -5.03604  -23.21344 1.000 71.56696  ? 119 GLY B CA  1 
ATOM   2090 C C   . GLY B 1 119 ? -11.89572 -4.43200  -24.30052 1.000 75.88591  ? 119 GLY B C   1 
ATOM   2091 O O   . GLY B 1 119 ? -11.92308 -3.21046  -24.49534 1.000 79.54974  ? 119 GLY B O   1 
ATOM   2092 N N   . VAL B 1 120 ? -12.60382 -5.30445  -25.00751 1.000 76.48432  ? 120 VAL B N   1 
ATOM   2093 C CA  . VAL B 1 120 ? -13.53558 -4.88618  -26.05050 1.000 74.68178  ? 120 VAL B CA  1 
ATOM   2094 C C   . VAL B 1 120 ? -14.94181 -5.17484  -25.53348 1.000 75.54187  ? 120 VAL B C   1 
ATOM   2095 O O   . VAL B 1 120 ? -15.34420 -6.34509  -25.45234 1.000 68.21854  ? 120 VAL B O   1 
ATOM   2096 C CB  . VAL B 1 120 ? -13.24437 -5.58744  -27.38713 1.000 69.21960  ? 120 VAL B CB  1 
ATOM   2097 C CG1 . VAL B 1 120 ? -14.50206 -5.68174  -28.23558 1.000 67.31549  ? 120 VAL B CG1 1 
ATOM   2098 C CG2 . VAL B 1 120 ? -12.14623 -4.85801  -28.13949 1.000 75.13335  ? 120 VAL B CG2 1 
ATOM   2099 N N   . PRO B 1 121 ? -15.68938 -4.16339  -25.09447 1.000 67.98053  ? 121 PRO B N   1 
ATOM   2100 C CA  . PRO B 1 121 ? -17.03360 -4.39851  -24.54774 1.000 57.70679  ? 121 PRO B CA  1 
ATOM   2101 C C   . PRO B 1 121 ? -18.16430 -4.33411  -25.56487 1.000 61.88446  ? 121 PRO B C   1 
ATOM   2102 O O   . PRO B 1 121 ? -19.32982 -4.36760  -25.16060 1.000 68.56675  ? 121 PRO B O   1 
ATOM   2103 C CB  . PRO B 1 121 ? -17.16794 -3.25916  -23.53007 1.000 67.41056  ? 121 PRO B CB  1 
ATOM   2104 C CG  . PRO B 1 121 ? -16.40408 -2.13434  -24.15127 1.000 66.53599  ? 121 PRO B CG  1 
ATOM   2105 C CD  . PRO B 1 121 ? -15.26814 -2.76039  -24.93870 1.000 68.05966  ? 121 PRO B CD  1 
ATOM   2106 N N   . VAL B 1 122 ? -17.85790 -4.21455  -26.85275 1.000 66.49570  ? 122 VAL B N   1 
ATOM   2107 C CA  . VAL B 1 122 ? -18.85467 -4.16414  -27.91718 1.000 69.21653  ? 122 VAL B CA  1 
ATOM   2108 C C   . VAL B 1 122 ? -18.69359 -5.40635  -28.77992 1.000 70.23240  ? 122 VAL B C   1 
ATOM   2109 O O   . VAL B 1 122 ? -17.59783 -5.68806  -29.28012 1.000 68.91929  ? 122 VAL B O   1 
ATOM   2110 C CB  . VAL B 1 122 ? -18.74187 -2.88544  -28.76280 1.000 66.41962  ? 122 VAL B CB  1 
ATOM   2111 C CG1 . VAL B 1 122 ? -19.69961 -2.95479  -29.94601 1.000 58.37251  ? 122 VAL B CG1 1 
ATOM   2112 C CG2 . VAL B 1 122 ? -19.06085 -1.68068  -27.90895 1.000 63.76667  ? 122 VAL B CG2 1 
ATOM   2113 N N   . ALA B 1 123 ? -19.78076 -6.14457  -28.95702 1.000 71.92393  ? 123 ALA B N   1 
ATOM   2114 C CA  . ALA B 1 123 ? -19.79211 -7.32895  -29.80098 1.000 65.06401  ? 123 ALA B CA  1 
ATOM   2115 C C   . ALA B 1 123 ? -20.74226 -7.10522  -30.96497 1.000 63.97629  ? 123 ALA B C   1 
ATOM   2116 O O   . ALA B 1 123 ? -21.86668 -6.62854  -30.77516 1.000 70.25345  ? 123 ALA B O   1 
ATOM   2117 C CB  . ALA B 1 123 ? -20.21127 -8.56969  -29.00602 1.000 69.12055  ? 123 ALA B CB  1 
ATOM   2118 N N   . GLY B 1 124 ? -20.26972 -7.40410  -32.17029 1.000 64.12568  ? 124 GLY B N   1 
ATOM   2119 C CA  . GLY B 1 124 ? -21.15036 -7.41714  -33.31444 1.000 75.89523  ? 124 GLY B CA  1 
ATOM   2120 C C   . GLY B 1 124 ? -21.94160 -8.70809  -33.39657 1.000 77.78305  ? 124 GLY B C   1 
ATOM   2121 O O   . GLY B 1 124 ? -21.59963 -9.72093  -32.78722 1.000 87.69288  ? 124 GLY B O   1 
ATOM   2122 N N   . VAL B 1 125 ? -23.02788 -8.66831  -34.15743 1.000 77.95786  ? 125 VAL B N   1 
ATOM   2123 C CA  . VAL B 1 125 ? -23.88930 -9.83668  -34.27523 1.000 81.15334  ? 125 VAL B CA  1 
ATOM   2124 C C   . VAL B 1 125 ? -23.31183 -10.77828 -35.32073 1.000 87.82564  ? 125 VAL B C   1 
ATOM   2125 O O   . VAL B 1 125 ? -22.74397 -10.34932 -36.33306 1.000 94.36777  ? 125 VAL B O   1 
ATOM   2126 C CB  . VAL B 1 125 ? -25.33251 -9.41809  -34.61771 1.000 78.23372  ? 125 VAL B CB  1 
ATOM   2127 C CG1 . VAL B 1 125 ? -25.40006 -8.76749  -35.99078 1.000 82.40338  ? 125 VAL B CG1 1 
ATOM   2128 C CG2 . VAL B 1 125 ? -26.27928 -10.61363 -34.52268 1.000 79.74822  ? 125 VAL B CG2 1 
ATOM   2129 N N   . ALA B 1 126 ? -23.44829 -12.07469 -35.06629 1.000 75.76016  ? 126 ALA B N   1 
ATOM   2130 C CA  . ALA B 1 126 ? -23.11909 -13.11075 -36.03292 1.000 94.07971  ? 126 ALA B CA  1 
ATOM   2131 C C   . ALA B 1 126 ? -24.32557 -14.02173 -36.17946 1.000 78.99842  ? 126 ALA B C   1 
ATOM   2132 O O   . ALA B 1 126 ? -24.84178 -14.53225 -35.18041 1.000 80.05635  ? 126 ALA B O   1 
ATOM   2133 C CB  . ALA B 1 126 ? -21.88525 -13.90525 -35.59436 1.000 79.65427  ? 126 ALA B CB  1 
ATOM   2134 N N   . TYR B 1 127 ? -24.80661 -14.17811 -37.40857 1.000 83.18503  ? 127 TYR B N   1 
ATOM   2135 C CA  . TYR B 1 127 ? -25.99530 -14.97537 -37.67543 1.000 88.63291  ? 127 TYR B CA  1 
ATOM   2136 C C   . TYR B 1 127 ? -25.58338 -16.43110 -37.87088 1.000 99.29678  ? 127 TYR B C   1 
ATOM   2137 O O   . TYR B 1 127 ? -24.73430 -16.73067 -38.71697 1.000 97.80197  ? 127 TYR B O   1 
ATOM   2138 C CB  . TYR B 1 127 ? -26.73867 -14.43797 -38.89708 1.000 89.85476  ? 127 TYR B CB  1 
ATOM   2139 C CG  . TYR B 1 127 ? -27.26412 -13.03262 -38.69704 1.000 94.45924  ? 127 TYR B CG  1 
ATOM   2140 C CD1 . TYR B 1 127 ? -28.40110 -12.80058 -37.93461 1.000 89.99651  ? 127 TYR B CD1 1 
ATOM   2141 C CD2 . TYR B 1 127 ? -26.61667 -11.93853 -39.25850 1.000 86.99701  ? 127 TYR B CD2 1 
ATOM   2142 C CE1 . TYR B 1 127 ? -28.88103 -11.52352 -37.74121 1.000 98.84187  ? 127 TYR B CE1 1 
ATOM   2143 C CE2 . TYR B 1 127 ? -27.09073 -10.65728 -39.07063 1.000 94.40558  ? 127 TYR B CE2 1 
ATOM   2144 C CZ  . TYR B 1 127 ? -28.22256 -10.45492 -38.31041 1.000 95.37537  ? 127 TYR B CZ  1 
ATOM   2145 O OH  . TYR B 1 127 ? -28.70104 -9.17994  -38.12037 1.000 93.97683  ? 127 TYR B OH  1 
ATOM   2146 N N   . LEU B 1 128 ? -26.17400 -17.32903 -37.08174 1.000 94.24782  ? 128 LEU B N   1 
ATOM   2147 C CA  . LEU B 1 128 ? -25.80766 -18.73829 -37.07392 1.000 109.59047 ? 128 LEU B CA  1 
ATOM   2148 C C   . LEU B 1 128 ? -27.06531 -19.59474 -37.08826 1.000 109.01432 ? 128 LEU B C   1 
ATOM   2149 O O   . LEU B 1 128 ? -28.12674 -19.17778 -36.61885 1.000 112.40843 ? 128 LEU B O   1 
ATOM   2150 C CB  . LEU B 1 128 ? -24.95923 -19.09809 -35.84214 1.000 97.69058  ? 128 LEU B CB  1 
ATOM   2151 C CG  . LEU B 1 128 ? -23.58297 -18.44898 -35.68612 1.000 99.43557  ? 128 LEU B CG  1 
ATOM   2152 C CD1 . LEU B 1 128 ? -22.82448 -19.11051 -34.55552 1.000 92.59642  ? 128 LEU B CD1 1 
ATOM   2153 C CD2 . LEU B 1 128 ? -22.78559 -18.57004 -36.97317 1.000 89.50556  ? 128 LEU B CD2 1 
ATOM   2154 N N   . ASP B 1 129 ? -26.93292 -20.80468 -37.62870 1.000 122.32631 ? 129 ASP B N   1 
ATOM   2155 C CA  . ASP B 1 129 ? -28.03464 -21.75595 -37.66565 1.000 130.74707 ? 129 ASP B CA  1 
ATOM   2156 C C   . ASP B 1 129 ? -28.01545 -22.73634 -36.50147 1.000 123.26612 ? 129 ASP B C   1 
ATOM   2157 O O   . ASP B 1 129 ? -29.06345 -23.30320 -36.17265 1.000 125.62769 ? 129 ASP B O   1 
ATOM   2158 C CB  . ASP B 1 129 ? -28.03150 -22.52219 -38.99375 1.000 145.91842 ? 129 ASP B CB  1 
ATOM   2159 C CG  . ASP B 1 129 ? -27.67210 -21.63646 -40.17415 1.000 162.01707 ? 129 ASP B CG  1 
ATOM   2160 O OD1 . ASP B 1 129 ? -28.55763 -20.89510 -40.65219 1.000 148.92929 ? 129 ASP B OD1 1 
ATOM   2161 O OD2 . ASP B 1 129 ? -26.50826 -21.68162 -40.62562 1.000 188.01715 ? 129 ASP B OD2 1 
ATOM   2162 N N   . LYS B 1 130 ? -26.85253 -22.95773 -35.88919 1.000 110.37485 ? 130 LYS B N   1 
ATOM   2163 C CA  . LYS B 1 130 ? -26.66619 -23.88622 -34.78638 1.000 114.44987 ? 130 LYS B CA  1 
ATOM   2164 C C   . LYS B 1 130 ? -26.03872 -23.16034 -33.60357 1.000 109.78817 ? 130 LYS B C   1 
ATOM   2165 O O   . LYS B 1 130 ? -25.13580 -22.33658 -33.79242 1.000 111.97801 ? 130 LYS B O   1 
ATOM   2166 C CB  . LYS B 1 130 ? -25.77590 -25.07069 -35.19978 1.000 112.54692 ? 130 LYS B CB  1 
ATOM   2167 C CG  . LYS B 1 130 ? -26.28189 -25.83400 -36.41455 1.000 115.90831 ? 130 LYS B CG  1 
ATOM   2168 C CD  . LYS B 1 130 ? -27.04024 -27.09591 -36.01842 1.000 122.16401 ? 130 LYS B CD  1 
ATOM   2169 C CE  . LYS B 1 130 ? -26.08652 -28.25009 -35.71121 1.000 125.08025 ? 130 LYS B CE  1 
ATOM   2170 N NZ  . LYS B 1 130 ? -26.52821 -29.53453 -36.33446 1.000 126.58959 ? 130 LYS B NZ  1 
ATOM   2171 N N   . PRO B 1 131 ? -26.48681 -23.44084 -32.36907 1.000 111.01723 ? 131 PRO B N   1 
ATOM   2172 C CA  . PRO B 1 131 ? -27.49490 -24.43754 -31.97484 1.000 111.70009 ? 131 PRO B CA  1 
ATOM   2173 C C   . PRO B 1 131 ? -28.91961 -24.02204 -32.32776 1.000 116.48769 ? 131 PRO B C   1 
ATOM   2174 O O   . PRO B 1 131 ? -29.81683 -24.85656 -32.40298 1.000 114.73458 ? 131 PRO B O   1 
ATOM   2175 C CB  . PRO B 1 131 ? -27.30202 -24.52439 -30.45486 1.000 93.16805  ? 131 PRO B CB  1 
ATOM   2176 C CG  . PRO B 1 131 ? -26.86105 -23.14178 -30.07549 1.000 97.00695  ? 131 PRO B CG  1 
ATOM   2177 C CD  . PRO B 1 131 ? -25.95754 -22.71153 -31.20246 1.000 87.22403  ? 131 PRO B CD  1 
ATOM   2178 N N   . ASN B 1 132 ? -29.13660 -22.73005 -32.56562 1.000 116.56343 ? 132 ASN B N   1 
ATOM   2179 C CA  . ASN B 1 132 ? -30.42830 -22.20524 -32.98210 1.000 103.71291 ? 132 ASN B CA  1 
ATOM   2180 C C   . ASN B 1 132 ? -30.22044 -21.19085 -34.09652 1.000 100.18703 ? 132 ASN B C   1 
ATOM   2181 O O   . ASN B 1 132 ? -29.13622 -20.62530 -34.25454 1.000 107.17244 ? 132 ASN B O   1 
ATOM   2182 C CB  . ASN B 1 132 ? -31.18872 -21.54927 -31.81851 1.000 107.55302 ? 132 ASN B CB  1 
ATOM   2183 C CG  . ASN B 1 132 ? -32.07043 -22.52751 -31.06189 1.000 123.14890 ? 132 ASN B CG  1 
ATOM   2184 O OD1 . ASN B 1 132 ? -31.69169 -23.67248 -30.82196 1.000 134.37565 ? 132 ASN B OD1 1 
ATOM   2185 N ND2 . ASN B 1 132 ? -33.26430 -22.07776 -30.69200 1.000 126.93816 ? 132 ASN B ND2 1 
ATOM   2186 N N   . ARG B 1 133 ? -31.27176 -20.98033 -34.88415 1.000 100.51547 ? 133 ARG B N   1 
ATOM   2187 C CA  . ARG B 1 133 ? -31.24320 -20.01288 -35.97992 1.000 110.38119 ? 133 ARG B CA  1 
ATOM   2188 C C   . ARG B 1 133 ? -31.52374 -18.63561 -35.38842 1.000 104.49919 ? 133 ARG B C   1 
ATOM   2189 O O   . ARG B 1 133 ? -32.67492 -18.23631 -35.20878 1.000 105.67046 ? 133 ARG B O   1 
ATOM   2190 C CB  . ARG B 1 133 ? -32.25616 -20.37243 -37.05871 1.000 107.10662 ? 133 ARG B CB  1 
ATOM   2191 C CG  . ARG B 1 133 ? -31.74719 -20.17700 -38.47941 1.000 121.99878 ? 133 ARG B CG  1 
ATOM   2192 C CD  . ARG B 1 133 ? -32.78201 -20.62770 -39.49895 1.000 140.13587 ? 133 ARG B CD  1 
ATOM   2193 N NE  . ARG B 1 133 ? -32.39883 -20.29631 -40.86684 1.000 151.41642 ? 133 ARG B NE  1 
ATOM   2194 C CZ  . ARG B 1 133 ? -32.85916 -19.25235 -41.54338 1.000 151.11645 ? 133 ARG B CZ  1 
ATOM   2195 N NH1 . ARG B 1 133 ? -33.73383 -18.41385 -41.01047 1.000 144.30416 ? 133 ARG B NH1 1 
ATOM   2196 N NH2 . ARG B 1 133 ? -32.44074 -19.05145 -42.79030 1.000 133.23387 ? 133 ARG B NH2 1 
ATOM   2197 N N   . ALA B 1 134 ? -30.45970 -17.90263 -35.06970 1.000 91.16734  ? 134 ALA B N   1 
ATOM   2198 C CA  . ALA B 1 134 ? -30.59050 -16.62871 -34.37444 1.000 105.07389 ? 134 ALA B CA  1 
ATOM   2199 C C   . ALA B 1 134 ? -29.29100 -15.84695 -34.51962 1.000 93.34809  ? 134 ALA B C   1 
ATOM   2200 O O   . ALA B 1 134 ? -28.33424 -16.29720 -35.15534 1.000 89.15018  ? 134 ALA B O   1 
ATOM   2201 C CB  . ALA B 1 134 ? -30.94047 -16.83593 -32.89734 1.000 97.21374  ? 134 ALA B CB  1 
ATOM   2202 N N   . GLY B 1 135 ? -29.28127 -14.64941 -33.94461 1.000 79.47278  ? 135 GLY B N   1 
ATOM   2203 C CA  . GLY B 1 135 ? -28.07366 -13.85763 -33.86097 1.000 79.27771  ? 135 GLY B CA  1 
ATOM   2204 C C   . GLY B 1 135 ? -27.31274 -14.16832 -32.58574 1.000 72.68045  ? 135 GLY B C   1 
ATOM   2205 O O   . GLY B 1 135 ? -27.88842 -14.55913 -31.57823 1.000 76.68925  ? 135 GLY B O   1 
ATOM   2206 N N   . TYR B 1 136 ? -25.99734 -14.01231 -32.64086 1.000 71.10230  ? 136 TYR B N   1 
ATOM   2207 C CA  . TYR B 1 136 ? -25.16968 -14.37339 -31.50310 1.000 74.95261  ? 136 TYR B CA  1 
ATOM   2208 C C   . TYR B 1 136 ? -24.10289 -13.31980 -31.26077 1.000 69.68220  ? 136 TYR B C   1 
ATOM   2209 O O   . TYR B 1 136 ? -23.49126 -12.80544 -32.20106 1.000 66.69092  ? 136 TYR B O   1 
ATOM   2210 C CB  . TYR B 1 136 ? -24.52461 -15.74677 -31.71042 1.000 75.34572  ? 136 TYR B CB  1 
ATOM   2211 C CG  . TYR B 1 136 ? -25.50544 -16.89624 -31.66612 1.000 80.62438  ? 136 TYR B CG  1 
ATOM   2212 C CD1 . TYR B 1 136 ? -25.87968 -17.46821 -30.45571 1.000 78.35301  ? 136 TYR B CD1 1 
ATOM   2213 C CD2 . TYR B 1 136 ? -26.06817 -17.40015 -32.83139 1.000 82.93056  ? 136 TYR B CD2 1 
ATOM   2214 C CE1 . TYR B 1 136 ? -26.77582 -18.52081 -30.40984 1.000 84.13301  ? 136 TYR B CE1 1 
ATOM   2215 C CE2 . TYR B 1 136 ? -26.96618 -18.45244 -32.79590 1.000 88.66735  ? 136 TYR B CE2 1 
ATOM   2216 C CZ  . TYR B 1 136 ? -27.31698 -19.00726 -31.58379 1.000 88.20723  ? 136 TYR B CZ  1 
ATOM   2217 O OH  . TYR B 1 136 ? -28.21137 -20.05262 -31.55094 1.000 89.93439  ? 136 TYR B OH  1 
ATOM   2218 N N   . PHE B 1 137 ? -23.87445 -13.02172 -29.98907 1.000 65.99365  ? 137 PHE B N   1 
ATOM   2219 C CA  . PHE B 1 137 ? -22.81330 -12.12538 -29.56735 1.000 68.31645  ? 137 PHE B CA  1 
ATOM   2220 C C   . PHE B 1 137 ? -21.90145 -12.86043 -28.60009 1.000 63.76295  ? 137 PHE B C   1 
ATOM   2221 O O   . PHE B 1 137 ? -22.37272 -13.58062 -27.71440 1.000 63.21264  ? 137 PHE B O   1 
ATOM   2222 C CB  . PHE B 1 137 ? -23.37677 -10.86895 -28.89242 1.000 62.90152  ? 137 PHE B CB  1 
ATOM   2223 C CG  . PHE B 1 137 ? -24.42483 -10.15809 -29.70261 1.000 73.65348  ? 137 PHE B CG  1 
ATOM   2224 C CD1 . PHE B 1 137 ? -25.75331 -10.55213 -29.64201 1.000 71.00421  ? 137 PHE B CD1 1 
ATOM   2225 C CD2 . PHE B 1 137 ? -24.08774 -9.07777  -30.50330 1.000 70.79579  ? 137 PHE B CD2 1 
ATOM   2226 C CE1 . PHE B 1 137 ? -26.72327 -9.89521  -30.38005 1.000 69.91497  ? 137 PHE B CE1 1 
ATOM   2227 C CE2 . PHE B 1 137 ? -25.05632 -8.41047  -31.23713 1.000 77.46422  ? 137 PHE B CE2 1 
ATOM   2228 C CZ  . PHE B 1 137 ? -26.37492 -8.82425  -31.17940 1.000 62.80679  ? 137 PHE B CZ  1 
ATOM   2229 N N   . ILE B 1 138 ? -20.59587 -12.70723 -28.78836 1.000 61.19326  ? 138 ILE B N   1 
ATOM   2230 C CA  . ILE B 1 138 ? -19.62016 -13.34223 -27.91615 1.000 71.78809  ? 138 ILE B CA  1 
ATOM   2231 C C   . ILE B 1 138 ? -18.65177 -12.27853 -27.41726 1.000 64.03419  ? 138 ILE B C   1 
ATOM   2232 O O   . ILE B 1 138 ? -18.27036 -11.36551 -28.16017 1.000 65.41608  ? 138 ILE B O   1 
ATOM   2233 C CB  . ILE B 1 138 ? -18.87915 -14.50042 -28.62654 1.000 73.21632  ? 138 ILE B CB  1 
ATOM   2234 C CG1 . ILE B 1 138 ? -18.00281 -15.27387 -27.63522 1.000 73.59893  ? 138 ILE B CG1 1 
ATOM   2235 C CG2 . ILE B 1 138 ? -18.06277 -14.00107 -29.80850 1.000 63.43002  ? 138 ILE B CG2 1 
ATOM   2236 C CD1 . ILE B 1 138 ? -17.69452 -16.71521 -28.06038 1.000 65.35620  ? 138 ILE B CD1 1 
ATOM   2237 N N   . PHE B 1 139 ? -18.28752 -12.37972 -26.13926 1.000 60.18721  ? 139 PHE B N   1 
ATOM   2238 C CA  . PHE B 1 139 ? -17.38966 -11.43783 -25.47286 1.000 61.89554  ? 139 PHE B CA  1 
ATOM   2239 C C   . PHE B 1 139 ? -16.17377 -12.20315 -24.96298 1.000 66.25465  ? 139 PHE B C   1 
ATOM   2240 O O   . PHE B 1 139 ? -16.16977 -12.68711 -23.81893 1.000 63.79143  ? 139 PHE B O   1 
ATOM   2241 C CB  . PHE B 1 139 ? -18.09621 -10.70341 -24.33405 1.000 61.73123  ? 139 PHE B CB  1 
ATOM   2242 C CG  . PHE B 1 139 ? -19.20652 -9.78978  -24.78794 1.000 65.28764  ? 139 PHE B CG  1 
ATOM   2243 C CD1 . PHE B 1 139 ? -20.50144 -10.27023 -24.93549 1.000 68.13693  ? 139 PHE B CD1 1 
ATOM   2244 C CD2 . PHE B 1 139 ? -18.95851 -8.45344  -25.06544 1.000 64.02250  ? 139 PHE B CD2 1 
ATOM   2245 C CE1 . PHE B 1 139 ? -21.52912 -9.43572  -25.34401 1.000 62.54364  ? 139 PHE B CE1 1 
ATOM   2246 C CE2 . PHE B 1 139 ? -19.98195 -7.61239  -25.47966 1.000 65.71078  ? 139 PHE B CE2 1 
ATOM   2247 C CZ  . PHE B 1 139 ? -21.26900 -8.10644  -25.61888 1.000 71.88370  ? 139 PHE B CZ  1 
ATOM   2248 N N   . PRO B 1 140 ? -15.12615 -12.36217 -25.77520 1.000 57.73317  ? 140 PRO B N   1 
ATOM   2249 C CA  . PRO B 1 140 ? -13.97385 -13.15174 -25.33755 1.000 66.99405  ? 140 PRO B CA  1 
ATOM   2250 C C   . PRO B 1 140 ? -12.90771 -12.34328 -24.61929 1.000 69.62496  ? 140 PRO B C   1 
ATOM   2251 O O   . PRO B 1 140 ? -12.01907 -12.94194 -23.99777 1.000 91.99713  ? 140 PRO B O   1 
ATOM   2252 C CB  . PRO B 1 140 ? -13.42741 -13.70150 -26.66026 1.000 62.00559  ? 140 PRO B CB  1 
ATOM   2253 C CG  . PRO B 1 140 ? -13.74996 -12.63636 -27.64168 1.000 62.32342  ? 140 PRO B CG  1 
ATOM   2254 C CD  . PRO B 1 140 ? -15.07370 -12.07133 -27.21818 1.000 59.42906  ? 140 PRO B CD  1 
ATOM   2255 N N   . ASP B 1 141 ? -12.96943 -11.01834 -24.67595 1.000 66.27173  ? 141 ASP B N   1 
ATOM   2256 C CA  . ASP B 1 141 ? -11.86511 -10.16006 -24.26377 1.000 76.92933  ? 141 ASP B CA  1 
ATOM   2257 C C   . ASP B 1 141 ? -12.34281 -9.14043  -23.23059 1.000 76.28661  ? 141 ASP B C   1 
ATOM   2258 O O   . ASP B 1 141 ? -12.14001 -7.93236  -23.36687 1.000 75.05707  ? 141 ASP B O   1 
ATOM   2259 C CB  . ASP B 1 141 ? -11.23060 -9.48650  -25.48105 1.000 76.53147  ? 141 ASP B CB  1 
ATOM   2260 C CG  . ASP B 1 141 ? -9.90323  -8.81459  -25.15587 1.000 104.85631 ? 141 ASP B CG  1 
ATOM   2261 O OD1 . ASP B 1 141 ? -9.32557  -9.10946  -24.08505 1.000 100.67284 ? 141 ASP B OD1 1 
ATOM   2262 O OD2 . ASP B 1 141 ? -9.43014  -8.00085  -25.97899 1.000 107.57391 ? 141 ASP B OD2 1 
ATOM   2263 N N   . LEU B 1 142 ? -13.01837 -9.61645  -22.18692 1.000 66.66393  ? 142 LEU B N   1 
ATOM   2264 C CA  . LEU B 1 142 ? -13.47079 -8.76542  -21.09508 1.000 62.49471  ? 142 LEU B CA  1 
ATOM   2265 C C   . LEU B 1 142 ? -12.64247 -9.06240  -19.85264 1.000 71.69806  ? 142 LEU B C   1 
ATOM   2266 O O   . LEU B 1 142 ? -12.54092 -10.21996 -19.43569 1.000 77.47850  ? 142 LEU B O   1 
ATOM   2267 C CB  . LEU B 1 142 ? -14.95234 -8.98812  -20.79221 1.000 63.35845  ? 142 LEU B CB  1 
ATOM   2268 C CG  . LEU B 1 142 ? -16.01849 -8.43194  -21.73507 1.000 64.99672  ? 142 LEU B CG  1 
ATOM   2269 C CD1 . LEU B 1 142 ? -17.36917 -8.99302  -21.33376 1.000 69.38526  ? 142 LEU B CD1 1 
ATOM   2270 C CD2 . LEU B 1 142 ? -16.03936 -6.90715  -21.73637 1.000 60.90911  ? 142 LEU B CD2 1 
ATOM   2271 N N   . SER B 1 143 ? -12.10719 -8.01346  -19.22887 1.000 78.59389  ? 143 SER B N   1 
ATOM   2272 C CA  . SER B 1 143 ? -11.28528 -8.14866  -18.03459 1.000 76.47420  ? 143 SER B CA  1 
ATOM   2273 C C   . SER B 1 143 ? -11.76156 -7.18643  -16.95731 1.000 75.22151  ? 143 SER B C   1 
ATOM   2274 O O   . SER B 1 143 ? -12.27710 -6.10366  -17.24855 1.000 72.39898  ? 143 SER B O   1 
ATOM   2275 C CB  . SER B 1 143 ? -9.80016  -7.88643  -18.33090 1.000 84.82525  ? 143 SER B CB  1 
ATOM   2276 O OG  . SER B 1 143 ? -9.41291  -8.44417  -19.57434 1.000 94.43297  ? 143 SER B OG  1 
ATOM   2277 N N   . VAL B 1 144 ? -11.57792 -7.59866  -15.70630 1.000 76.49047  ? 144 VAL B N   1 
ATOM   2278 C CA  . VAL B 1 144 ? -12.02346 -6.85389  -14.53572 1.000 66.48950  ? 144 VAL B CA  1 
ATOM   2279 C C   . VAL B 1 144 ? -10.79335 -6.49545  -13.71666 1.000 75.06683  ? 144 VAL B C   1 
ATOM   2280 O O   . VAL B 1 144 ? -9.95017  -7.35704  -13.44603 1.000 76.40661  ? 144 VAL B O   1 
ATOM   2281 C CB  . VAL B 1 144 ? -13.02691 -7.65991  -13.69586 1.000 72.96923  ? 144 VAL B CB  1 
ATOM   2282 C CG1 . VAL B 1 144 ? -13.56341 -6.80548  -12.55091 1.000 67.64404  ? 144 VAL B CG1 1 
ATOM   2283 C CG2 . VAL B 1 144 ? -14.14699 -8.18340  -14.57839 1.000 68.18849  ? 144 VAL B CG2 1 
ATOM   2284 N N   . ARG B 1 145 ? -10.69788 -5.23106  -13.30846 1.000 78.65316  ? 145 ARG B N   1 
ATOM   2285 C CA  . ARG B 1 145 ? -9.49015  -4.78027  -12.62987 1.000 86.81421  ? 145 ARG B CA  1 
ATOM   2286 C C   . ARG B 1 145 ? -9.43890  -5.18396  -11.16063 1.000 85.29568  ? 145 ARG B C   1 
ATOM   2287 O O   . ARG B 1 145 ? -8.35665  -5.50017  -10.65509 1.000 77.69156  ? 145 ARG B O   1 
ATOM   2288 C CB  . ARG B 1 145 ? -9.38775  -3.25731  -12.72210 1.000 99.27594  ? 145 ARG B CB  1 
ATOM   2289 C CG  . ARG B 1 145 ? -8.01257  -2.69850  -12.41862 1.000 117.59436 ? 145 ARG B CG  1 
ATOM   2290 C CD  . ARG B 1 145 ? -8.10980  -1.50231  -11.47967 1.000 126.14493 ? 145 ARG B CD  1 
ATOM   2291 N NE  . ARG B 1 145 ? -8.72318  -0.32645  -12.08682 1.000 128.23654 ? 145 ARG B NE  1 
ATOM   2292 C CZ  . ARG B 1 145 ? -8.94135  0.81548   -11.44646 1.000 137.68736 ? 145 ARG B CZ  1 
ATOM   2293 N NH1 . ARG B 1 145 ? -8.71351  0.93531   -10.14795 1.000 142.73827 ? 145 ARG B NH1 1 
ATOM   2294 N NH2 . ARG B 1 145 ? -9.44654  1.84819   -12.11453 1.000 127.14393 ? 145 ARG B NH2 1 
ATOM   2295 N N   . ASN B 1 146 ? -10.57388 -5.22355  -10.46831 1.000 78.85704  ? 146 ASN B N   1 
ATOM   2296 C CA  . ASN B 1 146 ? -10.57407 -5.46768  -9.03465  1.000 80.40243  ? 146 ASN B CA  1 
ATOM   2297 C C   . ASN B 1 146 ? -11.37388 -6.71197  -8.68851  1.000 83.16978  ? 146 ASN B C   1 
ATOM   2298 O O   . ASN B 1 146 ? -12.34020 -7.06354  -9.37162  1.000 81.83972  ? 146 ASN B O   1 
ATOM   2299 C CB  . ASN B 1 146 ? -11.15290 -4.26939  -8.26603  1.000 94.85962  ? 146 ASN B CB  1 
ATOM   2300 C CG  . ASN B 1 146 ? -10.51931 -2.95531  -8.67036  1.000 105.05015 ? 146 ASN B CG  1 
ATOM   2301 O OD1 . ASN B 1 146 ? -9.30273  -2.86555  -8.83546  1.000 108.71972 ? 146 ASN B OD1 1 
ATOM   2302 N ND2 . ASN B 1 146 ? -11.34396 -1.92586  -8.83591  1.000 104.97826 ? 146 ASN B ND2 1 
ATOM   2303 N N   . GLU B 1 147 ? -10.97384 -7.35708  -7.59797  1.000 78.68695  ? 147 GLU B N   1 
ATOM   2304 C CA  . GLU B 1 147 ? -11.67564 -8.54216  -7.14015  1.000 82.10034  ? 147 GLU B CA  1 
ATOM   2305 C C   . GLU B 1 147 ? -13.03510 -8.15903  -6.56810  1.000 75.87399  ? 147 GLU B C   1 
ATOM   2306 O O   . GLU B 1 147 ? -13.24103 -7.04385  -6.08472  1.000 84.60392  ? 147 GLU B O   1 
ATOM   2307 C CB  . GLU B 1 147 ? -10.85163 -9.28540  -6.08737  1.000 89.52430  ? 147 GLU B CB  1 
ATOM   2308 C CG  . GLU B 1 147 ? -10.69159 -8.54295  -4.76972  1.000 102.33686 ? 147 GLU B CG  1 
ATOM   2309 C CD  . GLU B 1 147 ? -9.69913  -9.21827  -3.83800  1.000 120.15084 ? 147 GLU B CD  1 
ATOM   2310 O OE1 . GLU B 1 147 ? -9.94279  -10.38185 -3.44484  1.000 110.52351 ? 147 GLU B OE1 1 
ATOM   2311 O OE2 . GLU B 1 147 ? -8.67760  -8.58348  -3.49340  1.000 108.59865 ? 147 GLU B OE2 1 
ATOM   2312 N N   . GLY B 1 148 ? -13.96304 -9.09177  -6.63096  1.000 80.11189  ? 148 GLY B N   1 
ATOM   2313 C CA  . GLY B 1 148 ? -15.28353 -8.88089  -6.07480  1.000 76.55392  ? 148 GLY B CA  1 
ATOM   2314 C C   . GLY B 1 148 ? -16.32143 -9.66503  -6.84888  1.000 75.72293  ? 148 GLY B C   1 
ATOM   2315 O O   . GLY B 1 148 ? -16.01868 -10.38523 -7.79635  1.000 81.03745  ? 148 GLY B O   1 
ATOM   2316 N N   . SER B 1 149 ? -17.56380 -9.51837  -6.40216  1.000 75.43095  ? 149 SER B N   1 
ATOM   2317 C CA  . SER B 1 149 ? -18.71027 -10.12436 -7.06236  1.000 77.94253  ? 149 SER B CA  1 
ATOM   2318 C C   . SER B 1 149 ? -19.32994 -9.11016  -8.01243  1.000 84.61425  ? 149 SER B C   1 
ATOM   2319 O O   . SER B 1 149 ? -19.61965 -7.97482  -7.61835  1.000 77.89280  ? 149 SER B O   1 
ATOM   2320 C CB  . SER B 1 149 ? -19.73890 -10.60815 -6.04180  1.000 74.01686  ? 149 SER B CB  1 
ATOM   2321 O OG  . SER B 1 149 ? -20.43612 -11.73928 -6.52924  1.000 98.28076  ? 149 SER B OG  1 
ATOM   2322 N N   . TYR B 1 150 ? -19.53264 -9.51635  -9.25907  1.000 74.97251  ? 150 TYR B N   1 
ATOM   2323 C CA  . TYR B 1 150 ? -20.00903 -8.59921  -10.27567 1.000 72.28628  ? 150 TYR B CA  1 
ATOM   2324 C C   . TYR B 1 150 ? -21.15259 -9.23279  -11.04952 1.000 75.13684  ? 150 TYR B C   1 
ATOM   2325 O O   . TYR B 1 150 ? -21.43632 -10.42766 -10.94268 1.000 75.51925  ? 150 TYR B O   1 
ATOM   2326 C CB  . TYR B 1 150 ? -18.89706 -8.20818  -11.25620 1.000 68.95353  ? 150 TYR B CB  1 
ATOM   2327 C CG  . TYR B 1 150 ? -17.75464 -7.44038  -10.64456 1.000 73.86171  ? 150 TYR B CG  1 
ATOM   2328 C CD1 . TYR B 1 150 ? -17.77772 -6.05351  -10.57950 1.000 79.53549  ? 150 TYR B CD1 1 
ATOM   2329 C CD2 . TYR B 1 150 ? -16.63531 -8.10132  -10.16075 1.000 65.62337  ? 150 TYR B CD2 1 
ATOM   2330 C CE1 . TYR B 1 150 ? -16.72332 -5.34782  -10.03220 1.000 70.24194  ? 150 TYR B CE1 1 
ATOM   2331 C CE2 . TYR B 1 150 ? -15.57880 -7.40631  -9.61100  1.000 77.77496  ? 150 TYR B CE2 1 
ATOM   2332 C CZ  . TYR B 1 150 ? -15.62601 -6.02991  -9.55027  1.000 71.64646  ? 150 TYR B CZ  1 
ATOM   2333 O OH  . TYR B 1 150 ? -14.57033 -5.33730  -9.00294  1.000 85.31134  ? 150 TYR B OH  1 
ATOM   2334 N N   . ARG B 1 151 ? -21.77550 -8.39883  -11.86742 1.000 70.78443  ? 151 ARG B N   1 
ATOM   2335 C CA  . ARG B 1 151 ? -22.80539 -8.78879  -12.80913 1.000 65.35884  ? 151 ARG B CA  1 
ATOM   2336 C C   . ARG B 1 151 ? -22.51817 -8.07935  -14.11849 1.000 69.30334  ? 151 ARG B C   1 
ATOM   2337 O O   . ARG B 1 151 ? -21.89626 -7.01457  -14.13866 1.000 81.60901  ? 151 ARG B O   1 
ATOM   2338 C CB  . ARG B 1 151 ? -24.20634 -8.43628  -12.31173 1.000 76.74127  ? 151 ARG B CB  1 
ATOM   2339 C CG  . ARG B 1 151 ? -25.04938 -9.63219  -11.94686 1.000 75.49666  ? 151 ARG B CG  1 
ATOM   2340 C CD  . ARG B 1 151 ? -26.45305 -9.18932  -11.58913 1.000 71.72285  ? 151 ARG B CD  1 
ATOM   2341 N NE  . ARG B 1 151 ? -26.94484 -9.81523  -10.37138 1.000 70.41826  ? 151 ARG B NE  1 
ATOM   2342 C CZ  . ARG B 1 151 ? -27.75659 -10.86249 -10.35892 1.000 82.04712  ? 151 ARG B CZ  1 
ATOM   2343 N NH1 . ARG B 1 151 ? -28.18300 -11.41844 -11.48263 1.000 76.24273  ? 151 ARG B NH1 1 
ATOM   2344 N NH2 . ARG B 1 151 ? -28.14736 -11.36630 -9.19195  1.000 80.13070  ? 151 ARG B NH2 1 
ATOM   2345 N N   . PHE B 1 152 ? -22.96922 -8.67210  -15.21240 1.000 59.46041  ? 152 PHE B N   1 
ATOM   2346 C CA  . PHE B 1 152 ? -22.82691 -8.05709  -16.52033 1.000 55.13727  ? 152 PHE B CA  1 
ATOM   2347 C C   . PHE B 1 152 ? -24.19901 -7.62584  -17.00899 1.000 68.28614  ? 152 PHE B C   1 
ATOM   2348 O O   . PHE B 1 152 ? -25.18781 -8.34610  -16.84379 1.000 68.77288  ? 152 PHE B O   1 
ATOM   2349 C CB  . PHE B 1 152 ? -22.19060 -9.00273  -17.53812 1.000 65.68786  ? 152 PHE B CB  1 
ATOM   2350 C CG  . PHE B 1 152 ? -20.69900 -8.86396  -17.64324 1.000 67.59539  ? 152 PHE B CG  1 
ATOM   2351 C CD1 . PHE B 1 152 ? -20.10851 -7.61843  -17.74606 1.000 62.38674  ? 152 PHE B CD1 1 
ATOM   2352 C CD2 . PHE B 1 152 ? -19.88616 -9.98986  -17.66423 1.000 72.47905  ? 152 PHE B CD2 1 
ATOM   2353 C CE1 . PHE B 1 152 ? -18.72933 -7.49193  -17.83954 1.000 61.31684  ? 152 PHE B CE1 1 
ATOM   2354 C CE2 . PHE B 1 152 ? -18.50977 -9.87127  -17.76645 1.000 70.10553  ? 152 PHE B CE2 1 
ATOM   2355 C CZ  . PHE B 1 152 ? -17.93192 -8.61842  -17.85360 1.000 73.36154  ? 152 PHE B CZ  1 
ATOM   2356 N N   . SER B 1 153 ? -24.26106 -6.42034  -17.55162 1.000 60.00656  ? 153 SER B N   1 
ATOM   2357 C CA  . SER B 1 153 ? -25.44786 -5.92860  -18.22505 1.000 51.77930  ? 153 SER B CA  1 
ATOM   2358 C C   . SER B 1 153 ? -25.11076 -5.77905  -19.69852 1.000 56.31029  ? 153 SER B C   1 
ATOM   2359 O O   . SER B 1 153 ? -24.05859 -5.23008  -20.04418 1.000 54.56281  ? 153 SER B O   1 
ATOM   2360 C CB  . SER B 1 153 ? -25.90927 -4.59536  -17.63231 1.000 62.48001  ? 153 SER B CB  1 
ATOM   2361 O OG  . SER B 1 153 ? -27.19379 -4.24293  -18.11236 1.000 75.88093  ? 153 SER B OG  1 
ATOM   2362 N N   . PHE B 1 154 ? -25.93381 -6.37764  -20.55281 1.000 54.40587  ? 154 PHE B N   1 
ATOM   2363 C CA  . PHE B 1 154 ? -25.73087 -6.33930  -21.99440 1.000 58.53192  ? 154 PHE B CA  1 
ATOM   2364 C C   . PHE B 1 154 ? -26.83930 -5.51901  -22.64157 1.000 58.20362  ? 154 PHE B C   1 
ATOM   2365 O O   . PHE B 1 154 ? -28.01198 -5.89284  -22.57384 1.000 65.01404  ? 154 PHE B O   1 
ATOM   2366 C CB  . PHE B 1 154 ? -25.68773 -7.75274  -22.57103 1.000 56.17676  ? 154 PHE B CB  1 
ATOM   2367 C CG  . PHE B 1 154 ? -24.61113 -8.61733  -21.97421 1.000 59.67050  ? 154 PHE B CG  1 
ATOM   2368 C CD1 . PHE B 1 154 ? -23.28895 -8.46106  -22.35987 1.000 59.70676  ? 154 PHE B CD1 1 
ATOM   2369 C CD2 . PHE B 1 154 ? -24.91691 -9.57758  -21.02550 1.000 61.18442  ? 154 PHE B CD2 1 
ATOM   2370 C CE1 . PHE B 1 154 ? -22.29570 -9.25077  -21.82201 1.000 54.13282  ? 154 PHE B CE1 1 
ATOM   2371 C CE2 . PHE B 1 154 ? -23.92577 -10.37494 -20.47888 1.000 53.16827  ? 154 PHE B CE2 1 
ATOM   2372 C CZ  . PHE B 1 154 ? -22.61564 -10.21186 -20.87664 1.000 56.81266  ? 154 PHE B CZ  1 
ATOM   2373 N N   . HIS B 1 155 ? -26.46168 -4.41362  -23.27833 1.000 56.96960  ? 155 HIS B N   1 
ATOM   2374 C CA  . HIS B 1 155 ? -27.39926 -3.47446  -23.88330 1.000 54.29159  ? 155 HIS B CA  1 
ATOM   2375 C C   . HIS B 1 155 ? -27.35627 -3.61801  -25.39823 1.000 55.22975  ? 155 HIS B C   1 
ATOM   2376 O O   . HIS B 1 155 ? -26.27488 -3.60827  -25.99213 1.000 61.48288  ? 155 HIS B O   1 
ATOM   2377 C CB  . HIS B 1 155 ? -27.05202 -2.03556  -23.48640 1.000 63.22556  ? 155 HIS B CB  1 
ATOM   2378 C CG  . HIS B 1 155 ? -26.59025 -1.88557  -22.06752 1.000 63.94056  ? 155 HIS B CG  1 
ATOM   2379 N ND1 . HIS B 1 155 ? -27.46234 -1.67992  -21.01941 1.000 62.35127  ? 155 HIS B ND1 1 
ATOM   2380 C CD2 . HIS B 1 155 ? -25.35619 -1.97578  -21.51612 1.000 64.43299  ? 155 HIS B CD2 1 
ATOM   2381 C CE1 . HIS B 1 155 ? -26.78029 -1.60172  -19.89045 1.000 58.29330  ? 155 HIS B CE1 1 
ATOM   2382 N NE2 . HIS B 1 155 ? -25.50097 -1.78697  -20.16305 1.000 65.56756  ? 155 HIS B NE2 1 
ATOM   2383 N N   . LEU B 1 156 ? -28.52890 -3.73433  -26.02137 1.000 57.16647  ? 156 LEU B N   1 
ATOM   2384 C CA  . LEU B 1 156 ? -28.63234 -3.95159  -27.45883 1.000 60.20702  ? 156 LEU B CA  1 
ATOM   2385 C C   . LEU B 1 156 ? -28.88894 -2.63095  -28.17454 1.000 68.14905  ? 156 LEU B C   1 
ATOM   2386 O O   . LEU B 1 156 ? -29.79351 -1.87764  -27.79422 1.000 68.20424  ? 156 LEU B O   1 
ATOM   2387 C CB  . LEU B 1 156 ? -29.75581 -4.94115  -27.76736 1.000 64.57632  ? 156 LEU B CB  1 
ATOM   2388 C CG  . LEU B 1 156 ? -29.96605 -5.24545  -29.24920 1.000 68.08023  ? 156 LEU B CG  1 
ATOM   2389 C CD1 . LEU B 1 156 ? -28.73894 -5.93479  -29.82759 1.000 64.54351  ? 156 LEU B CD1 1 
ATOM   2390 C CD2 . LEU B 1 156 ? -31.22279 -6.08678  -29.44989 1.000 65.46627  ? 156 LEU B CD2 1 
ATOM   2391 N N   . PHE B 1 157 ? -28.09056 -2.35727  -29.20422 1.000 65.32598  ? 157 PHE B N   1 
ATOM   2392 C CA  . PHE B 1 157 ? -28.23623 -1.18513  -30.05742 1.000 62.68954  ? 157 PHE B CA  1 
ATOM   2393 C C   . PHE B 1 157 ? -28.58028 -1.64329  -31.46805 1.000 73.42181  ? 157 PHE B C   1 
ATOM   2394 O O   . PHE B 1 157 ? -27.95322 -2.57814  -31.98728 1.000 65.78989  ? 157 PHE B O   1 
ATOM   2395 C CB  . PHE B 1 157 ? -26.94640 -0.35886  -30.05802 1.000 67.65012  ? 157 PHE B CB  1 
ATOM   2396 C CG  . PHE B 1 157 ? -26.61563 0.21941   -28.71582 1.000 68.03626  ? 157 PHE B CG  1 
ATOM   2397 C CD1 . PHE B 1 157 ? -27.47090 1.12497   -28.11781 1.000 69.68399  ? 157 PHE B CD1 1 
ATOM   2398 C CD2 . PHE B 1 157 ? -25.46231 -0.15187  -28.04340 1.000 65.72088  ? 157 PHE B CD2 1 
ATOM   2399 C CE1 . PHE B 1 157 ? -27.19000 1.64765   -26.87350 1.000 76.06199  ? 157 PHE B CE1 1 
ATOM   2400 C CE2 . PHE B 1 157 ? -25.17072 0.37581   -26.79393 1.000 68.24216  ? 157 PHE B CE2 1 
ATOM   2401 C CZ  . PHE B 1 157 ? -26.03878 1.27488   -26.21090 1.000 61.66042  ? 157 PHE B CZ  1 
ATOM   2402 N N   . GLU B 1 158 ? -29.57581 -1.00594  -32.07107 1.000 67.64634  ? 158 GLU B N   1 
ATOM   2403 C CA  . GLU B 1 158 ? -30.01919 -1.31046  -33.42050 1.000 70.59780  ? 158 GLU B CA  1 
ATOM   2404 C C   . GLU B 1 158 ? -29.68537 -0.11971  -34.31021 1.000 82.88777  ? 158 GLU B C   1 
ATOM   2405 O O   . GLU B 1 158 ? -30.12182 1.00124   -34.02892 1.000 87.09583  ? 158 GLU B O   1 
ATOM   2406 C CB  . GLU B 1 158 ? -31.51912 -1.60560  -33.44837 1.000 72.82196  ? 158 GLU B CB  1 
ATOM   2407 C CG  . GLU B 1 158 ? -32.06942 -1.77932  -34.82489 1.000 81.40747  ? 158 GLU B CG  1 
ATOM   2408 C CD  . GLU B 1 158 ? -33.53783 -2.11762  -34.81672 1.000 94.28097  ? 158 GLU B CD  1 
ATOM   2409 O OE1 . GLU B 1 158 ? -34.08622 -2.47163  -33.74687 1.000 91.07840  ? 158 GLU B OE1 1 
ATOM   2410 O OE2 . GLU B 1 158 ? -34.14828 -1.97801  -35.88961 1.000 102.99870 ? 158 GLU B OE2 1 
ATOM   2411 N N   . GLN B 1 159 ? -28.90244 -0.35701  -35.36139 1.000 86.51591  ? 159 GLN B N   1 
ATOM   2412 C CA  . GLN B 1 159 ? -28.56392 0.66509   -36.34640 1.000 98.74071  ? 159 GLN B CA  1 
ATOM   2413 C C   . GLN B 1 159 ? -29.43566 0.36370   -37.55686 1.000 101.08852 ? 159 GLN B C   1 
ATOM   2414 O O   . GLN B 1 159 ? -29.23372 -0.65698  -38.21569 1.000 114.35616 ? 159 GLN B O   1 
ATOM   2415 C CB  . GLN B 1 159 ? -27.09011 0.61469   -36.74316 1.000 107.40032 ? 159 GLN B CB  1 
ATOM   2416 C CG  . GLN B 1 159 ? -26.80038 1.23590   -38.09723 1.000 126.57876 ? 159 GLN B CG  1 
ATOM   2417 C CD  . GLN B 1 159 ? -25.36902 1.62438   -38.20308 1.000 136.55021 ? 159 GLN B CD  1 
ATOM   2418 O OE1 . GLN B 1 159 ? -24.51148 0.94871   -37.59731 1.000 134.07224 ? 159 GLN B OE1 1 
ATOM   2419 N NE2 . GLN B 1 159 ? -25.09630 2.75682   -38.87568 1.000 150.30347 ? 159 GLN B NE2 1 
ATOM   2420 N N   . ILE B 1 160 ? -30.42942 1.21926   -37.83338 1.000 115.93695 ? 160 ILE B N   1 
ATOM   2421 C CA  . ILE B 1 160 ? -31.47638 0.90462   -38.81047 1.000 136.11972 ? 160 ILE B CA  1 
ATOM   2422 C C   . ILE B 1 160 ? -31.01866 1.33223   -40.20110 1.000 140.07989 ? 160 ILE B C   1 
ATOM   2423 O O   . ILE B 1 160 ? -30.42493 2.40464   -40.37680 1.000 133.50344 ? 160 ILE B O   1 
ATOM   2424 C CB  . ILE B 1 160 ? -32.82183 1.56191   -38.43590 1.000 140.07277 ? 160 ILE B CB  1 
ATOM   2425 C CG1 . ILE B 1 160 ? -34.01089 0.65397   -38.79968 1.000 144.43036 ? 160 ILE B CG1 1 
ATOM   2426 C CG2 . ILE B 1 160 ? -33.00809 2.94736   -39.04731 1.000 141.38003 ? 160 ILE B CG2 1 
ATOM   2427 C CD1 . ILE B 1 160 ? -35.28932 1.04639   -38.09845 1.000 136.05119 ? 160 ILE B CD1 1 
ATOM   2428 N N   . LYS B 1 161 ? -31.21626 0.44333   -41.18078 1.000 159.01316 ? 161 LYS B N   1 
ATOM   2429 C CA  . LYS B 1 161 ? -30.95375 0.73824   -42.58553 1.000 180.33734 ? 161 LYS B CA  1 
ATOM   2430 C C   . LYS B 1 161 ? -32.20117 0.88205   -43.44466 1.000 207.62961 ? 161 LYS B C   1 
ATOM   2431 O O   . LYS B 1 161 ? -32.10596 1.42177   -44.55170 1.000 210.09168 ? 161 LYS B O   1 
ATOM   2432 C CB  . LYS B 1 161 ? -30.07799 -0.35829  -43.21656 1.000 170.08122 ? 161 LYS B CB  1 
ATOM   2433 C CG  . LYS B 1 161 ? -28.69385 -0.51939  -42.61574 1.000 160.47351 ? 161 LYS B CG  1 
ATOM   2434 C CD  . LYS B 1 161 ? -27.84974 -1.43577  -43.48763 1.000 169.83888 ? 161 LYS B CD  1 
ATOM   2435 C CE  . LYS B 1 161 ? -27.27403 -2.58525  -42.68794 1.000 164.38822 ? 161 LYS B CE  1 
ATOM   2436 N NZ  . LYS B 1 161 ? -26.61432 -3.59135  -43.56298 1.000 170.37208 ? 161 LYS B NZ  1 
ATOM   2437 N N   . ASP B 1 162 ? -33.35216 0.40386   -42.98201 1.000 256.01304 ? 162 ASP B N   1 
ATOM   2438 C CA  . ASP B 1 162 ? -34.58331 0.48930   -43.75734 1.000 267.55481 ? 162 ASP B CA  1 
ATOM   2439 C C   . ASP B 1 162 ? -35.55054 1.44215   -43.07047 1.000 272.44547 ? 162 ASP B C   1 
ATOM   2440 O O   . ASP B 1 162 ? -35.99716 1.16133   -41.94617 1.000 268.12068 ? 162 ASP B O   1 
ATOM   2441 C CB  . ASP B 1 162 ? -35.20705 -0.89676  -43.91236 1.000 267.07254 ? 162 ASP B CB  1 
ATOM   2442 C CG  . ASP B 1 162 ? -36.64307 -0.83982  -44.35903 1.000 274.85781 ? 162 ASP B CG  1 
ATOM   2443 O OD1 . ASP B 1 162 ? -36.95494 -0.01976  -45.24664 1.000 284.30919 ? 162 ASP B OD1 1 
ATOM   2444 O OD2 . ASP B 1 162 ? -37.45294 -1.63055  -43.83249 1.000 265.00174 ? 162 ASP B OD2 1 
ATOM   2445 N N   . PRO B 1 163 ? -35.88383 2.57703   -43.69291 1.000 237.24892 ? 163 PRO B N   1 
ATOM   2446 C CA  . PRO B 1 163 ? -36.64807 3.61609   -42.98013 1.000 221.40454 ? 163 PRO B CA  1 
ATOM   2447 C C   . PRO B 1 163 ? -38.01249 3.17075   -42.48225 1.000 213.03160 ? 163 PRO B C   1 
ATOM   2448 O O   . PRO B 1 163 ? -38.46559 3.67124   -41.44554 1.000 197.09049 ? 163 PRO B O   1 
ATOM   2449 C CB  . PRO B 1 163 ? -36.77163 4.74005   -44.02082 1.000 213.46721 ? 163 PRO B CB  1 
ATOM   2450 C CG  . PRO B 1 163 ? -35.73236 4.44763   -45.05175 1.000 221.44983 ? 163 PRO B CG  1 
ATOM   2451 C CD  . PRO B 1 163 ? -35.56715 2.96533   -45.07578 1.000 233.78973 ? 163 PRO B CD  1 
ATOM   2452 N N   . LYS B 1 164 ? -38.69349 2.26137   -43.18527 1.000 219.44249 ? 164 LYS B N   1 
ATOM   2453 C CA  . LYS B 1 164 ? -40.03667 1.88517   -42.75874 1.000 208.02699 ? 164 LYS B CA  1 
ATOM   2454 C C   . LYS B 1 164 ? -40.04046 1.00672   -41.51308 1.000 191.21786 ? 164 LYS B C   1 
ATOM   2455 O O   . LYS B 1 164 ? -41.09775 0.84943   -40.89280 1.000 175.30292 ? 164 LYS B O   1 
ATOM   2456 C CB  . LYS B 1 164 ? -40.78311 1.18290   -43.89745 1.000 212.82908 ? 164 LYS B CB  1 
ATOM   2457 C CG  . LYS B 1 164 ? -39.99917 0.08821   -44.59653 1.000 226.11078 ? 164 LYS B CG  1 
ATOM   2458 C CD  . LYS B 1 164 ? -40.92088 -0.96300  -45.19881 1.000 221.09679 ? 164 LYS B CD  1 
ATOM   2459 C CE  . LYS B 1 164 ? -40.13503 -2.15289  -45.72574 1.000 224.24298 ? 164 LYS B CE  1 
ATOM   2460 N NZ  . LYS B 1 164 ? -41.00675 -3.33902  -45.95098 1.000 219.68253 ? 164 LYS B NZ  1 
ATOM   2461 N N   . ASP B 1 165 ? -38.89475 0.43830   -41.13035 1.000 191.02038 ? 165 ASP B N   1 
ATOM   2462 C CA  . ASP B 1 165 ? -38.79011 -0.30808  -39.88108 1.000 177.67468 ? 165 ASP B CA  1 
ATOM   2463 C C   . ASP B 1 165 ? -38.83860 0.58841   -38.65009 1.000 163.62852 ? 165 ASP B C   1 
ATOM   2464 O O   . ASP B 1 165 ? -38.92236 0.06747   -37.53246 1.000 149.94740 ? 165 ASP B O   1 
ATOM   2465 C CB  . ASP B 1 165 ? -37.50292 -1.13632  -39.86439 1.000 176.98156 ? 165 ASP B CB  1 
ATOM   2466 C CG  . ASP B 1 165 ? -37.51055 -2.24824  -40.89440 1.000 181.88554 ? 165 ASP B CG  1 
ATOM   2467 O OD1 . ASP B 1 165 ? -38.61180 -2.68709  -41.28580 1.000 176.21209 ? 165 ASP B OD1 1 
ATOM   2468 O OD2 . ASP B 1 165 ? -36.41651 -2.68123  -41.31615 1.000 178.57492 ? 165 ASP B OD2 1 
ATOM   2469 N N   . ALA B 1 166 ? -38.77976 1.90718   -38.82705 1.000 166.82945 ? 166 ALA B N   1 
ATOM   2470 C CA  . ALA B 1 166 ? -38.75828 2.84124   -37.71182 1.000 152.71317 ? 166 ALA B CA  1 
ATOM   2471 C C   . ALA B 1 166 ? -40.06513 2.79314   -36.92339 1.000 147.27507 ? 166 ALA B C   1 
ATOM   2472 O O   . ALA B 1 166 ? -41.12422 2.42217   -37.43681 1.000 149.09113 ? 166 ALA B O   1 
ATOM   2473 C CB  . ALA B 1 166 ? -38.50362 4.26359   -38.21077 1.000 156.10605 ? 166 ALA B CB  1 
ATOM   2474 N N   . THR B 1 167 ? -39.97451 3.19134   -35.65672 1.000 155.28601 ? 167 THR B N   1 
ATOM   2475 C CA  . THR B 1 167 ? -41.11253 3.17408   -34.74179 1.000 154.32240 ? 167 THR B CA  1 
ATOM   2476 C C   . THR B 1 167 ? -42.21818 4.12632   -35.20007 1.000 156.69768 ? 167 THR B C   1 
ATOM   2477 O O   . THR B 1 167 ? -42.24934 5.29760   -34.81923 1.000 156.99073 ? 167 THR B O   1 
ATOM   2478 C CB  . THR B 1 167 ? -40.68226 3.55512   -33.30514 1.000 144.44218 ? 167 THR B CB  1 
ATOM   2479 O OG1 . THR B 1 167 ? -39.54506 2.77394   -32.91556 1.000 131.31543 ? 167 THR B OG1 1 
ATOM   2480 C CG2 . THR B 1 167 ? -41.81565 3.30638   -32.32257 1.000 135.90950 ? 167 THR B CG2 1 
ATOM   2481 N N   . PRO B 1 184 ? -24.18275 12.83954  -38.63302 1.000 216.63803 ? 184 PRO B N   1 
ATOM   2482 C CA  . PRO B 1 184 ? -25.27936 12.35018  -37.79191 1.000 214.94938 ? 184 PRO B CA  1 
ATOM   2483 C C   . PRO B 1 184 ? -26.46515 11.81719  -38.59566 1.000 218.89825 ? 184 PRO B C   1 
ATOM   2484 O O   . PRO B 1 184 ? -27.56118 11.67868  -38.05054 1.000 229.17553 ? 184 PRO B O   1 
ATOM   2485 C CB  . PRO B 1 184 ? -25.68278 13.59680  -36.99491 1.000 206.65391 ? 184 PRO B CB  1 
ATOM   2486 C CG  . PRO B 1 184 ? -24.40782 14.35455  -36.86559 1.000 196.94244 ? 184 PRO B CG  1 
ATOM   2487 C CD  . PRO B 1 184 ? -23.75482 14.18660  -38.22137 1.000 220.31857 ? 184 PRO B CD  1 
ATOM   2488 N N   . GLN B 1 185 ? -26.24850 11.52128  -39.88046 1.000 200.42368 ? 185 GLN B N   1 
ATOM   2489 C CA  . GLN B 1 185 ? -27.33283 10.97449  -40.68808 1.000 191.48215 ? 185 GLN B CA  1 
ATOM   2490 C C   . GLN B 1 185 ? -27.68259 9.55030   -40.28325 1.000 184.02983 ? 185 GLN B C   1 
ATOM   2491 O O   . GLN B 1 185 ? -28.79556 9.09191   -40.56340 1.000 178.52218 ? 185 GLN B O   1 
ATOM   2492 C CB  . GLN B 1 185 ? -26.95432 11.03223  -42.16655 1.000 185.76563 ? 185 GLN B CB  1 
ATOM   2493 C CG  . GLN B 1 185 ? -26.69646 12.44475  -42.66606 1.000 186.97221 ? 185 GLN B CG  1 
ATOM   2494 C CD  . GLN B 1 185 ? -25.86494 12.47644  -43.93214 1.000 189.09772 ? 185 GLN B CD  1 
ATOM   2495 O OE1 . GLN B 1 185 ? -25.40137 11.44175  -44.41039 1.000 185.79063 ? 185 GLN B OE1 1 
ATOM   2496 N NE2 . GLN B 1 185 ? -25.66586 13.67083  -44.47945 1.000 193.37062 ? 185 GLN B NE2 1 
ATOM   2497 N N   . GLU B 1 186 ? -26.75614 8.84109   -39.65117 1.000 173.61929 ? 186 GLU B N   1 
ATOM   2498 C CA  . GLU B 1 186 ? -27.00463 7.50741   -39.13654 1.000 154.45159 ? 186 GLU B CA  1 
ATOM   2499 C C   . GLU B 1 186 ? -27.33542 7.64441   -37.65730 1.000 143.64751 ? 186 GLU B C   1 
ATOM   2500 O O   . GLU B 1 186 ? -26.84008 8.54982   -36.98160 1.000 144.51059 ? 186 GLU B O   1 
ATOM   2501 C CB  . GLU B 1 186 ? -25.79329 6.59557   -39.34388 1.000 150.83217 ? 186 GLU B CB  1 
ATOM   2502 C CG  . GLU B 1 186 ? -25.98241 5.49471   -40.39419 1.000 164.19951 ? 186 GLU B CG  1 
ATOM   2503 C CD  . GLU B 1 186 ? -27.11843 4.51778   -40.10438 1.000 157.60602 ? 186 GLU B CD  1 
ATOM   2504 O OE1 . GLU B 1 186 ? -27.80921 4.64404   -39.07020 1.000 149.75168 ? 186 GLU B OE1 1 
ATOM   2505 O OE2 . GLU B 1 186 ? -27.30685 3.59582   -40.92642 1.000 152.07902 ? 186 GLU B OE2 1 
ATOM   2506 N N   . PHE B 1 187 ? -28.16506 6.74514   -37.14656 1.000 129.08790 ? 187 PHE B N   1 
ATOM   2507 C CA  . PHE B 1 187 ? -28.58852 6.85073   -35.76074 1.000 124.26798 ? 187 PHE B CA  1 
ATOM   2508 C C   . PHE B 1 187 ? -28.50727 5.49099   -35.08641 1.000 123.17518 ? 187 PHE B C   1 
ATOM   2509 O O   . PHE B 1 187 ? -28.62079 4.44570   -35.73272 1.000 126.46005 ? 187 PHE B O   1 
ATOM   2510 C CB  . PHE B 1 187 ? -30.01791 7.40607   -35.66300 1.000 124.22375 ? 187 PHE B CB  1 
ATOM   2511 C CG  . PHE B 1 187 ? -30.23546 8.34252   -34.50324 1.000 134.38855 ? 187 PHE B CG  1 
ATOM   2512 C CD1 . PHE B 1 187 ? -29.40888 8.30655   -33.38751 1.000 116.45914 ? 187 PHE B CD1 1 
ATOM   2513 C CD2 . PHE B 1 187 ? -31.26462 9.26939   -34.53647 1.000 131.65280 ? 187 PHE B CD2 1 
ATOM   2514 C CE1 . PHE B 1 187 ? -29.61223 9.16794   -32.32524 1.000 112.59530 ? 187 PHE B CE1 1 
ATOM   2515 C CE2 . PHE B 1 187 ? -31.47257 10.13668  -33.47914 1.000 140.78432 ? 187 PHE B CE2 1 
ATOM   2516 C CZ  . PHE B 1 187 ? -30.64492 10.08602  -32.37174 1.000 132.76105 ? 187 PHE B CZ  1 
ATOM   2517 N N   . LEU B 1 188 ? -28.29802 5.52224   -33.77540 1.000 86.50635  ? 188 LEU B N   1 
ATOM   2518 C CA  . LEU B 1 188 ? -28.27658 4.33152   -32.94456 1.000 85.88839  ? 188 LEU B CA  1 
ATOM   2519 C C   . LEU B 1 188 ? -29.46929 4.35841   -32.00041 1.000 86.42354  ? 188 LEU B C   1 
ATOM   2520 O O   . LEU B 1 188 ? -29.69895 5.36065   -31.31609 1.000 94.24531  ? 188 LEU B O   1 
ATOM   2521 C CB  . LEU B 1 188 ? -26.97778 4.27337   -32.13875 1.000 82.46940  ? 188 LEU B CB  1 
ATOM   2522 C CG  . LEU B 1 188 ? -25.97741 3.16215   -32.43754 1.000 89.59084  ? 188 LEU B CG  1 
ATOM   2523 C CD1 . LEU B 1 188 ? -25.04213 2.98868   -31.25464 1.000 93.66203  ? 188 LEU B CD1 1 
ATOM   2524 C CD2 . LEU B 1 188 ? -26.68092 1.86149   -32.79022 1.000 85.55636  ? 188 LEU B CD2 1 
ATOM   2525 N N   . GLU B 1 189 ? -30.22026 3.26198   -31.95855 1.000 80.31864  ? 189 GLU B N   1 
ATOM   2526 C CA  . GLU B 1 189 ? -31.38424 3.13977   -31.09008 1.000 75.96461  ? 189 GLU B CA  1 
ATOM   2527 C C   . GLU B 1 189 ? -31.16965 2.02345   -30.08297 1.000 79.86366  ? 189 GLU B C   1 
ATOM   2528 O O   . GLU B 1 189 ? -30.85483 0.89148   -30.45962 1.000 68.54024  ? 189 GLU B O   1 
ATOM   2529 C CB  . GLU B 1 189 ? -32.68279 2.91041   -31.86389 1.000 86.18515  ? 189 GLU B CB  1 
ATOM   2530 C CG  . GLU B 1 189 ? -32.95491 3.93110   -32.94519 1.000 105.05873 ? 189 GLU B CG  1 
ATOM   2531 C CD  . GLU B 1 189 ? -34.44180 4.17343   -33.12363 1.000 120.32998 ? 189 GLU B CD  1 
ATOM   2532 O OE1 . GLU B 1 189 ? -35.19405 3.98064   -32.14263 1.000 126.64411 ? 189 GLU B OE1 1 
ATOM   2533 O OE2 . GLU B 1 189 ? -34.85890 4.56356   -34.23263 1.000 132.03541 ? 189 GLU B OE2 1 
ATOM   2534 N N   . PHE B 1 190 ? -31.33084 2.35414   -28.80809 1.000 73.08842  ? 190 PHE B N   1 
ATOM   2535 C CA  . PHE B 1 190 ? -31.32683 1.34584   -27.76177 1.000 69.17224  ? 190 PHE B CA  1 
ATOM   2536 C C   . PHE B 1 190 ? -32.63860 0.57186   -27.78599 1.000 69.48976  ? 190 PHE B C   1 
ATOM   2537 O O   . PHE B 1 190 ? -33.71212 1.14305   -27.99587 1.000 66.33369  ? 190 PHE B O   1 
ATOM   2538 C CB  . PHE B 1 190 ? -31.13396 2.00938   -26.40139 1.000 59.96130  ? 190 PHE B CB  1 
ATOM   2539 C CG  . PHE B 1 190 ? -31.30897 1.07923   -25.24026 1.000 64.83079  ? 190 PHE B CG  1 
ATOM   2540 C CD1 . PHE B 1 190 ? -30.33606 0.13707   -24.93839 1.000 57.52916  ? 190 PHE B CD1 1 
ATOM   2541 C CD2 . PHE B 1 190 ? -32.45076 1.14267   -24.45237 1.000 56.98356  ? 190 PHE B CD2 1 
ATOM   2542 C CE1 . PHE B 1 190 ? -30.49259 -0.71963  -23.86500 1.000 62.45100  ? 190 PHE B CE1 1 
ATOM   2543 C CE2 . PHE B 1 190 ? -32.61570 0.28892   -23.37646 1.000 57.16738  ? 190 PHE B CE2 1 
ATOM   2544 C CZ  . PHE B 1 190 ? -31.63276 -0.64466  -23.08170 1.000 60.56244  ? 190 PHE B CZ  1 
ATOM   2545 N N   . ARG B 1 191 ? -32.55561 -0.73667  -27.55100 1.000 59.13345  ? 191 ARG B N   1 
ATOM   2546 C CA  . ARG B 1 191 ? -33.74042 -1.58398  -27.55556 1.000 61.93898  ? 191 ARG B CA  1 
ATOM   2547 C C   . ARG B 1 191 ? -34.02495 -2.17500  -26.18162 1.000 62.80012  ? 191 ARG B C   1 
ATOM   2548 O O   . ARG B 1 191 ? -35.10255 -1.95015  -25.62448 1.000 70.47542  ? 191 ARG B O   1 
ATOM   2549 C CB  . ARG B 1 191 ? -33.57453 -2.70688  -28.58788 1.000 69.50245  ? 191 ARG B CB  1 
ATOM   2550 C CG  . ARG B 1 191 ? -33.54460 -2.23134  -30.02640 1.000 75.44109  ? 191 ARG B CG  1 
ATOM   2551 C CD  . ARG B 1 191 ? -34.92202 -1.80328  -30.48281 1.000 71.02242  ? 191 ARG B CD  1 
ATOM   2552 N NE  . ARG B 1 191 ? -34.88741 -1.19777  -31.80650 1.000 86.40837  ? 191 ARG B NE  1 
ATOM   2553 C CZ  . ARG B 1 191 ? -35.41972 -0.02344  -32.11009 1.000 87.05839  ? 191 ARG B CZ  1 
ATOM   2554 N NH1 . ARG B 1 191 ? -36.06028 0.69970   -31.20592 1.000 91.20713  ? 191 ARG B NH1 1 
ATOM   2555 N NH2 . ARG B 1 191 ? -35.31564 0.43134   -33.35498 1.000 93.06258  ? 191 ARG B NH2 1 
ATOM   2556 N N   . LEU B 1 192 ? -33.08546 -2.91996  -25.61110 1.000 62.49487  ? 192 LEU B N   1 
ATOM   2557 C CA  . LEU B 1 192 ? -33.31649 -3.55721  -24.32233 1.000 55.47390  ? 192 LEU B CA  1 
ATOM   2558 C C   . LEU B 1 192 ? -31.98981 -4.07362  -23.79128 1.000 59.18716  ? 192 LEU B C   1 
ATOM   2559 O O   . LEU B 1 192 ? -30.99253 -4.15518  -24.51462 1.000 60.17127  ? 192 LEU B O   1 
ATOM   2560 C CB  . LEU B 1 192 ? -34.34157 -4.69402  -24.42109 1.000 60.43131  ? 192 LEU B CB  1 
ATOM   2561 C CG  . LEU B 1 192 ? -33.83957 -6.05454  -24.90405 1.000 61.13811  ? 192 LEU B CG  1 
ATOM   2562 C CD1 . LEU B 1 192 ? -34.85196 -7.14626  -24.59717 1.000 61.44391  ? 192 LEU B CD1 1 
ATOM   2563 C CD2 . LEU B 1 192 ? -33.55442 -5.97992  -26.39614 1.000 54.49016  ? 192 LEU B CD2 1 
ATOM   2564 N N   . GLU B 1 193 ? -32.00317 -4.44483  -22.51524 1.000 58.65440  ? 193 GLU B N   1 
ATOM   2565 C CA  . GLU B 1 193 ? -30.83562 -4.97976  -21.84225 1.000 63.97689  ? 193 GLU B CA  1 
ATOM   2566 C C   . GLU B 1 193 ? -31.19316 -6.31466  -21.20409 1.000 68.54280  ? 193 GLU B C   1 
ATOM   2567 O O   . GLU B 1 193 ? -32.35815 -6.59849  -20.91059 1.000 65.44041  ? 193 GLU B O   1 
ATOM   2568 C CB  . GLU B 1 193 ? -30.28907 -4.03488  -20.76276 1.000 54.28034  ? 193 GLU B CB  1 
ATOM   2569 C CG  . GLU B 1 193 ? -31.01425 -4.13440  -19.43142 1.000 65.06245  ? 193 GLU B CG  1 
ATOM   2570 C CD  . GLU B 1 193 ? -30.94522 -2.85916  -18.60988 1.000 92.00813  ? 193 GLU B CD  1 
ATOM   2571 O OE1 . GLU B 1 193 ? -30.57694 -1.80339  -19.16779 1.000 101.47415 ? 193 GLU B OE1 1 
ATOM   2572 O OE2 . GLU B 1 193 ? -31.26339 -2.91749  -17.40130 1.000 101.81791 ? 193 GLU B OE2 1 
ATOM   2573 N N   . VAL B 1 194 ? -30.17284 -7.14366  -21.01109 1.000 53.13200  ? 194 VAL B N   1 
ATOM   2574 C CA  . VAL B 1 194 ? -30.31027 -8.39508  -20.28189 1.000 63.29039  ? 194 VAL B CA  1 
ATOM   2575 C C   . VAL B 1 194 ? -29.17381 -8.45457  -19.27243 1.000 54.56852  ? 194 VAL B C   1 
ATOM   2576 O O   . VAL B 1 194 ? -28.01923 -8.14411  -19.59068 1.000 57.98245  ? 194 VAL B O   1 
ATOM   2577 C CB  . VAL B 1 194 ? -30.31348 -9.63037  -21.21231 1.000 69.93549  ? 194 VAL B CB  1 
ATOM   2578 C CG1 . VAL B 1 194 ? -28.97611 -9.79519  -21.93360 1.000 61.64031  ? 194 VAL B CG1 1 
ATOM   2579 C CG2 . VAL B 1 194 ? -30.66723 -10.88483 -20.42175 1.000 68.82311  ? 194 VAL B CG2 1 
ATOM   2580 N N   . ILE B 1 195 ? -29.50554 -8.85784  -18.05320 1.000 56.53936  ? 195 ILE B N   1 
ATOM   2581 C CA  . ILE B 1 195 ? -28.58387 -8.82868  -16.92860 1.000 55.27713  ? 195 ILE B CA  1 
ATOM   2582 C C   . ILE B 1 195 ? -28.16314 -10.25700 -16.62693 1.000 75.82535  ? 195 ILE B C   1 
ATOM   2583 O O   . ILE B 1 195 ? -29.01294 -11.14401 -16.48429 1.000 63.62327  ? 195 ILE B O   1 
ATOM   2584 C CB  . ILE B 1 195 ? -29.22349 -8.15616  -15.70451 1.000 61.91951  ? 195 ILE B CB  1 
ATOM   2585 C CG1 . ILE B 1 195 ? -29.31396 -6.64355  -15.93569 1.000 65.12202  ? 195 ILE B CG1 1 
ATOM   2586 C CG2 . ILE B 1 195 ? -28.40816 -8.44866  -14.46100 1.000 59.10474  ? 195 ILE B CG2 1 
ATOM   2587 C CD1 . ILE B 1 195 ? -30.56670 -6.01258  -15.36748 1.000 68.47744  ? 195 ILE B CD1 1 
ATOM   2588 N N   . SER B 1 196 ? -26.85713 -10.46807 -16.50283 1.000 65.87547  ? 196 SER B N   1 
ATOM   2589 C CA  . SER B 1 196 ? -26.28646 -11.78595 -16.30224 1.000 68.98366  ? 196 SER B CA  1 
ATOM   2590 C C   . SER B 1 196 ? -26.36350 -12.18516 -14.83297 1.000 74.64595  ? 196 SER B C   1 
ATOM   2591 O O   . SER B 1 196 ? -26.72619 -11.39500 -13.95635 1.000 70.12720  ? 196 SER B O   1 
ATOM   2592 C CB  . SER B 1 196 ? -24.83769 -11.82500 -16.79088 1.000 69.14412  ? 196 SER B CB  1 
ATOM   2593 O OG  . SER B 1 196 ? -23.94518 -11.30002 -15.82223 1.000 63.09648  ? 196 SER B OG  1 
ATOM   2594 N N   . ASN B 1 197 ? -26.04650 -13.44589 -14.58052 1.000 60.94360  ? 197 ASN B N   1 
ATOM   2595 C CA  . ASN B 1 197 ? -25.91503 -13.94826 -13.22745 1.000 68.13393  ? 197 ASN B CA  1 
ATOM   2596 C C   . ASN B 1 197 ? -24.59939 -13.47217 -12.62479 1.000 69.54982  ? 197 ASN B C   1 
ATOM   2597 O O   . ASN B 1 197 ? -23.64697 -13.17144 -13.34890 1.000 70.90115  ? 197 ASN B O   1 
ATOM   2598 C CB  . ASN B 1 197 ? -25.98386 -15.47272 -13.23296 1.000 77.10810  ? 197 ASN B CB  1 
ATOM   2599 C CG  . ASN B 1 197 ? -27.36251 -15.98967 -13.59217 1.000 85.94999  ? 197 ASN B CG  1 
ATOM   2600 O OD1 . ASN B 1 197 ? -28.37719 -15.43366 -13.16996 1.000 95.46304  ? 197 ASN B OD1 1 
ATOM   2601 N ND2 . ASN B 1 197 ? -27.40647 -17.04919 -14.39051 1.000 87.85277  ? 197 ASN B ND2 1 
ATOM   2602 N N   . PRO B 1 198 ? -24.51915 -13.38977 -11.29727 1.000 66.91333  ? 198 PRO B N   1 
ATOM   2603 C CA  . PRO B 1 198 ? -23.27649 -12.92633 -10.66981 1.000 70.70492  ? 198 PRO B CA  1 
ATOM   2604 C C   . PRO B 1 198 ? -22.11001 -13.86149 -10.94785 1.000 71.37101  ? 198 PRO B C   1 
ATOM   2605 O O   . PRO B 1 198 ? -22.26663 -15.07916 -11.05718 1.000 71.62064  ? 198 PRO B O   1 
ATOM   2606 C CB  . PRO B 1 198 ? -23.61706 -12.89927 -9.17323  1.000 62.28397  ? 198 PRO B CB  1 
ATOM   2607 C CG  . PRO B 1 198 ? -25.10514 -12.93067 -9.10090  1.000 69.57125  ? 198 PRO B CG  1 
ATOM   2608 C CD  . PRO B 1 198 ? -25.56981 -13.67558 -10.30702 1.000 61.99398  ? 198 PRO B CD  1 
ATOM   2609 N N   . PHE B 1 199 ? -20.92849 -13.26443 -11.08499 1.000 67.21218  ? 199 PHE B N   1 
ATOM   2610 C CA  . PHE B 1 199 ? -19.69129 -14.00312 -11.27015 1.000 63.82101  ? 199 PHE B CA  1 
ATOM   2611 C C   . PHE B 1 199 ? -18.62533 -13.40627 -10.36406 1.000 71.30765  ? 199 PHE B C   1 
ATOM   2612 O O   . PHE B 1 199 ? -18.70036 -12.24203 -9.96457  1.000 77.46200  ? 199 PHE B O   1 
ATOM   2613 C CB  . PHE B 1 199 ? -19.21730 -13.98222 -12.73382 1.000 68.38176  ? 199 PHE B CB  1 
ATOM   2614 C CG  . PHE B 1 199 ? -18.84224 -12.61630 -13.23224 1.000 72.36272  ? 199 PHE B CG  1 
ATOM   2615 C CD1 . PHE B 1 199 ? -19.81771 -11.71173 -13.62233 1.000 65.50611  ? 199 PHE B CD1 1 
ATOM   2616 C CD2 . PHE B 1 199 ? -17.51245 -12.23092 -13.29448 1.000 77.88755  ? 199 PHE B CD2 1 
ATOM   2617 C CE1 . PHE B 1 199 ? -19.47212 -10.45494 -14.07863 1.000 71.23059  ? 199 PHE B CE1 1 
ATOM   2618 C CE2 . PHE B 1 199 ? -17.16018 -10.97148 -13.74169 1.000 66.80754  ? 199 PHE B CE2 1 
ATOM   2619 C CZ  . PHE B 1 199 ? -18.14002 -10.08378 -14.13778 1.000 71.40088  ? 199 PHE B CZ  1 
ATOM   2620 N N   . ILE B 1 200 ? -17.62391 -14.21881 -10.04558 1.000 58.70039  ? 200 ILE B N   1 
ATOM   2621 C CA  . ILE B 1 200 ? -16.63066 -13.88711 -9.03346  1.000 73.39803  ? 200 ILE B CA  1 
ATOM   2622 C C   . ILE B 1 200 ? -15.31242 -13.56489 -9.71627  1.000 72.50947  ? 200 ILE B C   1 
ATOM   2623 O O   . ILE B 1 200 ? -14.84422 -14.32611 -10.57088 1.000 66.94084  ? 200 ILE B O   1 
ATOM   2624 C CB  . ILE B 1 200 ? -16.46561 -15.02403 -8.01031  1.000 75.06960  ? 200 ILE B CB  1 
ATOM   2625 C CG1 . ILE B 1 200 ? -17.67253 -15.05697 -7.06953  1.000 87.13489  ? 200 ILE B CG1 1 
ATOM   2626 C CG2 . ILE B 1 200 ? -15.17795 -14.86009 -7.22724  1.000 83.52531  ? 200 ILE B CG2 1 
ATOM   2627 C CD1 . ILE B 1 200 ? -18.32378 -16.41173 -6.94500  1.000 88.18240  ? 200 ILE B CD1 1 
ATOM   2628 N N   . VAL B 1 201 ? -14.72798 -12.42777 -9.35310  1.000 70.74313  ? 201 VAL B N   1 
ATOM   2629 C CA  . VAL B 1 201 ? -13.38247 -12.06113 -9.76850  1.000 74.00498  ? 201 VAL B CA  1 
ATOM   2630 C C   . VAL B 1 201 ? -12.48555 -12.21421 -8.54974  1.000 75.01618  ? 201 VAL B C   1 
ATOM   2631 O O   . VAL B 1 201 ? -12.73848 -11.59938 -7.50703  1.000 71.89989  ? 201 VAL B O   1 
ATOM   2632 C CB  . VAL B 1 201 ? -13.32947 -10.62516 -10.31316 1.000 76.32121  ? 201 VAL B CB  1 
ATOM   2633 C CG1 . VAL B 1 201 ? -11.88920 -10.19103 -10.52783 1.000 69.82251  ? 201 VAL B CG1 1 
ATOM   2634 C CG2 . VAL B 1 201 ? -14.12628 -10.51325 -11.60274 1.000 76.07475  ? 201 VAL B CG2 1 
ATOM   2635 N N   . TYR B 1 202 ? -11.46092 -13.05193 -8.66460  1.000 72.16410  ? 202 TYR B N   1 
ATOM   2636 C CA  . TYR B 1 202 ? -10.59931 -13.37688 -7.53958  1.000 78.66105  ? 202 TYR B CA  1 
ATOM   2637 C C   . TYR B 1 202 ? -9.19071  -12.85691 -7.80664  1.000 77.43901  ? 202 TYR B C   1 
ATOM   2638 O O   . TYR B 1 202 ? -8.81121  -12.59144 -8.95004  1.000 78.21514  ? 202 TYR B O   1 
ATOM   2639 C CB  . TYR B 1 202 ? -10.59221 -14.89104 -7.27340  1.000 74.08882  ? 202 TYR B CB  1 
ATOM   2640 C CG  . TYR B 1 202 ? -10.14410 -15.72118 -8.45023  1.000 78.02987  ? 202 TYR B CG  1 
ATOM   2641 C CD1 . TYR B 1 202 ? -8.79583  -15.97442 -8.66900  1.000 75.09189  ? 202 TYR B CD1 1 
ATOM   2642 C CD2 . TYR B 1 202 ? -11.06155 -16.21795 -9.36569  1.000 74.13338  ? 202 TYR B CD2 1 
ATOM   2643 C CE1 . TYR B 1 202 ? -8.37462  -16.71753 -9.75256  1.000 70.66911  ? 202 TYR B CE1 1 
ATOM   2644 C CE2 . TYR B 1 202 ? -10.64910 -16.96290 -10.45460 1.000 74.09086  ? 202 TYR B CE2 1 
ATOM   2645 C CZ  . TYR B 1 202 ? -9.30512  -17.20759 -10.64293 1.000 67.41133  ? 202 TYR B CZ  1 
ATOM   2646 O OH  . TYR B 1 202 ? -8.88928  -17.94683 -11.72312 1.000 73.57572  ? 202 TYR B OH  1 
ATOM   2647 N N   . SER B 1 203 ? -8.41622  -12.70134 -6.73707  1.000 82.46954  ? 203 SER B N   1 
ATOM   2648 C CA  . SER B 1 203 ? -7.03813  -12.24065 -6.83224  1.000 96.01069  ? 203 SER B CA  1 
ATOM   2649 C C   . SER B 1 203 ? -6.08718  -13.35129 -6.40610  1.000 91.05192  ? 203 SER B C   1 
ATOM   2650 O O   . SER B 1 203 ? -6.37782  -14.10784 -5.47488  1.000 81.23815  ? 203 SER B O   1 
ATOM   2651 C CB  . SER B 1 203 ? -6.80196  -11.00576 -5.96210  1.000 90.91977  ? 203 SER B CB  1 
ATOM   2652 O OG  . SER B 1 203 ? -7.58875  -11.07093 -4.78883  1.000 109.33555 ? 203 SER B OG  1 
ATOM   2653 N N   . ALA B 1 204 ? -4.95143  -13.44241 -7.08792  1.000 92.19623  ? 204 ALA B N   1 
ATOM   2654 C CA  . ALA B 1 204 ? -3.92083  -14.42131 -6.77335  1.000 83.95717  ? 204 ALA B CA  1 
ATOM   2655 C C   . ALA B 1 204 ? -2.85886  -13.74655 -5.91386  1.000 86.36449  ? 204 ALA B C   1 
ATOM   2656 O O   . ALA B 1 204 ? -2.27980  -12.73202 -6.31935  1.000 110.59718 ? 204 ALA B O   1 
ATOM   2657 C CB  . ALA B 1 204 ? -3.30487  -15.00173 -8.04465  1.000 93.54159  ? 204 ALA B CB  1 
ATOM   2658 N N   . LYS B 1 205 ? -2.60136  -14.31142 -4.73773  1.000 85.18209  ? 205 LYS B N   1 
ATOM   2659 C CA  . LYS B 1 205 ? -1.58409  -13.76893 -3.85209  1.000 84.69905  ? 205 LYS B CA  1 
ATOM   2660 C C   . LYS B 1 205 ? -0.18947  -14.01897 -4.42013  1.000 86.66773  ? 205 LYS B C   1 
ATOM   2661 O O   . LYS B 1 205 ? 0.03210   -14.90305 -5.25124  1.000 97.86918  ? 205 LYS B O   1 
ATOM   2662 C CB  . LYS B 1 205 ? -1.70868  -14.36255 -2.44917  1.000 96.44599  ? 205 LYS B CB  1 
ATOM   2663 C CG  . LYS B 1 205 ? -2.90695  -13.84446 -1.66601  1.000 89.98067  ? 205 LYS B CG  1 
ATOM   2664 C CD  . LYS B 1 205 ? -3.53308  -14.93986 -0.81455  1.000 111.77074 ? 205 LYS B CD  1 
ATOM   2665 C CE  . LYS B 1 205 ? -3.66868  -14.50464 0.63652   1.000 114.13898 ? 205 LYS B CE  1 
ATOM   2666 N NZ  . LYS B 1 205 ? -4.74764  -15.25793 1.33482   1.000 120.14001 ? 205 LYS B NZ  1 
ATOM   2667 N N   . LYS B 1 206 ? 0.75870   -13.21892 -3.95319  1.000 98.08036  ? 206 LYS B N   1 
ATOM   2668 C CA  . LYS B 1 206 ? 2.15043   -13.32793 -4.35895  1.000 104.64025 ? 206 LYS B CA  1 
ATOM   2669 C C   . LYS B 1 206 ? 2.95033   -14.00630 -3.25696  1.000 111.11420 ? 206 LYS B C   1 
ATOM   2670 O O   . LYS B 1 206 ? 2.90325   -13.58885 -2.09509  1.000 112.98538 ? 206 LYS B O   1 
ATOM   2671 C CB  . LYS B 1 206 ? 2.72495   -11.94365 -4.66822  1.000 111.17071 ? 206 LYS B CB  1 
ATOM   2672 C CG  . LYS B 1 206 ? 2.80383   -11.62950 -6.15640  1.000 125.47626 ? 206 LYS B CG  1 
ATOM   2673 C CD  . LYS B 1 206 ? 3.45621   -10.27855 -6.41147  1.000 141.98037 ? 206 LYS B CD  1 
ATOM   2674 C CE  . LYS B 1 206 ? 4.10204   -10.21944 -7.79014  1.000 146.51633 ? 206 LYS B CE  1 
ATOM   2675 N NZ  . LYS B 1 206 ? 3.34347   -11.00952 -8.80474  1.000 133.48532 ? 206 LYS B NZ  1 
ATOM   2676 N N   . PHE B 1 207 ? 3.67195   -15.06276 -3.62560  1.000 112.12223 ? 207 PHE B N   1 
ATOM   2677 C CA  . PHE B 1 207 ? 4.50317   -15.82744 -2.69989  1.000 116.92043 ? 207 PHE B CA  1 
ATOM   2678 C C   . PHE B 1 207 ? 5.91714   -15.80803 -3.26431  1.000 129.78829 ? 207 PHE B C   1 
ATOM   2679 O O   . PHE B 1 207 ? 6.29806   -16.69038 -4.04993  1.000 140.74930 ? 207 PHE B O   1 
ATOM   2680 C CB  . PHE B 1 207 ? 3.98073   -17.25414 -2.53537  1.000 104.46021 ? 207 PHE B CB  1 
ATOM   2681 C CG  . PHE B 1 207 ? 2.63894   -17.33749 -1.85635  1.000 96.49279  ? 207 PHE B CG  1 
ATOM   2682 C CD1 . PHE B 1 207 ? 2.53733   -17.30465 -0.47501  1.000 98.55507  ? 207 PHE B CD1 1 
ATOM   2683 C CD2 . PHE B 1 207 ? 1.47480   -17.44519 -2.60761  1.000 92.54676  ? 207 PHE B CD2 1 
ATOM   2684 C CE1 . PHE B 1 207 ? 1.29826   -17.37831 0.14486   1.000 100.94551 ? 207 PHE B CE1 1 
ATOM   2685 C CE2 . PHE B 1 207 ? 0.23400   -17.52002 -1.99501  1.000 90.75882  ? 207 PHE B CE2 1 
ATOM   2686 C CZ  . PHE B 1 207 ? 0.14492   -17.48522 -0.61783  1.000 92.97641  ? 207 PHE B CZ  1 
ATOM   2687 N N   . PRO B 1 208 ? 6.72449   -14.81357 -2.89919  1.000 134.51941 ? 208 PRO B N   1 
ATOM   2688 C CA  . PRO B 1 208 ? 8.08142   -14.71805 -3.45356  1.000 141.15081 ? 208 PRO B CA  1 
ATOM   2689 C C   . PRO B 1 208 ? 8.93030   -15.90824 -3.03541  1.000 126.89536 ? 208 PRO B C   1 
ATOM   2690 O O   . PRO B 1 208 ? 8.91933   -16.32782 -1.87629  1.000 132.49926 ? 208 PRO B O   1 
ATOM   2691 C CB  . PRO B 1 208 ? 8.62154   -13.40213 -2.87935  1.000 149.93430 ? 208 PRO B CB  1 
ATOM   2692 C CG  . PRO B 1 208 ? 7.71158   -13.01682 -1.77198  1.000 149.48161 ? 208 PRO B CG  1 
ATOM   2693 C CD  . PRO B 1 208 ? 6.45724   -13.82604 -1.84004  1.000 142.05962 ? 208 PRO B CD  1 
ATOM   2694 N N   . GLY B 1 209 ? 9.66339   -16.46269 -4.00308  1.000 128.24080 ? 209 GLY B N   1 
ATOM   2695 C CA  . GLY B 1 209 ? 10.38389  -17.69661 -3.78764  1.000 126.55876 ? 209 GLY B CA  1 
ATOM   2696 C C   . GLY B 1 209 ? 9.54182   -18.93326 -3.96817  1.000 126.75511 ? 209 GLY B C   1 
ATOM   2697 O O   . GLY B 1 209 ? 10.09005  -20.04284 -3.99844  1.000 132.13064 ? 209 GLY B O   1 
ATOM   2698 N N   . LEU B 1 210 ? 8.22725   -18.77584 -4.07784  1.000 121.48148 ? 210 LEU B N   1 
ATOM   2699 C CA  . LEU B 1 210 ? 7.29526   -19.85466 -4.36462  1.000 119.57183 ? 210 LEU B CA  1 
ATOM   2700 C C   . LEU B 1 210 ? 6.57439   -19.64285 -5.68718  1.000 130.69515 ? 210 LEU B C   1 
ATOM   2701 O O   . LEU B 1 210 ? 6.56023   -20.54629 -6.53175  1.000 133.62142 ? 210 LEU B O   1 
ATOM   2702 C CB  . LEU B 1 210 ? 6.27882   -19.96931 -3.21987  1.000 118.13922 ? 210 LEU B CB  1 
ATOM   2703 C CG  . LEU B 1 210 ? 5.41495   -21.22395 -3.16314  1.000 117.86363 ? 210 LEU B CG  1 
ATOM   2704 C CD1 . LEU B 1 210 ? 6.30386   -22.44486 -2.95485  1.000 105.62837 ? 210 LEU B CD1 1 
ATOM   2705 C CD2 . LEU B 1 210 ? 4.36246   -21.10192 -2.07639  1.000 100.85058 ? 210 LEU B CD2 1 
ATOM   2706 N N   . THR B 1 211 ? 5.97816   -18.46702 -5.89582  1.000 134.29977 ? 211 THR B N   1 
ATOM   2707 C CA  . THR B 1 211 ? 5.30101   -18.11240 -7.14109  1.000 141.80999 ? 211 THR B CA  1 
ATOM   2708 C C   . THR B 1 211 ? 6.05743   -17.03517 -7.91570  1.000 164.45533 ? 211 THR B C   1 
ATOM   2709 O O   . THR B 1 211 ? 5.44927   -16.16714 -8.54698  1.000 170.40159 ? 211 THR B O   1 
ATOM   2710 C CB  . THR B 1 211 ? 3.87879   -17.62714 -6.87139  1.000 139.10631 ? 211 THR B CB  1 
ATOM   2711 O OG1 . THR B 1 211 ? 3.91042   -16.24500 -6.49197  1.000 138.83438 ? 211 THR B OG1 1 
ATOM   2712 C CG2 . THR B 1 211 ? 3.25855   -18.40936 -5.75065  1.000 124.87466 ? 211 THR B CG2 1 
ATOM   2713 N N   . THR B 1 212 ? 7.38804   -17.07559 -7.86597  1.000 169.79923 ? 212 THR B N   1 
ATOM   2714 C CA  . THR B 1 212 ? 8.23908   -16.06636 -8.50267  1.000 177.42605 ? 212 THR B CA  1 
ATOM   2715 C C   . THR B 1 212 ? 7.91333   -14.65832 -8.00831  1.000 170.87100 ? 212 THR B C   1 
ATOM   2716 O O   . THR B 1 212 ? 8.61062   -14.11331 -7.15194  1.000 158.96833 ? 212 THR B O   1 
ATOM   2717 C CB  . THR B 1 212 ? 8.11910   -16.09924 -10.04502 1.000 185.90279 ? 212 THR B CB  1 
ATOM   2718 O OG1 . THR B 1 212 ? 8.50886   -17.38923 -10.53381 1.000 180.75104 ? 212 THR B OG1 1 
ATOM   2719 C CG2 . THR B 1 212 ? 9.00066   -15.02938 -10.67368 1.000 187.31224 ? 212 THR B CG2 1 
ATOM   2720 N N   . GLY C 1 15  ? -41.46345 54.71628  -9.96480  1.000 130.56183 ? 15  GLY C N   1 
ATOM   2721 C CA  . GLY C 1 15  ? -41.28812 53.56370  -9.10145  1.000 132.53925 ? 15  GLY C CA  1 
ATOM   2722 C C   . GLY C 1 15  ? -42.32830 53.48704  -8.00077  1.000 135.26006 ? 15  GLY C C   1 
ATOM   2723 O O   . GLY C 1 15  ? -42.33986 52.54502  -7.20891  1.000 138.52917 ? 15  GLY C O   1 
ATOM   2724 N N   . ASN C 1 16  ? -43.20895 54.48511  -7.95147  1.000 117.09446 ? 16  ASN C N   1 
ATOM   2725 C CA  . ASN C 1 16  ? -44.26897 54.52980  -6.95173  1.000 107.11805 ? 16  ASN C CA  1 
ATOM   2726 C C   . ASN C 1 16  ? -45.48946 53.70535  -7.34148  1.000 97.23148  ? 16  ASN C C   1 
ATOM   2727 O O   . ASN C 1 16  ? -46.44235 53.63438  -6.55693  1.000 84.84498  ? 16  ASN C O   1 
ATOM   2728 C CB  . ASN C 1 16  ? -44.69803 55.98197  -6.70981  1.000 110.01185 ? 16  ASN C CB  1 
ATOM   2729 C CG  . ASN C 1 16  ? -44.20046 56.53164  -5.38281  1.000 129.85884 ? 16  ASN C CG  1 
ATOM   2730 O OD1 . ASN C 1 16  ? -43.36943 55.91813  -4.71224  1.000 135.06004 ? 16  ASN C OD1 1 
ATOM   2731 N ND2 . ASN C 1 16  ? -44.69601 57.70613  -5.00763  1.000 125.48352 ? 16  ASN C ND2 1 
ATOM   2732 N N   . SER C 1 17  ? -45.49321 53.09533  -8.52623  1.000 90.33075  ? 17  SER C N   1 
ATOM   2733 C CA  . SER C 1 17  ? -46.68988 52.46965  -9.06659  1.000 97.34478  ? 17  SER C CA  1 
ATOM   2734 C C   . SER C 1 17  ? -46.33979 51.14870  -9.74333  1.000 94.35709  ? 17  SER C C   1 
ATOM   2735 O O   . SER C 1 17  ? -45.16977 50.81670  -9.95374  1.000 93.16501  ? 17  SER C O   1 
ATOM   2736 C CB  . SER C 1 17  ? -47.40605 53.40315  -10.05556 1.000 91.64159  ? 17  SER C CB  1 
ATOM   2737 O OG  . SER C 1 17  ? -47.03910 53.12347  -11.39652 1.000 104.17058 ? 17  SER C OG  1 
ATOM   2738 N N   . ASN C 1 18  ? -47.38352 50.38467  -10.06378 1.000 80.06861  ? 18  ASN C N   1 
ATOM   2739 C CA  . ASN C 1 18  ? -47.26265 49.15940  -10.84162 1.000 82.10937  ? 18  ASN C CA  1 
ATOM   2740 C C   . ASN C 1 18  ? -48.59031 48.91835  -11.54617 1.000 67.65138  ? 18  ASN C C   1 
ATOM   2741 O O   . ASN C 1 18  ? -49.64158 49.38451  -11.10006 1.000 80.28221  ? 18  ASN C O   1 
ATOM   2742 C CB  . ASN C 1 18  ? -46.87639 47.96635  -9.95825  1.000 76.97435  ? 18  ASN C CB  1 
ATOM   2743 C CG  . ASN C 1 18  ? -46.44245 46.75119  -10.76447 1.000 80.43535  ? 18  ASN C CG  1 
ATOM   2744 O OD1 . ASN C 1 18  ? -45.90542 46.87538  -11.86501 1.000 76.99052  ? 18  ASN C OD1 1 
ATOM   2745 N ND2 . ASN C 1 18  ? -46.66284 45.56664  -10.20681 1.000 79.93221  ? 18  ASN C ND2 1 
ATOM   2746 N N   . SER C 1 19  ? -48.54513 48.15469  -12.63481 1.000 70.06889  ? 19  SER C N   1 
ATOM   2747 C CA  . SER C 1 19  ? -49.76342 47.87159  -13.37894 1.000 84.33235  ? 19  SER C CA  1 
ATOM   2748 C C   . SER C 1 19  ? -49.72074 46.46948  -13.96818 1.000 91.95428  ? 19  SER C C   1 
ATOM   2749 O O   . SER C 1 19  ? -48.66687 46.00681  -14.41291 1.000 89.64278  ? 19  SER C O   1 
ATOM   2750 C CB  . SER C 1 19  ? -49.96952 48.90142  -14.49456 1.000 88.55817  ? 19  SER C CB  1 
ATOM   2751 O OG  . SER C 1 19  ? -51.34709 49.10807  -14.74707 1.000 110.96000 ? 19  SER C OG  1 
ATOM   2752 N N   . VAL C 1 20  ? -50.87857 45.80483  -13.97719 1.000 90.27185  ? 20  VAL C N   1 
ATOM   2753 C CA  . VAL C 1 20  ? -51.01632 44.47324  -14.54808 1.000 90.39872  ? 20  VAL C CA  1 
ATOM   2754 C C   . VAL C 1 20  ? -52.27939 44.44098  -15.40089 1.000 86.92294  ? 20  VAL C C   1 
ATOM   2755 O O   . VAL C 1 20  ? -53.18929 45.25667  -15.23883 1.000 86.23817  ? 20  VAL C O   1 
ATOM   2756 C CB  . VAL C 1 20  ? -51.05677 43.37836  -13.45602 1.000 86.85063  ? 20  VAL C CB  1 
ATOM   2757 C CG1 . VAL C 1 20  ? -52.47422 43.18892  -12.93666 1.000 80.00126  ? 20  VAL C CG1 1 
ATOM   2758 C CG2 . VAL C 1 20  ? -50.48707 42.06381  -13.98452 1.000 83.00759  ? 20  VAL C CG2 1 
ATOM   2759 N N   . SER C 1 21  ? -52.32908 43.47389  -16.31550 1.000 90.97899  ? 21  SER C N   1 
ATOM   2760 C CA  . SER C 1 21  ? -53.43663 43.33949  -17.25010 1.000 85.38961  ? 21  SER C CA  1 
ATOM   2761 C C   . SER C 1 21  ? -53.88418 41.88787  -17.34715 1.000 85.79689  ? 21  SER C C   1 
ATOM   2762 O O   . SER C 1 21  ? -53.07919 40.95984  -17.23192 1.000 85.79578  ? 21  SER C O   1 
ATOM   2763 C CB  . SER C 1 21  ? -53.06734 43.86113  -18.65186 1.000 85.60608  ? 21  SER C CB  1 
ATOM   2764 O OG  . SER C 1 21  ? -51.70414 43.62112  -18.95432 1.000 100.87760 ? 21  SER C OG  1 
ATOM   2765 N N   . ARG C 1 22  ? -55.18378 41.70402  -17.56703 1.000 78.86512  ? 22  ARG C N   1 
ATOM   2766 C CA  . ARG C 1 22  ? -55.76352 40.38949  -17.78302 1.000 85.99499  ? 22  ARG C CA  1 
ATOM   2767 C C   . ARG C 1 22  ? -56.82313 40.52102  -18.86866 1.000 94.96903  ? 22  ARG C C   1 
ATOM   2768 O O   . ARG C 1 22  ? -57.11915 41.62126  -19.34585 1.000 93.45642  ? 22  ARG C O   1 
ATOM   2769 C CB  . ARG C 1 22  ? -56.34666 39.80869  -16.48956 1.000 79.96827  ? 22  ARG C CB  1 
ATOM   2770 C CG  . ARG C 1 22  ? -57.65037 40.43642  -16.04685 1.000 84.12474  ? 22  ARG C CG  1 
ATOM   2771 C CD  . ARG C 1 22  ? -58.18632 39.75229  -14.79961 1.000 91.54736  ? 22  ARG C CD  1 
ATOM   2772 N NE  . ARG C 1 22  ? -59.34388 40.44970  -14.25643 1.000 94.66817  ? 22  ARG C NE  1 
ATOM   2773 C CZ  . ARG C 1 22  ? -60.59628 40.17751  -14.59473 1.000 104.71242 ? 22  ARG C CZ  1 
ATOM   2774 N NH1 . ARG C 1 22  ? -60.88451 39.22119  -15.46271 1.000 105.34955 ? 22  ARG C NH1 1 
ATOM   2775 N NH2 . ARG C 1 22  ? -61.58444 40.88127  -14.04974 1.000 109.99017 ? 22  ARG C NH2 1 
ATOM   2776 N N   . ILE C 1 23  ? -57.39899 39.39191  -19.26821 1.000 105.84483 ? 23  ILE C N   1 
ATOM   2777 C CA  . ILE C 1 23  ? -58.39444 39.36431  -20.33052 1.000 101.73080 ? 23  ILE C CA  1 
ATOM   2778 C C   . ILE C 1 23  ? -59.62223 38.63919  -19.80465 1.000 99.87809  ? 23  ILE C C   1 
ATOM   2779 O O   . ILE C 1 23  ? -59.50501 37.57008  -19.19672 1.000 99.50294  ? 23  ILE C O   1 
ATOM   2780 C CB  . ILE C 1 23  ? -57.85609 38.68812  -21.60448 1.000 87.76723  ? 23  ILE C CB  1 
ATOM   2781 C CG1 . ILE C 1 23  ? -57.12706 39.71411  -22.47493 1.000 96.35022  ? 23  ILE C CG1 1 
ATOM   2782 C CG2 . ILE C 1 23  ? -58.98986 38.06628  -22.38911 1.000 90.21233  ? 23  ILE C CG2 1 
ATOM   2783 C CD1 . ILE C 1 23  ? -56.14982 39.10503  -23.45679 1.000 87.72099  ? 23  ILE C CD1 1 
ATOM   2784 N N   . THR C 1 24  ? -60.79292 39.22637  -20.02926 1.000 110.17376 ? 24  THR C N   1 
ATOM   2785 C CA  . THR C 1 24  ? -62.04486 38.68524  -19.53177 1.000 124.28789 ? 24  THR C CA  1 
ATOM   2786 C C   . THR C 1 24  ? -62.64722 37.70029  -20.53016 1.000 127.58808 ? 24  THR C C   1 
ATOM   2787 O O   . THR C 1 24  ? -62.11199 37.45481  -21.61411 1.000 119.14422 ? 24  THR C O   1 
ATOM   2788 C CB  . THR C 1 24  ? -63.03551 39.80943  -19.23346 1.000 121.87958 ? 24  THR C CB  1 
ATOM   2789 O OG1 . THR C 1 24  ? -63.27938 40.56370  -20.42720 1.000 121.26219 ? 24  THR C OG1 1 
ATOM   2790 C CG2 . THR C 1 24  ? -62.47922 40.73064  -18.16865 1.000 111.82692 ? 24  THR C CG2 1 
ATOM   2791 N N   . ARG C 1 25  ? -63.78637 37.12302  -20.14414 1.000 133.66459 ? 25  ARG C N   1 
ATOM   2792 C CA  . ARG C 1 25  ? -64.48155 36.17795  -21.00884 1.000 133.27461 ? 25  ARG C CA  1 
ATOM   2793 C C   . ARG C 1 25  ? -65.05143 36.87070  -22.23813 1.000 128.41603 ? 25  ARG C C   1 
ATOM   2794 O O   . ARG C 1 25  ? -65.17730 36.24587  -23.29731 1.000 123.31061 ? 25  ARG C O   1 
ATOM   2795 C CB  . ARG C 1 25  ? -65.58595 35.46026  -20.23489 1.000 138.94501 ? 25  ARG C CB  1 
ATOM   2796 C CG  . ARG C 1 25  ? -65.06722 34.46605  -19.20902 1.000 151.96556 ? 25  ARG C CG  1 
ATOM   2797 C CD  . ARG C 1 25  ? -65.93650 33.21810  -19.16816 1.000 169.61047 ? 25  ARG C CD  1 
ATOM   2798 N NE  . ARG C 1 25  ? -66.68989 33.11063  -17.92461 1.000 173.10133 ? 25  ARG C NE  1 
ATOM   2799 C CZ  . ARG C 1 25  ? -66.32772 32.36242  -16.89121 1.000 170.51893 ? 25  ARG C CZ  1 
ATOM   2800 N NH1 . ARG C 1 25  ? -65.21478 31.64693  -16.91159 1.000 169.29990 ? 25  ARG C NH1 1 
ATOM   2801 N NH2 . ARG C 1 25  ? -67.09931 32.33474  -15.80821 1.000 174.99101 ? 25  ARG C NH2 1 
ATOM   2802 N N   . GLU C 1 26  ? -65.39561 38.15227  -22.12232 1.000 119.20507 ? 26  GLU C N   1 
ATOM   2803 C CA  . GLU C 1 26  ? -65.91751 38.89562  -23.25869 1.000 119.68473 ? 26  GLU C CA  1 
ATOM   2804 C C   . GLU C 1 26  ? -64.82040 39.39657  -24.18588 1.000 124.99290 ? 26  GLU C C   1 
ATOM   2805 O O   . GLU C 1 26  ? -65.13059 40.04768  -25.18949 1.000 116.52023 ? 26  GLU C O   1 
ATOM   2806 C CB  . GLU C 1 26  ? -66.71385 40.10233  -22.76384 1.000 118.70132 ? 26  GLU C CB  1 
ATOM   2807 C CG  . GLU C 1 26  ? -67.44815 39.88627  -21.45614 1.000 130.36342 ? 26  GLU C CG  1 
ATOM   2808 C CD  . GLU C 1 26  ? -68.13823 41.15020  -20.97408 1.000 145.53473 ? 26  GLU C CD  1 
ATOM   2809 O OE1 . GLU C 1 26  ? -68.00506 42.19390  -21.64743 1.000 142.19407 ? 26  GLU C OE1 1 
ATOM   2810 O OE2 . GLU C 1 26  ? -68.80265 41.10666  -19.91816 1.000 145.51674 ? 26  GLU C OE2 1 
ATOM   2811 N N   . GLY C 1 27  ? -63.55539 39.12731  -23.86992 1.000 120.46718 ? 27  GLY C N   1 
ATOM   2812 C CA  . GLY C 1 27  ? -62.44855 39.52138  -24.71221 1.000 120.53525 ? 27  GLY C CA  1 
ATOM   2813 C C   . GLY C 1 27  ? -61.89084 40.89753  -24.43351 1.000 118.57447 ? 27  GLY C C   1 
ATOM   2814 O O   . GLY C 1 27  ? -60.97572 41.33239  -25.14404 1.000 120.31893 ? 27  GLY C O   1 
ATOM   2815 N N   . LYS C 1 28  ? -62.41153 41.59886  -23.43195 1.000 121.45011 ? 28  LYS C N   1 
ATOM   2816 C CA  . LYS C 1 28  ? -61.89455 42.91102  -23.07220 1.000 131.50363 ? 28  LYS C CA  1 
ATOM   2817 C C   . LYS C 1 28  ? -60.68645 42.79644  -22.15284 1.000 116.15744 ? 28  LYS C C   1 
ATOM   2818 O O   . LYS C 1 28  ? -60.68167 42.00331  -21.20573 1.000 112.33949 ? 28  LYS C O   1 
ATOM   2819 C CB  . LYS C 1 28  ? -62.98646 43.75287  -22.41202 1.000 120.70964 ? 28  LYS C CB  1 
ATOM   2820 C CG  . LYS C 1 28  ? -64.20257 43.96685  -23.29426 1.000 136.29675 ? 28  LYS C CG  1 
ATOM   2821 C CD  . LYS C 1 28  ? -65.41902 44.36760  -22.48271 1.000 151.13068 ? 28  LYS C CD  1 
ATOM   2822 C CE  . LYS C 1 28  ? -66.62350 44.59361  -23.38388 1.000 156.80814 ? 28  LYS C CE  1 
ATOM   2823 N NZ  . LYS C 1 28  ? -67.85503 44.89606  -22.60297 1.000 156.48982 ? 28  LYS C NZ  1 
ATOM   2824 N N   . LYS C 1 29  ? -59.65485 43.57728  -22.45317 1.000 108.32813 ? 29  LYS C N   1 
ATOM   2825 C CA  . LYS C 1 29  ? -58.49250 43.67406  -21.58690 1.000 99.85972  ? 29  LYS C CA  1 
ATOM   2826 C C   . LYS C 1 29  ? -58.83667 44.54874  -20.38758 1.000 93.72779  ? 29  LYS C C   1 
ATOM   2827 O O   . LYS C 1 29  ? -59.48404 45.59076  -20.52764 1.000 94.90070  ? 29  LYS C O   1 
ATOM   2828 C CB  . LYS C 1 29  ? -57.30557 44.25668  -22.35203 1.000 90.34635  ? 29  LYS C CB  1 
ATOM   2829 C CG  . LYS C 1 29  ? -56.06732 44.48879  -21.51231 1.000 74.70942  ? 29  LYS C CG  1 
ATOM   2830 C CD  . LYS C 1 29  ? -54.83211 43.98704  -22.23610 1.000 83.48842  ? 29  LYS C CD  1 
ATOM   2831 C CE  . LYS C 1 29  ? -54.21726 45.08718  -23.08447 1.000 107.39309 ? 29  LYS C CE  1 
ATOM   2832 N NZ  . LYS C 1 29  ? -52.75704 44.88871  -23.28741 1.000 118.66583 ? 29  LYS C NZ  1 
ATOM   2833 N N   . ILE C 1 30  ? -58.40336 44.12332  -19.20447 1.000 77.59664  ? 30  ILE C N   1 
ATOM   2834 C CA  . ILE C 1 30  ? -58.65725 44.85121  -17.96676 1.000 76.36853  ? 30  ILE C CA  1 
ATOM   2835 C C   . ILE C 1 30  ? -57.33378 45.10522  -17.26487 1.000 79.03219  ? 30  ILE C C   1 
ATOM   2836 O O   . ILE C 1 30  ? -56.57096 44.16959  -17.00425 1.000 83.45279  ? 30  ILE C O   1 
ATOM   2837 C CB  . ILE C 1 30  ? -59.63750 44.10551  -17.04118 1.000 81.16508  ? 30  ILE C CB  1 
ATOM   2838 C CG1 . ILE C 1 30  ? -61.05488 44.18313  -17.61218 1.000 88.09177  ? 30  ILE C CG1 1 
ATOM   2839 C CG2 . ILE C 1 30  ? -59.57488 44.65917  -15.62348 1.000 68.26029  ? 30  ILE C CG2 1 
ATOM   2840 C CD1 . ILE C 1 30  ? -62.14226 43.99195  -16.57958 1.000 99.45292  ? 30  ILE C CD1 1 
ATOM   2841 N N   . THR C 1 31  ? -57.06694 46.37115  -16.96022 1.000 76.78191  ? 31  THR C N   1 
ATOM   2842 C CA  . THR C 1 31  ? -55.79671 46.80666  -16.40180 1.000 78.52483  ? 31  THR C CA  1 
ATOM   2843 C C   . THR C 1 31  ? -56.01939 47.34502  -14.99797 1.000 78.33176  ? 31  THR C C   1 
ATOM   2844 O O   . THR C 1 31  ? -56.90174 48.18065  -14.78101 1.000 85.15886  ? 31  THR C O   1 
ATOM   2845 C CB  . THR C 1 31  ? -55.15171 47.88903  -17.27735 1.000 86.42732  ? 31  THR C CB  1 
ATOM   2846 O OG1 . THR C 1 31  ? -55.30186 47.54917  -18.66314 1.000 84.82577  ? 31  THR C OG1 1 
ATOM   2847 C CG2 . THR C 1 31  ? -53.67729 48.05230  -16.93955 1.000 77.10898  ? 31  THR C CG2 1 
ATOM   2848 N N   . TYR C 1 32  ? -55.21617 46.86418  -14.05389 1.000 76.46523  ? 32  TYR C N   1 
ATOM   2849 C CA  . TYR C 1 32  ? -55.23092 47.32888  -12.67477 1.000 66.01257  ? 32  TYR C CA  1 
ATOM   2850 C C   . TYR C 1 32  ? -53.96025 48.12684  -12.44006 1.000 77.75556  ? 32  TYR C C   1 
ATOM   2851 O O   . TYR C 1 32  ? -52.85801 47.63395  -12.70080 1.000 83.38376  ? 32  TYR C O   1 
ATOM   2852 C CB  . TYR C 1 32  ? -55.31899 46.15695  -11.68882 1.000 67.30473  ? 32  TYR C CB  1 
ATOM   2853 C CG  . TYR C 1 32  ? -56.45179 45.19066  -11.96653 1.000 71.21101  ? 32  TYR C CG  1 
ATOM   2854 C CD1 . TYR C 1 32  ? -56.31790 44.17412  -12.90784 1.000 61.30496  ? 32  TYR C CD1 1 
ATOM   2855 C CD2 . TYR C 1 32  ? -57.65221 45.28803  -11.27235 1.000 69.24950  ? 32  TYR C CD2 1 
ATOM   2856 C CE1 . TYR C 1 32  ? -57.35692 43.29594  -13.16207 1.000 73.75839  ? 32  TYR C CE1 1 
ATOM   2857 C CE2 . TYR C 1 32  ? -58.69158 44.41587  -11.51544 1.000 74.19656  ? 32  TYR C CE2 1 
ATOM   2858 C CZ  . TYR C 1 32  ? -58.54050 43.42190  -12.45961 1.000 84.19440  ? 32  TYR C CZ  1 
ATOM   2859 O OH  . TYR C 1 32  ? -59.58100 42.55507  -12.69835 1.000 88.78541  ? 32  TYR C OH  1 
ATOM   2860 N N   . LYS C 1 33  ? -54.11588 49.35182  -11.94593 1.000 74.64511  ? 33  LYS C N   1 
ATOM   2861 C CA  . LYS C 1 33  ? -52.99271 50.23346  -11.65987 1.000 70.32447  ? 33  LYS C CA  1 
ATOM   2862 C C   . LYS C 1 33  ? -53.00221 50.56641  -10.17650 1.000 67.96359  ? 33  LYS C C   1 
ATOM   2863 O O   . LYS C 1 33  ? -53.98042 51.12001  -9.66302  1.000 69.78203  ? 33  LYS C O   1 
ATOM   2864 C CB  . LYS C 1 33  ? -53.05361 51.50169  -12.51452 1.000 69.43908  ? 33  LYS C CB  1 
ATOM   2865 C CG  . LYS C 1 33  ? -51.83841 52.40033  -12.36252 1.000 79.90676  ? 33  LYS C CG  1 
ATOM   2866 C CD  . LYS C 1 33  ? -52.16745 53.85146  -12.64877 1.000 88.91956  ? 33  LYS C CD  1 
ATOM   2867 C CE  . LYS C 1 33  ? -50.98829 54.55906  -13.29416 1.000 87.56139  ? 33  LYS C CE  1 
ATOM   2868 N NZ  . LYS C 1 33  ? -51.41578 55.80430  -13.98207 1.000 91.96216  ? 33  LYS C NZ  1 
ATOM   2869 N N   . LEU C 1 34  ? -51.91455 50.22147  -9.49927  1.000 64.65336  ? 34  LEU C N   1 
ATOM   2870 C CA  . LEU C 1 34  ? -51.68558 50.54622  -8.10220  1.000 64.21533  ? 34  LEU C CA  1 
ATOM   2871 C C   . LEU C 1 34  ? -50.61977 51.62311  -8.03260  1.000 73.89265  ? 34  LEU C C   1 
ATOM   2872 O O   . LEU C 1 34  ? -49.63680 51.57902  -8.77606  1.000 75.29425  ? 34  LEU C O   1 
ATOM   2873 C CB  . LEU C 1 34  ? -51.22210 49.31915  -7.31615  1.000 71.21118  ? 34  LEU C CB  1 
ATOM   2874 C CG  . LEU C 1 34  ? -52.26002 48.29567  -6.87647  1.000 67.84000  ? 34  LEU C CG  1 
ATOM   2875 C CD1 . LEU C 1 34  ? -51.58133 47.19239  -6.07309  1.000 68.26558  ? 34  LEU C CD1 1 
ATOM   2876 C CD2 . LEU C 1 34  ? -53.33176 48.97907  -6.05949  1.000 61.29529  ? 34  LEU C CD2 1 
ATOM   2877 N N   . ASN C 1 35  ? -50.82660 52.60283  -7.16070  1.000 66.95654  ? 35  ASN C N   1 
ATOM   2878 C CA  . ASN C 1 35  ? -49.85225 53.67128  -7.02498  1.000 77.20029  ? 35  ASN C CA  1 
ATOM   2879 C C   . ASN C 1 35  ? -49.89923 54.19094  -5.59824  1.000 69.13514  ? 35  ASN C C   1 
ATOM   2880 O O   . ASN C 1 35  ? -50.98136 54.44451  -5.06184  1.000 74.58483  ? 35  ASN C O   1 
ATOM   2881 C CB  . ASN C 1 35  ? -50.15322 54.78641  -8.03903  1.000 72.04978  ? 35  ASN C CB  1 
ATOM   2882 C CG  . ASN C 1 35  ? -49.58393 56.13105  -7.63857  1.000 89.90546  ? 35  ASN C CG  1 
ATOM   2883 O OD1 . ASN C 1 35  ? -48.54619 56.22012  -6.98095  1.000 108.31602 ? 35  ASN C OD1 1 
ATOM   2884 N ND2 . ASN C 1 35  ? -50.27046 57.19555  -8.03594  1.000 114.12272 ? 35  ASN C ND2 1 
ATOM   2885 N N   . ILE C 1 36  ? -48.72767 54.32509  -4.98600  1.000 71.19451  ? 36  ILE C N   1 
ATOM   2886 C CA  . ILE C 1 36  ? -48.63647 54.65638  -3.56929  1.000 70.14037  ? 36  ILE C CA  1 
ATOM   2887 C C   . ILE C 1 36  ? -48.74339 56.17166  -3.45212  1.000 83.52835  ? 36  ILE C C   1 
ATOM   2888 O O   . ILE C 1 36  ? -47.91276 56.90700  -3.99602  1.000 75.63758  ? 36  ILE C O   1 
ATOM   2889 C CB  . ILE C 1 36  ? -47.33212 54.12903  -2.95948  1.000 80.61242  ? 36  ILE C CB  1 
ATOM   2890 C CG1 . ILE C 1 36  ? -47.30139 52.59925  -3.05941  1.000 69.31701  ? 36  ILE C CG1 1 
ATOM   2891 C CG2 . ILE C 1 36  ? -47.19033 54.60017  -1.51912  1.000 71.54405  ? 36  ILE C CG2 1 
ATOM   2892 C CD1 . ILE C 1 36  ? -46.02518 51.97687  -2.57665  1.000 70.95016  ? 36  ILE C CD1 1 
ATOM   2893 N N   . MET C 1 37  ? -49.77227 56.63715  -2.74304  1.000 76.58422  ? 37  MET C N   1 
ATOM   2894 C CA  . MET C 1 37  ? -49.96218 58.06025  -2.48197  1.000 73.85451  ? 37  MET C CA  1 
ATOM   2895 C C   . MET C 1 37  ? -49.12745 58.55942  -1.30789  1.000 74.97295  ? 37  MET C C   1 
ATOM   2896 O O   . MET C 1 37  ? -48.54876 59.64893  -1.37450  1.000 90.93030  ? 37  MET C O   1 
ATOM   2897 C CB  . MET C 1 37  ? -51.44427 58.33862  -2.24451  1.000 81.60109  ? 37  MET C CB  1 
ATOM   2898 C CG  . MET C 1 37  ? -52.29967 58.22507  -3.49908  1.000 84.16726  ? 37  MET C CG  1 
ATOM   2899 S SD  . MET C 1 37  ? -51.34950 58.24824  -5.03203  1.000 92.77345  ? 37  MET C SD  1 
ATOM   2900 C CE  . MET C 1 37  ? -51.21716 60.01338  -5.32230  1.000 92.74356  ? 37  MET C CE  1 
ATOM   2901 N N   . GLN C 1 38  ? -49.06927 57.79338  -0.22377  1.000 75.78616  ? 38  GLN C N   1 
ATOM   2902 C CA  . GLN C 1 38  ? -48.39801 58.20253  1.00538   1.000 74.35749  ? 38  GLN C CA  1 
ATOM   2903 C C   . GLN C 1 38  ? -47.44680 57.09060  1.42622   1.000 78.01378  ? 38  GLN C C   1 
ATOM   2904 O O   . GLN C 1 38  ? -47.88203 56.01058  1.83984   1.000 72.01596  ? 38  GLN C O   1 
ATOM   2905 C CB  . GLN C 1 38  ? -49.41026 58.50948  2.11027   1.000 73.44340  ? 38  GLN C CB  1 
ATOM   2906 C CG  . GLN C 1 38  ? -48.77896 58.91553  3.42846   1.000 74.72726  ? 38  GLN C CG  1 
ATOM   2907 C CD  . GLN C 1 38  ? -49.59068 59.94932  4.18016   1.000 76.74599  ? 38  GLN C CD  1 
ATOM   2908 O OE1 . GLN C 1 38  ? -49.34834 61.15464  4.06211   1.000 88.13168  ? 38  GLN C OE1 1 
ATOM   2909 N NE2 . GLN C 1 38  ? -50.55502 59.48582  4.96845   1.000 73.94410  ? 38  GLN C NE2 1 
ATOM   2910 N N   . GLN C 1 39  ? -46.16224 57.34406  1.28988   1.000 79.12199  ? 39  GLN C N   1 
ATOM   2911 C CA  . GLN C 1 39  ? -45.16751 56.35153  1.63681   1.000 78.43321  ? 39  GLN C CA  1 
ATOM   2912 C C   . GLN C 1 39  ? -44.98973 56.28408  3.15079   1.000 76.82897  ? 39  GLN C C   1 
ATOM   2913 O O   . GLN C 1 39  ? -45.16983 57.28170  3.85040   1.000 77.08949  ? 39  GLN C O   1 
ATOM   2914 C CB  . GLN C 1 39  ? -43.83652 56.68570  0.97992   1.000 76.42482  ? 39  GLN C CB  1 
ATOM   2915 C CG  . GLN C 1 39  ? -43.87867 56.56076  -0.52291  1.000 80.49461  ? 39  GLN C CG  1 
ATOM   2916 C CD  . GLN C 1 39  ? -43.61129 55.15765  -0.98934  1.000 82.34248  ? 39  GLN C CD  1 
ATOM   2917 O OE1 . GLN C 1 39  ? -43.27375 54.28062  -0.19562  1.000 83.47296  ? 39  GLN C OE1 1 
ATOM   2918 N NE2 . GLN C 1 39  ? -43.75818 54.93208  -2.28682  1.000 98.15444  ? 39  GLN C NE2 1 
ATOM   2919 N N   . PRO C 1 40  ? -44.68660 55.10684  3.68780   1.000 84.30967  ? 40  PRO C N   1 
ATOM   2920 C CA  . PRO C 1 40  ? -44.32347 55.03167  5.10457   1.000 73.89037  ? 40  PRO C CA  1 
ATOM   2921 C C   . PRO C 1 40  ? -42.93652 55.60226  5.33267   1.000 74.14465  ? 40  PRO C C   1 
ATOM   2922 O O   . PRO C 1 40  ? -42.03757 55.44994  4.50202   1.000 84.01212  ? 40  PRO C O   1 
ATOM   2923 C CB  . PRO C 1 40  ? -44.34991 53.52938  5.39601   1.000 79.93950  ? 40  PRO C CB  1 
ATOM   2924 C CG  . PRO C 1 40  ? -44.02500 52.90393  4.08461   1.000 79.85511  ? 40  PRO C CG  1 
ATOM   2925 C CD  . PRO C 1 40  ? -44.62324 53.79213  3.02740   1.000 77.59820  ? 40  PRO C CD  1 
ATOM   2926 N N   . LYS C 1 41  ? -42.76413 56.26347  6.46995   1.000 69.14790  ? 41  LYS C N   1 
ATOM   2927 C CA  . LYS C 1 41  ? -41.51387 56.95419  6.74973   1.000 76.73070  ? 41  LYS C CA  1 
ATOM   2928 C C   . LYS C 1 41  ? -40.78677 56.36603  7.94588   1.000 76.79395  ? 41  LYS C C   1 
ATOM   2929 O O   . LYS C 1 41  ? -39.60206 56.02907  7.84171   1.000 79.37722  ? 41  LYS C O   1 
ATOM   2930 C CB  . LYS C 1 41  ? -41.76378 58.46075  6.96659   1.000 84.25077  ? 41  LYS C CB  1 
ATOM   2931 C CG  . LYS C 1 41  ? -41.92506 59.25551  5.67321   1.000 79.27517  ? 41  LYS C CG  1 
ATOM   2932 C CD  . LYS C 1 41  ? -40.78654 58.95575  4.70714   1.000 82.14285  ? 41  LYS C CD  1 
ATOM   2933 C CE  . LYS C 1 41  ? -41.21109 59.10462  3.24868   1.000 105.15353 ? 41  LYS C CE  1 
ATOM   2934 N NZ  . LYS C 1 41  ? -40.65826 57.99214  2.39640   1.000 106.73891 ? 41  LYS C NZ  1 
ATOM   2935 N N   . ARG C 1 42  ? -41.46386 56.24175  9.08628   1.000 78.52583  ? 42  ARG C N   1 
ATOM   2936 C CA  . ARG C 1 42  ? -40.79946 55.84112  10.31409  1.000 76.67470  ? 42  ARG C CA  1 
ATOM   2937 C C   . ARG C 1 42  ? -41.75604 55.08063  11.21075  1.000 79.99621  ? 42  ARG C C   1 
ATOM   2938 O O   . ARG C 1 42  ? -42.97888 55.18957  11.09312  1.000 80.31774  ? 42  ARG C O   1 
ATOM   2939 C CB  . ARG C 1 42  ? -40.26051 57.03778  11.08637  1.000 75.35577  ? 42  ARG C CB  1 
ATOM   2940 C CG  . ARG C 1 42  ? -41.31377 57.97375  11.68135  1.000 97.63306  ? 42  ARG C CG  1 
ATOM   2941 C CD  . ARG C 1 42  ? -41.55097 57.65617  13.16532  1.000 97.18233  ? 42  ARG C CD  1 
ATOM   2942 N NE  . ARG C 1 42  ? -42.79101 58.22265  13.68014  1.000 78.68877  ? 42  ARG C NE  1 
ATOM   2943 C CZ  . ARG C 1 42  ? -42.85740 59.31016  14.43665  1.000 90.38863  ? 42  ARG C CZ  1 
ATOM   2944 N NH1 . ARG C 1 42  ? -41.77196 59.98998  14.76846  1.000 96.79007  ? 42  ARG C NH1 1 
ATOM   2945 N NH2 . ARG C 1 42  ? -44.04481 59.74042  14.85172  1.000 89.08295  ? 42  ARG C NH2 1 
ATOM   2946 N N   . ALA C 1 43  ? -41.17126 54.32410  12.13023  1.000 87.51156  ? 43  ALA C N   1 
ATOM   2947 C CA  . ALA C 1 43  ? -41.93823 53.65973  13.16838  1.000 90.60170  ? 43  ALA C CA  1 
ATOM   2948 C C   . ALA C 1 43  ? -41.00089 53.38332  14.33086  1.000 80.36935  ? 43  ALA C C   1 
ATOM   2949 O O   . ALA C 1 43  ? -39.78772 53.26046  14.14974  1.000 80.66046  ? 43  ALA C O   1 
ATOM   2950 C CB  . ALA C 1 43  ? -42.58131 52.36217  12.66368  1.000 77.81172  ? 43  ALA C CB  1 
ATOM   2951 N N   . ARG C 1 44  ? -41.57690 53.27597  15.52058  1.000 90.77669  ? 44  ARG C N   1 
ATOM   2952 C CA  . ARG C 1 44  ? -40.82561 52.94059  16.71976  1.000 92.66034  ? 44  ARG C CA  1 
ATOM   2953 C C   . ARG C 1 44  ? -41.06464 51.46976  17.01808  1.000 88.34240  ? 44  ARG C C   1 
ATOM   2954 O O   . ARG C 1 44  ? -42.21621 51.02291  17.04836  1.000 88.55056  ? 44  ARG C O   1 
ATOM   2955 C CB  . ARG C 1 44  ? -41.27109 53.80159  17.90300  1.000 87.36637  ? 44  ARG C CB  1 
ATOM   2956 C CG  . ARG C 1 44  ? -40.44868 53.61744  19.16408  1.000 93.29940  ? 44  ARG C CG  1 
ATOM   2957 C CD  . ARG C 1 44  ? -41.24340 54.08544  20.37271  1.000 93.65047  ? 44  ARG C CD  1 
ATOM   2958 N NE  . ARG C 1 44  ? -41.06715 55.50274  20.66188  1.000 92.01508  ? 44  ARG C NE  1 
ATOM   2959 C CZ  . ARG C 1 44  ? -40.57951 55.96609  21.80432  1.000 94.58185  ? 44  ARG C CZ  1 
ATOM   2960 N NH1 . ARG C 1 44  ? -40.24547 55.15209  22.79224  1.000 98.16876  ? 44  ARG C NH1 1 
ATOM   2961 N NH2 . ARG C 1 44  ? -40.43421 57.27771  21.96529  1.000 93.68912  ? 44  ARG C NH2 1 
ATOM   2962 N N   . ALA C 1 45  ? -39.97682 50.72033  17.20345  1.000 90.17117  ? 45  ALA C N   1 
ATOM   2963 C CA  . ALA C 1 45  ? -40.08172 49.28698  17.44422  1.000 92.57852  ? 45  ALA C CA  1 
ATOM   2964 C C   . ALA C 1 45  ? -41.07567 49.00021  18.55737  1.000 95.08744  ? 45  ALA C C   1 
ATOM   2965 O O   . ALA C 1 45  ? -41.03615 49.62242  19.62140  1.000 106.20405 ? 45  ALA C O   1 
ATOM   2966 C CB  . ALA C 1 45  ? -38.70992 48.71027  17.79565  1.000 94.77498  ? 45  ALA C CB  1 
ATOM   2967 N N   . CYS C 1 46  ? -41.94866 48.03288  18.31902  1.000 95.57867  ? 46  CYS C N   1 
ATOM   2968 C CA  . CYS C 1 46  ? -42.98084 47.69448  19.28474  1.000 97.94707  ? 46  CYS C CA  1 
ATOM   2969 C C   . CYS C 1 46  ? -42.56407 46.55511  20.20081  1.000 101.94750 ? 46  CYS C C   1 
ATOM   2970 O O   . CYS C 1 46  ? -43.33590 46.17134  21.08395  1.000 110.66846 ? 46  CYS C O   1 
ATOM   2971 C CB  . CYS C 1 46  ? -44.30449 47.39053  18.57007  1.000 96.34072  ? 46  CYS C CB  1 
ATOM   2972 S SG  . CYS C 1 46  ? -44.39855 45.84920  17.67233  1.000 100.17062 ? 46  CYS C SG  1 
ATOM   2973 N N   . GLY C 1 47  ? -41.36262 46.01660  20.01491  1.000 102.74365 ? 47  GLY C N   1 
ATOM   2974 C CA  . GLY C 1 47  ? -40.90985 44.86578  20.76671  1.000 107.28947 ? 47  GLY C CA  1 
ATOM   2975 C C   . GLY C 1 47  ? -39.58832 45.10755  21.46096  1.000 113.83593 ? 47  GLY C C   1 
ATOM   2976 O O   . GLY C 1 47  ? -39.00093 44.18189  22.02945  1.000 122.76820 ? 47  GLY C O   1 
ATOM   2977 N N   . GLN C 1 48  ? -39.10835 46.35038  21.42574  1.000 119.59693 ? 48  GLN C N   1 
ATOM   2978 C CA  . GLN C 1 48  ? -37.79768 46.67480  21.97459  1.000 129.08322 ? 48  GLN C CA  1 
ATOM   2979 C C   . GLN C 1 48  ? -37.79504 48.10030  22.50308  1.000 124.43405 ? 48  GLN C C   1 
ATOM   2980 O O   . GLN C 1 48  ? -38.60043 48.94336  22.09431  1.000 119.91779 ? 48  GLN C O   1 
ATOM   2981 C CB  . GLN C 1 48  ? -36.69140 46.54503  20.92052  1.000 123.98929 ? 48  GLN C CB  1 
ATOM   2982 C CG  . GLN C 1 48  ? -36.44465 45.15280  20.37475  1.000 136.89708 ? 48  GLN C CG  1 
ATOM   2983 C CD  . GLN C 1 48  ? -35.46707 45.16952  19.21823  1.000 137.01677 ? 48  GLN C CD  1 
ATOM   2984 O OE1 . GLN C 1 48  ? -35.03975 46.23463  18.77521  1.000 117.54193 ? 48  GLN C OE1 1 
ATOM   2985 N NE2 . GLN C 1 48  ? -35.09921 43.98980  18.72952  1.000 143.67690 ? 48  GLN C NE2 1 
ATOM   2986 N N   . GLY C 1 49  ? -36.87179 48.35175  23.42780  1.000 112.89961 ? 49  GLY C N   1 
ATOM   2987 C CA  . GLY C 1 49  ? -36.67143 49.67065  23.98265  1.000 109.89872 ? 49  GLY C CA  1 
ATOM   2988 C C   . GLY C 1 49  ? -37.81149 50.08444  24.89716  1.000 111.21982 ? 49  GLY C C   1 
ATOM   2989 O O   . GLY C 1 49  ? -38.53112 49.26244  25.47461  1.000 116.58051 ? 49  GLY C O   1 
ATOM   2990 N N   . SER C 1 50  ? -37.94864 51.40090  25.03324  1.000 109.82212 ? 50  SER C N   1 
ATOM   2991 C CA  . SER C 1 50  ? -38.98603 51.97433  25.87601  1.000 110.92130 ? 50  SER C CA  1 
ATOM   2992 C C   . SER C 1 50  ? -40.35678 51.50700  25.40208  1.000 118.47551 ? 50  SER C C   1 
ATOM   2993 O O   . SER C 1 50  ? -40.60644 51.38953  24.19876  1.000 110.50081 ? 50  SER C O   1 
ATOM   2994 C CB  . SER C 1 50  ? -38.90398 53.50124  25.84265  1.000 109.02461 ? 50  SER C CB  1 
ATOM   2995 O OG  . SER C 1 50  ? -40.04597 54.09138  26.43682  1.000 110.33801 ? 50  SER C OG  1 
ATOM   2996 N N   . LYS C 1 51  ? -41.25539 51.23618  26.34818  1.000 129.54678 ? 51  LYS C N   1 
ATOM   2997 C CA  . LYS C 1 51  ? -42.61364 50.86290  25.98357  1.000 124.09567 ? 51  LYS C CA  1 
ATOM   2998 C C   . LYS C 1 51  ? -43.59690 52.00344  26.20105  1.000 121.92275 ? 51  LYS C C   1 
ATOM   2999 O O   . LYS C 1 51  ? -44.80966 51.77216  26.26584  1.000 117.68298 ? 51  LYS C O   1 
ATOM   3000 C CB  . LYS C 1 51  ? -43.04646 49.61636  26.75513  1.000 138.85659 ? 51  LYS C CB  1 
ATOM   3001 C CG  . LYS C 1 51  ? -42.15411 48.41340  26.48991  1.000 139.31994 ? 51  LYS C CG  1 
ATOM   3002 C CD  . LYS C 1 51  ? -42.74182 47.13422  27.06343  1.000 145.46134 ? 51  LYS C CD  1 
ATOM   3003 C CE  . LYS C 1 51  ? -41.89685 45.92196  26.68590  1.000 150.89996 ? 51  LYS C CE  1 
ATOM   3004 N NZ  . LYS C 1 51  ? -42.50325 44.62744  27.11970  1.000 153.35519 ? 51  LYS C NZ  1 
ATOM   3005 N N   . SER C 1 52  ? -43.08838 53.22674  26.31280  1.000 116.01868 ? 52  SER C N   1 
ATOM   3006 C CA  . SER C 1 52  ? -43.88634 54.42686  26.48703  1.000 111.13985 ? 52  SER C CA  1 
ATOM   3007 C C   . SER C 1 52  ? -44.25062 54.95928  25.10634  1.000 107.97732 ? 52  SER C C   1 
ATOM   3008 O O   . SER C 1 52  ? -43.71029 54.51000  24.09202  1.000 105.42103 ? 52  SER C O   1 
ATOM   3009 C CB  . SER C 1 52  ? -43.12603 55.47551  27.29855  1.000 109.01814 ? 52  SER C CB  1 
ATOM   3010 O OG  . SER C 1 52  ? -42.75462 54.97017  28.56892  1.000 126.46159 ? 52  SER C OG  1 
ATOM   3011 N N   . HIS C 1 53  ? -45.13850 55.95463  25.07051  1.000 101.45620 ? 53  HIS C N   1 
ATOM   3012 C CA  . HIS C 1 53  ? -45.52227 56.59994  23.81426  1.000 105.74613 ? 53  HIS C CA  1 
ATOM   3013 C C   . HIS C 1 53  ? -45.82905 55.54357  22.74997  1.000 95.51851  ? 53  HIS C C   1 
ATOM   3014 O O   . HIS C 1 53  ? -45.12543 55.38756  21.75106  1.000 93.35436  ? 53  HIS C O   1 
ATOM   3015 C CB  . HIS C 1 53  ? -44.44105 57.58065  23.34670  1.000 105.37135 ? 53  HIS C CB  1 
ATOM   3016 C CG  . HIS C 1 53  ? -43.93874 58.48445  24.42955  1.000 99.58085  ? 53  HIS C CG  1 
ATOM   3017 N ND1 . HIS C 1 53  ? -44.57160 59.66325  24.75990  1.000 97.96467  ? 53  HIS C ND1 1 
ATOM   3018 C CD2 . HIS C 1 53  ? -42.85790 58.39732  25.24130  1.000 102.10776 ? 53  HIS C CD2 1 
ATOM   3019 C CE1 . HIS C 1 53  ? -43.91375 60.25485  25.74040  1.000 106.50875 ? 53  HIS C CE1 1 
ATOM   3020 N NE2 . HIS C 1 53  ? -42.86813 59.50908  26.04941  1.000 103.80991 ? 53  HIS C NE2 1 
ATOM   3021 N N   . THR C 1 54  ? -46.92027 54.81708  23.00347  1.000 99.55623  ? 54  THR C N   1 
ATOM   3022 C CA  . THR C 1 54  ? -47.32083 53.75696  22.08500  1.000 92.34112  ? 54  THR C CA  1 
ATOM   3023 C C   . THR C 1 54  ? -47.73853 54.31525  20.73222  1.000 89.78939  ? 54  THR C C   1 
ATOM   3024 O O   . THR C 1 54  ? -47.44570 53.70293  19.69932  1.000 93.89868  ? 54  THR C O   1 
ATOM   3025 C CB  . THR C 1 54  ? -48.44558 52.91516  22.69061  1.000 93.29059  ? 54  THR C CB  1 
ATOM   3026 O OG1 . THR C 1 54  ? -49.59015 53.73567  22.95270  1.000 99.47199  ? 54  THR C OG1 1 
ATOM   3027 C CG2 . THR C 1 54  ? -47.98169 52.27952  23.98933  1.000 89.96470  ? 54  THR C CG2 1 
ATOM   3028 N N   . ASP C 1 55  ? -48.44270 55.45044  20.69762  1.000 86.76242  ? 55  ASP C N   1 
ATOM   3029 C CA  . ASP C 1 55  ? -48.92215 55.92590  19.40234  1.000 87.86273  ? 55  ASP C CA  1 
ATOM   3030 C C   . ASP C 1 55  ? -47.75582 56.28014  18.48018  1.000 91.19168  ? 55  ASP C C   1 
ATOM   3031 O O   . ASP C 1 55  ? -47.96902 56.69770  17.33782  1.000 96.43526  ? 55  ASP C O   1 
ATOM   3032 C CB  . ASP C 1 55  ? -49.84111 57.13928  19.56650  1.000 85.55066  ? 55  ASP C CB  1 
ATOM   3033 C CG  . ASP C 1 55  ? -50.76060 57.34285  18.37279  1.000 103.26985 ? 55  ASP C CG  1 
ATOM   3034 O OD1 . ASP C 1 55  ? -50.76503 56.48149  17.46543  1.000 114.90105 ? 55  ASP C OD1 1 
ATOM   3035 O OD2 . ASP C 1 55  ? -51.46529 58.37213  18.33014  1.000 109.48564 ? 55  ASP C OD2 1 
ATOM   3036 N N   . ARG C 1 56  ? -46.52078 56.12353  18.95864  1.000 90.04878  ? 56  ARG C N   1 
ATOM   3037 C CA  . ARG C 1 56  ? -45.34601 56.34662  18.13031  1.000 95.34536  ? 56  ARG C CA  1 
ATOM   3038 C C   . ARG C 1 56  ? -44.91278 55.07859  17.41091  1.000 88.85491  ? 56  ARG C C   1 
ATOM   3039 O O   . ARG C 1 56  ? -43.94611 55.11339  16.64148  1.000 87.50629  ? 56  ARG C O   1 
ATOM   3040 C CB  . ARG C 1 56  ? -44.18426 56.86570  18.98232  1.000 89.58728  ? 56  ARG C CB  1 
ATOM   3041 C CG  . ARG C 1 56  ? -44.49060 58.12938  19.76495  1.000 94.64341  ? 56  ARG C CG  1 
ATOM   3042 C CD  . ARG C 1 56  ? -43.57214 59.27272  19.36414  1.000 85.98018  ? 56  ARG C CD  1 
ATOM   3043 N NE  . ARG C 1 56  ? -43.71286 60.42678  20.24535  1.000 91.25561  ? 56  ARG C NE  1 
ATOM   3044 C CZ  . ARG C 1 56  ? -43.07584 60.57513  21.39982  1.000 93.05845  ? 56  ARG C CZ  1 
ATOM   3045 N NH1 . ARG C 1 56  ? -42.24543 59.65224  21.85356  1.000 106.69288 ? 56  ARG C NH1 1 
ATOM   3046 N NH2 . ARG C 1 56  ? -43.28941 61.67073  22.12538  1.000 94.17198  ? 56  ARG C NH2 1 
ATOM   3047 N N   . ARG C 1 57  ? -45.61550 53.96807  17.63587  1.000 88.46498  ? 57  ARG C N   1 
ATOM   3048 C CA  . ARG C 1 57  ? -45.24837 52.67853  17.06683  1.000 84.43598  ? 57  ARG C CA  1 
ATOM   3049 C C   . ARG C 1 57  ? -45.90878 52.46192  15.70547  1.000 77.50183  ? 57  ARG C C   1 
ATOM   3050 O O   . ARG C 1 57  ? -45.23985 51.96621  14.78948  1.000 75.38766  ? 57  ARG C O   1 
ATOM   3051 C CB  . ARG C 1 57  ? -45.60178 51.58319  18.07762  1.000 78.39980  ? 57  ARG C CB  1 
ATOM   3052 C CG  . ARG C 1 57  ? -44.97961 51.89082  19.44241  1.000 97.39448  ? 57  ARG C CG  1 
ATOM   3053 C CD  . ARG C 1 57  ? -44.41377 50.69383  20.16956  1.000 90.11998  ? 57  ARG C CD  1 
ATOM   3054 N NE  . ARG C 1 57  ? -45.44697 49.79397  20.66526  1.000 92.61976  ? 57  ARG C NE  1 
ATOM   3055 C CZ  . ARG C 1 57  ? -45.53415 49.38822  21.92554  1.000 109.35743 ? 57  ARG C CZ  1 
ATOM   3056 N NH1 . ARG C 1 57  ? -44.60317 49.69331  22.81642  1.000 114.22852 ? 57  ARG C NH1 1 
ATOM   3057 N NH2 . ARG C 1 57  ? -46.56474 48.63373  22.29464  1.000 103.24733 ? 57  ARG C NH2 1 
ATOM   3058 N N   . PRO C 1 58  ? -47.21215 52.72769  15.54104  1.000 68.04951  ? 58  PRO C N   1 
ATOM   3059 C CA  . PRO C 1 58  ? -47.81721 52.60318  14.20794  1.000 65.62182  ? 58  PRO C CA  1 
ATOM   3060 C C   . PRO C 1 58  ? -46.95704 53.27432  13.14602  1.000 65.80552  ? 58  PRO C C   1 
ATOM   3061 O O   . PRO C 1 58  ? -46.45387 54.38390  13.34018  1.000 84.85967  ? 58  PRO C O   1 
ATOM   3062 C CB  . PRO C 1 58  ? -49.17439 53.27959  14.38066  1.000 66.59084  ? 58  PRO C CB  1 
ATOM   3063 C CG  . PRO C 1 58  ? -49.50821 52.96613  15.78350  1.000 71.34153  ? 58  PRO C CG  1 
ATOM   3064 C CD  . PRO C 1 58  ? -48.22880 53.14207  16.53513  1.000 70.34199  ? 58  PRO C CD  1 
ATOM   3065 N N   . VAL C 1 59  ? -46.78491 52.59069  12.01601  1.000 67.04354  ? 59  VAL C N   1 
ATOM   3066 C CA  . VAL C 1 59  ? -45.97646 53.14158  10.93880  1.000 67.73692  ? 59  VAL C CA  1 
ATOM   3067 C C   . VAL C 1 59  ? -46.60719 54.43938  10.46233  1.000 74.15080  ? 59  VAL C C   1 
ATOM   3068 O O   . VAL C 1 59  ? -47.78894 54.48349  10.09676  1.000 68.64830  ? 59  VAL C O   1 
ATOM   3069 C CB  . VAL C 1 59  ? -45.83609 52.12977  9.79500   1.000 60.79840  ? 59  VAL C CB  1 
ATOM   3070 C CG1 . VAL C 1 59  ? -44.88567 52.67047  8.75195   1.000 68.95314  ? 59  VAL C CG1 1 
ATOM   3071 C CG2 . VAL C 1 59  ? -45.33545 50.79771  10.32715  1.000 72.86654  ? 59  VAL C CG2 1 
ATOM   3072 N N   . ASP C 1 60  ? -45.81533 55.50911  10.47026  1.000 80.97298  ? 60  ASP C N   1 
ATOM   3073 C CA  . ASP C 1 60  ? -46.28644 56.82169  10.07623  1.000 67.18471  ? 60  ASP C CA  1 
ATOM   3074 C C   . ASP C 1 60  ? -45.44082 57.39356  8.94562   1.000 70.27193  ? 60  ASP C C   1 
ATOM   3075 O O   . ASP C 1 60  ? -44.23974 57.12184  8.85420   1.000 76.69490  ? 60  ASP C O   1 
ATOM   3076 C CB  . ASP C 1 60  ? -46.24075 57.77030  11.28252  1.000 69.98707  ? 60  ASP C CB  1 
ATOM   3077 C CG  . ASP C 1 60  ? -47.35022 58.80371  11.26533  1.000 90.99226  ? 60  ASP C CG  1 
ATOM   3078 O OD1 . ASP C 1 60  ? -48.53019 58.40133  11.33139  1.000 91.67635  ? 60  ASP C OD1 1 
ATOM   3079 O OD2 . ASP C 1 60  ? -47.04481 60.01838  11.24505  1.000 91.75274  ? 60  ASP C OD2 1 
ATOM   3080 N N   . PRO C 1 61  ? -46.04667 58.18003  8.05846   1.000 65.20905  ? 61  PRO C N   1 
ATOM   3081 C CA  . PRO C 1 61  ? -47.49310 58.38281  7.88688   1.000 70.65258  ? 61  PRO C CA  1 
ATOM   3082 C C   . PRO C 1 61  ? -48.15504 57.09796  7.40513   1.000 69.69779  ? 61  PRO C C   1 
ATOM   3083 O O   . PRO C 1 61  ? -47.52909 56.31063  6.70717   1.000 63.92668  ? 61  PRO C O   1 
ATOM   3084 C CB  . PRO C 1 61  ? -47.55865 59.50390  6.84732   1.000 73.56296  ? 61  PRO C CB  1 
ATOM   3085 C CG  . PRO C 1 61  ? -46.27694 59.36526  6.07206   1.000 69.28538  ? 61  PRO C CG  1 
ATOM   3086 C CD  . PRO C 1 61  ? -45.26207 58.96511  7.09068   1.000 70.43965  ? 61  PRO C CD  1 
ATOM   3087 N N   . PRO C 1 62  ? -49.40531 56.87311  7.79597   1.000 71.90038  ? 62  PRO C N   1 
ATOM   3088 C CA  . PRO C 1 62  ? -50.11880 55.65458  7.39826   1.000 59.28713  ? 62  PRO C CA  1 
ATOM   3089 C C   . PRO C 1 62  ? -50.11673 55.48228  5.89160   1.000 67.16205  ? 62  PRO C C   1 
ATOM   3090 O O   . PRO C 1 62  ? -50.53023 56.38700  5.15050   1.000 63.61278  ? 62  PRO C O   1 
ATOM   3091 C CB  . PRO C 1 62  ? -51.53760 55.89185  7.93027   1.000 62.70807  ? 62  PRO C CB  1 
ATOM   3092 C CG  . PRO C 1 62  ? -51.62137 57.38747  8.09111   1.000 62.61817  ? 62  PRO C CG  1 
ATOM   3093 C CD  . PRO C 1 62  ? -50.27361 57.78105  8.56650   1.000 67.21585  ? 62  PRO C CD  1 
ATOM   3094 N N   . PRO C 1 63  ? -49.60094 54.36067  5.39733   1.000 68.40362  ? 63  PRO C N   1 
ATOM   3095 C CA  . PRO C 1 63  ? -49.48452 54.18816  3.94711   1.000 61.40394  ? 63  PRO C CA  1 
ATOM   3096 C C   . PRO C 1 63  ? -50.85410 54.25950  3.29027   1.000 66.15817  ? 63  PRO C C   1 
ATOM   3097 O O   . PRO C 1 63  ? -51.84727 53.74125  3.80715   1.000 67.69035  ? 63  PRO C O   1 
ATOM   3098 C CB  . PRO C 1 63  ? -48.84013 52.80444  3.79897   1.000 54.25543  ? 63  PRO C CB  1 
ATOM   3099 C CG  . PRO C 1 63  ? -48.20587 52.53834  5.11237   1.000 60.14943  ? 63  PRO C CG  1 
ATOM   3100 C CD  . PRO C 1 63  ? -49.02112 53.23642  6.14407   1.000 56.05476  ? 63  PRO C CD  1 
ATOM   3101 N N   . VAL C 1 64  ? -50.88360 54.90720  2.12994   1.000 64.37175  ? 64  VAL C N   1 
ATOM   3102 C CA  . VAL C 1 64  ? -52.07944 55.08225  1.31708   1.000 66.22621  ? 64  VAL C CA  1 
ATOM   3103 C C   . VAL C 1 64  ? -51.76191 54.64104  -0.09964  1.000 62.07523  ? 64  VAL C C   1 
ATOM   3104 O O   . VAL C 1 64  ? -50.76372 55.07708  -0.68383  1.000 66.20857  ? 64  VAL C O   1 
ATOM   3105 C CB  . VAL C 1 64  ? -52.57117 56.54123  1.33499   1.000 66.60858  ? 64  VAL C CB  1 
ATOM   3106 C CG1 . VAL C 1 64  ? -53.61871 56.75586  0.26223   1.000 62.20685  ? 64  VAL C CG1 1 
ATOM   3107 C CG2 . VAL C 1 64  ? -53.11735 56.88760  2.70870   1.000 63.75448  ? 64  VAL C CG2 1 
ATOM   3108 N N   . ILE C 1 65  ? -52.60556 53.76739  -0.63929  1.000 63.48810  ? 65  ILE C N   1 
ATOM   3109 C CA  . ILE C 1 65  ? -52.44136 53.19615  -1.96724  1.000 58.04669  ? 65  ILE C CA  1 
ATOM   3110 C C   . ILE C 1 65  ? -53.68630 53.49188  -2.79010  1.000 62.69222  ? 65  ILE C C   1 
ATOM   3111 O O   . ILE C 1 65  ? -54.81486 53.31068  -2.31741  1.000 62.01239  ? 65  ILE C O   1 
ATOM   3112 C CB  . ILE C 1 65  ? -52.15269 51.68204  -1.93446  1.000 67.45174  ? 65  ILE C CB  1 
ATOM   3113 C CG1 . ILE C 1 65  ? -50.94249 51.33406  -1.04483  1.000 64.78698  ? 65  ILE C CG1 1 
ATOM   3114 C CG2 . ILE C 1 65  ? -51.92754 51.16262  -3.34885  1.000 59.23991  ? 65  ILE C CG2 1 
ATOM   3115 C CD1 . ILE C 1 65  ? -51.15796 51.40906  0.46566   1.000 61.65345  ? 65  ILE C CD1 1 
ATOM   3116 N N   . GLU C 1 66  ? -53.46728 53.97710  -4.00750  1.000 67.73143  ? 66  GLU C N   1 
ATOM   3117 C CA  . GLU C 1 66  ? -54.50595 54.36123  -4.94984  1.000 60.56709  ? 66  GLU C CA  1 
ATOM   3118 C C   . GLU C 1 66  ? -54.66412 53.30042  -6.03533  1.000 77.91993  ? 66  GLU C C   1 
ATOM   3119 O O   . GLU C 1 66  ? -53.67630 52.77324  -6.55427  1.000 66.97407  ? 66  GLU C O   1 
ATOM   3120 C CB  . GLU C 1 66  ? -54.13945 55.69644  -5.59410  1.000 70.34063  ? 66  GLU C CB  1 
ATOM   3121 C CG  . GLU C 1 66  ? -54.69946 55.89844  -6.98813  1.000 99.12008  ? 66  GLU C CG  1 
ATOM   3122 C CD  . GLU C 1 66  ? -54.41534 57.28428  -7.52723  1.000 99.57797  ? 66  GLU C CD  1 
ATOM   3123 O OE1 . GLU C 1 66  ? -54.86052 58.26367  -6.89632  1.000 96.91239  ? 66  GLU C OE1 1 
ATOM   3124 O OE2 . GLU C 1 66  ? -53.74299 57.39360  -8.57697  1.000 108.62815 ? 66  GLU C OE2 1 
ATOM   3125 N N   . LEU C 1 67  ? -55.91690 52.95624  -6.34044  1.000 70.01288  ? 67  LEU C N   1 
ATOM   3126 C CA  . LEU C 1 67  ? -56.24557 51.90114  -7.29201  1.000 72.18505  ? 67  LEU C CA  1 
ATOM   3127 C C   . LEU C 1 67  ? -57.09558 52.47038  -8.41667  1.000 68.93064  ? 67  LEU C C   1 
ATOM   3128 O O   . LEU C 1 67  ? -58.09628 53.14553  -8.16085  1.000 70.90916  ? 67  LEU C O   1 
ATOM   3129 C CB  . LEU C 1 67  ? -56.99591 50.74988  -6.61253  1.000 64.20450  ? 67  LEU C CB  1 
ATOM   3130 C CG  . LEU C 1 67  ? -57.64510 49.71580  -7.54330  1.000 66.13670  ? 67  LEU C CG  1 
ATOM   3131 C CD1 . LEU C 1 67  ? -56.61688 48.99376  -8.40648  1.000 65.43538  ? 67  LEU C CD1 1 
ATOM   3132 C CD2 . LEU C 1 67  ? -58.48500 48.71739  -6.75070  1.000 72.80430  ? 67  LEU C CD2 1 
ATOM   3133 N N   . ASN C 1 68  ? -56.72062 52.15738  -9.65529  1.000 69.49066  ? 68  ASN C N   1 
ATOM   3134 C CA  . ASN C 1 68  ? -57.50711 52.49721  -10.83173 1.000 70.15983  ? 68  ASN C CA  1 
ATOM   3135 C C   . ASN C 1 68  ? -57.67372 51.25919  -11.70200 1.000 71.42117  ? 68  ASN C C   1 
ATOM   3136 O O   . ASN C 1 68  ? -56.78192 50.41038  -11.77601 1.000 78.44380  ? 68  ASN C O   1 
ATOM   3137 C CB  . ASN C 1 68  ? -56.86180 53.61975  -11.64832 1.000 72.06350  ? 68  ASN C CB  1 
ATOM   3138 C CG  . ASN C 1 68  ? -56.95262 54.96522  -10.95752 1.000 81.68893  ? 68  ASN C CG  1 
ATOM   3139 O OD1 . ASN C 1 68  ? -58.00228 55.60757  -10.96299 1.000 72.88774  ? 68  ASN C OD1 1 
ATOM   3140 N ND2 . ASN C 1 68  ? -55.84538 55.40525  -10.36953 1.000 70.19439  ? 68  ASN C ND2 1 
ATOM   3141 N N   . ILE C 1 69  ? -58.81959 51.16906  -12.37139 1.000 74.56602  ? 69  ILE C N   1 
ATOM   3142 C CA  . ILE C 1 69  ? -59.15356 50.03453  -13.22189 1.000 76.56781  ? 69  ILE C CA  1 
ATOM   3143 C C   . ILE C 1 69  ? -59.52011 50.56535  -14.59814 1.000 80.33780  ? 69  ILE C C   1 
ATOM   3144 O O   . ILE C 1 69  ? -60.30477 51.51331  -14.71407 1.000 90.23306  ? 69  ILE C O   1 
ATOM   3145 C CB  . ILE C 1 69  ? -60.31411 49.20652  -12.63594 1.000 79.84193  ? 69  ILE C CB  1 
ATOM   3146 C CG1 . ILE C 1 69  ? -59.97469 48.72195  -11.22657 1.000 75.19628  ? 69  ILE C CG1 1 
ATOM   3147 C CG2 . ILE C 1 69  ? -60.65430 48.03138  -13.54228 1.000 80.57535  ? 69  ILE C CG2 1 
ATOM   3148 C CD1 . ILE C 1 69  ? -61.18877 48.53848  -10.35868 1.000 82.67335  ? 69  ILE C CD1 1 
ATOM   3149 N N   . PHE C 1 70  ? -58.96549 49.94537  -15.63793 1.000 88.63420  ? 70  PHE C N   1 
ATOM   3150 C CA  . PHE C 1 70  ? -59.14400 50.40435  -17.00624 1.000 83.80173  ? 70  PHE C CA  1 
ATOM   3151 C C   . PHE C 1 70  ? -59.66650 49.27624  -17.88547 1.000 87.50861  ? 70  PHE C C   1 
ATOM   3152 O O   . PHE C 1 70  ? -59.20636 48.13380  -17.79025 1.000 92.10188  ? 70  PHE C O   1 
ATOM   3153 C CB  . PHE C 1 70  ? -57.82450 50.94313  -17.56496 1.000 87.56623  ? 70  PHE C CB  1 
ATOM   3154 C CG  . PHE C 1 70  ? -57.27948 52.11489  -16.79582 1.000 79.90724  ? 70  PHE C CG  1 
ATOM   3155 C CD1 . PHE C 1 70  ? -57.71084 53.40373  -17.06394 1.000 93.09682  ? 70  PHE C CD1 1 
ATOM   3156 C CD2 . PHE C 1 70  ? -56.34317 51.92456  -15.79643 1.000 76.20115  ? 70  PHE C CD2 1 
ATOM   3157 C CE1 . PHE C 1 70  ? -57.21259 54.48049  -16.34989 1.000 79.79473  ? 70  PHE C CE1 1 
ATOM   3158 C CE2 . PHE C 1 70  ? -55.83673 52.99875  -15.08173 1.000 82.51854  ? 70  PHE C CE2 1 
ATOM   3159 C CZ  . PHE C 1 70  ? -56.27304 54.27606  -15.35717 1.000 76.09517  ? 70  PHE C CZ  1 
ATOM   3160 N N   . GLU C 1 71  ? -60.63054 49.60739  -18.73924 1.000 90.96700  ? 71  GLU C N   1 
ATOM   3161 C CA  . GLU C 1 71  ? -61.14176 48.69939  -19.75504 1.000 94.79315  ? 71  GLU C CA  1 
ATOM   3162 C C   . GLU C 1 71  ? -60.52900 49.06075  -21.09891 1.000 96.76837  ? 71  GLU C C   1 
ATOM   3163 O O   . GLU C 1 71  ? -60.35371 50.24028  -21.41692 1.000 106.61833 ? 71  GLU C O   1 
ATOM   3164 C CB  . GLU C 1 71  ? -62.66656 48.76417  -19.85008 1.000 98.69340  ? 71  GLU C CB  1 
ATOM   3165 C CG  . GLU C 1 71  ? -63.32576 47.43368  -20.18374 1.000 108.41016 ? 71  GLU C CG  1 
ATOM   3166 C CD  . GLU C 1 71  ? -64.83610 47.46381  -20.01968 1.000 126.88850 ? 71  GLU C CD  1 
ATOM   3167 O OE1 . GLU C 1 71  ? -65.48097 48.39445  -20.55420 1.000 110.50057 ? 71  GLU C OE1 1 
ATOM   3168 O OE2 . GLU C 1 71  ? -65.37856 46.55216  -19.35860 1.000 137.98847 ? 71  GLU C OE2 1 
ATOM   3169 N N   . SER C 1 72  ? -60.20684 48.04104  -21.88745 1.000 103.84707 ? 72  SER C N   1 
ATOM   3170 C CA  . SER C 1 72  ? -59.52722 48.26719  -23.15040 1.000 109.46153 ? 72  SER C CA  1 
ATOM   3171 C C   . SER C 1 72  ? -59.85382 47.13918  -24.11499 1.000 118.73267 ? 72  SER C C   1 
ATOM   3172 O O   . SER C 1 72  ? -60.33103 46.07151  -23.72224 1.000 117.74155 ? 72  SER C O   1 
ATOM   3173 C CB  . SER C 1 72  ? -58.01036 48.37953  -22.94813 1.000 98.84051  ? 72  SER C CB  1 
ATOM   3174 O OG  . SER C 1 72  ? -57.30943 48.07999  -24.14158 1.000 119.47904 ? 72  SER C OG  1 
ATOM   3175 N N   . ASP C 1 73  ? -59.60086 47.40068  -25.38460 1.000 138.17928 ? 73  ASP C N   1 
ATOM   3176 C CA  . ASP C 1 73  ? -59.64036 46.39813  -26.43701 1.000 145.39718 ? 73  ASP C CA  1 
ATOM   3177 C C   . ASP C 1 73  ? -58.22860 45.92849  -26.73511 1.000 152.93237 ? 73  ASP C C   1 
ATOM   3178 O O   . ASP C 1 73  ? -57.34089 46.76482  -26.95916 1.000 154.21527 ? 73  ASP C O   1 
ATOM   3179 C CB  . ASP C 1 73  ? -60.27970 46.96137  -27.70156 1.000 154.60184 ? 73  ASP C CB  1 
ATOM   3180 C CG  . ASP C 1 73  ? -61.74778 47.28963  -27.51674 1.000 167.17229 ? 73  ASP C CG  1 
ATOM   3181 O OD1 . ASP C 1 73  ? -62.22397 47.26012  -26.36219 1.000 167.40925 ? 73  ASP C OD1 1 
ATOM   3182 O OD2 . ASP C 1 73  ? -62.42598 47.57545  -28.52711 1.000 171.38713 ? 73  ASP C OD2 1 
ATOM   3183 N N   . PRO C 1 74  ? -57.97602 44.61814  -26.73386 1.000 147.18923 ? 74  PRO C N   1 
ATOM   3184 C CA  . PRO C 1 74  ? -56.59074 44.13869  -26.87741 1.000 135.83090 ? 74  PRO C CA  1 
ATOM   3185 C C   . PRO C 1 74  ? -55.95092 44.52548  -28.19739 1.000 148.88383 ? 74  PRO C C   1 
ATOM   3186 O O   . PRO C 1 74  ? -54.71685 44.55535  -28.28140 1.000 140.84731 ? 74  PRO C O   1 
ATOM   3187 C CB  . PRO C 1 74  ? -56.71321 42.61384  -26.73359 1.000 132.07977 ? 74  PRO C CB  1 
ATOM   3188 C CG  . PRO C 1 74  ? -58.12313 42.33341  -26.33879 1.000 121.54913 ? 74  PRO C CG  1 
ATOM   3189 C CD  . PRO C 1 74  ? -58.95785 43.52603  -26.64493 1.000 129.97891 ? 74  PRO C CD  1 
ATOM   3190 N N   . HIS C 1 75  ? -56.74229 44.82855  -29.22908 1.000 155.90459 ? 75  HIS C N   1 
ATOM   3191 C CA  . HIS C 1 75  ? -56.15310 45.21295  -30.50640 1.000 172.73520 ? 75  HIS C CA  1 
ATOM   3192 C C   . HIS C 1 75  ? -55.52242 46.59861  -30.42131 1.000 175.14195 ? 75  HIS C C   1 
ATOM   3193 O O   . HIS C 1 75  ? -54.46376 46.84059  -31.01288 1.000 179.23043 ? 75  HIS C O   1 
ATOM   3194 C CB  . HIS C 1 75  ? -57.20500 45.15983  -31.61718 1.000 189.29899 ? 75  HIS C CB  1 
ATOM   3195 C CG  . HIS C 1 75  ? -58.36597 46.08276  -31.40459 1.000 206.66638 ? 75  HIS C CG  1 
ATOM   3196 N ND1 . HIS C 1 75  ? -58.34373 47.40805  -31.78396 1.000 206.67293 ? 75  HIS C ND1 1 
ATOM   3197 C CD2 . HIS C 1 75  ? -59.59104 45.86630  -30.86985 1.000 204.74508 ? 75  HIS C CD2 1 
ATOM   3198 C CE1 . HIS C 1 75  ? -59.50012 47.97089  -31.48150 1.000 199.05589 ? 75  HIS C CE1 1 
ATOM   3199 N NE2 . HIS C 1 75  ? -60.27552 47.05651  -30.92749 1.000 206.43925 ? 75  HIS C NE2 1 
ATOM   3200 N N   . ASP C 1 76  ? -56.15088 47.51883  -29.68944 1.000 166.02629 ? 76  ASP C N   1 
ATOM   3201 C CA  . ASP C 1 76  ? -55.66770 48.89057  -29.55677 1.000 163.91105 ? 76  ASP C CA  1 
ATOM   3202 C C   . ASP C 1 76  ? -55.40375 49.16696  -28.08189 1.000 152.05678 ? 76  ASP C C   1 
ATOM   3203 O O   . ASP C 1 76  ? -56.34352 49.35555  -27.30138 1.000 143.45779 ? 76  ASP C O   1 
ATOM   3204 C CB  . ASP C 1 76  ? -56.67803 49.88401  -30.13040 1.000 165.56326 ? 76  ASP C CB  1 
ATOM   3205 C CG  . ASP C 1 76  ? -56.09338 51.27132  -30.31855 1.000 151.55681 ? 76  ASP C CG  1 
ATOM   3206 O OD1 . ASP C 1 76  ? -54.90680 51.47297  -29.98413 1.000 146.73220 ? 76  ASP C OD1 1 
ATOM   3207 O OD2 . ASP C 1 76  ? -56.82348 52.16146  -30.80395 1.000 149.30775 ? 76  ASP C OD2 1 
ATOM   3208 N N   . ASP C 1 77  ? -54.12752 49.20333  -27.70690 1.000 158.93421 ? 77  ASP C N   1 
ATOM   3209 C CA  . ASP C 1 77  ? -53.72410 49.40249  -26.32200 1.000 157.12576 ? 77  ASP C CA  1 
ATOM   3210 C C   . ASP C 1 77  ? -53.45993 50.86299  -25.98275 1.000 151.45070 ? 77  ASP C C   1 
ATOM   3211 O O   . ASP C 1 77  ? -53.12863 51.16607  -24.83177 1.000 145.99144 ? 77  ASP C O   1 
ATOM   3212 C CB  . ASP C 1 77  ? -52.46940 48.57568  -26.01923 1.000 166.86437 ? 77  ASP C CB  1 
ATOM   3213 C CG  . ASP C 1 77  ? -52.75703 47.09027  -25.93125 1.000 168.75325 ? 77  ASP C CG  1 
ATOM   3214 O OD1 . ASP C 1 77  ? -53.94829 46.71713  -25.88059 1.000 165.43763 ? 77  ASP C OD1 1 
ATOM   3215 O OD2 . ASP C 1 77  ? -51.79176 46.29602  -25.91753 1.000 174.39505 ? 77  ASP C OD2 1 
ATOM   3216 N N   . SER C 1 78  ? -53.59809 51.77057  -26.94679 1.000 151.87956 ? 78  SER C N   1 
ATOM   3217 C CA  . SER C 1 78  ? -53.33420 53.18179  -26.71156 1.000 140.79889 ? 78  SER C CA  1 
ATOM   3218 C C   . SER C 1 78  ? -54.53264 53.92914  -26.14337 1.000 139.60758 ? 78  SER C C   1 
ATOM   3219 O O   . SER C 1 78  ? -54.37827 55.07414  -25.70409 1.000 147.09926 ? 78  SER C O   1 
ATOM   3220 C CB  . SER C 1 78  ? -52.88766 53.84328  -28.01765 1.000 138.48990 ? 78  SER C CB  1 
ATOM   3221 O OG  . SER C 1 78  ? -51.55831 53.47510  -28.34253 1.000 130.83260 ? 78  SER C OG  1 
ATOM   3222 N N   . ASN C 1 79  ? -55.71193 53.31407  -26.14347 1.000 134.97055 ? 79  ASN C N   1 
ATOM   3223 C CA  . ASN C 1 79  ? -56.93566 53.91902  -25.63618 1.000 130.02304 ? 79  ASN C CA  1 
ATOM   3224 C C   . ASN C 1 79  ? -57.49357 53.02654  -24.53930 1.000 117.79320 ? 79  ASN C C   1 
ATOM   3225 O O   . ASN C 1 79  ? -57.64288 51.81643  -24.73608 1.000 124.87398 ? 79  ASN C O   1 
ATOM   3226 C CB  . ASN C 1 79  ? -57.96548 54.13297  -26.74861 1.000 131.11523 ? 79  ASN C CB  1 
ATOM   3227 C CG  . ASN C 1 79  ? -57.32411 54.50863  -28.06686 1.000 140.76777 ? 79  ASN C CG  1 
ATOM   3228 O OD1 . ASN C 1 79  ? -56.49325 53.77395  -28.59664 1.000 143.97230 ? 79  ASN C OD1 1 
ATOM   3229 N ND2 . ASN C 1 79  ? -57.69708 55.66789  -28.59751 1.000 146.77045 ? 79  ASN C ND2 1 
ATOM   3230 N N   . LYS C 1 80  ? -57.79157 53.62174  -23.38828 1.000 116.25096 ? 80  LYS C N   1 
ATOM   3231 C CA  . LYS C 1 80  ? -58.34391 52.89302  -22.25864 1.000 112.48759 ? 80  LYS C CA  1 
ATOM   3232 C C   . LYS C 1 80  ? -59.48170 53.71598  -21.67927 1.000 106.43023 ? 80  LYS C C   1 
ATOM   3233 O O   . LYS C 1 80  ? -59.61433 54.90882  -21.96074 1.000 106.91950 ? 80  LYS C O   1 
ATOM   3234 C CB  . LYS C 1 80  ? -57.30661 52.65228  -21.14374 1.000 111.41019 ? 80  LYS C CB  1 
ATOM   3235 C CG  . LYS C 1 80  ? -55.89543 52.29682  -21.59630 1.000 118.56446 ? 80  LYS C CG  1 
ATOM   3236 C CD  . LYS C 1 80  ? -55.12152 53.58517  -21.90980 1.000 139.89168 ? 80  LYS C CD  1 
ATOM   3237 C CE  . LYS C 1 80  ? -53.61664 53.43519  -21.79727 1.000 141.12755 ? 80  LYS C CE  1 
ATOM   3238 N NZ  . LYS C 1 80  ? -52.93993 54.65881  -22.31579 1.000 138.17180 ? 80  LYS C NZ  1 
ATOM   3239 N N   . THR C 1 81  ? -60.30510 53.06979  -20.86024 1.000 91.43822  ? 81  THR C N   1 
ATOM   3240 C CA  . THR C 1 81  ? -61.44892 53.72565  -20.24283 1.000 95.27802  ? 81  THR C CA  1 
ATOM   3241 C C   . THR C 1 81  ? -61.37617 53.48166  -18.74581 1.000 84.69918  ? 81  THR C C   1 
ATOM   3242 O O   . THR C 1 81  ? -61.30625 52.32920  -18.30908 1.000 93.19926  ? 81  THR C O   1 
ATOM   3243 C CB  . THR C 1 81  ? -62.77293 53.19748  -20.80698 1.000 81.83645  ? 81  THR C CB  1 
ATOM   3244 O OG1 . THR C 1 81  ? -62.71806 53.19863  -22.23787 1.000 86.17754  ? 81  THR C OG1 1 
ATOM   3245 C CG2 . THR C 1 81  ? -63.93662 54.05878  -20.34416 1.000 81.83469  ? 81  THR C CG2 1 
ATOM   3246 N N   . ASP C 1 82  ? -61.40464 54.55620  -17.96161 1.000 76.80142  ? 82  ASP C N   1 
ATOM   3247 C CA  . ASP C 1 82  ? -61.39099 54.41196  -16.51024 1.000 83.37394  ? 82  ASP C CA  1 
ATOM   3248 C C   . ASP C 1 82  ? -62.76226 53.92720  -16.05399 1.000 87.84990  ? 82  ASP C C   1 
ATOM   3249 O O   . ASP C 1 82  ? -63.75672 54.65041  -16.17742 1.000 86.49741  ? 82  ASP C O   1 
ATOM   3250 C CB  . ASP C 1 82  ? -61.02371 55.74754  -15.86811 1.000 69.82199  ? 82  ASP C CB  1 
ATOM   3251 C CG  . ASP C 1 82  ? -60.66139 55.61850  -14.40127 1.000 81.71946  ? 82  ASP C CG  1 
ATOM   3252 O OD1 . ASP C 1 82  ? -61.23188 54.75095  -13.70716 1.000 88.44778  ? 82  ASP C OD1 1 
ATOM   3253 O OD2 . ASP C 1 82  ? -59.79644 56.39271  -13.94008 1.000 99.98881  ? 82  ASP C OD2 1 
ATOM   3254 N N   . ILE C 1 83  ? -62.81831 52.71069  -15.51270 1.000 78.73605  ? 83  ILE C N   1 
ATOM   3255 C CA  . ILE C 1 83  ? -64.08260 52.13001  -15.07106 1.000 78.31974  ? 83  ILE C CA  1 
ATOM   3256 C C   . ILE C 1 83  ? -64.05300 51.83011  -13.57865 1.000 83.65577  ? 83  ILE C C   1 
ATOM   3257 O O   . ILE C 1 83  ? -64.70467 50.88600  -13.11791 1.000 88.08812  ? 83  ILE C O   1 
ATOM   3258 C CB  . ILE C 1 83  ? -64.42296 50.86459  -15.87511 1.000 81.65899  ? 83  ILE C CB  1 
ATOM   3259 C CG1 . ILE C 1 83  ? -63.25748 49.87731  -15.83939 1.000 82.68256  ? 83  ILE C CG1 1 
ATOM   3260 C CG2 . ILE C 1 83  ? -64.74685 51.23382  -17.30708 1.000 77.51676  ? 83  ILE C CG2 1 
ATOM   3261 C CD1 . ILE C 1 83  ? -63.59654 48.53454  -16.42175 1.000 73.86076  ? 83  ILE C CD1 1 
ATOM   3262 N N   . THR C 1 84  ? -63.28863 52.61370  -12.81567 1.000 77.55882  ? 84  THR C N   1 
ATOM   3263 C CA  . THR C 1 84  ? -63.05098 52.26967  -11.41640 1.000 78.36246  ? 84  THR C CA  1 
ATOM   3264 C C   . THR C 1 84  ? -64.34775 52.24341  -10.61306 1.000 82.50197  ? 84  THR C C   1 
ATOM   3265 O O   . THR C 1 84  ? -64.53927 51.36425  -9.76501  1.000 91.31342  ? 84  THR C O   1 
ATOM   3266 C CB  . THR C 1 84  ? -62.04427 53.23850  -10.79564 1.000 73.83135  ? 84  THR C CB  1 
ATOM   3267 O OG1 . THR C 1 84  ? -61.07545 53.62054  -11.78055 1.000 73.50214  ? 84  THR C OG1 1 
ATOM   3268 C CG2 . THR C 1 84  ? -61.33825 52.58944  -9.61987  1.000 79.26514  ? 84  THR C CG2 1 
ATOM   3269 N N   . PHE C 1 85  ? -65.24345 53.20101  -10.85056 1.000 90.25525  ? 85  PHE C N   1 
ATOM   3270 C CA  . PHE C 1 85  ? -66.49321 53.27009  -10.10254 1.000 94.25208  ? 85  PHE C CA  1 
ATOM   3271 C C   . PHE C 1 85  ? -67.59248 52.39323  -10.68658 1.000 94.15315  ? 85  PHE C C   1 
ATOM   3272 O O   . PHE C 1 85  ? -68.63039 52.21868  -10.03948 1.000 97.39656  ? 85  PHE C O   1 
ATOM   3273 C CB  . PHE C 1 85  ? -67.00492 54.71644  -10.01763 1.000 109.08474 ? 85  PHE C CB  1 
ATOM   3274 C CG  . PHE C 1 85  ? -66.05049 55.67133  -9.35200  1.000 106.10963 ? 85  PHE C CG  1 
ATOM   3275 C CD1 . PHE C 1 85  ? -64.84690 56.01583  -9.94745  1.000 113.22658 ? 85  PHE C CD1 1 
ATOM   3276 C CD2 . PHE C 1 85  ? -66.36115 56.22129  -8.12009  1.000 116.50389 ? 85  PHE C CD2 1 
ATOM   3277 C CE1 . PHE C 1 85  ? -63.97531 56.89363  -9.32954  1.000 123.71467 ? 85  PHE C CE1 1 
ATOM   3278 C CE2 . PHE C 1 85  ? -65.49391 57.09916  -7.49716  1.000 132.95078 ? 85  PHE C CE2 1 
ATOM   3279 C CZ  . PHE C 1 85  ? -64.29925 57.43554  -8.10270  1.000 124.80445 ? 85  PHE C CZ  1 
ATOM   3280 N N   . VAL C 1 86  ? -67.39450 51.84304  -11.88028 1.000 97.19264  ? 86  VAL C N   1 
ATOM   3281 C CA  . VAL C 1 86  ? -68.39668 51.01488  -12.53682 1.000 91.13849  ? 86  VAL C CA  1 
ATOM   3282 C C   . VAL C 1 86  ? -68.08975 49.53007  -12.37394 1.000 98.27469  ? 86  VAL C C   1 
ATOM   3283 O O   . VAL C 1 86  ? -69.00369 48.71620  -12.22859 1.000 90.28846  ? 86  VAL C O   1 
ATOM   3284 C CB  . VAL C 1 86  ? -68.50627 51.41332  -14.02589 1.000 91.10817  ? 86  VAL C CB  1 
ATOM   3285 C CG1 . VAL C 1 86  ? -68.95867 50.24003  -14.88256 1.000 104.99081 ? 86  VAL C CG1 1 
ATOM   3286 C CG2 . VAL C 1 86  ? -69.45626 52.59547  -14.18898 1.000 94.36014  ? 86  VAL C CG2 1 
ATOM   3287 N N   . TYR C 1 87  ? -66.80476 49.17008  -12.37431 1.000 91.02426  ? 87  TYR C N   1 
ATOM   3288 C CA  . TYR C 1 87  ? -66.36999 47.79156  -12.18439 1.000 80.52200  ? 87  TYR C CA  1 
ATOM   3289 C C   . TYR C 1 87  ? -66.83814 47.27314  -10.83025 1.000 91.52882  ? 87  TYR C C   1 
ATOM   3290 O O   . TYR C 1 87  ? -66.36346 47.73711  -9.78834  1.000 98.12788  ? 87  TYR C O   1 
ATOM   3291 C CB  . TYR C 1 87  ? -64.84952 47.69990  -12.29463 1.000 78.23905  ? 87  TYR C CB  1 
ATOM   3292 C CG  . TYR C 1 87  ? -64.30903 46.29304  -12.38765 1.000 77.02887  ? 87  TYR C CG  1 
ATOM   3293 C CD1 . TYR C 1 87  ? -64.48927 45.53478  -13.53665 1.000 86.27712  ? 87  TYR C CD1 1 
ATOM   3294 C CD2 . TYR C 1 87  ? -63.62436 45.71962  -11.32523 1.000 82.34278  ? 87  TYR C CD2 1 
ATOM   3295 C CE1 . TYR C 1 87  ? -63.99621 44.24969  -13.62743 1.000 88.85057  ? 87  TYR C CE1 1 
ATOM   3296 C CE2 . TYR C 1 87  ? -63.12936 44.43320  -11.40722 1.000 88.10459  ? 87  TYR C CE2 1 
ATOM   3297 C CZ  . TYR C 1 87  ? -63.31737 43.70502  -12.56255 1.000 85.23657  ? 87  TYR C CZ  1 
ATOM   3298 O OH  . TYR C 1 87  ? -62.82762 42.42566  -12.65563 1.000 100.19668 ? 87  TYR C OH  1 
ATOM   3299 N N   . ASN C 1 88  ? -67.75153 46.30395  -10.82824 1.000 92.02800  ? 88  ASN C N   1 
ATOM   3300 C CA  . ASN C 1 88  ? -68.36592 45.81020  -9.59669  1.000 101.28330 ? 88  ASN C CA  1 
ATOM   3301 C C   . ASN C 1 88  ? -67.60517 44.57658  -9.12371  1.000 104.62375 ? 88  ASN C C   1 
ATOM   3302 O O   . ASN C 1 88  ? -67.78547 43.47736  -9.65351  1.000 112.84282 ? 88  ASN C O   1 
ATOM   3303 C CB  . ASN C 1 88  ? -69.84302 45.50361  -9.82157  1.000 112.68401 ? 88  ASN C CB  1 
ATOM   3304 C CG  . ASN C 1 88  ? -70.52780 44.98802  -8.57263  1.000 122.72163 ? 88  ASN C CG  1 
ATOM   3305 O OD1 . ASN C 1 88  ? -70.35701 45.53866  -7.48363  1.000 121.67421 ? 88  ASN C OD1 1 
ATOM   3306 N ND2 . ASN C 1 88  ? -71.31581 43.92886  -8.72519  1.000 117.46377 ? 88  ASN C ND2 1 
ATOM   3307 N N   . ALA C 1 89  ? -66.75004 44.76995  -8.12227  1.000 101.32633 ? 89  ALA C N   1 
ATOM   3308 C CA  . ALA C 1 89  ? -66.02249 43.67953  -7.49140  1.000 91.63149  ? 89  ALA C CA  1 
ATOM   3309 C C   . ALA C 1 89  ? -65.53090 44.15380  -6.13241  1.000 92.62893  ? 89  ALA C C   1 
ATOM   3310 O O   . ALA C 1 89  ? -65.40713 45.35594  -5.88504  1.000 95.80917  ? 89  ALA C O   1 
ATOM   3311 C CB  . ALA C 1 89  ? -64.85063 43.20967  -8.36090  1.000 88.82557  ? 89  ALA C CB  1 
ATOM   3312 N N   . ASN C 1 90  ? -65.24537 43.19616  -5.25482  1.000 80.33169  ? 90  ASN C N   1 
ATOM   3313 C CA  . ASN C 1 90  ? -64.67482 43.50736  -3.95301  1.000 84.78134  ? 90  ASN C CA  1 
ATOM   3314 C C   . ASN C 1 90  ? -63.15911 43.47937  -4.06009  1.000 82.02732  ? 90  ASN C C   1 
ATOM   3315 O O   . ASN C 1 90  ? -62.59199 42.64168  -4.76524  1.000 82.66076  ? 90  ASN C O   1 
ATOM   3316 C CB  . ASN C 1 90  ? -65.14109 42.51141  -2.88983  1.000 92.32979  ? 90  ASN C CB  1 
ATOM   3317 C CG  . ASN C 1 90  ? -66.53322 42.81124  -2.38522  1.000 119.18295 ? 90  ASN C CG  1 
ATOM   3318 O OD1 . ASN C 1 90  ? -67.00824 43.94231  -2.48573  1.000 129.80305 ? 90  ASN C OD1 1 
ATOM   3319 N ND2 . ASN C 1 90  ? -67.19623 41.80045  -1.83444  1.000 121.73835 ? 90  ASN C ND2 1 
ATOM   3320 N N   . PHE C 1 91  ? -62.50566 44.41165  -3.37666  1.000 76.68100  ? 91  PHE C N   1 
ATOM   3321 C CA  . PHE C 1 91  ? -61.06083 44.54183  -3.46215  1.000 68.15525  ? 91  PHE C CA  1 
ATOM   3322 C C   . PHE C 1 91  ? -60.46299 44.56468  -2.06574  1.000 68.41721  ? 91  PHE C C   1 
ATOM   3323 O O   . PHE C 1 91  ? -61.02493 45.17575  -1.15176  1.000 81.12270  ? 91  PHE C O   1 
ATOM   3324 C CB  . PHE C 1 91  ? -60.66115 45.81907  -4.21398  1.000 76.49245  ? 91  PHE C CB  1 
ATOM   3325 C CG  . PHE C 1 91  ? -60.81941 45.72188  -5.70558  1.000 73.19343  ? 91  PHE C CG  1 
ATOM   3326 C CD1 . PHE C 1 91  ? -59.95723 44.94247  -6.46066  1.000 69.20612  ? 91  PHE C CD1 1 
ATOM   3327 C CD2 . PHE C 1 91  ? -61.82053 46.42911  -6.35539  1.000 65.79652  ? 91  PHE C CD2 1 
ATOM   3328 C CE1 . PHE C 1 91  ? -60.10150 44.85370  -7.83871  1.000 66.82123  ? 91  PHE C CE1 1 
ATOM   3329 C CE2 . PHE C 1 91  ? -61.97170 46.34667  -7.73153  1.000 65.14643  ? 91  PHE C CE2 1 
ATOM   3330 C CZ  . PHE C 1 91  ? -61.11049 45.55683  -8.47442  1.000 72.17626  ? 91  PHE C CZ  1 
ATOM   3331 N N   . PHE C 1 92  ? -59.32425 43.89980  -1.90311  1.000 62.23620  ? 92  PHE C N   1 
ATOM   3332 C CA  . PHE C 1 92  ? -58.60811 43.91947  -0.63930  1.000 69.13467  ? 92  PHE C CA  1 
ATOM   3333 C C   . PHE C 1 92  ? -57.13340 44.13551  -0.92849  1.000 67.08933  ? 92  PHE C C   1 
ATOM   3334 O O   . PHE C 1 92  ? -56.62160 43.71255  -1.96694  1.000 67.43953  ? 92  PHE C O   1 
ATOM   3335 C CB  . PHE C 1 92  ? -58.81158 42.62640  0.15410   1.000 65.53259  ? 92  PHE C CB  1 
ATOM   3336 C CG  . PHE C 1 92  ? -60.25136 42.25627  0.33748   1.000 81.76975  ? 92  PHE C CG  1 
ATOM   3337 C CD1 . PHE C 1 92  ? -60.90372 41.46563  -0.59404  1.000 82.50097  ? 92  PHE C CD1 1 
ATOM   3338 C CD2 . PHE C 1 92  ? -60.95581 42.70289  1.44054   1.000 81.29366  ? 92  PHE C CD2 1 
ATOM   3339 C CE1 . PHE C 1 92  ? -62.23254 41.12633  -0.42741  1.000 80.24536  ? 92  PHE C CE1 1 
ATOM   3340 C CE2 . PHE C 1 92  ? -62.28049 42.36426  1.61381   1.000 95.52027  ? 92  PHE C CE2 1 
ATOM   3341 C CZ  . PHE C 1 92  ? -62.92106 41.57666  0.67863   1.000 88.74714  ? 92  PHE C CZ  1 
ATOM   3342 N N   . LEU C 1 93  ? -56.44689 44.77326  0.01213   1.000 57.43098  ? 93  LEU C N   1 
ATOM   3343 C CA  . LEU C 1 93  ? -55.01480 45.00335  -0.09932  1.000 49.03220  ? 93  LEU C CA  1 
ATOM   3344 C C   . LEU C 1 93  ? -54.33967 44.45759  1.14239   1.000 59.41722  ? 93  LEU C C   1 
ATOM   3345 O O   . LEU C 1 93  ? -54.69814 44.82867  2.26522   1.000 64.93342  ? 93  LEU C O   1 
ATOM   3346 C CB  . LEU C 1 93  ? -54.69972 46.49014  -0.28615  1.000 58.79005  ? 93  LEU C CB  1 
ATOM   3347 C CG  . LEU C 1 93  ? -53.39819 46.83571  -1.00950  1.000 61.78796  ? 93  LEU C CG  1 
ATOM   3348 C CD1 . LEU C 1 93  ? -53.40358 46.33312  -2.43853  1.000 55.84599  ? 93  LEU C CD1 1 
ATOM   3349 C CD2 . LEU C 1 93  ? -53.16923 48.34471  -0.96350  1.000 62.20098  ? 93  LEU C CD2 1 
ATOM   3350 N N   . PHE C 1 94  ? -53.37137 43.57727  0.93225   1.000 65.79071  ? 94  PHE C N   1 
ATOM   3351 C CA  . PHE C 1 94  ? -52.68119 42.87144  1.99712   1.000 55.03780  ? 94  PHE C CA  1 
ATOM   3352 C C   . PHE C 1 94  ? -51.24397 43.36915  2.04653   1.000 58.51764  ? 94  PHE C C   1 
ATOM   3353 O O   . PHE C 1 94  ? -50.57870 43.45067  1.00801   1.000 56.54878  ? 94  PHE C O   1 
ATOM   3354 C CB  . PHE C 1 94  ? -52.76107 41.35832  1.76232   1.000 52.74840  ? 94  PHE C CB  1 
ATOM   3355 C CG  . PHE C 1 94  ? -52.00541 40.53358  2.76775   1.000 60.30451  ? 94  PHE C CG  1 
ATOM   3356 C CD1 . PHE C 1 94  ? -52.24683 40.66749  4.12593   1.000 60.08862  ? 94  PHE C CD1 1 
ATOM   3357 C CD2 . PHE C 1 94  ? -51.08794 39.58164  2.34535   1.000 57.88093  ? 94  PHE C CD2 1 
ATOM   3358 C CE1 . PHE C 1 94  ? -51.55323 39.89801  5.04775   1.000 63.78682  ? 94  PHE C CE1 1 
ATOM   3359 C CE2 . PHE C 1 94  ? -50.40234 38.79578  3.26094   1.000 56.83397  ? 94  PHE C CE2 1 
ATOM   3360 C CZ  . PHE C 1 94  ? -50.63313 38.95610  4.61192   1.000 63.54446  ? 94  PHE C CZ  1 
ATOM   3361 N N   . ALA C 1 95  ? -50.77026 43.70014  3.24552   1.000 58.87188  ? 95  ALA C N   1 
ATOM   3362 C CA  . ALA C 1 95  ? -49.44436 44.27260  3.43687   1.000 51.25572  ? 95  ALA C CA  1 
ATOM   3363 C C   . ALA C 1 95  ? -48.51165 43.20348  3.99231   1.000 56.81078  ? 95  ALA C C   1 
ATOM   3364 O O   . ALA C 1 95  ? -48.84159 42.53372  4.97838   1.000 57.53294  ? 95  ALA C O   1 
ATOM   3365 C CB  . ALA C 1 95  ? -49.49877 45.47267  4.38432   1.000 55.27650  ? 95  ALA C CB  1 
ATOM   3366 N N   . THR C 1 96  ? -47.34613 43.05642  3.36748   1.000 54.25539  ? 96  THR C N   1 
ATOM   3367 C CA  . THR C 1 96  ? -46.28704 42.19109  3.86726   1.000 60.34410  ? 96  THR C CA  1 
ATOM   3368 C C   . THR C 1 96  ? -45.02768 43.00546  4.10510   1.000 59.01173  ? 96  THR C C   1 
ATOM   3369 O O   . THR C 1 96  ? -44.75878 43.98540  3.40398   1.000 59.94108  ? 96  THR C O   1 
ATOM   3370 C CB  . THR C 1 96  ? -45.96336 41.01411  2.91733   1.000 51.18424  ? 96  THR C CB  1 
ATOM   3371 O OG1 . THR C 1 96  ? -45.73585 41.49083  1.58701   1.000 69.41339  ? 96  THR C OG1 1 
ATOM   3372 C CG2 . THR C 1 96  ? -47.11502 40.03491  2.88447   1.000 56.86819  ? 96  THR C CG2 1 
ATOM   3373 N N   . LEU C 1 97  ? -44.26705 42.58717  5.11163   1.000 61.99703  ? 97  LEU C N   1 
ATOM   3374 C CA  . LEU C 1 97  ? -43.06676 43.28189  5.54342   1.000 57.07627  ? 97  LEU C CA  1 
ATOM   3375 C C   . LEU C 1 97  ? -41.85209 42.53784  5.00385   1.000 65.46899  ? 97  LEU C C   1 
ATOM   3376 O O   . LEU C 1 97  ? -41.67411 41.34597  5.27610   1.000 76.40743  ? 97  LEU C O   1 
ATOM   3377 C CB  . LEU C 1 97  ? -43.02188 43.33990  7.06887   1.000 56.54154  ? 97  LEU C CB  1 
ATOM   3378 C CG  . LEU C 1 97  ? -41.90277 44.14558  7.71046   1.000 70.94324  ? 97  LEU C CG  1 
ATOM   3379 C CD1 . LEU C 1 97  ? -42.09095 45.60237  7.36401   1.000 66.25208  ? 97  LEU C CD1 1 
ATOM   3380 C CD2 . LEU C 1 97  ? -41.89368 43.94498  9.21294   1.000 73.51800  ? 97  LEU C CD2 1 
ATOM   3381 N N   . GLU C 1 98  ? -41.01882 43.24419  4.24638   1.000 70.05034  ? 98  GLU C N   1 
ATOM   3382 C CA  . GLU C 1 98  ? -39.82311 42.66661  3.65182   1.000 73.96291  ? 98  GLU C CA  1 
ATOM   3383 C C   . GLU C 1 98  ? -38.59918 43.33912  4.24918   1.000 67.71606  ? 98  GLU C C   1 
ATOM   3384 O O   . GLU C 1 98  ? -38.45360 44.56782  4.12260   1.000 75.82644  ? 98  GLU C O   1 
ATOM   3385 C CB  . GLU C 1 98  ? -39.81149 42.82556  2.13017   1.000 80.84513  ? 98  GLU C CB  1 
ATOM   3386 C CG  . GLU C 1 98  ? -41.04247 42.30793  1.41365   1.000 87.79245  ? 98  GLU C CG  1 
ATOM   3387 C CD  . GLU C 1 98  ? -40.89262 42.39150  -0.09581  1.000 123.43227 ? 98  GLU C CD  1 
ATOM   3388 O OE1 . GLU C 1 98  ? -40.16418 43.29256  -0.56899  1.000 109.72894 ? 98  GLU C OE1 1 
ATOM   3389 O OE2 . GLU C 1 98  ? -41.49760 41.55857  -0.80763  1.000 117.77240 ? 98  GLU C OE2 1 
ATOM   3390 N N   . PRO C 1 99  ? -37.71184 42.60318  4.91251   1.000 80.08356  ? 99  PRO C N   1 
ATOM   3391 C CA  . PRO C 1 99  ? -36.45796 43.21014  5.36838   1.000 74.96229  ? 99  PRO C CA  1 
ATOM   3392 C C   . PRO C 1 99  ? -35.66515 43.72594  4.17759   1.000 85.00006  ? 99  PRO C C   1 
ATOM   3393 O O   . PRO C 1 99  ? -35.63668 43.10573  3.11203   1.000 96.34064  ? 99  PRO C O   1 
ATOM   3394 C CB  . PRO C 1 99  ? -35.73809 42.05755  6.08143   1.000 75.06634  ? 99  PRO C CB  1 
ATOM   3395 C CG  . PRO C 1 99  ? -36.79859 41.04203  6.36358   1.000 80.45988  ? 99  PRO C CG  1 
ATOM   3396 C CD  . PRO C 1 99  ? -37.81572 41.18205  5.27974   1.000 74.73919  ? 99  PRO C CD  1 
ATOM   3397 N N   . GLU C 1 100 ? -35.03222 44.88555  4.35771   1.000 89.95415  ? 100 GLU C N   1 
ATOM   3398 C CA  . GLU C 1 100 ? -34.21767 45.44158  3.28316   1.000 105.83956 ? 100 GLU C CA  1 
ATOM   3399 C C   . GLU C 1 100 ? -32.90931 44.67180  3.14232   1.000 114.47973 ? 100 GLU C C   1 
ATOM   3400 O O   . GLU C 1 100 ? -32.63158 44.08709  2.08859   1.000 124.89397 ? 100 GLU C O   1 
ATOM   3401 C CB  . GLU C 1 100 ? -33.95771 46.92881  3.53291   1.000 102.53911 ? 100 GLU C CB  1 
ATOM   3402 C CG  . GLU C 1 100 ? -34.81282 47.85975  2.67673   1.000 95.05241  ? 100 GLU C CG  1 
ATOM   3403 C CD  . GLU C 1 100 ? -34.55085 47.70452  1.18881   1.000 111.51384 ? 100 GLU C CD  1 
ATOM   3404 O OE1 . GLU C 1 100 ? -33.65449 48.39766  0.66308   1.000 117.97114 ? 100 GLU C OE1 1 
ATOM   3405 O OE2 . GLU C 1 100 ? -35.24553 46.89173  0.54252   1.000 111.80440 ? 100 GLU C OE2 1 
ATOM   3406 N N   . ARG C 1 101 ? -32.09563 44.64545  4.20382   1.000 124.73836 ? 101 ARG C N   1 
ATOM   3407 C CA  . ARG C 1 101 ? -30.85899 43.86933  4.18287   1.000 159.52464 ? 101 ARG C CA  1 
ATOM   3408 C C   . ARG C 1 101 ? -30.29758 43.64765  5.58510   1.000 174.54824 ? 101 ARG C C   1 
ATOM   3409 O O   . ARG C 1 101 ? -29.35681 44.34315  5.99157   1.000 173.98525 ? 101 ARG C O   1 
ATOM   3410 C CB  . ARG C 1 101 ? -29.80781 44.55964  3.30815   1.000 164.64906 ? 101 ARG C CB  1 
ATOM   3411 C CG  . ARG C 1 101 ? -28.82559 43.59855  2.65897   1.000 166.56299 ? 101 ARG C CG  1 
ATOM   3412 C CD  . ARG C 1 101 ? -28.23063 44.17061  1.38433   1.000 162.92246 ? 101 ARG C CD  1 
ATOM   3413 N NE  . ARG C 1 101 ? -27.38319 43.19542  0.70877   1.000 176.29010 ? 101 ARG C NE  1 
ATOM   3414 C CZ  . ARG C 1 101 ? -26.59585 43.47071  -0.32173  1.000 182.76431 ? 101 ARG C CZ  1 
ATOM   3415 N NH1 . ARG C 1 101 ? -26.53444 44.68661  -0.83912  1.000 188.91698 ? 101 ARG C NH1 1 
ATOM   3416 N NH2 . ARG C 1 101 ? -25.85047 42.50162  -0.84564  1.000 180.42719 ? 101 ARG C NH2 1 
ATOM   3417 N N   . PRO C 1 102 ? -30.83821 42.69760  6.35345   1.000 172.06556 ? 102 PRO C N   1 
ATOM   3418 C CA  . PRO C 1 102 ? -30.23362 42.34659  7.64574   1.000 179.19180 ? 102 PRO C CA  1 
ATOM   3419 C C   . PRO C 1 102 ? -28.98896 41.47725  7.54243   1.000 187.17695 ? 102 PRO C C   1 
ATOM   3420 O O   . PRO C 1 102 ? -28.41542 41.13478  8.58324   1.000 192.13923 ? 102 PRO C O   1 
ATOM   3421 C CB  . PRO C 1 102 ? -31.36607 41.59472  8.36169   1.000 167.38639 ? 102 PRO C CB  1 
ATOM   3422 C CG  . PRO C 1 102 ? -32.19241 41.03065  7.26790   1.000 156.41155 ? 102 PRO C CG  1 
ATOM   3423 C CD  . PRO C 1 102 ? -32.12683 42.01751  6.13914   1.000 148.04589 ? 102 PRO C CD  1 
ATOM   3424 N N   . ILE C 1 103 ? -28.56626 41.11194  6.33232   1.000 185.98932 ? 103 ILE C N   1 
ATOM   3425 C CA  . ILE C 1 103 ? -27.39435 40.26114  6.11229   1.000 199.12963 ? 103 ILE C CA  1 
ATOM   3426 C C   . ILE C 1 103 ? -27.52026 38.95171  6.88719   1.000 206.74208 ? 103 ILE C C   1 
ATOM   3427 O O   . ILE C 1 103 ? -27.45260 37.86590  6.30955   1.000 209.68302 ? 103 ILE C O   1 
ATOM   3428 C CB  . ILE C 1 103 ? -26.08140 40.98998  6.48268   1.000 202.07603 ? 103 ILE C CB  1 
ATOM   3429 C CG1 . ILE C 1 103 ? -25.87184 42.21336  5.58754   1.000 196.52047 ? 103 ILE C CG1 1 
ATOM   3430 C CG2 . ILE C 1 103 ? -24.89198 40.04223  6.37787   1.000 194.37646 ? 103 ILE C CG2 1 
ATOM   3431 C CD1 . ILE C 1 103 ? -24.62481 43.00827  5.92158   1.000 188.63977 ? 103 ILE C CD1 1 
ATOM   3432 N N   . GLY C 1 113 ? -44.38590 30.85311  16.02024  1.000 113.94372 ? 113 GLY C N   1 
ATOM   3433 C CA  . GLY C 1 113 ? -44.00477 31.82562  17.02569  1.000 134.87700 ? 113 GLY C CA  1 
ATOM   3434 C C   . GLY C 1 113 ? -44.71523 33.15725  16.87499  1.000 146.39936 ? 113 GLY C C   1 
ATOM   3435 O O   . GLY C 1 113 ? -45.89376 33.21041  16.51784  1.000 141.25599 ? 113 GLY C O   1 
ATOM   3436 N N   . SER C 1 114 ? -43.99041 34.23743  17.15423  1.000 154.08906 ? 114 SER C N   1 
ATOM   3437 C CA  . SER C 1 114 ? -44.55085 35.57885  17.06735  1.000 157.11080 ? 114 SER C CA  1 
ATOM   3438 C C   . SER C 1 114 ? -44.10262 36.28575  15.79333  1.000 155.17374 ? 114 SER C C   1 
ATOM   3439 O O   . SER C 1 114 ? -42.95760 36.11935  15.35602  1.000 155.86602 ? 114 SER C O   1 
ATOM   3440 C CB  . SER C 1 114 ? -44.14064 36.41807  18.27799  1.000 162.47619 ? 114 SER C CB  1 
ATOM   3441 O OG  . SER C 1 114 ? -42.73488 36.58308  18.34268  1.000 166.16470 ? 114 SER C OG  1 
ATOM   3442 N N   . PRO C 1 115 ? -44.98747 37.07158  15.19124  1.000 137.32462 ? 115 PRO C N   1 
ATOM   3443 C CA  . PRO C 1 115 ? -44.67745 37.72510  13.91912  1.000 132.26792 ? 115 PRO C CA  1 
ATOM   3444 C C   . PRO C 1 115 ? -43.96006 39.05811  14.11848  1.000 119.45456 ? 115 PRO C C   1 
ATOM   3445 O O   . PRO C 1 115 ? -43.86618 39.59455  15.22525  1.000 120.45982 ? 115 PRO C O   1 
ATOM   3446 C CB  . PRO C 1 115 ? -46.06649 37.91868  13.31261  1.000 114.75810 ? 115 PRO C CB  1 
ATOM   3447 C CG  . PRO C 1 115 ? -46.91911 38.21149  14.50120  1.000 121.03263 ? 115 PRO C CG  1 
ATOM   3448 C CD  . PRO C 1 115 ? -46.35418 37.39645  15.64933  1.000 125.85201 ? 115 PRO C CD  1 
ATOM   3449 N N   . VAL C 1 116 ? -43.45604 39.59025  13.00988  1.000 108.49251 ? 116 VAL C N   1 
ATOM   3450 C CA  . VAL C 1 116 ? -42.79090 40.88714  13.04418  1.000 99.93456  ? 116 VAL C CA  1 
ATOM   3451 C C   . VAL C 1 116 ? -43.76472 41.99987  12.69115  1.000 86.92756  ? 116 VAL C C   1 
ATOM   3452 O O   . VAL C 1 116 ? -43.73845 43.06730  13.30577  1.000 81.52520  ? 116 VAL C O   1 
ATOM   3453 C CB  . VAL C 1 116 ? -41.56383 40.89037  12.11142  1.000 95.24805  ? 116 VAL C CB  1 
ATOM   3454 C CG1 . VAL C 1 116 ? -40.40261 40.16387  12.76685  1.000 99.27655  ? 116 VAL C CG1 1 
ATOM   3455 C CG2 . VAL C 1 116 ? -41.90419 40.25693  10.77438  1.000 108.45849 ? 116 VAL C CG2 1 
ATOM   3456 N N   . LEU C 1 117 ? -44.62117 41.78454  11.69744  1.000 81.66673  ? 117 LEU C N   1 
ATOM   3457 C CA  . LEU C 1 117 ? -45.65140 42.75200  11.35224  1.000 74.79223  ? 117 LEU C CA  1 
ATOM   3458 C C   . LEU C 1 117 ? -46.87806 42.43545  12.20212  1.000 73.90588  ? 117 LEU C C   1 
ATOM   3459 O O   . LEU C 1 117 ? -47.41972 41.32696  12.12821  1.000 79.17006  ? 117 LEU C O   1 
ATOM   3460 C CB  . LEU C 1 117 ? -45.98955 42.69963  9.86510   1.000 63.63694  ? 117 LEU C CB  1 
ATOM   3461 C CG  . LEU C 1 117 ? -46.93695 43.81387  9.42389   1.000 69.18457  ? 117 LEU C CG  1 
ATOM   3462 C CD1 . LEU C 1 117 ? -46.29281 45.17240  9.65687   1.000 68.39978  ? 117 LEU C CD1 1 
ATOM   3463 C CD2 . LEU C 1 117 ? -47.35509 43.64911  7.97643   1.000 70.91487  ? 117 LEU C CD2 1 
ATOM   3464 N N   . THR C 1 118 ? -47.31096 43.39849  13.00557  1.000 73.47729  ? 118 THR C N   1 
ATOM   3465 C CA  . THR C 1 118 ? -48.47241 43.24319  13.86712  1.000 74.86633  ? 118 THR C CA  1 
ATOM   3466 C C   . THR C 1 118 ? -49.51710 44.30205  13.53375  1.000 71.76805  ? 118 THR C C   1 
ATOM   3467 O O   . THR C 1 118 ? -49.21459 45.34364  12.94586  1.000 69.49645  ? 118 THR C O   1 
ATOM   3468 C CB  . THR C 1 118 ? -48.08179 43.31199  15.35116  1.000 73.53258  ? 118 THR C CB  1 
ATOM   3469 O OG1 . THR C 1 118 ? -47.03414 44.27269  15.52712  1.000 82.41134  ? 118 THR C OG1 1 
ATOM   3470 C CG2 . THR C 1 118 ? -47.60652 41.95284  15.84234  1.000 76.59459  ? 118 THR C CG2 1 
ATOM   3471 N N   . GLY C 1 119 ? -50.75735 44.02835  13.92457  1.000 74.39409  ? 119 GLY C N   1 
ATOM   3472 C CA  . GLY C 1 119 ? -51.84203 44.93029  13.60336  1.000 63.79414  ? 119 GLY C CA  1 
ATOM   3473 C C   . GLY C 1 119 ? -52.77671 44.35191  12.56401  1.000 71.93762  ? 119 GLY C C   1 
ATOM   3474 O O   . GLY C 1 119 ? -52.89273 43.12871  12.44327  1.000 75.58387  ? 119 GLY C O   1 
ATOM   3475 N N   . VAL C 1 120 ? -53.44835 45.20987  11.80294  1.000 74.32526  ? 120 VAL C N   1 
ATOM   3476 C CA  . VAL C 1 120 ? -54.38529 44.77250  10.77319  1.000 74.36460  ? 120 VAL C CA  1 
ATOM   3477 C C   . VAL C 1 120 ? -53.70522 44.96257  9.42030   1.000 66.88089  ? 120 VAL C C   1 
ATOM   3478 O O   . VAL C 1 120 ? -53.56430 46.10865  8.96355   1.000 65.63361  ? 120 VAL C O   1 
ATOM   3479 C CB  . VAL C 1 120 ? -55.70483 45.55011  10.84421  1.000 69.87987  ? 120 VAL C CB  1 
ATOM   3480 C CG1 . VAL C 1 120 ? -56.60389 45.16505  9.68515   1.000 74.95395  ? 120 VAL C CG1 1 
ATOM   3481 C CG2 . VAL C 1 120 ? -56.39647 45.28832  12.16571  1.000 82.20208  ? 120 VAL C CG2 1 
ATOM   3482 N N   . PRO C 1 121 ? -53.26507 43.89361  8.76149   1.000 74.03013  ? 121 PRO C N   1 
ATOM   3483 C CA  . PRO C 1 121 ? -52.54906 44.02169  7.48527   1.000 62.03005  ? 121 PRO C CA  1 
ATOM   3484 C C   . PRO C 1 121 ? -53.43245 43.96721  6.24776   1.000 61.78457  ? 121 PRO C C   1 
ATOM   3485 O O   . PRO C 1 121 ? -52.89402 43.89969  5.13944   1.000 61.69195  ? 121 PRO C O   1 
ATOM   3486 C CB  . PRO C 1 121 ? -51.61370 42.80736  7.52126   1.000 60.91992  ? 121 PRO C CB  1 
ATOM   3487 C CG  . PRO C 1 121 ? -52.42082 41.77361  8.24908   1.000 60.86589  ? 121 PRO C CG  1 
ATOM   3488 C CD  . PRO C 1 121 ? -53.25015 42.51112  9.27091   1.000 61.42340  ? 121 PRO C CD  1 
ATOM   3489 N N   . VAL C 1 122 ? -54.75326 43.96059  6.40115   1.000 62.42077  ? 122 VAL C N   1 
ATOM   3490 C CA  . VAL C 1 122 ? -55.68287 43.92795  5.27863   1.000 64.88674  ? 122 VAL C CA  1 
ATOM   3491 C C   . VAL C 1 122 ? -56.54082 45.18324  5.32074   1.000 68.35738  ? 122 VAL C C   1 
ATOM   3492 O O   . VAL C 1 122 ? -57.15782 45.48583  6.34872   1.000 73.55671  ? 122 VAL C O   1 
ATOM   3493 C CB  . VAL C 1 122 ? -56.56760 42.66967  5.29485   1.000 63.32582  ? 122 VAL C CB  1 
ATOM   3494 C CG1 . VAL C 1 122 ? -57.49959 42.67710  4.09878   1.000 74.85138  ? 122 VAL C CG1 1 
ATOM   3495 C CG2 . VAL C 1 122 ? -55.71076 41.41776  5.29169   1.000 72.17835  ? 122 VAL C CG2 1 
ATOM   3496 N N   . ALA C 1 123 ? -56.57231 45.91463  4.21238   1.000 65.55128  ? 123 ALA C N   1 
ATOM   3497 C CA  . ALA C 1 123 ? -57.36236 47.13331  4.10079   1.000 74.93287  ? 123 ALA C CA  1 
ATOM   3498 C C   . ALA C 1 123 ? -58.41018 46.94654  3.01522   1.000 68.99299  ? 123 ALA C C   1 
ATOM   3499 O O   . ALA C 1 123 ? -58.11755 46.40645  1.94282   1.000 68.72578  ? 123 ALA C O   1 
ATOM   3500 C CB  . ALA C 1 123 ? -56.49029 48.35762  3.77723   1.000 67.90685  ? 123 ALA C CB  1 
ATOM   3501 N N   . GLY C 1 124 ? -59.62944 47.40256  3.29175   1.000 70.94919  ? 124 GLY C N   1 
ATOM   3502 C CA  . GLY C 1 124 ? -60.65180 47.41964  2.27045   1.000 73.13106  ? 124 GLY C CA  1 
ATOM   3503 C C   . GLY C 1 124 ? -60.58372 48.68488  1.43602   1.000 75.02045  ? 124 GLY C C   1 
ATOM   3504 O O   . GLY C 1 124 ? -59.92257 49.66075  1.78632   1.000 82.35277  ? 124 GLY C O   1 
ATOM   3505 N N   . VAL C 1 125 ? -61.29361 48.66800  0.32144   1.000 74.45225  ? 125 VAL C N   1 
ATOM   3506 C CA  . VAL C 1 125 ? -61.23292 49.77362  -0.62481  1.000 70.23165  ? 125 VAL C CA  1 
ATOM   3507 C C   . VAL C 1 125 ? -62.28890 50.80596  -0.26342  1.000 81.40493  ? 125 VAL C C   1 
ATOM   3508 O O   . VAL C 1 125 ? -63.39067 50.46728  0.18402   1.000 72.66605  ? 125 VAL C O   1 
ATOM   3509 C CB  . VAL C 1 125 ? -61.41252 49.26405  -2.06873  1.000 67.74719  ? 125 VAL C CB  1 
ATOM   3510 C CG1 . VAL C 1 125 ? -62.77681 48.60974  -2.24722  1.000 80.59771  ? 125 VAL C CG1 1 
ATOM   3511 C CG2 . VAL C 1 125 ? -61.21223 50.39528  -3.06895  1.000 77.90106  ? 125 VAL C CG2 1 
ATOM   3512 N N   . ALA C 1 126 ? -61.93052 52.07876  -0.42261  1.000 77.95690  ? 126 ALA C N   1 
ATOM   3513 C CA  . ALA C 1 126 ? -62.85473 53.19462  -0.28160  1.000 77.12701  ? 126 ALA C CA  1 
ATOM   3514 C C   . ALA C 1 126 ? -62.76472 54.05815  -1.52835  1.000 78.51419  ? 126 ALA C C   1 
ATOM   3515 O O   . ALA C 1 126 ? -61.67128 54.48869  -1.90960  1.000 85.73331  ? 126 ALA C O   1 
ATOM   3516 C CB  . ALA C 1 126 ? -62.55017 54.02679  0.96722   1.000 65.13075  ? 126 ALA C CB  1 
ATOM   3517 N N   . TYR C 1 127 ? -63.90450 54.29560  -2.16709  1.000 78.65927  ? 127 TYR C N   1 
ATOM   3518 C CA  . TYR C 1 127 ? -63.94705 55.05085  -3.40927  1.000 90.02175  ? 127 TYR C CA  1 
ATOM   3519 C C   . TYR C 1 127 ? -64.10780 56.53160  -3.08539  1.000 89.38022  ? 127 TYR C C   1 
ATOM   3520 O O   . TYR C 1 127 ? -65.02772 56.91525  -2.35629  1.000 93.83898  ? 127 TYR C O   1 
ATOM   3521 C CB  . TYR C 1 127 ? -65.09104 54.55357  -4.29525  1.000 83.33345  ? 127 TYR C CB  1 
ATOM   3522 C CG  . TYR C 1 127 ? -64.87296 53.14480  -4.81395  1.000 83.07889  ? 127 TYR C CG  1 
ATOM   3523 C CD1 . TYR C 1 127 ? -64.06771 52.90253  -5.92104  1.000 91.85920  ? 127 TYR C CD1 1 
ATOM   3524 C CD2 . TYR C 1 127 ? -65.47214 52.05653  -4.19232  1.000 72.79938  ? 127 TYR C CD2 1 
ATOM   3525 C CE1 . TYR C 1 127 ? -63.86484 51.61589  -6.39328  1.000 87.15676  ? 127 TYR C CE1 1 
ATOM   3526 C CE2 . TYR C 1 127 ? -65.27313 50.76474  -4.65728  1.000 88.38762  ? 127 TYR C CE2 1 
ATOM   3527 C CZ  . TYR C 1 127 ? -64.47041 50.55171  -5.75817  1.000 87.69821  ? 127 TYR C CZ  1 
ATOM   3528 O OH  . TYR C 1 127 ? -64.27311 49.27069  -6.22412  1.000 85.21772  ? 127 TYR C OH  1 
ATOM   3529 N N   . LEU C 1 128 ? -63.20872 57.35805  -3.61694  1.000 97.25571  ? 128 LEU C N   1 
ATOM   3530 C CA  . LEU C 1 128 ? -63.16404 58.77324  -3.27532  1.000 97.01117  ? 128 LEU C CA  1 
ATOM   3531 C C   . LEU C 1 128 ? -62.97715 59.59709  -4.54144  1.000 96.30549  ? 128 LEU C C   1 
ATOM   3532 O O   . LEU C 1 128 ? -62.47005 59.10796  -5.55320  1.000 84.46032  ? 128 LEU C O   1 
ATOM   3533 C CB  . LEU C 1 128 ? -62.02838 59.08081  -2.28868  1.000 94.88177  ? 128 LEU C CB  1 
ATOM   3534 C CG  . LEU C 1 128 ? -62.06132 58.40262  -0.91805  1.000 92.96537  ? 128 LEU C CG  1 
ATOM   3535 C CD1 . LEU C 1 128 ? -60.85176 58.82481  -0.10177  1.000 92.82531  ? 128 LEU C CD1 1 
ATOM   3536 C CD2 . LEU C 1 128 ? -63.34944 58.73185  -0.18324  1.000 88.81782  ? 128 LEU C CD2 1 
ATOM   3537 N N   . ASP C 1 129 ? -63.40619 60.86215  -4.47878  1.000 112.27829 ? 129 ASP C N   1 
ATOM   3538 C CA  . ASP C 1 129 ? -63.24228 61.78061  -5.60014  1.000 103.31509 ? 129 ASP C CA  1 
ATOM   3539 C C   . ASP C 1 129 ? -62.02994 62.68947  -5.45578  1.000 96.06036  ? 129 ASP C C   1 
ATOM   3540 O O   . ASP C 1 129 ? -61.60076 63.28419  -6.44994  1.000 103.23140 ? 129 ASP C O   1 
ATOM   3541 C CB  . ASP C 1 129 ? -64.49545 62.64864  -5.79118  1.000 110.26277 ? 129 ASP C CB  1 
ATOM   3542 C CG  . ASP C 1 129 ? -65.78511 61.88719  -5.54467  1.000 124.42579 ? 129 ASP C CG  1 
ATOM   3543 O OD1 . ASP C 1 129 ? -66.09034 60.96368  -6.33045  1.000 129.82877 ? 129 ASP C OD1 1 
ATOM   3544 O OD2 . ASP C 1 129 ? -66.50157 62.22098  -4.57811  1.000 125.59438 ? 129 ASP C OD2 1 
ATOM   3545 N N   . LYS C 1 130 ? -61.46866 62.80552  -4.25359  1.000 97.62599  ? 130 LYS C N   1 
ATOM   3546 C CA  . LYS C 1 130 ? -60.29948 63.63072  -4.00114  1.000 94.45609  ? 130 LYS C CA  1 
ATOM   3547 C C   . LYS C 1 130 ? -59.24001 62.81322  -3.27721  1.000 102.38877 ? 130 LYS C C   1 
ATOM   3548 O O   . LYS C 1 130 ? -59.56988 61.97314  -2.43091  1.000 105.56945 ? 130 LYS C O   1 
ATOM   3549 C CB  . LYS C 1 130 ? -60.64984 64.89242  -3.19652  1.000 98.23722  ? 130 LYS C CB  1 
ATOM   3550 C CG  . LYS C 1 130 ? -61.11744 66.04513  -4.07473  1.000 95.97450  ? 130 LYS C CG  1 
ATOM   3551 C CD  . LYS C 1 130 ? -60.25553 66.13137  -5.33556  1.000 112.87767 ? 130 LYS C CD  1 
ATOM   3552 C CE  . LYS C 1 130 ? -60.20086 67.53725  -5.90666  1.000 102.80130 ? 130 LYS C CE  1 
ATOM   3553 N NZ  . LYS C 1 130 ? -61.52771 68.19601  -5.85154  1.000 104.43121 ? 130 LYS C NZ  1 
ATOM   3554 N N   . PRO C 1 131 ? -57.95537 63.04424  -3.58078  1.000 108.39446 ? 131 PRO C N   1 
ATOM   3555 C CA  . PRO C 1 131 ? -57.42444 64.01600  -4.55306  1.000 94.20076  ? 131 PRO C CA  1 
ATOM   3556 C C   . PRO C 1 131 ? -57.67147 63.59832  -5.99400  1.000 104.07663 ? 131 PRO C C   1 
ATOM   3557 O O   . PRO C 1 131 ? -57.71030 64.42628  -6.90149  1.000 99.76783  ? 131 PRO C O   1 
ATOM   3558 C CB  . PRO C 1 131 ? -55.92877 64.04274  -4.21433  1.000 98.27066  ? 131 PRO C CB  1 
ATOM   3559 C CG  . PRO C 1 131 ? -55.64834 62.64268  -3.74510  1.000 96.33808  ? 131 PRO C CG  1 
ATOM   3560 C CD  . PRO C 1 131 ? -56.87760 62.25349  -2.95793  1.000 96.30463  ? 131 PRO C CD  1 
ATOM   3561 N N   . ASN C 1 132 ? -57.86728 62.30419  -6.21349  1.000 107.74362 ? 132 ASN C N   1 
ATOM   3562 C CA  . ASN C 1 132 ? -58.22930 61.76680  -7.51272  1.000 100.21955 ? 132 ASN C CA  1 
ATOM   3563 C C   . ASN C 1 132 ? -59.44099 60.86361  -7.34755  1.000 96.77088  ? 132 ASN C C   1 
ATOM   3564 O O   . ASN C 1 132 ? -59.70273 60.32587  -6.26800  1.000 94.77783  ? 132 ASN C O   1 
ATOM   3565 C CB  . ASN C 1 132 ? -57.07478 60.96986  -8.14915  1.000 102.93986 ? 132 ASN C CB  1 
ATOM   3566 C CG  . ASN C 1 132 ? -55.77303 61.75104  -8.20525  1.000 101.62140 ? 132 ASN C CG  1 
ATOM   3567 O OD1 . ASN C 1 132 ? -55.77022 62.97921  -8.24736  1.000 114.50517 ? 132 ASN C OD1 1 
ATOM   3568 N ND2 . ASN C 1 132 ? -54.65510 61.03482  -8.17822  1.000 107.00274 ? 132 ASN C ND2 1 
ATOM   3569 N N   . ARG C 1 133 ? -60.18749 60.70634  -8.43231  1.000 90.25173  ? 133 ARG C N   1 
ATOM   3570 C CA  . ARG C 1 133 ? -61.35637 59.83437  -8.42193  1.000 103.71666 ? 133 ARG C CA  1 
ATOM   3571 C C   . ARG C 1 133 ? -60.87109 58.40718  -8.64525  1.000 95.14731  ? 133 ARG C C   1 
ATOM   3572 O O   . ARG C 1 133 ? -60.60006 58.00219  -9.77860  1.000 93.25198  ? 133 ARG C O   1 
ATOM   3573 C CB  . ARG C 1 133 ? -62.36276 60.27262  -9.47853  1.000 107.23261 ? 133 ARG C CB  1 
ATOM   3574 C CG  . ARG C 1 133 ? -62.86735 61.69348  -9.27936  1.000 102.34231 ? 133 ARG C CG  1 
ATOM   3575 C CD  . ARG C 1 133 ? -63.65200 62.17620  -10.47790 1.000 110.15882 ? 133 ARG C CD  1 
ATOM   3576 N NE  . ARG C 1 133 ? -65.03190 61.70203  -10.46116 1.000 131.77438 ? 133 ARG C NE  1 
ATOM   3577 C CZ  . ARG C 1 133 ? -66.01101 62.24683  -9.75103  1.000 129.23967 ? 133 ARG C CZ  1 
ATOM   3578 N NH1 . ARG C 1 133 ? -65.80461 63.30754  -8.98715  1.000 113.21418 ? 133 ARG C NH1 1 
ATOM   3579 N NH2 . ARG C 1 133 ? -67.23066 61.71836  -9.81583  1.000 128.29209 ? 133 ARG C NH2 1 
ATOM   3580 N N   . ALA C 1 134 ? -60.75885 57.64113  -7.56071  1.000 89.90966  ? 134 ALA C N   1 
ATOM   3581 C CA  . ALA C 1 134 ? -60.18209 56.29926  -7.60177  1.000 91.17131  ? 134 ALA C CA  1 
ATOM   3582 C C   . ALA C 1 134 ? -60.52057 55.58011  -6.30132  1.000 92.47089  ? 134 ALA C C   1 
ATOM   3583 O O   . ALA C 1 134 ? -61.14273 56.14443  -5.39561  1.000 86.75793  ? 134 ALA C O   1 
ATOM   3584 C CB  . ALA C 1 134 ? -58.66537 56.34444  -7.80611  1.000 63.35100  ? 134 ALA C CB  1 
ATOM   3585 N N   . GLY C 1 135 ? -60.09310 54.32029  -6.21903  1.000 85.10671  ? 135 GLY C N   1 
ATOM   3586 C CA  . GLY C 1 135 ? -60.17979 53.56584  -4.98696  1.000 70.82497  ? 135 GLY C CA  1 
ATOM   3587 C C   . GLY C 1 135 ? -58.95684 53.82596  -4.12703  1.000 67.54190  ? 135 GLY C C   1 
ATOM   3588 O O   . GLY C 1 135 ? -57.87487 54.11896  -4.62949  1.000 71.55108  ? 135 GLY C O   1 
ATOM   3589 N N   . TYR C 1 136 ? -59.13378 53.69970  -2.81462  1.000 66.77991  ? 136 TYR C N   1 
ATOM   3590 C CA  . TYR C 1 136 ? -58.07916 54.04002  -1.87277  1.000 69.75599  ? 136 TYR C CA  1 
ATOM   3591 C C   . TYR C 1 136 ? -58.02654 53.02488  -0.74514  1.000 62.89228  ? 136 TYR C C   1 
ATOM   3592 O O   . TYR C 1 136 ? -59.06736 52.57945  -0.25359  1.000 67.67992  ? 136 TYR C O   1 
ATOM   3593 C CB  . TYR C 1 136 ? -58.30405 55.45014  -1.29969  1.000 67.16505  ? 136 TYR C CB  1 
ATOM   3594 C CG  . TYR C 1 136 ? -58.01794 56.56202  -2.28497  1.000 67.23894  ? 136 TYR C CG  1 
ATOM   3595 C CD1 . TYR C 1 136 ? -56.74167 57.10039  -2.40505  1.000 68.75481  ? 136 TYR C CD1 1 
ATOM   3596 C CD2 . TYR C 1 136 ? -59.01462 57.04864  -3.11978  1.000 76.63472  ? 136 TYR C CD2 1 
ATOM   3597 C CE1 . TYR C 1 136 ? -56.47350 58.10949  -3.31093  1.000 74.63833  ? 136 TYR C CE1 1 
ATOM   3598 C CE2 . TYR C 1 136 ? -58.75664 58.05606  -4.02992  1.000 85.53041  ? 136 TYR C CE2 1 
ATOM   3599 C CZ  . TYR C 1 136 ? -57.48725 58.58370  -4.12293  1.000 87.45770  ? 136 TYR C CZ  1 
ATOM   3600 O OH  . TYR C 1 136 ? -57.23621 59.58824  -5.03194  1.000 89.35808  ? 136 TYR C OH  1 
ATOM   3601 N N   . PHE C 1 137 ? -56.80633 52.65497  -0.35398  1.000 54.14606  ? 137 PHE C N   1 
ATOM   3602 C CA  . PHE C 1 137 ? -56.55495 51.80344  0.79971   1.000 50.36298  ? 137 PHE C CA  1 
ATOM   3603 C C   . PHE C 1 137 ? -55.64031 52.53476  1.77423   1.000 58.94653  ? 137 PHE C C   1 
ATOM   3604 O O   . PHE C 1 137 ? -54.66330 53.16714  1.36059   1.000 64.64995  ? 137 PHE C O   1 
ATOM   3605 C CB  . PHE C 1 137 ? -55.89134 50.48274  0.38729   1.000 53.53756  ? 137 PHE C CB  1 
ATOM   3606 C CG  . PHE C 1 137 ? -56.65041 49.69950  -0.65464  1.000 62.16784  ? 137 PHE C CG  1 
ATOM   3607 C CD1 . PHE C 1 137 ? -56.46061 49.95355  -2.00396  1.000 63.02324  ? 137 PHE C CD1 1 
ATOM   3608 C CD2 . PHE C 1 137 ? -57.50446 48.67159  -0.28903  1.000 67.37610  ? 137 PHE C CD2 1 
ATOM   3609 C CE1 . PHE C 1 137 ? -57.13419 49.22637  -2.96821  1.000 61.14911  ? 137 PHE C CE1 1 
ATOM   3610 C CE2 . PHE C 1 137 ? -58.17642 47.93002  -1.24951  1.000 57.96148  ? 137 PHE C CE2 1 
ATOM   3611 C CZ  . PHE C 1 137 ? -57.99300 48.21209  -2.59097  1.000 61.59472  ? 137 PHE C CZ  1 
ATOM   3612 N N   . ILE C 1 138 ? -55.94763 52.44450  3.06836   1.000 50.74320  ? 138 ILE C N   1 
ATOM   3613 C CA  . ILE C 1 138 ? -55.15582 53.08482  4.11339   1.000 56.50131  ? 138 ILE C CA  1 
ATOM   3614 C C   . ILE C 1 138 ? -54.79553 52.04517  5.16483   1.000 61.52200  ? 138 ILE C C   1 
ATOM   3615 O O   . ILE C 1 138 ? -55.63613 51.22666  5.55512   1.000 59.24174  ? 138 ILE C O   1 
ATOM   3616 C CB  . ILE C 1 138 ? -55.89113 54.28203  4.75604   1.000 65.80599  ? 138 ILE C CB  1 
ATOM   3617 C CG1 . ILE C 1 138 ? -55.03042 54.92565  5.84476   1.000 69.10423  ? 138 ILE C CG1 1 
ATOM   3618 C CG2 . ILE C 1 138 ? -57.22187 53.86337  5.34408   1.000 55.67726  ? 138 ILE C CG2 1 
ATOM   3619 C CD1 . ILE C 1 138 ? -55.11011 56.43589  5.85620   1.000 56.70878  ? 138 ILE C CD1 1 
ATOM   3620 N N   . PHE C 1 139 ? -53.54943 52.09741  5.64379   1.000 51.50552  ? 139 PHE C N   1 
ATOM   3621 C CA  . PHE C 1 139 ? -53.01806 51.15020  6.62090   1.000 65.31961  ? 139 PHE C CA  1 
ATOM   3622 C C   . PHE C 1 139 ? -52.58077 51.91504  7.86386   1.000 57.39892  ? 139 PHE C C   1 
ATOM   3623 O O   . PHE C 1 139 ? -51.39534 52.24394  8.01412   1.000 63.12278  ? 139 PHE C O   1 
ATOM   3624 C CB  . PHE C 1 139 ? -51.85242 50.35359  6.04349   1.000 62.82855  ? 139 PHE C CB  1 
ATOM   3625 C CG  . PHE C 1 139 ? -52.25149 49.34634  5.00652   1.000 61.19636  ? 139 PHE C CG  1 
ATOM   3626 C CD1 . PHE C 1 139 ? -52.62560 48.06508  5.37416   1.000 64.64469  ? 139 PHE C CD1 1 
ATOM   3627 C CD2 . PHE C 1 139 ? -52.22469 49.67278  3.66296   1.000 65.68068  ? 139 PHE C CD2 1 
ATOM   3628 C CE1 . PHE C 1 139 ? -52.97396 47.13237  4.42144   1.000 62.37003  ? 139 PHE C CE1 1 
ATOM   3629 C CE2 . PHE C 1 139 ? -52.57375 48.74657  2.70618   1.000 66.59559  ? 139 PHE C CE2 1 
ATOM   3630 C CZ  . PHE C 1 139 ? -52.94790 47.47324  3.08509   1.000 62.86888  ? 139 PHE C CZ  1 
ATOM   3631 N N   . PRO C 1 140 ? -53.49916 52.20195  8.78879   1.000 63.53813  ? 140 PRO C N   1 
ATOM   3632 C CA  . PRO C 1 140 ? -53.13072 53.01877  9.94788   1.000 65.89833  ? 140 PRO C CA  1 
ATOM   3633 C C   . PRO C 1 140 ? -52.67350 52.22607  11.15984  1.000 59.89977  ? 140 PRO C C   1 
ATOM   3634 O O   . PRO C 1 140 ? -52.26625 52.84112  12.15506  1.000 80.05156  ? 140 PRO C O   1 
ATOM   3635 C CB  . PRO C 1 140 ? -54.44243 53.75776  10.25944  1.000 57.26668  ? 140 PRO C CB  1 
ATOM   3636 C CG  . PRO C 1 140 ? -55.49652 52.77157  9.86705   1.000 66.20655  ? 140 PRO C CG  1 
ATOM   3637 C CD  . PRO C 1 140 ? -54.95904 52.04110  8.66300   1.000 61.82367  ? 140 PRO C CD  1 
ATOM   3638 N N   . ASP C 1 141 ? -52.73918 50.90054  11.12209  1.000 68.16840  ? 141 ASP C N   1 
ATOM   3639 C CA  . ASP C 1 141 ? -52.53982 50.07489  12.30898  1.000 72.54779  ? 141 ASP C CA  1 
ATOM   3640 C C   . ASP C 1 141 ? -51.48741 49.00259  12.02942  1.000 69.80826  ? 141 ASP C C   1 
ATOM   3641 O O   . ASP C 1 141 ? -51.70707 47.80982  12.24428  1.000 87.53362  ? 141 ASP C O   1 
ATOM   3642 C CB  . ASP C 1 141 ? -53.86350 49.46884  12.76926  1.000 85.13297  ? 141 ASP C CB  1 
ATOM   3643 C CG  . ASP C 1 141 ? -53.73551 48.70719  14.07552  1.000 104.25797 ? 141 ASP C CG  1 
ATOM   3644 O OD1 . ASP C 1 141 ? -52.76120 48.96089  14.81594  1.000 106.82805 ? 141 ASP C OD1 1 
ATOM   3645 O OD2 . ASP C 1 141 ? -54.60265 47.85141  14.35714  1.000 115.59259 ? 141 ASP C OD2 1 
ATOM   3646 N N   . LEU C 1 142 ? -50.32384 49.41103  11.53071  1.000 68.15772  ? 142 LEU C N   1 
ATOM   3647 C CA  . LEU C 1 142 ? -49.21628 48.49785  11.27442  1.000 68.43639  ? 142 LEU C CA  1 
ATOM   3648 C C   . LEU C 1 142 ? -48.07797 48.75009  12.25396  1.000 60.89581  ? 142 LEU C C   1 
ATOM   3649 O O   . LEU C 1 142 ? -47.62896 49.88961  12.40574  1.000 78.40205  ? 142 LEU C O   1 
ATOM   3650 C CB  . LEU C 1 142 ? -48.70803 48.67367  9.84448   1.000 63.17478  ? 142 LEU C CB  1 
ATOM   3651 C CG  . LEU C 1 142 ? -49.70206 48.34270  8.73994   1.000 65.15810  ? 142 LEU C CG  1 
ATOM   3652 C CD1 . LEU C 1 142 ? -49.08009 48.66355  7.39606   1.000 61.25001  ? 142 LEU C CD1 1 
ATOM   3653 C CD2 . LEU C 1 142 ? -50.11266 46.87755  8.82300   1.000 63.78569  ? 142 LEU C CD2 1 
ATOM   3654 N N   . SER C 1 143 ? -47.59517 47.68194  12.89028  1.000 68.67212  ? 143 SER C N   1 
ATOM   3655 C CA  . SER C 1 143 ? -46.51172 47.75857  13.86049  1.000 63.13065  ? 143 SER C CA  1 
ATOM   3656 C C   . SER C 1 143 ? -45.42141 46.75184  13.51925  1.000 64.58659  ? 143 SER C C   1 
ATOM   3657 O O   . SER C 1 143 ? -45.69063 45.67661  12.97898  1.000 75.95413  ? 143 SER C O   1 
ATOM   3658 C CB  . SER C 1 143 ? -47.00893 47.52803  15.29129  1.000 60.07179  ? 143 SER C CB  1 
ATOM   3659 O OG  . SER C 1 143 ? -47.86667 48.57911  15.69981  1.000 83.68458  ? 143 SER C OG  1 
ATOM   3660 N N   . VAL C 1 144 ? -44.18310 47.13154  13.81907  1.000 64.64209  ? 144 VAL C N   1 
ATOM   3661 C CA  . VAL C 1 144 ? -42.99442 46.33853  13.53648  1.000 53.72865  ? 144 VAL C CA  1 
ATOM   3662 C C   . VAL C 1 144 ? -42.30282 46.03803  14.85743  1.000 70.59632  ? 144 VAL C C   1 
ATOM   3663 O O   . VAL C 1 144 ? -42.06558 46.94440  15.66296  1.000 80.59069  ? 144 VAL C O   1 
ATOM   3664 C CB  . VAL C 1 144 ? -42.05071 47.04440  12.54882  1.000 69.82658  ? 144 VAL C CB  1 
ATOM   3665 C CG1 . VAL C 1 144 ? -40.89953 46.13541  12.18937  1.000 69.96561  ? 144 VAL C CG1 1 
ATOM   3666 C CG2 . VAL C 1 144 ? -42.81556 47.38056  11.28749  1.000 54.89279  ? 144 VAL C CG2 1 
ATOM   3667 N N   . ARG C 1 145 ? -41.95868 44.76773  15.06084  1.000 77.71072  ? 145 ARG C N   1 
ATOM   3668 C CA  . ARG C 1 145 ? -41.44235 44.31357  16.34738  1.000 83.69579  ? 145 ARG C CA  1 
ATOM   3669 C C   . ARG C 1 145 ? -40.00425 44.77500  16.57706  1.000 83.69593  ? 145 ARG C C   1 
ATOM   3670 O O   . ARG C 1 145 ? -39.66336 45.21743  17.68068  1.000 95.04368  ? 145 ARG C O   1 
ATOM   3671 C CB  . ARG C 1 145 ? -41.56695 42.78887  16.41699  1.000 91.91245  ? 145 ARG C CB  1 
ATOM   3672 C CG  . ARG C 1 145 ? -40.50368 42.07035  17.21019  1.000 100.77449 ? 145 ARG C CG  1 
ATOM   3673 C CD  . ARG C 1 145 ? -40.96686 40.67929  17.62968  1.000 106.14835 ? 145 ARG C CD  1 
ATOM   3674 N NE  . ARG C 1 145 ? -41.87098 40.71097  18.77148  1.000 115.70283 ? 145 ARG C NE  1 
ATOM   3675 C CZ  . ARG C 1 145 ? -41.47393 40.67421  20.03584  1.000 120.52971 ? 145 ARG C CZ  1 
ATOM   3676 N NH1 . ARG C 1 145 ? -40.19250 40.59205  20.35498  1.000 116.43615 ? 145 ARG C NH1 1 
ATOM   3677 N NH2 . ARG C 1 145 ? -42.38476 40.71888  21.00404  1.000 122.45951 ? 145 ARG C NH2 1 
ATOM   3678 N N   . ASN C 1 146 ? -39.14684 44.68728  15.56053  1.000 84.80949  ? 146 ASN C N   1 
ATOM   3679 C CA  . ASN C 1 146 ? -37.71418 44.90695  15.72276  1.000 86.86882  ? 146 ASN C CA  1 
ATOM   3680 C C   . ASN C 1 146 ? -37.23459 46.02695  14.81053  1.000 76.95974  ? 146 ASN C C   1 
ATOM   3681 O O   . ASN C 1 146 ? -37.76687 46.23265  13.71724  1.000 75.34741  ? 146 ASN C O   1 
ATOM   3682 C CB  . ASN C 1 146 ? -36.90256 43.64195  15.41134  1.000 100.65067 ? 146 ASN C CB  1 
ATOM   3683 C CG  . ASN C 1 146 ? -37.37001 42.43842  16.19186  1.000 97.93530  ? 146 ASN C CG  1 
ATOM   3684 O OD1 . ASN C 1 146 ? -37.62632 41.37761  15.62319  1.000 94.70278  ? 146 ASN C OD1 1 
ATOM   3685 N ND2 . ASN C 1 146 ? -37.44104 42.58147  17.51060  1.000 102.83614 ? 146 ASN C ND2 1 
ATOM   3686 N N   . GLU C 1 147 ? -36.20178 46.73396  15.26086  1.000 73.77342  ? 147 GLU C N   1 
ATOM   3687 C CA  . GLU C 1 147 ? -35.67229 47.84351  14.48565  1.000 79.64398  ? 147 GLU C CA  1 
ATOM   3688 C C   . GLU C 1 147 ? -34.97060 47.34288  13.22839  1.000 78.97108  ? 147 GLU C C   1 
ATOM   3689 O O   . GLU C 1 147 ? -34.44589 46.22778  13.18183  1.000 86.90243  ? 147 GLU C O   1 
ATOM   3690 C CB  . GLU C 1 147 ? -34.69770 48.66045  15.33027  1.000 86.57007  ? 147 GLU C CB  1 
ATOM   3691 C CG  . GLU C 1 147 ? -33.94468 47.83647  16.35261  1.000 98.60047  ? 147 GLU C CG  1 
ATOM   3692 C CD  . GLU C 1 147 ? -32.75489 48.57061  16.93948  1.000 110.60027 ? 147 GLU C CD  1 
ATOM   3693 O OE1 . GLU C 1 147 ? -32.39736 49.64715  16.41328  1.000 111.49575 ? 147 GLU C OE1 1 
ATOM   3694 O OE2 . GLU C 1 147 ? -32.17522 48.06547  17.92518  1.000 108.76136 ? 147 GLU C OE2 1 
ATOM   3695 N N   . GLY C 1 148 ? -34.94168 48.19261  12.21327  1.000 72.01451  ? 148 GLY C N   1 
ATOM   3696 C CA  . GLY C 1 148 ? -34.25674 47.86264  10.98271  1.000 68.24203  ? 148 GLY C CA  1 
ATOM   3697 C C   . GLY C 1 148 ? -34.78820 48.68505  9.82466   1.000 75.84373  ? 148 GLY C C   1 
ATOM   3698 O O   . GLY C 1 148 ? -35.61531 49.58107  9.99494   1.000 75.38531  ? 148 GLY C O   1 
ATOM   3699 N N   . SER C 1 149 ? -34.33237 48.31327  8.63387   1.000 69.27324  ? 149 SER C N   1 
ATOM   3700 C CA  . SER C 1 149 ? -34.79231 48.91032  7.39081   1.000 69.77154  ? 149 SER C CA  1 
ATOM   3701 C C   . SER C 1 149 ? -35.71656 47.93416  6.67755   1.000 73.77728  ? 149 SER C C   1 
ATOM   3702 O O   . SER C 1 149 ? -35.36161 46.76971  6.46982   1.000 77.27416  ? 149 SER C O   1 
ATOM   3703 C CB  . SER C 1 149 ? -33.60373 49.27771  6.49986   1.000 74.47205  ? 149 SER C CB  1 
ATOM   3704 O OG  . SER C 1 149 ? -33.87922 50.42557  5.71628   1.000 95.63978  ? 149 SER C OG  1 
ATOM   3705 N N   . TYR C 1 150 ? -36.90507 48.40421  6.32243   1.000 74.67615  ? 150 TYR C N   1 
ATOM   3706 C CA  . TYR C 1 150 ? -37.94150 47.53835  5.79515   1.000 68.01879  ? 150 TYR C CA  1 
ATOM   3707 C C   . TYR C 1 150 ? -38.57403 48.16890  4.56517   1.000 75.20013  ? 150 TYR C C   1 
ATOM   3708 O O   . TYR C 1 150 ? -38.46722 49.37262  4.32256   1.000 76.53555  ? 150 TYR C O   1 
ATOM   3709 C CB  . TYR C 1 150 ? -39.02779 47.25387  6.83435   1.000 64.21353  ? 150 TYR C CB  1 
ATOM   3710 C CG  . TYR C 1 150 ? -38.54926 46.48443  8.04297   1.000 72.28431  ? 150 TYR C CG  1 
ATOM   3711 C CD1 . TYR C 1 150 ? -38.54463 45.09277  8.05725   1.000 72.48117  ? 150 TYR C CD1 1 
ATOM   3712 C CD2 . TYR C 1 150 ? -38.11887 47.14972  9.17638   1.000 57.12362  ? 150 TYR C CD2 1 
ATOM   3713 C CE1 . TYR C 1 150 ? -38.11339 44.39248  9.17433   1.000 63.70223  ? 150 TYR C CE1 1 
ATOM   3714 C CE2 . TYR C 1 150 ? -37.68877 46.46690  10.28603  1.000 70.17853  ? 150 TYR C CE2 1 
ATOM   3715 C CZ  . TYR C 1 150 ? -37.68519 45.09209  10.28766  1.000 68.07198  ? 150 TYR C CZ  1 
ATOM   3716 O OH  . TYR C 1 150 ? -37.24769 44.43797  11.41882  1.000 71.88489  ? 150 TYR C OH  1 
ATOM   3717 N N   . ARG C 1 151 ? -39.24604 47.32435  3.79798   1.000 70.19308  ? 151 ARG C N   1 
ATOM   3718 C CA  . ARG C 1 151 ? -40.09549 47.74607  2.70266   1.000 63.73104  ? 151 ARG C CA  1 
ATOM   3719 C C   . ARG C 1 151 ? -41.45493 47.10701  2.91759   1.000 64.47961  ? 151 ARG C C   1 
ATOM   3720 O O   . ARG C 1 151 ? -41.56933 46.06269  3.56441   1.000 68.11036  ? 151 ARG C O   1 
ATOM   3721 C CB  . ARG C 1 151 ? -39.54247 47.33063  1.33370   1.000 68.18464  ? 151 ARG C CB  1 
ATOM   3722 C CG  . ARG C 1 151 ? -38.55171 48.30649  0.72523   1.000 79.49909  ? 151 ARG C CG  1 
ATOM   3723 C CD  . ARG C 1 151 ? -38.13143 47.85528  -0.66702  1.000 74.06268  ? 151 ARG C CD  1 
ATOM   3724 N NE  . ARG C 1 151 ? -36.99370 48.61466  -1.17281  1.000 82.90394  ? 151 ARG C NE  1 
ATOM   3725 C CZ  . ARG C 1 151 ? -37.07779 49.65924  -1.98438  1.000 84.52723  ? 151 ARG C CZ  1 
ATOM   3726 N NH1 . ARG C 1 151 ? -38.24579 50.11380  -2.41003  1.000 84.53192  ? 151 ARG C NH1 1 
ATOM   3727 N NH2 . ARG C 1 151 ? -35.95998 50.26148  -2.38204  1.000 87.74674  ? 151 ARG C NH2 1 
ATOM   3728 N N   . PHE C 1 152 ? -42.48423 47.74358  2.38155   1.000 62.90617  ? 152 PHE C N   1 
ATOM   3729 C CA  . PHE C 1 152 ? -43.83289 47.20266  2.41201   1.000 60.94133  ? 152 PHE C CA  1 
ATOM   3730 C C   . PHE C 1 152 ? -44.18437 46.72325  1.01972   1.000 60.72754  ? 152 PHE C C   1 
ATOM   3731 O O   . PHE C 1 152 ? -43.95088 47.42767  0.03098   1.000 59.93874  ? 152 PHE C O   1 
ATOM   3732 C CB  . PHE C 1 152 ? -44.86925 48.22728  2.87996   1.000 62.71237  ? 152 PHE C CB  1 
ATOM   3733 C CG  . PHE C 1 152 ? -45.12609 48.20539  4.35857   1.000 72.28265  ? 152 PHE C CG  1 
ATOM   3734 C CD1 . PHE C 1 152 ? -45.30201 47.00095  5.02573   1.000 60.67151  ? 152 PHE C CD1 1 
ATOM   3735 C CD2 . PHE C 1 152 ? -45.21062 49.38699  5.07977   1.000 62.12310  ? 152 PHE C CD2 1 
ATOM   3736 C CE1 . PHE C 1 152 ? -45.54307 46.97415  6.39173   1.000 55.77639  ? 152 PHE C CE1 1 
ATOM   3737 C CE2 . PHE C 1 152 ? -45.45492 49.36879  6.44483   1.000 67.16844  ? 152 PHE C CE2 1 
ATOM   3738 C CZ  . PHE C 1 152 ? -45.62048 48.16026  7.10119   1.000 66.75566  ? 152 PHE C CZ  1 
ATOM   3739 N N   . SER C 1 153 ? -44.73637 45.52402  0.95467   1.000 58.67694  ? 153 SER C N   1 
ATOM   3740 C CA  . SER C 1 153 ? -45.28803 44.97319  -0.26548  1.000 51.71789  ? 153 SER C CA  1 
ATOM   3741 C C   . SER C 1 153 ? -46.79287 44.87096  -0.07370  1.000 52.63014  ? 153 SER C C   1 
ATOM   3742 O O   . SER C 1 153 ? -47.25862 44.25564  0.89298   1.000 54.68381  ? 153 SER C O   1 
ATOM   3743 C CB  . SER C 1 153 ? -44.66919 43.61126  -0.57511  1.000 66.42386  ? 153 SER C CB  1 
ATOM   3744 O OG  . SER C 1 153 ? -45.02950 43.17542  -1.86903  1.000 68.96200  ? 153 SER C OG  1 
ATOM   3745 N N   . PHE C 1 154 ? -47.54402 45.53114  -0.94865  1.000 56.95117  ? 154 PHE C N   1 
ATOM   3746 C CA  . PHE C 1 154 ? -48.99905 45.56049  -0.87915  1.000 62.67823  ? 154 PHE C CA  1 
ATOM   3747 C C   . PHE C 1 154 ? -49.55055 44.69473  -2.00295  1.000 60.47984  ? 154 PHE C C   1 
ATOM   3748 O O   . PHE C 1 154 ? -49.30037 44.97045  -3.18238  1.000 62.64179  ? 154 PHE C O   1 
ATOM   3749 C CB  . PHE C 1 154 ? -49.51774 46.99518  -0.98209  1.000 49.69254  ? 154 PHE C CB  1 
ATOM   3750 C CG  . PHE C 1 154 ? -48.96234 47.91743  0.06919   1.000 59.76027  ? 154 PHE C CG  1 
ATOM   3751 C CD1 . PHE C 1 154 ? -49.40092 47.83142  1.38264   1.000 62.84814  ? 154 PHE C CD1 1 
ATOM   3752 C CD2 . PHE C 1 154 ? -47.98313 48.84669  -0.24383  1.000 59.35079  ? 154 PHE C CD2 1 
ATOM   3753 C CE1 . PHE C 1 154 ? -48.90008 48.67655  2.35893   1.000 47.81773  ? 154 PHE C CE1 1 
ATOM   3754 C CE2 . PHE C 1 154 ? -47.46926 49.69054  0.72944   1.000 55.85096  ? 154 PHE C CE2 1 
ATOM   3755 C CZ  . PHE C 1 154 ? -47.92873 49.60112  2.03400   1.000 50.29532  ? 154 PHE C CZ  1 
ATOM   3756 N N   . HIS C 1 155 ? -50.32083 43.67080  -1.63621  1.000 50.13073  ? 155 HIS C N   1 
ATOM   3757 C CA  . HIS C 1 155 ? -50.84804 42.69819  -2.58323  1.000 45.38886  ? 155 HIS C CA  1 
ATOM   3758 C C   . HIS C 1 155 ? -52.34769 42.89322  -2.73498  1.000 51.56363  ? 155 HIS C C   1 
ATOM   3759 O O   . HIS C 1 155 ? -53.08438 42.89064  -1.74352  1.000 51.36045  ? 155 HIS C O   1 
ATOM   3760 C CB  . HIS C 1 155 ? -50.53717 41.27425  -2.11758  1.000 56.45567  ? 155 HIS C CB  1 
ATOM   3761 C CG  . HIS C 1 155 ? -49.15512 41.09927  -1.56419  1.000 58.10136  ? 155 HIS C CG  1 
ATOM   3762 N ND1 . HIS C 1 155 ? -48.07156 40.79291  -2.36036  1.000 62.90127  ? 155 HIS C ND1 1 
ATOM   3763 C CD2 . HIS C 1 155 ? -48.67479 41.20491  -0.30226  1.000 60.80306  ? 155 HIS C CD2 1 
ATOM   3764 C CE1 . HIS C 1 155 ? -46.98764 40.69833  -1.61159  1.000 54.70005  ? 155 HIS C CE1 1 
ATOM   3765 N NE2 . HIS C 1 155 ? -47.32450 40.95000  -0.35888  1.000 61.00614  ? 155 HIS C NE2 1 
ATOM   3766 N N   . LEU C 1 156 ? -52.79911 43.01199  -3.97819  1.000 48.08567  ? 156 LEU C N   1 
ATOM   3767 C CA  . LEU C 1 156 ? -54.19770 43.28046  -4.27662  1.000 54.10817  ? 156 LEU C CA  1 
ATOM   3768 C C   . LEU C 1 156 ? -54.95264 41.99037  -4.56501  1.000 60.04847  ? 156 LEU C C   1 
ATOM   3769 O O   . LEU C 1 156 ? -54.53524 41.18995  -5.40848  1.000 57.46341  ? 156 LEU C O   1 
ATOM   3770 C CB  . LEU C 1 156 ? -54.31689 44.24794  -5.45885  1.000 51.22053  ? 156 LEU C CB  1 
ATOM   3771 C CG  . LEU C 1 156 ? -55.74288 44.57862  -5.91127  1.000 55.20571  ? 156 LEU C CG  1 
ATOM   3772 C CD1 . LEU C 1 156 ? -56.48042 45.37278  -4.84370  1.000 58.70687  ? 156 LEU C CD1 1 
ATOM   3773 C CD2 . LEU C 1 156 ? -55.73152 45.33388  -7.22546  1.000 65.33566  ? 156 LEU C CD2 1 
ATOM   3774 N N   . PHE C 1 157 ? -56.07957 41.81523  -3.88425  1.000 62.71656  ? 157 PHE C N   1 
ATOM   3775 C CA  . PHE C 1 157 ? -56.95083 40.66207  -4.05008  1.000 64.57148  ? 157 PHE C CA  1 
ATOM   3776 C C   . PHE C 1 157 ? -58.29691 41.11576  -4.58708  1.000 71.27859  ? 157 PHE C C   1 
ATOM   3777 O O   . PHE C 1 157 ? -58.88551 42.07174  -4.07014  1.000 71.85219  ? 157 PHE C O   1 
ATOM   3778 C CB  . PHE C 1 157 ? -57.13404 39.92061  -2.72755  1.000 69.24826  ? 157 PHE C CB  1 
ATOM   3779 C CG  . PHE C 1 157 ? -55.88365 39.27908  -2.22793  1.000 75.22702  ? 157 PHE C CG  1 
ATOM   3780 C CD1 . PHE C 1 157 ? -55.21969 38.34137  -3.00176  1.000 69.02003  ? 157 PHE C CD1 1 
ATOM   3781 C CD2 . PHE C 1 157 ? -55.34625 39.64162  -1.00930  1.000 59.87704  ? 157 PHE C CD2 1 
ATOM   3782 C CE1 . PHE C 1 157 ? -54.06346 37.75563  -2.55300  1.000 68.06251  ? 157 PHE C CE1 1 
ATOM   3783 C CE2 . PHE C 1 157 ? -54.18691 39.05977  -0.55527  1.000 71.40086  ? 157 PHE C CE2 1 
ATOM   3784 C CZ  . PHE C 1 157 ? -53.54303 38.11777  -1.32872  1.000 77.94850  ? 157 PHE C CZ  1 
ATOM   3785 N N   . GLU C 1 158 ? -58.76750 40.44858  -5.63392  1.000 71.21955  ? 158 GLU C N   1 
ATOM   3786 C CA  . GLU C 1 158 ? -60.05826 40.74369  -6.23370  1.000 69.09850  ? 158 GLU C CA  1 
ATOM   3787 C C   . GLU C 1 158 ? -61.00287 39.57442  -6.00178  1.000 80.00960  ? 158 GLU C C   1 
ATOM   3788 O O   . GLU C 1 158 ? -60.65512 38.42273  -6.28081  1.000 90.78575  ? 158 GLU C O   1 
ATOM   3789 C CB  . GLU C 1 158 ? -59.93408 41.01226  -7.73251  1.000 69.31832  ? 158 GLU C CB  1 
ATOM   3790 C CG  . GLU C 1 158 ? -61.27841 41.26490  -8.39425  1.000 79.64937  ? 158 GLU C CG  1 
ATOM   3791 C CD  . GLU C 1 158 ? -61.16189 41.58776  -9.86627  1.000 87.04625  ? 158 GLU C CD  1 
ATOM   3792 O OE1 . GLU C 1 158 ? -60.03353 41.83397  -10.33505 1.000 84.87088  ? 158 GLU C OE1 1 
ATOM   3793 O OE2 . GLU C 1 158 ? -62.20040 41.57134  -10.55834 1.000 89.40656  ? 158 GLU C OE2 1 
ATOM   3794 N N   . GLN C 1 159 ? -62.18642 39.87701  -5.48356  1.000 85.81787  ? 159 GLN C N   1 
ATOM   3795 C CA  . GLN C 1 159 ? -63.26095 38.91134  -5.29358  1.000 82.20866  ? 159 GLN C CA  1 
ATOM   3796 C C   . GLN C 1 159 ? -64.34133 39.27982  -6.30215  1.000 93.65822  ? 159 GLN C C   1 
ATOM   3797 O O   . GLN C 1 159 ? -64.97759 40.33165  -6.18106  1.000 95.20305  ? 159 GLN C O   1 
ATOM   3798 C CB  . GLN C 1 159 ? -63.77119 38.94978  -3.85670  1.000 90.90132  ? 159 GLN C CB  1 
ATOM   3799 C CG  . GLN C 1 159 ? -64.73679 37.85499  -3.48818  1.000 102.90250 ? 159 GLN C CG  1 
ATOM   3800 C CD  . GLN C 1 159 ? -64.72646 37.58222  -2.00045  1.000 111.18087 ? 159 GLN C CD  1 
ATOM   3801 O OE1 . GLN C 1 159 ? -65.17064 38.40904  -1.20259  1.000 113.80371 ? 159 GLN C OE1 1 
ATOM   3802 N NE2 . GLN C 1 159 ? -64.21627 36.41736  -1.61664  1.000 112.56177 ? 159 GLN C NE2 1 
ATOM   3803 N N   . ILE C 1 160 ? -64.56029 38.41635  -7.28175  1.000 117.66029 ? 160 ILE C N   1 
ATOM   3804 C CA  . ILE C 1 160 ? -65.38928 38.75240  -8.43242  1.000 116.03771 ? 160 ILE C CA  1 
ATOM   3805 C C   . ILE C 1 160 ? -66.85145 38.48104  -8.10691  1.000 121.51198 ? 160 ILE C C   1 
ATOM   3806 O O   . ILE C 1 160 ? -67.19570 37.42835  -7.55542  1.000 117.14624 ? 160 ILE C O   1 
ATOM   3807 C CB  . ILE C 1 160 ? -64.93495 37.96652  -9.67475  1.000 123.29098 ? 160 ILE C CB  1 
ATOM   3808 C CG1 . ILE C 1 160 ? -63.80687 38.71544  -10.39083 1.000 111.59376 ? 160 ILE C CG1 1 
ATOM   3809 C CG2 . ILE C 1 160 ? -66.09832 37.70806  -10.61235 1.000 138.32348 ? 160 ILE C CG2 1 
ATOM   3810 C CD1 . ILE C 1 160 ? -63.43562 38.13033  -11.73486 1.000 118.38014 ? 160 ILE C CD1 1 
ATOM   3811 N N   . LYS C 1 161 ? -67.71036 39.44494  -8.44110  1.000 126.74111 ? 161 LYS C N   1 
ATOM   3812 C CA  . LYS C 1 161 ? -69.14942 39.33802  -8.24070  1.000 141.15962 ? 161 LYS C CA  1 
ATOM   3813 C C   . LYS C 1 161 ? -69.91513 38.99798  -9.51125  1.000 151.89567 ? 161 LYS C C   1 
ATOM   3814 O O   . LYS C 1 161 ? -70.95401 38.33441  -9.43323  1.000 154.98272 ? 161 LYS C O   1 
ATOM   3815 C CB  . LYS C 1 161 ? -69.70544 40.64498  -7.66286  1.000 126.81033 ? 161 LYS C CB  1 
ATOM   3816 C CG  . LYS C 1 161 ? -69.06615 41.07546  -6.35407  1.000 117.04718 ? 161 LYS C CG  1 
ATOM   3817 C CD  . LYS C 1 161 ? -69.92069 42.11594  -5.64619  1.000 121.49425 ? 161 LYS C CD  1 
ATOM   3818 C CE  . LYS C 1 161 ? -69.07950 43.28117  -5.14853  1.000 134.45547 ? 161 LYS C CE  1 
ATOM   3819 N NZ  . LYS C 1 161 ? -69.91777 44.40467  -4.64191  1.000 142.90793 ? 161 LYS C NZ  1 
ATOM   3820 N N   . ASP C 1 162 ? -69.43668 39.43766  -10.67505 1.000 159.91042 ? 162 ASP C N   1 
ATOM   3821 C CA  . ASP C 1 162 ? -70.08041 39.13230  -11.94623 1.000 170.27170 ? 162 ASP C CA  1 
ATOM   3822 C C   . ASP C 1 162 ? -69.26005 38.10735  -12.71321 1.000 171.19449 ? 162 ASP C C   1 
ATOM   3823 O O   . ASP C 1 162 ? -68.07547 38.35320  -12.98575 1.000 168.81216 ? 162 ASP C O   1 
ATOM   3824 C CB  . ASP C 1 162 ? -70.24821 40.40514  -12.77513 1.000 171.55573 ? 162 ASP C CB  1 
ATOM   3825 C CG  . ASP C 1 162 ? -71.58747 41.07699  -12.54817 1.000 184.88006 ? 162 ASP C CG  1 
ATOM   3826 O OD1 . ASP C 1 162 ? -72.54609 40.37891  -12.15442 1.000 196.88131 ? 162 ASP C OD1 1 
ATOM   3827 O OD2 . ASP C 1 162 ? -71.67977 42.30483  -12.76018 1.000 177.68937 ? 162 ASP C OD2 1 
ATOM   3828 N N   . PRO C 1 163 ? -69.83725 36.96068  -13.08475 1.000 181.46586 ? 163 PRO C N   1 
ATOM   3829 C CA  . PRO C 1 163 ? -69.04542 35.92825  -13.77797 1.000 184.68357 ? 163 PRO C CA  1 
ATOM   3830 C C   . PRO C 1 163 ? -68.49522 36.36857  -15.12673 1.000 178.06562 ? 163 PRO C C   1 
ATOM   3831 O O   . PRO C 1 163 ? -67.54132 35.74996  -15.61653 1.000 167.38080 ? 163 PRO C O   1 
ATOM   3832 C CB  . PRO C 1 163 ? -70.03472 34.76130  -13.92932 1.000 192.00061 ? 163 PRO C CB  1 
ATOM   3833 C CG  . PRO C 1 163 ? -71.17324 35.07125  -12.99618 1.000 196.32372 ? 163 PRO C CG  1 
ATOM   3834 C CD  . PRO C 1 163 ? -71.24118 36.55950  -12.90324 1.000 187.92856 ? 163 PRO C CD  1 
ATOM   3835 N N   . LYS C 1 164 ? -69.06775 37.40148  -15.75174 1.000 163.76343 ? 164 LYS C N   1 
ATOM   3836 C CA  . LYS C 1 164 ? -68.51919 37.91588  -17.00221 1.000 154.33970 ? 164 LYS C CA  1 
ATOM   3837 C C   . LYS C 1 164 ? -67.17452 38.61654  -16.81561 1.000 152.52113 ? 164 LYS C C   1 
ATOM   3838 O O   . LYS C 1 164 ? -66.48368 38.86940  -17.80977 1.000 140.42369 ? 164 LYS C O   1 
ATOM   3839 C CB  . LYS C 1 164 ? -69.53968 38.84473  -17.67770 1.000 141.04226 ? 164 LYS C CB  1 
ATOM   3840 C CG  . LYS C 1 164 ? -70.13300 39.94765  -16.80073 1.000 146.44496 ? 164 LYS C CG  1 
ATOM   3841 C CD  . LYS C 1 164 ? -69.20267 41.14343  -16.69308 1.000 152.16711 ? 164 LYS C CD  1 
ATOM   3842 C CE  . LYS C 1 164 ? -69.95537 42.44704  -16.50258 1.000 144.92993 ? 164 LYS C CE  1 
ATOM   3843 N NZ  . LYS C 1 164 ? -69.05470 43.50981  -15.97164 1.000 155.86495 ? 164 LYS C NZ  1 
ATOM   3844 N N   . ASP C 1 165 ? -66.78519 38.92646  -15.57691 1.000 132.34230 ? 165 ASP C N   1 
ATOM   3845 C CA  . ASP C 1 165 ? -65.47908 39.50906  -15.29233 1.000 137.63197 ? 165 ASP C CA  1 
ATOM   3846 C C   . ASP C 1 165 ? -64.38210 38.46482  -15.14828 1.000 138.06566 ? 165 ASP C C   1 
ATOM   3847 O O   . ASP C 1 165 ? -63.22419 38.83986  -14.93848 1.000 127.32949 ? 165 ASP C O   1 
ATOM   3848 C CB  . ASP C 1 165 ? -65.52573 40.35100  -14.00984 1.000 132.80321 ? 165 ASP C CB  1 
ATOM   3849 C CG  . ASP C 1 165 ? -66.40568 41.57870  -14.13726 1.000 131.36082 ? 165 ASP C CG  1 
ATOM   3850 O OD1 . ASP C 1 165 ? -66.61888 42.05077  -15.27384 1.000 128.01416 ? 165 ASP C OD1 1 
ATOM   3851 O OD2 . ASP C 1 165 ? -66.88032 42.07349  -13.09179 1.000 116.23251 ? 165 ASP C OD2 1 
ATOM   3852 N N   . ALA C 1 166 ? -64.71088 37.17860  -15.23315 1.000 152.95898 ? 166 ALA C N   1 
ATOM   3853 C CA  . ALA C 1 166 ? -63.71549 36.14336  -15.00266 1.000 148.41073 ? 166 ALA C CA  1 
ATOM   3854 C C   . ALA C 1 166 ? -62.64342 36.17891  -16.08530 1.000 143.69164 ? 166 ALA C C   1 
ATOM   3855 O O   . ALA C 1 166 ? -62.88011 36.61713  -17.21518 1.000 138.95807 ? 166 ALA C O   1 
ATOM   3856 C CB  . ALA C 1 166 ? -64.37347 34.76416  -14.96302 1.000 157.76686 ? 166 ALA C CB  1 
ATOM   3857 N N   . THR C 1 167 ? -61.45531 35.70230  -15.72876 1.000 125.00435 ? 167 THR C N   1 
ATOM   3858 C CA  . THR C 1 167 ? -60.33530 35.66321  -16.66029 1.000 121.50523 ? 167 THR C CA  1 
ATOM   3859 C C   . THR C 1 167 ? -60.55825 34.62540  -17.76046 1.000 133.73583 ? 167 THR C C   1 
ATOM   3860 O O   . THR C 1 167 ? -60.14045 33.47369  -17.64269 1.000 139.45803 ? 167 THR C O   1 
ATOM   3861 C CB  . THR C 1 167 ? -59.00910 35.36723  -15.93004 1.000 119.43704 ? 167 THR C CB  1 
ATOM   3862 O OG1 . THR C 1 167 ? -59.02500 35.97214  -14.62799 1.000 104.79899 ? 167 THR C OG1 1 
ATOM   3863 C CG2 . THR C 1 167 ? -57.83425 35.90608  -16.72509 1.000 118.20765 ? 167 THR C CG2 1 
ATOM   3864 N N   . PRO C 1 184 ? -70.80736 28.04782  2.61280   1.000 182.70978 ? 184 PRO C N   1 
ATOM   3865 C CA  . PRO C 1 184 ? -70.52654 27.99754  1.18056   1.000 181.55864 ? 184 PRO C CA  1 
ATOM   3866 C C   . PRO C 1 184 ? -69.07785 28.33472  0.81261   1.000 167.17178 ? 184 PRO C C   1 
ATOM   3867 O O   . PRO C 1 184 ? -68.17732 28.11004  1.62311   1.000 138.73354 ? 184 PRO C O   1 
ATOM   3868 C CB  . PRO C 1 184 ? -71.49889 29.03590  0.65490   1.000 180.95928 ? 184 PRO C CB  1 
ATOM   3869 C CG  . PRO C 1 184 ? -72.76820 28.67091  1.43942   1.000 175.63254 ? 184 PRO C CG  1 
ATOM   3870 C CD  . PRO C 1 184 ? -72.25821 28.20530  2.83069   1.000 180.24258 ? 184 PRO C CD  1 
ATOM   3871 N N   . GLN C 1 185 ? -68.86493 28.86527  -0.39186  1.000 200.69042 ? 185 GLN C N   1 
ATOM   3872 C CA  . GLN C 1 185 ? -67.52536 29.18385  -0.86735  1.000 199.50101 ? 185 GLN C CA  1 
ATOM   3873 C C   . GLN C 1 185 ? -67.57293 30.36403  -1.83005  1.000 182.46808 ? 185 GLN C C   1 
ATOM   3874 O O   . GLN C 1 185 ? -68.63581 30.76260  -2.31360  1.000 185.53341 ? 185 GLN C O   1 
ATOM   3875 C CB  . GLN C 1 185 ? -66.87799 27.96605  -1.53998  1.000 201.05999 ? 185 GLN C CB  1 
ATOM   3876 C CG  . GLN C 1 185 ? -67.83317 27.13849  -2.40351  1.000 202.83393 ? 185 GLN C CG  1 
ATOM   3877 C CD  . GLN C 1 185 ? -68.28455 27.86290  -3.65930  1.000 196.95613 ? 185 GLN C CD  1 
ATOM   3878 O OE1 . GLN C 1 185 ? -67.46832 28.22440  -4.50636  1.000 195.02540 ? 185 GLN C OE1 1 
ATOM   3879 N NE2 . GLN C 1 185 ? -69.59032 28.07822  -3.78440  1.000 194.56027 ? 185 GLN C NE2 1 
ATOM   3880 N N   . GLU C 1 186 ? -66.39518 30.92312  -2.09955  1.000 163.00627 ? 186 GLU C N   1 
ATOM   3881 C CA  . GLU C 1 186 ? -66.25339 32.03082  -3.03139  1.000 162.00488 ? 186 GLU C CA  1 
ATOM   3882 C C   . GLU C 1 186 ? -64.85167 31.94588  -3.62222  1.000 154.40649 ? 186 GLU C C   1 
ATOM   3883 O O   . GLU C 1 186 ? -64.07966 31.03834  -3.29962  1.000 155.53301 ? 186 GLU C O   1 
ATOM   3884 C CB  . GLU C 1 186 ? -66.50111 33.37448  -2.33483  1.000 153.91271 ? 186 GLU C CB  1 
ATOM   3885 C CG  . GLU C 1 186 ? -67.56303 34.24627  -2.99088  1.000 156.42064 ? 186 GLU C CG  1 
ATOM   3886 C CD  . GLU C 1 186 ? -67.31910 34.45929  -4.46968  1.000 149.54605 ? 186 GLU C CD  1 
ATOM   3887 O OE1 . GLU C 1 186 ? -66.25927 35.01589  -4.82431  1.000 137.29150 ? 186 GLU C OE1 1 
ATOM   3888 O OE2 . GLU C 1 186 ? -68.19059 34.07487  -5.27818  1.000 160.61933 ? 186 GLU C OE2 1 
ATOM   3889 N N   . PHE C 1 187 ? -64.51769 32.89566  -4.49350  1.000 127.72232 ? 187 PHE C N   1 
ATOM   3890 C CA  . PHE C 1 187 ? -63.23915 32.88926  -5.19592  1.000 116.69216 ? 187 PHE C CA  1 
ATOM   3891 C C   . PHE C 1 187 ? -62.45076 34.16234  -4.90994  1.000 110.92618 ? 187 PHE C C   1 
ATOM   3892 O O   . PHE C 1 187 ? -62.96880 35.26947  -5.08797  1.000 101.28275 ? 187 PHE C O   1 
ATOM   3893 C CB  . PHE C 1 187 ? -63.44049 32.73086  -6.71073  1.000 101.83367 ? 187 PHE C CB  1 
ATOM   3894 C CG  . PHE C 1 187 ? -63.68829 31.30814  -7.15794  1.000 127.91659 ? 187 PHE C CG  1 
ATOM   3895 C CD1 . PHE C 1 187 ? -64.42056 30.42797  -6.37511  1.000 145.30575 ? 187 PHE C CD1 1 
ATOM   3896 C CD2 . PHE C 1 187 ? -63.18865 30.85407  -8.36856  1.000 125.07739 ? 187 PHE C CD2 1 
ATOM   3897 C CE1 . PHE C 1 187 ? -64.65155 29.12644  -6.78645  1.000 135.30306 ? 187 PHE C CE1 1 
ATOM   3898 C CE2 . PHE C 1 187 ? -63.41575 29.55111  -8.78700  1.000 144.19191 ? 187 PHE C CE2 1 
ATOM   3899 C CZ  . PHE C 1 187 ? -64.14841 28.68708  -7.99296  1.000 135.25461 ? 187 PHE C CZ  1 
ATOM   3900 N N   . LEU C 1 188 ? -61.20580 34.00567  -4.46532  1.000 101.15676 ? 188 LEU C N   1 
ATOM   3901 C CA  . LEU C 1 188 ? -60.30655 35.12538  -4.20942  1.000 80.38526  ? 188 LEU C CA  1 
ATOM   3902 C C   . LEU C 1 188 ? -59.16561 35.03617  -5.21410  1.000 77.78853  ? 188 LEU C C   1 
ATOM   3903 O O   . LEU C 1 188 ? -58.46972 34.01735  -5.27339  1.000 79.46458  ? 188 LEU C O   1 
ATOM   3904 C CB  . LEU C 1 188 ? -59.77158 35.09574  -2.77818  1.000 72.04383  ? 188 LEU C CB  1 
ATOM   3905 C CG  . LEU C 1 188 ? -59.01871 36.33425  -2.29122  1.000 83.61319  ? 188 LEU C CG  1 
ATOM   3906 C CD1 . LEU C 1 188 ? -59.95942 37.50945  -2.11560  1.000 73.80142  ? 188 LEU C CD1 1 
ATOM   3907 C CD2 . LEU C 1 188 ? -58.29758 36.03090  -0.98811  1.000 80.54167  ? 188 LEU C CD2 1 
ATOM   3908 N N   . GLU C 1 189 ? -58.95155 36.10599  -5.97607  1.000 78.11468  ? 189 GLU C N   1 
ATOM   3909 C CA  . GLU C 1 189 ? -57.94101 36.12451  -7.02547  1.000 71.78272  ? 189 GLU C CA  1 
ATOM   3910 C C   . GLU C 1 189 ? -56.90760 37.20136  -6.72517  1.000 74.48267  ? 189 GLU C C   1 
ATOM   3911 O O   . GLU C 1 189 ? -57.26846 38.36542  -6.52208  1.000 70.34312  ? 189 GLU C O   1 
ATOM   3912 C CB  . GLU C 1 189 ? -58.61453 36.39852  -8.37641  1.000 80.45975  ? 189 GLU C CB  1 
ATOM   3913 C CG  . GLU C 1 189 ? -58.94181 35.16928  -9.20779  1.000 91.98755  ? 189 GLU C CG  1 
ATOM   3914 C CD  . GLU C 1 189 ? -59.31743 35.51361  -10.64600 1.000 112.02201 ? 189 GLU C CD  1 
ATOM   3915 O OE1 . GLU C 1 189 ? -60.47953 35.91719  -10.87970 1.000 101.64023 ? 189 GLU C OE1 1 
ATOM   3916 O OE2 . GLU C 1 189 ? -58.45599 35.38640  -11.54230 1.000 109.95243 ? 189 GLU C OE2 1 
ATOM   3917 N N   . PHE C 1 190 ? -55.62964 36.82408  -6.72292  1.000 67.75414  ? 190 PHE C N   1 
ATOM   3918 C CA  . PHE C 1 190 ? -54.55546 37.80891  -6.64551  1.000 66.99000  ? 190 PHE C CA  1 
ATOM   3919 C C   . PHE C 1 190 ? -54.37611 38.53008  -7.97805  1.000 65.50872  ? 190 PHE C C   1 
ATOM   3920 O O   . PHE C 1 190 ? -54.40797 37.90945  -9.04345  1.000 72.11698  ? 190 PHE C O   1 
ATOM   3921 C CB  . PHE C 1 190 ? -53.24469 37.13507  -6.23622  1.000 64.94452  ? 190 PHE C CB  1 
ATOM   3922 C CG  . PHE C 1 190 ? -52.03499 38.02644  -6.35617  1.000 69.04402  ? 190 PHE C CG  1 
ATOM   3923 C CD1 . PHE C 1 190 ? -51.78140 39.01312  -5.41266  1.000 62.63556  ? 190 PHE C CD1 1 
ATOM   3924 C CD2 . PHE C 1 190 ? -51.15286 37.87997  -7.41429  1.000 67.20433  ? 190 PHE C CD2 1 
ATOM   3925 C CE1 . PHE C 1 190 ? -50.66778 39.83298  -5.52501  1.000 62.80649  ? 190 PHE C CE1 1 
ATOM   3926 C CE2 . PHE C 1 190 ? -50.04183 38.69653  -7.53171  1.000 67.53458  ? 190 PHE C CE2 1 
ATOM   3927 C CZ  . PHE C 1 190 ? -49.79901 39.67187  -6.58778  1.000 65.28072  ? 190 PHE C CZ  1 
ATOM   3928 N N   . ARG C 1 191 ? -54.15826 39.84490  -7.92665  1.000 64.44278  ? 191 ARG C N   1 
ATOM   3929 C CA  . ARG C 1 191 ? -54.04279 40.62735  -9.15296  1.000 67.03550  ? 191 ARG C CA  1 
ATOM   3930 C C   . ARG C 1 191 ? -52.63031 41.16505  -9.35316  1.000 67.87854  ? 191 ARG C C   1 
ATOM   3931 O O   . ARG C 1 191 ? -51.98504 40.84808  -10.35794 1.000 69.29343  ? 191 ARG C O   1 
ATOM   3932 C CB  . ARG C 1 191 ? -55.05899 41.77804  -9.16400  1.000 68.78428  ? 191 ARG C CB  1 
ATOM   3933 C CG  . ARG C 1 191 ? -56.50580 41.32482  -9.27706  1.000 69.42142  ? 191 ARG C CG  1 
ATOM   3934 C CD  . ARG C 1 191 ? -56.82400 40.80395  -10.66890 1.000 68.39751  ? 191 ARG C CD  1 
ATOM   3935 N NE  . ARG C 1 191 ? -58.15811 40.21987  -10.73365 1.000 83.35674  ? 191 ARG C NE  1 
ATOM   3936 C CZ  . ARG C 1 191 ? -58.42029 38.99893  -11.17528 1.000 83.33632  ? 191 ARG C CZ  1 
ATOM   3937 N NH1 . ARG C 1 191 ? -57.45763 38.19920  -11.60525 1.000 91.03174  ? 191 ARG C NH1 1 
ATOM   3938 N NH2 . ARG C 1 191 ? -59.67973 38.57110  -11.18879 1.000 89.71051  ? 191 ARG C NH2 1 
ATOM   3939 N N   . LEU C 1 192 ? -52.10841 41.94270  -8.40915  1.000 65.04591  ? 192 LEU C N   1 
ATOM   3940 C CA  . LEU C 1 192 ? -50.76908 42.49749  -8.56235  1.000 66.72529  ? 192 LEU C CA  1 
ATOM   3941 C C   . LEU C 1 192 ? -50.27388 42.98427  -7.20663  1.000 63.91241  ? 192 LEU C C   1 
ATOM   3942 O O   . LEU C 1 192 ? -50.98981 42.94984  -6.20079  1.000 61.79471  ? 192 LEU C O   1 
ATOM   3943 C CB  . LEU C 1 192 ? -50.72340 43.62358  -9.60261  1.000 67.74411  ? 192 LEU C CB  1 
ATOM   3944 C CG  . LEU C 1 192 ? -51.11121 45.05158  -9.20403  1.000 69.75125  ? 192 LEU C CG  1 
ATOM   3945 C CD1 . LEU C 1 192 ? -50.62907 46.04222  -10.25932 1.000 69.11931  ? 192 LEU C CD1 1 
ATOM   3946 C CD2 . LEU C 1 192 ? -52.60879 45.17150  -8.98838  1.000 65.21130  ? 192 LEU C CD2 1 
ATOM   3947 N N   . GLU C 1 193 ? -49.05426 43.50707  -7.21526  1.000 64.84384  ? 193 GLU C N   1 
ATOM   3948 C CA  . GLU C 1 193 ? -48.33592 43.89847  -6.01525  1.000 63.38680  ? 193 GLU C CA  1 
ATOM   3949 C C   . GLU C 1 193 ? -47.58361 45.19397  -6.28202  1.000 68.59514  ? 193 GLU C C   1 
ATOM   3950 O O   . GLU C 1 193 ? -47.15034 45.45728  -7.40711  1.000 69.51800  ? 193 GLU C O   1 
ATOM   3951 C CB  . GLU C 1 193 ? -47.39316 42.77075  -5.56905  1.000 64.03988  ? 193 GLU C CB  1 
ATOM   3952 C CG  . GLU C 1 193 ? -46.14240 43.18385  -4.83001  1.000 70.08355  ? 193 GLU C CG  1 
ATOM   3953 C CD  . GLU C 1 193 ? -45.02460 42.15194  -4.97714  1.000 87.21516  ? 193 GLU C CD  1 
ATOM   3954 O OE1 . GLU C 1 193 ? -44.46937 42.02881  -6.09064  1.000 84.99627  ? 193 GLU C OE1 1 
ATOM   3955 O OE2 . GLU C 1 193 ? -44.70526 41.45909  -3.98418  1.000 79.73587  ? 193 GLU C OE2 1 
ATOM   3956 N N   . VAL C 1 194 ? -47.48210 46.02719  -5.25275  1.000 62.78192  ? 194 VAL C N   1 
ATOM   3957 C CA  . VAL C 1 194 ? -46.71399 47.26206  -5.32378  1.000 63.88372  ? 194 VAL C CA  1 
ATOM   3958 C C   . VAL C 1 194 ? -45.83889 47.34253  -4.07773  1.000 62.83501  ? 194 VAL C C   1 
ATOM   3959 O O   . VAL C 1 194 ? -46.28802 47.02698  -2.96970  1.000 60.62187  ? 194 VAL C O   1 
ATOM   3960 C CB  . VAL C 1 194 ? -47.62331 48.50480  -5.46722  1.000 63.62558  ? 194 VAL C CB  1 
ATOM   3961 C CG1 . VAL C 1 194 ? -48.56506 48.66258  -4.27445  1.000 61.05417  ? 194 VAL C CG1 1 
ATOM   3962 C CG2 . VAL C 1 194 ? -46.78991 49.76291  -5.68300  1.000 72.07926  ? 194 VAL C CG2 1 
ATOM   3963 N N   . ILE C 1 195 ? -44.57184 47.69619  -4.27287  1.000 64.79872  ? 195 ILE C N   1 
ATOM   3964 C CA  . ILE C 1 195 ? -43.56822 47.69616  -3.21550  1.000 64.42494  ? 195 ILE C CA  1 
ATOM   3965 C C   . ILE C 1 195 ? -43.25461 49.13979  -2.85067  1.000 69.44335  ? 195 ILE C C   1 
ATOM   3966 O O   . ILE C 1 195 ? -43.02372 49.97519  -3.73443  1.000 73.13506  ? 195 ILE C O   1 
ATOM   3967 C CB  . ILE C 1 195 ? -42.29186 46.94508  -3.63700  1.000 70.20295  ? 195 ILE C CB  1 
ATOM   3968 C CG1 . ILE C 1 195 ? -42.59700 45.46937  -3.91760  1.000 75.81153  ? 195 ILE C CG1 1 
ATOM   3969 C CG2 . ILE C 1 195 ? -41.21286 47.08660  -2.57994  1.000 67.00897  ? 195 ILE C CG2 1 
ATOM   3970 C CD1 . ILE C 1 195 ? -41.88605 44.92069  -5.13414  1.000 70.66461  ? 195 ILE C CD1 1 
ATOM   3971 N N   . SER C 1 196 ? -43.23757 49.42487  -1.55035  1.000 62.88992  ? 196 SER C N   1 
ATOM   3972 C CA  . SER C 1 196 ? -43.02969 50.76310  -1.02634  1.000 63.15099  ? 196 SER C CA  1 
ATOM   3973 C C   . SER C 1 196 ? -41.54683 51.12017  -1.00882  1.000 74.34060  ? 196 SER C C   1 
ATOM   3974 O O   . SER C 1 196 ? -40.66455 50.26971  -1.15457  1.000 74.40640  ? 196 SER C O   1 
ATOM   3975 C CB  . SER C 1 196 ? -43.59855 50.88355  0.38359   1.000 60.72866  ? 196 SER C CB  1 
ATOM   3976 O OG  . SER C 1 196 ? -42.72969 50.28640  1.32686   1.000 60.27679  ? 196 SER C OG  1 
ATOM   3977 N N   . ASN C 1 197 ? -41.28542 52.40721  -0.80381  1.000 71.40930  ? 197 ASN C N   1 
ATOM   3978 C CA  . ASN C 1 197 ? -39.93884 52.87151  -0.52874  1.000 68.55858  ? 197 ASN C CA  1 
ATOM   3979 C C   . ASN C 1 197 ? -39.49917 52.37302  0.84449   1.000 74.90143  ? 197 ASN C C   1 
ATOM   3980 O O   . ASN C 1 197 ? -40.33641 52.08978  1.70625   1.000 70.26036  ? 197 ASN C O   1 
ATOM   3981 C CB  . ASN C 1 197 ? -39.87473 54.39658  -0.55810  1.000 76.65537  ? 197 ASN C CB  1 
ATOM   3982 C CG  . ASN C 1 197 ? -40.03868 54.96106  -1.94936  1.000 76.49230  ? 197 ASN C CG  1 
ATOM   3983 O OD1 . ASN C 1 197 ? -39.67253 54.32756  -2.94045  1.000 84.28417  ? 197 ASN C OD1 1 
ATOM   3984 N ND2 . ASN C 1 197 ? -40.58120 56.16842  -2.03154  1.000 91.08350  ? 197 ASN C ND2 1 
ATOM   3985 N N   . PRO C 1 198 ? -38.19578 52.20703  1.06043   1.000 80.68615  ? 198 PRO C N   1 
ATOM   3986 C CA  . PRO C 1 198 ? -37.73931 51.74448  2.37239   1.000 74.94887  ? 198 PRO C CA  1 
ATOM   3987 C C   . PRO C 1 198 ? -38.08548 52.75003  3.45663   1.000 72.44672  ? 198 PRO C C   1 
ATOM   3988 O O   . PRO C 1 198 ? -38.14658 53.95972  3.22368   1.000 74.88514  ? 198 PRO C O   1 
ATOM   3989 C CB  . PRO C 1 198 ? -36.22129 51.61716  2.20177   1.000 70.49468  ? 198 PRO C CB  1 
ATOM   3990 C CG  . PRO C 1 198 ? -35.99529 51.56746  0.73056   1.000 77.42213  ? 198 PRO C CG  1 
ATOM   3991 C CD  . PRO C 1 198 ? -37.07769 52.39521  0.12176   1.000 72.39628  ? 198 PRO C CD  1 
ATOM   3992 N N   . PHE C 1 199 ? -38.34817 52.22704  4.64768   1.000 64.11687  ? 199 PHE C N   1 
ATOM   3993 C CA  . PHE C 1 199 ? -38.59190 53.05760  5.81208   1.000 66.30945  ? 199 PHE C CA  1 
ATOM   3994 C C   . PHE C 1 199 ? -37.81524 52.47139  6.97805   1.000 77.22425  ? 199 PHE C C   1 
ATOM   3995 O O   . PHE C 1 199 ? -37.38608 51.31550  6.94552   1.000 74.27875  ? 199 PHE C O   1 
ATOM   3996 C CB  . PHE C 1 199 ? -40.09549 53.16491  6.13162   1.000 70.20810  ? 199 PHE C CB  1 
ATOM   3997 C CG  . PHE C 1 199 ? -40.71088 51.88432  6.63517   1.000 70.63904  ? 199 PHE C CG  1 
ATOM   3998 C CD1 . PHE C 1 199 ? -41.06311 50.87567  5.74834   1.000 68.76936  ? 199 PHE C CD1 1 
ATOM   3999 C CD2 . PHE C 1 199 ? -40.93863 51.68819  7.98759   1.000 72.81872  ? 199 PHE C CD2 1 
ATOM   4000 C CE1 . PHE C 1 199 ? -41.63235 49.69486  6.20065   1.000 68.25841  ? 199 PHE C CE1 1 
ATOM   4001 C CE2 . PHE C 1 199 ? -41.50369 50.50678  8.44833   1.000 71.15104  ? 199 PHE C CE2 1 
ATOM   4002 C CZ  . PHE C 1 199 ? -41.85042 49.50756  7.55246   1.000 64.70385  ? 199 PHE C CZ  1 
ATOM   4003 N N   . ILE C 1 200 ? -37.67105 53.27160  8.02750   1.000 74.65954  ? 200 ILE C N   1 
ATOM   4004 C CA  . ILE C 1 200 ? -36.78350 52.96220  9.14066   1.000 72.43007  ? 200 ILE C CA  1 
ATOM   4005 C C   . ILE C 1 200 ? -37.61895 52.74256  10.38951  1.000 71.42569  ? 200 ILE C C   1 
ATOM   4006 O O   . ILE C 1 200 ? -38.48674 53.56069  10.71970  1.000 74.68328  ? 200 ILE C O   1 
ATOM   4007 C CB  . ILE C 1 200 ? -35.72194 54.05839  9.34636   1.000 78.43849  ? 200 ILE C CB  1 
ATOM   4008 C CG1 . ILE C 1 200 ? -34.77047 54.09353  8.14478   1.000 80.37226  ? 200 ILE C CG1 1 
ATOM   4009 C CG2 . ILE C 1 200 ? -34.95878 53.84490  10.64449  1.000 89.57962  ? 200 ILE C CG2 1 
ATOM   4010 C CD1 . ILE C 1 200 ? -34.13696 55.43619  7.87253   1.000 89.36081  ? 200 ILE C CD1 1 
ATOM   4011 N N   . VAL C 1 201 ? -37.37695 51.62205  11.06075  1.000 78.39095  ? 201 VAL C N   1 
ATOM   4012 C CA  . VAL C 1 201 ? -37.92079 51.35371  12.38336  1.000 80.00202  ? 201 VAL C CA  1 
ATOM   4013 C C   . VAL C 1 201 ? -36.76885 51.48191  13.36641  1.000 80.76577  ? 201 VAL C C   1 
ATOM   4014 O O   . VAL C 1 201 ? -35.73265 50.82427  13.20902  1.000 78.22278  ? 201 VAL C O   1 
ATOM   4015 C CB  . VAL C 1 201 ? -38.56527 49.95952  12.45478  1.000 72.65530  ? 201 VAL C CB  1 
ATOM   4016 C CG1 . VAL C 1 201 ? -39.25283 49.74353  13.79483  1.000 73.04971  ? 201 VAL C CG1 1 
ATOM   4017 C CG2 . VAL C 1 201 ? -39.54840 49.78543  11.31884  1.000 64.54333  ? 201 VAL C CG2 1 
ATOM   4018 N N   . TYR C 1 202 ? -36.93750 52.34269  14.36294  1.000 77.24808  ? 202 TYR C N   1 
ATOM   4019 C CA  . TYR C 1 202 ? -35.88176 52.66249  15.30923  1.000 81.95436  ? 202 TYR C CA  1 
ATOM   4020 C C   . TYR C 1 202 ? -36.29559 52.23253  16.70885  1.000 74.85925  ? 202 TYR C C   1 
ATOM   4021 O O   . TYR C 1 202 ? -37.48357 52.09059  17.01064  1.000 72.98812  ? 202 TYR C O   1 
ATOM   4022 C CB  . TYR C 1 202 ? -35.55941 54.16782  15.27060  1.000 66.39763  ? 202 TYR C CB  1 
ATOM   4023 C CG  . TYR C 1 202 ? -36.76477 55.03905  15.55387  1.000 64.86218  ? 202 TYR C CG  1 
ATOM   4024 C CD1 . TYR C 1 202 ? -37.15238 55.33807  16.85299  1.000 70.90566  ? 202 TYR C CD1 1 
ATOM   4025 C CD2 . TYR C 1 202 ? -37.54607 55.52277  14.51150  1.000 64.32053  ? 202 TYR C CD2 1 
ATOM   4026 C CE1 . TYR C 1 202 ? -38.26445 56.11662  17.10307  1.000 65.32931  ? 202 TYR C CE1 1 
ATOM   4027 C CE2 . TYR C 1 202 ? -38.65755 56.30236  14.75352  1.000 74.98395  ? 202 TYR C CE2 1 
ATOM   4028 C CZ  . TYR C 1 202 ? -39.01226 56.59485  16.05088  1.000 64.99307  ? 202 TYR C CZ  1 
ATOM   4029 O OH  . TYR C 1 202 ? -40.12101 57.37074  16.28930  1.000 74.64912  ? 202 TYR C OH  1 
ATOM   4030 N N   . SER C 1 203 ? -35.29937 52.03846  17.56778  1.000 78.35407  ? 203 SER C N   1 
ATOM   4031 C CA  . SER C 1 203 ? -35.52057 51.68398  18.96246  1.000 87.00561  ? 203 SER C CA  1 
ATOM   4032 C C   . SER C 1 203 ? -35.19744 52.88112  19.84845  1.000 86.68987  ? 203 SER C C   1 
ATOM   4033 O O   . SER C 1 203 ? -34.16658 53.53638  19.66256  1.000 90.32849  ? 203 SER C O   1 
ATOM   4034 C CB  . SER C 1 203 ? -34.66911 50.47535  19.36144  1.000 90.26126  ? 203 SER C CB  1 
ATOM   4035 O OG  . SER C 1 203 ? -34.56110 50.35834  20.77057  1.000 103.16988 ? 203 SER C OG  1 
ATOM   4036 N N   . ALA C 1 204 ? -36.08523 53.17480  20.79333  1.000 85.70187  ? 204 ALA C N   1 
ATOM   4037 C CA  . ALA C 1 204 ? -35.85979 54.22384  21.78182  1.000 82.14912  ? 204 ALA C CA  1 
ATOM   4038 C C   . ALA C 1 204 ? -35.22617 53.58291  23.01197  1.000 85.20498  ? 204 ALA C C   1 
ATOM   4039 O O   . ALA C 1 204 ? -35.86725 52.78204  23.69972  1.000 101.14559 ? 204 ALA C O   1 
ATOM   4040 C CB  . ALA C 1 204 ? -37.16025 54.93920  22.13062  1.000 87.54850  ? 204 ALA C CB  1 
ATOM   4041 N N   . LYS C 1 205 ? -33.97340 53.93485  23.29210  1.000 92.95703  ? 205 LYS C N   1 
ATOM   4042 C CA  . LYS C 1 205 ? -33.26607 53.34191  24.41965  1.000 87.10803  ? 205 LYS C CA  1 
ATOM   4043 C C   . LYS C 1 205 ? -33.91692 53.71453  25.74673  1.000 84.17370  ? 205 LYS C C   1 
ATOM   4044 O O   . LYS C 1 205 ? -34.47076 54.80370  25.91600  1.000 95.01742  ? 205 LYS C O   1 
ATOM   4045 C CB  . LYS C 1 205 ? -31.80065 53.77658  24.43872  1.000 80.99013  ? 205 LYS C CB  1 
ATOM   4046 C CG  . LYS C 1 205 ? -30.83431 52.72642  23.93323  1.000 88.58801  ? 205 LYS C CG  1 
ATOM   4047 C CD  . LYS C 1 205 ? -29.41781 53.27640  23.82158  1.000 102.97568 ? 205 LYS C CD  1 
ATOM   4048 C CE  . LYS C 1 205 ? -29.31621 54.40301  22.80917  1.000 97.46883  ? 205 LYS C CE  1 
ATOM   4049 N NZ  . LYS C 1 205 ? -27.91440 54.56340  22.33608  1.000 98.01930  ? 205 LYS C NZ  1 
ATOM   4050 N N   . LYS C 1 206 ? -33.84985 52.78084  26.69026  1.000 92.37317  ? 206 LYS C N   1 
ATOM   4051 C CA  . LYS C 1 206 ? -34.35754 53.00645  28.03420  1.000 92.91757  ? 206 LYS C CA  1 
ATOM   4052 C C   . LYS C 1 206 ? -33.31210 53.74419  28.86073  1.000 95.65250  ? 206 LYS C C   1 
ATOM   4053 O O   . LYS C 1 206 ? -32.13143 53.38036  28.86374  1.000 87.83693  ? 206 LYS C O   1 
ATOM   4054 C CB  . LYS C 1 206 ? -34.73762 51.68856  28.70867  1.000 88.70404  ? 206 LYS C CB  1 
ATOM   4055 C CG  . LYS C 1 206 ? -35.95468 51.01566  28.10066  1.000 101.80516 ? 206 LYS C CG  1 
ATOM   4056 C CD  . LYS C 1 206 ? -35.79262 49.50659  28.02921  1.000 104.75107 ? 206 LYS C CD  1 
ATOM   4057 C CE  . LYS C 1 206 ? -37.00008 48.79593  28.62914  1.000 102.19504 ? 206 LYS C CE  1 
ATOM   4058 N NZ  . LYS C 1 206 ? -37.04396 47.35099  28.26722  1.000 102.09835 ? 206 LYS C NZ  1 
ATOM   4059 N N   . PHE C 1 207 ? -33.74867 54.79972  29.54043  1.000 94.04339  ? 207 PHE C N   1 
ATOM   4060 C CA  . PHE C 1 207 ? -32.89146 55.60502  30.40491  1.000 104.32304 ? 207 PHE C CA  1 
ATOM   4061 C C   . PHE C 1 207 ? -33.57460 55.73654  31.75806  1.000 110.81093 ? 207 PHE C C   1 
ATOM   4062 O O   . PHE C 1 207 ? -34.28170 56.72065  32.02108  1.000 111.73000 ? 207 PHE C O   1 
ATOM   4063 C CB  . PHE C 1 207 ? -32.59222 56.97413  29.79273  1.000 88.98730  ? 207 PHE C CB  1 
ATOM   4064 C CG  . PHE C 1 207 ? -31.62901 56.93012  28.63605  1.000 84.47508  ? 207 PHE C CG  1 
ATOM   4065 C CD1 . PHE C 1 207 ? -30.26840 56.75952  28.85427  1.000 86.14738  ? 207 PHE C CD1 1 
ATOM   4066 C CD2 . PHE C 1 207 ? -32.08073 57.06236  27.33250  1.000 82.18240  ? 207 PHE C CD2 1 
ATOM   4067 C CE1 . PHE C 1 207 ? -29.37670 56.72361  27.79408  1.000 85.74306  ? 207 PHE C CE1 1 
ATOM   4068 C CE2 . PHE C 1 207 ? -31.19370 57.02447  26.26644  1.000 81.68764  ? 207 PHE C CE2 1 
ATOM   4069 C CZ  . PHE C 1 207 ? -29.83950 56.85586  26.49924  1.000 83.56937  ? 207 PHE C CZ  1 
ATOM   4070 N N   . PRO C 1 208 ? -33.36248 54.76933  32.65351  1.000 110.20827 ? 208 PRO C N   1 
ATOM   4071 C CA  . PRO C 1 208 ? -34.00916 54.80807  33.97461  1.000 112.44479 ? 208 PRO C CA  1 
ATOM   4072 C C   . PRO C 1 208 ? -33.45985 56.00680  34.72817  1.000 103.55104 ? 208 PRO C C   1 
ATOM   4073 O O   . PRO C 1 208 ? -32.24739 56.13809  34.90858  1.000 95.70224  ? 208 PRO C O   1 
ATOM   4074 C CB  . PRO C 1 208 ? -33.59943 53.48110  34.62601  1.000 112.17834 ? 208 PRO C CB  1 
ATOM   4075 C CG  . PRO C 1 208 ? -32.47554 52.94907  33.82370  1.000 96.65538  ? 208 PRO C CG  1 
ATOM   4076 C CD  . PRO C 1 208 ? -32.34411 53.71083  32.54376  1.000 98.50429  ? 208 PRO C CD  1 
ATOM   4077 N N   . GLY C 1 209 ? -34.36784 56.87380  35.18774  1.000 109.49177 ? 209 GLY C N   1 
ATOM   4078 C CA  . GLY C 1 209 ? -34.01989 58.12576  35.82523  1.000 118.73406 ? 209 GLY C CA  1 
ATOM   4079 C C   . GLY C 1 209 ? -34.37138 59.31714  34.95823  1.000 117.70371 ? 209 GLY C C   1 
ATOM   4080 O O   . GLY C 1 209 ? -34.73856 60.37763  35.48511  1.000 111.45446 ? 209 GLY C O   1 
ATOM   4081 N N   . LEU C 1 210 ? -34.26044 59.15926  33.63911  1.000 116.00839 ? 210 LEU C N   1 
ATOM   4082 C CA  . LEU C 1 210 ? -34.60564 60.19832  32.67578  1.000 122.58475 ? 210 LEU C CA  1 
ATOM   4083 C C   . LEU C 1 210 ? -35.93188 59.85056  32.01446  1.000 121.82730 ? 210 LEU C C   1 
ATOM   4084 O O   . LEU C 1 210 ? -36.93479 60.53884  32.23045  1.000 123.51034 ? 210 LEU C O   1 
ATOM   4085 C CB  . LEU C 1 210 ? -33.53697 60.30219  31.59407  1.000 105.52535 ? 210 LEU C CB  1 
ATOM   4086 C CG  . LEU C 1 210 ? -32.17855 60.91364  31.87100  1.000 107.75233 ? 210 LEU C CG  1 
ATOM   4087 C CD1 . LEU C 1 210 ? -31.36257 60.69868  30.61006  1.000 97.04295  ? 210 LEU C CD1 1 
ATOM   4088 C CD2 . LEU C 1 210 ? -32.31184 62.38728  32.23453  1.000 104.63323 ? 210 LEU C CD2 1 
ATOM   4089 N N   . THR C 1 211 ? -35.94490 58.78540  31.20577  1.000 124.34005 ? 211 THR C N   1 
ATOM   4090 C CA  . THR C 1 211 ? -37.14786 58.44026  30.44908  1.000 127.93113 ? 211 THR C CA  1 
ATOM   4091 C C   . THR C 1 211 ? -38.34110 58.20523  31.36552  1.000 140.11105 ? 211 THR C C   1 
ATOM   4092 O O   . THR C 1 211 ? -39.47257 58.56559  31.02038  1.000 142.44524 ? 211 THR C O   1 
ATOM   4093 C CB  . THR C 1 211 ? -36.90002 57.21121  29.57631  1.000 109.65071 ? 211 THR C CB  1 
ATOM   4094 O OG1 . THR C 1 211 ? -36.38247 56.14075  30.37739  1.000 119.07991 ? 211 THR C OG1 1 
ATOM   4095 C CG2 . THR C 1 211 ? -35.92193 57.55315  28.48141  1.000 90.04286  ? 211 THR C CG2 1 
ATOM   4096 N N   . THR C 1 212 ? -38.09724 57.62875  32.54259  1.000 157.49201 ? 212 THR C N   1 
ATOM   4097 C CA  . THR C 1 212 ? -39.10978 57.34128  33.56974  1.000 159.68661 ? 212 THR C CA  1 
ATOM   4098 C C   . THR C 1 212 ? -40.52346 57.02808  33.05138  1.000 158.05772 ? 212 THR C C   1 
ATOM   4099 O O   . THR C 1 212 ? -40.89800 55.86747  32.85192  1.000 156.68529 ? 212 THR C O   1 
ATOM   4100 C CB  . THR C 1 212 ? -39.22381 58.53086  34.56350  1.000 158.24135 ? 212 THR C CB  1 
ATOM   4101 O OG1 . THR C 1 212 ? -37.94729 58.81755  35.15415  1.000 149.12451 ? 212 THR C OG1 1 
ATOM   4102 C CG2 . THR C 1 212 ? -40.22029 58.21081  35.65419  1.000 162.58309 ? 212 THR C CG2 1 
ATOM   4103 N N   . GLY D 1 15  ? -39.31675 24.96560  11.73077  1.000 133.15456 ? 15  GLY D N   1 
ATOM   4104 C CA  . GLY D 1 15  ? -40.42926 24.04545  11.87940  1.000 130.86819 ? 15  GLY D CA  1 
ATOM   4105 C C   . GLY D 1 15  ? -41.33718 24.00540  10.66581  1.000 133.59568 ? 15  GLY D C   1 
ATOM   4106 O O   . GLY D 1 15  ? -41.28015 24.88560  9.80716   1.000 136.51525 ? 15  GLY D O   1 
ATOM   4107 N N   . ASN D 1 16  ? -42.17847 22.97654  10.59177  1.000 114.98573 ? 16  ASN D N   1 
ATOM   4108 C CA  . ASN D 1 16  ? -43.11289 22.81101  9.48766   1.000 102.09726 ? 16  ASN D CA  1 
ATOM   4109 C C   . ASN D 1 16  ? -44.50834 23.33718  9.79664   1.000 89.36628  ? 16  ASN D C   1 
ATOM   4110 O O   . ASN D 1 16  ? -45.39391 23.22815  8.94398   1.000 89.80930  ? 16  ASN D O   1 
ATOM   4111 C CB  . ASN D 1 16  ? -43.20252 21.33142  9.09193   1.000 104.64358 ? 16  ASN D CB  1 
ATOM   4112 C CG  . ASN D 1 16  ? -42.31118 20.98564  7.91211   1.000 126.71748 ? 16  ASN D CG  1 
ATOM   4113 O OD1 . ASN D 1 16  ? -41.66400 21.85763  7.33069   1.000 123.59665 ? 16  ASN D OD1 1 
ATOM   4114 N ND2 . ASN D 1 16  ? -42.27103 19.70484  7.55473   1.000 124.03864 ? 16  ASN D ND2 1 
ATOM   4115 N N   . SER D 1 17  ? -44.72024 23.94465  10.96346  1.000 88.13301  ? 17  SER D N   1 
ATOM   4116 C CA  . SER D 1 17  ? -46.06214 24.30891  11.39159  1.000 80.07123  ? 17  SER D CA  1 
ATOM   4117 C C   . SER D 1 17  ? -46.03220 25.63310  12.14352  1.000 80.13255  ? 17  SER D C   1 
ATOM   4118 O O   . SER D 1 17  ? -44.99411 26.06681  12.64902  1.000 82.56677  ? 17  SER D O   1 
ATOM   4119 C CB  . SER D 1 17  ? -46.68365 23.19922  12.26002  1.000 82.92926  ? 17  SER D CB  1 
ATOM   4120 O OG  . SER D 1 17  ? -46.49177 23.43492  13.64542  1.000 81.77430  ? 17  SER D OG  1 
ATOM   4121 N N   . ASN D 1 18  ? -47.20680 26.25822  12.22544  1.000 74.93212  ? 18  ASN D N   1 
ATOM   4122 C CA  . ASN D 1 18  ? -47.41203 27.49613  12.96486  1.000 82.84221  ? 18  ASN D CA  1 
ATOM   4123 C C   . ASN D 1 18  ? -48.87244 27.59786  13.38190  1.000 89.39746  ? 18  ASN D C   1 
ATOM   4124 O O   . ASN D 1 18  ? -49.76232 27.16641  12.64412  1.000 84.81874  ? 18  ASN D O   1 
ATOM   4125 C CB  . ASN D 1 18  ? -47.00977 28.71410  12.12877  1.000 72.39037  ? 18  ASN D CB  1 
ATOM   4126 C CG  . ASN D 1 18  ? -46.96828 29.98944  12.94153  1.000 88.28709  ? 18  ASN D CG  1 
ATOM   4127 O OD1 . ASN D 1 18  ? -46.61550 29.97775  14.12261  1.000 91.36627  ? 18  ASN D OD1 1 
ATOM   4128 N ND2 . ASN D 1 18  ? -47.32897 31.10332  12.31062  1.000 71.88114  ? 18  ASN D ND2 1 
ATOM   4129 N N   . SER D 1 19  ? -49.10862 28.10962  14.59019  1.000 87.44534  ? 19  SER D N   1 
ATOM   4130 C CA  . SER D 1 19  ? -50.45575 28.19987  15.13354  1.000 96.12801  ? 19  SER D CA  1 
ATOM   4131 C C   . SER D 1 19  ? -50.69335 29.55913  15.76981  1.000 96.88953  ? 19  SER D C   1 
ATOM   4132 O O   . SER D 1 19  ? -49.75750 30.22893  16.21503  1.000 99.46844  ? 19  SER D O   1 
ATOM   4133 C CB  . SER D 1 19  ? -50.69788 27.13295  16.19267  1.000 89.34029  ? 19  SER D CB  1 
ATOM   4134 O OG  . SER D 1 19  ? -49.93629 25.99273  15.88294  1.000 113.85640 ? 19  SER D OG  1 
ATOM   4135 N N   . VAL D 1 20  ? -51.96346 29.96254  15.79176  1.000 81.08551  ? 20  VAL D N   1 
ATOM   4136 C CA  . VAL D 1 20  ? -52.38500 31.21106  16.41032  1.000 96.18283  ? 20  VAL D CA  1 
ATOM   4137 C C   . VAL D 1 20  ? -53.75730 30.98412  17.03124  1.000 96.65323  ? 20  VAL D C   1 
ATOM   4138 O O   . VAL D 1 20  ? -54.56531 30.19605  16.52977  1.000 93.16475  ? 20  VAL D O   1 
ATOM   4139 C CB  . VAL D 1 20  ? -52.40822 32.38662  15.40607  1.000 95.66969  ? 20  VAL D CB  1 
ATOM   4140 C CG1 . VAL D 1 20  ? -53.64397 32.32526  14.51854  1.000 93.03966  ? 20  VAL D CG1 1 
ATOM   4141 C CG2 . VAL D 1 20  ? -52.34086 33.70963  16.14581  1.000 96.18774  ? 20  VAL D CG2 1 
ATOM   4142 N N   . SER D 1 21  ? -54.01444 31.67543  18.13922  1.000 116.75051 ? 21  SER D N   1 
ATOM   4143 C CA  . SER D 1 21  ? -55.25704 31.53401  18.88275  1.000 111.19841 ? 21  SER D CA  1 
ATOM   4144 C C   . SER D 1 21  ? -56.00651 32.85777  18.93181  1.000 113.79471 ? 21  SER D C   1 
ATOM   4145 O O   . SER D 1 21  ? -55.40091 33.93426  18.93203  1.000 123.69667 ? 21  SER D O   1 
ATOM   4146 C CB  . SER D 1 21  ? -54.99549 31.04274  20.31337  1.000 116.80012 ? 21  SER D CB  1 
ATOM   4147 O OG  . SER D 1 21  ? -55.11176 29.63409  20.40179  1.000 132.64411 ? 21  SER D OG  1 
ATOM   4148 N N   . ARG D 1 22  ? -57.33392 32.76940  18.96511  1.000 108.43037 ? 22  ARG D N   1 
ATOM   4149 C CA  . ARG D 1 22  ? -58.16954 33.94950  19.12344  1.000 110.86980 ? 22  ARG D CA  1 
ATOM   4150 C C   . ARG D 1 22  ? -59.38716 33.55677  19.94665  1.000 106.06915 ? 22  ARG D C   1 
ATOM   4151 O O   . ARG D 1 22  ? -59.61940 32.37785  20.22357  1.000 118.14879 ? 22  ARG D O   1 
ATOM   4152 C CB  . ARG D 1 22  ? -58.56577 34.55181  17.76790  1.000 112.38403 ? 22  ARG D CB  1 
ATOM   4153 C CG  . ARG D 1 22  ? -59.91102 34.10596  17.21458  1.000 105.10542 ? 22  ARG D CG  1 
ATOM   4154 C CD  . ARG D 1 22  ? -60.21170 34.83318  15.91074  1.000 107.54950 ? 22  ARG D CD  1 
ATOM   4155 N NE  . ARG D 1 22  ? -60.95181 34.01550  14.95733  1.000 109.87257 ? 22  ARG D NE  1 
ATOM   4156 C CZ  . ARG D 1 22  ? -62.26369 33.82344  15.00298  1.000 112.28057 ? 22  ARG D CZ  1 
ATOM   4157 N NH1 . ARG D 1 22  ? -63.00839 34.36654  15.95049  1.000 118.52483 ? 22  ARG D NH1 1 
ATOM   4158 N NH2 . ARG D 1 22  ? -62.84375 33.07319  14.07075  1.000 116.78562 ? 22  ARG D NH2 1 
ATOM   4159 N N   . ILE D 1 23  ? -60.16858 34.55910  20.33978  1.000 122.45246 ? 23  ILE D N   1 
ATOM   4160 C CA  . ILE D 1 23  ? -61.37166 34.35019  21.13564  1.000 122.03238 ? 23  ILE D CA  1 
ATOM   4161 C C   . ILE D 1 23  ? -62.53751 35.00454  20.41078  1.000 122.18818 ? 23  ILE D C   1 
ATOM   4162 O O   . ILE D 1 23  ? -62.44155 36.16262  19.98998  1.000 121.29162 ? 23  ILE D O   1 
ATOM   4163 C CB  . ILE D 1 23  ? -61.22230 34.90895  22.56355  1.000 101.27314 ? 23  ILE D CB  1 
ATOM   4164 C CG1 . ILE D 1 23  ? -60.12397 34.14544  23.30836  1.000 102.16299 ? 23  ILE D CG1 1 
ATOM   4165 C CG2 . ILE D 1 23  ? -62.54158 34.81946  23.31318  1.000 116.48560 ? 23  ILE D CG2 1 
ATOM   4166 C CD1 . ILE D 1 23  ? -59.61153 34.84410  24.53892  1.000 105.05871 ? 23  ILE D CD1 1 
ATOM   4167 N N   . THR D 1 24  ? -63.63263 34.26431  20.26559  1.000 132.26153 ? 24  THR D N   1 
ATOM   4168 C CA  . THR D 1 24  ? -64.79345 34.73389  19.53032  1.000 142.27624 ? 24  THR D CA  1 
ATOM   4169 C C   . THR D 1 24  ? -65.73712 35.49843  20.45595  1.000 149.38221 ? 24  THR D C   1 
ATOM   4170 O O   . THR D 1 24  ? -65.50830 35.62580  21.66174  1.000 142.55572 ? 24  THR D O   1 
ATOM   4171 C CB  . THR D 1 24  ? -65.51358 33.55989  18.86597  1.000 141.79561 ? 24  THR D CB  1 
ATOM   4172 O OG1 . THR D 1 24  ? -66.63293 34.04393  18.11232  1.000 148.70456 ? 24  THR D OG1 1 
ATOM   4173 C CG2 . THR D 1 24  ? -65.99570 32.56402  19.91499  1.000 138.37662 ? 24  THR D CG2 1 
ATOM   4174 N N   . ARG D 1 25  ? -66.81741 36.02200  19.87242  1.000 152.12343 ? 25  ARG D N   1 
ATOM   4175 C CA  . ARG D 1 25  ? -67.80321 36.75884  20.65431  1.000 160.24558 ? 25  ARG D CA  1 
ATOM   4176 C C   . ARG D 1 25  ? -68.50171 35.86148  21.66636  1.000 165.56716 ? 25  ARG D C   1 
ATOM   4177 O O   . ARG D 1 25  ? -68.92361 36.33405  22.72819  1.000 174.03434 ? 25  ARG D O   1 
ATOM   4178 C CB  . ARG D 1 25  ? -68.82817 37.40795  19.72430  1.000 153.82528 ? 25  ARG D CB  1 
ATOM   4179 C CG  . ARG D 1 25  ? -68.24276 38.45302  18.79178  1.000 150.22725 ? 25  ARG D CG  1 
ATOM   4180 C CD  . ARG D 1 25  ? -68.99695 39.76745  18.89953  1.000 156.80401 ? 25  ARG D CD  1 
ATOM   4181 N NE  . ARG D 1 25  ? -68.12211 40.92128  18.72686  1.000 157.21334 ? 25  ARG D NE  1 
ATOM   4182 C CZ  . ARG D 1 25  ? -68.21367 42.04225  19.43011  1.000 153.62617 ? 25  ARG D CZ  1 
ATOM   4183 N NH1 . ARG D 1 25  ? -69.13074 42.19500  20.37193  1.000 142.60145 ? 25  ARG D NH1 1 
ATOM   4184 N NH2 . ARG D 1 25  ? -67.36324 43.03477  19.18310  1.000 150.37852 ? 25  ARG D NH2 1 
ATOM   4185 N N   . GLU D 1 26  ? -68.63407 34.57393  21.36002  1.000 177.03913 ? 26  GLU D N   1 
ATOM   4186 C CA  . GLU D 1 26  ? -69.37915 33.64458  22.19742  1.000 187.82758 ? 26  GLU D CA  1 
ATOM   4187 C C   . GLU D 1 26  ? -68.53439 33.02733  23.30637  1.000 184.00661 ? 26  GLU D C   1 
ATOM   4188 O O   . GLU D 1 26  ? -69.04399 32.19155  24.06070  1.000 171.95149 ? 26  GLU D O   1 
ATOM   4189 C CB  . GLU D 1 26  ? -69.99677 32.54422  21.32715  1.000 191.54468 ? 26  GLU D CB  1 
ATOM   4190 C CG  . GLU D 1 26  ? -70.96156 33.08534  20.27773  1.000 199.17839 ? 26  GLU D CG  1 
ATOM   4191 C CD  . GLU D 1 26  ? -71.76843 32.00024  19.58981  1.000 210.98402 ? 26  GLU D CD  1 
ATOM   4192 O OE1 . GLU D 1 26  ? -71.35566 30.82438  19.63363  1.000 204.98979 ? 26  GLU D OE1 1 
ATOM   4193 O OE2 . GLU D 1 26  ? -72.82680 32.32408  19.01159  1.000 219.77317 ? 26  GLU D OE2 1 
ATOM   4194 N N   . GLY D 1 27  ? -67.26536 33.41574  23.42523  1.000 170.49831 ? 27  GLY D N   1 
ATOM   4195 C CA  . GLY D 1 27  ? -66.43627 33.02054  24.54376  1.000 159.93847 ? 27  GLY D CA  1 
ATOM   4196 C C   . GLY D 1 27  ? -65.55197 31.81419  24.31442  1.000 159.98378 ? 27  GLY D C   1 
ATOM   4197 O O   . GLY D 1 27  ? -64.88299 31.37523  25.25828  1.000 152.13499 ? 27  GLY D O   1 
ATOM   4198 N N   . LYS D 1 28  ? -65.52687 31.26116  23.10394  1.000 156.57117 ? 28  LYS D N   1 
ATOM   4199 C CA  . LYS D 1 28  ? -64.72050 30.08349  22.81506  1.000 148.52913 ? 28  LYS D CA  1 
ATOM   4200 C C   . LYS D 1 28  ? -63.35922 30.48238  22.26125  1.000 131.70659 ? 28  LYS D C   1 
ATOM   4201 O O   . LYS D 1 28  ? -63.24328 31.43366  21.48302  1.000 125.70713 ? 28  LYS D O   1 
ATOM   4202 C CB  . LYS D 1 28  ? -65.42844 29.16385  21.81829  1.000 145.33204 ? 28  LYS D CB  1 
ATOM   4203 C CG  . LYS D 1 28  ? -66.92375 29.38457  21.69992  1.000 155.64980 ? 28  LYS D CG  1 
ATOM   4204 C CD  . LYS D 1 28  ? -67.42707 28.93326  20.33854  1.000 160.26404 ? 28  LYS D CD  1 
ATOM   4205 C CE  . LYS D 1 28  ? -68.93820 29.01963  20.25453  1.000 160.77486 ? 28  LYS D CE  1 
ATOM   4206 N NZ  . LYS D 1 28  ? -69.43429 28.80900  18.86549  1.000 158.56577 ? 28  LYS D NZ  1 
ATOM   4207 N N   . LYS D 1 29  ? -62.33147 29.74180  22.66909  1.000 134.78610 ? 29  LYS D N   1 
ATOM   4208 C CA  . LYS D 1 29  ? -60.98021 29.91541  22.15151  1.000 128.51167 ? 29  LYS D CA  1 
ATOM   4209 C C   . LYS D 1 29  ? -60.82293 29.06129  20.89929  1.000 118.75793 ? 29  LYS D C   1 
ATOM   4210 O O   . LYS D 1 29  ? -60.99195 27.83777  20.94661  1.000 123.18008 ? 29  LYS D O   1 
ATOM   4211 C CB  . LYS D 1 29  ? -59.93613 29.53807  23.20113  1.000 135.97516 ? 29  LYS D CB  1 
ATOM   4212 C CG  . LYS D 1 29  ? -58.51420 29.92615  22.82702  1.000 116.96630 ? 29  LYS D CG  1 
ATOM   4213 C CD  . LYS D 1 29  ? -57.54657 29.65065  23.96787  1.000 135.67470 ? 29  LYS D CD  1 
ATOM   4214 C CE  . LYS D 1 29  ? -56.25314 29.03461  23.46037  1.000 127.19966 ? 29  LYS D CE  1 
ATOM   4215 N NZ  . LYS D 1 29  ? -55.06479 29.55910  24.18721  1.000 125.29865 ? 29  LYS D NZ  1 
ATOM   4216 N N   . ILE D 1 30  ? -60.49242 29.70470  19.78689  1.000 118.08444 ? 30  ILE D N   1 
ATOM   4217 C CA  . ILE D 1 30  ? -60.39852 29.05544  18.48682  1.000 113.94994 ? 30  ILE D CA  1 
ATOM   4218 C C   . ILE D 1 30  ? -58.93992 29.09573  18.05756  1.000 109.60709 ? 30  ILE D C   1 
ATOM   4219 O O   . ILE D 1 30  ? -58.32149 30.16719  18.03597  1.000 112.41288 ? 30  ILE D O   1 
ATOM   4220 C CB  . ILE D 1 30  ? -61.31697 29.73407  17.45802  1.000 101.21447 ? 30  ILE D CB  1 
ATOM   4221 C CG1 . ILE D 1 30  ? -62.74384 29.21135  17.63126  1.000 116.49869 ? 30  ILE D CG1 1 
ATOM   4222 C CG2 . ILE D 1 30  ? -60.82821 29.45731  16.04628  1.000 102.89910 ? 30  ILE D CG2 1 
ATOM   4223 C CD1 . ILE D 1 30  ? -63.66328 29.53678  16.49408  1.000 116.01481 ? 30  ILE D CD1 1 
ATOM   4224 N N   . THR D 1 31  ? -58.39263 27.93179  17.71598  1.000 109.26379 ? 31  THR D N   1 
ATOM   4225 C CA  . THR D 1 31  ? -56.98611 27.79160  17.36538  1.000 101.14195 ? 31  THR D CA  1 
ATOM   4226 C C   . THR D 1 31  ? -56.87046 27.32816  15.92239  1.000 91.21180  ? 31  THR D C   1 
ATOM   4227 O O   . THR D 1 31  ? -57.48908 26.33656  15.52501  1.000 108.38453 ? 31  THR D O   1 
ATOM   4228 C CB  . THR D 1 31  ? -56.27391 26.80288  18.29460  1.000 106.34402 ? 31  THR D CB  1 
ATOM   4229 O OG1 . THR D 1 31  ? -55.98437 27.44043  19.54473  1.000 111.56184 ? 31  THR D OG1 1 
ATOM   4230 C CG2 . THR D 1 31  ? -54.96637 26.33895  17.67036  1.000 90.12425  ? 31  THR D CG2 1 
ATOM   4231 N N   . TYR D 1 32  ? -56.08397 28.06182  15.14830  1.000 89.54512  ? 32  TYR D N   1 
ATOM   4232 C CA  . TYR D 1 32  ? -55.76975 27.72982  13.76941  1.000 84.75046  ? 32  TYR D CA  1 
ATOM   4233 C C   . TYR D 1 32  ? -54.37446 27.12724  13.68793  1.000 91.41598  ? 32  TYR D C   1 
ATOM   4234 O O   . TYR D 1 32  ? -53.42771 27.66446  14.27032  1.000 92.04665  ? 32  TYR D O   1 
ATOM   4235 C CB  . TYR D 1 32  ? -55.84295 28.96919  12.87203  1.000 84.98055  ? 32  TYR D CB  1 
ATOM   4236 C CG  . TYR D 1 32  ? -57.13405 29.75857  12.95384  1.000 92.52869  ? 32  TYR D CG  1 
ATOM   4237 C CD1 . TYR D 1 32  ? -57.36000 30.65681  13.98977  1.000 93.45801  ? 32  TYR D CD1 1 
ATOM   4238 C CD2 . TYR D 1 32  ? -58.12362 29.60877  11.98935  1.000 93.44512  ? 32  TYR D CD2 1 
ATOM   4239 C CE1 . TYR D 1 32  ? -58.53278 31.37818  14.06476  1.000 99.09408  ? 32  TYR D CE1 1 
ATOM   4240 C CE2 . TYR D 1 32  ? -59.29915 30.32789  12.05522  1.000 94.49112  ? 32  TYR D CE2 1 
ATOM   4241 C CZ  . TYR D 1 32  ? -59.49820 31.21101  13.09697  1.000 99.53092  ? 32  TYR D CZ  1 
ATOM   4242 O OH  . TYR D 1 32  ? -60.66387 31.93550  13.17531  1.000 92.36410  ? 32  TYR D OH  1 
ATOM   4243 N N   . LYS D 1 33  ? -54.25621 26.00644  12.97825  1.000 82.84957  ? 33  LYS D N   1 
ATOM   4244 C CA  . LYS D 1 33  ? -52.98193 25.32881  12.77644  1.000 75.60642  ? 33  LYS D CA  1 
ATOM   4245 C C   . LYS D 1 33  ? -52.75030 25.11157  11.29548  1.000 80.09789  ? 33  LYS D C   1 
ATOM   4246 O O   . LYS D 1 33  ? -53.57131 24.48701  10.61574  1.000 85.01758  ? 33  LYS D O   1 
ATOM   4247 C CB  . LYS D 1 33  ? -52.94936 23.96313  13.47386  1.000 93.90898  ? 33  LYS D CB  1 
ATOM   4248 C CG  . LYS D 1 33  ? -51.56899 23.45510  13.90653  1.000 104.34852 ? 33  LYS D CG  1 
ATOM   4249 C CD  . LYS D 1 33  ? -51.31472 23.30700  15.38918  1.000 126.41014 ? 33  LYS D CD  1 
ATOM   4250 C CE  . LYS D 1 33  ? -49.84409 22.91379  15.59687  1.000 126.92388 ? 33  LYS D CE  1 
ATOM   4251 N NZ  . LYS D 1 33  ? -48.98659 23.99068  16.16787  1.000 127.99081 ? 33  LYS D NZ  1 
ATOM   4252 N N   . LEU D 1 34  ? -51.61546 25.60508  10.81436  1.000 76.01730  ? 34  LEU D N   1 
ATOM   4253 C CA  . LEU D 1 34  ? -51.16688 25.40549  9.44877   1.000 76.64955  ? 34  LEU D CA  1 
ATOM   4254 C C   . LEU D 1 34  ? -49.93236 24.52759  9.51284   1.000 80.59870  ? 34  LEU D C   1 
ATOM   4255 O O   . LEU D 1 34  ? -49.01094 24.81329  10.28459  1.000 79.69156  ? 34  LEU D O   1 
ATOM   4256 C CB  . LEU D 1 34  ? -50.83627 26.72104  8.74585   1.000 73.72550  ? 34  LEU D CB  1 
ATOM   4257 C CG  . LEU D 1 34  ? -51.97402 27.59897  8.24166   1.000 78.56591  ? 34  LEU D CG  1 
ATOM   4258 C CD1 . LEU D 1 34  ? -51.38354 28.85157  7.61874   1.000 63.14771  ? 34  LEU D CD1 1 
ATOM   4259 C CD2 . LEU D 1 34  ? -52.83681 26.84404  7.24880   1.000 81.68009  ? 34  LEU D CD2 1 
ATOM   4260 N N   . ASN D 1 35  ? -49.91544 23.45542  8.73362   1.000 76.17003  ? 35  ASN D N   1 
ATOM   4261 C CA  . ASN D 1 35  ? -48.74744 22.59439  8.73644   1.000 72.60871  ? 35  ASN D CA  1 
ATOM   4262 C C   . ASN D 1 35  ? -48.46087 22.19175  7.29973   1.000 75.26839  ? 35  ASN D C   1 
ATOM   4263 O O   . ASN D 1 35  ? -49.37431 21.78964  6.57263   1.000 77.15947  ? 35  ASN D O   1 
ATOM   4264 C CB  . ASN D 1 35  ? -48.96571 21.37481  9.64256   1.000 77.95622  ? 35  ASN D CB  1 
ATOM   4265 C CG  . ASN D 1 35  ? -47.97777 20.27169  9.38275   1.000 78.45078  ? 35  ASN D CG  1 
ATOM   4266 O OD1 . ASN D 1 35  ? -46.90353 20.23412  9.98509   1.000 97.60776  ? 35  ASN D OD1 1 
ATOM   4267 N ND2 . ASN D 1 35  ? -48.33212 19.35711  8.49652   1.000 103.24925 ? 35  ASN D ND2 1 
ATOM   4268 N N   . ILE D 1 36  ? -47.20083 22.31578  6.89314   1.000 76.53422  ? 36  ILE D N   1 
ATOM   4269 C CA  . ILE D 1 36  ? -46.80437 22.07088  5.51050   1.000 77.12285  ? 36  ILE D CA  1 
ATOM   4270 C C   . ILE D 1 36  ? -46.57931 20.56950  5.34335   1.000 81.15110  ? 36  ILE D C   1 
ATOM   4271 O O   . ILE D 1 36  ? -45.62058 20.01194  5.88173   1.000 74.67223  ? 36  ILE D O   1 
ATOM   4272 C CB  . ILE D 1 36  ? -45.55864 22.87781  5.13287   1.000 69.26511  ? 36  ILE D CB  1 
ATOM   4273 C CG1 . ILE D 1 36  ? -45.84800 24.37125  5.30218   1.000 79.36454  ? 36  ILE D CG1 1 
ATOM   4274 C CG2 . ILE D 1 36  ? -45.16014 22.60612  3.69062   1.000 68.48848  ? 36  ILE D CG2 1 
ATOM   4275 C CD1 . ILE D 1 36  ? -44.65105 25.25914  5.10224   1.000 67.29684  ? 36  ILE D CD1 1 
ATOM   4276 N N   . MET D 1 37  ? -47.47967 19.91419  4.60389   1.000 79.25084  ? 37  MET D N   1 
ATOM   4277 C CA  . MET D 1 37  ? -47.40002 18.47710  4.35239   1.000 81.51277  ? 37  MET D CA  1 
ATOM   4278 C C   . MET D 1 37  ? -46.35197 18.13276  3.30217   1.000 76.42038  ? 37  MET D C   1 
ATOM   4279 O O   . MET D 1 37  ? -45.68240 17.09758  3.40617   1.000 81.65615  ? 37  MET D O   1 
ATOM   4280 C CB  . MET D 1 37  ? -48.76611 17.94676  3.90466   1.000 88.44302  ? 37  MET D CB  1 
ATOM   4281 C CG  . MET D 1 37  ? -49.85218 17.96314  4.96615   1.000 86.56983  ? 37  MET D CG  1 
ATOM   4282 S SD  . MET D 1 37  ? -49.16783 17.92963  6.62715   1.000 109.62048 ? 37  MET D SD  1 
ATOM   4283 C CE  . MET D 1 37  ? -48.98110 16.16764  6.90809   1.000 96.76247  ? 37  MET D CE  1 
ATOM   4284 N N   . GLN D 1 38  ? -46.21696 18.96886  2.27549   1.000 72.17181  ? 38  GLN D N   1 
ATOM   4285 C CA  . GLN D 1 38  ? -45.33016 18.70778  1.14540   1.000 71.11020  ? 38  GLN D CA  1 
ATOM   4286 C C   . GLN D 1 38  ? -44.54954 19.97558  0.82938   1.000 76.44910  ? 38  GLN D C   1 
ATOM   4287 O O   . GLN D 1 38  ? -45.11840 20.95481  0.33555   1.000 72.31640  ? 38  GLN D O   1 
ATOM   4288 C CB  . GLN D 1 38  ? -46.12459 18.24550  -0.07222  1.000 71.56658  ? 38  GLN D CB  1 
ATOM   4289 C CG  . GLN D 1 38  ? -45.29870 18.00770  -1.31020  1.000 76.14123  ? 38  GLN D CG  1 
ATOM   4290 C CD  . GLN D 1 38  ? -45.87462 16.90959  -2.17016  1.000 86.66703  ? 38  GLN D CD  1 
ATOM   4291 O OE1 . GLN D 1 38  ? -45.39482 15.77432  -2.16286  1.000 99.98636  ? 38  GLN D OE1 1 
ATOM   4292 N NE2 . GLN D 1 38  ? -46.92890 17.23995  -2.91099  1.000 74.66144  ? 38  GLN D NE2 1 
ATOM   4293 N N   . GLN D 1 39  ? -43.26734 19.96013  1.12315   1.000 79.44090  ? 39  GLN D N   1 
ATOM   4294 C CA  . GLN D 1 39  ? -42.39917 21.09262  0.86428   1.000 81.03132  ? 39  GLN D CA  1 
ATOM   4295 C C   . GLN D 1 39  ? -41.92071 21.08480  -0.58538  1.000 83.49234  ? 39  GLN D C   1 
ATOM   4296 O O   . GLN D 1 39  ? -41.80988 20.02824  -1.20976  1.000 77.89192  ? 39  GLN D O   1 
ATOM   4297 C CB  . GLN D 1 39  ? -41.19238 21.05316  1.79161   1.000 80.12229  ? 39  GLN D CB  1 
ATOM   4298 C CG  . GLN D 1 39  ? -41.53069 21.22957  3.25451   1.000 84.10039  ? 39  GLN D CG  1 
ATOM   4299 C CD  . GLN D 1 39  ? -41.28520 22.63541  3.72185   1.000 94.47380  ? 39  GLN D CD  1 
ATOM   4300 O OE1 . GLN D 1 39  ? -40.64152 23.42511  3.02657   1.000 89.49716  ? 39  GLN D OE1 1 
ATOM   4301 N NE2 . GLN D 1 39  ? -41.79102 22.96388  4.90719   1.000 89.53228  ? 39  GLN D NE2 1 
ATOM   4302 N N   . PRO D 1 40  ? -41.63458 22.25256  -1.14510  1.000 93.39012  ? 40  PRO D N   1 
ATOM   4303 C CA  . PRO D 1 40  ? -40.88890 22.29249  -2.40534  1.000 87.28940  ? 40  PRO D CA  1 
ATOM   4304 C C   . PRO D 1 40  ? -39.40256 22.13055  -2.13695  1.000 72.01393  ? 40  PRO D C   1 
ATOM   4305 O O   . PRO D 1 40  ? -38.85409 22.68166  -1.18037  1.000 80.58786  ? 40  PRO D O   1 
ATOM   4306 C CB  . PRO D 1 40  ? -41.19954 23.69025  -2.95269  1.000 89.09724  ? 40  PRO D CB  1 
ATOM   4307 C CG  . PRO D 1 40  ? -41.41967 24.51711  -1.71007  1.000 78.13799  ? 40  PRO D CG  1 
ATOM   4308 C CD  . PRO D 1 40  ? -42.03456 23.59267  -0.68273  1.000 80.24632  ? 40  PRO D CD  1 
ATOM   4309 N N   . LYS D 1 41  ? -38.75319 21.33525  -2.97522  1.000 75.45843  ? 41  LYS D N   1 
ATOM   4310 C CA  . LYS D 1 41  ? -37.33101 21.05753  -2.83178  1.000 87.93029  ? 41  LYS D CA  1 
ATOM   4311 C C   . LYS D 1 41  ? -36.49188 21.89896  -3.78377  1.000 92.29137  ? 41  LYS D C   1 
ATOM   4312 O O   . LYS D 1 41  ? -35.55543 22.58360  -3.36159  1.000 90.05195  ? 41  LYS D O   1 
ATOM   4313 C CB  . LYS D 1 41  ? -37.06093 19.56643  -3.05113  1.000 88.26174  ? 41  LYS D CB  1 
ATOM   4314 C CG  . LYS D 1 41  ? -37.97276 18.65151  -2.25271  1.000 103.26259 ? 41  LYS D CG  1 
ATOM   4315 C CD  . LYS D 1 41  ? -38.51738 17.53918  -3.12007  1.000 89.60086  ? 41  LYS D CD  1 
ATOM   4316 C CE  . LYS D 1 41  ? -39.47483 16.66904  -2.33370  1.000 119.25856 ? 41  LYS D CE  1 
ATOM   4317 N NZ  . LYS D 1 41  ? -38.73812 15.80211  -1.36808  1.000 131.57043 ? 41  LYS D NZ  1 
ATOM   4318 N N   A ARG D 1 42  ? -36.83356 21.87350  -5.06628  0.695 89.05610  ? 42  ARG D N   1 
ATOM   4319 N N   B ARG D 1 42  ? -36.79085 21.82884  -5.07956  0.305 90.81568  ? 42  ARG D N   1 
ATOM   4320 C CA  A ARG D 1 42  ? -36.10107 22.63232  -6.05947  0.695 86.14328  ? 42  ARG D CA  1 
ATOM   4321 C CA  B ARG D 1 42  ? -36.07476 22.60010  -6.08560  0.305 80.66172  ? 42  ARG D CA  1 
ATOM   4322 C C   A ARG D 1 42  ? -37.03069 22.91350  -7.23194  0.695 86.58307  ? 42  ARG D C   1 
ATOM   4323 C C   B ARG D 1 42  ? -37.00688 22.88322  -7.25610  0.305 90.95236  ? 42  ARG D C   1 
ATOM   4324 O O   A ARG D 1 42  ? -38.06903 22.26613  -7.39798  0.695 85.92682  ? 42  ARG D O   1 
ATOM   4325 O O   B ARG D 1 42  ? -38.01317 22.19703  -7.45487  0.305 86.70476  ? 42  ARG D O   1 
ATOM   4326 C CB  A ARG D 1 42  ? -34.86083 21.86052  -6.53106  0.695 90.94166  ? 42  ARG D CB  1 
ATOM   4327 C CB  B ARG D 1 42  ? -34.81494 21.86684  -6.56496  0.305 97.55578  ? 42  ARG D CB  1 
ATOM   4328 C CG  A ARG D 1 42  ? -33.56502 22.16481  -5.78417  0.695 95.20142  ? 42  ARG D CG  1 
ATOM   4329 C CG  B ARG D 1 42  ? -33.54571 22.18971  -5.78870  0.305 93.55036  ? 42  ARG D CG  1 
ATOM   4330 C CD  A ARG D 1 42  ? -32.65912 20.92191  -5.75162  0.695 97.66341  ? 42  ARG D CD  1 
ATOM   4331 C CD  B ARG D 1 42  ? -32.55212 21.03422  -5.86428  0.305 97.09412  ? 42  ARG D CD  1 
ATOM   4332 N NE  A ARG D 1 42  ? -33.10677 19.92638  -4.78213  0.695 96.37873  ? 42  ARG D NE  1 
ATOM   4333 N NE  B ARG D 1 42  ? -31.41701 21.22724  -4.97022  0.305 95.53484  ? 42  ARG D NE  1 
ATOM   4334 C CZ  A ARG D 1 42  ? -33.33846 18.65249  -5.07396  0.695 97.98124  ? 42  ARG D CZ  1 
ATOM   4335 C CZ  B ARG D 1 42  ? -30.49726 20.30647  -4.71602  0.305 90.32636  ? 42  ARG D CZ  1 
ATOM   4336 N NH1 A ARG D 1 42  ? -33.17487 18.18480  -6.29991  0.695 102.55093 ? 42  ARG D NH1 1 
ATOM   4337 N NH1 B ARG D 1 42  ? -30.54561 19.10847  -5.27500  0.305 83.78150  ? 42  ARG D NH1 1 
ATOM   4338 N NH2 A ARG D 1 42  ? -33.76729 17.83183  -4.11772  0.695 85.38873  ? 42  ARG D NH2 1 
ATOM   4339 N NH2 B ARG D 1 42  ? -29.51133 20.59064  -3.86904  0.305 84.88431  ? 42  ARG D NH2 1 
ATOM   4340 N N   . ALA D 1 43  ? -36.66402 23.91172  -8.02940  1.000 86.00212  ? 43  ALA D N   1 
ATOM   4341 C CA  . ALA D 1 43  ? -37.48078 24.30207  -9.16577  1.000 82.29557  ? 43  ALA D CA  1 
ATOM   4342 C C   . ALA D 1 43  ? -36.56893 24.86946  -10.24362 1.000 85.55746  ? 43  ALA D C   1 
ATOM   4343 O O   . ALA D 1 43  ? -35.42495 25.24782  -9.97978  1.000 87.39488  ? 43  ALA D O   1 
ATOM   4344 C CB  . ALA D 1 43  ? -38.55218 25.32264  -8.76053  1.000 92.79081  ? 43  ALA D CB  1 
ATOM   4345 N N   . ARG D 1 44  ? -37.10099 24.95200  -11.46029 1.000 82.61616  ? 44  ARG D N   1 
ATOM   4346 C CA  . ARG D 1 44  ? -36.37958 25.49600  -12.60475 1.000 80.47812  ? 44  ARG D CA  1 
ATOM   4347 C C   . ARG D 1 44  ? -36.87226 26.90971  -12.88654 1.000 89.77010  ? 44  ARG D C   1 
ATOM   4348 O O   . ARG D 1 44  ? -38.08091 27.13517  -13.01298 1.000 83.69933  ? 44  ARG D O   1 
ATOM   4349 C CB  . ARG D 1 44  ? -36.55712 24.61044  -13.83952 1.000 81.79764  ? 44  ARG D CB  1 
ATOM   4350 C CG  . ARG D 1 44  ? -35.98392 25.18837  -15.13023 1.000 90.34421  ? 44  ARG D CG  1 
ATOM   4351 C CD  . ARG D 1 44  ? -36.50564 24.42797  -16.34121 1.000 99.68313  ? 44  ARG D CD  1 
ATOM   4352 N NE  . ARG D 1 44  ? -36.43243 25.20654  -17.57174 1.000 97.55922  ? 44  ARG D NE  1 
ATOM   4353 C CZ  . ARG D 1 44  ? -35.91929 24.75644  -18.70949 1.000 111.65069 ? 44  ARG D CZ  1 
ATOM   4354 N NH1 . ARG D 1 44  ? -35.43024 23.53025  -18.81003 1.000 104.01113 ? 44  ARG D NH1 1 
ATOM   4355 N NH2 . ARG D 1 44  ? -35.90035 25.55415  -19.77458 1.000 100.76550 ? 44  ARG D NH2 1 
ATOM   4356 N N   . ALA D 1 45  ? -35.93939 27.85460  -12.97131 1.000 80.78477  ? 45  ALA D N   1 
ATOM   4357 C CA  . ALA D 1 45  ? -36.29802 29.23785  -13.24921 1.000 83.00059  ? 45  ALA D CA  1 
ATOM   4358 C C   . ALA D 1 45  ? -36.99022 29.34422  -14.60049 1.000 87.15787  ? 45  ALA D C   1 
ATOM   4359 O O   . ALA D 1 45  ? -36.51793 28.79145  -15.59792 1.000 91.47876  ? 45  ALA D O   1 
ATOM   4360 C CB  . ALA D 1 45  ? -35.05233 30.12208  -13.22185 1.000 81.96791  ? 45  ALA D CB  1 
ATOM   4361 N N   . CYS D 1 46  ? -38.11684 30.05630  -14.62974 1.000 89.88167  ? 46  CYS D N   1 
ATOM   4362 C CA  . CYS D 1 46  ? -38.87991 30.24398  -15.85608 1.000 94.47436  ? 46  CYS D CA  1 
ATOM   4363 C C   . CYS D 1 46  ? -38.46009 31.48217  -16.63680 1.000 106.62999 ? 46  CYS D C   1 
ATOM   4364 O O   . CYS D 1 46  ? -38.95016 31.68409  -17.75367 1.000 133.80906 ? 46  CYS D O   1 
ATOM   4365 C CB  . CYS D 1 46  ? -40.38144 30.30882  -15.55558 1.000 96.76473  ? 46  CYS D CB  1 
ATOM   4366 S SG  . CYS D 1 46  ? -40.88112 31.61229  -14.42969 1.000 113.36430 ? 46  CYS D SG  1 
ATOM   4367 N N   . GLY D 1 47  ? -37.56896 32.30398  -16.08745 1.000 106.33749 ? 47  GLY D N   1 
ATOM   4368 C CA  . GLY D 1 47  ? -37.11363 33.48463  -16.78800 1.000 123.95009 ? 47  GLY D CA  1 
ATOM   4369 C C   . GLY D 1 47  ? -38.24203 34.47936  -17.02212 1.000 141.23475 ? 47  GLY D C   1 
ATOM   4370 O O   . GLY D 1 47  ? -39.25908 34.49492  -16.32701 1.000 137.35350 ? 47  GLY D O   1 
ATOM   4371 N N   . GLN D 1 48  ? -38.05265 35.31162  -18.04296 1.000 166.33141 ? 48  GLN D N   1 
ATOM   4372 C CA  . GLN D 1 48  ? -39.06796 36.26339  -18.46897 1.000 174.03637 ? 48  GLN D CA  1 
ATOM   4373 C C   . GLN D 1 48  ? -39.09483 36.31034  -19.98999 1.000 201.77853 ? 48  GLN D C   1 
ATOM   4374 O O   . GLN D 1 48  ? -38.37605 35.57168  -20.67056 1.000 198.76780 ? 48  GLN D O   1 
ATOM   4375 C CB  . GLN D 1 48  ? -38.81860 37.65678  -17.87542 1.000 160.10458 ? 48  GLN D CB  1 
ATOM   4376 C CG  . GLN D 1 48  ? -37.35236 38.03201  -17.73732 1.000 159.81060 ? 48  GLN D CG  1 
ATOM   4377 C CD  . GLN D 1 48  ? -36.76423 37.59303  -16.41089 1.000 151.15067 ? 48  GLN D CD  1 
ATOM   4378 O OE1 . GLN D 1 48  ? -37.43955 37.62021  -15.38205 1.000 132.24204 ? 48  GLN D OE1 1 
ATOM   4379 N NE2 . GLN D 1 48  ? -35.50142 37.17948  -16.42892 1.000 150.59858 ? 48  GLN D NE2 1 
ATOM   4380 N N   . GLY D 1 49  ? -39.93713 37.18754  -20.52148 1.000 233.72675 ? 49  GLY D N   1 
ATOM   4381 C CA  . GLY D 1 49  ? -40.02515 37.38292  -21.95191 1.000 256.39280 ? 49  GLY D CA  1 
ATOM   4382 C C   . GLY D 1 49  ? -41.11302 36.54781  -22.59635 1.000 258.14324 ? 49  GLY D C   1 
ATOM   4383 O O   . GLY D 1 49  ? -41.93496 35.90045  -21.94075 1.000 252.68411 ? 49  GLY D O   1 
ATOM   4384 N N   . SER D 1 50  ? -41.10307 36.57156  -23.93160 1.000 234.49761 ? 50  SER D N   1 
ATOM   4385 C CA  . SER D 1 50  ? -42.13644 35.89135  -24.70880 1.000 226.98374 ? 50  SER D CA  1 
ATOM   4386 C C   . SER D 1 50  ? -42.15135 34.38742  -24.45615 1.000 225.07843 ? 50  SER D C   1 
ATOM   4387 O O   . SER D 1 50  ? -43.22454 33.78757  -24.32150 1.000 224.94781 ? 50  SER D O   1 
ATOM   4388 C CB  . SER D 1 50  ? -41.93903 36.17898  -26.19676 1.000 221.23188 ? 50  SER D CB  1 
ATOM   4389 O OG  . SER D 1 50  ? -40.93907 35.33951  -26.74684 1.000 210.09549 ? 50  SER D OG  1 
ATOM   4390 N N   . LYS D 1 51  ? -40.97611 33.75725  -24.39444 1.000 218.58355 ? 51  LYS D N   1 
ATOM   4391 C CA  . LYS D 1 51  ? -40.92907 32.31506  -24.16898 1.000 208.56521 ? 51  LYS D CA  1 
ATOM   4392 C C   . LYS D 1 51  ? -41.43616 31.93051  -22.78256 1.000 218.39434 ? 51  LYS D C   1 
ATOM   4393 O O   . LYS D 1 51  ? -42.02199 30.85424  -22.61907 1.000 215.32211 ? 51  LYS D O   1 
ATOM   4394 C CB  . LYS D 1 51  ? -39.50264 31.80069  -24.36863 1.000 193.19169 ? 51  LYS D CB  1 
ATOM   4395 C CG  . LYS D 1 51  ? -39.30609 30.97316  -25.62838 1.000 180.24530 ? 51  LYS D CG  1 
ATOM   4396 C CD  . LYS D 1 51  ? -39.16889 31.86199  -26.85287 1.000 173.50887 ? 51  LYS D CD  1 
ATOM   4397 C CE  . LYS D 1 51  ? -38.60840 31.08864  -28.03320 1.000 160.45556 ? 51  LYS D CE  1 
ATOM   4398 N NZ  . LYS D 1 51  ? -38.26791 31.98579  -29.17006 1.000 146.89568 ? 51  LYS D NZ  1 
ATOM   4399 N N   . SER D 1 52  ? -41.21732 32.78286  -21.77737 1.000 241.18187 ? 52  SER D N   1 
ATOM   4400 C CA  . SER D 1 52  ? -41.60617 32.44330  -20.40995 1.000 233.14141 ? 52  SER D CA  1 
ATOM   4401 C C   . SER D 1 52  ? -43.11623 32.29960  -20.25126 1.000 236.63645 ? 52  SER D C   1 
ATOM   4402 O O   . SER D 1 52  ? -43.57800 31.53614  -19.39505 1.000 221.98124 ? 52  SER D O   1 
ATOM   4403 C CB  . SER D 1 52  ? -41.07941 33.49793  -19.43875 1.000 213.54968 ? 52  SER D CB  1 
ATOM   4404 O OG  . SER D 1 52  ? -41.75031 34.73407  -19.61539 1.000 214.80779 ? 52  SER D OG  1 
ATOM   4405 N N   . HIS D 1 53  ? -43.89924 33.01667  -21.05772 1.000 226.10633 ? 53  HIS D N   1 
ATOM   4406 C CA  . HIS D 1 53  ? -45.35061 33.01798  -20.91346 1.000 221.94723 ? 53  HIS D CA  1 
ATOM   4407 C C   . HIS D 1 53  ? -46.01601 31.74927  -21.43377 1.000 218.66692 ? 53  HIS D C   1 
ATOM   4408 O O   . HIS D 1 53  ? -47.21376 31.55962  -21.19472 1.000 211.36165 ? 53  HIS D O   1 
ATOM   4409 C CB  . HIS D 1 53  ? -45.95116 34.23409  -21.62702 1.000 220.98725 ? 53  HIS D CB  1 
ATOM   4410 C CG  . HIS D 1 53  ? -45.51056 35.54841  -21.06000 1.000 219.07468 ? 53  HIS D CG  1 
ATOM   4411 N ND1 . HIS D 1 53  ? -45.81230 35.94370  -19.77449 1.000 213.28150 ? 53  HIS D ND1 1 
ATOM   4412 C CD2 . HIS D 1 53  ? -44.80459 36.56486  -21.60941 1.000 219.66721 ? 53  HIS D CD2 1 
ATOM   4413 C CE1 . HIS D 1 53  ? -45.30134 37.14162  -19.55261 1.000 208.64378 ? 53  HIS D CE1 1 
ATOM   4414 N NE2 . HIS D 1 53  ? -44.68483 37.54106  -20.65023 1.000 215.13234 ? 53  HIS D NE2 1 
ATOM   4415 N N   . THR D 1 54  ? -45.28203 30.88008  -22.12922 1.000 223.12896 ? 54  THR D N   1 
ATOM   4416 C CA  . THR D 1 54  ? -45.84771 29.62874  -22.61457 1.000 214.98206 ? 54  THR D CA  1 
ATOM   4417 C C   . THR D 1 54  ? -44.91609 28.43124  -22.48184 1.000 209.48773 ? 54  THR D C   1 
ATOM   4418 O O   . THR D 1 54  ? -45.27625 27.34620  -22.94929 1.000 206.42272 ? 54  THR D O   1 
ATOM   4419 C CB  . THR D 1 54  ? -46.27494 29.76705  -24.08771 1.000 212.48973 ? 54  THR D CB  1 
ATOM   4420 O OG1 . THR D 1 54  ? -45.37075 30.64332  -24.77218 1.000 214.55613 ? 54  THR D OG1 1 
ATOM   4421 C CG2 . THR D 1 54  ? -47.68960 30.32257  -24.18814 1.000 206.83161 ? 54  THR D CG2 1 
ATOM   4422 N N   . ASP D 1 55  ? -43.74415 28.58019  -21.86745 1.000 207.25178 ? 55  ASP D N   1 
ATOM   4423 C CA  . ASP D 1 55  ? -42.78346 27.48904  -21.74124 1.000 200.51945 ? 55  ASP D CA  1 
ATOM   4424 C C   . ASP D 1 55  ? -42.22313 27.40745  -20.32537 1.000 195.38151 ? 55  ASP D C   1 
ATOM   4425 O O   . ASP D 1 55  ? -41.02140 27.20717  -20.12457 1.000 190.71954 ? 55  ASP D O   1 
ATOM   4426 C CB  . ASP D 1 55  ? -41.65538 27.64854  -22.76016 1.000 201.76738 ? 55  ASP D CB  1 
ATOM   4427 C CG  . ASP D 1 55  ? -40.95444 26.33992  -23.07107 1.000 203.53803 ? 55  ASP D CG  1 
ATOM   4428 O OD1 . ASP D 1 55  ? -41.29513 25.31635  -22.44223 1.000 207.46552 ? 55  ASP D OD1 1 
ATOM   4429 O OD2 . ASP D 1 55  ? -40.06475 26.33522  -23.94915 1.000 195.71177 ? 55  ASP D OD2 1 
ATOM   4430 N N   . ARG D 1 56  ? -43.08135 27.56285  -19.31971 1.000 192.33404 ? 56  ARG D N   1 
ATOM   4431 C CA  . ARG D 1 56  ? -42.66102 27.51214  -17.92623 1.000 169.58386 ? 56  ARG D CA  1 
ATOM   4432 C C   . ARG D 1 56  ? -43.02382 26.16700  -17.30060 1.000 146.07800 ? 56  ARG D C   1 
ATOM   4433 O O   . ARG D 1 56  ? -43.82941 25.40016  -17.83551 1.000 138.11682 ? 56  ARG D O   1 
ATOM   4434 C CB  . ARG D 1 56  ? -43.28483 28.65890  -17.12753 1.000 158.78687 ? 56  ARG D CB  1 
ATOM   4435 C CG  . ARG D 1 56  ? -44.77146 28.84266  -17.34890 1.000 159.60416 ? 56  ARG D CG  1 
ATOM   4436 C CD  . ARG D 1 56  ? -45.46759 29.16676  -16.04575 1.000 150.32810 ? 56  ARG D CD  1 
ATOM   4437 N NE  . ARG D 1 56  ? -46.90007 29.36410  -16.22286 1.000 142.82664 ? 56  ARG D NE  1 
ATOM   4438 C CZ  . ARG D 1 56  ? -47.78162 29.34193  -15.23358 1.000 128.37367 ? 56  ARG D CZ  1 
ATOM   4439 N NH1 . ARG D 1 56  ? -47.41116 29.11336  -13.98398 1.000 112.82312 ? 56  ARG D NH1 1 
ATOM   4440 N NH2 . ARG D 1 56  ? -49.06623 29.55565  -15.50375 1.000 130.71485 ? 56  ARG D NH2 1 
ATOM   4441 N N   . ARG D 1 57  ? -42.41196 25.88982  -16.14919 1.000 130.77003 ? 57  ARG D N   1 
ATOM   4442 C CA  . ARG D 1 57  ? -42.54224 24.59586  -15.48165 1.000 108.23778 ? 57  ARG D CA  1 
ATOM   4443 C C   . ARG D 1 57  ? -42.83047 24.79738  -13.99889 1.000 99.35958  ? 57  ARG D C   1 
ATOM   4444 O O   . ARG D 1 57  ? -41.98213 25.36015  -13.27537 1.000 92.48256  ? 57  ARG D O   1 
ATOM   4445 C CB  . ARG D 1 57  ? -41.26173 23.79198  -15.72467 1.000 99.90796  ? 57  ARG D CB  1 
ATOM   4446 C CG  . ARG D 1 57  ? -41.45316 22.31523  -16.02766 1.000 107.37098 ? 57  ARG D CG  1 
ATOM   4447 C CD  . ARG D 1 57  ? -40.09757 21.60916  -16.09525 1.000 110.64999 ? 57  ARG D CD  1 
ATOM   4448 N NE  . ARG D 1 57  ? -39.44924 21.41291  -14.80527 1.000 120.85107 ? 57  ARG D NE  1 
ATOM   4449 C CZ  . ARG D 1 57  ? -38.90957 20.26672  -14.41254 1.000 119.02468 ? 57  ARG D CZ  1 
ATOM   4450 N NH1 . ARG D 1 57  ? -38.94118 19.18835  -15.18127 1.000 106.44232 ? 57  ARG D NH1 1 
ATOM   4451 N NH2 . ARG D 1 57  ? -38.32939 20.19839  -13.21691 1.000 113.66134 ? 57  ARG D NH2 1 
ATOM   4452 N N   . PRO D 1 58  ? -43.98576 24.36192  -13.50012 1.000 89.91224  ? 58  PRO D N   1 
ATOM   4453 C CA  . PRO D 1 58  ? -44.35721 24.65919  -12.11102 1.000 88.89131  ? 58  PRO D CA  1 
ATOM   4454 C C   . PRO D 1 58  ? -43.46261 23.94110  -11.11139 1.000 89.37927  ? 58  PRO D C   1 
ATOM   4455 O O   . PRO D 1 58  ? -42.83612 22.92283  -11.41129 1.000 102.63471 ? 58  PRO D O   1 
ATOM   4456 C CB  . PRO D 1 58  ? -45.80722 24.16733  -12.00303 1.000 78.35717  ? 58  PRO D CB  1 
ATOM   4457 C CG  . PRO D 1 58  ? -46.25742 23.88242  -13.40553 1.000 87.98514  ? 58  PRO D CG  1 
ATOM   4458 C CD  . PRO D 1 58  ? -45.03762 23.63492  -14.22895 1.000 92.33883  ? 58  PRO D CD  1 
ATOM   4459 N N   . VAL D 1 59  ? -43.40670 24.50084  -9.89785  1.000 93.68009  ? 59  VAL D N   1 
ATOM   4460 C CA  . VAL D 1 59  ? -42.64116 23.86894  -8.83075  1.000 92.94162  ? 59  VAL D CA  1 
ATOM   4461 C C   . VAL D 1 59  ? -43.19714 22.47757  -8.56623  1.000 94.15632  ? 59  VAL D C   1 
ATOM   4462 O O   . VAL D 1 59  ? -44.41683 22.26294  -8.54954  1.000 84.43253  ? 59  VAL D O   1 
ATOM   4463 C CB  . VAL D 1 59  ? -42.68370 24.72995  -7.55620  1.000 73.32664  ? 59  VAL D CB  1 
ATOM   4464 C CG1 . VAL D 1 59  ? -41.65528 24.25206  -6.55383  1.000 83.29367  ? 59  VAL D CG1 1 
ATOM   4465 C CG2 . VAL D 1 59  ? -42.44241 26.18691  -7.89267  1.000 91.94571  ? 59  VAL D CG2 1 
ATOM   4466 N N   . ASP D 1 60  ? -42.29477 21.52170  -8.34551  1.000 90.45796  ? 60  ASP D N   1 
ATOM   4467 C CA  . ASP D 1 60  ? -42.66376 20.13696  -8.11246  1.000 88.61161  ? 60  ASP D CA  1 
ATOM   4468 C C   . ASP D 1 60  ? -41.80796 19.57971  -6.98299  1.000 86.67738  ? 60  ASP D C   1 
ATOM   4469 O O   . ASP D 1 60  ? -40.59431 19.82958  -6.94570  1.000 97.75620  ? 60  ASP D O   1 
ATOM   4470 C CB  . ASP D 1 60  ? -42.50227 19.28853  -9.37965  1.000 113.97568 ? 60  ASP D CB  1 
ATOM   4471 C CG  . ASP D 1 60  ? -43.24201 17.96665  -9.29820  1.000 113.00086 ? 60  ASP D CG  1 
ATOM   4472 O OD1 . ASP D 1 60  ? -44.48903 17.98669  -9.21718  1.000 108.62813 ? 60  ASP D OD1 1 
ATOM   4473 O OD2 . ASP D 1 60  ? -42.58153 16.90801  -9.34869  1.000 109.93188 ? 60  ASP D OD2 1 
ATOM   4474 N N   . PRO D 1 61  ? -42.40774 18.84903  -6.03684  1.000 87.23301  ? 61  PRO D N   1 
ATOM   4475 C CA  . PRO D 1 61  ? -43.83842 18.55086  -5.91274  1.000 82.25335  ? 61  PRO D CA  1 
ATOM   4476 C C   . PRO D 1 61  ? -44.60797 19.78296  -5.46277  1.000 82.83059  ? 61  PRO D C   1 
ATOM   4477 O O   . PRO D 1 61  ? -44.05830 20.63778  -4.77081  1.000 78.75269  ? 61  PRO D O   1 
ATOM   4478 C CB  . PRO D 1 61  ? -43.85963 17.42756  -4.86889  1.000 81.10820  ? 61  PRO D CB  1 
ATOM   4479 C CG  . PRO D 1 61  ? -42.68374 17.73215  -3.99310  1.000 74.61359  ? 61  PRO D CG  1 
ATOM   4480 C CD  . PRO D 1 61  ? -41.62798 18.21797  -4.95548  1.000 87.06534  ? 61  PRO D CD  1 
ATOM   4481 N N   . PRO D 1 62  ? -45.87037 19.89930  -5.86393  1.000 82.91664  ? 62  PRO D N   1 
ATOM   4482 C CA  . PRO D 1 62  ? -46.66210 21.07561  -5.50419  1.000 71.47468  ? 62  PRO D CA  1 
ATOM   4483 C C   . PRO D 1 62  ? -46.78813 21.18584  -3.99782  1.000 69.83690  ? 62  PRO D C   1 
ATOM   4484 O O   . PRO D 1 62  ? -47.02730 20.18196  -3.31011  1.000 79.31933  ? 62  PRO D O   1 
ATOM   4485 C CB  . PRO D 1 62  ? -48.02203 20.80745  -6.16778  1.000 67.15545  ? 62  PRO D CB  1 
ATOM   4486 C CG  . PRO D 1 62  ? -48.07306 19.32793  -6.31251  1.000 74.40818  ? 62  PRO D CG  1 
ATOM   4487 C CD  . PRO D 1 62  ? -46.66335 18.92185  -6.62864  1.000 77.91844  ? 62  PRO D CD  1 
ATOM   4488 N N   . PRO D 1 63  ? -46.62773 22.38688  -3.44883  1.000 69.98246  ? 63  PRO D N   1 
ATOM   4489 C CA  . PRO D 1 63  ? -46.77190 22.55483  -1.99997  1.000 63.10210  ? 63  PRO D CA  1 
ATOM   4490 C C   . PRO D 1 63  ? -48.17911 22.20834  -1.53587  1.000 68.52335  ? 63  PRO D C   1 
ATOM   4491 O O   . PRO D 1 63  ? -49.17496 22.52513  -2.19121  1.000 65.59357  ? 63  PRO D O   1 
ATOM   4492 C CB  . PRO D 1 63  ? -46.46243 24.04217  -1.78218  1.000 66.03693  ? 63  PRO D CB  1 
ATOM   4493 C CG  . PRO D 1 63  ? -45.65175 24.44558  -2.96075  1.000 61.56125  ? 63  PRO D CG  1 
ATOM   4494 C CD  . PRO D 1 63  ? -46.15825 23.61800  -4.10959  1.000 70.68024  ? 63  PRO D CD  1 
ATOM   4495 N N   . VAL D 1 64  ? -48.23638 21.50813  -0.40615  1.000 71.86225  ? 64  VAL D N   1 
ATOM   4496 C CA  . VAL D 1 64  ? -49.47233 21.09193  0.24200   1.000 64.67681  ? 64  VAL D CA  1 
ATOM   4497 C C   . VAL D 1 64  ? -49.43182 21.61424  1.66715   1.000 70.34395  ? 64  VAL D C   1 
ATOM   4498 O O   . VAL D 1 64  ? -48.46218 21.37041  2.39466   1.000 73.71704  ? 64  VAL D O   1 
ATOM   4499 C CB  . VAL D 1 64  ? -49.64483 19.55979  0.24314   1.000 73.59290  ? 64  VAL D CB  1 
ATOM   4500 C CG1 . VAL D 1 64  ? -50.91626 19.16686  0.97904   1.000 67.51318  ? 64  VAL D CG1 1 
ATOM   4501 C CG2 . VAL D 1 64  ? -49.64902 19.01206  -1.15965  1.000 77.22197  ? 64  VAL D CG2 1 
ATOM   4502 N N   . ILE D 1 65  ? -50.47685 22.33018  2.06380   1.000 67.61724  ? 65  ILE D N   1 
ATOM   4503 C CA  . ILE D 1 65  ? -50.57832 22.89108  3.40262   1.000 71.38353  ? 65  ILE D CA  1 
ATOM   4504 C C   . ILE D 1 65  ? -51.86323 22.38293  4.03381   1.000 70.72123  ? 65  ILE D C   1 
ATOM   4505 O O   . ILE D 1 65  ? -52.92842 22.40995  3.40615   1.000 71.51936  ? 65  ILE D O   1 
ATOM   4506 C CB  . ILE D 1 65  ? -50.53979 24.43101  3.39333   1.000 66.88901  ? 65  ILE D CB  1 
ATOM   4507 C CG1 . ILE D 1 65  ? -49.13675 24.94113  3.04845   1.000 61.23938  ? 65  ILE D CG1 1 
ATOM   4508 C CG2 . ILE D 1 65  ? -50.95824 24.97144  4.74157   1.000 66.80167  ? 65  ILE D CG2 1 
ATOM   4509 C CD1 . ILE D 1 65  ? -48.85688 25.06475  1.56290   1.000 62.08538  ? 65  ILE D CD1 1 
ATOM   4510 N N   . GLU D 1 66  ? -51.74102 21.88172  5.25700   1.000 69.01085  ? 66  GLU D N   1 
ATOM   4511 C CA  . GLU D 1 66  ? -52.83865 21.32356  6.03029   1.000 76.17750  ? 66  GLU D CA  1 
ATOM   4512 C C   . GLU D 1 66  ? -53.30041 22.35710  7.04969   1.000 81.42781  ? 66  GLU D C   1 
ATOM   4513 O O   . GLU D 1 66  ? -52.47766 22.95944  7.74608   1.000 77.17990  ? 66  GLU D O   1 
ATOM   4514 C CB  . GLU D 1 66  ? -52.41332 20.02912  6.72487   1.000 78.58869  ? 66  GLU D CB  1 
ATOM   4515 C CG  . GLU D 1 66  ? -53.56572 19.19885  7.23246   1.000 87.00240  ? 66  GLU D CG  1 
ATOM   4516 C CD  . GLU D 1 66  ? -53.11842 17.88896  7.85002   1.000 99.91033  ? 66  GLU D CD  1 
ATOM   4517 O OE1 . GLU D 1 66  ? -52.78151 16.95296  7.09311   1.000 114.64632 ? 66  GLU D OE1 1 
ATOM   4518 O OE2 . GLU D 1 66  ? -53.12087 17.79070  9.09479   1.000 108.11867 ? 66  GLU D OE2 1 
ATOM   4519 N N   . LEU D 1 67  ? -54.60812 22.58321  7.10650   1.000 81.59004  ? 67  LEU D N   1 
ATOM   4520 C CA  . LEU D 1 67  ? -55.22599 23.51326  8.04286   1.000 77.42502  ? 67  LEU D CA  1 
ATOM   4521 C C   . LEU D 1 67  ? -56.11205 22.74313  9.01138   1.000 78.97410  ? 67  LEU D C   1 
ATOM   4522 O O   . LEU D 1 67  ? -56.95053 21.94136  8.58708   1.000 83.62645  ? 67  LEU D O   1 
ATOM   4523 C CB  . LEU D 1 67  ? -56.05584 24.57004  7.30939   1.000 84.14452  ? 67  LEU D CB  1 
ATOM   4524 C CG  . LEU D 1 67  ? -57.04124 25.35543  8.18859   1.000 80.31726  ? 67  LEU D CG  1 
ATOM   4525 C CD1 . LEU D 1 67  ? -56.31807 26.20516  9.22980   1.000 71.72645  ? 67  LEU D CD1 1 
ATOM   4526 C CD2 . LEU D 1 67  ? -57.99855 26.19667  7.35353   1.000 79.45530  ? 67  LEU D CD2 1 
ATOM   4527 N N   . ASN D 1 68  ? -55.94791 23.01460  10.30743  1.000 79.93036  ? 68  ASN D N   1 
ATOM   4528 C CA  . ASN D 1 68  ? -56.78467 22.41891  11.33957  1.000 89.51519  ? 68  ASN D CA  1 
ATOM   4529 C C   . ASN D 1 68  ? -57.27835 23.50779  12.27440  1.000 94.20208  ? 68  ASN D C   1 
ATOM   4530 O O   . ASN D 1 68  ? -56.50019 24.36897  12.69610  1.000 95.78535  ? 68  ASN D O   1 
ATOM   4531 C CB  . ASN D 1 68  ? -55.99596 21.41573  12.19642  1.000 87.14089  ? 68  ASN D CB  1 
ATOM   4532 C CG  . ASN D 1 68  ? -55.75678 20.10493  11.50688  1.000 101.49144 ? 68  ASN D CG  1 
ATOM   4533 O OD1 . ASN D 1 68  ? -56.01337 19.96732  10.32603  1.000 95.39407  ? 68  ASN D OD1 1 
ATOM   4534 N ND2 . ASN D 1 68  ? -55.24481 19.12958  12.24666  1.000 110.98632 ? 68  ASN D ND2 1 
ATOM   4535 N N   . ILE D 1 69  ? -58.57215 23.47414  12.58219  1.000 99.90712  ? 69  ILE D N   1 
ATOM   4536 C CA  . ILE D 1 69  ? -59.20400 24.44387  13.46596  1.000 100.16676 ? 69  ILE D CA  1 
ATOM   4537 C C   . ILE D 1 69  ? -59.65712 23.69670  14.70969  1.000 107.24730 ? 69  ILE D C   1 
ATOM   4538 O O   . ILE D 1 69  ? -60.34033 22.66980  14.60911  1.000 113.11238 ? 69  ILE D O   1 
ATOM   4539 C CB  . ILE D 1 69  ? -60.38347 25.15762  12.78107  1.000 112.50990 ? 69  ILE D CB  1 
ATOM   4540 C CG1 . ILE D 1 69  ? -60.05543 25.44439  11.31270  1.000 99.90074  ? 69  ILE D CG1 1 
ATOM   4541 C CG2 . ILE D 1 69  ? -60.75604 26.43163  13.53047  1.000 112.29775 ? 69  ILE D CG2 1 
ATOM   4542 C CD1 . ILE D 1 69  ? -61.21621 25.99858  10.52186  1.000 103.89308 ? 69  ILE D CD1 1 
ATOM   4543 N N   . PHE D 1 70  ? -59.28518 24.20879  15.87692  1.000 111.21435 ? 70  PHE D N   1 
ATOM   4544 C CA  . PHE D 1 70  ? -59.58329 23.55850  17.14416  1.000 118.72878 ? 70  PHE D CA  1 
ATOM   4545 C C   . PHE D 1 70  ? -60.44071 24.47302  18.00408  1.000 122.76588 ? 70  PHE D C   1 
ATOM   4546 O O   . PHE D 1 70  ? -60.09660 25.64308  18.20482  1.000 121.70167 ? 70  PHE D O   1 
ATOM   4547 C CB  . PHE D 1 70  ? -58.29556 23.17564  17.87610  1.000 115.26863 ? 70  PHE D CB  1 
ATOM   4548 C CG  . PHE D 1 70  ? -57.45393 22.18710  17.12660  1.000 125.81490 ? 70  PHE D CG  1 
ATOM   4549 C CD1 . PHE D 1 70  ? -57.83417 20.85690  17.04804  1.000 125.26388 ? 70  PHE D CD1 1 
ATOM   4550 C CD2 . PHE D 1 70  ? -56.29652 22.59049  16.47798  1.000 117.58924 ? 70  PHE D CD2 1 
ATOM   4551 C CE1 . PHE D 1 70  ? -57.06687 19.94199  16.35002  1.000 132.40156 ? 70  PHE D CE1 1 
ATOM   4552 C CE2 . PHE D 1 70  ? -55.52452 21.68223  15.77744  1.000 115.29070 ? 70  PHE D CE2 1 
ATOM   4553 C CZ  . PHE D 1 70  ? -55.91040 20.35517  15.71389  1.000 134.77505 ? 70  PHE D CZ  1 
ATOM   4554 N N   . GLU D 1 71  ? -61.55121 23.94634  18.50688  1.000 122.89993 ? 71  GLU D N   1 
ATOM   4555 C CA  . GLU D 1 71  ? -62.35822 24.66289  19.48017  1.000 128.46424 ? 71  GLU D CA  1 
ATOM   4556 C C   . GLU D 1 71  ? -61.94953 24.21324  20.87322  1.000 130.91950 ? 71  GLU D C   1 
ATOM   4557 O O   . GLU D 1 71  ? -61.67778 23.03075  21.09969  1.000 137.06580 ? 71  GLU D O   1 
ATOM   4558 C CB  . GLU D 1 71  ? -63.85241 24.40413  19.26540  1.000 129.55901 ? 71  GLU D CB  1 
ATOM   4559 C CG  . GLU D 1 71  ? -64.77198 24.96599  20.34093  1.000 125.05229 ? 71  GLU D CG  1 
ATOM   4560 C CD  . GLU D 1 71  ? -66.15715 24.34441  20.30228  1.000 145.38128 ? 71  GLU D CD  1 
ATOM   4561 O OE1 . GLU D 1 71  ? -66.85649 24.51529  19.28125  1.000 136.95008 ? 71  GLU D OE1 1 
ATOM   4562 O OE2 . GLU D 1 71  ? -66.55008 23.69095  21.29272  1.000 152.80978 ? 71  GLU D OE2 1 
ATOM   4563 N N   . SER D 1 72  ? -61.88874 25.16113  21.80081  1.000 126.42886 ? 72  SER D N   1 
ATOM   4564 C CA  . SER D 1 72  ? -61.65114 24.81824  23.19058  1.000 145.45568 ? 72  SER D CA  1 
ATOM   4565 C C   . SER D 1 72  ? -62.32143 25.86517  24.06352  1.000 163.92674 ? 72  SER D C   1 
ATOM   4566 O O   . SER D 1 72  ? -62.58957 26.98771  23.62758  1.000 155.85786 ? 72  SER D O   1 
ATOM   4567 C CB  . SER D 1 72  ? -60.15211 24.71271  23.49898  1.000 141.99411 ? 72  SER D CB  1 
ATOM   4568 O OG  . SER D 1 72  ? -59.50529 25.96124  23.33523  1.000 146.46413 ? 72  SER D OG  1 
ATOM   4569 N N   . ASP D 1 73  ? -62.59146 25.48516  25.29564  1.000 203.24637 ? 73  ASP D N   1 
ATOM   4570 C CA  . ASP D 1 73  ? -62.91221 26.46797  26.31863  1.000 218.72660 ? 73  ASP D CA  1 
ATOM   4571 C C   . ASP D 1 73  ? -61.61628 27.03371  26.89553  1.000 222.30706 ? 73  ASP D C   1 
ATOM   4572 O O   . ASP D 1 73  ? -60.71172 26.26564  27.23956  1.000 220.85645 ? 73  ASP D O   1 
ATOM   4573 C CB  . ASP D 1 73  ? -63.81479 25.84590  27.39261  1.000 224.93631 ? 73  ASP D CB  1 
ATOM   4574 C CG  . ASP D 1 73  ? -63.06227 24.98209  28.38060  1.000 236.26150 ? 73  ASP D CG  1 
ATOM   4575 O OD1 . ASP D 1 73  ? -62.51143 25.53040  29.35214  1.000 235.02125 ? 73  ASP D OD1 1 
ATOM   4576 O OD2 . ASP D 1 73  ? -63.02403 23.74924  28.18363  1.000 248.03567 ? 73  ASP D OD2 1 
ATOM   4577 N N   . PRO D 1 74  ? -61.46384 28.36015  26.95810  1.000 201.81591 ? 74  PRO D N   1 
ATOM   4578 C CA  . PRO D 1 74  ? -60.22722 28.93039  27.52635  1.000 193.72947 ? 74  PRO D CA  1 
ATOM   4579 C C   . PRO D 1 74  ? -59.96792 28.52520  28.96771  1.000 206.91208 ? 74  PRO D C   1 
ATOM   4580 O O   . PRO D 1 74  ? -58.81635 28.59896  29.41562  1.000 191.71659 ? 74  PRO D O   1 
ATOM   4581 C CB  . PRO D 1 74  ? -60.43438 30.44837  27.40192  1.000 176.33404 ? 74  PRO D CB  1 
ATOM   4582 C CG  . PRO D 1 74  ? -61.63300 30.64416  26.53334  1.000 170.09010 ? 74  PRO D CG  1 
ATOM   4583 C CD  . PRO D 1 74  ? -62.43316 29.38590  26.53750  1.000 187.10526 ? 74  PRO D CD  1 
ATOM   4584 N N   . HIS D 1 75  ? -60.99492 28.09933  29.70650  1.000 239.79224 ? 75  HIS D N   1 
ATOM   4585 C CA  . HIS D 1 75  ? -60.78167 27.61014  31.06495  1.000 239.98371 ? 75  HIS D CA  1 
ATOM   4586 C C   . HIS D 1 75  ? -60.00307 26.29737  31.05664  1.000 238.28964 ? 75  HIS D C   1 
ATOM   4587 O O   . HIS D 1 75  ? -59.01266 26.14676  31.78198  1.000 236.28249 ? 75  HIS D O   1 
ATOM   4588 C CB  . HIS D 1 75  ? -62.12523 27.44550  31.78119  1.000 244.42820 ? 75  HIS D CB  1 
ATOM   4589 C CG  . HIS D 1 75  ? -63.14784 28.47235  31.39844  1.000 246.70186 ? 75  HIS D CG  1 
ATOM   4590 N ND1 . HIS D 1 75  ? -64.06975 28.26752  30.39404  1.000 248.30589 ? 75  HIS D ND1 1 
ATOM   4591 C CD2 . HIS D 1 75  ? -63.39645 29.71003  31.88912  1.000 245.57650 ? 75  HIS D CD2 1 
ATOM   4592 C CE1 . HIS D 1 75  ? -64.83979 29.33521  30.28065  1.000 249.20503 ? 75  HIS D CE1 1 
ATOM   4593 N NE2 . HIS D 1 75  ? -64.45226 30.22511  31.17649  1.000 239.66514 ? 75  HIS D NE2 1 
ATOM   4594 N N   . ASP D 1 76  ? -60.43426 25.33648  30.23785  1.000 222.63840 ? 76  ASP D N   1 
ATOM   4595 C CA  . ASP D 1 76  ? -59.80776 24.01932  30.14322  1.000 213.04988 ? 76  ASP D CA  1 
ATOM   4596 C C   . ASP D 1 76  ? -59.32677 23.80695  28.71271  1.000 205.60198 ? 76  ASP D C   1 
ATOM   4597 O O   . ASP D 1 76  ? -60.13308 23.55953  27.80912  1.000 198.70126 ? 76  ASP D O   1 
ATOM   4598 C CB  . ASP D 1 76  ? -60.78225 22.91697  30.55994  1.000 208.57198 ? 76  ASP D CB  1 
ATOM   4599 C CG  . ASP D 1 76  ? -60.10853 21.56292  30.70205  1.000 196.96097 ? 76  ASP D CG  1 
ATOM   4600 O OD1 . ASP D 1 76  ? -58.86458 21.50064  30.60596  1.000 194.68769 ? 76  ASP D OD1 1 
ATOM   4601 O OD2 . ASP D 1 76  ? -60.82391 20.55963  30.90976  1.000 172.07719 ? 76  ASP D OD2 1 
ATOM   4602 N N   . ASP D 1 77  ? -58.01464 23.88689  28.51487  1.000 205.56472 ? 77  ASP D N   1 
ATOM   4603 C CA  . ASP D 1 77  ? -57.39234 23.62519  27.22505  1.000 205.87244 ? 77  ASP D CA  1 
ATOM   4604 C C   . ASP D 1 77  ? -56.95062 22.17754  27.06471  1.000 206.87063 ? 77  ASP D C   1 
ATOM   4605 O O   . ASP D 1 77  ? -56.46184 21.80935  25.99114  1.000 199.68805 ? 77  ASP D O   1 
ATOM   4606 C CB  . ASP D 1 77  ? -56.19469 24.55649  27.01859  1.000 212.06416 ? 77  ASP D CB  1 
ATOM   4607 C CG  . ASP D 1 77  ? -56.59868 25.90751  26.46370  1.000 204.47988 ? 77  ASP D CG  1 
ATOM   4608 O OD1 . ASP D 1 77  ? -57.78055 26.28391  26.61578  1.000 202.52357 ? 77  ASP D OD1 1 
ATOM   4609 O OD2 . ASP D 1 77  ? -55.73546 26.59273  25.87560  1.000 200.85686 ? 77  ASP D OD2 1 
ATOM   4610 N N   . SER D 1 78  ? -57.11260 21.35057  28.10050  1.000 210.99478 ? 78  SER D N   1 
ATOM   4611 C CA  . SER D 1 78  ? -56.79758 19.93283  27.97994  1.000 210.58447 ? 78  SER D CA  1 
ATOM   4612 C C   . SER D 1 78  ? -57.77087 19.19520  27.07130  1.000 205.22151 ? 78  SER D C   1 
ATOM   4613 O O   . SER D 1 78  ? -57.45383 18.09111  26.61627  1.000 204.85373 ? 78  SER D O   1 
ATOM   4614 C CB  . SER D 1 78  ? -56.78503 19.27536  29.36192  1.000 209.60683 ? 78  SER D CB  1 
ATOM   4615 O OG  . SER D 1 78  ? -55.60458 19.59937  30.07552  1.000 214.75164 ? 78  SER D OG  1 
ATOM   4616 N N   . ASN D 1 79  ? -58.93979 19.76778  26.79641  1.000 198.16618 ? 79  ASN D N   1 
ATOM   4617 C CA  . ASN D 1 79  ? -59.89781 19.17584  25.87243  1.000 189.99276 ? 79  ASN D CA  1 
ATOM   4618 C C   . ASN D 1 79  ? -59.98401 20.04455  24.62473  1.000 182.81461 ? 79  ASN D C   1 
ATOM   4619 O O   . ASN D 1 79  ? -60.37179 21.21578  24.70498  1.000 177.74541 ? 79  ASN D O   1 
ATOM   4620 C CB  . ASN D 1 79  ? -61.27520 19.03829  26.52401  1.000 189.18698 ? 79  ASN D CB  1 
ATOM   4621 C CG  . ASN D 1 79  ? -61.27266 18.08699  27.70797  1.000 190.41586 ? 79  ASN D CG  1 
ATOM   4622 O OD1 . ASN D 1 79  ? -60.27409 17.42252  27.98434  1.000 189.24470 ? 79  ASN D OD1 1 
ATOM   4623 N ND2 . ASN D 1 79  ? -62.39590 18.01982  28.41552  1.000 180.17630 ? 79  ASN D ND2 1 
ATOM   4624 N N   . LYS D 1 80  ? -59.62265 19.47029  23.47875  1.000 172.41663 ? 80  LYS D N   1 
ATOM   4625 C CA  . LYS D 1 80  ? -59.65074 20.16929  22.20423  1.000 155.72067 ? 80  LYS D CA  1 
ATOM   4626 C C   . LYS D 1 80  ? -60.54037 19.41006  21.22976  1.000 144.00836 ? 80  LYS D C   1 
ATOM   4627 O O   . LYS D 1 80  ? -60.64135 18.18112  21.28582  1.000 148.90176 ? 80  LYS D O   1 
ATOM   4628 C CB  . LYS D 1 80  ? -58.24251 20.31922  21.62114  1.000 155.49277 ? 80  LYS D CB  1 
ATOM   4629 C CG  . LYS D 1 80  ? -57.33931 21.23489  22.42529  1.000 159.35475 ? 80  LYS D CG  1 
ATOM   4630 C CD  . LYS D 1 80  ? -55.95894 21.31746  21.80524  1.000 158.97518 ? 80  LYS D CD  1 
ATOM   4631 C CE  . LYS D 1 80  ? -55.05554 22.25048  22.59015  1.000 163.41664 ? 80  LYS D CE  1 
ATOM   4632 N NZ  . LYS D 1 80  ? -53.69135 22.31436  21.99705  1.000 166.29338 ? 80  LYS D NZ  1 
ATOM   4633 N N   . THR D 1 81  ? -61.17721 20.14880  20.32506  1.000 138.35090 ? 81  THR D N   1 
ATOM   4634 C CA  . THR D 1 81  ? -62.10477 19.57064  19.36007  1.000 131.96724 ? 81  THR D CA  1 
ATOM   4635 C C   . THR D 1 81  ? -61.82700 20.14939  17.98132  1.000 120.48869 ? 81  THR D C   1 
ATOM   4636 O O   . THR D 1 81  ? -61.92914 21.36407  17.78501  1.000 118.43605 ? 81  THR D O   1 
ATOM   4637 C CB  . THR D 1 81  ? -63.56014 19.81386  19.76440  1.000 126.47014 ? 81  THR D CB  1 
ATOM   4638 O OG1 . THR D 1 81  ? -63.85037 19.06797  20.95191  1.000 124.86151 ? 81  THR D OG1 1 
ATOM   4639 C CG2 . THR D 1 81  ? -64.49753 19.35079  18.65729  1.000 110.40605 ? 81  THR D CG2 1 
ATOM   4640 N N   . ASP D 1 82  ? -61.48468 19.28319  17.03279  1.000 120.07752 ? 82  ASP D N   1 
ATOM   4641 C CA  . ASP D 1 82  ? -61.27495 19.70588  15.65382  1.000 110.62348 ? 82  ASP D CA  1 
ATOM   4642 C C   . ASP D 1 82  ? -62.61935 20.07317  15.03274  1.000 116.45987 ? 82  ASP D C   1 
ATOM   4643 O O   . ASP D 1 82  ? -63.51603 19.22909  14.93594  1.000 118.67615 ? 82  ASP D O   1 
ATOM   4644 C CB  . ASP D 1 82  ? -60.59629 18.58658  14.86773  1.000 106.27532 ? 82  ASP D CB  1 
ATOM   4645 C CG  . ASP D 1 82  ? -59.95040 19.07611  13.58792  1.000 113.27043 ? 82  ASP D CG  1 
ATOM   4646 O OD1 . ASP D 1 82  ? -60.65295 19.71338  12.77758  1.000 118.54675 ? 82  ASP D OD1 1 
ATOM   4647 O OD2 . ASP D 1 82  ? -58.74154 18.82246  13.39172  1.000 100.39644 ? 82  ASP D OD2 1 
ATOM   4648 N N   . ILE D 1 83  ? -62.75681 21.32396  14.59906  1.000 114.19912 ? 83  ILE D N   1 
ATOM   4649 C CA  . ILE D 1 83  ? -64.00771 21.81954  14.03789  1.000 113.71531 ? 83  ILE D CA  1 
ATOM   4650 C C   . ILE D 1 83  ? -63.86212 22.16143  12.55754  1.000 115.16784 ? 83  ILE D C   1 
ATOM   4651 O O   . ILE D 1 83  ? -64.63662 22.96117  12.03457  1.000 119.85921 ? 83  ILE D O   1 
ATOM   4652 C CB  . ILE D 1 83  ? -64.52729 23.04655  14.80000  1.000 111.92889 ? 83  ILE D CB  1 
ATOM   4653 C CG1 . ILE D 1 83  ? -63.36826 23.96479  15.18018  1.000 107.81159 ? 83  ILE D CG1 1 
ATOM   4654 C CG2 . ILE D 1 83  ? -65.27689 22.60393  16.04067  1.000 103.77888 ? 83  ILE D CG2 1 
ATOM   4655 C CD1 . ILE D 1 83  ? -63.78712 25.14636  15.99250  1.000 112.29104 ? 83  ILE D CD1 1 
ATOM   4656 N N   . THR D 1 84  ? -62.87405 21.57916  11.87698  1.000 97.38759  ? 84  THR D N   1 
ATOM   4657 C CA  . THR D 1 84  ? -62.50456 22.05564  10.54658  1.000 112.26831 ? 84  THR D CA  1 
ATOM   4658 C C   . THR D 1 84  ? -63.66858 21.94067  9.56895   1.000 116.06064 ? 84  THR D C   1 
ATOM   4659 O O   . THR D 1 84  ? -63.91345 22.85708  8.77471   1.000 124.94483 ? 84  THR D O   1 
ATOM   4660 C CB  . THR D 1 84  ? -61.28936 21.29068  10.02262  1.000 106.56373 ? 84  THR D CB  1 
ATOM   4661 O OG1 . THR D 1 84  ? -60.31504 21.16653  11.06517  1.000 104.31190 ? 84  THR D OG1 1 
ATOM   4662 C CG2 . THR D 1 84  ? -60.66378 22.03391  8.84853   1.000 98.01773  ? 84  THR D CG2 1 
ATOM   4663 N N   . PHE D 1 85  ? -64.40024 20.82550  9.61487   1.000 119.27159 ? 85  PHE D N   1 
ATOM   4664 C CA  . PHE D 1 85  ? -65.50713 20.61366  8.68914   1.000 116.16959 ? 85  PHE D CA  1 
ATOM   4665 C C   . PHE D 1 85  ? -66.74884 21.42238  9.05640   1.000 113.56903 ? 85  PHE D C   1 
ATOM   4666 O O   . PHE D 1 85  ? -67.51976 21.79350  8.16407   1.000 112.23492 ? 85  PHE D O   1 
ATOM   4667 C CB  . PHE D 1 85  ? -65.85711 19.12547  8.64671   1.000 122.56936 ? 85  PHE D CB  1 
ATOM   4668 C CG  . PHE D 1 85  ? -65.07398 18.34437  7.63114   1.000 129.07939 ? 85  PHE D CG  1 
ATOM   4669 C CD1 . PHE D 1 85  ? -63.72826 18.08116  7.83079   1.000 128.14969 ? 85  PHE D CD1 1 
ATOM   4670 C CD2 . PHE D 1 85  ? -65.68454 17.85782  6.48723   1.000 141.56633 ? 85  PHE D CD2 1 
ATOM   4671 C CE1 . PHE D 1 85  ? -63.00270 17.35915  6.90158   1.000 133.03307 ? 85  PHE D CE1 1 
ATOM   4672 C CE2 . PHE D 1 85  ? -64.96501 17.13227  5.55498   1.000 142.72619 ? 85  PHE D CE2 1 
ATOM   4673 C CZ  . PHE D 1 85  ? -63.62208 16.88351  5.76274   1.000 136.12933 ? 85  PHE D CZ  1 
ATOM   4674 N N   . VAL D 1 86  ? -66.95790 21.72069  10.33802  1.000 104.20038 ? 86  VAL D N   1 
ATOM   4675 C CA  . VAL D 1 86  ? -68.18362 22.40065  10.74620  1.000 104.97609 ? 86  VAL D CA  1 
ATOM   4676 C C   . VAL D 1 86  ? -68.02523 23.92046  10.72011  1.000 121.22647 ? 86  VAL D C   1 
ATOM   4677 O O   . VAL D 1 86  ? -68.98708 24.63512  10.41298  1.000 120.99314 ? 86  VAL D O   1 
ATOM   4678 C CB  . VAL D 1 86  ? -68.63189 21.90998  12.13661  1.000 108.16922 ? 86  VAL D CB  1 
ATOM   4679 C CG1 . VAL D 1 86  ? -67.46414 21.88211  13.10085  1.000 101.18740 ? 86  VAL D CG1 1 
ATOM   4680 C CG2 . VAL D 1 86  ? -69.75977 22.77329  12.68838  1.000 108.25111 ? 86  VAL D CG2 1 
ATOM   4681 N N   . TYR D 1 87  ? -66.83248 24.42683  11.02914  1.000 107.39583 ? 87  TYR D N   1 
ATOM   4682 C CA  . TYR D 1 87  ? -66.57448 25.86149  11.01133  1.000 110.13911 ? 87  TYR D CA  1 
ATOM   4683 C C   . TYR D 1 87  ? -66.95491 26.45560  9.66180   1.000 126.01921 ? 87  TYR D C   1 
ATOM   4684 O O   . TYR D 1 87  ? -66.34724 26.13625  8.63466   1.000 123.16224 ? 87  TYR D O   1 
ATOM   4685 C CB  . TYR D 1 87  ? -65.10027 26.11846  11.32489  1.000 123.72405 ? 87  TYR D CB  1 
ATOM   4686 C CG  . TYR D 1 87  ? -64.77057 27.55860  11.62874  1.000 118.58023 ? 87  TYR D CG  1 
ATOM   4687 C CD1 . TYR D 1 87  ? -64.49927 28.45779  10.60964  1.000 115.36241 ? 87  TYR D CD1 1 
ATOM   4688 C CD2 . TYR D 1 87  ? -64.73821 28.02115  12.93632  1.000 116.10540 ? 87  TYR D CD2 1 
ATOM   4689 C CE1 . TYR D 1 87  ? -64.19717 29.77139  10.88471  1.000 113.38920 ? 87  TYR D CE1 1 
ATOM   4690 C CE2 . TYR D 1 87  ? -64.44063 29.33461  13.21805  1.000 110.97877 ? 87  TYR D CE2 1 
ATOM   4691 C CZ  . TYR D 1 87  ? -64.17052 30.20620  12.19089  1.000 114.47739 ? 87  TYR D CZ  1 
ATOM   4692 O OH  . TYR D 1 87  ? -63.87060 31.51865  12.47368  1.000 116.93185 ? 87  TYR D OH  1 
ATOM   4693 N N   . ASN D 1 88  ? -67.95154 27.33928  9.67281   1.000 127.78039 ? 88  ASN D N   1 
ATOM   4694 C CA  . ASN D 1 88  ? -68.58616 27.82502  8.44841   1.000 135.41848 ? 88  ASN D CA  1 
ATOM   4695 C C   . ASN D 1 88  ? -67.95469 29.16603  8.08911   1.000 128.08062 ? 88  ASN D C   1 
ATOM   4696 O O   . ASN D 1 88  ? -68.38036 30.22603  8.55043   1.000 130.64605 ? 88  ASN D O   1 
ATOM   4697 C CB  . ASN D 1 88  ? -70.09759 27.92686  8.63795   1.000 146.07259 ? 88  ASN D CB  1 
ATOM   4698 C CG  . ASN D 1 88  ? -70.77210 28.78768  7.58185   1.000 159.25790 ? 88  ASN D CG  1 
ATOM   4699 O OD1 . ASN D 1 88  ? -70.32833 28.85290  6.43351   1.000 157.58187 ? 88  ASN D OD1 1 
ATOM   4700 N ND2 . ASN D 1 88  ? -71.85825 29.44932  7.96825   1.000 156.44396 ? 88  ASN D ND2 1 
ATOM   4701 N N   . ALA D 1 89  ? -66.91701 29.10481  7.25970   1.000 129.97867 ? 89  ALA D N   1 
ATOM   4702 C CA  . ALA D 1 89  ? -66.23005 30.29323  6.78199   1.000 115.55766 ? 89  ALA D CA  1 
ATOM   4703 C C   . ALA D 1 89  ? -65.38392 29.91615  5.57856   1.000 89.34801  ? 89  ALA D C   1 
ATOM   4704 O O   . ALA D 1 89  ? -64.92454 28.77784  5.45648   1.000 105.39357 ? 89  ALA D O   1 
ATOM   4705 C CB  . ALA D 1 89  ? -65.35183 30.92224  7.86768   1.000 114.04373 ? 89  ALA D CB  1 
ATOM   4706 N N   . ASN D 1 90  ? -65.18472 30.88486  4.69532   1.000 95.65079  ? 90  ASN D N   1 
ATOM   4707 C CA  . ASN D 1 90  ? -64.31134 30.69398  3.55026   1.000 99.31435  ? 90  ASN D CA  1 
ATOM   4708 C C   . ASN D 1 90  ? -62.86296 30.86653  3.98102   1.000 92.08612  ? 90  ASN D C   1 
ATOM   4709 O O   . ASN D 1 90  ? -62.55074 31.69172  4.84215   1.000 93.58602  ? 90  ASN D O   1 
ATOM   4710 C CB  . ASN D 1 90  ? -64.65097 31.68451  2.43731   1.000 106.10781 ? 90  ASN D CB  1 
ATOM   4711 C CG  . ASN D 1 90  ? -65.89231 31.29158  1.67273   1.000 123.32995 ? 90  ASN D CG  1 
ATOM   4712 O OD1 . ASN D 1 90  ? -66.24087 31.91157  0.66866   1.000 134.59963 ? 90  ASN D OD1 1 
ATOM   4713 N ND2 . ASN D 1 90  ? -66.56592 30.24875  2.14055   1.000 132.62169 ? 90  ASN D ND2 1 
ATOM   4714 N N   . PHE D 1 91  ? -61.98097 30.06234  3.40217   1.000 83.06052  ? 91  PHE D N   1 
ATOM   4715 C CA  . PHE D 1 91  ? -60.56339 30.13243  3.71158   1.000 75.12698  ? 91  PHE D CA  1 
ATOM   4716 C C   . PHE D 1 91  ? -59.78836 30.22245  2.41046   1.000 73.30030  ? 91  PHE D C   1 
ATOM   4717 O O   . PHE D 1 91  ? -60.11177 29.54024  1.43382   1.000 80.39179  ? 91  PHE D O   1 
ATOM   4718 C CB  . PHE D 1 91  ? -60.09396 28.91483  4.51613   1.000 80.79534  ? 91  PHE D CB  1 
ATOM   4719 C CG  . PHE D 1 91  ? -60.39546 29.00384  5.98198   1.000 74.89581  ? 91  PHE D CG  1 
ATOM   4720 C CD1 . PHE D 1 91  ? -59.66470 29.84468  6.80532   1.000 84.77383  ? 91  PHE D CD1 1 
ATOM   4721 C CD2 . PHE D 1 91  ? -61.41815 28.25286  6.53577   1.000 84.13344  ? 91  PHE D CD2 1 
ATOM   4722 C CE1 . PHE D 1 91  ? -59.94540 29.93152  8.15887   1.000 82.92245  ? 91  PHE D CE1 1 
ATOM   4723 C CE2 . PHE D 1 91  ? -61.70473 28.33561  7.88465   1.000 97.49855  ? 91  PHE D CE2 1 
ATOM   4724 C CZ  . PHE D 1 91  ? -60.96587 29.17581  8.69896   1.000 89.77454  ? 91  PHE D CZ  1 
ATOM   4725 N N   . PHE D 1 92  ? -58.77606 31.07784  2.39837   1.000 75.31894  ? 92  PHE D N   1 
ATOM   4726 C CA  . PHE D 1 92  ? -57.88127 31.19361  1.26298   1.000 73.17851  ? 92  PHE D CA  1 
ATOM   4727 C C   . PHE D 1 92  ? -56.45606 31.20236  1.77980   1.000 67.45639  ? 92  PHE D C   1 
ATOM   4728 O O   . PHE D 1 92  ? -56.18044 31.69125  2.87822   1.000 73.24769  ? 92  PHE D O   1 
ATOM   4729 C CB  . PHE D 1 92  ? -58.15666 32.47389  0.45048   1.000 70.55390  ? 92  PHE D CB  1 
ATOM   4730 C CG  . PHE D 1 92  ? -59.58036 32.59668  -0.02586  1.000 74.31522  ? 92  PHE D CG  1 
ATOM   4731 C CD1 . PHE D 1 92  ? -59.98038 32.02284  -1.22016  1.000 80.94446  ? 92  PHE D CD1 1 
ATOM   4732 C CD2 . PHE D 1 92  ? -60.52018 33.27921  0.72826   1.000 80.09831  ? 92  PHE D CD2 1 
ATOM   4733 C CE1 . PHE D 1 92  ? -61.28844 32.13166  -1.65576  1.000 78.70562  ? 92  PHE D CE1 1 
ATOM   4734 C CE2 . PHE D 1 92  ? -61.83105 33.39015  0.29861   1.000 86.55273  ? 92  PHE D CE2 1 
ATOM   4735 C CZ  . PHE D 1 92  ? -62.21424 32.81641  -0.89510  1.000 85.21455  ? 92  PHE D CZ  1 
ATOM   4736 N N   . LEU D 1 93  ? -55.55015 30.65447  0.98256   1.000 62.07529  ? 93  LEU D N   1 
ATOM   4737 C CA  . LEU D 1 93  ? -54.13891 30.63780  1.32428   1.000 57.12083  ? 93  LEU D CA  1 
ATOM   4738 C C   . LEU D 1 93  ? -53.35489 31.31898  0.21706   1.000 61.43881  ? 93  LEU D C   1 
ATOM   4739 O O   . LEU D 1 93  ? -53.51107 30.98481  -0.96238  1.000 67.08156  ? 93  LEU D O   1 
ATOM   4740 C CB  . LEU D 1 93  ? -53.63859 29.20849  1.54848   1.000 62.46356  ? 93  LEU D CB  1 
ATOM   4741 C CG  . LEU D 1 93  ? -52.35080 29.06591  2.36415   1.000 67.36079  ? 93  LEU D CG  1 
ATOM   4742 C CD1 . LEU D 1 93  ? -52.50975 29.53415  3.80713   1.000 52.51375  ? 93  LEU D CD1 1 
ATOM   4743 C CD2 . LEU D 1 93  ? -51.86355 27.62269  2.30530   1.000 52.51890  ? 93  LEU D CD2 1 
ATOM   4744 N N   . PHE D 1 94  ? -52.51635 32.27052  0.60561   1.000 61.30944  ? 94  PHE D N   1 
ATOM   4745 C CA  . PHE D 1 94  ? -51.75688 33.09412  -0.31949  1.000 53.46745  ? 94  PHE D CA  1 
ATOM   4746 C C   . PHE D 1 94  ? -50.27616 32.80877  -0.13919  1.000 58.30684  ? 94  PHE D C   1 
ATOM   4747 O O   . PHE D 1 94  ? -49.77825 32.79080  0.99174   1.000 62.31607  ? 94  PHE D O   1 
ATOM   4748 C CB  . PHE D 1 94  ? -52.07042 34.58069  -0.09788  1.000 62.84320  ? 94  PHE D CB  1 
ATOM   4749 C CG  . PHE D 1 94  ? -51.30962 35.50844  -1.00339  1.000 64.66535  ? 94  PHE D CG  1 
ATOM   4750 C CD1 . PHE D 1 94  ? -51.32488 35.33272  -2.37606  1.000 62.68929  ? 94  PHE D CD1 1 
ATOM   4751 C CD2 . PHE D 1 94  ? -50.59720 36.57930  -0.47387  1.000 61.90262  ? 94  PHE D CD2 1 
ATOM   4752 C CE1 . PHE D 1 94  ? -50.61910 36.18751  -3.20614  1.000 65.92108  ? 94  PHE D CE1 1 
ATOM   4753 C CE2 . PHE D 1 94  ? -49.90181 37.44638  -1.29792  1.000 58.67627  ? 94  PHE D CE2 1 
ATOM   4754 C CZ  . PHE D 1 94  ? -49.90819 37.24631  -2.66617  1.000 63.65041  ? 94  PHE D CZ  1 
ATOM   4755 N N   . ALA D 1 95  ? -49.58234 32.57656  -1.24933  1.000 54.59102  ? 95  ALA D N   1 
ATOM   4756 C CA  . ALA D 1 95  ? -48.16776 32.23227  -1.23845  1.000 51.28732  ? 95  ALA D CA  1 
ATOM   4757 C C   . ALA D 1 95  ? -47.34682 33.44067  -1.68141  1.000 62.40345  ? 95  ALA D C   1 
ATOM   4758 O O   . ALA D 1 95  ? -47.64428 34.05731  -2.70911  1.000 60.12666  ? 95  ALA D O   1 
ATOM   4759 C CB  . ALA D 1 95  ? -47.88432 31.03963  -2.15232  1.000 57.20594  ? 95  ALA D CB  1 
ATOM   4760 N N   . THR D 1 96  ? -46.29631 33.74882  -0.93028  1.000 56.73565  ? 96  THR D N   1 
ATOM   4761 C CA  . THR D 1 96  ? -45.33553 34.78202  -1.28826  1.000 68.55725  ? 96  THR D CA  1 
ATOM   4762 C C   . THR D 1 96  ? -43.94292 34.17356  -1.29654  1.000 67.71091  ? 96  THR D C   1 
ATOM   4763 O O   . THR D 1 96  ? -43.66955 33.19515  -0.59402  1.000 62.70929  ? 96  THR D O   1 
ATOM   4764 C CB  . THR D 1 96  ? -45.35294 35.99435  -0.33356  1.000 60.25583  ? 96  THR D CB  1 
ATOM   4765 O OG1 . THR D 1 96  ? -45.31857 35.55486  1.03070   1.000 66.02285  ? 96  THR D OG1 1 
ATOM   4766 C CG2 . THR D 1 96  ? -46.59026 36.84696  -0.56804  1.000 52.39790  ? 96  THR D CG2 1 
ATOM   4767 N N   . LEU D 1 97  ? -43.07020 34.76200  -2.10698  1.000 68.07335  ? 97  LEU D N   1 
ATOM   4768 C CA  . LEU D 1 97  ? -41.69916 34.30146  -2.27171  1.000 63.88975  ? 97  LEU D CA  1 
ATOM   4769 C C   . LEU D 1 97  ? -40.76132 35.23489  -1.52002  1.000 67.86497  ? 97  LEU D C   1 
ATOM   4770 O O   . LEU D 1 97  ? -40.75925 36.44656  -1.76132  1.000 78.36666  ? 97  LEU D O   1 
ATOM   4771 C CB  . LEU D 1 97  ? -41.32770 34.27180  -3.75180  1.000 68.54857  ? 97  LEU D CB  1 
ATOM   4772 C CG  . LEU D 1 97  ? -40.16672 33.37078  -4.14387  1.000 78.68360  ? 97  LEU D CG  1 
ATOM   4773 C CD1 . LEU D 1 97  ? -40.51141 31.92076  -3.85667  1.000 63.31108  ? 97  LEU D CD1 1 
ATOM   4774 C CD2 . LEU D 1 97  ? -39.84785 33.58285  -5.60778  1.000 75.63776  ? 97  LEU D CD2 1 
ATOM   4775 N N   . GLU D 1 98  ? -39.96996 34.67279  -0.61617  1.000 70.86529  ? 98  GLU D N   1 
ATOM   4776 C CA  . GLU D 1 98  ? -39.04954 35.46405  0.19394   1.000 75.44825  ? 98  GLU D CA  1 
ATOM   4777 C C   . GLU D 1 98  ? -37.62491 34.98114  -0.00861  1.000 65.19569  ? 98  GLU D C   1 
ATOM   4778 O O   . GLU D 1 98  ? -37.31049 33.83022  0.34890   1.000 79.51574  ? 98  GLU D O   1 
ATOM   4779 C CB  . GLU D 1 98  ? -39.42920 35.37822  1.67207   1.000 89.12593  ? 98  GLU D CB  1 
ATOM   4780 C CG  . GLU D 1 98  ? -40.87916 35.72043  1.97517   1.000 91.95664  ? 98  GLU D CG  1 
ATOM   4781 C CD  . GLU D 1 98  ? -41.04210 36.34433  3.34702   1.000 117.45019 ? 98  GLU D CD  1 
ATOM   4782 O OE1 . GLU D 1 98  ? -40.61747 35.71451  4.34033   1.000 116.18594 ? 98  GLU D OE1 1 
ATOM   4783 O OE2 . GLU D 1 98  ? -41.59195 37.46371  3.43194   1.000 127.12693 ? 98  GLU D OE2 1 
ATOM   4784 N N   . PRO D 1 99  ? -36.73895 35.79803  -0.57831  1.000 81.09327  ? 99  PRO D N   1 
ATOM   4785 C CA  . PRO D 1 99  ? -35.34169 35.37699  -0.73075  1.000 84.70486  ? 99  PRO D CA  1 
ATOM   4786 C C   . PRO D 1 99  ? -34.70772 35.07248  0.61896   1.000 92.92364  ? 99  PRO D C   1 
ATOM   4787 O O   . PRO D 1 99  ? -34.91608 35.79220  1.59789   1.000 103.46521 ? 99  PRO D O   1 
ATOM   4788 C CB  . PRO D 1 99  ? -34.68057 36.58568  -1.40146  1.000 89.24435  ? 99  PRO D CB  1 
ATOM   4789 C CG  . PRO D 1 99  ? -35.80753 37.31633  -2.06638  1.000 87.01544  ? 99  PRO D CG  1 
ATOM   4790 C CD  . PRO D 1 99  ? -36.98249 37.13071  -1.15835  1.000 76.86959  ? 99  PRO D CD  1 
ATOM   4791 N N   . GLU D 1 100 ? -33.92920 33.98777  0.66745   1.000 94.28352  ? 100 GLU D N   1 
ATOM   4792 C CA  . GLU D 1 100 ? -33.17534 33.68861  1.88165   1.000 108.62596 ? 100 GLU D CA  1 
ATOM   4793 C C   . GLU D 1 100 ? -32.12491 34.75755  2.14426   1.000 120.14387 ? 100 GLU D C   1 
ATOM   4794 O O   . GLU D 1 100 ? -31.84701 35.09560  3.30075   1.000 122.23989 ? 100 GLU D O   1 
ATOM   4795 C CB  . GLU D 1 100 ? -32.53033 32.30721  1.78762   1.000 103.78529 ? 100 GLU D CB  1 
ATOM   4796 C CG  . GLU D 1 100 ? -33.33180 31.17474  2.43199   1.000 103.44979 ? 100 GLU D CG  1 
ATOM   4797 C CD  . GLU D 1 100 ? -33.56066 31.36805  3.92762   1.000 112.74623 ? 100 GLU D CD  1 
ATOM   4798 O OE1 . GLU D 1 100 ? -34.34306 32.26441  4.31025   1.000 113.04144 ? 100 GLU D OE1 1 
ATOM   4799 O OE2 . GLU D 1 100 ? -32.95605 30.61478  4.72523   1.000 106.46685 ? 100 GLU D OE2 1 
ATOM   4800 N N   . ARG D 1 101 ? -31.51358 35.28050  1.08312   1.000 121.33203 ? 101 ARG D N   1 
ATOM   4801 C CA  . ARG D 1 101 ? -30.61227 36.41471  1.19528   1.000 139.61135 ? 101 ARG D CA  1 
ATOM   4802 C C   . ARG D 1 101 ? -31.39917 37.67317  0.86070   1.000 147.52593 ? 101 ARG D C   1 
ATOM   4803 O O   . ARG D 1 101 ? -31.80409 37.84487  -0.30002  1.000 139.92960 ? 101 ARG D O   1 
ATOM   4804 C CB  . ARG D 1 101 ? -29.41776 36.26158  0.25173   1.000 153.61401 ? 101 ARG D CB  1 
ATOM   4805 C CG  . ARG D 1 101 ? -28.31132 35.31369  0.73162   1.000 159.64644 ? 101 ARG D CG  1 
ATOM   4806 C CD  . ARG D 1 101 ? -28.77631 33.86296  0.82957   1.000 155.88303 ? 101 ARG D CD  1 
ATOM   4807 N NE  . ARG D 1 101 ? -27.87232 32.93822  0.15499   1.000 157.80928 ? 101 ARG D NE  1 
ATOM   4808 C CZ  . ARG D 1 101 ? -28.05033 31.62502  0.09895   1.000 150.52804 ? 101 ARG D CZ  1 
ATOM   4809 N NH1 . ARG D 1 101 ? -29.08281 31.04188  0.68558   1.000 144.22464 ? 101 ARG D NH1 1 
ATOM   4810 N NH2 . ARG D 1 101 ? -27.16754 30.87762  -0.55739  1.000 145.24352 ? 101 ARG D NH2 1 
ATOM   4811 N N   . PRO D 1 102 ? -31.64446 38.57677  1.82257   1.000 156.15862 ? 102 PRO D N   1 
ATOM   4812 C CA  . PRO D 1 102 ? -32.43432 39.78620  1.53240   1.000 154.77186 ? 102 PRO D CA  1 
ATOM   4813 C C   . PRO D 1 102 ? -31.82511 40.68922  0.46645   1.000 164.09692 ? 102 PRO D C   1 
ATOM   4814 O O   . PRO D 1 102 ? -32.38065 41.74789  0.15268   1.000 159.41572 ? 102 PRO D O   1 
ATOM   4815 C CB  . PRO D 1 102 ? -32.49131 40.49052  2.89292   1.000 146.23815 ? 102 PRO D CB  1 
ATOM   4816 C CG  . PRO D 1 102 ? -32.38295 39.37399  3.88131   1.000 145.10183 ? 102 PRO D CG  1 
ATOM   4817 C CD  . PRO D 1 102 ? -31.41626 38.40177  3.26756   1.000 155.96075 ? 102 PRO D CD  1 
ATOM   4818 N N   . ILE D 1 103 ? -30.67623 40.28714  -0.07237  1.000 161.59360 ? 103 ILE D N   1 
ATOM   4819 C CA  . ILE D 1 103 ? -30.07546 40.89934  -1.25314  1.000 161.79448 ? 103 ILE D CA  1 
ATOM   4820 C C   . ILE D 1 103 ? -31.10093 41.11085  -2.36452  1.000 153.97803 ? 103 ILE D C   1 
ATOM   4821 O O   . ILE D 1 103 ? -31.58932 42.22337  -2.56946  1.000 136.72730 ? 103 ILE D O   1 
ATOM   4822 C CB  . ILE D 1 103 ? -28.89950 40.03989  -1.76210  1.000 157.02635 ? 103 ILE D CB  1 
ATOM   4823 C CG1 . ILE D 1 103 ? -27.99832 40.84786  -2.69653  1.000 155.62643 ? 103 ILE D CG1 1 
ATOM   4824 C CG2 . ILE D 1 103 ? -29.41507 38.78970  -2.46269  1.000 144.46922 ? 103 ILE D CG2 1 
ATOM   4825 C CD1 . ILE D 1 103 ? -26.75933 40.09781  -3.14297  1.000 144.13121 ? 103 ILE D CD1 1 
ATOM   4826 N N   . PRO D 1 115 ? -42.90504 40.92755  -10.51658 1.000 125.91099 ? 115 PRO D N   1 
ATOM   4827 C CA  . PRO D 1 115 ? -43.45509 39.58517  -10.30610 1.000 125.80244 ? 115 PRO D CA  1 
ATOM   4828 C C   . PRO D 1 115 ? -42.37087 38.50637  -10.31655 1.000 129.90084 ? 115 PRO D C   1 
ATOM   4829 O O   . PRO D 1 115 ? -42.13954 37.90648  -11.35824 1.000 129.23922 ? 115 PRO D O   1 
ATOM   4830 C CB  . PRO D 1 115 ? -44.40382 39.41604  -11.49296 1.000 121.96855 ? 115 PRO D CB  1 
ATOM   4831 C CG  . PRO D 1 115 ? -44.86883 40.79645  -11.77898 1.000 122.32576 ? 115 PRO D CG  1 
ATOM   4832 C CD  . PRO D 1 115 ? -43.66863 41.67770  -11.53048 1.000 135.49074 ? 115 PRO D CD  1 
ATOM   4833 N N   . VAL D 1 116 ? -41.72980 38.25880  -9.17272  1.000 108.71489 ? 116 VAL D N   1 
ATOM   4834 C CA  . VAL D 1 116 ? -40.71825 37.20636  -9.09358  1.000 87.36559  ? 116 VAL D CA  1 
ATOM   4835 C C   . VAL D 1 116 ? -41.36659 35.82569  -8.95582  1.000 86.35739  ? 116 VAL D C   1 
ATOM   4836 O O   . VAL D 1 116 ? -40.83949 34.83250  -9.47191  1.000 83.78200  ? 116 VAL D O   1 
ATOM   4837 C CB  . VAL D 1 116 ? -39.72871 37.50148  -7.94903  1.000 87.34275  ? 116 VAL D CB  1 
ATOM   4838 C CG1 . VAL D 1 116 ? -40.44834 37.59838  -6.61135  1.000 90.43441  ? 116 VAL D CG1 1 
ATOM   4839 C CG2 . VAL D 1 116 ? -38.62208 36.45853  -7.90275  1.000 94.86166  ? 116 VAL D CG2 1 
ATOM   4840 N N   . LEU D 1 117 ? -42.52205 35.74215  -8.30567  1.000 82.60057  ? 117 LEU D N   1 
ATOM   4841 C CA  . LEU D 1 117 ? -43.33440 34.53318  -8.28488  1.000 74.07208  ? 117 LEU D CA  1 
ATOM   4842 C C   . LEU D 1 117 ? -44.51649 34.70524  -9.22739  1.000 81.34568  ? 117 LEU D C   1 
ATOM   4843 O O   . LEU D 1 117 ? -45.22264 35.71682  -9.16945  1.000 85.21586  ? 117 LEU D O   1 
ATOM   4844 C CB  . LEU D 1 117 ? -43.83792 34.22856  -6.87550  1.000 65.75912  ? 117 LEU D CB  1 
ATOM   4845 C CG  . LEU D 1 117 ? -44.67457 32.94957  -6.77959  1.000 77.31184  ? 117 LEU D CG  1 
ATOM   4846 C CD1 . LEU D 1 117 ? -43.79494 31.71891  -6.89293  1.000 63.22406  ? 117 LEU D CD1 1 
ATOM   4847 C CD2 . LEU D 1 117 ? -45.48287 32.92179  -5.49435  1.000 74.15081  ? 117 LEU D CD2 1 
ATOM   4848 N N   . THR D 1 118 ? -44.72342 33.71661  -10.09405 1.000 76.98828  ? 118 THR D N   1 
ATOM   4849 C CA  . THR D 1 118 ? -45.73986 33.77887  -11.13153 1.000 82.95286  ? 118 THR D CA  1 
ATOM   4850 C C   . THR D 1 118 ? -46.63060 32.54597  -11.07231 1.000 81.12761  ? 118 THR D C   1 
ATOM   4851 O O   . THR D 1 118 ? -46.27823 31.52165  -10.48088 1.000 80.51380  ? 118 THR D O   1 
ATOM   4852 C CB  . THR D 1 118 ? -45.10627 33.90031  -12.51967 1.000 89.34277  ? 118 THR D CB  1 
ATOM   4853 O OG1 . THR D 1 118 ? -46.08451 33.60908  -13.52583 1.000 115.18096 ? 118 THR D OG1 1 
ATOM   4854 C CG2 . THR D 1 118 ? -43.95453 32.93659  -12.64682 1.000 80.28992  ? 118 THR D CG2 1 
ATOM   4855 N N   . GLY D 1 119 ? -47.80235 32.66781  -11.69304 1.000 77.72876  ? 119 GLY D N   1 
ATOM   4856 C CA  . GLY D 1 119 ? -48.78843 31.60771  -11.68355 1.000 79.44257  ? 119 GLY D CA  1 
ATOM   4857 C C   . GLY D 1 119 ? -50.01231 31.99392  -10.88205 1.000 83.59091  ? 119 GLY D C   1 
ATOM   4858 O O   . GLY D 1 119 ? -50.40476 33.16387  -10.86091 1.000 84.97613  ? 119 GLY D O   1 
ATOM   4859 N N   . VAL D 1 120 ? -50.62734 31.02547  -10.21667 1.000 80.76791  ? 120 VAL D N   1 
ATOM   4860 C CA  . VAL D 1 120 ? -51.77243 31.28636  -9.35457  1.000 67.72488  ? 120 VAL D CA  1 
ATOM   4861 C C   . VAL D 1 120 ? -51.29560 31.13591  -7.91309  1.000 69.95572  ? 120 VAL D C   1 
ATOM   4862 O O   . VAL D 1 120 ? -51.04464 30.01184  -7.45632  1.000 69.48484  ? 120 VAL D O   1 
ATOM   4863 C CB  . VAL D 1 120 ? -52.94991 30.35250  -9.65290  1.000 69.66677  ? 120 VAL D CB  1 
ATOM   4864 C CG1 . VAL D 1 120 ? -54.04723 30.56690  -8.62227  1.000 68.99863  ? 120 VAL D CG1 1 
ATOM   4865 C CG2 . VAL D 1 120 ? -53.47110 30.60234  -11.05078 1.000 67.96939  ? 120 VAL D CG2 1 
ATOM   4866 N N   . PRO D 1 121 ? -51.12577 32.23011  -7.17476  1.000 66.93434  ? 121 PRO D N   1 
ATOM   4867 C CA  . PRO D 1 121 ? -50.58885 32.15322  -5.81310  1.000 56.15434  ? 121 PRO D CA  1 
ATOM   4868 C C   . PRO D 1 121 ? -51.64034 32.00666  -4.72745  1.000 55.81069  ? 121 PRO D C   1 
ATOM   4869 O O   . PRO D 1 121 ? -51.28404 32.04736  -3.54385  1.000 57.33679  ? 121 PRO D O   1 
ATOM   4870 C CB  . PRO D 1 121 ? -49.86935 33.50062  -5.67975  1.000 63.94782  ? 121 PRO D CB  1 
ATOM   4871 C CG  . PRO D 1 121 ? -50.73642 34.43062  -6.46898  1.000 60.39603  ? 121 PRO D CG  1 
ATOM   4872 C CD  . PRO D 1 121 ? -51.24892 33.62382  -7.64095  1.000 62.14539  ? 121 PRO D CD  1 
ATOM   4873 N N   . VAL D 1 122 ? -52.91112 31.86742  -5.09159  1.000 63.60831  ? 122 VAL D N   1 
ATOM   4874 C CA  . VAL D 1 122 ? -54.00286 31.74028  -4.13451  1.000 65.78966  ? 122 VAL D CA  1 
ATOM   4875 C C   . VAL D 1 122 ? -54.64607 30.37321  -4.31041  1.000 71.72161  ? 122 VAL D C   1 
ATOM   4876 O O   . VAL D 1 122 ? -54.96103 29.96947  -5.43569  1.000 68.69767  ? 122 VAL D O   1 
ATOM   4877 C CB  . VAL D 1 122 ? -55.04939 32.85562  -4.30447  1.000 65.64201  ? 122 VAL D CB  1 
ATOM   4878 C CG1 . VAL D 1 122 ? -56.24380 32.59150  -3.40548  1.000 64.57373  ? 122 VAL D CG1 1 
ATOM   4879 C CG2 . VAL D 1 122 ? -54.43585 34.20102  -3.97665  1.000 64.74351  ? 122 VAL D CG2 1 
ATOM   4880 N N   . ALA D 1 123 ? -54.80576 29.65194  -3.20461  1.000 63.44278  ? 123 ALA D N   1 
ATOM   4881 C CA  . ALA D 1 123 ? -55.42725 28.33536  -3.19948  1.000 66.50492  ? 123 ALA D CA  1 
ATOM   4882 C C   . ALA D 1 123 ? -56.64594 28.35853  -2.29046  1.000 61.82351  ? 123 ALA D C   1 
ATOM   4883 O O   . ALA D 1 123 ? -56.58085 28.86914  -1.16757  1.000 73.26037  ? 123 ALA D O   1 
ATOM   4884 C CB  . ALA D 1 123 ? -54.44793 27.25069  -2.73687  1.000 61.73799  ? 123 ALA D CB  1 
ATOM   4885 N N   . GLY D 1 124 ? -57.75462 27.82096  -2.78683  1.000 72.15603  ? 124 GLY D N   1 
ATOM   4886 C CA  . GLY D 1 124 ? -58.91053 27.60398  -1.94650  1.000 76.68555  ? 124 GLY D CA  1 
ATOM   4887 C C   . GLY D 1 124 ? -58.80474 26.30412  -1.17574  1.000 71.53462  ? 124 GLY D C   1 
ATOM   4888 O O   . GLY D 1 124 ? -58.02545 25.41632  -1.51631  1.000 80.98853  ? 124 GLY D O   1 
ATOM   4889 N N   . VAL D 1 125 ? -59.60517 26.18994  -0.12133  1.000 78.77256  ? 125 VAL D N   1 
ATOM   4890 C CA  . VAL D 1 125 ? -59.51433 25.03076  0.75862   1.000 81.01086  ? 125 VAL D CA  1 
ATOM   4891 C C   . VAL D 1 125 ? -60.31639 23.88152  0.16360   1.000 88.50382  ? 125 VAL D C   1 
ATOM   4892 O O   . VAL D 1 125 ? -61.35555 24.07667  -0.48178  1.000 84.86314  ? 125 VAL D O   1 
ATOM   4893 C CB  . VAL D 1 125 ? -59.99161 25.38220  2.18510   1.000 82.30302  ? 125 VAL D CB  1 
ATOM   4894 C CG1 . VAL D 1 125 ? -61.49534 25.60873  2.21533   1.000 84.35202  ? 125 VAL D CG1 1 
ATOM   4895 C CG2 . VAL D 1 125 ? -59.59402 24.29603  3.16833   1.000 74.82895  ? 125 VAL D CG2 1 
ATOM   4896 N N   . ALA D 1 126 ? -59.82186 22.66669  0.38334   1.000 82.21966  ? 126 ALA D N   1 
ATOM   4897 C CA  . ALA D 1 126 ? -60.55663 21.43978  0.09735   1.000 80.68231  ? 126 ALA D CA  1 
ATOM   4898 C C   . ALA D 1 126 ? -60.56513 20.56784  1.34407   1.000 86.12692  ? 126 ALA D C   1 
ATOM   4899 O O   . ALA D 1 126 ? -59.50300 20.23087  1.87600   1.000 88.05488  ? 126 ALA D O   1 
ATOM   4900 C CB  . ALA D 1 126 ? -59.93702 20.68559  -1.08249  1.000 85.87334  ? 126 ALA D CB  1 
ATOM   4901 N N   . TYR D 1 127 ? -61.75835 20.20811  1.80515   1.000 87.84758  ? 127 TYR D N   1 
ATOM   4902 C CA  . TYR D 1 127 ? -61.92954 19.43633  3.02952   1.000 102.00854 ? 127 TYR D CA  1 
ATOM   4903 C C   . TYR D 1 127 ? -61.83426 17.95606  2.67756   1.000 104.10293 ? 127 TYR D C   1 
ATOM   4904 O O   . TYR D 1 127 ? -62.57141 17.47330  1.81646   1.000 108.13566 ? 127 TYR D O   1 
ATOM   4905 C CB  . TYR D 1 127 ? -63.26459 19.77492  3.69249   1.000 100.54855 ? 127 TYR D CB  1 
ATOM   4906 C CG  . TYR D 1 127 ? -63.34238 21.21649  4.14541   1.000 93.98375  ? 127 TYR D CG  1 
ATOM   4907 C CD1 . TYR D 1 127 ? -62.81407 21.60851  5.36971   1.000 92.48446  ? 127 TYR D CD1 1 
ATOM   4908 C CD2 . TYR D 1 127 ? -63.92441 22.18932  3.33946   1.000 92.75934  ? 127 TYR D CD2 1 
ATOM   4909 C CE1 . TYR D 1 127 ? -62.87461 22.92434  5.78704   1.000 88.08190  ? 127 TYR D CE1 1 
ATOM   4910 C CE2 . TYR D 1 127 ? -63.98517 23.51264  3.74998   1.000 88.90105  ? 127 TYR D CE2 1 
ATOM   4911 C CZ  . TYR D 1 127 ? -63.45946 23.87085  4.97410   1.000 86.88361  ? 127 TYR D CZ  1 
ATOM   4912 O OH  . TYR D 1 127 ? -63.51917 25.17968  5.39006   1.000 95.48230  ? 127 TYR D OH  1 
ATOM   4913 N N   . LEU D 1 128 ? -60.93389 17.24220  3.34707   1.000 105.09980 ? 128 LEU D N   1 
ATOM   4914 C CA  . LEU D 1 128 ? -60.65993 15.84726  3.02886   1.000 111.76372 ? 128 LEU D CA  1 
ATOM   4915 C C   . LEU D 1 128 ? -60.51455 15.03482  4.30682   1.000 109.47344 ? 128 LEU D C   1 
ATOM   4916 O O   . LEU D 1 128 ? -60.22395 15.57541  5.38269   1.000 103.97902 ? 128 LEU D O   1 
ATOM   4917 C CB  . LEU D 1 128 ? -59.38658 15.70512  2.18291   1.000 105.86786 ? 128 LEU D CB  1 
ATOM   4918 C CG  . LEU D 1 128 ? -59.40811 16.27784  0.76628   1.000 91.59573  ? 128 LEU D CG  1 
ATOM   4919 C CD1 . LEU D 1 128 ? -58.04834 16.10366  0.11231   1.000 89.51447  ? 128 LEU D CD1 1 
ATOM   4920 C CD2 . LEU D 1 128 ? -60.49815 15.63756  -0.06949  1.000 96.78053  ? 128 LEU D CD2 1 
ATOM   4921 N N   . ASP D 1 129 ? -60.72455 13.72169  4.18777   1.000 121.81751 ? 129 ASP D N   1 
ATOM   4922 C CA  . ASP D 1 129 ? -60.61279 12.83697  5.33607   1.000 119.63910 ? 129 ASP D CA  1 
ATOM   4923 C C   . ASP D 1 129 ? -59.28641 12.08879  5.39909   1.000 113.46215 ? 129 ASP D C   1 
ATOM   4924 O O   . ASP D 1 129 ? -58.90306 11.64846  6.48613   1.000 122.07756 ? 129 ASP D O   1 
ATOM   4925 C CB  . ASP D 1 129 ? -61.75163 11.80995  5.32073   1.000 126.70843 ? 129 ASP D CB  1 
ATOM   4926 C CG  . ASP D 1 129 ? -63.09940 12.42115  5.01094   1.000 138.69823 ? 129 ASP D CG  1 
ATOM   4927 O OD1 . ASP D 1 129 ? -63.27297 13.64017  5.24390   1.000 141.42597 ? 129 ASP D OD1 1 
ATOM   4928 O OD2 . ASP D 1 129 ? -63.98685 11.69465  4.51415   1.000 156.40188 ? 129 ASP D OD2 1 
ATOM   4929 N N   . LYS D 1 130 ? -58.60162 11.92890  4.27054   1.000 105.46571 ? 130 LYS D N   1 
ATOM   4930 C CA  . LYS D 1 130 ? -57.31894 11.23389  4.20066   1.000 113.14090 ? 130 LYS D CA  1 
ATOM   4931 C C   . LYS D 1 130 ? -56.24960 12.12599  3.57497   1.000 117.49452 ? 130 LYS D C   1 
ATOM   4932 O O   . LYS D 1 130 ? -56.53121 12.82203  2.58621   1.000 104.80785 ? 130 LYS D O   1 
ATOM   4933 C CB  . LYS D 1 130 ? -57.44341 9.92907   3.38636   1.000 117.03795 ? 130 LYS D CB  1 
ATOM   4934 C CG  . LYS D 1 130 ? -58.82934 9.30227   3.51543   1.000 120.19139 ? 130 LYS D CG  1 
ATOM   4935 C CD  . LYS D 1 130 ? -58.81554 8.01698   4.33555   1.000 121.39357 ? 130 LYS D CD  1 
ATOM   4936 C CE  . LYS D 1 130 ? -60.07421 7.18015   4.11375   1.000 141.17057 ? 130 LYS D CE  1 
ATOM   4937 N NZ  . LYS D 1 130 ? -61.20726 7.70439   4.94085   1.000 155.36861 ? 130 LYS D NZ  1 
ATOM   4938 N N   . PRO D 1 131 ? -55.01852 12.11854  4.09623   1.000 112.61646 ? 131 PRO D N   1 
ATOM   4939 C CA  . PRO D 1 131 ? -54.48635 11.26871  5.17924   1.000 105.69769 ? 131 PRO D CA  1 
ATOM   4940 C C   . PRO D 1 131 ? -54.98093 11.66936  6.57272   1.000 114.40500 ? 131 PRO D C   1 
ATOM   4941 O O   . PRO D 1 131 ? -54.85763 10.91388  7.52999   1.000 123.72605 ? 131 PRO D O   1 
ATOM   4942 C CB  . PRO D 1 131 ? -52.97681 11.46983  5.04561   1.000 103.13592 ? 131 PRO D CB  1 
ATOM   4943 C CG  . PRO D 1 131 ? -52.85034 12.87833  4.55844   1.000 103.16338 ? 131 PRO D CG  1 
ATOM   4944 C CD  . PRO D 1 131 ? -53.99855 13.05630  3.59778   1.000 108.82063 ? 131 PRO D CD  1 
ATOM   4945 N N   . ASN D 1 132 ? -55.54232 12.86638  6.68454   1.000 113.78940 ? 132 ASN D N   1 
ATOM   4946 C CA  . ASN D 1 132 ? -56.10092 13.35264  7.93244   1.000 114.65636 ? 132 ASN D CA  1 
ATOM   4947 C C   . ASN D 1 132 ? -57.37639 14.12174  7.63433   1.000 109.97618 ? 132 ASN D C   1 
ATOM   4948 O O   . ASN D 1 132 ? -57.57306 14.63671  6.53501   1.000 108.13522 ? 132 ASN D O   1 
ATOM   4949 C CB  . ASN D 1 132 ? -55.10998 14.25435  8.68438   1.000 106.88979 ? 132 ASN D CB  1 
ATOM   4950 C CG  . ASN D 1 132 ? -53.85378 13.51759  9.11019   1.000 116.02055 ? 132 ASN D CG  1 
ATOM   4951 O OD1 . ASN D 1 132 ? -53.92140 12.44806  9.72034   1.000 118.10031 ? 132 ASN D OD1 1 
ATOM   4952 N ND2 . ASN D 1 132 ? -52.69755 14.08882  8.79118   1.000 102.94533 ? 132 ASN D ND2 1 
ATOM   4953 N N   . ARG D 1 133 ? -58.24777 14.19183  8.63556   1.000 116.28020 ? 133 ARG D N   1 
ATOM   4954 C CA  . ARG D 1 133 ? -59.48541 14.95782  8.52172   1.000 121.50165 ? 133 ARG D CA  1 
ATOM   4955 C C   . ARG D 1 133 ? -59.11736 16.41998  8.72231   1.000 117.07635 ? 133 ARG D C   1 
ATOM   4956 O O   . ARG D 1 133 ? -58.93105 16.88001  9.85193   1.000 119.11788 ? 133 ARG D O   1 
ATOM   4957 C CB  . ARG D 1 133 ? -60.51047 14.50066  9.55129   1.000 125.71949 ? 133 ARG D CB  1 
ATOM   4958 C CG  . ARG D 1 133 ? -60.80114 13.01157  9.53549   1.000 153.83969 ? 133 ARG D CG  1 
ATOM   4959 C CD  . ARG D 1 133 ? -61.83353 12.66298  10.59554  1.000 159.43085 ? 133 ARG D CD  1 
ATOM   4960 N NE  . ARG D 1 133 ? -62.92160 13.63390  10.63324  1.000 166.42093 ? 133 ARG D NE  1 
ATOM   4961 C CZ  . ARG D 1 133 ? -63.90350 13.69711  9.74391   1.000 167.77435 ? 133 ARG D CZ  1 
ATOM   4962 N NH1 . ARG D 1 133 ? -63.97821 12.84534  8.73450   1.000 163.99169 ? 133 ARG D NH1 1 
ATOM   4963 N NH2 . ARG D 1 133 ? -64.83490 14.63845  9.87069   1.000 167.55652 ? 133 ARG D NH2 1 
ATOM   4964 N N   . ALA D 1 134 ? -58.99862 17.15475  7.61933   1.000 98.36727  ? 134 ALA D N   1 
ATOM   4965 C CA  . ALA D 1 134 ? -58.59019 18.55232  7.68422   1.000 100.93786 ? 134 ALA D CA  1 
ATOM   4966 C C   . ALA D 1 134 ? -58.85914 19.23176  6.34875   1.000 90.92964  ? 134 ALA D C   1 
ATOM   4967 O O   . ALA D 1 134 ? -59.30107 18.60572  5.38097   1.000 97.34820  ? 134 ALA D O   1 
ATOM   4968 C CB  . ALA D 1 134 ? -57.10443 18.64651  8.01770   1.000 94.57033  ? 134 ALA D CB  1 
ATOM   4969 N N   . GLY D 1 135 ? -58.58158 20.53332  6.30957   1.000 95.79231  ? 135 GLY D N   1 
ATOM   4970 C CA  . GLY D 1 135 ? -58.59955 21.27245  5.06810   1.000 79.03830  ? 135 GLY D CA  1 
ATOM   4971 C C   . GLY D 1 135 ? -57.22802 21.23263  4.42270   1.000 79.52881  ? 135 GLY D C   1 
ATOM   4972 O O   . GLY D 1 135 ? -56.20608 21.14738  5.09825   1.000 89.10019  ? 135 GLY D O   1 
ATOM   4973 N N   . TYR D 1 136 ? -57.21161 21.29925  3.09747   1.000 84.93950  ? 136 TYR D N   1 
ATOM   4974 C CA  . TYR D 1 136 ? -55.98145 21.16425  2.33200   1.000 84.75543  ? 136 TYR D CA  1 
ATOM   4975 C C   . TYR D 1 136 ? -55.90077 22.23533  1.25693   1.000 78.98876  ? 136 TYR D C   1 
ATOM   4976 O O   . TYR D 1 136 ? -56.89846 22.54827  0.59846   1.000 77.09268  ? 136 TYR D O   1 
ATOM   4977 C CB  . TYR D 1 136 ? -55.87755 19.76778  1.70863   1.000 79.91452  ? 136 TYR D CB  1 
ATOM   4978 C CG  . TYR D 1 136 ? -55.66024 18.66295  2.71757   1.000 87.97026  ? 136 TYR D CG  1 
ATOM   4979 C CD1 . TYR D 1 136 ? -54.38258 18.36908  3.18257   1.000 74.20230  ? 136 TYR D CD1 1 
ATOM   4980 C CD2 . TYR D 1 136 ? -56.72863 17.93966  3.23261   1.000 93.42249  ? 136 TYR D CD2 1 
ATOM   4981 C CE1 . TYR D 1 136 ? -54.17213 17.37313  4.10932   1.000 92.61406  ? 136 TYR D CE1 1 
ATOM   4982 C CE2 . TYR D 1 136 ? -56.52797 16.93838  4.16497   1.000 93.87053  ? 136 TYR D CE2 1 
ATOM   4983 C CZ  . TYR D 1 136 ? -55.24763 16.66106  4.60009   1.000 99.97459  ? 136 TYR D CZ  1 
ATOM   4984 O OH  . TYR D 1 136 ? -55.03342 15.66774  5.52592   1.000 95.88549  ? 136 TYR D OH  1 
ATOM   4985 N N   . PHE D 1 137 ? -54.70599 22.79226  1.08142   1.000 67.08311  ? 137 PHE D N   1 
ATOM   4986 C CA  . PHE D 1 137 ? -54.43627 23.73662  0.00792   1.000 78.06785  ? 137 PHE D CA  1 
ATOM   4987 C C   . PHE D 1 137 ? -53.35783 23.17611  -0.90556  1.000 76.51333  ? 137 PHE D C   1 
ATOM   4988 O O   . PHE D 1 137 ? -52.29645 22.75272  -0.43537  1.000 78.05439  ? 137 PHE D O   1 
ATOM   4989 C CB  . PHE D 1 137 ? -53.99809 25.10483  0.54993   1.000 57.96049  ? 137 PHE D CB  1 
ATOM   4990 C CG  . PHE D 1 137 ? -54.95028 25.70604  1.55010   1.000 72.28762  ? 137 PHE D CG  1 
ATOM   4991 C CD1 . PHE D 1 137 ? -54.82634 25.43672  2.90301   1.000 72.86253  ? 137 PHE D CD1 1 
ATOM   4992 C CD2 . PHE D 1 137 ? -55.97838 26.53589  1.12977   1.000 70.12358  ? 137 PHE D CD2 1 
ATOM   4993 C CE1 . PHE D 1 137 ? -55.70227 25.99391  3.81905   1.000 77.18913  ? 137 PHE D CE1 1 
ATOM   4994 C CE2 . PHE D 1 137 ? -56.85812 27.09260  2.03764   1.000 68.95530  ? 137 PHE D CE2 1 
ATOM   4995 C CZ  . PHE D 1 137 ? -56.72056 26.82272  3.38458   1.000 72.92998  ? 137 PHE D CZ  1 
ATOM   4996 N N   . ILE D 1 138 ? -53.64204 23.17100  -2.20430  1.000 75.73523  ? 138 ILE D N   1 
ATOM   4997 C CA  . ILE D 1 138 ? -52.71967 22.72169  -3.23993  1.000 75.55688  ? 138 ILE D CA  1 
ATOM   4998 C C   . ILE D 1 138 ? -52.23876 23.94562  -4.00538  1.000 65.27549  ? 138 ILE D C   1 
ATOM   4999 O O   . ILE D 1 138 ? -53.01907 24.86876  -4.26894  1.000 79.72539  ? 138 ILE D O   1 
ATOM   5000 C CB  . ILE D 1 138 ? -53.38242 21.67993  -4.17173  1.000 71.87157  ? 138 ILE D CB  1 
ATOM   5001 C CG1 . ILE D 1 138 ? -52.34675 20.74930  -4.81311  1.000 84.51763  ? 138 ILE D CG1 1 
ATOM   5002 C CG2 . ILE D 1 138 ? -54.28959 22.32867  -5.21413  1.000 94.79863  ? 138 ILE D CG2 1 
ATOM   5003 C CD1 . ILE D 1 138 ? -51.37194 20.16766  -3.86700  1.000 84.05037  ? 138 ILE D CD1 1 
ATOM   5004 N N   . PHE D 1 139 ? -50.95471 23.95142  -4.36763  1.000 57.81275  ? 139 PHE D N   1 
ATOM   5005 C CA  . PHE D 1 139 ? -50.36787 24.99468  -5.20935  1.000 65.44917  ? 139 PHE D CA  1 
ATOM   5006 C C   . PHE D 1 139 ? -49.68283 24.33677  -6.39640  1.000 62.75150  ? 139 PHE D C   1 
ATOM   5007 O O   . PHE D 1 139 ? -48.45743 24.14528  -6.39973  1.000 64.50358  ? 139 PHE D O   1 
ATOM   5008 C CB  . PHE D 1 139 ? -49.38493 25.87087  -4.43041  1.000 65.91776  ? 139 PHE D CB  1 
ATOM   5009 C CG  . PHE D 1 139 ? -50.03692 26.74478  -3.40393  1.000 60.08547  ? 139 PHE D CG  1 
ATOM   5010 C CD1 . PHE D 1 139 ? -50.24289 26.28880  -2.11369  1.000 59.32188  ? 139 PHE D CD1 1 
ATOM   5011 C CD2 . PHE D 1 139 ? -50.46112 28.01811  -3.73533  1.000 63.27745  ? 139 PHE D CD2 1 
ATOM   5012 C CE1 . PHE D 1 139 ? -50.84863 27.09146  -1.16946  1.000 65.50872  ? 139 PHE D CE1 1 
ATOM   5013 C CE2 . PHE D 1 139 ? -51.06405 28.82405  -2.80029  1.000 52.84752  ? 139 PHE D CE2 1 
ATOM   5014 C CZ  . PHE D 1 139 ? -51.25819 28.36134  -1.51254  1.000 65.18180  ? 139 PHE D CZ  1 
ATOM   5015 N N   . PRO D 1 140 ? -50.44189 23.99242  -7.43873  1.000 58.64369  ? 140 PRO D N   1 
ATOM   5016 C CA  . PRO D 1 140 ? -49.84923 23.28899  -8.57863  1.000 71.17856  ? 140 PRO D CA  1 
ATOM   5017 C C   . PRO D 1 140 ? -49.30339 24.20366  -9.66159  1.000 84.56852  ? 140 PRO D C   1 
ATOM   5018 O O   . PRO D 1 140 ? -48.69018 23.70397  -10.61440 1.000 92.40490  ? 140 PRO D O   1 
ATOM   5019 C CB  . PRO D 1 140 ? -51.03121 22.46165  -9.10195  1.000 61.86387  ? 140 PRO D CB  1 
ATOM   5020 C CG  . PRO D 1 140 ? -52.22694 23.29644  -8.79035  1.000 61.80609  ? 140 PRO D CG  1 
ATOM   5021 C CD  . PRO D 1 140 ? -51.91587 24.01273  -7.49882  1.000 59.79474  ? 140 PRO D CD  1 
ATOM   5022 N N   . ASP D 1 141 ? -49.49974 25.51337  -9.55130  1.000 83.25981  ? 141 ASP D N   1 
ATOM   5023 C CA  . ASP D 1 141 ? -49.21616 26.43428  -10.64398 1.000 76.82706  ? 141 ASP D CA  1 
ATOM   5024 C C   . ASP D 1 141 ? -48.31796 27.56672  -10.14268 1.000 80.57218  ? 141 ASP D C   1 
ATOM   5025 O O   . ASP D 1 141 ? -48.60777 28.75258  -10.30950 1.000 85.42674  ? 141 ASP D O   1 
ATOM   5026 C CB  . ASP D 1 141 ? -50.51706 26.96512  -11.24001 1.000 79.49297  ? 141 ASP D CB  1 
ATOM   5027 C CG  . ASP D 1 141 ? -50.31092 27.69395  -12.55961 1.000 103.20570 ? 141 ASP D CG  1 
ATOM   5028 O OD1 . ASP D 1 141 ? -49.20804 28.22148  -12.80534 1.000 109.83080 ? 141 ASP D OD1 1 
ATOM   5029 O OD2 . ASP D 1 141 ? -51.27284 27.75283  -13.35499 1.000 123.38509 ? 141 ASP D OD2 1 
ATOM   5030 N N   . LEU D 1 142 ? -47.22667 27.21371  -9.47338  1.000 73.99203  ? 142 LEU D N   1 
ATOM   5031 C CA  . LEU D 1 142 ? -46.27316 28.19377  -8.97767  1.000 70.15739  ? 142 LEU D CA  1 
ATOM   5032 C C   . LEU D 1 142 ? -44.99945 28.11541  -9.80608  1.000 78.02842  ? 142 LEU D C   1 
ATOM   5033 O O   . LEU D 1 142 ? -44.51100 27.02223  -10.10290 1.000 94.55534  ? 142 LEU D O   1 
ATOM   5034 C CB  . LEU D 1 142 ? -45.94207 27.93856  -7.50729  1.000 67.44932  ? 142 LEU D CB  1 
ATOM   5035 C CG  . LEU D 1 142 ? -47.04384 28.20018  -6.48818  1.000 57.53280  ? 142 LEU D CG  1 
ATOM   5036 C CD1 . LEU D 1 142 ? -46.46667 28.17564  -5.08750  1.000 70.18613  ? 142 LEU D CD1 1 
ATOM   5037 C CD2 . LEU D 1 142 ? -47.71189 29.53954  -6.75956  1.000 78.34757  ? 142 LEU D CD2 1 
ATOM   5038 N N   . SER D 1 143 ? -44.46145 29.27243  -10.17798 1.000 80.38654  ? 143 SER D N   1 
ATOM   5039 C CA  . SER D 1 143 ? -43.21706 29.32498  -10.92708 1.000 73.34834  ? 143 SER D CA  1 
ATOM   5040 C C   . SER D 1 143 ? -42.37522 30.48713  -10.42517 1.000 71.83456  ? 143 SER D C   1 
ATOM   5041 O O   . SER D 1 143 ? -42.90309 31.49593  -9.95003  1.000 76.15367  ? 143 SER D O   1 
ATOM   5042 C CB  . SER D 1 143 ? -43.47035 29.46072  -12.43085 1.000 83.30092  ? 143 SER D CB  1 
ATOM   5043 O OG  . SER D 1 143 ? -44.53737 28.62587  -12.84129 1.000 101.87337 ? 143 SER D OG  1 
ATOM   5044 N N   . VAL D 1 144 ? -41.05951 30.33487  -10.54047 1.000 74.91557  ? 144 VAL D N   1 
ATOM   5045 C CA  . VAL D 1 144 ? -40.09593 31.32797  -10.08560 1.000 58.84372  ? 144 VAL D CA  1 
ATOM   5046 C C   . VAL D 1 144 ? -39.27745 31.77644  -11.28648 1.000 77.01568  ? 144 VAL D C   1 
ATOM   5047 O O   . VAL D 1 144 ? -38.81306 30.94128  -12.07077 1.000 78.76803  ? 144 VAL D O   1 
ATOM   5048 C CB  . VAL D 1 144 ? -39.19300 30.76843  -8.97339  1.000 68.08721  ? 144 VAL D CB  1 
ATOM   5049 C CG1 . VAL D 1 144 ? -38.33934 31.87138  -8.37602  1.000 63.28214  ? 144 VAL D CG1 1 
ATOM   5050 C CG2 . VAL D 1 144 ? -40.04991 30.10310  -7.89897  1.000 60.17628  ? 144 VAL D CG2 1 
ATOM   5051 N N   . ARG D 1 145 ? -39.09768 33.09187  -11.43013 1.000 75.02905  ? 145 ARG D N   1 
ATOM   5052 C CA  . ARG D 1 145 ? -38.46095 33.61124  -12.63758 1.000 77.07036  ? 145 ARG D CA  1 
ATOM   5053 C C   . ARG D 1 145 ? -36.94207 33.56079  -12.56357 1.000 75.22606  ? 145 ARG D C   1 
ATOM   5054 O O   . ARG D 1 145 ? -36.28446 33.25864  -13.56541 1.000 73.89494  ? 145 ARG D O   1 
ATOM   5055 C CB  . ARG D 1 145 ? -38.91625 35.04104  -12.93835 1.000 94.56051  ? 145 ARG D CB  1 
ATOM   5056 C CG  . ARG D 1 145 ? -40.31894 35.14840  -13.51035 1.000 102.16224 ? 145 ARG D CG  1 
ATOM   5057 C CD  . ARG D 1 145 ? -40.75143 36.60426  -13.62837 1.000 109.49023 ? 145 ARG D CD  1 
ATOM   5058 N NE  . ARG D 1 145 ? -41.51016 36.93594  -14.83505 1.000 118.57097 ? 145 ARG D NE  1 
ATOM   5059 C CZ  . ARG D 1 145 ? -42.57353 36.28864  -15.30008 1.000 115.59056 ? 145 ARG D CZ  1 
ATOM   5060 N NH1 . ARG D 1 145 ? -43.07343 35.23225  -14.68371 1.000 118.07361 ? 145 ARG D NH1 1 
ATOM   5061 N NH2 . ARG D 1 145 ? -43.15302 36.71558  -16.41869 1.000 131.84787 ? 145 ARG D NH2 1 
ATOM   5062 N N   . ASN D 1 146 ? -36.36979 33.82797  -11.39465 1.000 71.92416  ? 146 ASN D N   1 
ATOM   5063 C CA  . ASN D 1 146 ? -34.93300 33.98434  -11.25223 1.000 74.52889  ? 146 ASN D CA  1 
ATOM   5064 C C   . ASN D 1 146 ? -34.37209 32.96150  -10.27668 1.000 74.64249  ? 146 ASN D C   1 
ATOM   5065 O O   . ASN D 1 146 ? -35.04159 32.55033  -9.32532  1.000 78.36297  ? 146 ASN D O   1 
ATOM   5066 C CB  . ASN D 1 146 ? -34.58437 35.39204  -10.74797 1.000 85.43751  ? 146 ASN D CB  1 
ATOM   5067 C CG  . ASN D 1 146 ? -35.23549 36.49133  -11.56655 1.000 85.31489  ? 146 ASN D CG  1 
ATOM   5068 O OD1 . ASN D 1 146 ? -35.34393 36.40051  -12.79056 1.000 79.75306  ? 146 ASN D OD1 1 
ATOM   5069 N ND2 . ASN D 1 146 ? -35.68204 37.53852  -10.88496 1.000 86.92642  ? 146 ASN D ND2 1 
ATOM   5070 N N   . GLU D 1 147 ? -33.12763 32.56192  -10.52480 1.000 81.23609  ? 147 GLU D N   1 
ATOM   5071 C CA  . GLU D 1 147 ? -32.48123 31.56140  -9.69606  1.000 82.07500  ? 147 GLU D CA  1 
ATOM   5072 C C   . GLU D 1 147 ? -32.20162 32.12689  -8.30853  1.000 78.28063  ? 147 GLU D C   1 
ATOM   5073 O O   . GLU D 1 147 ? -32.19554 33.34066  -8.08892  1.000 90.39331  ? 147 GLU D O   1 
ATOM   5074 C CB  . GLU D 1 147 ? -31.17648 31.08109  -10.33394 1.000 80.84658  ? 147 GLU D CB  1 
ATOM   5075 C CG  . GLU D 1 147 ? -30.40813 32.13970  -11.10030 1.000 98.07579  ? 147 GLU D CG  1 
ATOM   5076 C CD  . GLU D 1 147 ? -29.22442 31.55704  -11.84964 1.000 121.04536 ? 147 GLU D CD  1 
ATOM   5077 O OE1 . GLU D 1 147 ? -28.65108 30.55446  -11.36871 1.000 111.78573 ? 147 GLU D OE1 1 
ATOM   5078 O OE2 . GLU D 1 147 ? -28.85516 32.11292  -12.90726 1.000 118.68619 ? 147 GLU D OE2 1 
ATOM   5079 N N   . GLY D 1 148 ? -31.98066 31.22248  -7.36172  1.000 80.07701  ? 148 GLY D N   1 
ATOM   5080 C CA  . GLY D 1 148 ? -31.59727 31.62010  -6.02495  1.000 72.83219  ? 148 GLY D CA  1 
ATOM   5081 C C   . GLY D 1 148 ? -32.21510 30.74004  -4.96252  1.000 76.08172  ? 148 GLY D C   1 
ATOM   5082 O O   . GLY D 1 148 ? -32.93110 29.78394  -5.27226  1.000 77.76640  ? 148 GLY D O   1 
ATOM   5083 N N   . SER D 1 149 ? -31.93738 31.05071  -3.70345  1.000 75.94834  ? 149 SER D N   1 
ATOM   5084 C CA  . SER D 1 149 ? -32.47284 30.30665  -2.57382  1.000 86.16390  ? 149 SER D CA  1 
ATOM   5085 C C   . SER D 1 149 ? -33.61390 31.11179  -1.96346  1.000 84.82565  ? 149 SER D C   1 
ATOM   5086 O O   . SER D 1 149 ? -33.41728 32.26168  -1.55529  1.000 91.04230  ? 149 SER D O   1 
ATOM   5087 C CB  . SER D 1 149 ? -31.37977 30.02809  -1.54225  1.000 84.80876  ? 149 SER D CB  1 
ATOM   5088 O OG  . SER D 1 149 ? -31.90395 29.99836  -0.22847  1.000 109.69992 ? 149 SER D OG  1 
ATOM   5089 N N   . TYR D 1 150 ? -34.79768 30.50989  -1.89338  1.000 79.92668  ? 150 TYR D N   1 
ATOM   5090 C CA  . TYR D 1 150 ? -35.98761 31.20675  -1.43410  1.000 76.93531  ? 150 TYR D CA  1 
ATOM   5091 C C   . TYR D 1 150 ? -36.67643 30.39687  -0.34938  1.000 77.44020  ? 150 TYR D C   1 
ATOM   5092 O O   . TYR D 1 150 ? -36.35356 29.23345  -0.09427  1.000 77.37277  ? 150 TYR D O   1 
ATOM   5093 C CB  . TYR D 1 150 ? -36.99549 31.44870  -2.56829  1.000 60.93145  ? 150 TYR D CB  1 
ATOM   5094 C CG  . TYR D 1 150 ? -36.46709 32.20607  -3.75637  1.000 78.72789  ? 150 TYR D CG  1 
ATOM   5095 C CD1 . TYR D 1 150 ? -35.87375 31.54223  -4.81909  1.000 69.67598  ? 150 TYR D CD1 1 
ATOM   5096 C CD2 . TYR D 1 150 ? -36.59665 33.58751  -3.83267  1.000 80.34225  ? 150 TYR D CD2 1 
ATOM   5097 C CE1 . TYR D 1 150 ? -35.40116 32.23276  -5.91275  1.000 77.58630  ? 150 TYR D CE1 1 
ATOM   5098 C CE2 . TYR D 1 150 ? -36.12925 34.28657  -4.92271  1.000 70.83745  ? 150 TYR D CE2 1 
ATOM   5099 C CZ  . TYR D 1 150 ? -35.53050 33.60538  -5.96001  1.000 75.26478  ? 150 TYR D CZ  1 
ATOM   5100 O OH  . TYR D 1 150 ? -35.05804 34.29395  -7.05185  1.000 75.19086  ? 150 TYR D OH  1 
ATOM   5101 N N   . ARG D 1 151 ? -37.65209 31.04387  0.27295   1.000 68.74801  ? 151 ARG D N   1 
ATOM   5102 C CA  . ARG D 1 151 ? -38.61385 30.41078  1.15382   1.000 65.48033  ? 151 ARG D CA  1 
ATOM   5103 C C   . ARG D 1 151 ? -40.00186 30.80864  0.68593   1.000 68.16485  ? 151 ARG D C   1 
ATOM   5104 O O   . ARG D 1 151 ? -40.19512 31.87585  0.09801   1.000 75.14078  ? 151 ARG D O   1 
ATOM   5105 C CB  . ARG D 1 151 ? -38.42679 30.82649  2.61894   1.000 57.48680  ? 151 ARG D CB  1 
ATOM   5106 C CG  . ARG D 1 151 ? -37.33541 30.08547  3.34957   1.000 73.07177  ? 151 ARG D CG  1 
ATOM   5107 C CD  . ARG D 1 151 ? -37.14122 30.63935  4.74856   1.000 77.56241  ? 151 ARG D CD  1 
ATOM   5108 N NE  . ARG D 1 151 ? -35.99171 30.03071  5.40838   1.000 96.53218  ? 151 ARG D NE  1 
ATOM   5109 C CZ  . ARG D 1 151 ? -36.05867 29.04184  6.28882   1.000 82.76849  ? 151 ARG D CZ  1 
ATOM   5110 N NH1 . ARG D 1 151 ? -37.21698 28.52096  6.65777   1.000 86.05548  ? 151 ARG D NH1 1 
ATOM   5111 N NH2 . ARG D 1 151 ? -34.93397 28.56593  6.81469   1.000 77.16258  ? 151 ARG D NH2 1 
ATOM   5112 N N   . PHE D 1 152 ? -40.96198 29.93759  0.94019   1.000 55.44297  ? 152 PHE D N   1 
ATOM   5113 C CA  . PHE D 1 152 ? -42.35960 30.21720  0.66361   1.000 52.19083  ? 152 PHE D CA  1 
ATOM   5114 C C   . PHE D 1 152 ? -43.02348 30.65355  1.95526   1.000 57.90642  ? 152 PHE D C   1 
ATOM   5115 O O   . PHE D 1 152 ? -42.78963 30.05972  3.01323   1.000 64.68785  ? 152 PHE D O   1 
ATOM   5116 C CB  . PHE D 1 152 ? -43.08629 28.99984  0.08677   1.000 67.32895  ? 152 PHE D CB  1 
ATOM   5117 C CG  . PHE D 1 152 ? -43.07141 28.93071  -1.41311  1.000 70.25927  ? 152 PHE D CG  1 
ATOM   5118 C CD1 . PHE D 1 152 ? -43.44246 30.03140  -2.17105  1.000 70.99913  ? 152 PHE D CD1 1 
ATOM   5119 C CD2 . PHE D 1 152 ? -42.70352 27.76774  -2.06597  1.000 68.16682  ? 152 PHE D CD2 1 
ATOM   5120 C CE1 . PHE D 1 152 ? -43.43703 29.97467  -3.55462  1.000 74.92604  ? 152 PHE D CE1 1 
ATOM   5121 C CE2 . PHE D 1 152 ? -42.69395 27.70504  -3.45138  1.000 63.35041  ? 152 PHE D CE2 1 
ATOM   5122 C CZ  . PHE D 1 152 ? -43.06141 28.80741  -4.19382  1.000 70.79365  ? 152 PHE D CZ  1 
ATOM   5123 N N   . SER D 1 153 ? -43.77750 31.73928  1.88351   1.000 61.49097  ? 153 SER D N   1 
ATOM   5124 C CA  . SER D 1 153 ? -44.57577 32.19360  3.00708   1.000 58.83462  ? 153 SER D CA  1 
ATOM   5125 C C   . SER D 1 153 ? -46.03042 32.01817  2.61104   1.000 57.08686  ? 153 SER D C   1 
ATOM   5126 O O   . SER D 1 153 ? -46.45539 32.51198  1.56141   1.000 63.31888  ? 153 SER D O   1 
ATOM   5127 C CB  . SER D 1 153 ? -44.26930 33.64529  3.36650   1.000 66.22955  ? 153 SER D CB  1 
ATOM   5128 O OG  . SER D 1 153 ? -44.86983 33.98458  4.60064   1.000 79.13376  ? 153 SER D OG  1 
ATOM   5129 N N   . PHE D 1 154 ? -46.77127 31.26655  3.41366   1.000 59.96853  ? 154 PHE D N   1 
ATOM   5130 C CA  . PHE D 1 154 ? -48.17180 30.98540  3.14410   1.000 53.88888  ? 154 PHE D CA  1 
ATOM   5131 C C   . PHE D 1 154 ? -49.01508 31.71654  4.17706   1.000 59.44187  ? 154 PHE D C   1 
ATOM   5132 O O   . PHE D 1 154 ? -48.85635 31.49173  5.38214   1.000 66.93032  ? 154 PHE D O   1 
ATOM   5133 C CB  . PHE D 1 154 ? -48.43135 29.48332  3.18739   1.000 49.93020  ? 154 PHE D CB  1 
ATOM   5134 C CG  . PHE D 1 154 ? -47.64598 28.71818  2.17196   1.000 57.21004  ? 154 PHE D CG  1 
ATOM   5135 C CD1 . PHE D 1 154 ? -48.04159 28.69107  0.84640   1.000 56.07207  ? 154 PHE D CD1 1 
ATOM   5136 C CD2 . PHE D 1 154 ? -46.50094 28.03583  2.54117   1.000 56.86432  ? 154 PHE D CD2 1 
ATOM   5137 C CE1 . PHE D 1 154 ? -47.31116 27.99265  -0.09134  1.000 52.32362  ? 154 PHE D CE1 1 
ATOM   5138 C CE2 . PHE D 1 154 ? -45.76890 27.33109  1.61116   1.000 60.49512  ? 154 PHE D CE2 1 
ATOM   5139 C CZ  . PHE D 1 154 ? -46.17428 27.30970  0.29190   1.000 56.27409  ? 154 PHE D CZ  1 
ATOM   5140 N N   . HIS D 1 155 ? -49.90279 32.58540  3.70701   1.000 48.89244  ? 155 HIS D N   1 
ATOM   5141 C CA  . HIS D 1 155 ? -50.72066 33.42385  4.57209   1.000 59.83684  ? 155 HIS D CA  1 
ATOM   5142 C C   . HIS D 1 155 ? -52.17264 32.98108  4.47414   1.000 58.52044  ? 155 HIS D C   1 
ATOM   5143 O O   . HIS D 1 155 ? -52.72876 32.91028  3.37211   1.000 64.21026  ? 155 HIS D O   1 
ATOM   5144 C CB  . HIS D 1 155 ? -50.58908 34.89816  4.18346   1.000 57.80817  ? 155 HIS D CB  1 
ATOM   5145 C CG  . HIS D 1 155 ? -49.21587 35.28825  3.72555   1.000 50.92641  ? 155 HIS D CG  1 
ATOM   5146 N ND1 . HIS D 1 155 ? -48.23385 35.71764  4.59214   1.000 64.13407  ? 155 HIS D ND1 1 
ATOM   5147 C CD2 . HIS D 1 155 ? -48.66675 35.32691  2.48777   1.000 56.74636  ? 155 HIS D CD2 1 
ATOM   5148 C CE1 . HIS D 1 155 ? -47.13850 36.00082  3.90885   1.000 62.92345  ? 155 HIS D CE1 1 
ATOM   5149 N NE2 . HIS D 1 155 ? -47.37406 35.77141  2.62985   1.000 59.10038  ? 155 HIS D NE2 1 
ATOM   5150 N N   . LEU D 1 156 ? -52.80342 32.75104  5.62172   1.000 56.10371  ? 156 LEU D N   1 
ATOM   5151 C CA  . LEU D 1 156 ? -54.18224 32.28496  5.66364   1.000 60.66131  ? 156 LEU D CA  1 
ATOM   5152 C C   . LEU D 1 156 ? -55.12435 33.47001  5.83696   1.000 71.73962  ? 156 LEU D C   1 
ATOM   5153 O O   . LEU D 1 156 ? -54.93684 34.29520  6.73700   1.000 72.03641  ? 156 LEU D O   1 
ATOM   5154 C CB  . LEU D 1 156 ? -54.38167 31.28145  6.80206   1.000 69.05608  ? 156 LEU D CB  1 
ATOM   5155 C CG  . LEU D 1 156 ? -55.78305 30.67615  6.90584   1.000 66.28528  ? 156 LEU D CG  1 
ATOM   5156 C CD1 . LEU D 1 156 ? -56.08001 29.83116  5.68057   1.000 59.23002  ? 156 LEU D CD1 1 
ATOM   5157 C CD2 . LEU D 1 156 ? -55.96234 29.86941  8.18393   1.000 71.36592  ? 156 LEU D CD2 1 
ATOM   5158 N N   . PHE D 1 157 ? -56.14212 33.53778  4.98078   1.000 75.32763  ? 157 PHE D N   1 
ATOM   5159 C CA  . PHE D 1 157 ? -57.19688 34.53957  5.05750   1.000 70.58897  ? 157 PHE D CA  1 
ATOM   5160 C C   . PHE D 1 157 ? -58.53014 33.87211  5.34644   1.000 76.49634  ? 157 PHE D C   1 
ATOM   5161 O O   . PHE D 1 157 ? -58.90236 32.90113  4.67828   1.000 77.52354  ? 157 PHE D O   1 
ATOM   5162 C CB  . PHE D 1 157 ? -57.30648 35.32891  3.74882   1.000 78.15913  ? 157 PHE D CB  1 
ATOM   5163 C CG  . PHE D 1 157 ? -56.10722 36.16003  3.44104   1.000 86.67603  ? 157 PHE D CG  1 
ATOM   5164 C CD1 . PHE D 1 157 ? -55.73512 37.19460  4.28671   1.000 77.65722  ? 157 PHE D CD1 1 
ATOM   5165 C CD2 . PHE D 1 157 ? -55.33396 35.89536  2.31966   1.000 70.42534  ? 157 PHE D CD2 1 
ATOM   5166 C CE1 . PHE D 1 157 ? -54.62357 37.96090  4.01340   1.000 63.78303  ? 157 PHE D CE1 1 
ATOM   5167 C CE2 . PHE D 1 157 ? -54.21549 36.65826  2.04143   1.000 70.24806  ? 157 PHE D CE2 1 
ATOM   5168 C CZ  . PHE D 1 157 ? -53.85987 37.69062  2.89007   1.000 72.70403  ? 157 PHE D CZ  1 
ATOM   5169 N N   . GLU D 1 158 ? -59.23642 34.38910  6.34438   1.000 77.21047  ? 158 GLU D N   1 
ATOM   5170 C CA  . GLU D 1 158 ? -60.56158 33.91671  6.70640   1.000 77.04658  ? 158 GLU D CA  1 
ATOM   5171 C C   . GLU D 1 158 ? -61.58872 34.96290  6.30827   1.000 84.00308  ? 158 GLU D C   1 
ATOM   5172 O O   . GLU D 1 158 ? -61.41738 36.14892  6.60904   1.000 90.57161  ? 158 GLU D O   1 
ATOM   5173 C CB  . GLU D 1 158 ? -60.65930 33.62817  8.20371   1.000 73.50322  ? 158 GLU D CB  1 
ATOM   5174 C CG  . GLU D 1 158 ? -61.98747 33.02424  8.61160   1.000 79.87395  ? 158 GLU D CG  1 
ATOM   5175 C CD  . GLU D 1 158 ? -62.04704 32.71196  10.08578  1.000 90.56590  ? 158 GLU D CD  1 
ATOM   5176 O OE1 . GLU D 1 158 ? -60.97305 32.57122  10.70604  1.000 91.87390  ? 158 GLU D OE1 1 
ATOM   5177 O OE2 . GLU D 1 158 ? -63.16651 32.63616  10.63006  1.000 95.08872  ? 158 GLU D OE2 1 
ATOM   5178 N N   . GLN D 1 159 ? -62.63699 34.53238  5.61901   1.000 95.07156  ? 159 GLN D N   1 
ATOM   5179 C CA  . GLN D 1 159 ? -63.74317 35.40993  5.25574   1.000 98.32775  ? 159 GLN D CA  1 
ATOM   5180 C C   . GLN D 1 159 ? -64.95511 34.91445  6.03536   1.000 105.89819 ? 159 GLN D C   1 
ATOM   5181 O O   . GLN D 1 159 ? -65.62252 33.96397  5.61868   1.000 100.82129 ? 159 GLN D O   1 
ATOM   5182 C CB  . GLN D 1 159 ? -63.97544 35.39378  3.74842   1.000 85.04555  ? 159 GLN D CB  1 
ATOM   5183 C CG  . GLN D 1 159 ? -64.96779 36.42463  3.25699   1.000 109.25567 ? 159 GLN D CG  1 
ATOM   5184 C CD  . GLN D 1 159 ? -64.70877 36.82505  1.82090   1.000 117.16539 ? 159 GLN D CD  1 
ATOM   5185 O OE1 . GLN D 1 159 ? -64.70282 35.98509  0.92039   1.000 118.46011 ? 159 GLN D OE1 1 
ATOM   5186 N NE2 . GLN D 1 159 ? -64.49078 38.11602  1.59815   1.000 107.76142 ? 159 GLN D NE2 1 
ATOM   5187 N N   . ILE D 1 160 ? -65.21508 35.54361  7.18541   1.000 115.17988 ? 160 ILE D N   1 
ATOM   5188 C CA  . ILE D 1 160 ? -66.28156 35.07399  8.05988   1.000 119.68100 ? 160 ILE D CA  1 
ATOM   5189 C C   . ILE D 1 160 ? -67.62298 35.15802  7.34672   1.000 129.83395 ? 160 ILE D C   1 
ATOM   5190 O O   . ILE D 1 160 ? -67.89183 36.09213  6.57930   1.000 130.29793 ? 160 ILE D O   1 
ATOM   5191 C CB  . ILE D 1 160 ? -66.29509 35.86049  9.38277   1.000 131.50997 ? 160 ILE D CB  1 
ATOM   5192 C CG1 . ILE D 1 160 ? -66.72971 37.31192  9.16565   1.000 135.47634 ? 160 ILE D CG1 1 
ATOM   5193 C CG2 . ILE D 1 160 ? -64.93009 35.79751  10.05125  1.000 121.20553 ? 160 ILE D CG2 1 
ATOM   5194 C CD1 . ILE D 1 160 ? -68.11919 37.60604  9.68831   1.000 129.02102 ? 160 ILE D CD1 1 
ATOM   5195 N N   . LYS D 1 161 ? -68.47029 34.16495  7.58764   1.000 131.47382 ? 161 LYS D N   1 
ATOM   5196 C CA  . LYS D 1 161 ? -69.79362 34.13047  6.99521   1.000 136.80568 ? 161 LYS D CA  1 
ATOM   5197 C C   . LYS D 1 161 ? -70.88752 34.09604  8.05567   1.000 146.21094 ? 161 LYS D C   1 
ATOM   5198 O O   . LYS D 1 161 ? -72.07018 34.21974  7.71615   1.000 141.33952 ? 161 LYS D O   1 
ATOM   5199 C CB  . LYS D 1 161 ? -69.91507 32.92764  6.03969   1.000 134.00907 ? 161 LYS D CB  1 
ATOM   5200 C CG  . LYS D 1 161 ? -71.23231 32.83342  5.27657   1.000 166.30626 ? 161 LYS D CG  1 
ATOM   5201 C CD  . LYS D 1 161 ? -71.33087 31.56450  4.44729   1.000 178.32123 ? 161 LYS D CD  1 
ATOM   5202 C CE  . LYS D 1 161 ? -72.49393 31.64358  3.46273   1.000 179.10298 ? 161 LYS D CE  1 
ATOM   5203 N NZ  . LYS D 1 161 ? -73.80524 31.84763  4.14051   1.000 157.66006 ? 161 LYS D NZ  1 
ATOM   5204 N N   . ASP D 1 162 ? -70.51934 33.99095  9.33202   1.000 144.30679 ? 162 ASP D N   1 
ATOM   5205 C CA  . ASP D 1 162 ? -71.45036 34.00275  10.44666  1.000 146.61150 ? 162 ASP D CA  1 
ATOM   5206 C C   . ASP D 1 162 ? -70.97674 35.01573  11.48322  1.000 152.38684 ? 162 ASP D C   1 
ATOM   5207 O O   . ASP D 1 162 ? -69.80714 34.96943  11.90557  1.000 147.96052 ? 162 ASP D O   1 
ATOM   5208 C CB  . ASP D 1 162 ? -71.55951 32.60457  11.07143  1.000 155.59001 ? 162 ASP D CB  1 
ATOM   5209 C CG  . ASP D 1 162 ? -72.96875 32.27027  11.51647  1.000 165.23401 ? 162 ASP D CG  1 
ATOM   5210 O OD1 . ASP D 1 162 ? -73.54084 33.03214  12.32331  1.000 170.06059 ? 162 ASP D OD1 1 
ATOM   5211 O OD2 . ASP D 1 162 ? -73.50204 31.23447  11.06269  1.000 171.32153 ? 162 ASP D OD2 1 
ATOM   5212 N N   . PRO D 1 163 ? -71.83642 35.94711  11.90662  1.000 161.92288 ? 163 PRO D N   1 
ATOM   5213 C CA  . PRO D 1 163 ? -71.39255 36.99878  12.84123  1.000 159.17672 ? 163 PRO D CA  1 
ATOM   5214 C C   . PRO D 1 163 ? -70.93602 36.47172  14.19275  1.000 165.86858 ? 163 PRO D C   1 
ATOM   5215 O O   . PRO D 1 163 ? -70.10589 37.11662  14.84569  1.000 163.41545 ? 163 PRO D O   1 
ATOM   5216 C CB  . PRO D 1 163 ? -72.63613 37.89074  12.96901  1.000 150.90607 ? 163 PRO D CB  1 
ATOM   5217 C CG  . PRO D 1 163 ? -73.46339 37.56412  11.75572  1.000 150.59836 ? 163 PRO D CG  1 
ATOM   5218 C CD  . PRO D 1 163 ? -73.25590 36.10566  11.54683  1.000 157.63988 ? 163 PRO D CD  1 
ATOM   5219 N N   . LYS D 1 164 ? -71.47720 35.33651  14.64543  1.000 183.21688 ? 164 LYS D N   1 
ATOM   5220 C CA  . LYS D 1 164 ? -71.07559 34.76529  15.92914  1.000 176.19560 ? 164 LYS D CA  1 
ATOM   5221 C C   . LYS D 1 164 ? -69.58509 34.44952  15.97438  1.000 171.44730 ? 164 LYS D C   1 
ATOM   5222 O O   . LYS D 1 164 ? -68.95651 34.57851  17.03185  1.000 171.57566 ? 164 LYS D O   1 
ATOM   5223 C CB  . LYS D 1 164 ? -71.87459 33.49391  16.21490  1.000 178.58598 ? 164 LYS D CB  1 
ATOM   5224 C CG  . LYS D 1 164 ? -71.95662 32.54556  15.02952  1.000 177.95685 ? 164 LYS D CG  1 
ATOM   5225 C CD  . LYS D 1 164 ? -71.94872 31.08888  15.46761  1.000 177.46916 ? 164 LYS D CD  1 
ATOM   5226 C CE  . LYS D 1 164 ? -71.76683 30.15994  14.27489  1.000 166.70404 ? 164 LYS D CE  1 
ATOM   5227 N NZ  . LYS D 1 164 ? -71.32456 28.79933  14.68542  1.000 160.05689 ? 164 LYS D NZ  1 
ATOM   5228 N N   . ASP D 1 165 ? -69.00341 34.03327  14.85055  1.000 162.10169 ? 165 ASP D N   1 
ATOM   5229 C CA  . ASP D 1 165 ? -67.60152 33.63763  14.81727  1.000 154.29438 ? 165 ASP D CA  1 
ATOM   5230 C C   . ASP D 1 165 ? -66.64606 34.82494  14.81167  1.000 148.39392 ? 165 ASP D C   1 
ATOM   5231 O O   . ASP D 1 165 ? -65.42894 34.61536  14.84458  1.000 146.95932 ? 165 ASP D O   1 
ATOM   5232 C CB  . ASP D 1 165 ? -67.33900 32.75631  13.59198  1.000 145.58562 ? 165 ASP D CB  1 
ATOM   5233 C CG  . ASP D 1 165 ? -68.09064 31.43523  13.64918  1.000 145.92051 ? 165 ASP D CG  1 
ATOM   5234 O OD1 . ASP D 1 165 ? -68.43537 30.98509  14.76292  1.000 135.65596 ? 165 ASP D OD1 1 
ATOM   5235 O OD2 . ASP D 1 165 ? -68.33736 30.84501  12.57628  1.000 143.67805 ? 165 ASP D OD2 1 
ATOM   5236 N N   . ALA D 1 166 ? -67.15976 36.05181  14.75444  1.000 155.48735 ? 166 ALA D N   1 
ATOM   5237 C CA  . ALA D 1 166 ? -66.31710 37.23782  14.75007  1.000 144.27779 ? 166 ALA D CA  1 
ATOM   5238 C C   . ALA D 1 166 ? -65.57079 37.36428  16.07668  1.000 149.02996 ? 166 ALA D C   1 
ATOM   5239 O O   . ALA D 1 166 ? -65.94456 36.76908  17.09213  1.000 148.23941 ? 166 ALA D O   1 
ATOM   5240 C CB  . ALA D 1 166 ? -67.14730 38.49467  14.49058  1.000 145.86867 ? 166 ALA D CB  1 
ATOM   5241 N N   . THR D 1 167 ? -64.49898 38.15076  16.05759  1.000 144.17430 ? 167 THR D N   1 
ATOM   5242 C CA  . THR D 1 167 ? -63.64749 38.31278  17.23369  1.000 146.18304 ? 167 THR D CA  1 
ATOM   5243 C C   . THR D 1 167 ? -64.35071 39.09495  18.34890  1.000 139.50590 ? 167 THR D C   1 
ATOM   5244 O O   . THR D 1 167 ? -64.39126 40.32549  18.34621  1.000 127.75754 ? 167 THR D O   1 
ATOM   5245 C CB  . THR D 1 167 ? -62.32721 39.02383  16.87068  1.000 127.55527 ? 167 THR D CB  1 
ATOM   5246 O OG1 . THR D 1 167 ? -61.70586 38.35064  15.76699  1.000 123.75924 ? 167 THR D OG1 1 
ATOM   5247 C CG2 . THR D 1 167 ? -61.37675 39.02209  18.05818  1.000 120.12451 ? 167 THR D CG2 1 
ATOM   5248 N N   . PRO D 1 184 ? -71.49105 45.05140  -1.79195  1.000 200.60842 ? 184 PRO D N   1 
ATOM   5249 C CA  . PRO D 1 184 ? -71.24394 44.64074  -0.40811  1.000 208.29063 ? 184 PRO D CA  1 
ATOM   5250 C C   . PRO D 1 184 ? -69.83177 44.97590  0.06825   1.000 201.80610 ? 184 PRO D C   1 
ATOM   5251 O O   . PRO D 1 184 ? -68.91437 45.07560  -0.74521  1.000 192.10235 ? 184 PRO D O   1 
ATOM   5252 C CB  . PRO D 1 184 ? -71.45952 43.12164  -0.45141  1.000 200.37217 ? 184 PRO D CB  1 
ATOM   5253 C CG  . PRO D 1 184 ? -72.20715 42.84277  -1.75672  1.000 197.47588 ? 184 PRO D CG  1 
ATOM   5254 C CD  . PRO D 1 184 ? -72.44329 44.15049  -2.45731  1.000 194.32125 ? 184 PRO D CD  1 
ATOM   5255 N N   . GLN D 1 185 ? -69.67014 45.14589  1.37952   1.000 212.66280 ? 185 GLN D N   1 
ATOM   5256 C CA  . GLN D 1 185 ? -68.39234 45.50656  1.99288   1.000 198.66536 ? 185 GLN D CA  1 
ATOM   5257 C C   . GLN D 1 185 ? -67.73002 44.31236  2.66763   1.000 184.92220 ? 185 GLN D C   1 
ATOM   5258 O O   . GLN D 1 185 ? -67.18469 44.45066  3.76346   1.000 177.76446 ? 185 GLN D O   1 
ATOM   5259 C CB  . GLN D 1 185 ? -68.58028 46.64241  2.99581   1.000 206.17151 ? 185 GLN D CB  1 
ATOM   5260 C CG  . GLN D 1 185 ? -69.10368 47.94458  2.40534   1.000 220.91254 ? 185 GLN D CG  1 
ATOM   5261 C CD  . GLN D 1 185 ? -70.61663 48.05008  2.46731   1.000 223.25429 ? 185 GLN D CD  1 
ATOM   5262 O OE1 . GLN D 1 185 ? -71.29272 47.15630  2.97678   1.000 223.24836 ? 185 GLN D OE1 1 
ATOM   5263 N NE2 . GLN D 1 185 ? -71.15483 49.15088  1.95457   1.000 215.55908 ? 185 GLN D NE2 1 
ATOM   5264 N N   . GLU D 1 186 ? -67.78549 43.13637  2.03433   1.000 171.73526 ? 186 GLU D N   1 
ATOM   5265 C CA  . GLU D 1 186 ? -67.27469 41.88999  2.60201   1.000 152.89208 ? 186 GLU D CA  1 
ATOM   5266 C C   . GLU D 1 186 ? -65.91617 42.07030  3.26790   1.000 137.21195 ? 186 GLU D C   1 
ATOM   5267 O O   . GLU D 1 186 ? -65.04971 42.78512  2.76055   1.000 131.26880 ? 186 GLU D O   1 
ATOM   5268 C CB  . GLU D 1 186 ? -67.16145 40.83084  1.49953   1.000 145.26885 ? 186 GLU D CB  1 
ATOM   5269 C CG  . GLU D 1 186 ? -68.40420 39.98111  1.29263   1.000 159.96485 ? 186 GLU D CG  1 
ATOM   5270 C CD  . GLU D 1 186 ? -68.48281 38.80606  2.24768   1.000 157.21615 ? 186 GLU D CD  1 
ATOM   5271 O OE1 . GLU D 1 186 ? -68.19496 38.98568  3.45032   1.000 152.66167 ? 186 GLU D OE1 1 
ATOM   5272 O OE2 . GLU D 1 186 ? -68.82767 37.69637  1.78974   1.000 155.11621 ? 186 GLU D OE2 1 
ATOM   5273 N N   . PHE D 1 187 ? -65.74954 41.42558  4.42231   1.000 129.30351 ? 187 PHE D N   1 
ATOM   5274 C CA  . PHE D 1 187 ? -64.53482 41.52585  5.22275   1.000 121.26816 ? 187 PHE D CA  1 
ATOM   5275 C C   . PHE D 1 187 ? -63.58971 40.37450  4.89784   1.000 107.61321 ? 187 PHE D C   1 
ATOM   5276 O O   . PHE D 1 187 ? -64.01596 39.26129  4.57981   1.000 108.75659 ? 187 PHE D O   1 
ATOM   5277 C CB  . PHE D 1 187 ? -64.82630 41.54643  6.73133   1.000 119.78893 ? 187 PHE D CB  1 
ATOM   5278 C CG  . PHE D 1 187 ? -66.08497 42.28574  7.12264   1.000 136.79990 ? 187 PHE D CG  1 
ATOM   5279 C CD1 . PHE D 1 187 ? -66.47993 43.43230  6.45120   1.000 139.77909 ? 187 PHE D CD1 1 
ATOM   5280 C CD2 . PHE D 1 187 ? -66.86239 41.84063  8.17984   1.000 128.31538 ? 187 PHE D CD2 1 
ATOM   5281 C CE1 . PHE D 1 187 ? -67.62920 44.11156  6.81475   1.000 142.60997 ? 187 PHE D CE1 1 
ATOM   5282 C CE2 . PHE D 1 187 ? -68.01360 42.51736  8.54831   1.000 127.94101 ? 187 PHE D CE2 1 
ATOM   5283 C CZ  . PHE D 1 187 ? -68.39645 43.65382  7.86367   1.000 128.50497 ? 187 PHE D CZ  1 
ATOM   5284 N N   . LEU D 1 188 ? -62.29288 40.65715  4.98875   1.000 93.31405  ? 188 LEU D N   1 
ATOM   5285 C CA  . LEU D 1 188 ? -61.24571 39.65186  4.84964   1.000 90.42592  ? 188 LEU D CA  1 
ATOM   5286 C C   . LEU D 1 188 ? -60.26014 39.82352  5.99481   1.000 83.51658  ? 188 LEU D C   1 
ATOM   5287 O O   . LEU D 1 188 ? -59.66025 40.89284  6.14457   1.000 91.84227  ? 188 LEU D O   1 
ATOM   5288 C CB  . LEU D 1 188 ? -60.53525 39.77386  3.50087   1.000 77.25328  ? 188 LEU D CB  1 
ATOM   5289 C CG  . LEU D 1 188 ? -59.53319 38.65745  3.21907   1.000 77.96921  ? 188 LEU D CG  1 
ATOM   5290 C CD1 . LEU D 1 188 ? -60.21698 37.31179  3.38098   1.000 88.69507  ? 188 LEU D CD1 1 
ATOM   5291 C CD2 . LEU D 1 188 ? -58.94511 38.80038  1.82813   1.000 70.28912  ? 188 LEU D CD2 1 
ATOM   5292 N N   . GLU D 1 189 ? -60.06578 38.76664  6.77731   1.000 77.50681  ? 189 GLU D N   1 
ATOM   5293 C CA  . GLU D 1 189 ? -59.24551 38.82024  7.97961   1.000 77.00558  ? 189 GLU D CA  1 
ATOM   5294 C C   . GLU D 1 189 ? -58.04690 37.90060  7.82214   1.000 80.59590  ? 189 GLU D C   1 
ATOM   5295 O O   . GLU D 1 189 ? -58.20688 36.69433  7.60919   1.000 84.60380  ? 189 GLU D O   1 
ATOM   5296 C CB  . GLU D 1 189 ? -60.05329 38.40329  9.20948   1.000 80.86223  ? 189 GLU D CB  1 
ATOM   5297 C CG  . GLU D 1 189 ? -61.23049 39.28764  9.54904   1.000 98.54574  ? 189 GLU D CG  1 
ATOM   5298 C CD  . GLU D 1 189 ? -61.27354 39.61860  11.03102  1.000 118.08376 ? 189 GLU D CD  1 
ATOM   5299 O OE1 . GLU D 1 189 ? -60.63801 40.61481  11.43685  1.000 112.32403 ? 189 GLU D OE1 1 
ATOM   5300 O OE2 . GLU D 1 189 ? -61.94927 38.88355  11.78746  1.000 123.51904 ? 189 GLU D OE2 1 
ATOM   5301 N N   . PHE D 1 190 ? -56.85136 38.47479  7.93275   1.000 87.64109  ? 190 PHE D N   1 
ATOM   5302 C CA  . PHE D 1 190 ? -55.63900 37.67575  8.00705   1.000 68.52838  ? 190 PHE D CA  1 
ATOM   5303 C C   . PHE D 1 190 ? -55.60264 36.95004  9.34456   1.000 70.46386  ? 190 PHE D C   1 
ATOM   5304 O O   . PHE D 1 190 ? -55.96760 37.50837  10.38257  1.000 83.47130  ? 190 PHE D O   1 
ATOM   5305 C CB  . PHE D 1 190 ? -54.40326 38.56080  7.83122   1.000 66.28612  ? 190 PHE D CB  1 
ATOM   5306 C CG  . PHE D 1 190 ? -53.10133 37.85269  8.09595   1.000 65.52085  ? 190 PHE D CG  1 
ATOM   5307 C CD1 . PHE D 1 190 ? -52.55198 36.99680  7.14639   1.000 63.63873  ? 190 PHE D CD1 1 
ATOM   5308 C CD2 . PHE D 1 190 ? -52.42011 38.04713  9.28538   1.000 65.47935  ? 190 PHE D CD2 1 
ATOM   5309 C CE1 . PHE D 1 190 ? -51.35562 36.34132  7.38507   1.000 60.90514  ? 190 PHE D CE1 1 
ATOM   5310 C CE2 . PHE D 1 190 ? -51.21973 37.39289  9.52828   1.000 64.86782  ? 190 PHE D CE2 1 
ATOM   5311 C CZ  . PHE D 1 190 ? -50.69072 36.53771  8.57563   1.000 62.04324  ? 190 PHE D CZ  1 
ATOM   5312 N N   . ARG D 1 191 ? -55.16422 35.69305  9.31926   1.000 69.51202  ? 191 ARG D N   1 
ATOM   5313 C CA  . ARG D 1 191 ? -55.12756 34.87519  10.52232  1.000 71.65347  ? 191 ARG D CA  1 
ATOM   5314 C C   . ARG D 1 191 ? -53.70392 34.54145  10.94637  1.000 70.23518  ? 191 ARG D C   1 
ATOM   5315 O O   . ARG D 1 191 ? -53.30480 34.87047  12.06615  1.000 71.92906  ? 191 ARG D O   1 
ATOM   5316 C CB  . ARG D 1 191 ? -55.93031 33.58424  10.30807  1.000 78.13754  ? 191 ARG D CB  1 
ATOM   5317 C CG  . ARG D 1 191 ? -57.43727 33.76703  10.36013  1.000 84.00212  ? 191 ARG D CG  1 
ATOM   5318 C CD  . ARG D 1 191 ? -57.90754 34.27572  11.70846  1.000 83.80202  ? 191 ARG D CD  1 
ATOM   5319 N NE  . ARG D 1 191 ? -59.32758 34.60676  11.68470  1.000 90.94976  ? 191 ARG D NE  1 
ATOM   5320 C CZ  . ARG D 1 191 ? -59.84160 35.75480  12.10158  1.000 104.88119 ? 191 ARG D CZ  1 
ATOM   5321 N NH1 . ARG D 1 191 ? -59.07609 36.71777  12.59022  1.000 112.91212 ? 191 ARG D NH1 1 
ATOM   5322 N NH2 . ARG D 1 191 ? -61.15873 35.93613  12.03898  1.000 101.87932 ? 191 ARG D NH2 1 
ATOM   5323 N N   . LEU D 1 192 ? -52.92149 33.90004  10.08415  1.000 67.63555  ? 192 LEU D N   1 
ATOM   5324 C CA  . LEU D 1 192 ? -51.58106 33.47540  10.46169  1.000 66.86261  ? 192 LEU D CA  1 
ATOM   5325 C C   . LEU D 1 192 ? -50.79960 33.12412  9.20343   1.000 63.91779  ? 192 LEU D C   1 
ATOM   5326 O O   . LEU D 1 192 ? -51.33685 33.09566  8.09256   1.000 65.96461  ? 192 LEU D O   1 
ATOM   5327 C CB  . LEU D 1 192 ? -51.62191 32.29402  11.43747  1.000 77.84362  ? 192 LEU D CB  1 
ATOM   5328 C CG  . LEU D 1 192 ? -51.79293 30.88339  10.86769  1.000 77.49973  ? 192 LEU D CG  1 
ATOM   5329 C CD1 . LEU D 1 192 ? -51.36670 29.85192  11.90133  1.000 75.91666  ? 192 LEU D CD1 1 
ATOM   5330 C CD2 . LEU D 1 192 ? -53.22633 30.65402  10.42841  1.000 71.45719  ? 192 LEU D CD2 1 
ATOM   5331 N N   . GLU D 1 193 ? -49.53099 32.79057  9.40848   1.000 69.11101  ? 193 GLU D N   1 
ATOM   5332 C CA  . GLU D 1 193 ? -48.56331 32.57263  8.34863   1.000 64.06139  ? 193 GLU D CA  1 
ATOM   5333 C C   . GLU D 1 193 ? -47.65865 31.41358  8.72757   1.000 68.68215  ? 193 GLU D C   1 
ATOM   5334 O O   . GLU D 1 193 ? -47.35694 31.21641  9.90852   1.000 69.01302  ? 193 GLU D O   1 
ATOM   5335 C CB  . GLU D 1 193 ? -47.75134 33.85696  8.12962   1.000 59.71297  ? 193 GLU D CB  1 
ATOM   5336 C CG  . GLU D 1 193 ? -46.36482 33.70819  7.54953   1.000 73.72145  ? 193 GLU D CG  1 
ATOM   5337 C CD  . GLU D 1 193 ? -45.48737 34.91192  7.88800   1.000 95.61842  ? 193 GLU D CD  1 
ATOM   5338 O OE1 . GLU D 1 193 ? -45.54071 35.37167  9.05126   1.000 82.78393  ? 193 GLU D OE1 1 
ATOM   5339 O OE2 . GLU D 1 193 ? -44.74395 35.39395  7.00341   1.000 92.64958  ? 193 GLU D OE2 1 
ATOM   5340 N N   . VAL D 1 194 ? -47.28479 30.61189  7.73374   1.000 60.93829  ? 194 VAL D N   1 
ATOM   5341 C CA  . VAL D 1 194 ? -46.35458 29.50515  7.92438   1.000 72.51120  ? 194 VAL D CA  1 
ATOM   5342 C C   . VAL D 1 194 ? -45.25635 29.62345  6.87495   1.000 64.01824  ? 194 VAL D C   1 
ATOM   5343 O O   . VAL D 1 194 ? -45.52700 29.93321  5.70847   1.000 62.54114  ? 194 VAL D O   1 
ATOM   5344 C CB  . VAL D 1 194 ? -47.05694 28.12899  7.86053   1.000 63.56052  ? 194 VAL D CB  1 
ATOM   5345 C CG1 . VAL D 1 194 ? -47.70120 27.88993  6.49785   1.000 62.10056  ? 194 VAL D CG1 1 
ATOM   5346 C CG2 . VAL D 1 194 ? -46.07214 27.02290  8.20293   1.000 65.36744  ? 194 VAL D CG2 1 
ATOM   5347 N N   . ILE D 1 195 ? -44.01579 29.38466  7.29098   1.000 66.15057  ? 195 ILE D N   1 
ATOM   5348 C CA  . ILE D 1 195 ? -42.84038 29.59869  6.45300   1.000 68.26661  ? 195 ILE D CA  1 
ATOM   5349 C C   . ILE D 1 195 ? -42.24085 28.24306  6.10373   1.000 69.60815  ? 195 ILE D C   1 
ATOM   5350 O O   . ILE D 1 195 ? -42.02603 27.40300  6.98684   1.000 73.09201  ? 195 ILE D O   1 
ATOM   5351 C CB  . ILE D 1 195 ? -41.80601 30.50761  7.13725   1.000 77.63765  ? 195 ILE D CB  1 
ATOM   5352 C CG1 . ILE D 1 195 ? -42.31595 31.94846  7.17422   1.000 77.88876  ? 195 ILE D CG1 1 
ATOM   5353 C CG2 . ILE D 1 195 ? -40.48917 30.47229  6.37960   1.000 65.96541  ? 195 ILE D CG2 1 
ATOM   5354 C CD1 . ILE D 1 195 ? -41.84017 32.72777  8.37944   1.000 106.09869 ? 195 ILE D CD1 1 
ATOM   5355 N N   . SER D 1 196 ? -41.98182 28.03080  4.81633   1.000 60.86258  ? 196 SER D N   1 
ATOM   5356 C CA  . SER D 1 196 ? -41.48938 26.76160  4.31403   1.000 73.03478  ? 196 SER D CA  1 
ATOM   5357 C C   . SER D 1 196 ? -39.97800 26.65528  4.49151   1.000 78.01860  ? 196 SER D C   1 
ATOM   5358 O O   . SER D 1 196 ? -39.28513 27.61577  4.83431   1.000 73.90471  ? 196 SER D O   1 
ATOM   5359 C CB  . SER D 1 196 ? -41.84977 26.59247  2.83888   1.000 71.27860  ? 196 SER D CB  1 
ATOM   5360 O OG  . SER D 1 196 ? -40.93436 27.29074  2.01113   1.000 64.13441  ? 196 SER D OG  1 
ATOM   5361 N N   . ASN D 1 197 ? -39.47696 25.45026  4.26479   1.000 76.07567  ? 197 ASN D N   1 
ATOM   5362 C CA  . ASN D 1 197 ? -38.04708 25.22424  4.22551   1.000 76.72360  ? 197 ASN D CA  1 
ATOM   5363 C C   . ASN D 1 197 ? -37.45121 25.88553  2.98649   1.000 78.62414  ? 197 ASN D C   1 
ATOM   5364 O O   . ASN D 1 197 ? -38.15542 26.11724  1.99914   1.000 74.86296  ? 197 ASN D O   1 
ATOM   5365 C CB  . ASN D 1 197 ? -37.73561 23.72888  4.19682   1.000 83.72049  ? 197 ASN D CB  1 
ATOM   5366 C CG  . ASN D 1 197 ? -38.05670 23.03997  5.50240   1.000 76.03651  ? 197 ASN D CG  1 
ATOM   5367 O OD1 . ASN D 1 197 ? -37.83388 23.59051  6.57923   1.000 91.44900  ? 197 ASN D OD1 1 
ATOM   5368 N ND2 . ASN D 1 197 ? -38.54643 21.80892  5.41410   1.000 79.19592  ? 197 ASN D ND2 1 
ATOM   5369 N N   . PRO D 1 198 ? -36.17435 26.26357  3.04019   1.000 88.36104  ? 198 PRO D N   1 
ATOM   5370 C CA  . PRO D 1 198 ? -35.54149 26.87088  1.86488   1.000 75.37177  ? 198 PRO D CA  1 
ATOM   5371 C C   . PRO D 1 198 ? -35.55383 25.89009  0.70196   1.000 71.03346  ? 198 PRO D C   1 
ATOM   5372 O O   . PRO D 1 198 ? -35.41462 24.67967  0.88440   1.000 86.77767  ? 198 PRO D O   1 
ATOM   5373 C CB  . PRO D 1 198 ? -34.11451 27.17351  2.33318   1.000 72.50635  ? 198 PRO D CB  1 
ATOM   5374 C CG  . PRO D 1 198 ? -34.13524 27.05771  3.81360   1.000 77.75280  ? 198 PRO D CG  1 
ATOM   5375 C CD  . PRO D 1 198 ? -35.24195 26.13014  4.17262   1.000 77.41577  ? 198 PRO D CD  1 
ATOM   5376 N N   . PHE D 1 199 ? -35.74517 26.42307  -0.49893  1.000 75.85584  ? 199 PHE D N   1 
ATOM   5377 C CA  . PHE D 1 199 ? -35.68764 25.63175  -1.71656  1.000 74.14895  ? 199 PHE D CA  1 
ATOM   5378 C C   . PHE D 1 199 ? -34.90169 26.41821  -2.75344  1.000 82.59932  ? 199 PHE D C   1 
ATOM   5379 O O   . PHE D 1 199 ? -34.86068 27.64979  -2.71994  1.000 78.37687  ? 199 PHE D O   1 
ATOM   5380 C CB  . PHE D 1 199 ? -37.08537 25.24365  -2.23298  1.000 85.37122  ? 199 PHE D CB  1 
ATOM   5381 C CG  . PHE D 1 199 ? -37.85841 26.37469  -2.84402  1.000 75.38659  ? 199 PHE D CG  1 
ATOM   5382 C CD1 . PHE D 1 199 ? -38.36379 27.39499  -2.06027  1.000 74.10516  ? 199 PHE D CD1 1 
ATOM   5383 C CD2 . PHE D 1 199 ? -38.11268 26.39247  -4.20483  1.000 78.61849  ? 199 PHE D CD2 1 
ATOM   5384 C CE1 . PHE D 1 199 ? -39.08653 28.42898  -2.62794  1.000 72.38228  ? 199 PHE D CE1 1 
ATOM   5385 C CE2 . PHE D 1 199 ? -38.83174 27.42170  -4.77892  1.000 67.74089  ? 199 PHE D CE2 1 
ATOM   5386 C CZ  . PHE D 1 199 ? -39.32122 28.44099  -3.98936  1.000 64.27603  ? 199 PHE D CZ  1 
ATOM   5387 N N   . ILE D 1 200 ? -34.26457 25.69014  -3.66634  1.000 86.09439  ? 200 ILE D N   1 
ATOM   5388 C CA  . ILE D 1 200 ? -33.28365 26.23944  -4.59570  1.000 87.37595  ? 200 ILE D CA  1 
ATOM   5389 C C   . ILE D 1 200 ? -33.88949 26.22660  -5.98893  1.000 81.18338  ? 200 ILE D C   1 
ATOM   5390 O O   . ILE D 1 200 ? -34.42257 25.20572  -6.43387  1.000 76.15719  ? 200 ILE D O   1 
ATOM   5391 C CB  . ILE D 1 200 ? -31.97365 25.42797  -4.56263  1.000 91.20143  ? 200 ILE D CB  1 
ATOM   5392 C CG1 . ILE D 1 200 ? -31.10561 25.84326  -3.37554  1.000 89.79313  ? 200 ILE D CG1 1 
ATOM   5393 C CG2 . ILE D 1 200 ? -31.19143 25.58704  -5.86636  1.000 85.61880  ? 200 ILE D CG2 1 
ATOM   5394 C CD1 . ILE D 1 200 ? -30.51768 27.22135  -3.51288  1.000 87.50879  ? 200 ILE D CD1 1 
ATOM   5395 N N   . VAL D 1 201 ? -33.84138 27.37051  -6.66114  1.000 80.07537  ? 201 VAL D N   1 
ATOM   5396 C CA  . VAL D 1 201 ? -34.27517 27.47785  -8.04596  1.000 80.70855  ? 201 VAL D CA  1 
ATOM   5397 C C   . VAL D 1 201 ? -33.02883 27.56755  -8.91221  1.000 82.08534  ? 201 VAL D C   1 
ATOM   5398 O O   . VAL D 1 201 ? -32.19041 28.45538  -8.71466  1.000 79.10666  ? 201 VAL D O   1 
ATOM   5399 C CB  . VAL D 1 201 ? -35.18366 28.70280  -8.24972  1.000 74.04864  ? 201 VAL D CB  1 
ATOM   5400 C CG1 . VAL D 1 201 ? -35.43250 28.95313  -9.72366  1.000 73.49926  ? 201 VAL D CG1 1 
ATOM   5401 C CG2 . VAL D 1 201 ? -36.49195 28.54130  -7.49247  1.000 66.76647  ? 201 VAL D CG2 1 
ATOM   5402 N N   . TYR D 1 202 ? -32.88849 26.64036  -9.85386  1.000 78.59575  ? 202 TYR D N   1 
ATOM   5403 C CA  . TYR D 1 202 ? -31.70339 26.58384  -10.69539 1.000 85.58563  ? 202 TYR D CA  1 
ATOM   5404 C C   . TYR D 1 202 ? -32.03614 27.10960  -12.08544 1.000 84.01595  ? 202 TYR D C   1 
ATOM   5405 O O   . TYR D 1 202 ? -33.20196 27.19367  -12.47930 1.000 82.06281  ? 202 TYR D O   1 
ATOM   5406 C CB  . TYR D 1 202 ? -31.14789 25.15446  -10.77377 1.000 83.63243  ? 202 TYR D CB  1 
ATOM   5407 C CG  . TYR D 1 202 ? -32.13098 24.11585  -11.27407 1.000 85.22735  ? 202 TYR D CG  1 
ATOM   5408 C CD1 . TYR D 1 202 ? -32.49351 24.05916  -12.61550 1.000 85.91770  ? 202 TYR D CD1 1 
ATOM   5409 C CD2 . TYR D 1 202 ? -32.71005 23.20366  -10.40209 1.000 89.08738  ? 202 TYR D CD2 1 
ATOM   5410 C CE1 . TYR D 1 202 ? -33.39391 23.12178  -13.07428 1.000 90.80817  ? 202 TYR D CE1 1 
ATOM   5411 C CE2 . TYR D 1 202 ? -33.61715 22.26104  -10.85260 1.000 98.58350  ? 202 TYR D CE2 1 
ATOM   5412 C CZ  . TYR D 1 202 ? -33.95565 22.22476  -12.19006 1.000 99.26678  ? 202 TYR D CZ  1 
ATOM   5413 O OH  . TYR D 1 202 ? -34.85337 21.28543  -12.64801 1.000 94.60520  ? 202 TYR D OH  1 
ATOM   5414 N N   . SER D 1 203 ? -30.99240 27.43652  -12.84006 1.000 99.33890  ? 203 SER D N   1 
ATOM   5415 C CA  . SER D 1 203 ? -31.13867 27.93090  -14.20128 1.000 98.22702  ? 203 SER D CA  1 
ATOM   5416 C C   . SER D 1 203 ? -30.56781 26.91081  -15.17392 1.000 101.05135 ? 203 SER D C   1 
ATOM   5417 O O   . SER D 1 203 ? -29.46225 26.39923  -14.96602 1.000 89.63498  ? 203 SER D O   1 
ATOM   5418 C CB  . SER D 1 203 ? -30.43687 29.27818  -14.37618 1.000 96.55644  ? 203 SER D CB  1 
ATOM   5419 O OG  . SER D 1 203 ? -31.07542 30.05224  -15.37851 1.000 116.08278 ? 203 SER D OG  1 
ATOM   5420 N N   . ALA D 1 204 ? -31.32842 26.61029  -16.22308 1.000 106.08374 ? 204 ALA D N   1 
ATOM   5421 C CA  . ALA D 1 204 ? -30.86548 25.71627  -17.27605 1.000 99.91449  ? 204 ALA D CA  1 
ATOM   5422 C C   . ALA D 1 204 ? -30.00495 26.50632  -18.25328 1.000 104.93244 ? 204 ALA D C   1 
ATOM   5423 O O   . ALA D 1 204 ? -30.47716 27.47784  -18.85641 1.000 108.21412 ? 204 ALA D O   1 
ATOM   5424 C CB  . ALA D 1 204 ? -32.04712 25.06591  -17.99196 1.000 96.98111  ? 204 ALA D CB  1 
ATOM   5425 N N   . LYS D 1 205 ? -28.74490 26.09885  -18.39971 1.000 91.57896  ? 205 LYS D N   1 
ATOM   5426 C CA  . LYS D 1 205 ? -27.82894 26.80574  -19.28358 1.000 90.61773  ? 205 LYS D CA  1 
ATOM   5427 C C   . LYS D 1 205 ? -28.33763 26.77288  -20.71782 1.000 94.26638  ? 205 LYS D C   1 
ATOM   5428 O O   . LYS D 1 205 ? -28.98487 25.81774  -21.15352 1.000 99.49052  ? 205 LYS D O   1 
ATOM   5429 C CB  . LYS D 1 205 ? -26.42871 26.20227  -19.20759 1.000 90.37995  ? 205 LYS D CB  1 
ATOM   5430 C CG  . LYS D 1 205 ? -25.69759 26.52333  -17.91946 1.000 92.62016  ? 205 LYS D CG  1 
ATOM   5431 C CD  . LYS D 1 205 ? -24.28476 25.97425  -17.93361 1.000 103.33909 ? 205 LYS D CD  1 
ATOM   5432 C CE  . LYS D 1 205 ? -24.16243 24.77692  -17.00782 1.000 97.42062  ? 205 LYS D CE  1 
ATOM   5433 N NZ  . LYS D 1 205 ? -23.64485 25.13491  -15.65824 1.000 109.45866 ? 205 LYS D NZ  1 
ATOM   5434 N N   . LYS D 1 206 ? -28.04360 27.83839  -21.45204 1.000 117.25962 ? 206 LYS D N   1 
ATOM   5435 C CA  . LYS D 1 206 ? -28.53185 28.00459  -22.81133 1.000 119.49686 ? 206 LYS D CA  1 
ATOM   5436 C C   . LYS D 1 206 ? -27.46896 27.54705  -23.80157 1.000 110.69461 ? 206 LYS D C   1 
ATOM   5437 O O   . LYS D 1 206 ? -26.34426 28.05918  -23.80397 1.000 113.35089 ? 206 LYS D O   1 
ATOM   5438 C CB  . LYS D 1 206 ? -28.92039 29.45973  -23.07593 1.000 113.38847 ? 206 LYS D CB  1 
ATOM   5439 C CG  . LYS D 1 206 ? -28.10585 30.47817  -22.29247 1.000 133.34090 ? 206 LYS D CG  1 
ATOM   5440 C CD  . LYS D 1 206 ? -28.24368 31.87224  -22.89057 1.000 146.16348 ? 206 LYS D CD  1 
ATOM   5441 C CE  . LYS D 1 206 ? -27.63438 31.93012  -24.28507 1.000 128.00820 ? 206 LYS D CE  1 
ATOM   5442 N NZ  . LYS D 1 206 ? -28.21746 33.02250  -25.10977 1.000 143.49140 ? 206 LYS D NZ  1 
ATOM   5443 N N   . PHE D 1 207 ? -27.82703 26.56633  -24.62019 1.000 104.54536 ? 207 PHE D N   1 
ATOM   5444 C CA  . PHE D 1 207 ? -26.98031 26.07767  -25.70499 1.000 116.73055 ? 207 PHE D CA  1 
ATOM   5445 C C   . PHE D 1 207 ? -27.74131 26.37400  -26.98550 1.000 123.48906 ? 207 PHE D C   1 
ATOM   5446 O O   . PHE D 1 207 ? -28.67483 25.63129  -27.33887 1.000 129.99637 ? 207 PHE D O   1 
ATOM   5447 C CB  . PHE D 1 207 ? -26.69560 24.58630  -25.55755 1.000 106.82667 ? 207 PHE D CB  1 
ATOM   5448 C CG  . PHE D 1 207 ? -26.02333 24.22613  -24.26614 1.000 103.14358 ? 207 PHE D CG  1 
ATOM   5449 C CD1 . PHE D 1 207 ? -24.65159 24.34811  -24.12789 1.000 102.58560 ? 207 PHE D CD1 1 
ATOM   5450 C CD2 . PHE D 1 207 ? -26.76574 23.79701  -23.17825 1.000 100.61068 ? 207 PHE D CD2 1 
ATOM   5451 C CE1 . PHE D 1 207 ? -24.02902 24.02115  -22.93650 1.000 99.70773  ? 207 PHE D CE1 1 
ATOM   5452 C CE2 . PHE D 1 207 ? -26.14950 23.47403  -21.98364 1.000 97.58338  ? 207 PHE D CE2 1 
ATOM   5453 C CZ  . PHE D 1 207 ? -24.78061 23.58612  -21.86233 1.000 97.18736  ? 207 PHE D CZ  1 
ATOM   5454 N N   . PRO D 1 208 ? -27.38781 27.44362  -27.70790 1.000 128.86193 ? 208 PRO D N   1 
ATOM   5455 C CA  . PRO D 1 208 ? -28.24731 27.93574  -28.79737 1.000 136.97421 ? 208 PRO D CA  1 
ATOM   5456 C C   . PRO D 1 208 ? -28.63252 26.88522  -29.82836 1.000 132.32389 ? 208 PRO D C   1 
ATOM   5457 O O   . PRO D 1 208 ? -29.82316 26.66567  -30.07312 1.000 139.76380 ? 208 PRO D O   1 
ATOM   5458 C CB  . PRO D 1 208 ? -27.40381 29.05013  -29.43706 1.000 147.71396 ? 208 PRO D CB  1 
ATOM   5459 C CG  . PRO D 1 208 ? -26.04090 28.96442  -28.80292 1.000 138.84758 ? 208 PRO D CG  1 
ATOM   5460 C CD  . PRO D 1 208 ? -26.22293 28.31147  -27.48016 1.000 121.41406 ? 208 PRO D CD  1 
ATOM   5461 N N   . GLY D 1 209 ? -27.65052 26.22744  -30.43627 1.000 122.46303 ? 209 GLY D N   1 
ATOM   5462 C CA  . GLY D 1 209 ? -27.98405 25.24067  -31.44475 1.000 126.05697 ? 209 GLY D CA  1 
ATOM   5463 C C   . GLY D 1 209 ? -28.45011 23.90458  -30.91430 1.000 124.72660 ? 209 GLY D C   1 
ATOM   5464 O O   . GLY D 1 209 ? -28.85406 23.04802  -31.70556 1.000 127.99764 ? 209 GLY D O   1 
ATOM   5465 N N   . LEU D 1 210 ? -28.41173 23.70844  -29.59751 1.000 120.35596 ? 210 LEU D N   1 
ATOM   5466 C CA  . LEU D 1 210 ? -28.70433 22.42086  -28.97968 1.000 119.00798 ? 210 LEU D CA  1 
ATOM   5467 C C   . LEU D 1 210 ? -30.12816 22.31273  -28.44504 1.000 122.83748 ? 210 LEU D C   1 
ATOM   5468 O O   . LEU D 1 210 ? -30.85546 21.37871  -28.79650 1.000 121.31980 ? 210 LEU D O   1 
ATOM   5469 C CB  . LEU D 1 210 ? -27.70822 22.17283  -27.84359 1.000 114.92777 ? 210 LEU D CB  1 
ATOM   5470 C CG  . LEU D 1 210 ? -27.50651 20.74896  -27.33985 1.000 113.84100 ? 210 LEU D CG  1 
ATOM   5471 C CD1 . LEU D 1 210 ? -27.08018 19.84212  -28.48084 1.000 117.46822 ? 210 LEU D CD1 1 
ATOM   5472 C CD2 . LEU D 1 210 ? -26.48360 20.74276  -26.21710 1.000 110.03664 ? 210 LEU D CD2 1 
ATOM   5473 N N   . THR D 1 211 ? -30.53946 23.25371  -27.59196 1.000 126.65899 ? 211 THR D N   1 
ATOM   5474 C CA  . THR D 1 211 ? -31.90036 23.24281  -27.06352 1.000 125.42156 ? 211 THR D CA  1 
ATOM   5475 C C   . THR D 1 211 ? -32.92757 23.70051  -28.09509 1.000 147.22805 ? 211 THR D C   1 
ATOM   5476 O O   . THR D 1 211 ? -34.09312 23.29199  -28.02172 1.000 143.26352 ? 211 THR D O   1 
ATOM   5477 C CB  . THR D 1 211 ? -31.97767 24.11326  -25.80908 1.000 122.56820 ? 211 THR D CB  1 
ATOM   5478 O OG1 . THR D 1 211 ? -31.25440 25.33101  -26.02561 1.000 128.09130 ? 211 THR D OG1 1 
ATOM   5479 C CG2 . THR D 1 211 ? -31.37504 23.38180  -24.61866 1.000 108.00816 ? 211 THR D CG2 1 
ATOM   5480 N N   . THR D 1 212 ? -32.52092 24.53913  -29.04900 1.000 158.85775 ? 212 THR D N   1 
ATOM   5481 C CA  . THR D 1 212 ? -33.39938 25.04031  -30.11282 1.000 159.98425 ? 212 THR D CA  1 
ATOM   5482 C C   . THR D 1 212 ? -34.65647 25.71006  -29.55694 1.000 158.98085 ? 212 THR D C   1 
ATOM   5483 O O   . THR D 1 212 ? -34.99332 26.83491  -29.93183 1.000 157.17536 ? 212 THR D O   1 
ATOM   5484 C CB  . THR D 1 212 ? -33.82902 23.91265  -31.08191 1.000 160.63081 ? 212 THR D CB  1 
ATOM   5485 O OG1 . THR D 1 212 ? -32.67136 23.32841  -31.69251 1.000 141.47874 ? 212 THR D OG1 1 
ATOM   5486 C CG2 . THR D 1 212 ? -34.75080 24.46082  -32.16548 1.000 156.19900 ? 212 THR D CG2 1 
HETATM 5487 O O   . HOH E 2 .   ? -48.52164 15.53108  -4.34649  1.000 78.41041  ? 301 HOH A O   1 
HETATM 5488 O O   . HOH E 2 .   ? -4.58443  17.26106  -37.54880 1.000 81.70881  ? 302 HOH A O   1 
HETATM 5489 O O   . HOH E 2 .   ? -27.08705 15.63549  -28.73833 1.000 65.03752  ? 303 HOH A O   1 
HETATM 5490 O O   . HOH E 2 .   ? -19.56974 14.32094  -12.68762 1.000 76.42539  ? 304 HOH A O   1 
HETATM 5491 O O   . HOH E 2 .   ? -2.83979  -0.62645  -33.37661 1.000 92.57216  ? 305 HOH A O   1 
HETATM 5492 O O   . HOH E 2 .   ? -11.230   21.136    -34.893   1.000 73.14552  ? 306 HOH A O   1 
HETATM 5493 O O   . HOH E 2 .   ? -29.92890 2.74105   -20.40978 1.000 65.00807  ? 307 HOH A O   1 
HETATM 5494 O O   . HOH E 2 .   ? -24.00026 18.24879  -9.78171  1.000 73.64584  ? 308 HOH A O   1 
HETATM 5495 O O   . HOH E 2 .   ? -16.11549 10.36302  -14.33360 1.000 68.72292  ? 309 HOH A O   1 
HETATM 5496 O O   . HOH E 2 .   ? -12.61219 -0.24427  -26.27489 1.000 73.31459  ? 310 HOH A O   1 
HETATM 5497 O O   . HOH E 2 .   ? -23.03426 27.23103  -32.85746 1.000 82.61104  ? 311 HOH A O   1 
HETATM 5498 O O   . HOH E 2 .   ? -13.57410 4.87627   -19.31571 1.000 61.49078  ? 312 HOH A O   1 
HETATM 5499 O O   . HOH E 2 .   ? -13.20344 8.34013   -13.21297 1.000 89.16833  ? 313 HOH A O   1 
HETATM 5500 O O   . HOH E 2 .   ? -11.78784 9.82414   -11.64514 1.000 81.17553  ? 314 HOH A O   1 
HETATM 5501 O O   . HOH F 2 .   ? -14.17211 -12.10486 -21.80689 1.000 62.73863  ? 301 HOH B O   1 
HETATM 5502 O O   . HOH F 2 .   ? -32.31429 5.00259   -27.92790 1.000 67.11707  ? 302 HOH B O   1 
HETATM 5503 O O   . HOH F 2 .   ? -18.37445 -0.93592  -19.80404 1.000 53.60876  ? 303 HOH B O   1 
HETATM 5504 O O   . HOH F 2 .   ? -42.69311 -4.87954  -24.30669 1.000 82.39706  ? 304 HOH B O   1 
HETATM 5505 O O   . HOH F 2 .   ? -32.54122 -10.80738 -16.58156 1.000 93.18179  ? 305 HOH B O   1 
HETATM 5506 O O   . HOH F 2 .   ? -24.26920 -20.94595 -18.42382 1.000 68.39672  ? 306 HOH B O   1 
HETATM 5507 O O   . HOH F 2 .   ? -29.04572 -31.76323 -36.21851 1.000 86.14060  ? 307 HOH B O   1 
HETATM 5508 O O   . HOH F 2 .   ? 0.66364   -6.04717  -15.60802 1.000 91.49368  ? 308 HOH B O   1 
HETATM 5509 O O   . HOH F 2 .   ? -9.09962  -1.30768  -22.44187 1.000 68.57385  ? 309 HOH B O   1 
HETATM 5510 O O   . HOH F 2 .   ? 0.19450   -7.13215  -18.06821 1.000 76.23339  ? 310 HOH B O   1 
HETATM 5511 O O   . HOH G 2 .   ? -51.96311 40.60022  12.21160  1.000 67.25825  ? 301 HOH C O   1 
HETATM 5512 O O   . HOH G 2 .   ? -42.88125 53.12244  -4.18501  1.000 72.76046  ? 302 HOH C O   1 
HETATM 5513 O O   . HOH G 2 .   ? -60.28996 48.92339  5.62943   1.000 70.23055  ? 303 HOH C O   1 
HETATM 5514 O O   . HOH G 2 .   ? -47.80443 40.47452  6.70911   1.000 62.68995  ? 304 HOH C O   1 
HETATM 5515 O O   . HOH G 2 .   ? -54.65018 34.23855  -7.96826  1.000 66.20469  ? 305 HOH C O   1 
HETATM 5516 O O   . HOH G 2 .   ? -43.52853 48.33442  -7.17801  1.000 73.90022  ? 306 HOH C O   1 
HETATM 5517 O O   . HOH G 2 .   ? -47.42978 42.13461  -9.56776  1.000 73.33580  ? 307 HOH C O   1 
HETATM 5518 O O   . HOH G 2 .   ? -46.30907 45.69602  23.58767  1.000 97.86164  ? 308 HOH C O   1 
HETATM 5519 O O   . HOH G 2 .   ? -53.38152 35.03658  -10.29298 1.000 82.10188  ? 309 HOH C O   1 
HETATM 5520 O O   . HOH G 2 .   ? -39.01366 57.26945  25.58868  1.000 69.79897  ? 310 HOH C O   1 
HETATM 5521 O O   . HOH G 2 .   ? -57.51392 32.40445  -8.44482  1.000 78.43683  ? 311 HOH C O   1 
HETATM 5522 O O   . HOH G 2 .   ? -42.29473 60.37198  -0.40495  1.000 79.66166  ? 312 HOH C O   1 
HETATM 5523 O O   . HOH G 2 .   ? -42.02933 29.69739  12.74547  1.000 82.85072  ? 313 HOH C O   1 
HETATM 5524 O O   . HOH G 2 .   ? -41.72888 62.43476  0.93925   1.000 73.65393  ? 314 HOH C O   1 
HETATM 5525 O O   . HOH H 2 .   ? -43.80440 38.07296  3.98386   1.000 79.71687  ? 301 HOH D O   1 
HETATM 5526 O O   . HOH H 2 .   ? -41.46357 24.52991  7.31120   1.000 83.65331  ? 302 HOH D O   1 
HETATM 5527 O O   . HOH H 2 .   ? -43.40003 28.97368  9.93777   1.000 69.33524  ? 303 HOH D O   1 
HETATM 5528 O O   . HOH H 2 .   ? -44.50960 36.57127  -3.91382  1.000 58.65633  ? 304 HOH D O   1 
HETATM 5529 O O   . HOH H 2 .   ? -47.19973 36.20202  -4.79279  1.000 54.42212  ? 305 HOH D O   1 
HETATM 5530 O O   . HOH H 2 .   ? -29.26916 22.42849  -6.83816  1.000 70.54013  ? 306 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 15  ? 1.37132 1.42910 1.09291 -0.12679 -0.14679 -0.17560 15  GLY A N   
2    C CA  . GLY A 15  ? 1.50983 1.56757 1.22547 -0.09187 -0.14088 -0.13023 15  GLY A CA  
3    C C   . GLY A 15  ? 1.49264 1.50227 1.23683 -0.07514 -0.10274 -0.11961 15  GLY A C   
4    O O   . GLY A 15  ? 1.43453 1.43001 1.16415 -0.05293 -0.08839 -0.09618 15  GLY A O   
5    N N   . ASN A 16  ? 1.36556 1.35461 1.15438 -0.08617 -0.08530 -0.13606 16  ASN A N   
6    C CA  . ASN A 16  ? 1.17111 1.12813 0.98776 -0.06976 -0.05207 -0.12412 16  ASN A CA  
7    C C   . ASN A 16  ? 1.03181 1.01439 0.90444 -0.05425 -0.05387 -0.09736 16  ASN A C   
8    O O   . ASN A 16  ? 0.94389 0.91474 0.83544 -0.03913 -0.03137 -0.08538 16  ASN A O   
9    C CB  . ASN A 16  ? 1.38166 1.30037 1.21523 -0.08418 -0.02407 -0.14897 16  ASN A CB  
10   C CG  . ASN A 16  ? 1.52551 1.45749 1.40418 -0.10849 -0.03318 -0.16779 16  ASN A CG  
11   O OD1 . ASN A 16  ? 1.42852 1.39059 1.29399 -0.12976 -0.06352 -0.18701 16  ASN A OD1 
12   N ND2 . ASN A 16  ? 1.49540 1.41038 1.43110 -0.10515 -0.00610 -0.16038 16  ASN A ND2 
13   N N   . SER A 17  ? 1.03426 1.05669 0.93325 -0.05671 -0.07933 -0.08735 17  SER A N   
14   C CA  . SER A 17  ? 1.03891 1.08230 0.99401 -0.04500 -0.07538 -0.06710 17  SER A CA  
15   C C   . SER A 17  ? 0.88259 0.96242 0.84912 -0.03298 -0.09557 -0.04450 17  SER A C   
16   O O   . SER A 17  ? 0.89796 0.99832 0.83899 -0.03592 -0.11882 -0.04139 17  SER A O   
17   C CB  . SER A 17  ? 0.92913 0.97982 0.93658 -0.06176 -0.07240 -0.07706 17  SER A CB  
18   O OG  . SER A 17  ? 1.02619 1.11955 1.06201 -0.07539 -0.10150 -0.07845 17  SER A OG  
19   N N   . ASN A 18  ? 0.85176 0.94083 0.85605 -0.01704 -0.08316 -0.02673 18  ASN A N   
20   C CA  . ASN A 18  ? 0.81492 0.93357 0.84697 -0.00326 -0.09219 -0.00367 18  ASN A CA  
21   C C   . ASN A 18  ? 0.75621 0.88532 0.83953 0.00499  -0.07508 0.00495  18  ASN A C   
22   O O   . ASN A 18  ? 0.77789 0.88973 0.85838 0.00807  -0.05338 -0.00168 18  ASN A O   
23   C CB  . ASN A 18  ? 0.78513 0.88772 0.78831 0.01392  -0.08230 0.00845  18  ASN A CB  
24   C CG  . ASN A 18  ? 0.82385 0.95193 0.85907 0.03049  -0.08691 0.03659  18  ASN A CG  
25   O OD1 . ASN A 18  ? 0.75462 0.92253 0.81364 0.02852  -0.11123 0.05021  18  ASN A OD1 
26   N ND2 . ASN A 18  ? 0.71047 0.81835 0.75264 0.04651  -0.06157 0.04502  18  ASN A ND2 
27   N N   . SER A 19  ? 0.84849 1.01126 0.97866 0.01071  -0.08381 0.02275  19  SER A N   
28   C CA  . SER A 19  ? 0.89466 1.06830 1.07399 0.01910  -0.06396 0.03171  19  SER A CA  
29   C C   . SER A 19  ? 0.89844 1.08806 1.10993 0.03881  -0.05645 0.05368  19  SER A C   
30   O O   . SER A 19  ? 0.79302 1.00232 1.01152 0.04466  -0.07449 0.07067  19  SER A O   
31   C CB  . SER A 19  ? 0.82687 1.02525 1.05595 0.00308  -0.07208 0.03033  19  SER A CB  
32   O OG  . SER A 19  ? 1.20949 1.44501 1.45694 -0.00931 -0.10582 0.03265  19  SER A OG  
33   N N   . VAL A 20  ? 0.78462 0.96693 1.01491 0.05083  -0.02645 0.05471  20  VAL A N   
34   C CA  . VAL A 20  ? 0.69843 0.88827 0.96740 0.06956  -0.00811 0.07171  20  VAL A CA  
35   C C   . VAL A 20  ? 0.69023 0.89545 1.00418 0.07420  0.01394  0.07636  20  VAL A C   
36   O O   . VAL A 20  ? 0.85331 1.05597 1.15601 0.06654  0.02154  0.06625  20  VAL A O   
37   C CB  . VAL A 20  ? 0.69623 0.85117 0.93377 0.07946  0.01743  0.05986  20  VAL A CB  
38   C CG1 . VAL A 20  ? 0.81726 0.96162 1.04008 0.07973  0.04653  0.03763  20  VAL A CG1 
39   C CG2 . VAL A 20  ? 0.74861 0.90325 1.02669 0.09837  0.03198  0.08282  20  VAL A CG2 
40   N N   . SER A 21  ? 0.83923 1.06015 1.20741 0.09000  0.02903  0.09631  21  SER A N   
41   C CA  . SER A 21  ? 0.80130 1.03718 1.21713 0.09713  0.05551  0.10395  21  SER A CA  
42   C C   . SER A 21  ? 0.86798 1.08749 1.30219 0.11772  0.09513  0.10634  21  SER A C   
43   O O   . SER A 21  ? 0.81400 1.02336 1.25953 0.12896  0.09787  0.11663  21  SER A O   
44   C CB  . SER A 21  ? 0.82220 1.10536 1.31213 0.09216  0.03536  0.12782  21  SER A CB  
45   O OG  . SER A 21  ? 0.94267 1.25407 1.45265 0.09353  0.00226  0.14589  21  SER A OG  
46   N N   . ARG A 22  ? 0.87452 1.08945 1.31097 0.12337  0.13057  0.09706  22  ARG A N   
47   C CA  . ARG A 22  ? 0.87614 1.07356 1.33140 0.14038  0.17614  0.09211  22  ARG A CA  
48   C C   . ARG A 22  ? 0.88910 1.10447 1.37916 0.14834  0.20675  0.10083  22  ARG A C   
49   O O   . ARG A 22  ? 0.83482 1.07136 1.32747 0.14011  0.19511  0.10891  22  ARG A O   
50   C CB  . ARG A 22  ? 0.77945 0.94079 1.16570 0.13538  0.19610  0.05213  22  ARG A CB  
51   C CG  . ARG A 22  ? 0.91479 1.08198 1.25368 0.13178  0.21698  0.02823  22  ARG A CG  
52   C CD  . ARG A 22  ? 0.90634 1.05713 1.17457 0.12116  0.22413  -0.01452 22  ARG A CD  
53   N NE  . ARG A 22  ? 0.91774 1.09432 1.13225 0.11756  0.22233  -0.02442 22  ARG A NE  
54   C CZ  . ARG A 22  ? 1.05540 1.24272 1.22898 0.11972  0.25242  -0.05131 22  ARG A CZ  
55   N NH1 . ARG A 22  ? 1.04842 1.21540 1.22758 0.12088  0.28968  -0.08064 22  ARG A NH1 
56   N NH2 . ARG A 22  ? 1.14998 1.37051 1.27531 0.12153  0.24770  -0.04843 22  ARG A NH2 
57   N N   . ILE A 23  ? 0.83787 1.04047 1.35807 0.16512  0.25244  0.09962  23  ILE A N   
58   C CA  . ILE A 23  ? 0.86937 1.08716 1.42807 0.17647  0.28982  0.11092  23  ILE A CA  
59   C C   . ILE A 23  ? 0.90535 1.09434 1.40711 0.18124  0.33902  0.07336  23  ILE A C   
60   O O   . ILE A 23  ? 1.01033 1.16644 1.50309 0.18434  0.36247  0.04987  23  ILE A O   
61   C CB  . ILE A 23  ? 1.01871 1.25783 1.68377 0.19454  0.30300  0.14930  23  ILE A CB  
62   C CG1 . ILE A 23  ? 0.97506 1.26453 1.69981 0.18512  0.25637  0.18247  23  ILE A CG1 
63   C CG2 . ILE A 23  ? 0.94470 1.18105 1.64291 0.21129  0.36241  0.15158  23  ILE A CG2 
64   C CD1 . ILE A 23  ? 0.79600 1.11864 1.60433 0.19749  0.23683  0.21903  23  ILE A CD1 
65   N N   . THR A 24  ? 1.00933 1.21209 1.47228 0.18112  0.35657  0.06682  24  THR A N   
66   C CA  . THR A 24  ? 1.11215 1.30179 1.50534 0.18326  0.39775  0.02769  24  THR A CA  
67   C C   . THR A 24  ? 1.20817 1.38853 1.64791 0.20184  0.45788  0.03105  24  THR A C   
68   O O   . THR A 24  ? 1.17191 1.36140 1.70427 0.21496  0.46676  0.06952  24  THR A O   
69   C CB  . THR A 24  ? 1.11350 1.33034 1.43546 0.17964  0.39045  0.02553  24  THR A CB  
70   O OG1 . THR A 24  ? 1.19802 1.43727 1.57193 0.19002  0.40044  0.06797  24  THR A OG1 
71   C CG2 . THR A 24  ? 1.06966 1.29267 1.34948 0.16355  0.33786  0.02169  24  THR A CG2 
72   N N   . ARG A 25  ? 1.19937 1.36642 1.57401 0.20214  0.50033  -0.01190 25  ARG A N   
73   C CA  . ARG A 25  ? 1.21321 1.36413 1.62177 0.21919  0.56636  -0.01722 25  ARG A CA  
74   C C   . ARG A 25  ? 1.33043 1.51182 1.77769 0.23570  0.58653  0.02608  25  ARG A C   
75   O O   . ARG A 25  ? 1.45675 1.63104 1.98138 0.25367  0.63073  0.04673  25  ARG A O   
76   C CB  . ARG A 25  ? 1.45694 1.59192 1.77278 0.21049  0.60537  -0.08226 25  ARG A CB  
77   C CG  . ARG A 25  ? 1.59364 1.69232 1.89122 0.19189  0.59890  -0.13012 25  ARG A CG  
78   C CD  . ARG A 25  ? 1.72780 1.82151 1.93205 0.17526  0.63154  -0.20414 25  ARG A CD  
79   N NE  . ARG A 25  ? 1.87433 1.92955 2.07698 0.15388  0.63178  -0.25300 25  ARG A NE  
80   C CZ  . ARG A 25  ? 2.02221 2.08334 2.14501 0.12752  0.63548  -0.32336 25  ARG A CZ  
81   N NH1 . ARG A 25  ? 2.07866 2.18909 2.10683 0.12134  0.63572  -0.35255 25  ARG A NH1 
82   N NH2 . ARG A 25  ? 2.04678 2.06865 2.18625 0.10628  0.63414  -0.36108 25  ARG A NH2 
83   N N   . GLU A 26  ? 1.39603 1.61028 1.79887 0.23143  0.55999  0.04322  26  GLU A N   
84   C CA  . GLU A 26  ? 1.39110 1.63169 1.83569 0.24555  0.58206  0.08725  26  GLU A CA  
85   C C   . GLU A 26  ? 1.26793 1.52416 1.83155 0.24451  0.55328  0.13564  26  GLU A C   
86   O O   . GLU A 26  ? 1.06740 1.34733 1.67940 0.25036  0.56574  0.17245  26  GLU A O   
87   C CB  . GLU A 26  ? 1.57986 1.84782 1.93938 0.24375  0.56949  0.09309  26  GLU A CB  
88   C CG  . GLU A 26  ? 1.73019 2.00341 1.96364 0.24126  0.58182  0.04465  26  GLU A CG  
89   C CD  . GLU A 26  ? 1.90569 2.21443 2.07053 0.25726  0.60984  0.06336  26  GLU A CD  
90   O OE1 . GLU A 26  ? 1.91908 2.22857 2.08105 0.27429  0.66828  0.06610  26  GLU A OE1 
91   O OE2 . GLU A 26  ? 1.90616 2.24256 2.02099 0.25553  0.57698  0.07909  26  GLU A OE2 
92   N N   . GLY A 27  ? 1.17777 1.42570 1.79058 0.23673  0.51692  0.13629  27  GLY A N   
93   C CA  . GLY A 27  ? 1.12842 1.40426 1.84380 0.23200  0.47943  0.17613  27  GLY A CA  
94   C C   . GLY A 27  ? 1.23852 1.53058 1.93255 0.21033  0.42105  0.18196  27  GLY A C   
95   O O   . GLY A 27  ? 1.13001 1.44998 1.90261 0.20055  0.38586  0.20700  27  GLY A O   
96   N N   . LYS A 28  ? 1.09206 1.37126 1.68468 0.20220  0.41063  0.15813  28  LYS A N   
97   C CA  . LYS A 28  ? 1.11844 1.40613 1.68887 0.18431  0.36512  0.16330  28  LYS A CA  
98   C C   . LYS A 28  ? 0.96423 1.24505 1.53643 0.16901  0.31244  0.15173  28  LYS A C   
99   O O   . LYS A 28  ? 0.97624 1.23600 1.51424 0.17149  0.31115  0.12867  28  LYS A O   
100  C CB  . LYS A 28  ? 1.19252 1.47470 1.65739 0.18622  0.37354  0.14661  28  LYS A CB  
101  C CG  . LYS A 28  ? 1.20587 1.50349 1.66488 0.20123  0.41708  0.17149  28  LYS A CG  
102  C CD  . LYS A 28  ? 1.41518 1.71962 1.75864 0.20958  0.42774  0.15443  28  LYS A CD  
103  C CE  . LYS A 28  ? 1.33728 1.65406 1.65988 0.20951  0.41396  0.18142  28  LYS A CE  
104  N NZ  . LYS A 28  ? 1.36736 1.70833 1.62835 0.23267  0.45478  0.20178  28  LYS A NZ  
105  N N   . LYS A 29  ? 1.03793 1.33544 1.65036 0.15217  0.27267  0.16620  29  LYS A N   
106  C CA  . LYS A 29  ? 0.88246 1.17755 1.48545 0.13716  0.22194  0.15639  29  LYS A CA  
107  C C   . LYS A 29  ? 0.83842 1.11663 1.36566 0.12313  0.19927  0.13897  29  LYS A C   
108  O O   . LYS A 29  ? 0.87505 1.15983 1.41747 0.11246  0.19443  0.14856  29  LYS A O   
109  C CB  . LYS A 29  ? 0.81505 1.14763 1.51032 0.12537  0.19039  0.17820  29  LYS A CB  
110  C CG  . LYS A 29  ? 0.65376 0.99060 1.32989 0.11076  0.13781  0.16937  29  LYS A CG  
111  C CD  . LYS A 29  ? 0.96097 1.34855 1.72040 0.09430  0.10209  0.18535  29  LYS A CD  
112  C CE  . LYS A 29  ? 1.04329 1.44870 1.78947 0.08907  0.05472  0.18505  29  LYS A CE  
113  N NZ  . LYS A 29  ? 1.12977 1.58812 1.92914 0.06275  0.01032  0.18615  29  LYS A NZ  
114  N N   . ILE A 30  ? 0.80754 1.06313 1.26230 0.12319  0.18937  0.11423  30  ILE A N   
115  C CA  . ILE A 30  ? 0.75448 0.99710 1.13777 0.11378  0.17156  0.09822  30  ILE A CA  
116  C C   . ILE A 30  ? 0.84445 1.07817 1.22187 0.09863  0.12878  0.09004  30  ILE A C   
117  O O   . ILE A 30  ? 0.86067 1.08751 1.24221 0.10153  0.12037  0.08508  30  ILE A O   
118  C CB  . ILE A 30  ? 0.63668 0.87020 0.94339 0.12256  0.19204  0.07343  30  ILE A CB  
119  C CG1 . ILE A 30  ? 0.79693 1.04563 1.09222 0.13833  0.23466  0.08062  30  ILE A CG1 
120  C CG2 . ILE A 30  ? 0.69399 0.92314 0.93815 0.11383  0.16876  0.06021  30  ILE A CG2 
121  C CD1 . ILE A 30  ? 0.91729 1.18054 1.26187 0.14231  0.24823  0.11540  30  ILE A CD1 
122  N N   . THR A 31  ? 0.82083 1.05251 1.18980 0.08397  0.10703  0.09035  31  THR A N   
123  C CA  . THR A 31  ? 0.79633 1.01895 1.14822 0.06837  0.06943  0.07966  31  THR A CA  
124  C C   . THR A 31  ? 0.72205 0.92296 1.00498 0.06549  0.06644  0.06367  31  THR A C   
125  O O   . THR A 31  ? 0.76455 0.96448 1.03628 0.06789  0.08190  0.06940  31  THR A O   
126  C CB  . THR A 31  ? 0.85105 1.09031 1.25694 0.04915  0.04761  0.08653  31  THR A CB  
127  O OG1 . THR A 31  ? 0.84852 1.11822 1.33198 0.05280  0.05857  0.10560  31  THR A OG1 
128  C CG2 . THR A 31  ? 0.76692 1.00980 1.15941 0.03540  0.00760  0.07660  31  THR A CG2 
129  N N   . TYR A 32  ? 0.64421 0.83030 0.88706 0.06299  0.05006  0.04842  32  TYR A N   
130  C CA  . TYR A 32  ? 0.64051 0.81028 0.82713 0.05918  0.04441  0.03364  32  TYR A CA  
131  C C   . TYR A 32  ? 0.76342 0.91975 0.94405 0.04330  0.01718  0.02891  32  TYR A C   
132  O O   . TYR A 32  ? 0.80155 0.96038 0.99270 0.03862  -0.00216 0.03003  32  TYR A O   
133  C CB  . TYR A 32  ? 0.66950 0.83137 0.81849 0.06494  0.05102  0.01570  32  TYR A CB  
134  C CG  . TYR A 32  ? 0.65438 0.82903 0.80241 0.07652  0.07932  0.00947  32  TYR A CG  
135  C CD1 . TYR A 32  ? 0.65009 0.82407 0.83643 0.08378  0.09449  0.01427  32  TYR A CD1 
136  C CD2 . TYR A 32  ? 0.72458 0.91649 0.83243 0.08120  0.09225  -0.00116 32  TYR A CD2 
137  C CE1 . TYR A 32  ? 0.69837 0.87933 0.87999 0.09308  0.12623  0.00298  32  TYR A CE1 
138  C CE2 . TYR A 32  ? 0.77371 0.98211 0.86993 0.08949  0.11810  -0.01292 32  TYR A CE2 
139  C CZ  . TYR A 32  ? 0.71855 0.91667 0.85007 0.09422  0.13725  -0.01381 32  TYR A CZ  
140  O OH  . TYR A 32  ? 0.73897 0.94881 0.85529 0.10127  0.16867  -0.03088 32  TYR A OH  
141  N N   . LYS A 33  ? 0.67305 0.81723 0.83647 0.03687  0.01849  0.02544  33  LYS A N   
142  C CA  . LYS A 33  ? 0.73289 0.85910 0.88395 0.02004  -0.00074 0.01420  33  LYS A CA  
143  C C   . LYS A 33  ? 0.78735 0.89360 0.89082 0.02340  0.00513  0.00516  33  LYS A C   
144  O O   . LYS A 33  ? 0.85746 0.96694 0.95622 0.03388  0.02435  0.01320  33  LYS A O   
145  C CB  . LYS A 33  ? 0.81645 0.94120 1.00958 0.00485  0.00178  0.01527  33  LYS A CB  
146  C CG  . LYS A 33  ? 0.86801 0.97316 1.04664 -0.01751 -0.01483 -0.00585 33  LYS A CG  
147  C CD  . LYS A 33  ? 1.00273 1.09877 1.22983 -0.03548 -0.00137 -0.01136 33  LYS A CD  
148  C CE  . LYS A 33  ? 1.05810 1.12259 1.26336 -0.05772 -0.00472 -0.03960 33  LYS A CE  
149  N NZ  . LYS A 33  ? 1.09826 1.17925 1.33707 -0.09027 -0.02673 -0.06465 33  LYS A NZ  
150  N N   . LEU A 34  ? 0.82671 0.91784 0.89748 0.01701  -0.00998 -0.00714 34  LEU A N   
151  C CA  . LEU A 34  ? 0.73429 0.80716 0.76689 0.01883  -0.00396 -0.01581 34  LEU A CA  
152  C C   . LEU A 34  ? 0.71925 0.76648 0.73747 0.00314  -0.01142 -0.02788 34  LEU A C   
153  O O   . LEU A 34  ? 0.83574 0.88381 0.84851 -0.00875 -0.03134 -0.03478 34  LEU A O   
154  C CB  . LEU A 34  ? 0.65261 0.72434 0.65971 0.02414  -0.00668 -0.02194 34  LEU A CB  
155  C CG  . LEU A 34  ? 0.76995 0.86173 0.78007 0.03497  0.00648  -0.02385 34  LEU A CG  
156  C CD1 . LEU A 34  ? 0.57552 0.65646 0.57028 0.03403  0.00839  -0.03529 34  LEU A CD1 
157  C CD2 . LEU A 34  ? 0.72781 0.83700 0.73094 0.04197  0.01808  -0.02156 34  LEU A CD2 
158  N N   . ASN A 35  ? 0.74568 0.77390 0.75716 0.00414  0.00591  -0.03011 35  ASN A N   
159  C CA  . ASN A 35  ? 0.72521 0.72145 0.72338 -0.01190 0.00809  -0.04736 35  ASN A CA  
160  C C   . ASN A 35  ? 0.84671 0.82237 0.81917 -0.00302 0.02608  -0.04856 35  ASN A C   
161  O O   . ASN A 35  ? 0.73283 0.71790 0.72197 0.01340  0.04524  -0.03176 35  ASN A O   
162  C CB  . ASN A 35  ? 0.99404 0.97943 1.03511 -0.02241 0.02282  -0.04871 35  ASN A CB  
163  C CG  . ASN A 35  ? 1.10019 1.06419 1.13571 -0.05090 0.01384  -0.07905 35  ASN A CG  
164  O OD1 . ASN A 35  ? 1.20123 1.16291 1.19192 -0.06016 -0.00570 -0.09586 35  ASN A OD1 
165  N ND2 . ASN A 35  ? 1.27780 1.22781 1.35898 -0.06602 0.03034  -0.08744 35  ASN A ND2 
166  N N   . ILE A 36  ? 0.85785 0.81216 0.79057 -0.01157 0.02040  -0.06476 36  ILE A N   
167  C CA  . ILE A 36  ? 0.83588 0.76836 0.74885 -0.00435 0.04089  -0.06680 36  ILE A CA  
168  C C   . ILE A 36  ? 0.96594 0.86165 0.88989 -0.01259 0.06556  -0.07793 36  ILE A C   
169  O O   . ILE A 36  ? 1.06144 0.93244 0.96578 -0.03396 0.06139  -0.10393 36  ILE A O   
170  C CB  . ILE A 36  ? 0.87294 0.79346 0.73897 -0.00850 0.03235  -0.07719 36  ILE A CB  
171  C CG1 . ILE A 36  ? 0.88443 0.83275 0.75006 -0.00127 0.01509  -0.06591 36  ILE A CG1 
172  C CG2 . ILE A 36  ? 0.92668 0.82594 0.78064 -0.00045 0.05815  -0.07794 36  ILE A CG2 
173  C CD1 . ILE A 36  ? 0.76479 0.69956 0.59207 -0.00079 0.01471  -0.06754 36  ILE A CD1 
174  N N   . MET A 37  ? 0.88623 0.78092 0.84326 0.00429  0.09306  -0.05863 37  MET A N   
175  C CA  . MET A 37  ? 0.98006 0.83153 0.95819 -0.00054 0.12688  -0.06589 37  MET A CA  
176  C C   . MET A 37  ? 1.06862 0.88920 1.02764 0.00569  0.15259  -0.07189 37  MET A C   
177  O O   . MET A 37  ? 1.18902 0.95992 1.14516 -0.00784 0.17861  -0.09517 37  MET A O   
178  C CB  . MET A 37  ? 1.07992 0.94277 1.11402 0.01855  0.15175  -0.03320 37  MET A CB  
179  C CG  . MET A 37  ? 0.90758 0.81856 0.95680 0.02689  0.13061  -0.01277 37  MET A CG  
180  S SD  . MET A 37  ? 1.20498 1.09841 1.28035 -0.00188 0.12308  -0.03404 37  MET A SD  
181  C CE  . MET A 37  ? 1.30636 1.18844 1.44907 0.01505  0.16892  0.00030  37  MET A CE  
182  N N   . GLN A 38  ? 0.96320 0.81178 0.91253 0.02352  0.14860  -0.05519 38  GLN A N   
183  C CA  . GLN A 38  ? 0.90624 0.73212 0.84415 0.03111  0.17395  -0.05755 38  GLN A CA  
184  C C   . GLN A 38  ? 0.96453 0.80033 0.85724 0.02487  0.15266  -0.06923 38  GLN A C   
185  O O   . GLN A 38  ? 0.81790 0.69776 0.71958 0.03426  0.13546  -0.05475 38  GLN A O   
186  C CB  . GLN A 38  ? 0.91970 0.77692 0.90607 0.06079  0.19640  -0.02062 38  GLN A CB  
187  C CG  . GLN A 38  ? 0.95968 0.79799 0.94945 0.07141  0.22721  -0.01834 38  GLN A CG  
188  C CD  . GLN A 38  ? 1.00392 0.85187 1.05371 0.10003  0.26421  0.01829  38  GLN A CD  
189  O OE1 . GLN A 38  ? 1.18765 0.97971 1.25592 0.10127  0.30539  0.01479  38  GLN A OE1 
190  N NE2 . GLN A 38  ? 0.97392 0.89618 1.05653 0.12362  0.25144  0.05394  38  GLN A NE2 
191  N N   . GLN A 39  ? 1.03698 0.83268 0.88049 0.00771  0.15530  -0.09678 39  GLN A N   
192  C CA  . GLN A 39  ? 1.07848 0.87618 0.87583 0.00428  0.14281  -0.10268 39  GLN A CA  
193  C C   . GLN A 39  ? 1.11725 0.90603 0.92046 0.01806  0.17333  -0.09399 39  GLN A C   
194  O O   . GLN A 39  ? 1.15925 0.92272 0.98245 0.02526  0.20773  -0.09370 39  GLN A O   
195  C CB  . GLN A 39  ? 1.12288 0.89032 0.85839 -0.01676 0.13425  -0.13174 39  GLN A CB  
196  C CG  . GLN A 39  ? 1.29543 1.08506 1.02798 -0.03190 0.09804  -0.13947 39  GLN A CG  
197  C CD  . GLN A 39  ? 1.17808 0.99956 0.88621 -0.02883 0.06671  -0.12602 39  GLN A CD  
198  O OE1 . GLN A 39  ? 1.15430 0.97396 0.84154 -0.01817 0.07440  -0.11423 39  GLN A OE1 
199  N NE2 . GLN A 39  ? 1.08550 0.93539 0.80374 -0.03717 0.03570  -0.12528 39  GLN A NE2 
200  N N   . PRO A 40  ? 1.20999 1.01765 1.00377 0.02213  0.16600  -0.08587 40  PRO A N   
201  C CA  . PRO A 40  ? 1.04022 0.83650 0.83828 0.03124  0.19726  -0.08085 40  PRO A CA  
202  C C   . PRO A 40  ? 1.12832 0.87017 0.86328 0.02303  0.22007  -0.10061 40  PRO A C   
203  O O   . PRO A 40  ? 1.19192 0.91876 0.86952 0.00924  0.20165  -0.11649 40  PRO A O   
204  C CB  . PRO A 40  ? 1.20236 1.03140 1.01129 0.03254  0.18287  -0.07067 40  PRO A CB  
205  C CG  . PRO A 40  ? 1.06253 0.89491 0.83983 0.02272  0.15010  -0.07508 40  PRO A CG  
206  C CD  . PRO A 40  ? 1.08617 0.92310 0.87331 0.01863  0.13483  -0.08036 40  PRO A CD  
207  N N   . LYS A 41  ? 0.99334 0.71137 0.73839 0.03226  0.26084  -0.09924 41  LYS A N   
208  C CA  . LYS A 41  ? 1.24890 0.91366 0.92702 0.02500  0.28884  -0.12093 41  LYS A CA  
209  C C   . LYS A 41  ? 1.29224 0.94970 0.96252 0.03511  0.31801  -0.10884 41  LYS A C   
210  O O   . LYS A 41  ? 1.35378 0.98389 0.95203 0.02976  0.32643  -0.11838 41  LYS A O   
211  C CB  . LYS A 41  ? 1.22418 0.84563 0.91305 0.02431  0.32612  -0.13867 41  LYS A CB  
212  C CG  . LYS A 41  ? 1.42430 1.05624 1.15648 0.02067  0.31070  -0.13922 41  LYS A CG  
213  C CD  . LYS A 41  ? 1.55004 1.14098 1.23871 -0.00401 0.31031  -0.17891 41  LYS A CD  
214  C CE  . LYS A 41  ? 1.60771 1.21666 1.35235 -0.00637 0.29375  -0.17152 41  LYS A CE  
215  N NZ  . LYS A 41  ? 1.52402 1.14062 1.23289 -0.03308 0.25472  -0.19806 41  LYS A NZ  
216  N N   . ARG A 42  ? 1.13959 0.82712 0.88396 0.04980  0.33379  -0.08643 42  ARG A N   
217  C CA  . ARG A 42  ? 1.09101 0.77034 0.84617 0.05890  0.37112  -0.07572 42  ARG A CA  
218  C C   . ARG A 42  ? 1.23214 0.97422 1.07885 0.06738  0.36383  -0.05283 42  ARG A C   
219  O O   . ARG A 42  ? 1.12454 0.91261 1.02488 0.07145  0.34064  -0.04449 42  ARG A O   
220  C CB  . ARG A 42  ? 1.38078 1.01395 1.13279 0.06750  0.42446  -0.08366 42  ARG A CB  
221  C CG  . ARG A 42  ? 1.35233 0.99664 1.17132 0.07827  0.43354  -0.07657 42  ARG A CG  
222  C CD  . ARG A 42  ? 1.39139 0.97484 1.20272 0.08499  0.49071  -0.08987 42  ARG A CD  
223  N NE  . ARG A 42  ? 1.48135 1.02486 1.24884 0.08644  0.53322  -0.09829 42  ARG A NE  
224  C CZ  . ARG A 42  ? 1.55296 1.11655 1.37597 0.10294  0.56443  -0.07359 42  ARG A CZ  
225  N NH1 . ARG A 42  ? 1.59908 1.23154 1.52222 0.11712  0.55151  -0.04145 42  ARG A NH1 
226  N NH2 . ARG A 42  ? 1.39046 0.90975 1.16782 0.10468  0.60981  -0.08178 42  ARG A NH2 
227  N N   . ALA A 43  ? 1.18100 0.92783 1.04557 0.06931  0.38618  -0.04355 43  ALA A N   
228  C CA  . ALA A 43  ? 1.15927 0.96974 1.11713 0.07247  0.38449  -0.02896 43  ALA A CA  
229  C C   . ALA A 43  ? 1.11933 0.91341 1.09508 0.07580  0.42990  -0.02102 43  ALA A C   
230  O O   . ALA A 43  ? 1.11845 0.85679 1.02443 0.07435  0.45302  -0.02399 43  ALA A O   
231  C CB  . ALA A 43  ? 1.17686 1.03146 1.15347 0.05935  0.34166  -0.03252 43  ALA A CB  
232  N N   . ARG A 44  ? 1.05280 0.90197 1.12343 0.08106  0.44287  -0.00888 44  ARG A N   
233  C CA  . ARG A 44  ? 1.17847 1.02244 1.28791 0.08276  0.48770  0.00016  44  ARG A CA  
234  C C   . ARG A 44  ? 1.11870 1.00912 1.28381 0.06483  0.47009  -0.00361 44  ARG A C   
235  O O   . ARG A 44  ? 1.01594 0.98128 1.24702 0.05666  0.43458  -0.00905 44  ARG A O   
236  C CB  . ARG A 44  ? 0.94691 0.82429 1.13742 0.09986  0.52018  0.01642  44  ARG A CB  
237  C CG  . ARG A 44  ? 1.09926 0.97224 1.33785 0.10130  0.57103  0.02663  44  ARG A CG  
238  C CD  . ARG A 44  ? 1.23170 1.14146 1.55958 0.12103  0.60712  0.04687  44  ARG A CD  
239  N NE  . ARG A 44  ? 1.32915 1.35190 1.77590 0.11733  0.57727  0.05641  44  ARG A NE  
240  C CZ  . ARG A 44  ? 1.39504 1.48574 1.89127 0.13138  0.54948  0.07060  44  ARG A CZ  
241  N NH1 . ARG A 44  ? 1.39976 1.44911 1.84712 0.14988  0.55236  0.07775  44  ARG A NH1 
242  N NH2 . ARG A 44  ? 1.37869 1.58491 1.97775 0.12641  0.51976  0.07801  44  ARG A NH2 
243  N N   . ALA A 45  ? 1.11961 0.96538 1.25654 0.05864  0.49753  -0.00139 45  ALA A N   
244  C CA  . ALA A 45  ? 1.13002 1.00494 1.32478 0.03993  0.49239  -0.00694 45  ALA A CA  
245  C C   . ALA A 45  ? 1.19336 1.14823 1.51339 0.03110  0.49849  -0.01027 45  ALA A C   
246  O O   . ALA A 45  ? 1.38612 1.34360 1.75030 0.04053  0.53989  0.00315  45  ALA A O   
247  C CB  . ALA A 45  ? 1.23313 1.04162 1.38563 0.04131  0.53600  0.00645  45  ALA A CB  
248  N N   . CYS A 46  ? 1.04132 1.06688 1.41906 0.01243  0.45723  -0.02963 46  CYS A N   
249  C CA  . CYS A 46  ? 1.05157 1.17627 1.54658 0.00046  0.44894  -0.03835 46  CYS A CA  
250  C C   . CYS A 46  ? 1.30948 1.44624 1.88778 -0.02396 0.48091  -0.05085 46  CYS A C   
251  O O   . CYS A 46  ? 1.45849 1.67873 2.14355 -0.03533 0.48276  -0.05762 46  CYS A O   
252  C CB  . CYS A 46  ? 1.05139 1.25580 1.56330 -0.01039 0.38893  -0.05821 46  CYS A CB  
253  S SG  . CYS A 46  ? 1.02333 1.19364 1.48443 -0.03272 0.36177  -0.08662 46  CYS A SG  
254  N N   . GLY A 47  ? 1.23977 1.29972 1.77891 -0.03159 0.50801  -0.05153 47  GLY A N   
255  C CA  . GLY A 47  ? 1.29606 1.35705 1.92060 -0.05535 0.54655  -0.06202 47  GLY A CA  
256  C C   . GLY A 47  ? 1.55217 1.69588 2.26576 -0.09142 0.51301  -0.10450 47  GLY A C   
257  O O   . GLY A 47  ? 1.56101 1.74110 2.24495 -0.09680 0.46139  -0.12436 47  GLY A O   
258  N N   . GLN A 48  ? 1.68389 1.86491 2.51220 -0.11801 0.54369  -0.12154 48  GLN A N   
259  C CA  . GLN A 48  ? 1.68862 1.95532 2.61207 -0.15972 0.51682  -0.17198 48  GLN A CA  
260  C C   . GLN A 48  ? 1.83109 2.20869 2.87860 -0.17493 0.51624  -0.18230 48  GLN A C   
261  O O   . GLN A 48  ? 1.87331 2.25487 2.93512 -0.14987 0.54008  -0.14639 48  GLN A O   
262  C CB  . GLN A 48  ? 1.65970 1.86362 2.61767 -0.18795 0.55696  -0.19446 48  GLN A CB  
263  C CG  . GLN A 48  ? 1.67656 1.78988 2.52788 -0.17376 0.55223  -0.18463 48  GLN A CG  
264  C CD  . GLN A 48  ? 1.73849 1.73811 2.52285 -0.14374 0.60677  -0.13410 48  GLN A CD  
265  O OE1 . GLN A 48  ? 1.58073 1.56183 2.38333 -0.13054 0.64917  -0.10547 48  GLN A OE1 
266  N NE2 . GLN A 48  ? 1.69509 1.62342 2.40009 -0.13090 0.60640  -0.12062 48  GLN A NE2 
267  N N   . GLY A 49  ? 1.95794 2.43033 3.09849 -0.21717 0.48989  -0.23365 49  GLY A N   
268  C CA  . GLY A 49  ? 1.98491 2.58301 3.25582 -0.23772 0.48255  -0.24914 49  GLY A CA  
269  C C   . GLY A 49  ? 2.05987 2.79336 3.33280 -0.23481 0.40855  -0.26066 49  GLY A C   
270  O O   . GLY A 49  ? 2.10926 2.83367 3.28398 -0.21826 0.36660  -0.25824 49  GLY A O   
271  N N   . SER A 50  ? 1.93654 2.79445 3.31463 -0.24768 0.39035  -0.26720 50  SER A N   
272  C CA  . SER A 50  ? 1.91139 2.92354 3.31077 -0.24368 0.32290  -0.27208 50  SER A CA  
273  C C   . SER A 50  ? 1.98761 2.99287 3.31743 -0.18513 0.31224  -0.20835 50  SER A C   
274  O O   . SER A 50  ? 2.00761 3.08441 3.29102 -0.16987 0.25755  -0.20271 50  SER A O   
275  C CB  . SER A 50  ? 1.64055 2.77353 3.14547 -0.26452 0.30136  -0.28083 50  SER A CB  
276  O OG  . SER A 50  ? 1.52179 2.67751 3.07273 -0.22753 0.32558  -0.22199 50  SER A OG  
277  N N   . LYS A 51  ? 1.90824 2.82144 3.22205 -0.15085 0.36593  -0.15933 51  LYS A N   
278  C CA  . LYS A 51  ? 1.87596 2.75869 3.11455 -0.09708 0.36305  -0.10357 51  LYS A CA  
279  C C   . LYS A 51  ? 2.13353 2.90421 3.22543 -0.08175 0.35122  -0.10144 51  LYS A C   
280  O O   . LYS A 51  ? 2.17133 2.94104 3.20198 -0.04614 0.33138  -0.06874 51  LYS A O   
281  C CB  . LYS A 51  ? 1.67757 2.49268 2.94097 -0.06839 0.42922  -0.05985 51  LYS A CB  
282  C CG  . LYS A 51  ? 1.44753 2.38087 2.81664 -0.04429 0.42830  -0.02305 51  LYS A CG  
283  C CD  . LYS A 51  ? 1.25110 2.30346 2.74048 -0.08265 0.40865  -0.05155 51  LYS A CD  
284  C CE  . LYS A 51  ? 1.24627 2.42178 2.81683 -0.05612 0.39297  -0.01085 51  LYS A CE  
285  N NZ  . LYS A 51  ? 1.23021 2.52219 2.91025 -0.09519 0.37229  -0.03794 51  LYS A NZ  
286  N N   . SER A 52  ? 2.49968 3.17745 3.54224 -0.10669 0.36632  -0.13264 52  SER A N   
287  C CA  . SER A 52  ? 2.77432 3.35029 3.68641 -0.09265 0.35622  -0.12893 52  SER A CA  
288  C C   . SER A 52  ? 2.88048 3.52590 3.75432 -0.09516 0.29322  -0.14614 52  SER A C   
289  O O   . SER A 52  ? 2.59658 3.17785 3.36995 -0.07515 0.27976  -0.13279 52  SER A O   
290  C CB  . SER A 52  ? 2.59483 3.06875 3.47889 -0.11619 0.38904  -0.15238 52  SER A CB  
291  O OG  . SER A 52  ? 2.37953 2.91046 3.32407 -0.15954 0.36960  -0.20471 52  SER A OG  
292  N N   . HIS A 53  ? 2.67033 3.44924 3.62131 -0.12025 0.25507  -0.17653 53  HIS A N   
293  C CA  . HIS A 53  ? 2.55738 3.41596 3.47136 -0.12235 0.19663  -0.19294 53  HIS A CA  
294  C C   . HIS A 53  ? 2.47692 3.44941 3.41363 -0.08893 0.16419  -0.15199 53  HIS A C   
295  O O   . HIS A 53  ? 2.43831 3.48311 3.33919 -0.08328 0.11752  -0.15501 53  HIS A O   
296  C CB  . HIS A 53  ? 2.51102 3.44913 3.48171 -0.17457 0.17290  -0.26031 53  HIS A CB  
297  C CG  . HIS A 53  ? 2.44245 3.26973 3.40105 -0.20614 0.20945  -0.29894 53  HIS A CG  
298  N ND1 . HIS A 53  ? 2.27834 3.10534 3.33280 -0.24437 0.24498  -0.33329 53  HIS A ND1 
299  C CD2 . HIS A 53  ? 2.30261 3.01799 3.17259 -0.20297 0.21941  -0.30416 53  HIS A CD2 
300  C CE1 . HIS A 53  ? 2.17566 2.89016 3.19926 -0.26098 0.27850  -0.35500 53  HIS A CE1 
301  N NE2 . HIS A 53  ? 2.26740 2.91624 3.17923 -0.23534 0.26189  -0.33676 53  HIS A NE2 
302  N N   . THR A 54  ? 2.43273 3.42329 3.42972 -0.06376 0.19185  -0.10991 54  THR A N   
303  C CA  . THR A 54  ? 2.33573 3.43444 3.36651 -0.02632 0.16824  -0.06198 54  THR A CA  
304  C C   . THR A 54  ? 2.33357 3.35653 3.35598 0.02047  0.21474  -0.00218 54  THR A C   
305  O O   . THR A 54  ? 2.34432 3.44169 3.39664 0.05820  0.20488  0.04595  54  THR A O   
306  C CB  . THR A 54  ? 2.20723 3.47831 3.36647 -0.04616 0.14297  -0.07437 54  THR A CB  
307  O OG1 . THR A 54  ? 2.12401 3.36622 3.35889 -0.08216 0.18062  -0.10731 54  THR A OG1 
308  C CG2 . THR A 54  ? 2.10491 3.50095 3.25800 -0.07546 0.07869  -0.11845 54  THR A CG2 
309  N N   . ASP A 55  ? 2.30307 3.18351 3.28584 0.02061  0.26763  -0.00265 55  ASP A N   
310  C CA  . ASP A 55  ? 2.16954 2.97261 3.14041 0.06031  0.31789  0.04424  55  ASP A CA  
311  C C   . ASP A 55  ? 2.07677 2.71589 2.92541 0.06477  0.34596  0.03834  55  ASP A C   
312  O O   . ASP A 55  ? 2.09587 2.63931 2.92559 0.07203  0.39913  0.04666  55  ASP A O   
313  C CB  . ASP A 55  ? 2.03569 2.85821 3.10851 0.05773  0.36399  0.05386  55  ASP A CB  
314  C CG  . ASP A 55  ? 2.02190 2.81786 3.11729 0.10385  0.41008  0.10747  55  ASP A CG  
315  O OD1 . ASP A 55  ? 2.07483 2.82205 3.10234 0.13536  0.41077  0.13365  55  ASP A OD1 
316  O OD2 . ASP A 55  ? 1.91896 2.73978 3.10570 0.10787  0.45053  0.12233  55  ASP A OD2 
317  N N   . ARG A 56  ? 1.96752 2.57841 2.73081 0.06064  0.31029  0.02406  56  ARG A N   
318  C CA  . ARG A 56  ? 1.74588 2.21930 2.39859 0.06030  0.32787  0.01474  56  ARG A CA  
319  C C   . ARG A 56  ? 1.54058 1.96994 2.13039 0.09235  0.32777  0.04281  56  ARG A C   
320  O O   . ARG A 56  ? 1.37697 1.88212 2.00014 0.11437  0.30758  0.06944  56  ARG A O   
321  C CB  . ARG A 56  ? 1.67507 2.13350 2.28185 0.02847  0.29570  -0.02534 56  ARG A CB  
322  C CG  . ARG A 56  ? 1.55473 2.10282 2.16014 0.02348  0.23975  -0.03626 56  ARG A CG  
323  C CD  . ARG A 56  ? 1.61540 2.14464 2.19066 -0.01092 0.21986  -0.08101 56  ARG A CD  
324  N NE  . ARG A 56  ? 1.60933 2.24315 2.20124 -0.02445 0.17124  -0.10313 56  ARG A NE  
325  C CZ  . ARG A 56  ? 1.21865 1.83614 1.74532 -0.02829 0.14421  -0.11776 56  ARG A CZ  
326  N NH1 . ARG A 56  ? 0.98959 1.49728 1.43707 -0.01969 0.15648  -0.11087 56  ARG A NH1 
327  N NH2 . ARG A 56  ? 1.03424 1.75398 1.57566 -0.04130 0.10389  -0.14040 56  ARG A NH2 
328  N N   . ARG A 57  ? 1.41538 1.72338 1.91575 0.09451  0.35261  0.03726  57  ARG A N   
329  C CA  . ARG A 57  ? 1.05609 1.30595 1.49161 0.11580  0.35566  0.05203  57  ARG A CA  
330  C C   . ARG A 57  ? 1.10427 1.30656 1.45359 0.09868  0.32346  0.02754  57  ARG A C   
331  O O   . ARG A 57  ? 0.88142 1.00662 1.17067 0.08410  0.33602  0.00868  57  ARG A O   
332  C CB  . ARG A 57  ? 1.07908 1.23367 1.48409 0.13081  0.41321  0.06118  57  ARG A CB  
333  C CG  . ARG A 57  ? 1.24679 1.33956 1.60007 0.14951  0.42598  0.07082  57  ARG A CG  
334  C CD  . ARG A 57  ? 1.26154 1.25562 1.57489 0.15713  0.48544  0.06674  57  ARG A CD  
335  N NE  . ARG A 57  ? 1.38927 1.39422 1.76971 0.18757  0.52818  0.09771  57  ARG A NE  
336  C CZ  . ARG A 57  ? 1.43379 1.36027 1.78327 0.20199  0.57034  0.09838  57  ARG A CZ  
337  N NH1 . ARG A 57  ? 1.58038 1.41826 1.82988 0.18557  0.57102  0.06574  57  ARG A NH1 
338  N NH2 . ARG A 57  ? 1.15952 1.09964 1.58536 0.23296  0.61458  0.13156  57  ARG A NH2 
339  N N   . PRO A 58  ? 0.95641 1.20518 1.29816 0.10203  0.28400  0.03079  58  PRO A N   
340  C CA  . PRO A 58  ? 0.92891 1.14304 1.20224 0.08486  0.25371  0.00762  58  PRO A CA  
341  C C   . PRO A 58  ? 0.94470 1.05646 1.13811 0.08915  0.26987  0.00562  58  PRO A C   
342  O O   . PRO A 58  ? 0.99928 1.06367 1.18473 0.10425  0.30474  0.01788  58  PRO A O   
343  C CB  . PRO A 58  ? 0.80241 1.10096 1.09575 0.09216  0.21448  0.01712  58  PRO A CB  
344  C CG  . PRO A 58  ? 0.84230 1.19886 1.19639 0.12144  0.22824  0.05511  58  PRO A CG  
345  C CD  . PRO A 58  ? 0.88806 1.22444 1.28447 0.12610  0.26973  0.06217  58  PRO A CD  
346  N N   . VAL A 59  ? 0.89934 0.98012 1.03601 0.07392  0.24487  -0.01303 59  VAL A N   
347  C CA  . VAL A 59  ? 0.91405 0.91258 0.97585 0.07261  0.25134  -0.01995 59  VAL A CA  
348  C C   . VAL A 59  ? 0.94347 0.93504 1.00758 0.08898  0.25638  -0.00530 59  VAL A C   
349  O O   . VAL A 59  ? 0.91108 0.95712 1.00468 0.09736  0.23416  0.00814  59  VAL A O   
350  C CB  . VAL A 59  ? 0.96490 0.95136 0.98292 0.05617  0.21981  -0.03646 59  VAL A CB  
351  C CG1 . VAL A 59  ? 0.93827 0.86822 0.89311 0.05494  0.21463  -0.04181 59  VAL A CG1 
352  C CG2 . VAL A 59  ? 0.93293 0.89940 0.94189 0.04321  0.22954  -0.04647 59  VAL A CG2 
353  N N   . ASP A 60  ? 1.07070 0.99270 1.10208 0.09316  0.28939  -0.00887 60  ASP A N   
354  C CA  . ASP A 60  ? 1.13052 1.03321 1.17465 0.10753  0.30666  0.00310  60  ASP A CA  
355  C C   . ASP A 60  ? 1.14783 0.97101 1.12304 0.09261  0.31383  -0.02350 60  ASP A C   
356  O O   . ASP A 60  ? 1.29950 1.07416 1.21792 0.07953  0.32521  -0.04583 60  ASP A O   
357  C CB  . ASP A 60  ? 1.12151 1.02556 1.22056 0.13005  0.35254  0.02514  60  ASP A CB  
358  C CG  . ASP A 60  ? 1.25522 1.15186 1.39062 0.15111  0.37457  0.04833  60  ASP A CG  
359  O OD1 . ASP A 60  ? 1.25683 1.22598 1.44217 0.16815  0.35472  0.07940  60  ASP A OD1 
360  O OD2 . ASP A 60  ? 1.51589 1.33470 1.63022 0.15084  0.41493  0.03542  60  ASP A OD2 
361  N N   . PRO A 61  ? 1.10518 0.91877 1.08404 0.09316  0.30719  -0.02207 61  PRO A N   
362  C CA  . PRO A 61  ? 1.03674 0.90611 1.07051 0.11016  0.29369  0.00806  61  PRO A CA  
363  C C   . PRO A 61  ? 1.05735 0.98567 1.08372 0.10150  0.24450  0.00749  61  PRO A C   
364  O O   . PRO A 61  ? 0.99159 0.90087 0.97022 0.08130  0.22272  -0.01672 61  PRO A O   
365  C CB  . PRO A 61  ? 1.01730 0.83199 1.04356 0.10613  0.31120  0.00021  61  PRO A CB  
366  C CG  . PRO A 61  ? 1.09660 0.85568 1.04943 0.07602  0.30034  -0.04322 61  PRO A CG  
367  C CD  . PRO A 61  ? 1.16771 0.91208 1.09201 0.07432  0.31506  -0.05335 61  PRO A CD  
368  N N   . PRO A 62  ? 0.96093 0.96340 1.03328 0.11789  0.22896  0.03477  62  PRO A N   
369  C CA  . PRO A 62  ? 0.68086 0.73943 0.74552 0.10827  0.18740  0.02825  62  PRO A CA  
370  C C   . PRO A 62  ? 0.92041 0.94446 0.94373 0.09296  0.16807  0.01181  62  PRO A C   
371  O O   . PRO A 62  ? 0.88299 0.88005 0.90900 0.09779  0.17883  0.02024  62  PRO A O   
372  C CB  . PRO A 62  ? 0.74551 0.88947 0.86021 0.13206  0.18004  0.06270  62  PRO A CB  
373  C CG  . PRO A 62  ? 0.87982 0.99536 1.02424 0.15589  0.21767  0.09320  62  PRO A CG  
374  C CD  . PRO A 62  ? 0.78811 0.82987 0.92063 0.14817  0.25119  0.07493  62  PRO A CD  
375  N N   . PRO A 63  ? 0.94273 0.96614 0.93537 0.07471  0.14331  -0.01018 63  PRO A N   
376  C CA  . PRO A 63  ? 0.73787 0.73740 0.69988 0.06224  0.12415  -0.02187 63  PRO A CA  
377  C C   . PRO A 63  ? 0.72630 0.76885 0.71182 0.07269  0.11258  -0.00441 63  PRO A C   
378  O O   . PRO A 63  ? 0.69689 0.80322 0.70570 0.08312  0.10351  0.00748  63  PRO A O   
379  C CB  . PRO A 63  ? 0.69690 0.69960 0.63703 0.04809  0.10585  -0.03925 63  PRO A CB  
380  C CG  . PRO A 63  ? 0.91859 0.91414 0.86339 0.04815  0.12450  -0.04241 63  PRO A CG  
381  C CD  . PRO A 63  ? 0.79366 0.82963 0.78404 0.06481  0.13878  -0.02398 63  PRO A CD  
382  N N   . VAL A 64  ? 0.74141 0.75252 0.72006 0.06838  0.11346  -0.00450 64  VAL A N   
383  C CA  . VAL A 64  ? 0.63919 0.68059 0.63931 0.07877  0.10945  0.01504  64  VAL A CA  
384  C C   . VAL A 64  ? 0.71859 0.74057 0.70108 0.06162  0.09090  -0.00105 64  VAL A C   
385  O O   . VAL A 64  ? 0.81453 0.78938 0.78068 0.04525  0.09159  -0.01898 64  VAL A O   
386  C CB  . VAL A 64  ? 0.77026 0.79260 0.80282 0.09463  0.14140  0.03989  64  VAL A CB  
387  C CG1 . VAL A 64  ? 0.75709 0.80014 0.80998 0.10397  0.14201  0.06182  64  VAL A CG1 
388  C CG2 . VAL A 64  ? 0.66830 0.72460 0.72936 0.11857  0.16003  0.06619  64  VAL A CG2 
389  N N   . ILE A 65  ? 0.64046 0.70378 0.62637 0.06484  0.07440  0.00375  65  ILE A N   
390  C CA  . ILE A 65  ? 0.72505 0.77832 0.70414 0.05214  0.05851  -0.00692 65  ILE A CA  
391  C C   . ILE A 65  ? 0.68351 0.76372 0.68660 0.06351  0.06404  0.01377  65  ILE A C   
392  O O   . ILE A 65  ? 0.67130 0.79959 0.67883 0.08008  0.06676  0.02981  65  ILE A O   
393  C CB  . ILE A 65  ? 0.76476 0.83148 0.72634 0.04451  0.04054  -0.02326 65  ILE A CB  
394  C CG1 . ILE A 65  ? 0.69292 0.72691 0.63080 0.03473  0.04005  -0.03785 65  ILE A CG1 
395  C CG2 . ILE A 65  ? 0.59273 0.65579 0.55841 0.03741  0.02812  -0.02603 65  ILE A CG2 
396  C CD1 . ILE A 65  ? 0.71484 0.76521 0.65581 0.04029  0.05019  -0.03907 65  ILE A CD1 
397  N N   . GLU A 66  ? 0.67141 0.72522 0.69048 0.05411  0.06677  0.01344  66  GLU A N   
398  C CA  . GLU A 66  ? 0.82304 0.89401 0.87110 0.06319  0.07765  0.03453  66  GLU A CA  
399  C C   . GLU A 66  ? 0.75027 0.83965 0.79771 0.05685  0.06040  0.02674  66  GLU A C   
400  O O   . GLU A 66  ? 0.75000 0.82360 0.78938 0.04071  0.04198  0.00724  66  GLU A O   
401  C CB  . GLU A 66  ? 0.68187 0.71187 0.76347 0.05376  0.09742  0.03707  66  GLU A CB  
402  C CG  . GLU A 66  ? 0.98054 1.02452 1.10128 0.06677  0.11941  0.06648  66  GLU A CG  
403  C CD  . GLU A 66  ? 1.00425 1.00292 1.17079 0.05461  0.14663  0.06652  66  GLU A CD  
404  O OE1 . GLU A 66  ? 1.22732 1.20139 1.40956 0.06546  0.17690  0.08072  66  GLU A OE1 
405  O OE2 . GLU A 66  ? 1.16972 1.15846 1.36300 0.03327  0.13996  0.05127  66  GLU A OE2 
406  N N   . LEU A 67  ? 0.67466 0.80073 0.72969 0.07248  0.06896  0.04507  67  LEU A N   
407  C CA  . LEU A 67  ? 0.74712 0.89066 0.80608 0.07050  0.06180  0.04001  67  LEU A CA  
408  C C   . LEU A 67  ? 0.76903 0.91825 0.86375 0.07797  0.08156  0.06397  67  LEU A C   
409  O O   . LEU A 67  ? 0.81099 0.97577 0.91134 0.09622  0.10340  0.09127  67  LEU A O   
410  C CB  . LEU A 67  ? 0.68854 0.87227 0.71775 0.08002  0.05848  0.03190  67  LEU A CB  
411  C CG  . LEU A 67  ? 0.67596 0.88196 0.70778 0.08431  0.06439  0.02958  67  LEU A CG  
412  C CD1 . LEU A 67  ? 0.68889 0.86736 0.74393 0.07108  0.05556  0.01825  67  LEU A CD1 
413  C CD2 . LEU A 67  ? 0.76868 1.01297 0.76691 0.08788  0.06311  0.01022  67  LEU A CD2 
414  N N   . ASN A 68  ? 0.68281 0.82339 0.80649 0.06592  0.07592  0.05812  68  ASN A N   
415  C CA  . ASN A 68  ? 0.70378 0.85160 0.87089 0.07062  0.09640  0.07910  68  ASN A CA  
416  C C   . ASN A 68  ? 0.77488 0.94226 0.95165 0.07140  0.09166  0.07430  68  ASN A C   
417  O O   . ASN A 68  ? 0.75204 0.91516 0.92269 0.06127  0.06995  0.05513  68  ASN A O   
418  C CB  . ASN A 68  ? 0.81388 0.93120 1.02988 0.05059  0.09949  0.07631  68  ASN A CB  
419  C CG  . ASN A 68  ? 0.95286 1.04360 1.17158 0.05353  0.11986  0.08530  68  ASN A CG  
420  O OD1 . ASN A 68  ? 0.80253 0.89501 1.04543 0.07057  0.15294  0.11632  68  ASN A OD1 
421  N ND2 . ASN A 68  ? 0.97325 1.03820 1.16825 0.03993  0.10519  0.06187  68  ASN A ND2 
422  N N   . ILE A 69  ? 0.79632 0.98407 0.99049 0.08630  0.11716  0.09575  69  ILE A N   
423  C CA  . ILE A 69  ? 0.80082 1.00563 1.00892 0.09089  0.12351  0.09411  69  ILE A CA  
424  C C   . ILE A 69  ? 0.74059 0.94673 1.01493 0.08979  0.14445  0.11660  69  ILE A C   
425  O O   . ILE A 69  ? 0.86783 1.07339 1.15692 0.09914  0.17077  0.14170  69  ILE A O   
426  C CB  . ILE A 69  ? 0.75866 0.99249 0.91635 0.11038  0.13996  0.09311  69  ILE A CB  
427  C CG1 . ILE A 69  ? 0.74561 0.98233 0.85071 0.10589  0.11939  0.06492  69  ILE A CG1 
428  C CG2 . ILE A 69  ? 0.82366 1.06708 0.99972 0.11535  0.15612  0.08939  69  ILE A CG2 
429  C CD1 . ILE A 69  ? 0.80447 1.08045 0.85667 0.12114  0.12860  0.06607  69  ILE A CD1 
430  N N   . PHE A 70  ? 0.82763 1.03865 1.14848 0.08024  0.13597  0.11149  70  PHE A N   
431  C CA  . PHE A 70  ? 0.80195 1.02012 1.20116 0.07355  0.15128  0.12889  70  PHE A CA  
432  C C   . PHE A 70  ? 0.92651 1.16644 1.35421 0.08696  0.17064  0.13902  70  PHE A C   
433  O O   . PHE A 70  ? 0.87061 1.11594 1.28908 0.08920  0.15700  0.12594  70  PHE A O   
434  C CB  . PHE A 70  ? 0.81863 1.03336 1.26521 0.04468  0.11873  0.11329  70  PHE A CB  
435  C CG  . PHE A 70  ? 0.82672 1.01385 1.25187 0.02896  0.10793  0.09948  70  PHE A CG  
436  C CD1 . PHE A 70  ? 0.88116 1.05145 1.35057 0.01985  0.13287  0.10870  70  PHE A CD1 
437  C CD2 . PHE A 70  ? 0.72028 0.89367 1.08547 0.02438  0.08018  0.07825  70  PHE A CD2 
438  C CE1 . PHE A 70  ? 0.77155 0.90943 1.22595 0.00622  0.13098  0.09433  70  PHE A CE1 
439  C CE2 . PHE A 70  ? 0.69275 0.83776 1.03906 0.01141  0.07616  0.06500  70  PHE A CE2 
440  C CZ  . PHE A 70  ? 0.64529 0.77124 1.03617 0.00235  0.10220  0.07185  70  PHE A CZ  
441  N N   . GLU A 71  ? 0.89981 1.14868 1.36495 0.09789  0.20870  0.16488  71  GLU A N   
442  C CA  . GLU A 71  ? 0.81195 1.08019 1.32651 0.10826  0.23402  0.17839  71  GLU A CA  
443  C C   . GLU A 71  ? 0.85543 1.13784 1.47414 0.08758  0.22383  0.18527  71  GLU A C   
444  O O   . GLU A 71  ? 0.82590 1.10179 1.48924 0.07147  0.22808  0.19169  71  GLU A O   
445  C CB  . GLU A 71  ? 0.96006 1.23422 1.45969 0.13192  0.28455  0.20579  71  GLU A CB  
446  C CG  . GLU A 71  ? 0.97552 1.26640 1.51851 0.14611  0.32097  0.22062  71  GLU A CG  
447  C CD  . GLU A 71  ? 1.18037 1.47973 1.65327 0.17437  0.36320  0.23162  71  GLU A CD  
448  O OE1 . GLU A 71  ? 1.19936 1.50037 1.58667 0.18251  0.35612  0.22494  71  GLU A OE1 
449  O OE2 . GLU A 71  ? 1.19759 1.50766 1.70266 0.18876  0.40447  0.24848  71  GLU A OE2 
450  N N   . SER A 72  ? 0.93597 1.24083 1.59975 0.08788  0.21306  0.18407  72  SER A N   
451  C CA  . SER A 72  ? 0.93166 1.26887 1.70273 0.07008  0.20098  0.19282  72  SER A CA  
452  C C   . SER A 72  ? 1.02168 1.37891 1.85828 0.08810  0.24602  0.21938  72  SER A C   
453  O O   . SER A 72  ? 1.16060 1.52022 1.98066 0.11016  0.26252  0.22272  72  SER A O   
454  C CB  . SER A 72  ? 0.83796 1.19885 1.62174 0.05980  0.15175  0.18001  72  SER A CB  
455  O OG  . SER A 72  ? 1.07049 1.40949 1.78445 0.04585  0.11597  0.15587  72  SER A OG  
456  N N   . ASP A 73  ? 1.29147 1.55758 1.56085 -0.10643 0.20742  -0.08627 73  ASP A N   
457  C CA  . ASP A 73  ? 1.41744 1.71242 1.73732 -0.11302 0.23862  -0.08872 73  ASP A CA  
458  C C   . ASP A 73  ? 1.40155 1.76156 1.79886 -0.10478 0.22130  -0.09653 73  ASP A C   
459  O O   . ASP A 73  ? 1.26580 1.65671 1.69102 -0.11041 0.18765  -0.10221 73  ASP A O   
460  C CB  . ASP A 73  ? 1.53407 1.82026 1.87496 -0.14228 0.26418  -0.09057 73  ASP A CB  
461  C CG  . ASP A 73  ? 1.49004 1.77878 1.84804 -0.16186 0.24089  -0.10138 73  ASP A CG  
462  O OD1 . ASP A 73  ? 1.33262 1.62545 1.67281 -0.15239 0.20509  -0.10587 73  ASP A OD1 
463  O OD2 . ASP A 73  ? 1.14955 1.43553 1.53843 -0.18870 0.26087  -0.10710 73  ASP A OD2 
464  N N   . PRO A 74  ? 1.56213 1.94524 1.99560 -0.09143 0.24388  -0.09621 74  PRO A N   
465  C CA  . PRO A 74  ? 1.58152 2.02568 2.09348 -0.07606 0.22607  -0.09710 74  PRO A CA  
466  C C   . PRO A 74  ? 1.53607 2.04058 2.12984 -0.09575 0.21204  -0.10328 74  PRO A C   
467  O O   . PRO A 74  ? 1.38299 1.94041 2.02741 -0.08625 0.17736  -0.09962 74  PRO A O   
468  C CB  . PRO A 74  ? 1.56449 2.01164 2.10179 -0.06174 0.26687  -0.09844 74  PRO A CB  
469  C CG  . PRO A 74  ? 1.60371 1.99077 2.05802 -0.06980 0.29963  -0.09898 74  PRO A CG  
470  C CD  . PRO A 74  ? 1.57500 1.93067 1.98125 -0.09139 0.28909  -0.09481 74  PRO A CD  
471  N N   . HIS A 75  ? 1.68452 2.18495 2.29343 -0.12425 0.23703  -0.11116 75  HIS A N   
472  C CA  . HIS A 75  ? 1.91896 2.48106 2.61270 -0.14743 0.22614  -0.12067 75  HIS A CA  
473  C C   . HIS A 75  ? 1.73705 2.31200 2.41555 -0.16114 0.17833  -0.12738 75  HIS A C   
474  O O   . HIS A 75  ? 1.93660 2.57570 2.66704 -0.15774 0.14091  -0.12689 75  HIS A O   
475  C CB  . HIS A 75  ? 1.89794 2.44438 2.60803 -0.17717 0.26931  -0.12805 75  HIS A CB  
476  C CG  . HIS A 75  ? 1.95544 2.45491 2.62322 -0.16917 0.31864  -0.12058 75  HIS A CG  
477  N ND1 . HIS A 75  ? 2.01753 2.44455 2.59092 -0.17226 0.33379  -0.11231 75  HIS A ND1 
478  C CD2 . HIS A 75  ? 1.93294 2.45010 2.63902 -0.15968 0.35690  -0.12034 75  HIS A CD2 
479  C CE1 . HIS A 75  ? 2.10710 2.51206 2.65550 -0.16690 0.37586  -0.10673 75  HIS A CE1 
480  N NE2 . HIS A 75  ? 2.03693 2.49283 2.66262 -0.16015 0.39311  -0.11403 75  HIS A NE2 
481  N N   . ASP A 76  ? 1.34084 1.85643 1.94848 -0.17695 0.17986  -0.13287 76  ASP A N   
482  C CA  . ASP A 76  ? 1.08239 1.60213 1.67306 -0.19726 0.14493  -0.14623 76  ASP A CA  
483  C C   . ASP A 76  ? 1.23348 1.70199 1.73678 -0.17713 0.12579  -0.13876 76  ASP A C   
484  O O   . ASP A 76  ? 1.34033 1.74189 1.78177 -0.17177 0.14870  -0.13212 76  ASP A O   
485  C CB  . ASP A 76  ? 0.90271 1.39307 1.49661 -0.23485 0.16958  -0.16188 76  ASP A CB  
486  C CG  . ASP A 76  ? 1.05403 1.54350 1.63121 -0.26148 0.14063  -0.18314 76  ASP A CG  
487  O OD1 . ASP A 76  ? 1.05321 1.54243 1.58691 -0.24900 0.10589  -0.18308 76  ASP A OD1 
488  O OD2 . ASP A 76  ? 1.06907 1.55627 1.67675 -0.29764 0.15616  -0.20202 76  ASP A OD2 
489  N N   . ASP A 77  ? 1.07835 1.58119 1.57830 -0.16660 0.08368  -0.13762 77  ASP A N   
490  C CA  . ASP A 77  ? 1.14074 1.59982 1.56319 -0.14907 0.06576  -0.13144 77  ASP A CA  
491  C C   . ASP A 77  ? 1.20572 1.63436 1.58362 -0.17424 0.05406  -0.14963 77  ASP A C   
492  O O   . ASP A 77  ? 1.20933 1.59645 1.52331 -0.16207 0.04478  -0.14634 77  ASP A O   
493  C CB  . ASP A 77  ? 0.97535 1.47917 1.40947 -0.12370 0.03049  -0.11756 77  ASP A CB  
494  C CG  . ASP A 77  ? 1.29511 1.77979 1.72237 -0.08844 0.04738  -0.09874 77  ASP A CG  
495  O OD1 . ASP A 77  ? 1.32880 1.78447 1.75626 -0.08643 0.08520  -0.09835 77  ASP A OD1 
496  O OD2 . ASP A 77  ? 1.55405 2.05116 1.97320 -0.06458 0.02453  -0.08494 77  ASP A OD2 
497  N N   . SER A 78  ? 1.11651 1.56330 1.52947 -0.21023 0.05750  -0.17094 78  SER A N   
498  C CA  . SER A 78  ? 1.04955 1.45323 1.42120 -0.23638 0.05884  -0.19246 78  SER A CA  
499  C C   . SER A 78  ? 1.17168 1.49221 1.50354 -0.23296 0.09871  -0.18562 78  SER A C   
500  O O   . SER A 78  ? 1.22649 1.49837 1.52030 -0.24570 0.10452  -0.19834 78  SER A O   
501  C CB  . SER A 78  ? 0.99010 1.43534 1.41455 -0.28000 0.05441  -0.22109 78  SER A CB  
502  O OG  . SER A 78  ? 0.87469 1.39753 1.32250 -0.28877 0.00923  -0.22926 78  SER A OG  
503  N N   . ASN A 79  ? 1.14520 1.44949 1.48405 -0.21557 0.12642  -0.16466 79  ASN A N   
504  C CA  . ASN A 79  ? 1.19557 1.42927 1.49656 -0.21093 0.16161  -0.15060 79  ASN A CA  
505  C C   . ASN A 79  ? 1.20853 1.41663 1.45583 -0.17511 0.15807  -0.12756 79  ASN A C   
506  O O   . ASN A 79  ? 1.20810 1.44902 1.46652 -0.15538 0.15167  -0.11822 79  ASN A O   
507  C CB  . ASN A 79  ? 1.09849 1.33297 1.44046 -0.22441 0.19881  -0.14425 79  ASN A CB  
508  C CG  . ASN A 79  ? 1.28649 1.53762 1.68326 -0.26394 0.20815  -0.16814 79  ASN A CG  
509  O OD1 . ASN A 79  ? 1.24560 1.50867 1.64682 -0.28349 0.18579  -0.19241 79  ASN A OD1 
510  N ND2 . ASN A 79  ? 1.17245 1.42449 1.60956 -0.27875 0.24316  -0.16328 79  ASN A ND2 
511  N N   . LYS A 80  ? 1.19852 1.34896 1.39338 -0.16758 0.16373  -0.11953 80  LYS A N   
512  C CA  . LYS A 80  ? 1.13193 1.25686 1.27629 -0.13785 0.16115  -0.09862 80  LYS A CA  
513  C C   . LYS A 80  ? 1.18300 1.25071 1.29677 -0.13680 0.18876  -0.07903 80  LYS A C   
514  O O   . LYS A 80  ? 1.38865 1.42515 1.51399 -0.15547 0.20603  -0.08266 80  LYS A O   
515  C CB  . LYS A 80  ? 1.14101 1.26302 1.25260 -0.12478 0.13125  -0.10458 80  LYS A CB  
516  C CG  . LYS A 80  ? 1.27008 1.44850 1.40845 -0.12820 0.10073  -0.11983 80  LYS A CG  
517  C CD  . LYS A 80  ? 1.27802 1.46541 1.38686 -0.10158 0.07703  -0.11058 80  LYS A CD  
518  C CE  . LYS A 80  ? 1.35565 1.60678 1.50436 -0.09724 0.05280  -0.11203 80  LYS A CE  
519  N NZ  . LYS A 80  ? 1.33208 1.59641 1.45495 -0.08995 0.02134  -0.11327 80  LYS A NZ  
520  N N   . THR A 81  ? 1.05490 1.10984 1.13097 -0.11558 0.19304  -0.05728 81  THR A N   
521  C CA  . THR A 81  ? 1.07068 1.07969 1.11280 -0.11101 0.21308  -0.03130 81  THR A CA  
522  C C   . THR A 81  ? 1.07258 1.06482 1.06869 -0.08759 0.19473  -0.01913 81  THR A C   
523  O O   . THR A 81  ? 1.05193 1.06671 1.02965 -0.07272 0.18142  -0.01954 81  THR A O   
524  C CB  . THR A 81  ? 1.12699 1.14223 1.16364 -0.11355 0.23859  -0.01442 81  THR A CB  
525  O OG1 . THR A 81  ? 1.05467 1.08902 1.14190 -0.13617 0.25775  -0.02683 81  THR A OG1 
526  C CG2 . THR A 81  ? 1.21205 1.18386 1.21062 -0.10994 0.25619  0.01850  81  THR A CG2 
527  N N   . ASP A 82  ? 1.00116 0.95354 0.98472 -0.08475 0.19672  -0.00895 82  ASP A N   
528  C CA  . ASP A 82  ? 1.05078 0.98895 0.99864 -0.06336 0.18115  0.00446  82  ASP A CA  
529  C C   . ASP A 82  ? 1.09236 1.02814 1.00636 -0.05328 0.18827  0.03465  82  ASP A C   
530  O O   . ASP A 82  ? 1.02523 0.93600 0.93502 -0.05680 0.20693  0.06056  82  ASP A O   
531  C CB  . ASP A 82  ? 1.02505 0.92283 0.97955 -0.06295 0.18552  0.00657  82  ASP A CB  
532  C CG  . ASP A 82  ? 1.11633 1.00880 1.04702 -0.04285 0.16643  0.01022  82  ASP A CG  
533  O OD1 . ASP A 82  ? 1.06112 0.96242 0.96459 -0.02750 0.15803  0.03077  82  ASP A OD1 
534  O OD2 . ASP A 82  ? 1.11423 0.99508 1.05262 -0.04471 0.16110  -0.00909 82  ASP A OD2 
535  N N   . ILE A 83  ? 0.96709 0.92849 0.85549 -0.04202 0.17401  0.03193  83  ILE A N   
536  C CA  . ILE A 83  ? 1.01106 0.97696 0.86008 -0.03733 0.17912  0.05398  83  ILE A CA  
537  C C   . ILE A 83  ? 0.96032 0.92309 0.77926 -0.02082 0.15821  0.06529  83  ILE A C   
538  O O   . ILE A 83  ? 1.04548 1.02390 0.82896 -0.01735 0.15306  0.07182  83  ILE A O   
539  C CB  . ILE A 83  ? 1.06480 1.06213 0.90995 -0.04222 0.18651  0.03805  83  ILE A CB  
540  C CG1 . ILE A 83  ? 0.96266 0.98237 0.82931 -0.03428 0.16874  0.01057  83  ILE A CG1 
541  C CG2 . ILE A 83  ? 1.14133 1.14268 1.01359 -0.05973 0.21325  0.03626  83  ILE A CG2 
542  C CD1 . ILE A 83  ? 1.06037 1.10088 0.90850 -0.02811 0.16900  0.00089  83  ILE A CD1 
543  N N   . THR A 84  ? 0.92419 0.86767 0.75860 -0.01285 0.14811  0.06539  84  THR A N   
544  C CA  . THR A 84  ? 0.96978 0.91313 0.78626 0.00272  0.12925  0.07457  84  THR A CA  
545  C C   . THR A 84  ? 1.08121 1.02427 0.86971 0.00729  0.12883  0.11063  84  THR A C   
546  O O   . THR A 84  ? 1.14205 1.10428 0.90362 0.01401  0.11242  0.11594  84  THR A O   
547  C CB  . THR A 84  ? 0.88405 0.80327 0.72639 0.00894  0.12611  0.06904  84  THR A CB  
548  O OG1 . THR A 84  ? 0.97474 0.89690 0.83781 -0.00035 0.12652  0.03759  84  THR A OG1 
549  C CG2 . THR A 84  ? 0.95060 0.87551 0.78184 0.02443  0.10755  0.07247  84  THR A CG2 
550  N N   . PHE A 85  ? 1.11451 1.03739 0.90987 0.00260  0.14616  0.13713  85  PHE A N   
551  C CA  . PHE A 85  ? 1.17787 1.10322 0.94561 0.00676  0.14485  0.17918  85  PHE A CA  
552  C C   . PHE A 85  ? 1.18267 1.13125 0.90606 -0.00653 0.15213  0.18371  85  PHE A C   
553  O O   . PHE A 85  ? 1.20925 1.16759 0.89701 -0.00637 0.14818  0.21840  85  PHE A O   
554  C CB  . PHE A 85  ? 1.28723 1.17583 1.08528 0.00924  0.16341  0.21039  85  PHE A CB  
555  C CG  . PHE A 85  ? 1.25777 1.12417 1.09264 0.02537  0.15754  0.21571  85  PHE A CG  
556  C CD1 . PHE A 85  ? 1.09047 0.93887 0.95811 0.02274  0.16284  0.17891  85  PHE A CD1 
557  C CD2 . PHE A 85  ? 1.39258 1.25931 1.23029 0.04237  0.14728  0.25722  85  PHE A CD2 
558  C CE1 . PHE A 85  ? 1.28001 1.10591 1.17930 0.03560  0.16292  0.17943  85  PHE A CE1 
559  C CE2 . PHE A 85  ? 1.43469 1.28085 1.31456 0.05827  0.14665  0.26057  85  PHE A CE2 
560  C CZ  . PHE A 85  ? 1.36260 1.18563 1.27167 0.05429  0.15698  0.21962  85  PHE A CZ  
561  N N   . VAL A 86  ? 1.29368 1.25355 1.01922 -0.01825 0.16324  0.15047  86  VAL A N   
562  C CA  . VAL A 86  ? 1.21650 1.19749 0.90345 -0.03169 0.17587  0.14668  86  VAL A CA  
563  C C   . VAL A 86  ? 1.30715 1.31474 0.97344 -0.03068 0.16288  0.11598  86  VAL A C   
564  O O   . VAL A 86  ? 1.35289 1.37914 0.97075 -0.03834 0.16278  0.11874  86  VAL A O   
565  C CB  . VAL A 86  ? 1.17199 1.14666 0.88603 -0.04621 0.20518  0.13363  86  VAL A CB  
566  C CG1 . VAL A 86  ? 1.26245 1.26292 0.95600 -0.05720 0.21913  0.10938  86  VAL A CG1 
567  C CG2 . VAL A 86  ? 1.21182 1.16340 0.92281 -0.05364 0.22609  0.17109  86  VAL A CG2 
568  N N   . TYR A 87  ? 1.13447 1.14297 0.83541 -0.02261 0.15283  0.08697  87  TYR A N   
569  C CA  . TYR A 87  ? 1.13309 1.16049 0.82458 -0.01994 0.14385  0.05886  87  TYR A CA  
570  C C   . TYR A 87  ? 1.17408 1.21221 0.82580 -0.01685 0.12426  0.06961  87  TYR A C   
571  O O   . TYR A 87  ? 1.32712 1.35872 0.98468 -0.00667 0.10640  0.08955  87  TYR A O   
572  C CB  . TYR A 87  ? 1.13424 1.15800 0.86970 -0.00954 0.13332  0.03679  87  TYR A CB  
573  C CG  . TYR A 87  ? 1.10275 1.14169 0.84355 -0.00579 0.13070  0.00890  87  TYR A CG  
574  C CD1 . TYR A 87  ? 1.06031 1.10202 0.78557 0.00163  0.11409  0.00326  87  TYR A CD1 
575  C CD2 . TYR A 87  ? 1.16104 1.21145 0.92994 -0.00910 0.14663  -0.01036 87  TYR A CD2 
576  C CE1 . TYR A 87  ? 1.14908 1.19867 0.88380 0.00527  0.11557  -0.02059 87  TYR A CE1 
577  C CE2 . TYR A 87  ? 1.13562 1.19660 0.91765 -0.00277 0.14711  -0.03193 87  TYR A CE2 
578  C CZ  . TYR A 87  ? 1.08804 1.14557 0.85149 0.00424  0.13261  -0.03686 87  TYR A CZ  
579  O OH  . TYR A 87  ? 1.19256 1.25491 0.97294 0.01064  0.13682  -0.05679 87  TYR A OH  
580  N N   . ASN A 88  ? 1.19819 1.25448 0.81331 -0.02698 0.12904  0.05415  88  ASN A N   
581  C CA  . ASN A 88  ? 1.40027 1.47423 0.97069 -0.03146 0.11129  0.06266  88  ASN A CA  
582  C C   . ASN A 88  ? 1.31150 1.39299 0.88822 -0.02930 0.10301  0.02923  88  ASN A C   
583  O O   . ASN A 88  ? 1.33620 1.42426 0.89736 -0.04014 0.11908  0.00072  88  ASN A O   
584  C CB  . ASN A 88  ? 1.55599 1.64491 1.06833 -0.05120 0.12552  0.07069  88  ASN A CB  
585  C CG  . ASN A 88  ? 1.72483 1.84028 1.18528 -0.06087 0.10422  0.07778  88  ASN A CG  
586  O OD1 . ASN A 88  ? 1.66696 1.79011 1.13926 -0.05023 0.07645  0.09417  88  ASN A OD1 
587  N ND2 . ASN A 88  ? 1.73707 1.86937 1.14097 -0.08298 0.11794  0.06322  88  ASN A ND2 
588  N N   . ALA A 89  ? 1.16846 1.24607 0.77102 -0.01554 0.08174  0.03270  89  ALA A N   
589  C CA  . ALA A 89  ? 1.16327 1.24530 0.77381 -0.01334 0.07378  0.00621  89  ALA A CA  
590  C C   . ALA A 89  ? 1.17145 1.25587 0.79747 -0.00212 0.04894  0.02227  89  ALA A C   
591  O O   . ALA A 89  ? 1.17191 1.24782 0.81567 0.00812  0.04200  0.04904  89  ALA A O   
592  C CB  . ALA A 89  ? 1.07614 1.14329 0.72683 -0.00472 0.08718  -0.01839 89  ALA A CB  
593  N N   . ASN A 90  ? 1.09673 1.19112 0.72104 -0.00469 0.03916  0.00436  90  ASN A N   
594  C CA  . ASN A 90  ? 1.00118 1.09943 0.64839 0.00568  0.01910  0.01530  90  ASN A CA  
595  C C   . ASN A 90  ? 1.02032 1.09396 0.70793 0.02073  0.02446  0.00415  90  ASN A C   
596  O O   . ASN A 90  ? 1.00543 1.06776 0.70123 0.02088  0.03800  -0.01818 90  ASN A O   
597  C CB  . ASN A 90  ? 0.98633 1.10879 0.61672 -0.00695 0.00671  0.00056  90  ASN A CB  
598  C CG  . ASN A 90  ? 1.38272 1.53730 0.96581 -0.02525 -0.00362 0.01219  90  ASN A CG  
599  O OD1 . ASN A 90  ? 1.50241 1.66834 1.04984 -0.04553 0.00434  -0.01362 90  ASN A OD1 
600  N ND2 . ASN A 90  ? 1.43727 1.60607 1.01889 -0.01883 -0.01961 0.05187  90  ASN A ND2 
601  N N   . PHE A 91  ? 0.84191 0.90847 0.55535 0.03341  0.01490  0.02108  91  PHE A N   
602  C CA  . PHE A 91  ? 0.72339 0.76822 0.46640 0.04503  0.01964  0.01173  91  PHE A CA  
603  C C   . PHE A 91  ? 0.78461 0.83252 0.54714 0.05209  0.00922  0.01614  91  PHE A C   
604  O O   . PHE A 91  ? 0.99681 1.05781 0.76663 0.05491  -0.00125 0.03731  91  PHE A O   
605  C CB  . PHE A 91  ? 0.83280 0.85843 0.59031 0.05112  0.02746  0.02247  91  PHE A CB  
606  C CG  . PHE A 91  ? 0.92357 0.94550 0.67551 0.04490  0.04015  0.01265  91  PHE A CG  
607  C CD1 . PHE A 91  ? 0.94987 0.96771 0.71385 0.04678  0.04554  -0.00692 91  PHE A CD1 
608  C CD2 . PHE A 91  ? 0.96001 0.98465 0.69890 0.03775  0.04725  0.02625  91  PHE A CD2 
609  C CE1 . PHE A 91  ? 0.97453 0.99528 0.74389 0.04206  0.05671  -0.01439 91  PHE A CE1 
610  C CE2 . PHE A 91  ? 0.96086 0.98458 0.70124 0.03115  0.06154  0.01662  91  PHE A CE2 
611  C CZ  . PHE A 91  ? 1.04163 1.06543 0.80055 0.03355  0.06577  -0.00455 91  PHE A CZ  
612  N N   . PHE A 92  ? 0.80457 0.84198 0.57919 0.05559  0.01312  -0.00108 92  PHE A N   
613  C CA  . PHE A 92  ? 0.76692 0.80409 0.56306 0.06172  0.00860  0.00111  92  PHE A CA  
614  C C   . PHE A 92  ? 0.79339 0.80558 0.60075 0.07001  0.01858  -0.00654 92  PHE A C   
615  O O   . PHE A 92  ? 0.83820 0.84088 0.63769 0.06951  0.02472  -0.01743 92  PHE A O   
616  C CB  . PHE A 92  ? 0.86856 0.92230 0.66315 0.05252  0.00374  -0.01264 92  PHE A CB  
617  C CG  . PHE A 92  ? 0.88607 0.96867 0.65854 0.03838  -0.00687 -0.01133 92  PHE A CG  
618  C CD1 . PHE A 92  ? 0.89134 0.97429 0.63592 0.02671  0.00108  -0.02780 92  PHE A CD1 
619  C CD2 . PHE A 92  ? 0.94530 1.05745 0.72514 0.03613  -0.02424 0.00701  92  PHE A CD2 
620  C CE1 . PHE A 92  ? 1.01695 1.12690 0.73161 0.00997  -0.00683 -0.02923 92  PHE A CE1 
621  C CE2 . PHE A 92  ? 1.01889 1.16345 0.77062 0.02038  -0.03738 0.01001  92  PHE A CE2 
622  C CZ  . PHE A 92  ? 0.98660 1.12890 0.70076 0.00574  -0.02803 -0.00975 92  PHE A CZ  
623  N N   . LEU A 93  ? 0.82945 0.83399 0.65602 0.07717  0.02053  -0.00010 93  LEU A N   
624  C CA  . LEU A 93  ? 0.70629 0.68905 0.53561 0.08194  0.03058  -0.00791 93  LEU A CA  
625  C C   . LEU A 93  ? 0.78534 0.76810 0.62931 0.08414  0.03413  -0.01090 93  LEU A C   
626  O O   . LEU A 93  ? 0.84687 0.84059 0.71390 0.08678  0.03229  -0.00197 93  LEU A O   
627  C CB  . LEU A 93  ? 0.66656 0.63291 0.50265 0.08545  0.03808  -0.00220 93  LEU A CB  
628  C CG  . LEU A 93  ? 0.77438 0.72206 0.59810 0.08375  0.04643  -0.01477 93  LEU A CG  
629  C CD1 . LEU A 93  ? 0.66731 0.62073 0.47455 0.07885  0.04090  -0.02114 93  LEU A CD1 
630  C CD2 . LEU A 93  ? 0.72015 0.64866 0.55323 0.08360  0.05841  -0.01506 93  LEU A CD2 
631  N N   . PHE A 94  ? 0.77267 0.74461 0.60749 0.08362  0.03998  -0.02069 94  PHE A N   
632  C CA  . PHE A 94  ? 0.66205 0.63111 0.50878 0.08361  0.04689  -0.02401 94  PHE A CA  
633  C C   . PHE A 94  ? 0.80307 0.75093 0.64084 0.08735  0.05948  -0.02488 94  PHE A C   
634  O O   . PHE A 94  ? 0.81363 0.75171 0.62905 0.08769  0.05941  -0.02651 94  PHE A O   
635  C CB  . PHE A 94  ? 0.80677 0.77743 0.64976 0.07857  0.04704  -0.03261 94  PHE A CB  
636  C CG  . PHE A 94  ? 0.80347 0.76613 0.65973 0.07696  0.05773  -0.03588 94  PHE A CG  
637  C CD1 . PHE A 94  ? 0.84759 0.82325 0.72937 0.07351  0.05885  -0.03536 94  PHE A CD1 
638  C CD2 . PHE A 94  ? 0.85442 0.79830 0.70266 0.07914  0.06738  -0.03683 94  PHE A CD2 
639  C CE1 . PHE A 94  ? 0.93806 0.90648 0.83586 0.06991  0.07158  -0.03918 94  PHE A CE1 
640  C CE2 . PHE A 94  ? 0.90118 0.83402 0.76225 0.07681  0.08054  -0.03751 94  PHE A CE2 
641  C CZ  . PHE A 94  ? 0.91701 0.86130 0.80218 0.07098  0.08372  -0.04044 94  PHE A CZ  
642  N N   . ALA A 95  ? 0.76638 0.71079 0.62160 0.08869  0.07040  -0.02401 95  ALA A N   
643  C CA  . ALA A 95  ? 0.77467 0.69888 0.61730 0.08956  0.08670  -0.02681 95  ALA A CA  
644  C C   . ALA A 95  ? 0.85695 0.77342 0.69612 0.08767  0.09716  -0.02692 95  ALA A C   
645  O O   . ALA A 95  ? 0.82386 0.75030 0.69029 0.08573  0.09916  -0.02689 95  ALA A O   
646  C CB  . ALA A 95  ? 0.69564 0.61705 0.56416 0.09284  0.09930  -0.02630 95  ALA A CB  
647  N N   . THR A 96  ? 0.79231 0.69294 0.59808 0.08677  0.10326  -0.02580 96  THR A N   
648  C CA  . THR A 96  ? 0.90076 0.78870 0.69723 0.08550  0.11708  -0.02078 96  THR A CA  
649  C C   . THR A 96  ? 0.89755 0.77034 0.66368 0.08188  0.13325  -0.02291 96  THR A C   
650  O O   . THR A 96  ? 0.94894 0.82000 0.69313 0.07902  0.13005  -0.02968 96  THR A O   
651  C CB  . THR A 96  ? 0.83286 0.71723 0.61398 0.08823  0.10916  -0.01107 96  THR A CB  
652  O OG1 . THR A 96  ? 0.96959 0.85786 0.72147 0.08970  0.09601  -0.00772 96  THR A OG1 
653  C CG2 . THR A 96  ? 0.72858 0.62300 0.53868 0.08871  0.10077  -0.01469 96  THR A CG2 
654  N N   . LEU A 97  ? 0.94643 0.80730 0.70998 0.07940  0.15320  -0.01908 97  LEU A N   
655  C CA  . LEU A 97  ? 0.95384 0.79925 0.68532 0.07318  0.17476  -0.02316 97  LEU A CA  
656  C C   . LEU A 97  ? 1.05286 0.88897 0.73719 0.07077  0.17487  -0.00787 97  LEU A C   
657  O O   . LEU A 97  ? 1.09785 0.92763 0.79264 0.07342  0.18111  0.00593  97  LEU A O   
658  C CB  . LEU A 97  ? 0.92873 0.76931 0.69516 0.07166  0.20180  -0.02822 97  LEU A CB  
659  C CG  . LEU A 97  ? 0.98036 0.80507 0.72650 0.06491  0.23114  -0.04000 97  LEU A CG  
660  C CD1 . LEU A 97  ? 0.99427 0.81925 0.74993 0.06562  0.23050  -0.05542 97  LEU A CD1 
661  C CD2 . LEU A 97  ? 1.05325 0.87591 0.84083 0.06428  0.25971  -0.04083 97  LEU A CD2 
662  N N   . GLU A 98  ? 1.14111 0.97763 0.77537 0.06477  0.16784  -0.00921 98  GLU A N   
663  C CA  . GLU A 98  ? 1.21494 1.05050 0.80130 0.06295  0.16206  0.01091  98  GLU A CA  
664  C C   . GLU A 98  ? 1.18782 1.01044 0.72164 0.04968  0.18533  0.00661  98  GLU A C   
665  O O   . GLU A 98  ? 1.27243 1.09558 0.77757 0.03799  0.18898  -0.01432 98  GLU A O   
666  C CB  . GLU A 98  ? 1.27846 1.13449 0.84553 0.06392  0.13101  0.01567  98  GLU A CB  
667  C CG  . GLU A 98  ? 1.35597 1.22474 0.97075 0.07286  0.11280  0.01004  98  GLU A CG  
668  C CD  . GLU A 98  ? 1.70368 1.57074 1.35670 0.08501  0.11021  0.02521  98  GLU A CD  
669  O OE1 . GLU A 98  ? 1.64791 1.50149 1.29720 0.08783  0.12299  0.04189  98  GLU A OE1 
670  O OE2 . GLU A 98  ? 1.46116 1.33810 1.14788 0.09007  0.09848  0.01888  98  GLU A OE2 
671  N N   . PRO A 99  ? 1.37209 1.18061 0.89146 0.04899  0.20506  0.02371  99  PRO A N   
672  C CA  . PRO A 99  ? 1.36827 1.16473 0.82732 0.03413  0.22946  0.02085  99  PRO A CA  
673  C C   . PRO A 99  ? 1.48212 1.29408 0.87031 0.02311  0.20827  0.02449  99  PRO A C   
674  O O   . PRO A 99  ? 1.53242 1.36306 0.91206 0.03049  0.17734  0.04823  99  PRO A O   
675  C CB  . PRO A 99  ? 1.29928 1.08028 0.75835 0.03796  0.24809  0.04844  99  PRO A CB  
676  C CG  . PRO A 99  ? 1.29285 1.07288 0.83182 0.05059  0.24678  0.04752  99  PRO A CG  
677  C CD  . PRO A 99  ? 1.39271 1.19258 0.95158 0.05925  0.21109  0.04383  99  PRO A CD  
678  N N   . GLU A 100 ? 1.62551 1.43168 0.96594 0.00409  0.22622  -0.00083 100 GLU A N   
679  C CA  . GLU A 100 ? 1.77481 1.59946 1.04034 -0.01294 0.20711  -0.00200 100 GLU A CA  
680  C C   . GLU A 100 ? 1.92859 1.75331 1.12309 -0.02123 0.21360  0.02679  100 GLU A C   
681  O O   . GLU A 100 ? 2.03925 1.88962 1.17255 -0.03205 0.18732  0.03990  100 GLU A O   
682  C CB  . GLU A 100 ? 1.86341 1.68022 1.10399 -0.03425 0.22527  -0.04672 100 GLU A CB  
683  C CG  . GLU A 100 ? 1.81205 1.64237 1.08768 -0.03371 0.20157  -0.06779 100 GLU A CG  
684  C CD  . GLU A 100 ? 2.00058 1.86594 1.23210 -0.04458 0.16130  -0.06019 100 GLU A CD  
685  O OE1 . GLU A 100 ? 1.95347 1.84168 1.18821 -0.03093 0.13168  -0.02309 100 GLU A OE1 
686  O OE2 . GLU A 100 ? 1.81437 1.68541 1.01283 -0.06740 0.16043  -0.09188 100 GLU A OE2 
687  N N   . ARG A 101 ? 1.98045 1.78015 1.18382 -0.01698 0.24696  0.03915  101 ARG A N   
688  C CA  . ARG A 101 ? 2.10914 1.90340 1.24909 -0.02330 0.25880  0.07209  101 ARG A CA  
689  C C   . ARG A 101 ? 2.00759 1.77731 1.19962 -0.00758 0.28326  0.09632  101 ARG A C   
690  O O   . ARG A 101 ? 1.96430 1.71045 1.17085 -0.01368 0.32485  0.08039  101 ARG A O   
691  C CB  . ARG A 101 ? 2.28114 2.06472 1.34149 -0.05138 0.29176  0.04671  101 ARG A CB  
692  C CG  . ARG A 101 ? 2.42054 2.20685 1.39231 -0.06278 0.29642  0.08294  101 ARG A CG  
693  C CD  . ARG A 101 ? 2.55003 2.32333 1.43947 -0.09379 0.33530  0.05211  101 ARG A CD  
694  N NE  . ARG A 101 ? 2.68951 2.46568 1.49079 -0.10559 0.34247  0.08987  101 ARG A NE  
695  C CZ  . ARG A 101 ? 2.71832 2.53385 1.46253 -0.10882 0.29918  0.12504  101 ARG A CZ  
696  N NH1 . ARG A 101 ? 2.67782 2.52609 1.41733 -0.10898 0.25173  0.12201  101 ARG A NH1 
697  N NH2 . ARG A 101 ? 2.67979 2.50681 1.37440 -0.11215 0.30362  0.16459  101 ARG A NH2 
698  N N   . PRO A 115 ? 1.46868 1.39497 1.60926 0.02100  0.27541  -0.04217 115 PRO A N   
699  C CA  . PRO A 115 ? 1.54367 1.44511 1.61605 0.03447  0.26391  -0.03373 115 PRO A CA  
700  C C   . PRO A 115 ? 1.43154 1.32794 1.48553 0.04471  0.27609  -0.03087 115 PRO A C   
701  O O   . PRO A 115 ? 1.41808 1.33927 1.52160 0.04645  0.28260  -0.03563 115 PRO A O   
702  C CB  . PRO A 115 ? 1.23899 1.16625 1.31476 0.03650  0.22601  -0.04008 115 PRO A CB  
703  C CG  . PRO A 115 ? 1.34491 1.30786 1.48224 0.02047  0.21772  -0.05275 115 PRO A CG  
704  C CD  . PRO A 115 ? 1.23633 1.18673 1.40421 0.00932  0.25102  -0.05378 115 PRO A CD  
705  N N   . VAL A 116 ? 1.38125 1.24760 1.36802 0.05053  0.27949  -0.02380 116 VAL A N   
706  C CA  . VAL A 116 ? 1.30652 1.16315 1.26765 0.05554  0.29467  -0.02687 116 VAL A CA  
707  C C   . VAL A 116 ? 1.12495 1.00378 1.10925 0.06447  0.27370  -0.03368 116 VAL A C   
708  O O   . VAL A 116 ? 1.23792 1.12036 1.24764 0.06847  0.29099  -0.03984 116 VAL A O   
709  C CB  . VAL A 116 ? 1.23750 1.06320 1.11695 0.05527  0.29854  -0.01875 116 VAL A CB  
710  C CG1 . VAL A 116 ? 1.34983 1.16053 1.20040 0.05218  0.32815  -0.02689 116 VAL A CG1 
711  C CG2 . VAL A 116 ? 1.39896 1.20492 1.25801 0.05011  0.30849  -0.00295 116 VAL A CG2 
712  N N   . LEU A 117 ? 1.05378 0.94545 1.03190 0.06801  0.23979  -0.03168 117 LEU A N   
713  C CA  . LEU A 117 ? 0.96046 0.87278 0.95947 0.07607  0.21891  -0.03334 117 LEU A CA  
714  C C   . LEU A 117 ? 1.06338 1.01562 1.12695 0.07484  0.20220  -0.03169 117 LEU A C   
715  O O   . LEU A 117 ? 1.16681 1.13076 1.23318 0.06696  0.18601  -0.03301 117 LEU A O   
716  C CB  . LEU A 117 ? 0.93077 0.83562 0.88153 0.07887  0.19347  -0.03152 117 LEU A CB  
717  C CG  . LEU A 117 ? 0.86593 0.78358 0.82752 0.08643  0.17643  -0.03122 117 LEU A CG  
718  C CD1 . LEU A 117 ? 0.96612 0.86769 0.92961 0.09062  0.19940  -0.03672 117 LEU A CD1 
719  C CD2 . LEU A 117 ? 0.94391 0.85664 0.86238 0.08669  0.15342  -0.03005 117 LEU A CD2 
720  N N   . THR A 118 ? 1.03792 1.01246 1.15444 0.08197  0.20621  -0.02887 118 THR A N   
721  C CA  . THR A 118 ? 1.03485 1.05720 1.21563 0.08105  0.18608  -0.02312 118 THR A CA  
722  C C   . THR A 118 ? 0.95666 0.99821 1.15413 0.09369  0.16510  -0.01136 118 THR A C   
723  O O   . THR A 118 ? 0.98588 1.00151 1.16402 0.10375  0.17640  -0.01019 118 THR A O   
724  C CB  . THR A 118 ? 1.13653 1.17920 1.38642 0.07938  0.20992  -0.02335 118 THR A CB  
725  O OG1 . THR A 118 ? 1.29791 1.30707 1.52261 0.07086  0.24275  -0.03195 118 THR A OG1 
726  C CG2 . THR A 118 ? 1.33160 1.42753 1.63862 0.06910  0.18594  -0.02141 118 THR A CG2 
727  N N   . GLY A 119 ? 0.89119 0.97891 1.12427 0.09118  0.13516  -0.00246 119 GLY A N   
728  C CA  . GLY A 119 ? 0.66749 0.77692 0.91398 0.10242  0.11198  0.01484  119 GLY A CA  
729  C C   . GLY A 119 ? 0.80394 0.92277 1.00368 0.09425  0.08020  0.01502  119 GLY A C   
730  O O   . GLY A 119 ? 0.95510 1.08404 1.13724 0.07816  0.06950  0.00256  119 GLY A O   
731  N N   . VAL A 120 ? 0.88973 1.00239 1.07084 0.10426  0.06904  0.02773  120 VAL A N   
732  C CA  . VAL A 120 ? 0.77565 0.89531 0.91083 0.09706  0.04322  0.02870  120 VAL A CA  
733  C C   . VAL A 120 ? 0.83415 0.90528 0.91178 0.09917  0.05582  0.01837  120 VAL A C   
734  O O   . VAL A 120 ? 0.79097 0.84165 0.86590 0.11010  0.06427  0.02626  120 VAL A O   
735  C CB  . VAL A 120 ? 0.70806 0.86365 0.86699 0.10494  0.01913  0.05534  120 VAL A CB  
736  C CG1 . VAL A 120 ? 0.69926 0.85734 0.80289 0.09614  -0.00198 0.05532  120 VAL A CG1 
737  C CG2 . VAL A 120 ? 0.65993 0.87416 0.87907 0.10160  0.00145  0.06780  120 VAL A CG2 
738  N N   . PRO A 121 ? 0.86474 0.91737 0.90113 0.08878  0.05837  0.00134  121 PRO A N   
739  C CA  . PRO A 121 ? 0.68045 0.69523 0.66817 0.09085  0.06726  -0.00595 121 PRO A CA  
740  C C   . PRO A 121 ? 0.71434 0.73183 0.66895 0.08835  0.04982  -0.00441 121 PRO A C   
741  O O   . PRO A 121 ? 0.80838 0.80165 0.72819 0.08852  0.05459  -0.01092 121 PRO A O   
742  C CB  . PRO A 121 ? 0.82457 0.82211 0.79537 0.08332  0.07951  -0.01911 121 PRO A CB  
743  C CG  . PRO A 121 ? 0.66591 0.69272 0.66076 0.07205  0.06845  -0.02380 121 PRO A CG  
744  C CD  . PRO A 121 ? 0.74668 0.81143 0.78765 0.07477  0.05674  -0.01165 121 PRO A CD  
745  N N   . VAL A 122 ? 0.68394 0.73309 0.64822 0.08518  0.03000  0.00505  122 VAL A N   
746  C CA  . VAL A 122 ? 0.76631 0.81945 0.69778 0.08098  0.01681  0.00677  122 VAL A CA  
747  C C   . VAL A 122 ? 0.84275 0.90824 0.78774 0.08921  0.00808  0.02985  122 VAL A C   
748  O O   . VAL A 122 ? 0.85435 0.95034 0.83386 0.09228  -0.00269 0.04652  122 VAL A O   
749  C CB  . VAL A 122 ? 0.84372 0.92172 0.76213 0.06544  0.00340  -0.00412 122 VAL A CB  
750  C CG1 . VAL A 122 ? 0.81396 0.89618 0.69763 0.06057  -0.00575 -0.00240 122 VAL A CG1 
751  C CG2 . VAL A 122 ? 0.87402 0.93274 0.78533 0.05861  0.01666  -0.02512 122 VAL A CG2 
752  N N   . ALA A 123 ? 0.83635 0.88042 0.75867 0.09261  0.01256  0.03305  123 ALA A N   
753  C CA  . ALA A 123 ? 0.77300 0.82068 0.70747 0.10028  0.00872  0.05680  123 ALA A CA  
754  C C   . ALA A 123 ? 0.75127 0.80554 0.64912 0.09213  -0.00127 0.06055  123 ALA A C   
755  O O   . ALA A 123 ? 0.85421 0.89188 0.72202 0.08566  0.00485  0.04290  123 ALA A O   
756  C CB  . ALA A 123 ? 0.72133 0.73225 0.66876 0.10977  0.03001  0.05661  123 ALA A CB  
757  N N   . GLY A 124 ? 0.74916 0.82983 0.65145 0.09280  -0.01591 0.08598  124 GLY A N   
758  C CA  . GLY A 124 ? 0.75325 0.83711 0.62002 0.08535  -0.02064 0.09379  124 GLY A CA  
759  C C   . GLY A 124 ? 0.79825 0.84990 0.67181 0.09356  -0.00513 0.10596  124 GLY A C   
760  O O   . GLY A 124 ? 0.89963 0.92752 0.80573 0.10460  0.00863  0.10854  124 GLY A O   
761  N N   . VAL A 125 ? 0.89187 0.94100 0.73497 0.08585  -0.00389 0.11054  125 VAL A N   
762  C CA  . VAL A 125 ? 0.92626 0.94390 0.77589 0.08928  0.01301  0.11850  125 VAL A CA  
763  C C   . VAL A 125 ? 0.90345 0.92574 0.77212 0.09817  0.01051  0.15974  125 VAL A C   
764  O O   . VAL A 125 ? 0.90412 0.96068 0.75901 0.09613  -0.00787 0.18366  125 VAL A O   
765  C CB  . VAL A 125 ? 0.89003 0.90101 0.70497 0.07618  0.02011  0.10177  125 VAL A CB  
766  C CG1 . VAL A 125 ? 0.90381 0.93939 0.68650 0.06713  0.01155  0.11929  125 VAL A CG1 
767  C CG2 . VAL A 125 ? 0.76232 0.73952 0.59128 0.07633  0.03937  0.09904  125 VAL A CG2 
768  N N   . ALA A 126 ? 0.91519 0.90306 0.81629 0.10729  0.02964  0.16887  126 ALA A N   
769  C CA  . ALA A 126 ? 0.83384 0.81562 0.75927 0.11750  0.03386  0.21095  126 ALA A CA  
770  C C   . ALA A 126 ? 0.85027 0.79239 0.77301 0.11090  0.05786  0.20642  126 ALA A C   
771  O O   . ALA A 126 ? 0.91891 0.82945 0.85336 0.10702  0.07612  0.17628  126 ALA A O   
772  C CB  . ALA A 126 ? 0.83969 0.81459 0.82527 0.13722  0.03962  0.23012  126 ALA A CB  
773  N N   . TYR A 127 ? 0.88714 0.83406 0.78997 0.10622  0.05745  0.23394  127 TYR A N   
774  C CA  . TYR A 127 ? 1.01242 0.92535 0.91310 0.09661  0.08103  0.23031  127 TYR A CA  
775  C C   . TYR A 127 ? 1.08894 0.96608 1.03978 0.11000  0.10160  0.26187  127 TYR A C   
776  O O   . TYR A 127 ? 1.18447 1.07418 1.14985 0.12356  0.09371  0.30942  127 TYR A O   
777  C CB  . TYR A 127 ? 0.92044 0.85363 0.77405 0.08316  0.07598  0.24301  127 TYR A CB  
778  C CG  . TYR A 127 ? 1.04649 1.00621 0.85881 0.06948  0.06440  0.20652  127 TYR A CG  
779  C CD1 . TYR A 127 ? 1.02613 0.97163 0.83673 0.05854  0.07694  0.16800  127 TYR A CD1 
780  C CD2 . TYR A 127 ? 0.88908 0.88915 0.66891 0.06706  0.04143  0.21024  127 TYR A CD2 
781  C CE1 . TYR A 127 ? 1.08093 1.04853 0.86371 0.04950  0.06910  0.13846  127 TYR A CE1 
782  C CE2 . TYR A 127 ? 0.96155 0.97929 0.70989 0.05481  0.03646  0.17516  127 TYR A CE2 
783  C CZ  . TYR A 127 ? 1.09205 1.09181 0.84477 0.04812  0.05142  0.14131  127 TYR A CZ  
784  O OH  . TYR A 127 ? 1.01679 1.03219 0.74758 0.03928  0.04909  0.11028  127 TYR A OH  
785  N N   . LEU A 128 ? 1.08069 0.91453 1.05968 0.10570  0.12807  0.23585  128 LEU A N   
786  C CA  . LEU A 128 ? 1.18118 0.97124 1.21395 0.11640  0.15555  0.25717  128 LEU A CA  
787  C C   . LEU A 128 ? 1.21810 0.96736 1.25457 0.09765  0.18431  0.23557  128 LEU A C   
788  O O   . LEU A 128 ? 1.15011 0.90543 1.15762 0.07812  0.18249  0.19521  128 LEU A O   
789  C CB  . LEU A 128 ? 1.11788 0.89029 1.19516 0.12948  0.16607  0.24129  128 LEU A CB  
790  C CG  . LEU A 128 ? 1.12790 0.93936 1.20290 0.14056  0.14136  0.23713  128 LEU A CG  
791  C CD1 . LEU A 128 ? 0.92875 0.71212 1.04581 0.14792  0.16308  0.21216  128 LEU A CD1 
792  C CD2 . LEU A 128 ? 1.23665 1.08562 1.32590 0.15866  0.11878  0.29107  128 LEU A CD2 
793  N N   . ASP A 129 ? 1.20980 0.91788 1.28898 0.10391  0.21181  0.26384  129 ASP A N   
794  C CA  . ASP A 129 ? 1.32191 0.98815 1.41281 0.08418  0.24284  0.24629  129 ASP A CA  
795  C C   . ASP A 129 ? 1.20140 0.82166 1.33186 0.07733  0.27226  0.20589  129 ASP A C   
796  O O   . ASP A 129 ? 1.30221 0.89701 1.43439 0.05303  0.29267  0.17170  129 ASP A O   
797  C CB  . ASP A 129 ? 1.41237 1.05415 1.52605 0.09140  0.26128  0.30138  129 ASP A CB  
798  C CG  . ASP A 129 ? 1.65759 1.34309 1.72116 0.09148  0.23647  0.33873  129 ASP A CG  
799  O OD1 . ASP A 129 ? 1.70664 1.41266 1.72674 0.07068  0.23012  0.31304  129 ASP A OD1 
800  O OD2 . ASP A 129 ? 1.69644 1.39763 1.76525 0.11165  0.22415  0.39413  129 ASP A OD2 
801  N N   . LYS A 130 ? 1.18510 0.79659 1.34770 0.09603  0.27599  0.20727  130 LYS A N   
802  C CA  . LYS A 130 ? 1.30147 0.86761 1.49937 0.08961  0.30821  0.16800  130 LYS A CA  
803  C C   . LYS A 130 ? 1.28883 0.88031 1.46775 0.09275  0.29156  0.13527  130 LYS A C   
804  O O   . LYS A 130 ? 1.27073 0.90151 1.44301 0.11214  0.26462  0.16003  130 LYS A O   
805  C CB  . LYS A 130 ? 1.31010 0.82891 1.58028 0.11126  0.34234  0.20391  130 LYS A CB  
806  C CG  . LYS A 130 ? 1.22917 0.70500 1.52673 0.10428  0.37157  0.22907  130 LYS A CG  
807  C CD  . LYS A 130 ? 1.86871 1.29653 2.24537 0.13018  0.40635  0.27097  130 LYS A CD  
808  C CE  . LYS A 130 ? 1.90235 1.36856 2.30191 0.16601  0.38153  0.31620  130 LYS A CE  
809  N NZ  . LYS A 130 ? 1.81813 1.24224 2.29681 0.18669  0.41789  0.31690  130 LYS A NZ  
810  N N   . PRO A 131 ? 1.31020 0.88190 1.47824 0.07186  0.30704  0.07985  131 PRO A N   
811  C CA  . PRO A 131 ? 1.22470 0.75449 1.39953 0.04337  0.33768  0.04164  131 PRO A CA  
812  C C   . PRO A 131 ? 1.16635 0.72203 1.30144 0.01924  0.31941  0.02922  131 PRO A C   
813  O O   . PRO A 131 ? 1.35012 0.87725 1.49761 -0.00465 0.34229  0.00809  131 PRO A O   
814  C CB  . PRO A 131 ? 1.10400 0.62272 1.26634 0.03014  0.34924  -0.01186 131 PRO A CB  
815  C CG  . PRO A 131 ? 1.29368 0.86548 1.41596 0.04221  0.31092  -0.00815 131 PRO A CG  
816  C CD  . PRO A 131 ? 1.17283 0.76602 1.31816 0.07331  0.29432  0.05015  131 PRO A CD  
817  N N   . ASN A 132 ? 1.24435 0.85369 1.33742 0.02455  0.28107  0.04182  132 ASN A N   
818  C CA  . ASN A 132 ? 1.07334 0.71091 1.13654 0.00592  0.26556  0.03484  132 ASN A CA  
819  C C   . ASN A 132 ? 1.12915 0.80449 1.17047 0.02262  0.24006  0.07737  132 ASN A C   
820  O O   . ASN A 132 ? 1.17836 0.87312 1.21394 0.04438  0.22278  0.10039  132 ASN A O   
821  C CB  . ASN A 132 ? 1.01173 0.68210 1.03759 -0.01247 0.24487  -0.01047 132 ASN A CB  
822  C CG  . ASN A 132 ? 1.32698 0.96930 1.36049 -0.03596 0.26563  -0.05792 132 ASN A CG  
823  O OD1 . ASN A 132 ? 1.27865 0.87785 1.34488 -0.04972 0.29797  -0.06730 132 ASN A OD1 
824  N ND2 . ASN A 132 ? 1.34394 1.00998 1.34505 -0.04255 0.24841  -0.08867 132 ASN A ND2 
825  N N   . ARG A 133 ? 1.13653 0.82353 1.16598 0.00980  0.23952  0.08564  133 ARG A N   
826  C CA  . ARG A 133 ? 1.21992 0.94334 1.21954 0.01971  0.21864  0.11938  133 ARG A CA  
827  C C   . ARG A 133 ? 1.10317 0.87165 1.06567 0.01820  0.18917  0.09349  133 ARG A C   
828  O O   . ARG A 133 ? 1.16481 0.95072 1.11621 0.00092  0.18527  0.06468  133 ARG A O   
829  C CB  . ARG A 133 ? 1.13471 0.85457 1.13284 0.00454  0.23306  0.13305  133 ARG A CB  
830  C CG  . ARG A 133 ? 1.23528 0.90324 1.27589 -0.00244 0.26907  0.14592  133 ARG A CG  
831  C CD  . ARG A 133 ? 1.42890 1.08989 1.46834 0.01046  0.27615  0.20496  133 ARG A CD  
832  N NE  . ARG A 133 ? 1.49495 1.10043 1.58078 0.00690  0.31395  0.22447  133 ARG A NE  
833  C CZ  . ARG A 133 ? 1.69014 1.27729 1.78770 0.02184  0.32562  0.28284  133 ARG A CZ  
834  N NH1 . ARG A 133 ? 1.45463 1.07929 1.51603 0.03904  0.29967  0.32623  133 ARG A NH1 
835  N NH2 . ARG A 133 ? 1.94169 1.47175 2.08875 0.01863  0.36441  0.29875  133 ARG A NH2 
836  N N   . ALA A 134 ? 1.18513 1.01293 1.15134 -0.00711 0.49158  0.04280  134 ALA A N   
837  C CA  . ALA A 134 ? 1.17032 1.04401 1.12520 -0.00330 0.44601  0.03010  134 ALA A CA  
838  C C   . ALA A 134 ? 1.12791 0.98349 1.00657 0.01869  0.40873  0.06071  134 ALA A C   
839  O O   . ALA A 134 ? 1.12540 0.93400 0.95859 0.03290  0.41681  0.08960  134 ALA A O   
840  C CB  . ALA A 134 ? 1.05171 0.98586 1.06838 -0.01556 0.41803  -0.00433 134 ALA A CB  
841  N N   . GLY A 135 ? 1.03017 0.92316 0.89808 0.02292  0.36754  0.05188  135 GLY A N   
842  C CA  . GLY A 135 ? 0.88131 0.76973 0.69697 0.04072  0.32801  0.07109  135 GLY A CA  
843  C C   . GLY A 135 ? 0.88629 0.80762 0.73111 0.03573  0.29727  0.06023  135 GLY A C   
844  O O   . GLY A 135 ? 0.99928 0.95715 0.89412 0.02171  0.29586  0.03473  135 GLY A O   
845  N N   . TYR A 136 ? 0.84712 0.75465 0.66017 0.04909  0.27260  0.07767  136 TYR A N   
846  C CA  . TYR A 136 ? 0.89106 0.82048 0.72967 0.04469  0.25001  0.07029  136 TYR A CA  
847  C C   . TYR A 136 ? 0.87302 0.80802 0.68183 0.05821  0.21320  0.07752  136 TYR A C   
848  O O   . TYR A 136 ? 0.81513 0.72465 0.58135 0.07537  0.20470  0.09405  136 TYR A O   
849  C CB  . TYR A 136 ? 0.93993 0.84328 0.79048 0.04371  0.26581  0.08033  136 TYR A CB  
850  C CG  . TYR A 136 ? 0.90259 0.80653 0.79990 0.02692  0.30243  0.06725  136 TYR A CG  
851  C CD1 . TYR A 136 ? 0.88584 0.82650 0.83748 0.01147  0.29989  0.04198  136 TYR A CD1 
852  C CD2 . TYR A 136 ? 0.94609 0.81289 0.83434 0.02751  0.34141  0.07793  136 TYR A CD2 
853  C CE1 . TYR A 136 ? 0.99750 0.94326 1.00113 -0.00358 0.33204  0.02407  136 TYR A CE1 
854  C CE2 . TYR A 136 ? 1.02124 0.88881 0.96288 0.01058  0.37887  0.06225  136 TYR A CE2 
855  C CZ  . TYR A 136 ? 1.03302 0.94304 1.03630 -0.00529 0.37244  0.03341  136 TYR A CZ  
856  O OH  . TYR A 136 ? 0.99037 0.90520 1.05525 -0.02169 0.40838  0.01234  136 TYR A OH  
857  N N   . PHE A 137 ? 0.74278 0.70967 0.57444 0.05189  0.19283  0.06329  137 PHE A N   
858  C CA  . PHE A 137 ? 0.74750 0.71994 0.56476 0.06132  0.16323  0.06649  137 PHE A CA  
859  C C   . PHE A 137 ? 0.75477 0.73309 0.59912 0.05559  0.15703  0.06200  137 PHE A C   
860  O O   . PHE A 137 ? 0.86088 0.85759 0.73433 0.04327  0.16542  0.04835  137 PHE A O   
861  C CB  . PHE A 137 ? 0.79845 0.79714 0.61292 0.06072  0.14864  0.05520  137 PHE A CB  
862  C CG  . PHE A 137 ? 0.71812 0.71648 0.51325 0.06388  0.15568  0.05530  137 PHE A CG  
863  C CD1 . PHE A 137 ? 0.73675 0.74867 0.55246 0.05338  0.17471  0.04189  137 PHE A CD1 
864  C CD2 . PHE A 137 ? 0.82979 0.81601 0.59046 0.07778  0.14320  0.06530  137 PHE A CD2 
865  C CE1 . PHE A 137 ? 0.79208 0.80373 0.59494 0.05515  0.18367  0.03983  137 PHE A CE1 
866  C CE2 . PHE A 137 ? 0.85169 0.83693 0.59381 0.08048  0.15135  0.06476  137 PHE A CE2 
867  C CZ  . PHE A 137 ? 0.82398 0.82105 0.58751 0.06837  0.17290  0.05273  137 PHE A CZ  
868  N N   . ILE A 138 ? 0.84623 0.81021 0.68289 0.06575  0.14157  0.07046  138 ILE A N   
869  C CA  . ILE A 138 ? 0.87202 0.83894 0.73635 0.06081  0.13663  0.06579  138 ILE A CA  
870  C C   . ILE A 138 ? 0.80931 0.78342 0.67492 0.06696  0.11465  0.06150  138 ILE A C   
871  O O   . ILE A 138 ? 0.79161 0.75842 0.63765 0.08063  0.09937  0.06573  138 ILE A O   
872  C CB  . ILE A 138 ? 0.77993 0.72043 0.64675 0.06672  0.14258  0.07639  138 ILE A CB  
873  C CG1 . ILE A 138 ? 0.75726 0.70291 0.65841 0.06025  0.13821  0.06903  138 ILE A CG1 
874  C CG2 . ILE A 138 ? 0.75997 0.67613 0.59148 0.08895  0.12720  0.08898  138 ILE A CG2 
875  C CD1 . ILE A 138 ? 0.83381 0.76626 0.75601 0.05377  0.15703  0.07186  138 ILE A CD1 
876  N N   . PHE A 139 ? 0.74020 0.72695 0.63005 0.05761  0.11511  0.05155  139 PHE A N   
877  C CA  . PHE A 139 ? 0.74301 0.73313 0.64185 0.06057  0.10257  0.04582  139 PHE A CA  
878  C C   . PHE A 139 ? 0.82269 0.80653 0.75312 0.05673  0.10374  0.04115  139 PHE A C   
879  O O   . PHE A 139 ? 0.84312 0.83296 0.78920 0.04624  0.11481  0.03421  139 PHE A O   
880  C CB  . PHE A 139 ? 0.79506 0.79938 0.68789 0.05512  0.10670  0.03892  139 PHE A CB  
881  C CG  . PHE A 139 ? 0.81475 0.82725 0.68173 0.05963  0.10317  0.04062  139 PHE A CG  
882  C CD1 . PHE A 139 ? 0.79507 0.81738 0.65540 0.05492  0.11292  0.03806  139 PHE A CD1 
883  C CD2 . PHE A 139 ? 0.85276 0.86464 0.70850 0.06821  0.09085  0.04161  139 PHE A CD2 
884  C CE1 . PHE A 139 ? 0.81826 0.84918 0.66015 0.05858  0.11046  0.03693  139 PHE A CE1 
885  C CE2 . PHE A 139 ? 0.84490 0.86480 0.67869 0.07209  0.08788  0.04225  139 PHE A CE2 
886  C CZ  . PHE A 139 ? 0.82864 0.85783 0.65498 0.06723  0.09771  0.04018  139 PHE A CZ  
887  N N   . PRO A 140 ? 0.86987 0.84119 0.80954 0.06697  0.09169  0.04297  140 PRO A N   
888  C CA  . PRO A 140 ? 0.91401 0.88022 0.88925 0.06343  0.09266  0.03632  140 PRO A CA  
889  C C   . PRO A 140 ? 0.98771 0.95739 0.99362 0.06303  0.08636  0.02287  140 PRO A C   
890  O O   . PRO A 140 ? 1.03224 0.99895 1.07363 0.05803  0.09010  0.01430  140 PRO A O   
891  C CB  . PRO A 140 ? 0.79032 0.73927 0.75777 0.07904  0.08087  0.04369  140 PRO A CB  
892  C CG  . PRO A 140 ? 0.87178 0.81772 0.80533 0.09498  0.06580  0.04851  140 PRO A CG  
893  C CD  . PRO A 140 ? 0.89469 0.85365 0.80812 0.08436  0.07795  0.05138  140 PRO A CD  
894  N N   . ASP A 141 ? 0.83685 0.81165 0.83494 0.06762  0.07933  0.01934  141 ASP A N   
895  C CA  . ASP A 141 ? 0.98395 0.95936 1.01821 0.06879  0.07497  0.00430  141 ASP A CA  
896  C C   . ASP A 141 ? 1.01057 0.98811 1.03648 0.06108  0.08968  0.00353  141 ASP A C   
897  O O   . ASP A 141 ? 0.94998 0.92927 0.98071 0.06683  0.08316  -0.00233 141 ASP A O   
898  C CB  . ASP A 141 ? 1.02583 1.00210 1.06573 0.08757  0.04844  -0.00316 141 ASP A CB  
899  C CG  . ASP A 141 ? 1.36312 1.34345 1.45398 0.08926  0.04307  -0.02535 141 ASP A CG  
900  O OD1 . ASP A 141 ? 1.27600 1.25358 1.39626 0.07476  0.06446  -0.03227 141 ASP A OD1 
901  O OD2 . ASP A 141 ? 1.27128 1.25644 1.37302 0.10631  0.01869  -0.03755 141 ASP A OD2 
902  N N   . LEU A 142 ? 0.92523 0.90153 0.93493 0.05043  0.10910  0.00907  142 LEU A N   
903  C CA  . LEU A 142 ? 0.88099 0.85268 0.87502 0.04712  0.12448  0.00964  142 LEU A CA  
904  C C   . LEU A 142 ? 0.98465 0.94270 1.00430 0.03856  0.14632  0.00229  142 LEU A C   
905  O O   . LEU A 142 ? 1.05686 1.01433 1.08546 0.03173  0.15431  0.00090  142 LEU A O   
906  C CB  . LEU A 142 ? 0.90801 0.88672 0.85868 0.04665  0.12884  0.01823  142 LEU A CB  
907  C CG  . LEU A 142 ? 0.81593 0.80691 0.74193 0.05257  0.11408  0.02467  142 LEU A CG  
908  C CD1 . LEU A 142 ? 0.94316 0.94327 0.83933 0.05134  0.12046  0.02600  142 LEU A CD1 
909  C CD2 . LEU A 142 ? 0.88447 0.87569 0.80612 0.06126  0.10198  0.02465  142 LEU A CD2 
910  N N   . SER A 143 ? 0.92879 0.87376 0.96108 0.03869  0.15911  -0.00280 143 SER A N   
911  C CA  . SER A 143 ? 0.96117 0.88651 1.01516 0.03082  0.18692  -0.00916 143 SER A CA  
912  C C   . SER A 143 ? 1.00789 0.91231 1.02662 0.03415  0.20925  -0.00183 143 SER A C   
913  O O   . SER A 143 ? 1.02149 0.92620 1.02599 0.04121  0.20258  0.00176  143 SER A O   
914  C CB  . SER A 143 ? 1.16423 1.08676 1.28519 0.02753  0.18759  -0.02727 143 SER A CB  
915  O OG  . SER A 143 ? 1.26838 1.21003 1.41177 0.03308  0.15746  -0.03340 143 SER A OG  
916  N N   . VAL A 144 ? 0.89748 0.78130 0.89843 0.03105  0.23612  0.00067  144 VAL A N   
917  C CA  . VAL A 144 ? 0.92719 0.78183 0.88404 0.03834  0.26132  0.00963  144 VAL A CA  
918  C C   . VAL A 144 ? 1.08239 0.90491 1.07590 0.03139  0.29708  0.00240  144 VAL A C   
919  O O   . VAL A 144 ? 1.09052 0.91023 1.11997 0.02128  0.30919  -0.00724 144 VAL A O   
920  C CB  . VAL A 144 ? 0.95699 0.80864 0.85330 0.04561  0.26509  0.01741  144 VAL A CB  
921  C CG1 . VAL A 144 ? 1.01486 0.83370 0.85349 0.06004  0.28595  0.02801  144 VAL A CG1 
922  C CG2 . VAL A 144 ? 0.93192 0.81849 0.80976 0.04933  0.23232  0.01883  144 VAL A CG2 
923  N N   . ARG A 145 ? 1.10075 0.89772 1.08893 0.03637  0.31653  0.00595  145 ARG A N   
924  C CA  . ARG A 145 ? 1.12388 0.88860 1.15863 0.02843  0.35497  -0.00362 145 ARG A CA  
925  C C   . ARG A 145 ? 1.20062 0.92370 1.19594 0.02978  0.39669  0.00478  145 ARG A C   
926  O O   . ARG A 145 ? 1.19101 0.89659 1.23246 0.01814  0.42582  -0.00688 145 ARG A O   
927  C CB  . ARG A 145 ? 1.31156 1.06018 1.35610 0.03342  0.36539  -0.00294 145 ARG A CB  
928  C CG  . ARG A 145 ? 1.47147 1.25568 1.57695 0.03041  0.33289  -0.01965 145 ARG A CG  
929  C CD  . ARG A 145 ? 1.60454 1.38030 1.79998 0.01949  0.35416  -0.04465 145 ARG A CD  
930  N NE  . ARG A 145 ? 1.70075 1.49843 1.94617 0.02209  0.33251  -0.06143 145 ARG A NE  
931  C CZ  . ARG A 145 ? 1.79668 1.63024 2.10357 0.02107  0.29935  -0.08507 145 ARG A CZ  
932  N NH1 . ARG A 145 ? 1.93507 1.78507 2.26462 0.01671  0.28504  -0.09375 145 ARG A NH1 
933  N NH2 . ARG A 145 ? 1.72821 1.58051 2.07324 0.02681  0.27929  -0.10143 145 ARG A NH2 
934  N N   . ASN A 146 ? 1.18631 0.89386 1.09638 0.04551  0.39881  0.02271  146 ASN A N   
935  C CA  . ASN A 146 ? 1.13004 0.78995 0.98625 0.05373  0.43962  0.03258  146 ASN A CA  
936  C C   . ASN A 146 ? 1.15689 0.83118 0.95118 0.06415  0.42149  0.03725  146 ASN A C   
937  O O   . ASN A 146 ? 1.23443 0.94688 1.00956 0.07005  0.38157  0.03777  146 ASN A O   
938  C CB  . ASN A 146 ? 1.29103 0.90390 1.09339 0.07062  0.46695  0.04899  146 ASN A CB  
939  C CG  . ASN A 146 ? 1.28618 0.88929 1.15489 0.06079  0.48252  0.04169  146 ASN A CG  
940  O OD1 . ASN A 146 ? 1.28481 0.87609 1.22488 0.04445  0.51040  0.02677  146 ASN A OD1 
941  N ND2 . ASN A 146 ? 1.23164 0.84167 1.08250 0.07089  0.46423  0.04889  146 ASN A ND2 
942  N N   . GLU A 147 ? 1.19592 0.83922 0.96294 0.06629  0.45306  0.03807  147 GLU A N   
943  C CA  . GLU A 147 ? 1.32671 0.98444 1.04194 0.07645  0.43758  0.03718  147 GLU A CA  
944  C C   . GLU A 147 ? 1.38097 1.02681 1.00341 0.10537  0.42566  0.04954  147 GLU A C   
945  O O   . GLU A 147 ? 1.56988 1.17992 1.15477 0.11948  0.44201  0.06304  147 GLU A O   
946  C CB  . GLU A 147 ? 1.34527 0.97068 1.05318 0.07294  0.47602  0.03330  147 GLU A CB  
947  C CG  . GLU A 147 ? 1.50493 1.06042 1.16463 0.08523  0.52954  0.04659  147 GLU A CG  
948  C CD  . GLU A 147 ? 1.89911 1.42954 1.63796 0.06268  0.57104  0.03864  147 GLU A CD  
949  O OE1 . GLU A 147 ? 1.81213 1.36525 1.62546 0.04784  0.55843  0.03052  147 GLU A OE1 
950  O OE2 . GLU A 147 ? 1.89237 1.38081 1.62076 0.06079  0.61644  0.03798  147 GLU A OE2 
951  N N   . GLY A 148 ? 1.40142 1.07803 0.99091 0.11517  0.39664  0.04242  148 GLY A N   
952  C CA  . GLY A 148 ? 1.20277 0.87427 0.70836 0.14538  0.38008  0.04716  148 GLY A CA  
953  C C   . GLY A 148 ? 1.33914 1.07058 0.85707 0.14544  0.33344  0.03197  148 GLY A C   
954  O O   . GLY A 148 ? 1.39318 1.16175 0.97202 0.12408  0.32037  0.02004  148 GLY A O   
955  N N   . SER A 149 ? 1.16297 0.90085 0.62447 0.17062  0.31040  0.03178  149 SER A N   
956  C CA  . SER A 149 ? 1.31351 1.10582 0.78596 0.17363  0.26884  0.01438  149 SER A CA  
957  C C   . SER A 149 ? 1.36283 1.17427 0.84915 0.17354  0.24649  0.01915  149 SER A C   
958  O O   . SER A 149 ? 1.38777 1.16932 0.82734 0.19249  0.25197  0.03156  149 SER A O   
959  C CB  . SER A 149 ? 1.45005 1.24091 0.85053 0.20588  0.25626  0.00161  149 SER A CB  
960  O OG  . SER A 149 ? 1.90720 1.66508 1.23438 0.23706  0.25590  0.01267  149 SER A OG  
961  N N   . TYR A 150 ? 1.27827 1.13637 0.82548 0.15370  0.22315  0.00969  150 TYR A N   
962  C CA  . TYR A 150 ? 1.11600 0.99223 0.68286 0.15010  0.20493  0.01405  150 TYR A CA  
963  C C   . TYR A 150 ? 1.13486 1.06124 0.72609 0.14719  0.17423  -0.00387 150 TYR A C   
964  O O   . TYR A 150 ? 1.22275 1.17215 0.83250 0.14188  0.16882  -0.01947 150 TYR A O   
965  C CB  . TYR A 150 ? 1.03200 0.90552 0.65715 0.12593  0.21495  0.02399  150 TYR A CB  
966  C CG  . TYR A 150 ? 1.19945 1.02645 0.82027 0.12453  0.24853  0.03695  150 TYR A CG  
967  C CD1 . TYR A 150 ? 1.05048 0.86039 0.69263 0.11298  0.27293  0.03523  150 TYR A CD1 
968  C CD2 . TYR A 150 ? 1.11289 0.91225 0.71394 0.13391  0.25865  0.04916  150 TYR A CD2 
969  C CE1 . TYR A 150 ? 1.17647 0.94269 0.82289 0.11010  0.30847  0.04405  150 TYR A CE1 
970  C CE2 . TYR A 150 ? 1.16077 0.91533 0.76603 0.13123  0.29481  0.05878  150 TYR A CE2 
971  C CZ  . TYR A 150 ? 1.20304 0.94095 0.83219 0.11898  0.32064  0.05558  150 TYR A CZ  
972  O OH  . TYR A 150 ? 1.36013 1.05230 1.00108 0.11486  0.36124  0.06225  150 TYR A OH  
973  N N   . ARG A 151 ? 1.11379 1.05571 0.70839 0.15020  0.15691  -0.00275 151 ARG A N   
974  C CA  . ARG A 151 ? 0.94375 0.92969 0.57314 0.14258  0.13402  -0.01774 151 ARG A CA  
975  C C   . ARG A 151 ? 0.93475 0.92667 0.60112 0.12592  0.13189  -0.00619 151 ARG A C   
976  O O   . ARG A 151 ? 1.05603 1.02404 0.71269 0.12763  0.13991  0.00874  151 ARG A O   
977  C CB  . ARG A 151 ? 1.03012 1.03274 0.62581 0.16628  0.11240  -0.03321 151 ARG A CB  
978  C CG  . ARG A 151 ? 1.16921 1.18062 0.73729 0.18513  0.10463  -0.05466 151 ARG A CG  
979  C CD  . ARG A 151 ? 1.33202 1.36342 0.87354 0.21104  0.07850  -0.07433 151 ARG A CD  
980  N NE  . ARG A 151 ? 1.37595 1.41799 0.88906 0.23455  0.06611  -0.09993 151 ARG A NE  
981  C CZ  . ARG A 151 ? 1.29188 1.37705 0.84832 0.22977  0.05212  -0.13142 151 ARG A CZ  
982  N NH1 . ARG A 151 ? 1.20114 1.31829 0.82853 0.20168  0.05278  -0.13841 151 ARG A NH1 
983  N NH2 . ARG A 151 ? 1.37067 1.46504 0.89790 0.25539  0.03851  -0.15764 151 ARG A NH2 
984  N N   . PHE A 152 ? 0.84507 0.86693 0.55314 0.11121  0.12259  -0.01414 152 PHE A N   
985  C CA  . PHE A 152 ? 0.79559 0.82394 0.53017 0.09988  0.11793  -0.00519 152 PHE A CA  
986  C C   . PHE A 152 ? 0.82552 0.87650 0.55402 0.10749  0.10194  -0.01473 152 PHE A C   
987  O O   . PHE A 152 ? 0.88925 0.96360 0.62192 0.11194  0.09392  -0.03365 152 PHE A O   
988  C CB  . PHE A 152 ? 0.88067 0.91878 0.65886 0.08115  0.12169  -0.00442 152 PHE A CB  
989  C CG  . PHE A 152 ? 0.95066 0.96719 0.74605 0.07248  0.13261  0.00756  152 PHE A CG  
990  C CD1 . PHE A 152 ? 0.94118 0.94095 0.73377 0.07489  0.13373  0.01793  152 PHE A CD1 
991  C CD2 . PHE A 152 ? 0.79849 0.81325 0.61923 0.06213  0.14152  0.00506  152 PHE A CD2 
992  C CE1 . PHE A 152 ? 1.00324 0.98663 0.82185 0.06749  0.14288  0.02278  152 PHE A CE1 
993  C CE2 . PHE A 152 ? 0.94889 0.94615 0.79206 0.05504  0.15005  0.01191  152 PHE A CE2 
994  C CZ  . PHE A 152 ? 1.11628 1.09872 0.96032 0.05789  0.15040  0.01936  152 PHE A CZ  
995  N N   . SER A 153 ? 0.78174 0.82662 0.50425 0.10959  0.09764  -0.00472 153 SER A N   
996  C CA  . SER A 153 ? 0.71940 0.78458 0.44246 0.11389  0.08438  -0.01234 153 SER A CA  
997  C C   . SER A 153 ? 0.79874 0.86844 0.54917 0.09961  0.08538  -0.00405 153 SER A C   
998  O O   . SER A 153 ? 0.78909 0.84162 0.54279 0.09599  0.08911  0.00957  153 SER A O   
999  C CB  . SER A 153 ? 1.00278 1.05495 0.69017 0.13169  0.07818  -0.00818 153 SER A CB  
1000 O OG  . SER A 153 ? 1.02988 1.10511 0.71792 0.13848  0.06365  -0.02099 153 SER A OG  
1001 N N   . PHE A 154 ? 0.73305 0.82382 0.50453 0.09249  0.08389  -0.01399 154 PHE A N   
1002 C CA  . PHE A 154 ? 0.66512 0.75558 0.45262 0.08267  0.08700  -0.00570 154 PHE A CA  
1003 C C   . PHE A 154 ? 0.76356 0.86736 0.54631 0.08713  0.08023  -0.01192 154 PHE A C   
1004 O O   . PHE A 154 ? 0.84414 0.96818 0.63659 0.08879  0.07867  -0.02993 154 PHE A O   
1005 C CB  . PHE A 154 ? 0.79608 0.89146 0.60999 0.07070  0.09831  -0.00947 154 PHE A CB  
1006 C CG  . PHE A 154 ? 0.69725 0.78146 0.51949 0.06598  0.10464  -0.00538 154 PHE A CG  
1007 C CD1 . PHE A 154 ? 0.67446 0.73929 0.49894 0.06312  0.10612  0.00979  154 PHE A CD1 
1008 C CD2 . PHE A 154 ? 0.69221 0.78663 0.52154 0.06617  0.10751  -0.01982 154 PHE A CD2 
1009 C CE1 . PHE A 154 ? 0.72829 0.78354 0.56508 0.05836  0.11257  0.01143  154 PHE A CE1 
1010 C CE2 . PHE A 154 ? 0.67981 0.76363 0.51684 0.06155  0.11466  -0.01682 154 PHE A CE2 
1011 C CZ  . PHE A 154 ? 0.71077 0.77465 0.55283 0.05666  0.11823  -0.00071 154 PHE A CZ  
1012 N N   . HIS A 155 ? 0.71242 0.80678 0.48491 0.08947  0.07582  -0.00040 155 HIS A N   
1013 C CA  . HIS A 155 ? 0.75080 0.85575 0.51745 0.09397  0.06966  -0.00525 155 HIS A CA  
1014 C C   . HIS A 155 ? 0.80499 0.90696 0.57746 0.08711  0.07669  0.00082  155 HIS A C   
1015 O O   . HIS A 155 ? 0.85014 0.93612 0.61774 0.08669  0.07655  0.01409  155 HIS A O   
1016 C CB  . HIS A 155 ? 0.76519 0.86041 0.51361 0.10407  0.06019  0.00158  155 HIS A CB  
1017 C CG  . HIS A 155 ? 0.65338 0.73588 0.38789 0.11194  0.06017  0.00358  155 HIS A CG  
1018 N ND1 . HIS A 155 ? 0.83906 0.92661 0.55569 0.12475  0.05417  -0.00629 155 HIS A ND1 
1019 C CD2 . HIS A 155 ? 0.82260 0.88472 0.55658 0.11046  0.06730  0.01346  155 HIS A CD2 
1020 C CE1 . HIS A 155 ? 0.73466 0.80113 0.43245 0.13212  0.05932  0.00047  155 HIS A CE1 
1021 N NE2 . HIS A 155 ? 0.88025 0.93141 0.59153 0.12178  0.06928  0.01211  155 HIS A NE2 
1022 N N   . LEU A 156 ? 0.76414 0.87974 0.54589 0.08401  0.08308  -0.01036 156 LEU A N   
1023 C CA  . LEU A 156 ? 0.72154 0.82808 0.50191 0.07918  0.09578  -0.00381 156 LEU A CA  
1024 C C   . LEU A 156 ? 0.78966 0.89646 0.55290 0.08590  0.08848  -0.00148 156 LEU A C   
1025 O O   . LEU A 156 ? 0.87973 1.00331 0.64701 0.08935  0.08159  -0.01415 156 LEU A O   
1026 C CB  . LEU A 156 ? 0.78473 0.90177 0.59088 0.06990  0.11477  -0.01860 156 LEU A CB  
1027 C CG  . LEU A 156 ? 0.79736 0.89665 0.59688 0.06583  0.13581  -0.00993 156 LEU A CG  
1028 C CD1 . LEU A 156 ? 0.76465 0.83582 0.54763 0.06677  0.14168  0.01096  156 LEU A CD1 
1029 C CD2 . LEU A 156 ? 0.81604 0.92603 0.65002 0.05537  0.15967  -0.02890 156 LEU A CD2 
1030 N N   . PHE A 157 ? 0.86027 0.94885 0.60415 0.08980  0.08851  0.01283  157 PHE A N   
1031 C CA  . PHE A 157 ? 0.83398 0.92146 0.55975 0.09713  0.08251  0.01431  157 PHE A CA  
1032 C C   . PHE A 157 ? 0.88522 0.95699 0.59483 0.09684  0.10102  0.02010  157 PHE A C   
1033 O O   . PHE A 157 ? 0.96094 1.01150 0.65951 0.09780  0.11036  0.03196  157 PHE A O   
1034 C CB  . PHE A 157 ? 0.80437 0.88353 0.51870 0.10669  0.06432  0.02228  157 PHE A CB  
1035 C CG  . PHE A 157 ? 0.82450 0.91159 0.55188 0.10769  0.05280  0.01824  157 PHE A CG  
1036 C CD1 . PHE A 157 ? 0.92178 1.02209 0.65095 0.11076  0.04679  0.00953  157 PHE A CD1 
1037 C CD2 . PHE A 157 ? 0.77134 0.84911 0.50778 0.10667  0.05047  0.02336  157 PHE A CD2 
1038 C CE1 . PHE A 157 ? 0.85504 0.95421 0.58826 0.11470  0.04015  0.00874  157 PHE A CE1 
1039 C CE2 . PHE A 157 ? 0.82043 0.89818 0.56434 0.10839  0.04614  0.02135  157 PHE A CE2 
1040 C CZ  . PHE A 157 ? 0.84014 0.92617 0.57925 0.11329  0.04185  0.01538  157 PHE A CZ  
1041 N N   . GLU A 158 ? 0.92567 1.00443 0.63177 0.09686  0.10803  0.01218  158 GLU A N   
1042 C CA  . GLU A 158 ? 0.88579 0.94476 0.57145 0.09768  0.13097  0.01778  158 GLU A CA  
1043 C C   . GLU A 158 ? 1.05336 1.10478 0.70516 0.11090  0.12043  0.02264  158 GLU A C   
1044 O O   . GLU A 158 ? 1.11251 1.18377 0.77178 0.11345  0.10344  0.01304  158 GLU A O   
1045 C CB  . GLU A 158 ? 1.00017 1.07162 0.71473 0.08556  0.15489  0.00084  158 GLU A CB  
1046 C CG  . GLU A 158 ? 0.86835 0.91382 0.56209 0.08542  0.18673  0.00659  158 GLU A CG  
1047 C CD  . GLU A 158 ? 1.03525 1.09449 0.77052 0.07130  0.21407  -0.01510 158 GLU A CD  
1048 O OE1 . GLU A 158 ? 1.09787 1.18889 0.87813 0.06355  0.20430  -0.03602 158 GLU A OE1 
1049 O OE2 . GLU A 158 ? 1.09348 1.13087 0.81693 0.06942  0.24588  -0.01319 158 GLU A OE2 
1050 N N   . GLN A 159 ? 1.16889 1.18984 0.78122 0.12162  0.12996  0.03710  159 GLN A N   
1051 C CA  . GLN A 159 ? 1.01526 1.02556 0.58807 0.13808  0.12060  0.04059  159 GLN A CA  
1052 C C   . GLN A 159 ? 1.34056 1.32384 0.88261 0.13973  0.15452  0.04638  159 GLN A C   
1053 O O   . GLN A 159 ? 1.42857 1.37719 0.94159 0.14564  0.17427  0.06172  159 GLN A O   
1054 C CB  . GLN A 159 ? 1.27895 1.27401 0.82476 0.15634  0.09735  0.05055  159 GLN A CB  
1055 C CG  . GLN A 159 ? 1.32091 1.33325 0.86666 0.16809  0.06638  0.04086  159 GLN A CG  
1056 C CD  . GLN A 159 ? 1.54969 1.54816 1.07364 0.18867  0.04346  0.04466  159 GLN A CD  
1057 O OE1 . GLN A 159 ? 1.53444 1.51243 1.04736 0.19311  0.04737  0.05553  159 GLN A OE1 
1058 N NE2 . GLN A 159 ? 1.73267 1.74229 1.25166 0.20320  0.01895  0.03323  159 GLN A NE2 
1059 N N   . ILE A 160 ? 1.58989 1.58579 1.13787 0.13523  0.16369  0.03433  160 ILE A N   
1060 C CA  . ILE A 160 ? 1.59537 1.56812 1.12761 0.13145  0.20375  0.03541  160 ILE A CA  
1061 C C   . ILE A 160 ? 1.71232 1.65125 1.17576 0.15401  0.20697  0.04864  160 ILE A C   
1062 O O   . ILE A 160 ? 1.69018 1.64136 1.13532 0.16799  0.17679  0.04464  160 ILE A O   
1063 C CB  . ILE A 160 ? 1.73031 1.73473 1.30839 0.11567  0.21275  0.01201  160 ILE A CB  
1064 C CG1 . ILE A 160 ? 1.60949 1.63823 1.24896 0.09673  0.21906  -0.00267 160 ILE A CG1 
1065 C CG2 . ILE A 160 ? 1.82906 1.80988 1.38658 0.11496  0.25150  0.01055  160 ILE A CG2 
1066 C CD1 . ILE A 160 ? 1.57346 1.62617 1.26090 0.08247  0.23765  -0.02892 160 ILE A CD1 
1067 N N   . LYS A 161 ? 1.76246 1.65611 1.18621 0.15939  0.24503  0.06375  161 LYS A N   
1068 C CA  . LYS A 161 ? 2.00606 1.85861 1.35238 0.18466  0.25423  0.07775  161 LYS A CA  
1069 C C   . LYS A 161 ? 2.08774 1.91697 1.41802 0.17926  0.30109  0.07561  161 LYS A C   
1070 O O   . LYS A 161 ? 1.98627 1.78720 1.25175 0.20058  0.30658  0.08297  161 LYS A O   
1071 C CB  . LYS A 161 ? 1.78776 1.59334 1.07890 0.20563  0.25794  0.10210  161 LYS A CB  
1072 C CG  . LYS A 161 ? 1.59269 1.41905 0.92076 0.20105  0.22753  0.10263  161 LYS A CG  
1073 C CD  . LYS A 161 ? 1.79956 1.58317 1.07072 0.22745  0.22101  0.12357  161 LYS A CD  
1074 C CE  . LYS A 161 ? 1.76224 1.49421 1.00807 0.22603  0.27077  0.14325  161 LYS A CE  
1075 N NZ  . LYS A 161 ? 1.69717 1.41246 0.94342 0.23226  0.26214  0.15620  161 LYS A NZ  
1076 N N   . ASP A 162 ? 2.19714 2.03799 1.58644 0.15250  0.33497  0.06290  162 ASP A N   
1077 C CA  . ASP A 162 ? 2.30176 2.12609 1.69198 0.14372  0.38144  0.05470  162 ASP A CA  
1078 C C   . ASP A 162 ? 2.25707 2.13739 1.71561 0.12504  0.36707  0.02375  162 ASP A C   
1079 O O   . ASP A 162 ? 2.12613 2.04598 1.65610 0.10614  0.35563  0.00599  162 ASP A O   
1080 C CB  . ASP A 162 ? 2.39102 2.18152 1.80279 0.12842  0.43818  0.05936  162 ASP A CB  
1081 C CG  . ASP A 162 ? 2.55359 2.27034 1.88230 0.14945  0.47341  0.08990  162 ASP A CG  
1082 O OD1 . ASP A 162 ? 2.66876 2.36614 1.92877 0.17655  0.44425  0.10475  162 ASP A OD1 
1083 O OD2 . ASP A 162 ? 2.55236 2.23677 1.90441 0.13670  0.51654  0.09502  162 ASP A OD2 
1084 N N   . PRO A 163 ? 2.39803 2.28233 1.83506 0.13189  0.36631  0.01562  163 PRO A N   
1085 C CA  . PRO A 163 ? 2.33957 2.27796 1.83896 0.11783  0.34594  -0.01356 163 PRO A CA  
1086 C C   . PRO A 163 ? 2.21074 2.16963 1.78868 0.09183  0.37767  -0.03894 163 PRO A C   
1087 O O   . PRO A 163 ? 1.99490 2.00327 1.63396 0.08133  0.35258  -0.06430 163 PRO A O   
1088 C CB  . PRO A 163 ? 2.41339 2.34068 1.86530 0.13194  0.34865  -0.01476 163 PRO A CB  
1089 C CG  . PRO A 163 ? 2.41994 2.29253 1.77777 0.15870  0.35626  0.01423  163 PRO A CG  
1090 C CD  . PRO A 163 ? 2.38866 2.22562 1.74062 0.15475  0.38551  0.03208  163 PRO A CD  
1091 N N   . LYS A 164 ? 2.19928 2.12046 1.77905 0.08289  0.43254  -0.03481 164 LYS A N   
1092 C CA  . LYS A 164 ? 2.08125 2.02430 1.74765 0.05784  0.46377  -0.06464 164 LYS A CA  
1093 C C   . LYS A 164 ? 1.98574 1.97008 1.71405 0.04772  0.43266  -0.07807 164 LYS A C   
1094 O O   . LYS A 164 ? 1.76062 1.78753 1.56782 0.03265  0.42964  -0.11231 164 LYS A O   
1095 C CB  . LYS A 164 ? 2.19607 2.08349 1.85188 0.05083  0.53347  -0.05542 164 LYS A CB  
1096 C CG  . LYS A 164 ? 2.21847 2.05060 1.79969 0.06719  0.54327  -0.01624 164 LYS A CG  
1097 C CD  . LYS A 164 ? 2.21683 2.01084 1.82797 0.05277  0.59956  -0.01347 164 LYS A CD  
1098 C CE  . LYS A 164 ? 2.25603 2.00309 1.80622 0.06888  0.59579  0.02344  164 LYS A CE  
1099 N NZ  . LYS A 164 ? 2.31886 2.04362 1.92149 0.05151  0.63392  0.02154  164 LYS A NZ  
1100 N N   . ASP A 165 ? 1.90505 1.87772 1.59808 0.05786  0.40807  -0.05363 165 ASP A N   
1101 C CA  . ASP A 165 ? 1.64065 1.64638 1.38302 0.05003  0.38122  -0.06343 165 ASP A CA  
1102 C C   . ASP A 165 ? 1.47240 1.53006 1.24124 0.05313  0.32802  -0.08016 165 ASP A C   
1103 O O   . ASP A 165 ? 1.30112 1.38801 1.11098 0.04819  0.30585  -0.09216 165 ASP A O   
1104 C CB  . ASP A 165 ? 1.69630 1.67131 1.39135 0.06058  0.37249  -0.03206 165 ASP A CB  
1105 C CG  . ASP A 165 ? 1.72476 1.64417 1.39418 0.05930  0.42600  -0.01405 165 ASP A CG  
1106 O OD1 . ASP A 165 ? 1.59627 1.50701 1.30601 0.04413  0.47331  -0.03078 165 ASP A OD1 
1107 O OD2 . ASP A 165 ? 1.75946 1.64210 1.37022 0.07445  0.42202  0.01574  165 ASP A OD2 
1108 N N   . ALA A 166 ? 1.47299 1.53976 1.21692 0.06264  0.30861  -0.08089 166 ALA A N   
1109 C CA  . ALA A 166 ? 1.45439 1.56306 1.21825 0.06767  0.26120  -0.09341 166 ALA A CA  
1110 C C   . ALA A 166 ? 1.41290 1.56286 1.25194 0.05619  0.25826  -0.12955 166 ALA A C   
1111 O O   . ALA A 166 ? 1.38825 1.54027 1.26980 0.04360  0.29315  -0.15130 166 ALA A O   
1112 C CB  . ALA A 166 ? 1.55235 1.66153 1.28140 0.07904  0.24667  -0.09027 166 ALA A CB  
1113 N N   . THR A 167 ? 1.24119 1.42248 1.09675 0.06252  0.21686  -0.13753 167 THR A N   
1114 C CA  . THR A 167 ? 1.10266 1.32373 1.02155 0.05877  0.20469  -0.17268 167 THR A CA  
1115 C C   . THR A 167 ? 1.29144 1.53272 1.24154 0.05698  0.21030  -0.19969 167 THR A C   
1116 O O   . THR A 167 ? 1.42535 1.67316 1.35359 0.06676  0.18808  -0.19582 167 THR A O   
1117 C CB  . THR A 167 ? 1.08434 1.32577 0.99775 0.07158  0.15919  -0.17084 167 THR A CB  
1118 O OG1 . THR A 167 ? 1.14047 1.36184 1.02435 0.07280  0.15505  -0.14537 167 THR A OG1 
1119 C CG2 . THR A 167 ? 1.03528 1.31402 1.00653 0.07286  0.14522  -0.20777 167 THR A CG2 
1120 N N   . PRO A 184 ? 2.52313 2.67779 2.17400 0.25435  -0.10814 -0.10318 184 PRO A N   
1121 C CA  . PRO A 184 ? 2.47261 2.60251 2.07541 0.25492  -0.09449 -0.08087 184 PRO A CA  
1122 C C   . PRO A 184 ? 2.43287 2.55122 1.99078 0.24924  -0.07025 -0.06704 184 PRO A C   
1123 O O   . PRO A 184 ? 2.51270 2.64176 2.09236 0.23123  -0.05559 -0.06527 184 PRO A O   
1124 C CB  . PRO A 184 ? 2.39161 2.51943 2.03152 0.23475  -0.08351 -0.06888 184 PRO A CB  
1125 C CG  . PRO A 184 ? 2.35694 2.50308 2.06019 0.22978  -0.09486 -0.08617 184 PRO A CG  
1126 C CD  . PRO A 184 ? 2.36287 2.52547 2.07486 0.24520  -0.11359 -0.11023 184 PRO A CD  
1127 N N   . GLN A 185 ? 2.33978 2.43405 1.83571 0.26615  -0.06487 -0.05842 185 GLN A N   
1128 C CA  . GLN A 185 ? 2.30563 2.38254 1.75897 0.26107  -0.03523 -0.04563 185 GLN A CA  
1129 C C   . GLN A 185 ? 2.26205 2.31935 1.70973 0.24494  -0.00761 -0.02439 185 GLN A C   
1130 O O   . GLN A 185 ? 2.21672 2.25621 1.63504 0.23944  0.02217  -0.01466 185 GLN A O   
1131 C CB  . GLN A 185 ? 2.31220 2.36564 1.69427 0.28971  -0.03722 -0.04613 185 GLN A CB  
1132 C CG  . GLN A 185 ? 2.32425 2.39941 1.71064 0.30703  -0.06407 -0.07115 185 GLN A CG  
1133 C CD  . GLN A 185 ? 2.36142 2.41114 1.66872 0.34104  -0.06966 -0.07291 185 GLN A CD  
1134 O OE1 . GLN A 185 ? 2.44095 2.45165 1.68627 0.35327  -0.05236 -0.05271 185 GLN A OE1 
1135 N NE2 . GLN A 185 ? 2.38636 2.45553 1.69361 0.35819  -0.09286 -0.09734 185 GLN A NE2 
1136 N N   . GLU A 186 ? 2.17164 2.23159 1.65043 0.23694  -0.01469 -0.01914 186 GLU A N   
1137 C CA  . GLU A 186 ? 2.06790 2.11551 1.55323 0.21972  0.00909  -0.00304 186 GLU A CA  
1138 C C   . GLU A 186 ? 1.91248 1.98587 1.45655 0.19743  0.00867  -0.00833 186 GLU A C   
1139 O O   . GLU A 186 ? 1.93733 2.02932 1.51613 0.19756  -0.01174 -0.01903 186 GLU A O   
1140 C CB  . GLU A 186 ? 2.06546 2.09160 1.53349 0.23054  0.00264  0.00812  186 GLU A CB  
1141 C CG  . GLU A 186 ? 2.17993 2.16648 1.58293 0.24560  0.02241  0.02450  186 GLU A CG  
1142 C CD  . GLU A 186 ? 2.23366 2.19959 1.60916 0.26888  0.00322  0.02991  186 GLU A CD  
1143 O OE1 . GLU A 186 ? 2.13214 2.11503 1.52306 0.28391  -0.03114 0.01366  186 GLU A OE1 
1144 O OE2 . GLU A 186 ? 2.33664 2.26956 1.67937 0.27272  0.02274  0.04832  186 GLU A OE2 
1145 N N   . PHE A 187 ? 1.68440 1.75665 1.23909 0.18010  0.03257  -0.00217 187 PHE A N   
1146 C CA  . PHE A 187 ? 1.51856 1.61216 1.11899 0.16346  0.03216  -0.00769 187 PHE A CA  
1147 C C   . PHE A 187 ? 1.41555 1.50119 1.02775 0.15347  0.04202  0.00200  187 PHE A C   
1148 O O   . PHE A 187 ? 1.46793 1.53308 1.05817 0.15334  0.05946  0.01224  187 PHE A O   
1149 C CB  . PHE A 187 ? 1.56372 1.67134 1.17642 0.15344  0.04686  -0.01737 187 PHE A CB  
1150 C CG  . PHE A 187 ? 1.84521 1.97010 1.46615 0.15892  0.03286  -0.03040 187 PHE A CG  
1151 C CD1 . PHE A 187 ? 1.99922 2.12272 1.60658 0.17371  0.01396  -0.03359 187 PHE A CD1 
1152 C CD2 . PHE A 187 ? 1.90893 2.05285 1.55480 0.15062  0.03740  -0.04243 187 PHE A CD2 
1153 C CE1 . PHE A 187 ? 2.08822 2.22841 1.70782 0.17819  0.00223  -0.04739 187 PHE A CE1 
1154 C CE2 . PHE A 187 ? 2.02340 2.18216 1.67847 0.15583  0.02525  -0.05432 187 PHE A CE2 
1155 C CZ  . PHE A 187 ? 2.08582 2.24241 1.72825 0.16866  0.00888  -0.05621 187 PHE A CZ  
1156 N N   . LEU A 188 ? 1.10871 1.20794 0.75391 0.14612  0.03278  -0.00115 188 LEU A N   
1157 C CA  . LEU A 188 ? 1.01323 1.10876 0.67311 0.13673  0.04012  0.00497  188 LEU A CA  
1158 C C   . LEU A 188 ? 1.05182 1.16527 0.73651 0.12677  0.04525  -0.00437 188 LEU A C   
1159 O O   . LEU A 188 ? 1.15672 1.28271 0.85412 0.12940  0.03332  -0.01159 188 LEU A O   
1160 C CB  . LEU A 188 ? 1.05357 1.14516 0.72613 0.14047  0.02472  0.00850  188 LEU A CB  
1161 C CG  . LEU A 188 ? 1.02560 1.10735 0.70587 0.13405  0.03143  0.01670  188 LEU A CG  
1162 C CD1 . LEU A 188 ? 1.06340 1.12463 0.71821 0.13980  0.03834  0.02666  188 LEU A CD1 
1163 C CD2 . LEU A 188 ? 1.02335 1.10538 0.72622 0.13512  0.01913  0.01550  188 LEU A CD2 
1164 N N   . GLU A 189 ? 1.13923 0.91669 1.13141 0.11083  0.11878  -0.22889 189 GLU A N   
1165 C CA  . GLU A 189 ? 1.02428 0.78090 1.05319 0.13575  0.13038  -0.18152 189 GLU A CA  
1166 C C   . GLU A 189 ? 0.94073 0.72274 0.96429 0.14751  0.09877  -0.14055 189 GLU A C   
1167 O O   . GLU A 189 ? 1.00682 0.82096 0.98782 0.14893  0.06809  -0.13520 189 GLU A O   
1168 C CB  . GLU A 189 ? 0.88160 0.63612 0.89771 0.15070  0.13790  -0.17129 189 GLU A CB  
1169 C CG  . GLU A 189 ? 1.06920 0.78713 1.10739 0.14475  0.18121  -0.20125 189 GLU A CG  
1170 C CD  . GLU A 189 ? 1.42953 1.13895 1.48321 0.16676  0.19631  -0.17472 189 GLU A CD  
1171 O OE1 . GLU A 189 ? 1.46383 1.19484 1.47407 0.17045  0.17979  -0.17505 189 GLU A OE1 
1172 O OE2 . GLU A 189 ? 1.63219 1.31524 1.74576 0.18180  0.22649  -0.15057 189 GLU A OE2 
1173 N N   . PHE A 190 ? 0.82579 0.59246 0.89269 0.15616  0.11017  -0.11092 190 PHE A N   
1174 C CA  . PHE A 190 ? 0.84921 0.64024 0.91066 0.16773  0.08510  -0.06988 190 PHE A CA  
1175 C C   . PHE A 190 ? 0.94390 0.75384 0.99690 0.18575  0.07584  -0.03977 190 PHE A C   
1176 O O   . PHE A 190 ? 0.90805 0.70435 0.98883 0.19777  0.09793  -0.03033 190 PHE A O   
1177 C CB  . PHE A 190 ? 0.91454 0.68766 1.02131 0.17338  0.10238  -0.04308 190 PHE A CB  
1178 C CG  . PHE A 190 ? 0.84220 0.64369 0.94068 0.18461  0.07986  -0.00010 190 PHE A CG  
1179 C CD1 . PHE A 190 ? 0.74945 0.57038 0.81944 0.17342  0.05547  -0.00447 190 PHE A CD1 
1180 C CD2 . PHE A 190 ? 0.81161 0.62514 0.93232 0.20549  0.08439  0.04411  190 PHE A CD2 
1181 C CE1 . PHE A 190 ? 0.82127 0.66759 0.87996 0.17996  0.03852  0.02986  190 PHE A CE1 
1182 C CE2 . PHE A 190 ? 0.76635 0.61457 0.87404 0.21158  0.06297  0.07932  190 PHE A CE2 
1183 C CZ  . PHE A 190 ? 0.76134 0.62291 0.83572 0.19730  0.04151  0.06979  190 PHE A CZ  
1184 N N   . ARG A 191 ? 0.80903 0.65093 0.82810 0.18635  0.04623  -0.02663 191 ARG A N   
1185 C CA  . ARG A 191 ? 0.83635 0.70139 0.84750 0.19781  0.03709  -0.00425 191 ARG A CA  
1186 C C   . ARG A 191 ? 0.84058 0.73334 0.86282 0.20434  0.02411  0.03345  191 ARG A C   
1187 O O   . ARG A 191 ? 0.82540 0.73267 0.87691 0.21788  0.03061  0.06171  191 ARG A O   
1188 C CB  . ARG A 191 ? 0.86561 0.74526 0.82927 0.19143  0.02015  -0.02230 191 ARG A CB  
1189 C CG  . ARG A 191 ? 0.91122 0.77523 0.85759 0.18861  0.03284  -0.05267 191 ARG A CG  
1190 C CD  . ARG A 191 ? 0.90472 0.76003 0.87408 0.20023  0.05298  -0.04432 191 ARG A CD  
1191 N NE  . ARG A 191 ? 0.88265 0.71732 0.83801 0.19582  0.07219  -0.07600 191 ARG A NE  
1192 C CZ  . ARG A 191 ? 1.06793 0.87450 1.05642 0.19760  0.10269  -0.08661 191 ARG A CZ  
1193 N NH1 . ARG A 191 ? 1.02309 0.81807 1.06588 0.20784  0.11856  -0.06243 191 ARG A NH1 
1194 N NH2 . ARG A 191 ? 1.19606 0.98643 1.16308 0.18965  0.12075  -0.12077 191 ARG A NH2 
1195 N N   . LEU A 192 ? 0.78711 0.69229 0.78777 0.19485  0.00678  0.03508  192 LEU A N   
1196 C CA  . LEU A 192 ? 0.76038 0.69589 0.76306 0.19699  -0.00489 0.06635  192 LEU A CA  
1197 C C   . LEU A 192 ? 0.75916 0.69282 0.74414 0.18499  -0.01400 0.06146  192 LEU A C   
1198 O O   . LEU A 192 ? 0.75356 0.66799 0.72890 0.17630  -0.01363 0.03564  192 LEU A O   
1199 C CB  . LEU A 192 ? 0.78327 0.75342 0.76745 0.19539  -0.01846 0.07163  192 LEU A CB  
1200 C CG  . LEU A 192 ? 0.68954 0.66382 0.63439 0.18184  -0.03038 0.05105  192 LEU A CG  
1201 C CD1 . LEU A 192 ? 0.81852 0.83131 0.75402 0.17470  -0.03990 0.06193  192 LEU A CD1 
1202 C CD2 . LEU A 192 ? 0.76338 0.71804 0.69177 0.18283  -0.02511 0.02641  192 LEU A CD2 
1203 N N   . GLU A 193 ? 0.85555 0.81640 0.83427 0.18317  -0.02320 0.08513  193 GLU A N   
1204 C CA  . GLU A 193 ? 0.89329 0.85210 0.86004 0.17304  -0.02687 0.08584  193 GLU A CA  
1205 C C   . GLU A 193 ? 0.79627 0.79004 0.73428 0.16300  -0.04052 0.09317  193 GLU A C   
1206 O O   . GLU A 193 ? 0.81530 0.84357 0.75252 0.16539  -0.04659 0.10922  193 GLU A O   
1207 C CB  . GLU A 193 ? 0.75200 0.69910 0.74899 0.18139  -0.01208 0.11108  193 GLU A CB  
1208 C CG  . GLU A 193 ? 0.78058 0.72931 0.76791 0.17299  -0.01220 0.12061  193 GLU A CG  
1209 C CD  . GLU A 193 ? 1.09111 1.04216 1.10391 0.18636  0.00245  0.16090  193 GLU A CD  
1210 O OE1 . GLU A 193 ? 1.14550 1.11359 1.17809 0.20291  0.00606  0.18804  193 GLU A OE1 
1211 O OE2 . GLU A 193 ? 1.10778 1.04509 1.12382 0.18218  0.01239  0.16863  193 GLU A OE2 
1212 N N   . VAL A 194 ? 0.73633 0.72401 0.65391 0.15013  -0.04337 0.07892  194 VAL A N   
1213 C CA  . VAL A 194 ? 0.77861 0.79257 0.66961 0.13630  -0.04917 0.07977  194 VAL A CA  
1214 C C   . VAL A 194 ? 0.79749 0.80519 0.68344 0.12866  -0.04428 0.08587  194 VAL A C   
1215 O O   . VAL A 194 ? 0.87151 0.85090 0.77038 0.12965  -0.03819 0.07652  194 VAL A O   
1216 C CB  . VAL A 194 ? 0.85182 0.86117 0.72432 0.12798  -0.04964 0.05494  194 VAL A CB  
1217 C CG1 . VAL A 194 ? 0.76401 0.74713 0.63539 0.12625  -0.04568 0.03919  194 VAL A CG1 
1218 C CG2 . VAL A 194 ? 0.85033 0.88859 0.70155 0.11126  -0.04957 0.05232  194 VAL A CG2 
1219 N N   . ILE A 195 ? 0.91903 0.95780 0.78635 0.11943  -0.04635 0.10035  195 ILE A N   
1220 C CA  . ILE A 195 ? 0.83016 0.86741 0.68899 0.11266  -0.03914 0.11152  195 ILE A CA  
1221 C C   . ILE A 195 ? 1.00297 1.04459 0.83358 0.09182  -0.03516 0.09002  195 ILE A C   
1222 O O   . ILE A 195 ? 1.07013 1.14022 0.87979 0.07893  -0.03874 0.08065  195 ILE A O   
1223 C CB  . ILE A 195 ? 0.90955 0.98341 0.76451 0.11862  -0.04148 0.14823  195 ILE A CB  
1224 C CG1 . ILE A 195 ? 0.99146 1.05027 0.88452 0.14234  -0.03534 0.17449  195 ILE A CG1 
1225 C CG2 . ILE A 195 ? 1.00473 1.08115 0.83970 0.10832  -0.03239 0.15814  195 ILE A CG2 
1226 C CD1 . ILE A 195 ? 1.03581 1.04091 0.95730 0.14705  -0.02296 0.15571  195 ILE A CD1 
1227 N N   . SER A 196 ? 0.91355 0.92761 0.74831 0.08719  -0.02434 0.08081  196 SER A N   
1228 C CA  . SER A 196 ? 0.87473 0.88635 0.69035 0.06934  -0.01381 0.06135  196 SER A CA  
1229 C C   . SER A 196 ? 0.97892 1.01688 0.76436 0.05313  -0.00753 0.07083  196 SER A C   
1230 O O   . SER A 196 ? 0.95108 1.00810 0.73198 0.05914  -0.01175 0.09789  196 SER A O   
1231 C CB  . SER A 196 ? 0.89364 0.87230 0.73090 0.07179  -0.00380 0.04989  196 SER A CB  
1232 O OG  . SER A 196 ? 0.93405 0.90510 0.77624 0.06915  0.00578  0.06204  196 SER A OG  
1233 N N   . ASN A 197 ? 1.04319 1.08333 0.80752 0.03244  0.00556  0.04885  197 ASN A N   
1234 C CA  . ASN A 197 ? 1.10861 1.16970 0.83989 0.01212  0.01672  0.04967  197 ASN A CA  
1235 C C   . ASN A 197 ? 1.06003 1.09210 0.80203 0.01608  0.03101  0.05936  197 ASN A C   
1236 O O   . ASN A 197 ? 0.95646 0.95307 0.73310 0.02804  0.03526  0.05443  197 ASN A O   
1237 C CB  . ASN A 197 ? 0.98954 1.05324 0.70039 -0.01421 0.03447  0.01629  197 ASN A CB  
1238 C CG  . ASN A 197 ? 1.16198 1.26446 0.85812 -0.02616 0.02418  0.00450  197 ASN A CG  
1239 O OD1 . ASN A 197 ? 0.96439 1.11154 0.65095 -0.02187 0.00309  0.02433  197 ASN A OD1 
1240 N ND2 . ASN A 197 ? 1.19526 1.28195 0.89533 -0.04004 0.04151  -0.02600 197 ASN A ND2 
1241 N N   . PRO A 198 ? 0.96729 1.01907 0.68089 0.00630  0.03819  0.07451  198 PRO A N   
1242 C CA  . PRO A 198 ? 0.95452 0.97710 0.68015 0.00931  0.05590  0.08457  198 PRO A CA  
1243 C C   . PRO A 198 ? 1.04530 1.03539 0.78301 -0.00294 0.07857  0.05572  198 PRO A C   
1244 O O   . PRO A 198 ? 1.14463 1.13956 0.86316 -0.02167 0.08992  0.03036  198 PRO A O   
1245 C CB  . PRO A 198 ? 0.98954 1.04797 0.67057 -0.00135 0.06077  0.10641  198 PRO A CB  
1246 C CG  . PRO A 198 ? 1.01682 1.13060 0.67173 -0.00326 0.03807  0.11568  198 PRO A CG  
1247 C CD  . PRO A 198 ? 1.00172 1.10965 0.67027 -0.00859 0.03055  0.08380  198 PRO A CD  
1248 N N   . PHE A 199 ? 1.02971 0.98751 0.80530 0.00759  0.08817  0.05972  199 PHE A N   
1249 C CA  . PHE A 199 ? 1.01892 0.95026 0.81647 0.00032  0.11096  0.03970  199 PHE A CA  
1250 C C   . PHE A 199 ? 1.13824 1.05237 0.95196 0.00061  0.12863  0.05236  199 PHE A C   
1251 O O   . PHE A 199 ? 1.22237 1.13615 1.04446 0.01139  0.12218  0.07536  199 PHE A O   
1252 C CB  . PHE A 199 ? 1.00647 0.92338 0.84860 0.01502  0.10217  0.02757  199 PHE A CB  
1253 C CG  . PHE A 199 ? 1.10178 1.01141 0.98471 0.03274  0.08757  0.03792  199 PHE A CG  
1254 C CD1 . PHE A 199 ? 0.99282 0.91128 0.87360 0.04402  0.06670  0.05062  199 PHE A CD1 
1255 C CD2 . PHE A 199 ? 1.05106 0.94734 0.97855 0.03617  0.09748  0.03255  199 PHE A CD2 
1256 C CE1 . PHE A 199 ? 0.97057 0.87917 0.89014 0.05582  0.05925  0.05356  199 PHE A CE1 
1257 C CE2 . PHE A 199 ? 1.04181 0.93610 1.00821 0.04659  0.08590  0.03479  199 PHE A CE2 
1258 C CZ  . PHE A 199 ? 0.96782 0.86547 0.92885 0.05509  0.06846  0.04325  199 PHE A CZ  
1259 N N   . ILE A 200 ? 1.07709 0.97414 0.89952 -0.01114 0.15588  0.03764  200 ILE A N   
1260 C CA  . ILE A 200 ? 1.24437 1.12565 1.07597 -0.01607 0.17998  0.04678  200 ILE A CA  
1261 C C   . ILE A 200 ? 1.16146 1.02258 1.06004 -0.00644 0.18729  0.03846  200 ILE A C   
1262 O O   . ILE A 200 ? 1.08765 0.94471 1.01091 -0.00577 0.19369  0.02139  200 ILE A O   
1263 C CB  . ILE A 200 ? 1.16197 1.04349 0.94934 -0.04034 0.21058  0.03565  200 ILE A CB  
1264 C CG1 . ILE A 200 ? 1.35762 1.27162 1.08163 -0.05621 0.20120  0.02915  200 ILE A CG1 
1265 C CG2 . ILE A 200 ? 1.25321 1.12626 1.03040 -0.04449 0.23171  0.05487  200 ILE A CG2 
1266 C CD1 . ILE A 200 ? 1.20477 1.15231 0.90014 -0.04613 0.17203  0.05820  200 ILE A CD1 
1267 N N   . VAL A 201 ? 1.17409 1.02582 1.10537 0.00080  0.18888  0.05168  201 VAL A N   
1268 C CA  . VAL A 201 ? 1.13758 0.97891 1.13426 0.00449  0.19912  0.04275  201 VAL A CA  
1269 C C   . VAL A 201 ? 1.22100 1.04489 1.21795 -0.00827 0.23598  0.04629  201 VAL A C   
1270 O O   . VAL A 201 ? 1.10392 0.91963 1.07427 -0.01211 0.24797  0.06519  201 VAL A O   
1271 C CB  . VAL A 201 ? 1.07104 0.91319 1.11047 0.01546  0.18204  0.04734  201 VAL A CB  
1272 C CG1 . VAL A 201 ? 0.99377 0.83817 1.10400 0.01521  0.18977  0.03301  201 VAL A CG1 
1273 C CG2 . VAL A 201 ? 0.99684 0.85456 1.02750 0.02685  0.14868  0.04401  201 VAL A CG2 
1274 N N   . TYR A 202 ? 1.07497 0.89350 1.10226 -0.01321 0.25692  0.03126  202 TYR A N   
1275 C CA  . TYR A 202 ? 1.05321 0.85329 1.08329 -0.02638 0.29679  0.03102  202 TYR A CA  
1276 C C   . TYR A 202 ? 1.06458 0.86239 1.17489 -0.02123 0.30600  0.02844  202 TYR A C   
1277 O O   . TYR A 202 ? 1.03476 0.85156 1.19658 -0.00958 0.28100  0.02238  202 TYR A O   
1278 C CB  . TYR A 202 ? 1.16133 0.95453 1.17367 -0.03772 0.32275  0.01406  202 TYR A CB  
1279 C CG  . TYR A 202 ? 1.02440 0.82620 1.09271 -0.02468 0.31610  0.00270  202 TYR A CG  
1280 C CD1 . TYR A 202 ? 1.01814 0.82129 1.16090 -0.01780 0.33248  0.00068  202 TYR A CD1 
1281 C CD2 . TYR A 202 ? 1.13506 0.94822 1.18545 -0.01738 0.29389  -0.00242 202 TYR A CD2 
1282 C CE1 . TYR A 202 ? 1.13971 0.96009 1.33549 -0.00172 0.32523  -0.00203 202 TYR A CE1 
1283 C CE2 . TYR A 202 ? 1.04285 0.86580 1.14363 -0.00163 0.28973  -0.00572 202 TYR A CE2 
1284 C CZ  . TYR A 202 ? 1.14367 0.97262 1.31630 0.00739  0.30462  -0.00345 202 TYR A CZ  
1285 O OH  . TYR A 202 ? 1.16980 1.01751 1.39438 0.02691  0.29989  0.00036  202 TYR A OH  
1286 N N   . SER A 203 ? 1.16093 0.93987 1.28118 -0.03194 0.34291  0.03151  203 SER A N   
1287 C CA  . SER A 203 ? 1.32043 1.09983 1.52199 -0.03104 0.35863  0.02601  203 SER A CA  
1288 C C   . SER A 203 ? 1.30206 1.07205 1.52370 -0.03835 0.39636  0.01642  203 SER A C   
1289 O O   . SER A 203 ? 1.34983 1.09739 1.51721 -0.05205 0.42763  0.01748  203 SER A O   
1290 C CB  . SER A 203 ? 1.18792 0.94894 1.39951 -0.03624 0.37545  0.03949  203 SER A CB  
1291 O OG  . SER A 203 ? 1.49011 1.22923 1.62863 -0.04504 0.39932  0.05697  203 SER A OG  
1292 N N   . ALA A 204 ? 1.51833 1.30949 1.81784 -0.02923 0.39442  0.00744  204 ALA A N   
1293 C CA  . ALA A 204 ? 1.52334 1.30618 1.86054 -0.03261 0.43473  0.00134  204 ALA A CA  
1294 C C   . ALA A 204 ? 1.45021 1.21616 1.82023 -0.04424 0.47022  0.00353  204 ALA A C   
1295 O O   . ALA A 204 ? 1.56601 1.34743 1.99037 -0.04260 0.45843  0.00435  204 ALA A O   
1296 C CB  . ALA A 204 ? 1.29371 1.11389 1.71049 -0.01429 0.42008  -0.00127 204 ALA A CB  
1297 N N   . LYS A 205 ? 1.35574 1.08919 1.69151 -0.05845 0.51671  0.00194  205 LYS A N   
1298 C CA  . LYS A 205 ? 1.31838 1.03143 1.68024 -0.06985 0.55662  0.00549  205 LYS A CA  
1299 C C   . LYS A 205 ? 1.23062 0.96817 1.70780 -0.06232 0.56564  -0.00060 205 LYS A C   
1300 O O   . LYS A 205 ? 1.35568 1.12102 1.88383 -0.04892 0.55523  -0.00527 205 LYS A O   
1301 C CB  . LYS A 205 ? 1.33167 1.00877 1.63238 -0.08763 0.60739  0.00173  205 LYS A CB  
1302 C CG  . LYS A 205 ? 1.42737 1.09130 1.61303 -0.09926 0.60162  0.00951  205 LYS A CG  
1303 C CD  . LYS A 205 ? 1.36650 1.00509 1.48919 -0.12096 0.65061  -0.00221 205 LYS A CD  
1304 C CE  . LYS A 205 ? 1.59457 1.23634 1.60095 -0.13423 0.64061  0.00543  205 LYS A CE  
1305 N NZ  . LYS A 205 ? 1.83925 1.50041 1.83070 -0.11921 0.59301  0.03028  205 LYS A NZ  
1306 N N   . LYS A 206 ? 1.42167 1.15292 1.94368 -0.07019 0.58598  0.00170  206 LYS A N   
1307 C CA  . LYS A 206 ? 1.38890 1.15319 2.02666 -0.06638 0.59210  -0.00576 206 LYS A CA  
1308 C C   . LYS A 206 ? 1.35371 1.09650 2.02563 -0.07361 0.65078  -0.00782 206 LYS A C   
1309 O O   . LYS A 206 ? 1.26371 0.96150 1.88691 -0.08874 0.69313  -0.00388 206 LYS A O   
1310 C CB  . LYS A 206 ? 1.29004 1.06215 1.97059 -0.07390 0.58328  -0.00764 206 LYS A CB  
1311 C CG  . LYS A 206 ? 1.29242 1.08731 1.95432 -0.06752 0.52938  -0.00973 206 LYS A CG  
1312 C CD  . LYS A 206 ? 1.38348 1.22241 2.14289 -0.07172 0.51098  -0.02615 206 LYS A CD  
1313 C CE  . LYS A 206 ? 1.39421 1.25844 2.13621 -0.06659 0.45925  -0.03334 206 LYS A CE  
1314 N NZ  . LYS A 206 ? 1.47656 1.37412 2.30128 -0.07927 0.44965  -0.05519 206 LYS A NZ  
1315 N N   . PHE A 207 ? 1.21280 0.99024 1.96862 -0.06127 0.65461  -0.01149 207 PHE A N   
1316 C CA  . PHE A 207 ? 1.31196 1.07648 2.12544 -0.06467 0.71141  -0.01330 207 PHE A CA  
1317 C C   . PHE A 207 ? 1.48745 1.31653 2.43377 -0.05363 0.69729  -0.01424 207 PHE A C   
1318 O O   . PHE A 207 ? 1.41646 1.29582 2.41537 -0.03279 0.67061  -0.00884 207 PHE A O   
1319 C CB  . PHE A 207 ? 1.39902 1.14162 2.18264 -0.05840 0.73817  -0.01399 207 PHE A CB  
1320 C CG  . PHE A 207 ? 1.34058 1.02973 1.99508 -0.07495 0.75358  -0.01922 207 PHE A CG  
1321 C CD1 . PHE A 207 ? 1.26113 0.89775 1.85372 -0.09194 0.79289  -0.02683 207 PHE A CD1 
1322 C CD2 . PHE A 207 ? 1.15018 0.84380 1.73240 -0.07001 0.71217  -0.01917 207 PHE A CD2 
1323 C CE1 . PHE A 207 ? 1.25409 0.85625 1.72595 -0.10837 0.80061  -0.03325 207 PHE A CE1 
1324 C CE2 . PHE A 207 ? 1.09188 0.74881 1.55975 -0.08732 0.72359  -0.02568 207 PHE A CE2 
1325 C CZ  . PHE A 207 ? 1.15741 0.77401 1.57423 -0.10948 0.77458  -0.03194 207 PHE A CZ  
1326 N N   . PRO A 208 ? 1.57427 1.40883 2.57940 -0.06713 0.71498  -0.01995 208 PRO A N   
1327 C CA  . PRO A 208 ? 1.53723 1.44751 2.66621 -0.06201 0.69048  -0.02631 208 PRO A CA  
1328 C C   . PRO A 208 ? 1.42322 1.37559 2.63201 -0.04100 0.69178  -0.01854 208 PRO A C   
1329 O O   . PRO A 208 ? 1.50013 1.52926 2.76906 -0.02318 0.65199  -0.01293 208 PRO A O   
1330 C CB  . PRO A 208 ? 1.56842 1.44987 2.72054 -0.08174 0.71786  -0.03632 208 PRO A CB  
1331 C CG  . PRO A 208 ? 1.57142 1.36335 2.61631 -0.08963 0.76006  -0.03025 208 PRO A CG  
1332 C CD  . PRO A 208 ? 1.43545 1.20753 2.38410 -0.08646 0.75038  -0.02129 208 PRO A CD  
1333 N N   . GLY A 209 ? 1.14929 1.05115 2.35345 -0.04069 0.73411  -0.01590 209 GLY A N   
1334 C CA  . GLY A 209 ? 1.13918 1.07282 2.41916 -0.02041 0.73749  -0.00395 209 GLY A CA  
1335 C C   . GLY A 209 ? 1.43497 1.36615 2.68606 0.00110  0.73253  0.01180  209 GLY A C   
1336 O O   . GLY A 209 ? 1.45531 1.42112 2.77326 0.02248  0.72975  0.02897  209 GLY A O   
1337 N N   . LEU A 210 ? 1.48906 1.38058 2.64275 -0.00398 0.73229  0.00804  210 LEU A N   
1338 C CA  . LEU A 210 ? 1.40504 1.28261 2.52145 0.01301  0.73243  0.01880  210 LEU A CA  
1339 C C   . LEU A 210 ? 1.46020 1.41357 2.60685 0.03484  0.68062  0.03096  210 LEU A C   
1340 O O   . LEU A 210 ? 1.49090 1.48533 2.69198 0.06148  0.66631  0.05173  210 LEU A O   
1341 C CB  . LEU A 210 ? 1.37510 1.17391 2.36530 -0.00632 0.75816  0.00464  210 LEU A CB  
1342 C CG  . LEU A 210 ? 1.44691 1.17262 2.38586 -0.01024 0.80243  -0.00165 210 LEU A CG  
1343 C CD1 . LEU A 210 ? 1.32500 1.00191 2.13689 -0.03031 0.80884  -0.01832 210 LEU A CD1 
1344 C CD2 . LEU A 210 ? 1.35576 1.09796 2.35270 0.01566  0.80236  0.01682  210 LEU A CD2 
1345 N N   . THR A 211 ? 1.38821 1.35370 2.48533 0.02441  0.64454  0.02052  211 THR A N   
1346 C CA  . THR A 211 ? 1.37998 1.40239 2.47311 0.04255  0.58003  0.02850  211 THR A CA  
1347 C C   . THR A 211 ? 1.69015 1.81178 2.89538 0.05498  0.54350  0.03426  211 THR A C   
1348 O O   . THR A 211 ? 1.66168 1.84695 2.89401 0.07931  0.50291  0.05005  211 THR A O   
1349 C CB  . THR A 211 ? 1.54894 1.54318 2.53972 0.02546  0.54304  0.01444  211 THR A CB  
1350 O OG1 . THR A 211 ? 1.60564 1.57002 2.58550 -0.00052 0.56093  -0.00013 211 THR A OG1 
1351 C CG2 . THR A 211 ? 1.15713 1.08683 2.04002 0.02302  0.55663  0.01451  211 THR A CG2 
1352 N N   . THR A 212 ? 2.08655 2.22700 3.35730 0.03776  0.55792  0.02155  212 THR A N   
1353 C CA  . THR A 212 ? 2.10008 2.34376 3.48581 0.04335  0.52669  0.02113  212 THR A CA  
1354 C C   . THR A 212 ? 2.06359 2.37292 3.43154 0.04588  0.45514  0.01396  212 THR A C   
1355 O O   . THR A 212 ? 2.19049 2.54321 3.59157 0.02544  0.42882  -0.00950 212 THR A O   
1356 C CB  . THR A 212 ? 2.09013 2.37812 3.55004 0.07240  0.53356  0.04965  212 THR A CB  
1357 O OG1 . THR A 212 ? 1.88661 2.09819 3.33974 0.06535  0.59051  0.05221  212 THR A OG1 
1358 C CG2 . THR A 212 ? 2.15631 2.56008 3.71763 0.07646  0.49075  0.04972  212 THR A CG2 
1359 N N   . GLY B 15  ? 1.27609 1.62851 1.88296 -0.04633 0.17081  0.37154  15  GLY B N   
1360 C CA  . GLY B 15  ? 1.23507 1.67911 1.74353 -0.00837 0.20850  0.35995  15  GLY B CA  
1361 C C   . GLY B 15  ? 1.30449 1.67849 1.69414 0.02347  0.17613  0.30535  15  GLY B C   
1362 O O   . GLY B 15  ? 1.21024 1.65211 1.53148 0.04730  0.19361  0.26594  15  GLY B O   
1363 N N   . ASN B 16  ? 1.39372 1.63401 1.76311 0.02247  0.12989  0.30009  16  ASN B N   
1364 C CA  . ASN B 16  ? 1.25095 1.41683 1.51099 0.05007  0.09449  0.24895  16  ASN B CA  
1365 C C   . ASN B 16  ? 1.18256 1.29533 1.45326 0.03771  0.04119  0.18448  16  ASN B C   
1366 O O   . ASN B 16  ? 1.29363 1.33655 1.48033 0.05650  0.00626  0.14199  16  ASN B O   
1367 C CB  . ASN B 16  ? 1.37339 1.42857 1.59963 0.06092  0.07300  0.27459  16  ASN B CB  
1368 C CG  . ASN B 16  ? 1.71157 1.69971 2.05362 0.02502  0.05764  0.31555  16  ASN B CG  
1369 O OD1 . ASN B 16  ? 1.65171 1.67935 2.09852 -0.00926 0.06181  0.32416  16  ASN B OD1 
1370 N ND2 . ASN B 16  ? 1.70458 1.59178 2.03287 0.03240  0.04076  0.33816  16  ASN B ND2 
1371 N N   . SER B 17  ? 1.08261 1.23013 1.45315 0.00866  0.03374  0.17724  17  SER B N   
1372 C CA  . SER B 17  ? 0.99889 1.09564 1.38705 -0.00054 -0.01979 0.12304  17  SER B CA  
1373 C C   . SER B 17  ? 0.91785 1.10872 1.35898 -0.00856 -0.00258 0.10266  17  SER B C   
1374 O O   . SER B 17  ? 0.80743 1.10224 1.29387 -0.01469 0.04720  0.13059  17  SER B O   
1375 C CB  . SER B 17  ? 0.88617 0.89639 1.35945 -0.02920 -0.06721 0.12805  17  SER B CB  
1376 O OG  . SER B 17  ? 0.99708 1.06030 1.59455 -0.06151 -0.06300 0.13930  17  SER B OG  
1377 N N   . ASN B 18  ? 0.77185 0.92817 1.20550 -0.00565 -0.04428 0.05311  18  ASN B N   
1378 C CA  . ASN B 18  ? 0.69963 0.92597 1.19251 -0.01157 -0.03848 0.02989  18  ASN B CA  
1379 C C   . ASN B 18  ? 0.71064 0.86844 1.21871 -0.01304 -0.10116 -0.01013 18  ASN B C   
1380 O O   . ASN B 18  ? 0.84418 0.91553 1.27658 0.00103  -0.14051 -0.03314 18  ASN B O   
1381 C CB  . ASN B 18  ? 0.73856 1.03730 1.16464 0.01265  0.00470  0.00777  18  ASN B CB  
1382 C CG  . ASN B 18  ? 0.76383 1.15308 1.26970 0.00556  0.02446  -0.00808 18  ASN B CG  
1383 O OD1 . ASN B 18  ? 0.73485 1.17649 1.34746 -0.01784 0.03136  0.01419  18  ASN B OD1 
1384 N ND2 . ASN B 18  ? 0.73776 1.14493 1.19577 0.02540  0.03453  -0.04838 18  ASN B ND2 
1385 N N   . SER B 19  ? 0.97927 1.18341 1.58536 -0.02797 -0.11061 -0.01873 19  SER B N   
1386 C CA  . SER B 19  ? 0.93878 1.09349 1.57343 -0.02786 -0.17071 -0.05249 19  SER B CA  
1387 C C   . SER B 19  ? 0.77364 0.99054 1.44033 -0.01707 -0.16281 -0.07628 19  SER B C   
1388 O O   . SER B 19  ? 0.81670 1.12648 1.53883 -0.02398 -0.11700 -0.06442 19  SER B O   
1389 C CB  . SER B 19  ? 0.87554 1.01421 1.62110 -0.05926 -0.20340 -0.04134 19  SER B CB  
1390 O OG  . SER B 19  ? 1.12874 1.17627 1.83952 -0.06298 -0.23600 -0.04018 19  SER B OG  
1391 N N   . VAL B 20  ? 0.76950 0.93687 1.40503 0.00122  -0.20851 -0.10944 20  VAL B N   
1392 C CA  . VAL B 20  ? 0.72615 0.93545 1.39274 0.01604  -0.20825 -0.13146 20  VAL B CA  
1393 C C   . VAL B 20  ? 0.78284 0.94260 1.46948 0.02476  -0.27562 -0.15411 20  VAL B C   
1394 O O   . VAL B 20  ? 0.88339 0.96513 1.49945 0.03487  -0.31693 -0.16570 20  VAL B O   
1395 C CB  . VAL B 20  ? 0.67531 0.88442 1.24561 0.04248  -0.17345 -0.14719 20  VAL B CB  
1396 C CG1 . VAL B 20  ? 0.72274 0.91891 1.29426 0.06534  -0.19598 -0.17316 20  VAL B CG1 
1397 C CG2 . VAL B 20  ? 0.81760 1.12265 1.41340 0.03602  -0.10446 -0.13585 20  VAL B CG2 
1398 N N   . SER B 21  ? 0.67374 0.88717 1.45771 0.02293  -0.28739 -0.16242 21  SER B N   
1399 C CA  . SER B 21  ? 0.94658 1.13334 1.76213 0.03408  -0.35113 -0.18399 21  SER B CA  
1400 C C   . SER B 21  ? 0.92166 1.11772 1.72027 0.06802  -0.35501 -0.20032 21  SER B C   
1401 O O   . SER B 21  ? 0.80915 1.06014 1.63281 0.07281  -0.30873 -0.19837 21  SER B O   
1402 C CB  . SER B 21  ? 0.81801 1.06002 1.77089 0.00558  -0.36941 -0.18257 21  SER B CB  
1403 O OG  . SER B 21  ? 1.05438 1.30884 2.04375 -0.02977 -0.34039 -0.15686 21  SER B OG  
1404 N N   . ARG B 22  ? 0.91501 1.05786 1.67102 0.09316  -0.40984 -0.21655 22  ARG B N   
1405 C CA  . ARG B 22  ? 0.96398 1.10487 1.70556 0.12924  -0.42097 -0.22646 22  ARG B CA  
1406 C C   . ARG B 22  ? 1.11807 1.24965 1.89155 0.14537  -0.49235 -0.24124 22  ARG B C   
1407 O O   . ARG B 22  ? 1.16294 1.28325 1.95725 0.12787  -0.53158 -0.24967 22  ARG B O   
1408 C CB  . ARG B 22  ? 1.10204 1.17932 1.71356 0.15392  -0.40082 -0.22586 22  ARG B CB  
1409 C CG  . ARG B 22  ? 1.16676 1.16791 1.68260 0.17411  -0.45342 -0.23307 22  ARG B CG  
1410 C CD  . ARG B 22  ? 1.10881 1.05655 1.50921 0.19971  -0.42988 -0.23155 22  ARG B CD  
1411 N NE  . ARG B 22  ? 1.10203 0.98225 1.39268 0.20806  -0.46275 -0.23705 22  ARG B NE  
1412 C CZ  . ARG B 22  ? 1.30898 1.15878 1.56604 0.23214  -0.52120 -0.24328 22  ARG B CZ  
1413 N NH1 . ARG B 22  ? 1.32539 1.20356 1.64704 0.25272  -0.55530 -0.24306 22  ARG B NH1 
1414 N NH2 . ARG B 22  ? 1.52878 1.32554 1.68427 0.23826  -0.54650 -0.25134 22  ARG B NH2 
1415 N N   . ILE B 23  ? 1.16030 1.29935 1.94075 0.18070  -0.50909 -0.24594 23  ILE B N   
1416 C CA  . ILE B 23  ? 1.20724 1.34923 2.01268 0.20505  -0.57703 -0.25968 23  ILE B CA  
1417 C C   . ILE B 23  ? 1.34458 1.42527 2.04096 0.25017  -0.59540 -0.25431 23  ILE B C   
1418 O O   . ILE B 23  ? 1.33143 1.39906 1.99974 0.27061  -0.55716 -0.24228 23  ILE B O   
1419 C CB  . ILE B 23  ? 0.96064 1.18542 1.89723 0.20925  -0.58581 -0.26744 23  ILE B CB  
1420 C CG1 . ILE B 23  ? 1.04033 1.33105 2.08306 0.16156  -0.55376 -0.26751 23  ILE B CG1 
1421 C CG2 . ILE B 23  ? 1.28175 1.50796 2.22454 0.22718  -0.64384 -0.28206 23  ILE B CG2 
1422 C CD1 . ILE B 23  ? 0.92291 1.28881 2.08282 0.15479  -0.56731 -0.27971 23  ILE B CD1 
1423 N N   . THR B 24  ? 1.37361 1.41909 2.01140 0.26499  -0.65190 -0.26405 24  THR B N   
1424 C CA  . THR B 24  ? 1.60577 1.59216 2.12617 0.30331  -0.66206 -0.25367 24  THR B CA  
1425 C C   . THR B 24  ? 1.65658 1.66797 2.20519 0.33557  -0.68088 -0.24847 24  THR B C   
1426 O O   . THR B 24  ? 1.69416 1.76823 2.35046 0.32957  -0.68613 -0.25639 24  THR B O   
1427 C CB  . THR B 24  ? 1.71959 1.65465 2.14016 0.29650  -0.68734 -0.26388 24  THR B CB  
1428 O OG1 . THR B 24  ? 1.88070 1.77514 2.19918 0.33170  -0.69679 -0.25273 24  THR B OG1 
1429 C CG2 . THR B 24  ? 1.73705 1.70488 2.22229 0.27589  -0.72127 -0.28654 24  THR B CG2 
1430 N N   . ARG B 25  ? 1.71995 1.68474 2.16853 0.37003  -0.68893 -0.23338 25  ARG B N   
1431 C CA  . ARG B 25  ? 1.77817 1.76427 2.24323 0.40599  -0.70468 -0.22154 25  ARG B CA  
1432 C C   . ARG B 25  ? 1.81546 1.85055 2.32254 0.40334  -0.75019 -0.24252 25  ARG B C   
1433 O O   . ARG B 25  ? 1.61469 1.69746 2.18296 0.42403  -0.76442 -0.24143 25  ARG B O   
1434 C CB  . ARG B 25  ? 1.68981 1.61491 2.03601 0.44123  -0.69769 -0.19429 25  ARG B CB  
1435 C CG  . ARG B 25  ? 1.78169 1.66110 2.10227 0.44998  -0.64735 -0.17430 25  ARG B CG  
1436 C CD  . ARG B 25  ? 1.95964 1.77285 2.16060 0.47896  -0.63598 -0.14588 25  ARG B CD  
1437 N NE  . ARG B 25  ? 2.17169 1.93971 2.36173 0.48723  -0.58209 -0.13029 25  ARG B NE  
1438 C CZ  . ARG B 25  ? 2.21428 1.91427 2.30212 0.50103  -0.55639 -0.10927 25  ARG B CZ  
1439 N NH1 . ARG B 25  ? 2.36990 2.04389 2.35446 0.50910  -0.58010 -0.09819 25  ARG B NH1 
1440 N NH2 . ARG B 25  ? 2.07524 1.73624 2.16912 0.50441  -0.50072 -0.10275 25  ARG B NH2 
1441 N N   . GLU B 26  ? 1.88045 1.90568 2.35851 0.37934  -0.77093 -0.26408 26  GLU B N   
1442 C CA  . GLU B 26  ? 1.77994 1.85008 2.29856 0.37552  -0.81086 -0.29031 26  GLU B CA  
1443 C C   . GLU B 26  ? 1.74052 1.87421 2.39577 0.34567  -0.81400 -0.31147 26  GLU B C   
1444 O O   . GLU B 26  ? 1.57753 1.75730 2.28284 0.34265  -0.84515 -0.33621 26  GLU B O   
1445 C CB  . GLU B 26  ? 1.83077 1.86633 2.28173 0.35892  -0.82452 -0.30889 26  GLU B CB  
1446 C CG  . GLU B 26  ? 2.03353 2.03371 2.36210 0.38990  -0.83232 -0.29677 26  GLU B CG  
1447 C CD  . GLU B 26  ? 2.24007 2.17828 2.47929 0.37233  -0.81358 -0.29859 26  GLU B CD  
1448 O OE1 . GLU B 26  ? 2.27081 2.16280 2.45609 0.37192  -0.78067 -0.27734 26  GLU B OE1 
1449 O OE2 . GLU B 26  ? 2.29076 2.22931 2.51693 0.36014  -0.82994 -0.32293 26  GLU B OE2 
1450 N N   . GLY B 27  ? 1.99767 2.14113 2.71633 0.32269  -0.77982 -0.30347 27  GLY B N   
1451 C CA  . GLY B 27  ? 1.91586 2.12129 2.76257 0.28780  -0.77411 -0.31993 27  GLY B CA  
1452 C C   . GLY B 27  ? 2.07811 2.27029 2.94842 0.24134  -0.76815 -0.33268 27  GLY B C   
1453 O O   . GLY B 27  ? 2.10618 2.34674 3.08312 0.20655  -0.75580 -0.34101 27  GLY B O   
1454 N N   . LYS B 28  ? 1.87374 2.00175 2.64784 0.23940  -0.77314 -0.33254 28  LYS B N   
1455 C CA  . LYS B 28  ? 1.74061 1.84735 2.53211 0.19840  -0.76493 -0.34083 28  LYS B CA  
1456 C C   . LYS B 28  ? 1.51631 1.62358 2.33323 0.17492  -0.72139 -0.31969 28  LYS B C   
1457 O O   . LYS B 28  ? 1.52612 1.61972 2.29447 0.19587  -0.69881 -0.30144 28  LYS B O   
1458 C CB  . LYS B 28  ? 1.84479 1.88461 2.52212 0.20702  -0.77955 -0.34791 28  LYS B CB  
1459 C CG  . LYS B 28  ? 1.96285 2.00968 2.60546 0.23285  -0.81804 -0.36884 28  LYS B CG  
1460 C CD  . LYS B 28  ? 2.00842 1.99422 2.53236 0.24352  -0.82118 -0.37168 28  LYS B CD  
1461 C CE  . LYS B 28  ? 2.07137 2.07180 2.54190 0.27790  -0.85159 -0.38380 28  LYS B CE  
1462 N NZ  . LYS B 28  ? 2.16955 2.11667 2.51776 0.29138  -0.84416 -0.37926 28  LYS B NZ  
1463 N N   . LYS B 29  ? 1.27107 1.39845 2.16853 0.13136  -0.70680 -0.32188 29  LYS B N   
1464 C CA  . LYS B 29  ? 1.21305 1.34853 2.13516 0.10493  -0.66355 -0.30119 29  LYS B CA  
1465 C C   . LYS B 29  ? 1.26005 1.32545 2.09299 0.09489  -0.66267 -0.29868 29  LYS B C   
1466 O O   . LYS B 29  ? 1.28312 1.31512 2.11017 0.08017  -0.68386 -0.31268 29  LYS B O   
1467 C CB  . LYS B 29  ? 1.09664 1.29533 2.15361 0.06170  -0.64046 -0.29761 29  LYS B CB  
1468 C CG  . LYS B 29  ? 1.00572 1.19757 2.07397 0.02492  -0.59262 -0.27321 29  LYS B CG  
1469 C CD  . LYS B 29  ? 0.94830 1.22267 2.12901 -0.00236 -0.54649 -0.25627 29  LYS B CD  
1470 C CE  . LYS B 29  ? 0.99959 1.26732 2.18351 -0.03888 -0.49174 -0.22448 29  LYS B CE  
1471 N NZ  . LYS B 29  ? 1.09552 1.45262 2.40284 -0.07096 -0.45318 -0.20889 29  LYS B NZ  
1472 N N   . ILE B 30  ? 1.18261 1.21632 1.92636 0.10478  -0.61801 -0.27753 30  ILE B N   
1473 C CA  . ILE B 30  ? 1.19049 1.15683 1.83022 0.09999  -0.60467 -0.27258 30  ILE B CA  
1474 C C   . ILE B 30  ? 1.00557 0.98584 1.65649 0.07331  -0.53670 -0.24490 30  ILE B C   
1475 O O   . ILE B 30  ? 1.04044 1.05897 1.69746 0.07882  -0.48938 -0.22986 30  ILE B O   
1476 C CB  . ILE B 30  ? 1.20050 1.11744 1.70624 0.13855  -0.60973 -0.27448 30  ILE B CB  
1477 C CG1 . ILE B 30  ? 1.19457 1.10361 1.68092 0.16832  -0.66871 -0.29419 30  ILE B CG1 
1478 C CG2 . ILE B 30  ? 1.07459 0.93027 1.47441 0.13345  -0.59389 -0.27291 30  ILE B CG2 
1479 C CD1 . ILE B 30  ? 1.41674 1.26015 1.75807 0.19546  -0.66968 -0.29446 30  ILE B CD1 
1480 N N   . THR B 31  ? 1.02878 0.98124 1.68432 0.04661  -0.53171 -0.23900 31  THR B N   
1481 C CA  . THR B 31  ? 0.94244 0.91023 1.60447 0.02406  -0.46986 -0.20819 31  THR B CA  
1482 C C   . THR B 31  ? 0.98677 0.89001 1.52653 0.03384  -0.45676 -0.20443 31  THR B C   
1483 O O   . THR B 31  ? 1.09132 0.93589 1.59292 0.03570  -0.49825 -0.22205 31  THR B O   
1484 C CB  . THR B 31  ? 0.91153 0.90406 1.69198 -0.01592 -0.46714 -0.19554 31  THR B CB  
1485 O OG1 . THR B 31  ? 1.02554 1.09545 1.92183 -0.02738 -0.46453 -0.19611 31  THR B OG1 
1486 C CG2 . THR B 31  ? 0.84653 0.84162 1.61358 -0.03464 -0.40804 -0.15813 31  THR B CG2 
1487 N N   . TYR B 32  ? 0.87243 0.79372 1.35436 0.04115  -0.39978 -0.18647 32  TYR B N   
1488 C CA  . TYR B 32  ? 0.88426 0.76090 1.25498 0.05043  -0.37789 -0.18210 32  TYR B CA  
1489 C C   . TYR B 32  ? 0.82257 0.72600 1.22858 0.02806  -0.33120 -0.14872 32  TYR B C   
1490 O O   . TYR B 32  ? 0.91713 0.89355 1.38129 0.01760  -0.28517 -0.12788 32  TYR B O   
1491 C CB  . TYR B 32  ? 0.98476 0.86898 1.26243 0.07611  -0.34502 -0.18984 32  TYR B CB  
1492 C CG  . TYR B 32  ? 0.88632 0.74876 1.13273 0.10030  -0.38128 -0.21265 32  TYR B CG  
1493 C CD1 . TYR B 32  ? 0.86440 0.77167 1.19010 0.10419  -0.38582 -0.21350 32  TYR B CD1 
1494 C CD2 . TYR B 32  ? 1.00634 0.80614 1.14285 0.12149  -0.41023 -0.23133 32  TYR B CD2 
1495 C CE1 . TYR B 32  ? 1.00759 0.89303 1.30271 0.13104  -0.41830 -0.22801 32  TYR B CE1 
1496 C CE2 . TYR B 32  ? 1.11074 0.89218 1.21459 0.14573  -0.44113 -0.24502 32  TYR B CE2 
1497 C CZ  . TYR B 32  ? 1.09556 0.91753 1.27800 0.15172  -0.44487 -0.24110 32  TYR B CZ  
1498 O OH  . TYR B 32  ? 1.11766 0.91907 1.26463 0.18050  -0.47501 -0.24880 32  TYR B OH  
1499 N N   . LYS B 33  ? 1.04115 0.88892 1.41174 0.02314  -0.34213 -0.14294 33  LYS B N   
1500 C CA  . LYS B 33  ? 0.96897 0.83254 1.36261 0.00711  -0.29871 -0.10480 33  LYS B CA  
1501 C C   . LYS B 33  ? 0.93010 0.75811 1.20086 0.02890  -0.27892 -0.10370 33  LYS B C   
1502 O O   . LYS B 33  ? 1.04886 0.80546 1.25238 0.04133  -0.31814 -0.12782 33  LYS B O   
1503 C CB  . LYS B 33  ? 1.06874 0.89840 1.55682 -0.02147 -0.32578 -0.09293 33  LYS B CB  
1504 C CG  . LYS B 33  ? 1.10105 0.96235 1.64571 -0.04275 -0.27481 -0.04184 33  LYS B CG  
1505 C CD  . LYS B 33  ? 1.29867 1.08633 1.87709 -0.05962 -0.29503 -0.02905 33  LYS B CD  
1506 C CE  . LYS B 33  ? 1.40109 1.22627 2.09057 -0.09252 -0.25540 0.02202  33  LYS B CE  
1507 N NZ  . LYS B 33  ? 1.46009 1.20806 2.17248 -0.10551 -0.26008 0.04526  33  LYS B NZ  
1508 N N   . LEU B 34  ? 0.91331 0.79992 1.15627 0.03485  -0.21880 -0.07949 34  LEU B N   
1509 C CA  . LEU B 34  ? 0.91894 0.79037 1.05373 0.05604  -0.19292 -0.07603 34  LEU B CA  
1510 C C   . LEU B 34  ? 0.94878 0.83583 1.12232 0.04525  -0.16017 -0.02758 34  LEU B C   
1511 O O   . LEU B 34  ? 0.88003 0.83773 1.13641 0.02796  -0.12452 0.00528  34  LEU B O   
1512 C CB  . LEU B 34  ? 0.88739 0.82419 0.95662 0.07483  -0.14684 -0.08985 34  LEU B CB  
1513 C CG  . LEU B 34  ? 0.92602 0.83751 0.92313 0.09225  -0.16647 -0.13372 34  LEU B CG  
1514 C CD1 . LEU B 34  ? 0.80788 0.79434 0.76873 0.10380  -0.10966 -0.14392 34  LEU B CD1 
1515 C CD2 . LEU B 34  ? 0.92387 0.75417 0.81800 0.10875  -0.20157 -0.15655 34  LEU B CD2 
1516 N N   . ASN B 35  ? 0.88736 0.70981 1.00429 0.05629  -0.17201 -0.02136 35  ASN B N   
1517 C CA  . ASN B 35  ? 1.02612 0.85762 1.17028 0.05198  -0.13761 0.03098  35  ASN B CA  
1518 C C   . ASN B 35  ? 0.93740 0.73694 0.96546 0.08376  -0.12887 0.02841  35  ASN B C   
1519 O O   . ASN B 35  ? 0.95902 0.68892 0.91701 0.09808  -0.16995 -0.01137 35  ASN B O   
1520 C CB  . ASN B 35  ? 0.99019 0.76284 1.24407 0.02162  -0.16767 0.05208  35  ASN B CB  
1521 C CG  . ASN B 35  ? 1.11659 0.85838 1.38681 0.02062  -0.14291 0.10547  35  ASN B CG  
1522 O OD1 . ASN B 35  ? 1.37973 1.11864 1.56287 0.04915  -0.11882 0.12107  35  ASN B OD1 
1523 N ND2 . ASN B 35  ? 1.40043 1.12929 1.79123 -0.01304 -0.14304 0.13806  35  ASN B ND2 
1524 N N   . ILE B 36  ? 0.98870 0.85044 0.99437 0.09709  -0.07457 0.06877  36  ILE B N   
1525 C CA  . ILE B 36  ? 0.94655 0.80149 0.84139 0.13199  -0.05834 0.06800  36  ILE B CA  
1526 C C   . ILE B 36  ? 1.02276 0.79148 0.93477 0.13400  -0.07645 0.10148  36  ILE B C   
1527 O O   . ILE B 36  ? 1.12191 0.89699 1.11655 0.11791  -0.05453 0.15796  36  ILE B O   
1528 C CB  . ILE B 36  ? 1.03032 1.00472 0.89492 0.14950  0.00816  0.09389  36  ILE B CB  
1529 C CG1 . ILE B 36  ? 0.95496 1.01269 0.82111 0.14416  0.02743  0.05654  36  ILE B CG1 
1530 C CG2 . ILE B 36  ? 0.93147 0.90789 0.68168 0.18875  0.02391  0.09035  36  ILE B CG2 
1531 C CD1 . ILE B 36  ? 0.77860 0.97022 0.66241 0.14997  0.09200  0.08267  36  ILE B CD1 
1532 N N   . MET B 37  ? 1.19186 0.88011 1.02864 0.15361  -0.11481 0.06651  37  MET B N   
1533 C CA  . MET B 37  ? 1.24104 0.84229 1.08259 0.16247  -0.13257 0.08969  37  MET B CA  
1534 C C   . MET B 37  ? 1.17438 0.80394 0.93601 0.20100  -0.09301 0.12207  37  MET B C   
1535 O O   . MET B 37  ? 1.39016 0.97575 1.18526 0.20658  -0.08381 0.17195  37  MET B O   
1536 C CB  . MET B 37  ? 1.17018 0.67369 0.97892 0.16540  -0.19774 0.03110  37  MET B CB  
1537 C CG  . MET B 37  ? 1.21356 0.69946 1.08752 0.13468  -0.24046 -0.00630 37  MET B CG  
1538 S SD  . MET B 37  ? 1.39873 0.91236 1.43247 0.09210  -0.21807 0.04895  37  MET B SD  
1539 C CE  . MET B 37  ? 1.63850 1.05785 1.76486 0.06276  -0.28869 0.01033  37  MET B CE  
1540 N N   . GLN B 38  ? 1.16620 0.86951 0.82680 0.22843  -0.06823 0.09515  38  GLN B N   
1541 C CA  . GLN B 38  ? 1.24850 0.99178 0.82318 0.27021  -0.03356 0.11566  38  GLN B CA  
1542 C C   . GLN B 38  ? 1.04195 0.92404 0.58357 0.28019  0.02176  0.11644  38  GLN B C   
1543 O O   . GLN B 38  ? 0.98255 0.90454 0.47283 0.28063  0.02079  0.06020  38  GLN B O   
1544 C CB  . GLN B 38  ? 1.13464 0.82052 0.60287 0.29971  -0.06830 0.06157  38  GLN B CB  
1545 C CG  . GLN B 38  ? 1.14985 0.88163 0.52682 0.34654  -0.03573 0.07664  38  GLN B CG  
1546 C CD  . GLN B 38  ? 1.34907 0.98671 0.66659 0.37310  -0.07623 0.05130  38  GLN B CD  
1547 O OE1 . GLN B 38  ? 1.44757 1.01701 0.80118 0.38340  -0.08371 0.09448  38  GLN B OE1 
1548 N NE2 . GLN B 38  ? 1.28887 0.92055 0.51852 0.38381  -0.10205 -0.01953 38  GLN B NE2 
1549 N N   . GLN B 39  ? 1.30074 0.70436 0.56587 -0.08645 -0.04394 0.10517  39  GLN B N   
1550 C CA  . GLN B 39  ? 1.41407 0.85436 0.72662 -0.09213 -0.06268 0.11469  39  GLN B CA  
1551 C C   . GLN B 39  ? 1.46563 0.90588 0.74849 -0.07598 -0.07076 0.13217  39  GLN B C   
1552 O O   . GLN B 39  ? 1.51344 0.91959 0.75102 -0.04383 -0.06885 0.12803  39  GLN B O   
1553 C CB  . GLN B 39  ? 1.42146 0.84642 0.75782 -0.08307 -0.07974 0.10251  39  GLN B CB  
1554 C CG  . GLN B 39  ? 1.36674 0.79719 0.72879 -0.09894 -0.07482 0.08417  39  GLN B CG  
1555 C CD  . GLN B 39  ? 1.48580 0.96347 0.90168 -0.11898 -0.08093 0.08166  39  GLN B CD  
1556 O OE1 . GLN B 39  ? 1.38060 0.88368 0.81757 -0.12255 -0.08988 0.09256  39  GLN B OE1 
1557 N NE2 . GLN B 39  ? 1.55251 1.02235 0.97186 -0.13549 -0.08161 0.06489  39  GLN B NE2 
1558 N N   . PRO B 40  ? 1.40058 0.88679 0.72081 -0.09323 -0.08155 0.14615  40  PRO B N   
1559 C CA  . PRO B 40  ? 1.27025 0.79408 0.62105 -0.07212 -0.09418 0.14869  40  PRO B CA  
1560 C C   . PRO B 40  ? 1.36569 0.85020 0.71043 -0.03977 -0.12502 0.14734  40  PRO B C   
1561 O O   . PRO B 40  ? 1.44618 0.90228 0.78868 -0.04760 -0.13619 0.14618  40  PRO B O   
1562 C CB  . PRO B 40  ? 1.35501 0.93486 0.75292 -0.10669 -0.10134 0.16370  40  PRO B CB  
1563 C CG  . PRO B 40  ? 1.38356 0.94453 0.78812 -0.12999 -0.10324 0.16221  40  PRO B CG  
1564 C CD  . PRO B 40  ? 1.42040 0.95346 0.80151 -0.12496 -0.08191 0.14602  40  PRO B CD  
1565 N N   . LYS B 41  ? 1.26901 0.78741 0.65711 -0.00170 -0.13027 0.13314  41  LYS B N   
1566 C CA  . LYS B 41  ? 1.30286 0.78095 0.68264 0.03130  -0.16292 0.13283  41  LYS B CA  
1567 C C   . LYS B 41  ? 1.30788 0.84862 0.75809 0.04342  -0.18709 0.13370  41  LYS B C   
1568 O O   . LYS B 41  ? 1.38768 0.90370 0.82679 0.03992  -0.21783 0.14548  41  LYS B O   
1569 C CB  . LYS B 41  ? 1.42006 0.85965 0.77914 0.07326  -0.15816 0.11499  41  LYS B CB  
1570 C CG  . LYS B 41  ? 1.50554 0.85419 0.77891 0.06529  -0.14973 0.11747  41  LYS B CG  
1571 C CD  . LYS B 41  ? 1.72190 1.04219 0.98341 0.03963  -0.16461 0.12591  41  LYS B CD  
1572 C CE  . LYS B 41  ? 1.77629 1.04919 1.01539 0.04164  -0.15774 0.10898  41  LYS B CE  
1573 N NZ  . LYS B 41  ? 2.01409 1.23512 1.19752 0.06112  -0.14304 0.10337  41  LYS B NZ  
1574 N N   . ARG B 42  ? 1.20314 0.82652 0.72561 0.05689  -0.17377 0.11993  42  ARG B N   
1575 C CA  . ARG B 42  ? 1.06787 0.75495 0.66390 0.07231  -0.19793 0.11800  42  ARG B CA  
1576 C C   . ARG B 42  ? 1.15852 0.94984 0.83125 0.05459  -0.17394 0.11136  42  ARG B C   
1577 O O   . ARG B 42  ? 1.09191 0.90978 0.76394 0.04146  -0.13662 0.10306  42  ARG B O   
1578 C CB  . ARG B 42  ? 1.28883 0.96455 0.90394 0.12628  -0.21860 0.10298  42  ARG B CB  
1579 C CG  . ARG B 42  ? 1.60090 1.17177 1.13998 0.14457  -0.24636 0.11127  42  ARG B CG  
1580 C CD  . ARG B 42  ? 1.60446 1.15227 1.12955 0.13425  -0.28585 0.12952  42  ARG B CD  
1581 N NE  . ARG B 42  ? 1.63889 1.10302 1.10915 0.16227  -0.31785 0.13438  42  ARG B NE  
1582 C CZ  . ARG B 42  ? 1.45007 0.83531 0.84253 0.14259  -0.32278 0.14635  42  ARG B CZ  
1583 N NH1 . ARG B 42  ? 1.54570 0.94016 0.92738 0.09581  -0.29033 0.14609  42  ARG B NH1 
1584 N NH2 . ARG B 42  ? 1.57015 0.91768 0.94981 0.15634  -0.33509 0.14003  42  ARG B NH2 
1585 N N   . ALA B 43  ? 1.01072 0.86103 0.74749 0.05221  -0.19639 0.11517  43  ALA B N   
1586 C CA  . ALA B 43  ? 1.06947 1.02551 0.88889 0.03801  -0.17793 0.10807  43  ALA B CA  
1587 C C   . ALA B 43  ? 0.99374 1.00117 0.88425 0.05703  -0.21315 0.10583  43  ALA B C   
1588 O O   . ALA B 43  ? 1.00079 0.96055 0.86728 0.06422  -0.25160 0.11659  43  ALA B O   
1589 C CB  . ALA B 43  ? 1.06998 1.04551 0.88215 -0.01890 -0.16083 0.12559  43  ALA B CB  
1590 N N   . ARG B 44  ? 0.97146 1.07848 0.94883 0.06374  -0.19945 0.09079  44  ARG B N   
1591 C CA  . ARG B 44  ? 0.96350 1.13388 1.02067 0.07888  -0.23158 0.08718  44  ARG B CA  
1592 C C   . ARG B 44  ? 0.94547 1.17972 1.04489 0.02799  -0.22674 0.10064  44  ARG B C   
1593 O O   . ARG B 44  ? 0.92836 1.21496 1.04692 -0.00276 -0.18829 0.09920  44  ARG B O   
1594 C CB  . ARG B 44  ? 0.98733 1.23112 1.12315 0.12302  -0.22220 0.05850  44  ARG B CB  
1595 C CG  . ARG B 44  ? 0.98506 1.29642 1.21002 0.14543  -0.25904 0.05198  44  ARG B CG  
1596 C CD  . ARG B 44  ? 1.01538 1.42688 1.33553 0.17673  -0.23656 0.02058  44  ARG B CD  
1597 N NE  . ARG B 44  ? 1.13362 1.57831 1.52508 0.22382  -0.27932 0.00780  44  ARG B NE  
1598 C CZ  . ARG B 44  ? 1.09788 1.63916 1.59040 0.25595  -0.26997 -0.02160 44  ARG B CZ  
1599 N NH1 . ARG B 44  ? 1.30591 1.92413 1.83902 0.24500  -0.21592 -0.04295 44  ARG B NH1 
1600 N NH2 . ARG B 44  ? 1.27733 1.84052 1.83220 0.29949  -0.31635 -0.03079 44  ARG B NH2 
1601 N N   . ALA B 45  ? 0.90883 1.13238 1.01561 0.01649  -0.26631 0.11439  45  ALA B N   
1602 C CA  . ALA B 45  ? 0.87006 1.14153 1.01246 -0.03249 -0.26765 0.12796  45  ALA B CA  
1603 C C   . ALA B 45  ? 0.86023 1.25017 1.09912 -0.04132 -0.24477 0.11583  45  ALA B C   
1604 O O   . ALA B 45  ? 0.94493 1.39523 1.25369 -0.00589 -0.25596 0.09801  45  ALA B O   
1605 C CB  . ALA B 45  ? 0.86367 1.11357 1.00972 -0.03476 -0.31709 0.13767  45  ALA B CB  
1606 N N   . CYS B 46  ? 0.84250 1.26610 1.08525 -0.08986 -0.21306 0.12557  46  CYS B N   
1607 C CA  . CYS B 46  ? 0.96296 1.50000 1.28846 -0.10654 -0.18334 0.11494  46  CYS B CA  
1608 C C   . CYS B 46  ? 1.12322 1.73114 1.52802 -0.13044 -0.20955 0.12116  46  CYS B C   
1609 O O   . CYS B 46  ? 1.35075 2.06413 1.84043 -0.13662 -0.19181 0.10859  46  CYS B O   
1610 C CB  . CYS B 46  ? 0.93000 1.47144 1.21887 -0.15229 -0.13777 0.12461  46  CYS B CB  
1611 S SG  . CYS B 46  ? 1.14987 1.62297 1.37706 -0.21371 -0.15143 0.15967  46  CYS B SG  
1612 N N   . GLY B 47  ? 0.91873 1.47405 1.29970 -0.14426 -0.25057 0.13786  47  GLY B N   
1613 C CA  . GLY B 47  ? 1.27981 1.89663 1.73243 -0.16893 -0.27784 0.14315  47  GLY B CA  
1614 C C   . GLY B 47  ? 1.48925 2.16735 1.97538 -0.22817 -0.24981 0.15530  47  GLY B C   
1615 O O   . GLY B 47  ? 1.45964 2.10491 1.89194 -0.25934 -0.21959 0.16779  47  GLY B O   
1616 N N   . GLN B 48  ? 1.58263 2.35077 2.15830 -0.24596 -0.26166 0.15268  48  GLN B N   
1617 C CA  . GLN B 48  ? 1.62331 2.45314 2.23525 -0.30710 -0.23887 0.16630  48  GLN B CA  
1618 C C   . GLN B 48  ? 1.54368 2.50093 2.24630 -0.30573 -0.20459 0.14707  48  GLN B C   
1619 O O   . GLN B 48  ? 1.53970 2.52447 2.25773 -0.25924 -0.18455 0.12293  48  GLN B O   
1620 C CB  . GLN B 48  ? 1.64899 2.47631 2.28858 -0.34318 -0.28076 0.18207  48  GLN B CB  
1621 C CG  . GLN B 48  ? 1.64798 2.36343 2.20389 -0.36659 -0.30293 0.20312  48  GLN B CG  
1622 C CD  . GLN B 48  ? 1.66164 2.29741 2.17240 -0.32342 -0.34241 0.19610  48  GLN B CD  
1623 O OE1 . GLN B 48  ? 1.62097 2.25796 2.13235 -0.27183 -0.34574 0.17916  48  GLN B OE1 
1624 N NE2 . GLN B 48  ? 1.64185 2.20743 2.11302 -0.34544 -0.37337 0.20844  48  GLN B NE2 
1625 N N   . LYS B 51  ? 1.16375 2.04151 2.00010 0.27807  -0.30115 -0.06603 51  LYS B N   
1626 C CA  . LYS B 51  ? 1.30336 2.18470 2.09140 0.21145  -0.25623 -0.04794 51  LYS B CA  
1627 C C   . LYS B 51  ? 1.29979 2.28822 2.14764 0.19460  -0.19213 -0.07333 51  LYS B C   
1628 O O   . LYS B 51  ? 1.25599 2.28680 2.10050 0.13467  -0.15911 -0.05986 51  LYS B O   
1629 C CB  . LYS B 51  ? 1.23551 2.13711 2.03661 0.16140  -0.28262 -0.02070 51  LYS B CB  
1630 C CG  . LYS B 51  ? 1.24678 2.04449 1.98000 0.16905  -0.34137 0.00398  51  LYS B CG  
1631 C CD  . LYS B 51  ? 1.20859 2.01963 1.94369 0.11339  -0.35927 0.02853  51  LYS B CD  
1632 C CE  . LYS B 51  ? 1.31496 2.02164 1.97364 0.11669  -0.41237 0.05039  51  LYS B CE  
1633 N NZ  . LYS B 51  ? 1.42218 2.12746 2.06873 0.06017  -0.42479 0.07218  51  LYS B NZ  
1634 N N   . SER B 52  ? 1.32548 2.35615 2.22637 0.24654  -0.17497 -0.11074 52  SER B N   
1635 C CA  . SER B 52  ? 1.29331 2.42411 2.24526 0.23476  -0.11018 -0.14073 52  SER B CA  
1636 C C   . SER B 52  ? 1.29577 2.35135 2.15309 0.24001  -0.06931 -0.14859 52  SER B C   
1637 O O   . SER B 52  ? 1.29133 2.41662 2.17657 0.23654  -0.01398 -0.17782 52  SER B O   
1638 C CB  . SER B 52  ? 1.12237 2.36641 2.20865 0.28795  -0.11243 -0.18445 52  SER B CB  
1639 O OG  . SER B 52  ? 1.12320 2.47660 2.26376 0.27184  -0.04587 -0.21623 52  SER B OG  
1640 N N   . HIS B 53  ? 1.10416 2.02112 1.85010 0.24672  -0.09526 -0.12431 53  HIS B N   
1641 C CA  . HIS B 53  ? 1.16882 1.99819 1.81520 0.25064  -0.06471 -0.12770 53  HIS B CA  
1642 C C   . HIS B 53  ? 1.11842 1.90788 1.67940 0.17971  -0.04237 -0.09263 53  HIS B C   
1643 O O   . HIS B 53  ? 1.00809 1.70282 1.49433 0.16237  -0.07533 -0.05934 53  HIS B O   
1644 C CB  . HIS B 53  ? 1.10243 1.80740 1.68578 0.30236  -0.10934 -0.12370 53  HIS B CB  
1645 C CG  . HIS B 53  ? 1.15024 1.88715 1.81827 0.37283  -0.13931 -0.15526 53  HIS B CG  
1646 N ND1 . HIS B 53  ? 1.21411 2.06081 1.98232 0.40198  -0.10666 -0.19961 53  HIS B ND1 
1647 C CD2 . HIS B 53  ? 1.19514 1.87026 1.86486 0.41954  -0.20065 -0.14931 53  HIS B CD2 
1648 C CE1 . HIS B 53  ? 1.17604 2.02582 2.00878 0.46707  -0.14846 -0.22069 53  HIS B CE1 
1649 N NE2 . HIS B 53  ? 1.18456 1.92840 1.95637 0.47802  -0.20738 -0.18887 53  HIS B NE2 
1650 N N   . THR B 54  ? 1.01828 1.88019 1.59008 0.13834  0.01325  -0.10096 54  THR B N   
1651 C CA  . THR B 54  ? 1.01193 1.84745 1.51478 0.06807  0.03200  -0.06697 54  THR B CA  
1652 C C   . THR B 54  ? 1.11739 1.84787 1.50204 0.05952  0.05236  -0.05887 54  THR B C   
1653 O O   . THR B 54  ? 0.99610 1.66640 1.30733 0.01190  0.04917  -0.02523 54  THR B O   
1654 C CB  . THR B 54  ? 0.98569 1.94609 1.54955 0.01888  0.07886  -0.07393 54  THR B CB  
1655 O OG1 . THR B 54  ? 1.02209 2.03245 1.59564 0.03419  0.13237  -0.11096 54  THR B OG1 
1656 C CG2 . THR B 54  ? 0.96474 2.03366 1.65040 0.02392  0.05809  -0.08193 54  THR B CG2 
1657 N N   . ASP B 55  ? 1.12098 1.82606 1.48761 0.10513  0.07041  -0.08964 55  ASP B N   
1658 C CA  . ASP B 55  ? 1.08161 1.68081 1.33508 0.09925  0.08479  -0.08248 55  ASP B CA  
1659 C C   . ASP B 55  ? 1.07729 1.55087 1.26398 0.12331  0.03433  -0.06069 55  ASP B C   
1660 O O   . ASP B 55  ? 1.23647 1.61377 1.32858 0.11919  0.03922  -0.05221 55  ASP B O   
1661 C CB  . ASP B 55  ? 1.12742 1.74268 1.38192 0.13602  0.12420  -0.12537 55  ASP B CB  
1662 C CG  . ASP B 55  ? 1.14840 1.71334 1.30418 0.09955  0.16414  -0.12047 55  ASP B CG  
1663 O OD1 . ASP B 55  ? 1.32011 1.77196 1.38222 0.08946  0.14421  -0.09477 55  ASP B OD1 
1664 O OD2 . ASP B 55  ? 1.29902 1.93946 1.47027 0.07947  0.21560  -0.14298 55  ASP B OD2 
1665 N N   . ARG B 56  ? 1.06049 1.53577 1.29357 0.14539  -0.01368 -0.05160 56  ARG B N   
1666 C CA  . ARG B 56  ? 1.06256 1.42783 1.23544 0.16317  -0.06317 -0.02957 56  ARG B CA  
1667 C C   . ARG B 56  ? 1.02170 1.34935 1.14815 0.10972  -0.08025 0.00908  56  ARG B C   
1668 O O   . ARG B 56  ? 1.02217 1.25731 1.08751 0.11440  -0.11533 0.02855  56  ARG B O   
1669 C CB  . ARG B 56  ? 1.07435 1.45946 1.31739 0.21424  -0.10905 -0.04021 56  ARG B CB  
1670 C CG  . ARG B 56  ? 1.12593 1.50951 1.39872 0.27867  -0.10760 -0.07628 56  ARG B CG  
1671 C CD  . ARG B 56  ? 1.21338 1.49623 1.44792 0.32347  -0.16251 -0.06792 56  ARG B CD  
1672 N NE  . ARG B 56  ? 1.25195 1.58598 1.58037 0.37684  -0.19645 -0.08871 56  ARG B NE  
1673 C CZ  . ARG B 56  ? 1.23353 1.57307 1.60051 0.43376  -0.19526 -0.12293 56  ARG B CZ  
1674 N NH1 . ARG B 56  ? 1.26680 1.56360 1.58487 0.44519  -0.16020 -0.14211 56  ARG B NH1 
1675 N NH2 . ARG B 56  ? 1.25364 1.64089 1.71161 0.48136  -0.23258 -0.13948 56  ARG B NH2 
1676 N N   . ARG B 57  ? 1.06697 1.20314 1.39535 0.14923  -0.03153 0.01233  57  ARG B N   
1677 C CA  . ARG B 57  ? 1.03507 1.15795 1.34678 0.13184  -0.05255 0.00364  57  ARG B CA  
1678 C C   . ARG B 57  ? 0.87876 0.96510 1.12477 0.12855  -0.03685 -0.00316 57  ARG B C   
1679 O O   . ARG B 57  ? 0.81992 0.88682 1.02549 0.12473  -0.05590 -0.01399 57  ARG B O   
1680 C CB  . ARG B 57  ? 1.03240 1.17943 1.41267 0.11557  -0.05643 0.01354  57  ARG B CB  
1681 C CG  . ARG B 57  ? 0.93614 1.11502 1.38409 0.11303  -0.09036 0.01509  57  ARG B CG  
1682 C CD  . ARG B 57  ? 1.18688 1.39855 1.72672 0.09838  -0.08371 0.03445  57  ARG B CD  
1683 N NE  . ARG B 57  ? 1.31229 1.54905 1.92236 0.09063  -0.12813 0.03247  57  ARG B NE  
1684 C CZ  . ARG B 57  ? 1.42495 1.69638 2.08746 0.10129  -0.13785 0.04004  57  ARG B CZ  
1685 N NH1 . ARG B 57  ? 1.37064 1.65513 2.02466 0.12115  -0.10424 0.05032  57  ARG B NH1 
1686 N NH2 . ARG B 57  ? 1.52183 1.81282 2.24764 0.09315  -0.18568 0.03590  57  ARG B NH2 
1687 N N   . PRO B 58  ? 0.90618 0.98263 1.13779 0.13248  -0.00396 0.00269  58  PRO B N   
1688 C CA  . PRO B 58  ? 0.88275 0.92322 1.05138 0.13016  0.00422  -0.00521 58  PRO B CA  
1689 C C   . PRO B 58  ? 0.93984 0.95903 1.06539 0.13590  -0.01118 -0.01545 58  PRO B C   
1690 O O   . PRO B 58  ? 0.93578 0.95942 1.06778 0.14779  -0.01368 -0.01419 58  PRO B O   
1691 C CB  . PRO B 58  ? 0.73833 0.77135 0.89250 0.14309  0.03878  0.00042  58  PRO B CB  
1692 C CG  . PRO B 58  ? 0.83180 0.90137 1.04625 0.15188  0.05438  0.01453  58  PRO B CG  
1693 C CD  . PRO B 58  ? 0.80480 0.90432 1.07764 0.14019  0.02654  0.01804  58  PRO B CD  
1694 N N   . VAL B 59  ? 0.87115 0.86868 0.95773 0.12805  -0.02033 -0.02218 59  VAL B N   
1695 C CA  . VAL B 59  ? 0.84230 0.82531 0.89731 0.13280  -0.03205 -0.02560 59  VAL B CA  
1696 C C   . VAL B 59  ? 0.90307 0.86567 0.94177 0.14212  -0.01932 -0.02578 59  VAL B C   
1697 O O   . VAL B 59  ? 0.86446 0.80757 0.88293 0.14324  -0.00504 -0.03021 59  VAL B O   
1698 C CB  . VAL B 59  ? 0.96389 0.93156 0.98702 0.12436  -0.04104 -0.03048 59  VAL B CB  
1699 C CG1 . VAL B 59  ? 0.95598 0.91065 0.95391 0.12933  -0.04534 -0.02804 59  VAL B CG1 
1700 C CG2 . VAL B 59  ? 0.90649 0.88809 0.94069 0.12090  -0.06069 -0.03436 59  VAL B CG2 
1701 N N   . ASP B 60  ? 0.95662 0.92046 1.00201 0.15080  -0.02662 -0.02100 60  ASP B N   
1702 C CA  . ASP B 60  ? 0.88280 0.82425 0.92323 0.16069  -0.02027 -0.02164 60  ASP B CA  
1703 C C   . ASP B 60  ? 0.93833 0.86533 0.96954 0.15922  -0.03292 -0.01452 60  ASP B C   
1704 O O   . ASP B 60  ? 1.02458 0.97071 1.06145 0.15932  -0.04256 -0.00355 60  ASP B O   
1705 C CB  . ASP B 60  ? 0.95790 0.91570 1.03161 0.17452  -0.01473 -0.01690 60  ASP B CB  
1706 C CG  . ASP B 60  ? 0.98090 0.91161 1.04672 0.18854  -0.00184 -0.02412 60  ASP B CG  
1707 O OD1 . ASP B 60  ? 1.03675 0.95961 1.08682 0.19296  0.01495  -0.03227 60  ASP B OD1 
1708 O OD2 . ASP B 60  ? 1.08799 1.00382 1.16197 0.19778  -0.00839 -0.02099 60  ASP B OD2 
1709 N N   . PRO B 61  ? 0.92354 0.81686 0.94080 0.15891  -0.03414 -0.01943 61  PRO B N   
1710 C CA  . PRO B 61  ? 1.03677 0.90010 1.03036 0.16311  -0.02651 -0.03584 61  PRO B CA  
1711 C C   . PRO B 61  ? 0.96925 0.83150 0.93556 0.15284  -0.02381 -0.04203 61  PRO B C   
1712 O O   . PRO B 61  ? 0.99132 0.86594 0.95796 0.14175  -0.03213 -0.03546 61  PRO B O   
1713 C CB  . PRO B 61  ? 0.94084 0.76658 0.93292 0.16465  -0.04070 -0.03832 61  PRO B CB  
1714 C CG  . PRO B 61  ? 0.89485 0.73509 0.90555 0.15284  -0.05241 -0.01967 61  PRO B CG  
1715 C CD  . PRO B 61  ? 0.89642 0.77770 0.92286 0.15629  -0.04615 -0.00685 61  PRO B CD  
1716 N N   . PRO B 62  ? 0.99308 0.84153 0.93386 0.15919  -0.01090 -0.05264 62  PRO B N   
1717 C CA  . PRO B 62  ? 0.81307 0.66059 0.72906 0.15033  -0.00760 -0.05440 62  PRO B CA  
1718 C C   . PRO B 62  ? 0.87830 0.70318 0.77460 0.14085  -0.02660 -0.05788 62  PRO B C   
1719 O O   . PRO B 62  ? 0.99963 0.79234 0.88160 0.14541  -0.03869 -0.06693 62  PRO B O   
1720 C CB  . PRO B 62  ? 0.89600 0.72828 0.78219 0.16583  0.01197  -0.06208 62  PRO B CB  
1721 C CG  . PRO B 62  ? 0.90573 0.71418 0.78687 0.18346  0.01028  -0.07243 62  PRO B CG  
1722 C CD  . PRO B 62  ? 0.87398 0.70535 0.80289 0.17892  0.00287  -0.06214 62  PRO B CD  
1723 N N   . PRO B 63  ? 0.99724 0.83730 0.89645 0.12854  -0.03203 -0.05125 63  PRO B N   
1724 C CA  . PRO B 63  ? 0.90173 0.72793 0.79180 0.12047  -0.04877 -0.05073 63  PRO B CA  
1725 C C   . PRO B 63  ? 0.97910 0.77091 0.83095 0.12364  -0.05427 -0.06326 63  PRO B C   
1726 O O   . PRO B 63  ? 1.00485 0.79076 0.82807 0.12970  -0.04092 -0.06794 63  PRO B O   
1727 C CB  . PRO B 63  ? 0.88318 0.73295 0.77851 0.11256  -0.04855 -0.04339 63  PRO B CB  
1728 C CG  . PRO B 63  ? 0.89469 0.77095 0.81198 0.11528  -0.04028 -0.03946 63  PRO B CG  
1729 C CD  . PRO B 63  ? 0.79488 0.66556 0.71220 0.12282  -0.02645 -0.04408 63  PRO B CD  
1730 N N   . VAL B 64  ? 1.01346 0.78296 0.86706 0.12048  -0.07539 -0.06658 64  VAL B N   
1731 C CA  . VAL B 64  ? 1.02805 0.75989 0.84407 0.12486  -0.09059 -0.08152 64  VAL B CA  
1732 C C   . VAL B 64  ? 0.98929 0.72188 0.82162 0.11182  -0.11236 -0.07462 64  VAL B C   
1733 O O   . VAL B 64  ? 0.99842 0.74355 0.87580 0.10307  -0.12270 -0.06178 64  VAL B O   
1734 C CB  . VAL B 64  ? 1.10948 0.80385 0.91595 0.13666  -0.10344 -0.09758 64  VAL B CB  
1735 C CG1 . VAL B 64  ? 1.03907 0.69017 0.80615 0.14163  -0.12979 -0.11587 64  VAL B CG1 
1736 C CG2 . VAL B 64  ? 0.94956 0.64407 0.73544 0.15502  -0.07837 -0.10450 64  VAL B CG2 
1737 N N   . ILE B 65  ? 0.98288 0.70495 0.78174 0.11208  -0.11735 -0.07946 65  ILE B N   
1738 C CA  . ILE B 65  ? 1.01963 0.74503 0.83330 0.10201  -0.13705 -0.07247 65  ILE B CA  
1739 C C   . ILE B 65  ? 1.06903 0.75346 0.84265 0.10821  -0.16228 -0.08965 65  ILE B C   
1740 O O   . ILE B 65  ? 1.11298 0.77705 0.82972 0.12197  -0.15325 -0.10145 65  ILE B O   
1741 C CB  . ILE B 65  ? 0.87114 0.62322 0.68203 0.09837  -0.12231 -0.06121 65  ILE B CB  
1742 C CG1 . ILE B 65  ? 0.89365 0.68222 0.73736 0.09558  -0.10392 -0.04828 65  ILE B CG1 
1743 C CG2 . ILE B 65  ? 1.00557 0.75893 0.82803 0.09231  -0.14234 -0.05501 65  ILE B CG2 
1744 C CD1 . ILE B 65  ? 0.76831 0.56330 0.60278 0.10099  -0.08290 -0.05203 65  ILE B CD1 
1745 N N   . GLU B 66  ? 0.97340 0.64631 0.77759 0.09977  -0.19455 -0.08948 66  GLU B N   
1746 C CA  . GLU B 66  ? 1.13146 0.76365 0.90033 0.10553  -0.22811 -0.10773 66  GLU B CA  
1747 C C   . GLU B 66  ? 1.05097 0.69821 0.83251 0.09738  -0.24198 -0.09633 66  GLU B C   
1748 O O   . GLU B 66  ? 1.07293 0.75847 0.91082 0.08515  -0.23550 -0.07434 66  GLU B O   
1749 C CB  . GLU B 66  ? 1.12434 0.72329 0.92209 0.10229  -0.26514 -0.12001 66  GLU B CB  
1750 C CG  . GLU B 66  ? 1.34729 0.95492 1.21319 0.08396  -0.29978 -0.10652 66  GLU B CG  
1751 C CD  . GLU B 66  ? 1.48769 1.05264 1.38344 0.07991  -0.34419 -0.12133 66  GLU B CD  
1752 O OE1 . GLU B 66  ? 1.45966 0.98159 1.30962 0.09528  -0.34994 -0.14738 66  GLU B OE1 
1753 O OE2 . GLU B 66  ? 1.60182 1.17567 1.57113 0.06227  -0.37420 -0.10626 66  GLU B OE2 
1754 N N   . LEU B 67  ? 1.08843 0.70707 0.81164 0.10838  -0.25727 -0.10999 67  LEU B N   
1755 C CA  . LEU B 67  ? 1.18996 0.81752 0.91680 0.10440  -0.27292 -0.10095 67  LEU B CA  
1756 C C   . LEU B 67  ? 1.15810 0.74769 0.87572 0.10675  -0.32439 -0.11789 67  LEU B C   
1757 O O   . LEU B 67  ? 1.30474 0.84873 0.96271 0.12262  -0.34140 -0.14333 67  LEU B O   
1758 C CB  . LEU B 67  ? 1.28006 0.90769 0.94570 0.11630  -0.24759 -0.09792 67  LEU B CB  
1759 C CG  . LEU B 67  ? 1.01966 0.64446 0.66972 0.11835  -0.26610 -0.09180 67  LEU B CG  
1760 C CD1 . LEU B 67  ? 0.96552 0.62939 0.68962 0.10334  -0.27027 -0.07167 67  LEU B CD1 
1761 C CD2 . LEU B 67  ? 1.22218 0.84275 0.81296 0.13065  -0.23733 -0.08563 67  LEU B CD2 
1762 N N   . ASN B 68  ? 1.17512 0.78342 0.95215 0.09333  -0.35063 -0.10429 68  ASN B N   
1763 C CA  . ASN B 68  ? 1.19533 0.77168 0.97349 0.09357  -0.40596 -0.11831 68  ASN B CA  
1764 C C   . ASN B 68  ? 1.29000 0.88817 1.07818 0.09230  -0.41502 -0.10299 68  ASN B C   
1765 O O   . ASN B 68  ? 1.30751 0.95262 1.14316 0.08415  -0.38715 -0.07717 68  ASN B O   
1766 C CB  . ASN B 68  ? 1.28891 0.86625 1.15718 0.07512  -0.44006 -0.11415 68  ASN B CB  
1767 C CG  . ASN B 68  ? 1.40816 0.94727 1.25994 0.07958  -0.44591 -0.13565 68  ASN B CG  
1768 O OD1 . ASN B 68  ? 1.36772 0.85063 1.16621 0.09299  -0.48318 -0.16772 68  ASN B OD1 
1769 N ND2 . ASN B 68  ? 1.19072 0.75779 1.08466 0.07152  -0.41077 -0.11915 68  ASN B ND2 
1770 N N   . ILE B 69  ? 1.38065 0.94248 1.12026 0.10365  -0.45562 -0.12008 69  ILE B N   
1771 C CA  . ILE B 69  ? 1.48177 1.05817 1.22570 0.10545  -0.47082 -0.10727 69  ILE B CA  
1772 C C   . ILE B 69  ? 1.59242 1.15296 1.38380 0.09789  -0.53681 -0.11520 69  ILE B C   
1773 O O   . ILE B 69  ? 1.67699 1.18618 1.42768 0.10610  -0.57878 -0.14486 69  ILE B O   
1774 C CB  . ILE B 69  ? 1.58084 1.12937 1.21610 0.12928  -0.45863 -0.11599 69  ILE B CB  
1775 C CG1 . ILE B 69  ? 1.45927 1.02771 1.06609 0.13298  -0.39580 -0.10337 69  ILE B CG1 
1776 C CG2 . ILE B 69  ? 1.53378 1.09186 1.17406 0.13255  -0.48148 -0.10316 69  ILE B CG2 
1777 C CD1 . ILE B 69  ? 1.52045 1.05158 1.02428 0.15611  -0.37752 -0.11856 69  ILE B CD1 
1778 N N   . PHE B 70  ? 1.56809 1.17167 1.44621 0.08434  -0.54776 -0.08940 70  PHE B N   
1779 C CA  . PHE B 70  ? 1.44250 1.04417 1.39568 0.07217  -0.60983 -0.08882 70  PHE B CA  
1780 C C   . PHE B 70  ? 1.57258 1.18680 1.52349 0.07995  -0.63197 -0.07869 70  PHE B C   
1781 O O   . PHE B 70  ? 1.62788 1.27937 1.58090 0.08460  -0.59160 -0.05606 70  PHE B O   
1782 C CB  . PHE B 70  ? 1.46745 1.11924 1.55488 0.04730  -0.60321 -0.05876 70  PHE B CB  
1783 C CG  . PHE B 70  ? 1.65004 1.29113 1.74983 0.03904  -0.58372 -0.06415 70  PHE B CG  
1784 C CD1 . PHE B 70  ? 1.68108 1.26210 1.69305 0.05117  -0.59381 -0.10070 70  PHE B CD1 
1785 C CD2 . PHE B 70  ? 1.76000 1.45213 1.95666 0.02285  -0.55317 -0.03069 70  PHE B CD2 
1786 C CE1 . PHE B 70  ? 1.60847 1.17942 1.63471 0.04535  -0.57654 -0.10499 70  PHE B CE1 
1787 C CE2 . PHE B 70  ? 1.76818 1.45013 1.97631 0.01650  -0.53611 -0.03302 70  PHE B CE2 
1788 C CZ  . PHE B 70  ? 1.54152 1.16229 1.66694 0.02682  -0.54896 -0.07082 70  PHE B CZ  
1789 N N   . GLU B 71  ? 1.68898 1.26878 1.63526 0.08286  -0.69975 -0.09700 71  GLU B N   
1790 C CA  . GLU B 71  ? 1.57723 1.16493 1.52474 0.09114  -0.73234 -0.08898 71  GLU B CA  
1791 C C   . GLU B 71  ? 1.68902 1.31238 1.77619 0.06930  -0.77976 -0.06948 71  GLU B C   
1792 O O   . GLU B 71  ? 1.81047 1.41501 1.95443 0.05366  -0.82369 -0.08103 71  GLU B O   
1793 C CB  . GLU B 71  ? 1.64748 1.16793 1.47293 0.11637  -0.77756 -0.12415 71  GLU B CB  
1794 C CG  . GLU B 71  ? 1.74320 1.26757 1.56533 0.12624  -0.80457 -0.11565 71  GLU B CG  
1795 C CD  . GLU B 71  ? 2.13438 1.59920 1.90348 0.13920  -0.85099 -0.14696 71  GLU B CD  
1796 O OE1 . GLU B 71  ? 2.19205 1.60401 1.84274 0.16314  -0.84250 -0.17436 71  GLU B OE1 
1797 O OE2 . GLU B 71  ? 2.17061 1.64238 2.01786 0.12785  -0.89488 -0.14278 71  GLU B OE2 
1798 N N   . SER B 72  ? 1.73552 1.41097 1.88421 0.06869  -0.77011 -0.03804 72  SER B N   
1799 C CA  . SER B 72  ? 1.82387 1.54083 2.10938 0.05155  -0.81353 -0.01392 72  SER B CA  
1800 C C   . SER B 72  ? 2.06102 1.77854 2.32284 0.06555  -0.82963 -0.01062 72  SER B C   
1801 O O   . SER B 72  ? 2.09136 1.82851 2.30968 0.08338  -0.79800 0.00273  72  SER B O   
1802 C CB  . SER B 72  ? 1.72927 1.52362 2.13387 0.03721  -0.76057 0.03066  72  SER B CB  
1803 O OG  . SER B 72  ? 1.87674 1.72491 2.40255 0.02989  -0.78542 0.06319  72  SER B OG  
1804 N N   . ASP B 73  ? 2.72987 2.42244 3.02119 0.05862  -0.88018 -0.02231 73  ASP B N   
1805 C CA  . ASP B 73  ? 2.72865 2.42075 2.99990 0.07201  -0.90061 -0.01975 73  ASP B CA  
1806 C C   . ASP B 73  ? 2.64778 2.42063 3.04362 0.06409  -0.88182 0.02530  73  ASP B C   
1807 O O   . ASP B 73  ? 2.62728 2.45074 3.14583 0.04386  -0.86888 0.05321  73  ASP B O   
1808 C CB  . ASP B 73  ? 2.89292 2.53211 3.15917 0.06947  -0.96357 -0.04637 73  ASP B CB  
1809 C CG  . ASP B 73  ? 2.98706 2.62784 3.37077 0.04121  -0.99267 -0.04233 73  ASP B CG  
1810 O OD1 . ASP B 73  ? 2.94135 2.60847 3.37806 0.02603  -0.96305 -0.02812 73  ASP B OD1 
1811 O OD2 . ASP B 73  ? 2.96104 2.57483 3.38544 0.03492  -1.04610 -0.05173 73  ASP B OD2 
1812 N N   . PRO B 74  ? 2.78908 2.57622 3.15547 0.08247  -0.87590 0.03560  74  PRO B N   
1813 C CA  . PRO B 74  ? 2.73684 2.59987 3.22051 0.07997  -0.85730 0.07735  74  PRO B CA  
1814 C C   . PRO B 74  ? 2.63755 2.52801 3.25465 0.05666  -0.89410 0.09295  74  PRO B C   
1815 O O   . PRO B 74  ? 2.54068 2.50279 3.28021 0.04865  -0.86874 0.13280  74  PRO B O   
1816 C CB  . PRO B 74  ? 2.75923 2.61306 3.16903 0.10585  -0.85630 0.07718  74  PRO B CB  
1817 C CG  . PRO B 74  ? 2.77656 2.55194 3.03718 0.12000  -0.87645 0.03865  74  PRO B CG  
1818 C CD  . PRO B 74  ? 2.81958 2.55511 3.04401 0.10869  -0.88073 0.01254  74  PRO B CD  
1819 N N   . HIS B 75  ? 2.69882 2.53187 3.29410 0.04817  -0.95176 0.06363  75  HIS B N   
1820 C CA  . HIS B 75  ? 2.68048 2.52859 3.40351 0.02468  -0.99295 0.07737  75  HIS B CA  
1821 C C   . HIS B 75  ? 2.62548 2.50070 3.45642 -0.00194 -0.97702 0.09824  75  HIS B C   
1822 O O   . HIS B 75  ? 2.52014 2.44829 3.49319 -0.02067 -0.97676 0.13573  75  HIS B O   
1823 C CB  . HIS B 75  ? 2.63751 2.40585 3.29652 0.02753  -1.06097 0.03656  75  HIS B CB  
1824 C CG  . HIS B 75  ? 2.68818 2.41954 3.21434 0.05744  -1.07180 0.01316  75  HIS B CG  
1825 N ND1 . HIS B 75  ? 2.75118 2.42295 3.12201 0.07922  -1.06173 -0.02093 75  HIS B ND1 
1826 C CD2 . HIS B 75  ? 2.52100 2.26838 3.04806 0.07038  -1.08871 0.02270  75  HIS B CD2 
1827 C CE1 . HIS B 75  ? 2.59621 2.24868 2.87811 0.10397  -1.07050 -0.02917 75  HIS B CE1 
1828 N NE2 . HIS B 75  ? 2.45157 2.14802 2.82485 0.09899  -1.08872 -0.00417 75  HIS B NE2 
1829 N N   . ASP B 76  ? 2.68927 2.52967 3.45630 -0.00306 -0.96175 0.07741  76  ASP B N   
1830 C CA  . ASP B 76  ? 2.61828 2.47886 3.47593 -0.02640 -0.94506 0.09647  76  ASP B CA  
1831 C C   . ASP B 76  ? 2.51361 2.39874 3.32010 -0.01606 -0.88497 0.10225  76  ASP B C   
1832 O O   . ASP B 76  ? 2.62137 2.45182 3.31173 -0.00586 -0.88518 0.06643  76  ASP B O   
1833 C CB  . ASP B 76  ? 2.64767 2.42995 3.48667 -0.03856 -0.99758 0.06188  76  ASP B CB  
1834 C CG  . ASP B 76  ? 2.44930 2.25094 3.40204 -0.06491 -0.98700 0.08772  76  ASP B CG  
1835 O OD1 . ASP B 76  ? 2.31181 2.19276 3.36633 -0.07475 -0.93923 0.13641  76  ASP B OD1 
1836 O OD2 . ASP B 76  ? 2.52193 2.25837 3.45981 -0.07236 -1.02450 0.06086  76  ASP B OD2 
1837 N N   . ASP B 77  ? 2.23615 2.20256 3.12788 -0.01579 -0.83227 0.14787  77  ASP B N   
1838 C CA  . ASP B 77  ? 2.08226 2.07590 2.93406 -0.00235 -0.77454 0.15730  77  ASP B CA  
1839 C C   . ASP B 77  ? 2.00073 2.01269 2.92257 -0.02117 -0.75363 0.17547  77  ASP B C   
1840 O O   . ASP B 77  ? 1.91815 1.95796 2.81976 -0.00981 -0.70450 0.18784  77  ASP B O   
1841 C CB  . ASP B 77  ? 1.88375 1.95018 2.77183 0.01805  -0.72348 0.19464  77  ASP B CB  
1842 C CG  . ASP B 77  ? 1.75721 1.79783 2.53959 0.04421  -0.72847 0.17401  77  ASP B CG  
1843 O OD1 . ASP B 77  ? 1.88476 1.85498 2.56095 0.04734  -0.76657 0.13353  77  ASP B OD1 
1844 O OD2 . ASP B 77  ? 1.63857 1.72744 2.44110 0.06424  -0.69151 0.19945  77  ASP B OD2 
1845 N N   . SER B 78  ? 2.19073 2.18426 3.19418 -0.04792 -0.79003 0.17884  78  SER B N   
1846 C CA  . SER B 78  ? 2.28705 2.29676 3.36716 -0.06699 -0.77102 0.20162  78  SER B CA  
1847 C C   . SER B 78  ? 2.36365 2.29348 3.36774 -0.07401 -0.80353 0.15700  78  SER B C   
1848 O O   . SER B 78  ? 2.31613 2.25384 3.36669 -0.08688 -0.78563 0.17193  78  SER B O   
1849 C CB  . SER B 78  ? 2.21863 2.26060 3.45370 -0.09203 -0.78424 0.24385  78  SER B CB  
1850 O OG  . SER B 78  ? 2.09403 2.22491 3.41294 -0.08412 -0.73375 0.29618  78  SER B OG  
1851 N N   . ASN B 79  ? 2.46068 2.31420 3.34650 -0.06272 -0.84717 0.10439  79  ASN B N   
1852 C CA  . ASN B 79  ? 2.31193 2.08411 3.11167 -0.06220 -0.87606 0.05826  79  ASN B CA  
1853 C C   . ASN B 79  ? 2.16594 1.90438 2.80414 -0.03530 -0.85823 0.02062  79  ASN B C   
1854 O O   . ASN B 79  ? 2.44108 2.19200 3.01777 -0.01642 -0.84684 0.01884  79  ASN B O   
1855 C CB  . ASN B 79  ? 2.45401 2.15424 3.24811 -0.06595 -0.94360 0.02821  79  ASN B CB  
1856 C CG  . ASN B 79  ? 2.36300 2.07920 3.31412 -0.09354 -0.96702 0.06276  79  ASN B CG  
1857 O OD1 . ASN B 79  ? 2.31823 2.10119 3.38226 -0.11045 -0.92814 0.11203  79  ASN B OD1 
1858 N ND2 . ASN B 79  ? 2.31648 1.97091 3.27452 -0.09516 -1.02971 0.03972  79  ASN B ND2 
1859 N N   . LYS B 80  ? 1.97802 1.67212 2.54919 -0.03292 -0.85410 -0.00721 80  LYS B N   
1860 C CA  . LYS B 80  ? 1.90201 1.56434 2.32073 -0.00797 -0.81579 -0.03636 80  LYS B CA  
1861 C C   . LYS B 80  ? 1.66382 1.23682 1.97827 0.00395  -0.85992 -0.08978 80  LYS B C   
1862 O O   . LYS B 80  ? 1.76074 1.29627 2.12116 -0.00734 -0.89372 -0.10054 80  LYS B O   
1863 C CB  . LYS B 80  ? 1.83162 1.52907 2.24859 -0.00902 -0.73526 -0.01495 80  LYS B CB  
1864 C CG  . LYS B 80  ? 1.82961 1.61278 2.35657 -0.01818 -0.68959 0.03875  80  LYS B CG  
1865 C CD  . LYS B 80  ? 1.85568 1.66565 2.44299 -0.03079 -0.64832 0.06340  80  LYS B CD  
1866 C CE  . LYS B 80  ? 1.91992 1.81004 2.65344 -0.04369 -0.62931 0.12059  80  LYS B CE  
1867 N NZ  . LYS B 80  ? 1.83194 1.73731 2.64988 -0.06131 -0.61533 0.14679  80  LYS B NZ  
1868 N N   . THR B 81  ? 1.69139 1.22801 1.85926 0.03188  -0.84257 -0.11847 81  THR B N   
1869 C CA  . THR B 81  ? 1.58497 1.03984 1.63358 0.05440  -0.86156 -0.16498 81  THR B CA  
1870 C C   . THR B 81  ? 1.72393 1.16538 1.64987 0.07563  -0.81027 -0.17985 81  THR B C   
1871 O O   . THR B 81  ? 1.74510 1.21020 1.61436 0.08939  -0.76849 -0.16652 81  THR B O   
1872 C CB  . THR B 81  ? 1.83521 1.25176 1.82407 0.07464  -0.89802 -0.18300 81  THR B CB  
1873 O OG1 . THR B 81  ? 1.83139 1.27431 1.94374 0.05346  -0.93697 -0.16092 81  THR B OG1 
1874 C CG2 . THR B 81  ? 1.86184 1.19813 1.75641 0.09940  -0.92391 -0.22609 81  THR B CG2 
1875 N N   . ASP B 82  ? 1.72102 1.12612 1.61334 0.07947  -0.79984 -0.20172 82  ASP B N   
1876 C CA  . ASP B 82  ? 1.66458 1.06404 1.45738 0.09938  -0.73400 -0.20807 82  ASP B CA  
1877 C C   . ASP B 82  ? 1.87362 1.22650 1.52074 0.13532  -0.74118 -0.23592 82  ASP B C   
1878 O O   . ASP B 82  ? 1.87483 1.17565 1.47467 0.15440  -0.77645 -0.26251 82  ASP B O   
1879 C CB  . ASP B 82  ? 1.44294 0.81350 1.23987 0.09732  -0.72643 -0.22502 82  ASP B CB  
1880 C CG  . ASP B 82  ? 1.66948 1.06207 1.41723 0.10685  -0.64884 -0.21532 82  ASP B CG  
1881 O OD1 . ASP B 82  ? 1.80902 1.19165 1.45195 0.13177  -0.61839 -0.22333 82  ASP B OD1 
1882 O OD2 . ASP B 82  ? 1.62306 1.04436 1.44096 0.08956  -0.61908 -0.19701 82  ASP B OD2 
1883 N N   . ILE B 83  ? 1.79139 1.17282 1.38232 0.14722  -0.68255 -0.21710 83  ILE B N   
1884 C CA  . ILE B 83  ? 1.91859 1.26395 1.37468 0.18217  -0.67784 -0.23283 83  ILE B CA  
1885 C C   . ILE B 83  ? 1.95970 1.31211 1.34757 0.19722  -0.60503 -0.22682 83  ILE B C   
1886 O O   . ILE B 83  ? 2.08789 1.43806 1.39235 0.21903  -0.57532 -0.21859 83  ILE B O   
1887 C CB  . ILE B 83  ? 1.95991 1.33044 1.41568 0.18399  -0.68451 -0.21043 83  ILE B CB  
1888 C CG1 . ILE B 83  ? 1.77796 1.21971 1.34714 0.15508  -0.64725 -0.17017 83  ILE B CG1 
1889 C CG2 . ILE B 83  ? 2.02322 1.36969 1.50294 0.18575  -0.74646 -0.22237 83  ILE B CG2 
1890 C CD1 . ILE B 83  ? 1.90540 1.37284 1.47859 0.15868  -0.64834 -0.14708 83  ILE B CD1 
1891 N N   . THR B 84  ? 1.90404 1.26708 1.33338 0.18534  -0.57617 -0.22733 84  THR B N   
1892 C CA  . THR B 84  ? 1.85521 1.23966 1.24961 0.19291  -0.50555 -0.21432 84  THR B CA  
1893 C C   . THR B 84  ? 1.96847 1.31087 1.23025 0.23244  -0.49063 -0.23270 84  THR B C   
1894 O O   . THR B 84  ? 2.05196 1.41518 1.27149 0.24301  -0.43827 -0.21225 84  THR B O   
1895 C CB  . THR B 84  ? 1.77663 1.17346 1.23414 0.17699  -0.48644 -0.21518 84  THR B CB  
1896 O OG1 . THR B 84  ? 1.68546 1.12780 1.26272 0.14392  -0.49181 -0.19063 84  THR B OG1 
1897 C CG2 . THR B 84  ? 1.69786 1.11852 1.12548 0.18475  -0.41820 -0.20216 84  THR B CG2 
1898 N N   . PHE B 85  ? 2.02345 1.30579 1.21904 0.25660  -0.53641 -0.27011 85  PHE B N   
1899 C CA  . PHE B 85  ? 2.00267 1.25168 1.07727 0.29968  -0.51501 -0.28204 85  PHE B CA  
1900 C C   . PHE B 85  ? 2.18498 1.42829 1.20471 0.31751  -0.52585 -0.27144 85  PHE B C   
1901 O O   . PHE B 85  ? 2.26203 1.49208 1.18873 0.35227  -0.49396 -0.26804 85  PHE B O   
1902 C CB  . PHE B 85  ? 2.04945 1.25256 1.10308 0.31993  -0.54030 -0.31454 85  PHE B CB  
1903 C CG  . PHE B 85  ? 2.26044 1.46408 1.33986 0.31520  -0.51517 -0.32378 85  PHE B CG  
1904 C CD1 . PHE B 85  ? 2.20164 1.42730 1.38148 0.27699  -0.52426 -0.31858 85  PHE B CD1 
1905 C CD2 . PHE B 85  ? 2.25250 1.43541 1.25820 0.35109  -0.48228 -0.33615 85  PHE B CD2 
1906 C CE1 . PHE B 85  ? 2.09563 1.32335 1.30511 0.27334  -0.49843 -0.32355 85  PHE B CE1 
1907 C CE2 . PHE B 85  ? 2.07295 1.25694 1.10547 0.34848  -0.45924 -0.34398 85  PHE B CE2 
1908 C CZ  . PHE B 85  ? 2.09662 1.29921 1.22773 0.30970  -0.46918 -0.33968 85  PHE B CZ  
1909 N N   . VAL B 86  ? 2.31963 1.57456 1.39814 0.29608  -0.56846 -0.26386 86  VAL B N   
1910 C CA  . VAL B 86  ? 2.28607 1.53363 1.31858 0.31268  -0.58359 -0.25487 86  VAL B CA  
1911 C C   . VAL B 86  ? 2.23087 1.51718 1.25719 0.30629  -0.54543 -0.21843 86  VAL B C   
1912 O O   . VAL B 86  ? 2.21505 1.49486 1.16983 0.33032  -0.52786 -0.20457 86  VAL B O   
1913 C CB  . VAL B 86  ? 2.23376 1.47125 1.33613 0.29607  -0.65267 -0.26603 86  VAL B CB  
1914 C CG1 . VAL B 86  ? 2.45935 1.66976 1.49251 0.32407  -0.67611 -0.27030 86  VAL B CG1 
1915 C CG2 . VAL B 86  ? 2.32997 1.53812 1.47861 0.28871  -0.69041 -0.29482 86  VAL B CG2 
1916 N N   . TYR B 87  ? 2.17398 1.50192 1.28259 0.27444  -0.53053 -0.19971 87  TYR B N   
1917 C CA  . TYR B 87  ? 1.82246 1.19462 0.96058 0.26321  -0.48557 -0.16058 87  TYR B CA  
1918 C C   . TYR B 87  ? 2.06601 1.43660 1.12434 0.28581  -0.42419 -0.14441 87  TYR B C   
1919 O O   . TYR B 87  ? 2.19688 1.57601 1.25852 0.28489  -0.38381 -0.14610 87  TYR B O   
1920 C CB  . TYR B 87  ? 1.79141 1.21577 1.05497 0.22535  -0.46387 -0.14324 87  TYR B CB  
1921 C CG  . TYR B 87  ? 1.81603 1.28124 1.12642 0.21227  -0.43707 -0.10954 87  TYR B CG  
1922 C CD1 . TYR B 87  ? 1.83513 1.31666 1.20191 0.20181  -0.47330 -0.10010 87  TYR B CD1 
1923 C CD2 . TYR B 87  ? 1.78985 1.27690 1.09511 0.21070  -0.37785 -0.08755 87  TYR B CD2 
1924 C CE1 . TYR B 87  ? 1.71001 1.22502 1.11730 0.19392  -0.44940 -0.07175 87  TYR B CE1 
1925 C CE2 . TYR B 87  ? 1.76688 1.28356 1.11451 0.20028  -0.35815 -0.06066 87  TYR B CE2 
1926 C CZ  . TYR B 87  ? 1.80309 1.33225 1.19786 0.19353  -0.39301 -0.05387 87  TYR B CZ  
1927 O OH  . TYR B 87  ? 1.60566 1.16052 1.03946 0.18734  -0.37361 -0.02934 87  TYR B OH  
1928 N N   . ASN B 88  ? 2.29766 1.65992 1.29104 0.30603  -0.41668 -0.12488 88  ASN B N   
1929 C CA  . ASN B 88  ? 2.40604 1.76430 1.31939 0.33176  -0.36131 -0.10391 88  ASN B CA  
1930 C C   . ASN B 88  ? 2.37832 1.78169 1.36081 0.30774  -0.31027 -0.06445 88  ASN B C   
1931 O O   . ASN B 88  ? 2.41061 1.82047 1.39486 0.30719  -0.30949 -0.03886 88  ASN B O   
1932 C CB  . ASN B 88  ? 2.58145 1.90650 1.39395 0.36821  -0.37739 -0.10178 88  ASN B CB  
1933 C CG  . ASN B 88  ? 2.78196 2.11598 1.53794 0.38783  -0.31951 -0.06108 88  ASN B CG  
1934 O OD1 . ASN B 88  ? 2.96661 2.30903 1.72738 0.38522  -0.31794 -0.03150 88  ASN B OD1 
1935 N ND2 . ASN B 88  ? 2.81543 2.14919 1.52517 0.40781  -0.27072 -0.05646 88  ASN B ND2 
1936 N N   . ALA B 89  ? 2.14895 1.58112 1.19267 0.28770  -0.27242 -0.06143 89  ALA B N   
1937 C CA  . ALA B 89  ? 2.04605 1.51543 1.15200 0.26688  -0.22699 -0.02899 89  ALA B CA  
1938 C C   . ALA B 89  ? 1.78973 1.27998 0.92779 0.25806  -0.18572 -0.03010 89  ALA B C   
1939 O O   . ALA B 89  ? 1.82251 1.30666 0.96684 0.25754  -0.19819 -0.05695 89  ALA B O   
1940 C CB  . ALA B 89  ? 1.96960 1.46493 1.16809 0.23735  -0.24776 -0.02404 89  ALA B CB  
1941 N N   . ASN B 90  ? 1.70682 1.22063 0.87069 0.25071  -0.13943 0.00013  90  ASN B N   
1942 C CA  . ASN B 90  ? 1.66587 1.20519 0.87398 0.23964  -0.10225 0.00258  90  ASN B CA  
1943 C C   . ASN B 90  ? 1.50012 1.06760 0.80432 0.20683  -0.11233 -0.00495 90  ASN B C   
1944 O O   . ASN B 90  ? 1.50163 1.07679 0.84548 0.19230  -0.12997 0.00127  90  ASN B O   
1945 C CB  . ASN B 90  ? 1.73652 1.29123 0.94463 0.24364  -0.05214 0.03994  90  ASN B CB  
1946 C CG  . ASN B 90  ? 2.10989 1.64290 1.22033 0.28126  -0.03151 0.05398  90  ASN B CG  
1947 O OD1 . ASN B 90  ? 2.28232 1.78671 1.31765 0.30765  -0.05222 0.02858  90  ASN B OD1 
1948 N ND2 . ASN B 90  ? 2.17599 1.72089 1.28661 0.28582  0.00861  0.09558  90  ASN B ND2 
1949 N N   . PHE B 91  ? 1.44992 1.03284 0.78805 0.19891  -0.10009 -0.01760 91  PHE B N   
1950 C CA  . PHE B 91  ? 1.31636 0.92637 0.73628 0.17295  -0.10682 -0.02376 91  PHE B CA  
1951 C C   . PHE B 91  ? 1.08883 0.72461 0.54785 0.16460  -0.07053 -0.01467 91  PHE B C   
1952 O O   . PHE B 91  ? 1.31476 0.94807 0.74472 0.17888  -0.04712 -0.01421 91  PHE B O   
1953 C CB  . PHE B 91  ? 1.27982 0.88294 0.71405 0.16941  -0.14045 -0.05015 91  PHE B CB  
1954 C CG  . PHE B 91  ? 1.41611 1.00637 0.85007 0.16789  -0.18253 -0.05661 91  PHE B CG  
1955 C CD1 . PHE B 91  ? 1.33226 0.94529 0.82330 0.15188  -0.19142 -0.04561 91  PHE B CD1 
1956 C CD2 . PHE B 91  ? 1.45491 1.01008 0.83292 0.18479  -0.21546 -0.07478 91  PHE B CD2 
1957 C CE1 . PHE B 91  ? 1.34615 0.95321 0.84665 0.15131  -0.22909 -0.04831 91  PHE B CE1 
1958 C CE2 . PHE B 91  ? 1.44654 0.99230 0.83394 0.18213  -0.25893 -0.07985 91  PHE B CE2 
1959 C CZ  . PHE B 91  ? 1.46285 1.03770 0.91606 0.16455  -0.26420 -0.06456 91  PHE B CZ  
1960 N N   . PHE B 92  ? 1.12287 0.78313 0.64652 0.14433  -0.06702 -0.00765 92  PHE B N   
1961 C CA  . PHE B 92  ? 1.01131 0.69678 0.58102 0.13429  -0.04224 -0.00227 92  PHE B CA  
1962 C C   . PHE B 92  ? 1.05815 0.76304 0.68258 0.11896  -0.05813 -0.01443 92  PHE B C   
1963 O O   . PHE B 92  ? 1.09619 0.80120 0.73484 0.11378  -0.07882 -0.01687 92  PHE B O   
1964 C CB  . PHE B 92  ? 1.14276 0.83579 0.73280 0.12845  -0.01907 0.02357  92  PHE B CB  
1965 C CG  . PHE B 92  ? 1.16329 0.84079 0.70050 0.14572  0.00141  0.04418  92  PHE B CG  
1966 C CD1 . PHE B 92  ? 1.14170 0.82732 0.66221 0.15900  0.03314  0.05430  92  PHE B CD1 
1967 C CD2 . PHE B 92  ? 1.26794 0.92458 0.77113 0.15198  -0.00906 0.05613  92  PHE B CD2 
1968 C CE1 . PHE B 92  ? 1.26227 0.93652 0.72874 0.18016  0.05707  0.07752  92  PHE B CE1 
1969 C CE2 . PHE B 92  ? 1.39472 1.03744 0.84294 0.17149  0.01163  0.07900  92  PHE B CE2 
1970 C CZ  . PHE B 92  ? 1.39476 1.04689 0.82261 0.18652  0.04629  0.09051  92  PHE B CZ  
1971 N N   . LEU B 93  ? 0.93165 0.65519 0.58654 0.11453  -0.04663 -0.01951 93  LEU B N   
1972 C CA  . LEU B 93  ? 0.96152 0.70550 0.66285 0.10397  -0.05740 -0.02728 93  LEU B CA  
1973 C C   . LEU B 93  ? 0.94959 0.71420 0.69023 0.09603  -0.04186 -0.02063 93  LEU B C   
1974 O O   . LEU B 93  ? 1.00936 0.78168 0.75553 0.09812  -0.02288 -0.01603 93  LEU B O   
1975 C CB  . LEU B 93  ? 1.00344 0.74813 0.70696 0.10701  -0.06653 -0.04073 93  LEU B CB  
1976 C CG  . LEU B 93  ? 0.92274 0.68560 0.66611 0.09964  -0.08146 -0.04349 93  LEU B CG  
1977 C CD1 . LEU B 93  ? 0.98078 0.73931 0.72482 0.09843  -0.10130 -0.04087 93  LEU B CD1 
1978 C CD2 . LEU B 93  ? 0.96881 0.73104 0.72230 0.10129  -0.08764 -0.05149 93  LEU B CD2 
1979 N N   . PHE B 94  ? 0.79488 0.56813 0.56374 0.08916  -0.05190 -0.02105 94  PHE B N   
1980 C CA  . PHE B 94  ? 0.91477 0.70062 0.72052 0.08182  -0.04705 -0.01814 94  PHE B CA  
1981 C C   . PHE B 94  ? 0.92821 0.73325 0.75736 0.08239  -0.05700 -0.02976 94  PHE B C   
1982 O O   . PHE B 94  ? 0.98060 0.78828 0.80516 0.08726  -0.06907 -0.03515 94  PHE B O   
1983 C CB  . PHE B 94  ? 0.93817 0.70973 0.75038 0.07786  -0.05401 -0.01148 94  PHE B CB  
1984 C CG  . PHE B 94  ? 0.89620 0.67305 0.75012 0.06961  -0.05785 -0.01177 94  PHE B CG  
1985 C CD1 . PHE B 94  ? 0.78690 0.57552 0.67147 0.06205  -0.04434 -0.00196 94  PHE B CD1 
1986 C CD2 . PHE B 94  ? 0.91175 0.68030 0.77606 0.07129  -0.07711 -0.02208 94  PHE B CD2 
1987 C CE1 . PHE B 94  ? 0.82631 0.61833 0.75798 0.05249  -0.05481 -0.00275 94  PHE B CE1 
1988 C CE2 . PHE B 94  ? 0.94802 0.71382 0.84868 0.06489  -0.08842 -0.02684 94  PHE B CE2 
1989 C CZ  . PHE B 94  ? 1.04059 0.81795 0.97836 0.05352  -0.07971 -0.01721 94  PHE B CZ  
1990 N N   . ALA B 95  ? 0.83101 0.65186 0.68693 0.07934  -0.05112 -0.03066 95  ALA B N   
1991 C CA  . ALA B 95  ? 0.71501 0.55451 0.58763 0.08300  -0.05973 -0.03963 95  ALA B CA  
1992 C C   . ALA B 95  ? 0.90437 0.74565 0.79869 0.08138  -0.07363 -0.04585 95  ALA B C   
1993 O O   . ALA B 95  ? 0.97424 0.81176 0.89398 0.07228  -0.07318 -0.04134 95  ALA B O   
1994 C CB  . ALA B 95  ? 0.80272 0.65722 0.68924 0.08381  -0.04875 -0.03827 95  ALA B CB  
1995 N N   . THR B 96  ? 0.84219 0.68848 0.72770 0.09192  -0.08668 -0.05529 96  THR B N   
1996 C CA  . THR B 96  ? 0.82523 0.66957 0.72007 0.09733  -0.10505 -0.06762 96  THR B CA  
1997 C C   . THR B 96  ? 0.96007 0.82549 0.84994 0.11075  -0.11005 -0.07348 96  THR B C   
1998 O O   . THR B 96  ? 0.83089 0.71017 0.70891 0.11745  -0.09963 -0.06591 96  THR B O   
1999 C CB  . THR B 96  ? 0.81325 0.63831 0.68925 0.10649  -0.11651 -0.07482 96  THR B CB  
2000 O OG1 . THR B 96  ? 0.93855 0.77275 0.79125 0.11849  -0.10912 -0.07005 96  THR B OG1 
2001 C CG2 . THR B 96  ? 0.84523 0.64623 0.73023 0.09372  -0.11546 -0.06764 96  THR B CG2 
2002 N N   . LEU B 97  ? 0.96448 0.83112 0.86636 0.11460  -0.12827 -0.08548 97  LEU B N   
2003 C CA  . LEU B 97  ? 0.94529 0.83135 0.83940 0.12952  -0.13528 -0.09008 97  LEU B CA  
2004 C C   . LEU B 97  ? 1.08475 0.96486 0.94215 0.15424  -0.14974 -0.10336 97  LEU B C   
2005 O O   . LEU B 97  ? 1.18162 1.03926 1.03519 0.15810  -0.17112 -0.12053 97  LEU B O   
2006 C CB  . LEU B 97  ? 0.81105 0.70355 0.74055 0.12144  -0.15039 -0.09575 97  LEU B CB  
2007 C CG  . LEU B 97  ? 0.97407 0.88891 0.89941 0.13545  -0.15683 -0.09670 97  LEU B CG  
2008 C CD1 . LEU B 97  ? 0.78630 0.71907 0.71166 0.13442  -0.13060 -0.07822 97  LEU B CD1 
2009 C CD2 . LEU B 97  ? 0.84631 0.76668 0.81365 0.12724  -0.17879 -0.10406 97  LEU B CD2 
2010 N N   . GLU B 98  ? 1.12607 1.02540 0.95787 0.17309  -0.13805 -0.09434 98  GLU B N   
2011 C CA  . GLU B 98  ? 1.18607 1.08473 0.97727 0.20333  -0.14480 -0.10286 98  GLU B CA  
2012 C C   . GLU B 98  ? 1.12052 1.03670 0.89032 0.22566  -0.15250 -0.10478 98  GLU B C   
2013 O O   . GLU B 98  ? 1.08853 1.02933 0.86556 0.22627  -0.13580 -0.08446 98  GLU B O   
2014 C CB  . GLU B 98  ? 1.03653 0.94764 0.81683 0.21227  -0.12190 -0.08472 98  GLU B CB  
2015 C CG  . GLU B 98  ? 1.00922 0.90501 0.80853 0.19130  -0.11537 -0.08005 98  GLU B CG  
2016 C CD  . GLU B 98  ? 1.56375 1.42732 1.35784 0.18978  -0.13340 -0.09951 98  GLU B CD  
2017 O OE1 . GLU B 98  ? 1.59920 1.45302 1.36442 0.21504  -0.14377 -0.11340 98  GLU B OE1 
2018 O OE2 . GLU B 98  ? 1.46264 1.30928 1.28127 0.16533  -0.13650 -0.09959 98  GLU B OE2 
2019 N N   . PRO B 99  ? 1.24501 1.14622 0.98801 0.24512  -0.18039 -0.12895 99  PRO B N   
2020 C CA  . PRO B 99  ? 1.25252 1.16909 0.96296 0.27277  -0.19024 -0.13125 99  PRO B CA  
2021 C C   . PRO B 99  ? 1.51565 1.45629 1.18506 0.30462  -0.16382 -0.11058 99  PRO B C   
2022 O O   . PRO B 99  ? 1.62495 1.56007 1.26507 0.32488  -0.15572 -0.11312 99  PRO B O   
2023 C CB  . PRO B 99  ? 1.33019 1.21575 1.01516 0.28878  -0.23157 -0.16719 99  PRO B CB  
2024 C CG  . PRO B 99  ? 1.28081 1.14099 1.01708 0.25337  -0.24349 -0.17671 99  PRO B CG  
2025 C CD  . PRO B 99  ? 1.31919 1.18455 1.06411 0.24140  -0.20959 -0.15633 99  PRO B CD  
2026 N N   . GLU B 100 ? 1.65866 1.06632 1.25535 0.16805  0.07374  -0.17560 100 GLU B N   
2027 C CA  . GLU B 100 ? 1.70838 1.12245 1.30520 0.16529  0.09633  -0.18183 100 GLU B CA  
2028 C C   . GLU B 100 ? 1.99217 1.36717 1.54037 0.16433  0.09946  -0.19248 100 GLU B C   
2029 O O   . GLU B 100 ? 2.08226 1.46185 1.63303 0.16258  0.11898  -0.20211 100 GLU B O   
2030 C CB  . GLU B 100 ? 1.67574 1.08779 1.25413 0.16919  0.10580  -0.16949 100 GLU B CB  
2031 C CG  . GLU B 100 ? 1.92685 1.32033 1.47677 0.16745  0.12822  -0.17116 100 GLU B CG  
2032 C CD  . GLU B 100 ? 1.82744 1.24829 1.41317 0.16512  0.14343  -0.16791 100 GLU B CD  
2033 O OE1 . GLU B 100 ? 1.79174 1.25875 1.43960 0.16093  0.14301  -0.17650 100 GLU B OE1 
2034 O OE2 . GLU B 100 ? 1.86233 1.25315 1.41005 0.16841  0.15439  -0.15739 100 GLU B OE2 
2035 N N   . ARG B 101 ? 2.25153 1.58809 1.75520 0.16558  0.07926  -0.19360 101 ARG B N   
2036 C CA  . ARG B 101 ? 2.48639 1.78229 1.93652 0.16441  0.07814  -0.20698 101 ARG B CA  
2037 C C   . ARG B 101 ? 2.49246 1.77438 1.95306 0.16027  0.05725  -0.21934 101 ARG B C   
2038 O O   . ARG B 101 ? 2.48566 1.72877 1.89931 0.15906  0.03207  -0.21977 101 ARG B O   
2039 C CB  . ARG B 101 ? 2.66183 1.91059 2.02870 0.16978  0.06932  -0.19806 101 ARG B CB  
2040 C CG  . ARG B 101 ? 2.70385 1.94897 2.04787 0.17460  0.09205  -0.18543 101 ARG B CG  
2041 C CD  . ARG B 101 ? 2.89588 2.11998 2.20133 0.17231  0.11593  -0.19600 101 ARG B CD  
2042 N NE  . ARG B 101 ? 3.01345 2.18714 2.23911 0.17378  0.10194  -0.20457 101 ARG B NE  
2043 C CZ  . ARG B 101 ? 3.01385 2.14053 2.15483 0.17852  0.10828  -0.19832 101 ARG B CZ  
2044 N NH1 . ARG B 101 ? 2.83583 1.95130 1.95823 0.18274  0.13083  -0.18165 101 ARG B NH1 
2045 N NH2 . ARG B 101 ? 3.09820 2.18488 2.16807 0.17837  0.09064  -0.20937 101 ARG B NH2 
2046 N N   . PRO B 102 ? 2.29152 1.60004 1.81258 0.15819  0.06431  -0.23023 102 PRO B N   
2047 C CA  . PRO B 102 ? 2.11224 1.39980 1.64600 0.15458  0.04502  -0.24011 102 PRO B CA  
2048 C C   . PRO B 102 ? 2.07382 1.33395 1.58494 0.15382  0.04892  -0.26507 102 PRO B C   
2049 O O   . PRO B 102 ? 2.21998 1.49775 1.77663 0.15678  0.06231  -0.28042 102 PRO B O   
2050 C CB  . PRO B 102 ? 2.09730 1.42380 1.70611 0.15601  0.05150  -0.23734 102 PRO B CB  
2051 C CG  . PRO B 102 ? 2.13721 1.50612 1.77383 0.15959  0.07790  -0.24005 102 PRO B CG  
2052 C CD  . PRO B 102 ? 2.15819 1.51257 1.73740 0.15983  0.08706  -0.23449 102 PRO B CD  
2053 N N   . SER B 114 ? 1.36551 0.93322 1.27327 -0.09348 -0.29950 0.08910  114 SER B N   
2054 C CA  . SER B 114 ? 1.78798 1.41711 1.68480 -0.06407 -0.27997 0.07795  114 SER B CA  
2055 C C   . SER B 114 ? 1.72965 1.31902 1.58503 -0.02255 -0.24941 0.04849  114 SER B C   
2056 O O   . SER B 114 ? 1.71148 1.22546 1.52147 -0.01028 -0.25090 0.01680  114 SER B O   
2057 C CB  . SER B 114 ? 1.69860 1.33200 1.58176 -0.07202 -0.30460 0.06430  114 SER B CB  
2058 O OG  . SER B 114 ? 1.89995 1.43626 1.73088 -0.06854 -0.31734 0.03049  114 SER B OG  
2059 N N   . PRO B 115 ? 1.66857 1.31205 1.53944 -0.00242 -0.22115 0.05811  115 PRO B N   
2060 C CA  . PRO B 115 ? 1.70465 1.31615 1.54481 0.03282  -0.19191 0.03220  115 PRO B CA  
2061 C C   . PRO B 115 ? 1.44493 1.06637 1.25611 0.05929  -0.17846 0.00954  115 PRO B C   
2062 O O   . PRO B 115 ? 1.43839 1.11410 1.26169 0.05788  -0.18654 0.01793  115 PRO B O   
2063 C CB  . PRO B 115 ? 1.50806 1.18131 1.37984 0.03833  -0.17242 0.05384  115 PRO B CB  
2064 C CG  . PRO B 115 ? 1.60650 1.37083 1.51624 0.01993  -0.18050 0.08327  115 PRO B CG  
2065 C CD  . PRO B 115 ? 1.54112 1.28215 1.45865 -0.01273 -0.21421 0.09234  115 PRO B CD  
2066 N N   . VAL B 116 ? 1.36209 0.93053 1.13705 0.08412  -0.15739 -0.01814 116 VAL B N   
2067 C CA  . VAL B 116 ? 1.37366 0.94130 1.11772 0.10934  -0.14189 -0.03728 116 VAL B CA  
2068 C C   . VAL B 116 ? 1.25199 0.88134 1.01755 0.13040  -0.11523 -0.03368 116 VAL B C   
2069 O O   . VAL B 116 ? 1.19917 0.86490 0.96436 0.14478  -0.11055 -0.03439 116 VAL B O   
2070 C CB  . VAL B 116 ? 1.23366 0.71655 0.92708 0.12295  -0.12979 -0.06811 116 VAL B CB  
2071 C CG1 . VAL B 116 ? 1.43227 0.90887 1.08936 0.14496  -0.11607 -0.08239 116 VAL B CG1 
2072 C CG2 . VAL B 116 ? 1.40310 0.82336 1.07420 0.10266  -0.15584 -0.07624 116 VAL B CG2 
2073 N N   . LEU B 117 ? 1.16722 0.80872 0.95177 0.13358  -0.09928 -0.03075 117 LEU B N   
2074 C CA  . LEU B 117 ? 1.14394 0.84647 0.94834 0.15090  -0.07618 -0.02982 117 LEU B CA  
2075 C C   . LEU B 117 ? 1.07544 0.85904 0.92175 0.13457  -0.08556 0.00049  117 LEU B C   
2076 O O   . LEU B 117 ? 1.15620 0.93863 1.01946 0.11156  -0.10045 0.02141  117 LEU B O   
2077 C CB  . LEU B 117 ? 1.03344 0.71302 0.83473 0.16310  -0.05498 -0.04425 117 LEU B CB  
2078 C CG  . LEU B 117 ? 1.05974 0.79177 0.87345 0.18246  -0.03055 -0.05251 117 LEU B CG  
2079 C CD1 . LEU B 117 ? 0.98894 0.70649 0.78040 0.20318  -0.01567 -0.07358 117 LEU B CD1 
2080 C CD2 . LEU B 117 ? 0.96694 0.68874 0.78671 0.18840  -0.01663 -0.06190 117 LEU B CD2 
2081 N N   . THR B 118 ? 1.04942 0.90253 0.91273 0.14678  -0.07575 0.00328  118 THR B N   
2082 C CA  . THR B 118 ? 0.94918 0.89073 0.85202 0.13293  -0.07978 0.03065  118 THR B CA  
2083 C C   . THR B 118 ? 0.92156 0.92536 0.83511 0.15499  -0.05330 0.02219  118 THR B C   
2084 O O   . THR B 118 ? 1.06417 1.04651 0.95938 0.18123  -0.03556 -0.00501 118 THR B O   
2085 C CB  . THR B 118 ? 0.92215 0.90339 0.84419 0.12246  -0.09897 0.04401  118 THR B CB  
2086 O OG1 . THR B 118 ? 1.13566 1.10398 1.03983 0.14903  -0.09396 0.02257  118 THR B OG1 
2087 C CG2 . THR B 118 ? 1.06855 1.00025 0.98646 0.09204  -0.12915 0.05598  118 THR B CG2 
2088 N N   . GLY B 119 ? 0.88005 0.96085 0.82199 0.14255  -0.05061 0.04569  119 GLY B N   
2089 C CA  . GLY B 119 ? 0.87381 1.02158 0.82383 0.16124  -0.02664 0.03692  119 GLY B CA  
2090 C C   . GLY B 119 ? 0.92527 1.08505 0.87300 0.15206  -0.02117 0.04836  119 GLY B C   
2091 O O   . GLY B 119 ? 0.97241 1.12278 0.92734 0.12583  -0.03719 0.07766  119 GLY B O   
2092 N N   . VAL B 120 ? 0.92976 1.10871 0.86759 0.17377  -0.00037 0.02527  120 VAL B N   
2093 C CA  . VAL B 120 ? 0.90406 1.09714 0.83637 0.16946  0.00378  0.03205  120 VAL B CA  
2094 C C   . VAL B 120 ? 0.94714 1.06379 0.85932 0.18409  0.00847  0.00264  120 VAL B C   
2095 O O   . VAL B 120 ? 0.85957 0.96992 0.76250 0.20640  0.02565  -0.03092 120 VAL B O   
2096 C CB  . VAL B 120 ? 0.80217 1.08851 0.73934 0.17967  0.02233  0.02812  120 VAL B CB  
2097 C CG1 . VAL B 120 ? 0.78342 1.06934 0.70493 0.18696  0.02919  0.01589  120 VAL B CG1 
2098 C CG2 . VAL B 120 ? 0.84387 1.20985 0.80101 0.15668  0.01740  0.06821  120 VAL B CG2 
2099 N N   . PRO B 121 ? 0.87353 0.92827 0.78115 0.17242  -0.00579 0.01273  121 PRO B N   
2100 C CA  . PRO B 121 ? 0.77034 0.75824 0.66402 0.18629  0.00074  -0.01556 121 PRO B CA  
2101 C C   . PRO B 121 ? 0.81534 0.82391 0.71207 0.19189  0.00545  -0.01945 121 PRO B C   
2102 O O   . PRO B 121 ? 0.91765 0.87693 0.81065 0.20096  0.00924  -0.03968 121 PRO B O   
2103 C CB  . PRO B 121 ? 0.91891 0.83341 0.80897 0.17237  -0.01789 -0.00381 121 PRO B CB  
2104 C CG  . PRO B 121 ? 0.89105 0.83925 0.79776 0.14787  -0.03685 0.03756  121 PRO B CG  
2105 C CD  . PRO B 121 ? 0.87684 0.91457 0.79455 0.14581  -0.02872 0.04885  121 PRO B CD  
2106 N N   . VAL B 122 ? 0.84669 0.92981 0.75003 0.18625  0.00479  0.00000  122 VAL B N   
2107 C CA  . VAL B 122 ? 0.87127 0.98428 0.77437 0.19120  0.00568  -0.00146 122 VAL B CA  
2108 C C   . VAL B 122 ? 0.86392 1.04412 0.76046 0.20487  0.02436  -0.02596 122 VAL B C   
2109 O O   . VAL B 122 ? 0.82684 1.06811 0.72366 0.20201  0.03036  -0.01605 122 VAL B O   
2110 C CB  . VAL B 122 ? 0.82458 0.96529 0.73377 0.17239  -0.01328 0.04454  122 VAL B CB  
2111 C CG1 . VAL B 122 ? 0.70998 0.89292 0.61499 0.17969  -0.01399 0.04362  122 VAL B CG1 
2112 C CG2 . VAL B 122 ? 0.81435 0.87700 0.73149 0.16190  -0.03242 0.06242  122 VAL B CG2 
2113 N N   . ALA B 123 ? 0.88968 1.06038 0.78272 0.21942  0.03383  -0.05971 123 ALA B N   
2114 C CA  . ALA B 123 ? 0.78673 1.01286 0.67255 0.23235  0.04988  -0.08930 123 ALA B CA  
2115 C C   . ALA B 123 ? 0.76009 1.02811 0.64260 0.23167  0.04284  -0.08861 123 ALA B C   
2116 O O   . ALA B 123 ? 0.84898 1.08042 0.73991 0.23145  0.03286  -0.08936 123 ALA B O   
2117 C CB  . ALA B 123 ? 0.85429 1.03284 0.73914 0.24824  0.06672  -0.13379 123 ALA B CB  
2118 N N   . GLY B 124 ? 0.73918 1.08788 0.60942 0.23194  0.04721  -0.08615 124 GLY B N   
2119 C CA  . GLY B 124 ? 0.87602 1.27098 0.73666 0.23340  0.04069  -0.09219 124 GLY B CA  
2120 C C   . GLY B 124 ? 0.90195 1.29168 0.76176 0.24816  0.05338  -0.14700 124 GLY B C   
2121 O O   . GLY B 124 ? 1.03557 1.39847 0.89790 0.25834  0.07058  -0.17898 124 GLY B O   
2122 N N   . VAL B 125 ? 1.24456 0.99190 0.72558 0.22267  -0.03465 -0.02530 125 VAL B N   
2123 C CA  . VAL B 125 ? 1.30192 1.01913 0.76241 0.21624  -0.07411 -0.05698 125 VAL B CA  
2124 C C   . VAL B 125 ? 1.43308 1.10137 0.80253 0.25080  -0.07602 -0.07149 125 VAL B C   
2125 O O   . VAL B 125 ? 1.53919 1.19893 0.84743 0.28514  -0.05691 -0.05865 125 VAL B O   
2126 C CB  . VAL B 125 ? 1.25906 0.98366 0.72981 0.20724  -0.11348 -0.06538 125 VAL B CB  
2127 C CG1 . VAL B 125 ? 1.34139 1.04862 0.74094 0.24118  -0.11888 -0.05753 125 VAL B CG1 
2128 C CG2 . VAL B 125 ? 1.28445 0.98743 0.75820 0.18779  -0.15767 -0.09466 125 VAL B CG2 
2129 N N   . ALA B 126 ? 1.29703 0.92882 0.65269 0.24355  -0.09812 -0.09737 126 ALA B N   
2130 C CA  . ALA B 126 ? 1.58182 1.15111 0.84166 0.27769  -0.11114 -0.11982 126 ALA B CA  
2131 C C   . ALA B 126 ? 1.41098 0.93538 0.65522 0.25738  -0.17016 -0.15173 126 ALA B C   
2132 O O   . ALA B 126 ? 1.40077 0.93197 0.70903 0.21782  -0.18677 -0.15805 126 ALA B O   
2133 C CB  . ALA B 126 ? 1.40663 0.96246 0.65740 0.29355  -0.08052 -0.11993 126 ALA B CB  
2134 N N   . TYR B 127 ? 1.50612 0.98684 0.66769 0.28205  -0.20321 -0.16928 127 TYR B N   
2135 C CA  . TYR B 127 ? 1.59420 1.03210 0.74134 0.26047  -0.26760 -0.19919 127 TYR B CA  
2136 C C   . TYR B 127 ? 1.78141 1.13464 0.85678 0.27392  -0.28691 -0.22893 127 TYR B C   
2137 O O   . TYR B 127 ? 1.81169 1.11705 0.78729 0.32451  -0.27105 -0.23780 127 TYR B O   
2138 C CB  . TYR B 127 ? 1.63301 1.05930 0.72176 0.28090  -0.30214 -0.20569 127 TYR B CB  
2139 C CG  . TYR B 127 ? 1.64304 1.14444 0.80154 0.26879  -0.28984 -0.17771 127 TYR B CG  
2140 C CD1 . TYR B 127 ? 1.53661 1.08785 0.79500 0.22478  -0.31636 -0.17538 127 TYR B CD1 
2141 C CD2 . TYR B 127 ? 1.55326 1.07463 0.67760 0.30278  -0.25021 -0.15167 127 TYR B CD2 
2142 C CE1 . TYR B 127 ? 1.60827 1.22237 0.92491 0.22053  -0.30537 -0.15195 127 TYR B CE1 
2143 C CE2 . TYR B 127 ? 1.60942 1.18645 0.79111 0.29345  -0.24197 -0.12677 127 TYR B CE2 
2144 C CZ  . TYR B 127 ? 1.57590 1.19687 0.85106 0.25504  -0.27031 -0.12897 127 TYR B CZ  
2145 O OH  . TYR B 127 ? 1.52424 1.19536 0.85109 0.25248  -0.26251 -0.10625 127 TYR B OH  
2146 N N   . LEU B 128 ? 1.70805 1.04109 0.83185 0.23071  -0.31916 -0.24250 128 LEU B N   
2147 C CA  . LEU B 128 ? 1.95137 1.19650 1.01606 0.23739  -0.33951 -0.26886 128 LEU B CA  
2148 C C   . LEU B 128 ? 1.95598 1.15425 1.03181 0.19326  -0.41074 -0.29283 128 LEU B C   
2149 O O   . LEU B 128 ? 1.94872 1.20616 1.11613 0.14650  -0.43143 -0.28137 128 LEU B O   
2150 C CB  . LEU B 128 ? 1.77707 1.03874 0.89598 0.22599  -0.29826 -0.25377 128 LEU B CB  
2151 C CG  . LEU B 128 ? 1.78414 1.09093 0.90303 0.26460  -0.23121 -0.22974 128 LEU B CG  
2152 C CD1 . LEU B 128 ? 1.68617 0.98882 0.84325 0.25528  -0.20770 -0.22307 128 LEU B CD1 
2153 C CD2 . LEU B 128 ? 1.71237 0.97389 0.71455 0.33002  -0.21794 -0.24146 128 LEU B CD2 
2154 N N   . ASP B 129 ? 2.19127 1.28230 1.17427 0.20910  -0.44879 -0.32557 129 ASP B N   
2155 C CA  . ASP B 129 ? 2.31623 1.34733 1.30424 0.16374  -0.52219 -0.34923 129 ASP B CA  
2156 C C   . ASP B 129 ? 2.21255 1.21576 1.25524 0.12031  -0.52526 -0.34544 129 ASP B C   
2157 O O   . ASP B 129 ? 2.22951 1.21892 1.32486 0.06308  -0.57603 -0.34961 129 ASP B O   
2158 C CB  . ASP B 129 ? 2.57388 1.51582 1.45453 0.20061  -0.55832 -0.37455 129 ASP B CB  
2159 C CG  . ASP B 129 ? 2.79614 1.75632 1.60345 0.25864  -0.53711 -0.37261 129 ASP B CG  
2160 O OD1 . ASP B 129 ? 2.61029 1.61103 1.43732 0.24625  -0.56538 -0.37037 129 ASP B OD1 
2161 O OD2 . ASP B 129 ? 3.15720 2.09527 1.89132 0.31695  -0.49126 -0.37009 129 ASP B OD2 
2162 N N   . LYS B 130 ? 2.05531 1.05090 1.08754 0.14589  -0.47367 -0.33544 130 LYS B N   
2163 C CA  . LYS B 130 ? 2.10587 1.06735 1.17536 0.11409  -0.47178 -0.32971 130 LYS B CA  
2164 C C   . LYS B 130 ? 1.98538 1.04251 1.14356 0.10777  -0.40557 -0.29318 130 LYS B C   
2165 O O   . LYS B 130 ? 2.00065 1.10720 1.14680 0.15126  -0.35564 -0.28115 130 LYS B O   
2166 C CB  . LYS B 130 ? 2.15592 1.00266 1.11770 0.15886  -0.47857 -0.35361 130 LYS B CB  
2167 C CG  . LYS B 130 ? 2.24309 1.02183 1.13908 0.17087  -0.52820 -0.37320 130 LYS B CG  
2168 C CD  . LYS B 130 ? 2.33525 1.04893 1.25750 0.11801  -0.57915 -0.37635 130 LYS B CD  
2169 C CE  . LYS B 130 ? 2.41608 1.05047 1.28594 0.14650  -0.56625 -0.37893 130 LYS B CE  
2170 N NZ  . LYS B 130 ? 2.48619 1.02128 1.30235 0.14068  -0.62159 -0.39509 130 LYS B NZ  
2171 N N   . PRO B 131 ? 1.96285 1.04645 1.20886 0.05362  -0.40441 -0.27359 131 PRO B N   
2172 C CA  . PRO B 131 ? 1.97866 1.01174 1.25370 -0.00517 -0.45636 -0.27858 131 PRO B CA  
2173 C C   . PRO B 131 ? 2.00278 1.08545 1.33778 -0.04937 -0.49798 -0.27749 131 PRO B C   
2174 O O   . PRO B 131 ? 1.99344 1.02666 1.33929 -0.09459 -0.55407 -0.28716 131 PRO B O   
2175 C CB  . PRO B 131 ? 1.70312 0.77857 1.05827 -0.03803 -0.41940 -0.24716 131 PRO B CB  
2176 C CG  . PRO B 131 ? 1.69666 0.88428 1.10488 -0.01807 -0.36162 -0.22376 131 PRO B CG  
2177 C CD  . PRO B 131 ? 1.60606 0.77716 0.93090 0.04717  -0.34650 -0.24071 131 PRO B CD  
2178 N N   . ASN B 132 ? 1.95770 1.13746 1.33372 -0.03657 -0.47355 -0.26475 132 ASN B N   
2179 C CA  . ASN B 132 ? 1.75725 0.99400 1.18937 -0.06724 -0.51086 -0.26327 132 ASN B CA  
2180 C C   . ASN B 132 ? 1.72194 0.98333 1.10138 -0.01666 -0.50413 -0.27209 132 ASN B C   
2181 O O   . ASN B 132 ? 1.82301 1.09185 1.15720 0.03223  -0.45537 -0.26726 132 ASN B O   
2182 C CB  . ASN B 132 ? 1.72321 1.07424 1.28907 -0.11339 -0.48487 -0.22847 132 ASN B CB  
2183 C CG  . ASN B 132 ? 1.90221 1.24196 1.53493 -0.17960 -0.51663 -0.21863 132 ASN B CG  
2184 O OD1 . ASN B 132 ? 2.08907 1.33763 1.67896 -0.19162 -0.53163 -0.22698 132 ASN B OD1 
2185 N ND2 . ASN B 132 ? 1.88332 1.31682 1.62293 -0.22206 -0.52658 -0.19855 132 ASN B ND2 
2186 N N   . ARG B 133 ? 1.71944 0.99366 1.10603 -0.02979 -0.55551 -0.28292 133 ARG B N   
2187 C CA  . ARG B 133 ? 1.85461 1.14982 1.18956 0.01532  -0.55634 -0.28910 133 ARG B CA  
2188 C C   . ARG B 133 ? 1.70720 1.12405 1.13925 0.01034  -0.51287 -0.25635 133 ARG B C   
2189 O O   . ARG B 133 ? 1.67045 1.15629 1.18825 -0.02287 -0.53768 -0.24610 133 ARG B O   
2190 C CB  . ARG B 133 ? 1.83931 1.09330 1.13696 0.00555  -0.63545 -0.31519 133 ARG B CB  
2191 C CG  . ARG B 133 ? 2.09581 1.28419 1.25540 0.06883  -0.64899 -0.33972 133 ARG B CG  
2192 C CD  . ARG B 133 ? 2.34679 1.49748 1.48025 0.05719  -0.72380 -0.36067 133 ARG B CD  
2193 N NE  . ARG B 133 ? 2.54002 1.65142 1.56170 0.11946  -0.72141 -0.37149 133 ARG B NE  
2194 C CZ  . ARG B 133 ? 2.52096 1.68244 1.53833 0.13959  -0.73048 -0.36462 133 ARG B CZ  
2195 N NH1 . ARG B 133 ? 2.36879 1.62526 1.48886 0.10650  -0.74499 -0.34828 133 ARG B NH1 
2196 N NH2 . ARG B 133 ? 2.34594 1.46183 1.25451 0.19644  -0.72449 -0.37224 133 ARG B NH2 
2197 N N   . ALA B 134 ? 1.53336 0.97669 0.95390 0.04435  -0.44872 -0.23944 134 ALA B N   
2198 C CA  . ALA B 134 ? 1.64799 1.19106 1.15328 0.04026  -0.40564 -0.20955 134 ALA B CA  
2199 C C   . ALA B 134 ? 1.51436 1.06035 0.97210 0.08682  -0.34883 -0.19733 134 ALA B C   
2200 O O   . ALA B 134 ? 1.51263 0.99535 0.87932 0.12297  -0.33971 -0.20975 134 ALA B O   
2201 C CB  . ALA B 134 ? 1.49706 1.09045 1.10617 -0.00660 -0.38631 -0.19069 134 ALA B CB  
2202 N N   . GLY B 135 ? 1.29263 0.91343 0.81355 0.08656  -0.31149 -0.17197 135 GLY B N   
2203 C CA  . GLY B 135 ? 1.29350 0.92624 0.79245 0.11842  -0.25754 -0.15450 135 GLY B CA  
2204 C C   . GLY B 135 ? 1.19237 0.83520 0.73396 0.10212  -0.22050 -0.14343 135 GLY B C   
2205 O O   . GLY B 135 ? 1.21451 0.87827 0.82106 0.06472  -0.22680 -0.14069 135 GLY B O   
2206 N N   . TYR B 136 ? 1.18907 0.81910 0.69339 0.13130  -0.18176 -0.13512 136 TYR B N   
2207 C CA  . TYR B 136 ? 1.22541 0.86031 0.76213 0.12061  -0.15155 -0.12601 136 TYR B CA  
2208 C C   . TYR B 136 ? 1.14071 0.81460 0.69229 0.13942  -0.10514 -0.10220 136 TYR B C   
2209 O O   . TYR B 136 ? 1.11933 0.79032 0.62431 0.17230  -0.08955 -0.09547 136 TYR B O   
2210 C CB  . TYR B 136 ? 1.27388 0.83902 0.74989 0.13450  -0.16073 -0.14448 136 TYR B CB  
2211 C CG  . TYR B 136 ? 1.35803 0.87570 0.82963 0.10492  -0.20859 -0.16551 136 TYR B CG  
2212 C CD1 . TYR B 136 ? 1.30761 0.83107 0.83837 0.06417  -0.21235 -0.15975 136 TYR B CD1 
2213 C CD2 . TYR B 136 ? 1.42650 0.89122 0.83327 0.11584  -0.25203 -0.18944 136 TYR B CD2 
2214 C CE1 . TYR B 136 ? 1.39445 0.87473 0.92749 0.03109  -0.25622 -0.17394 136 TYR B CE1 
2215 C CE2 . TYR B 136 ? 1.51459 0.93232 0.92204 0.08289  -0.30166 -0.20774 136 TYR B CE2 
2216 C CZ  . TYR B 136 ? 1.48303 0.91046 0.95799 0.03840  -0.30266 -0.19816 136 TYR B CZ  
2217 O OH  . TYR B 136 ? 1.51825 0.89918 0.99966 0.00002  -0.35216 -0.21157 136 TYR B OH  
2218 N N   . PHE B 137 ? 1.06159 0.76968 0.67619 0.11731  -0.08434 -0.08823 137 PHE B N   
2219 C CA  . PHE B 137 ? 1.07273 0.81335 0.70964 0.12728  -0.04659 -0.06637 137 PHE B CA  
2220 C C   . PHE B 137 ? 1.01313 0.74533 0.66425 0.12246  -0.03160 -0.06437 137 PHE B C   
2221 O O   . PHE B 137 ? 1.00240 0.72314 0.67625 0.09781  -0.04460 -0.07159 137 PHE B O   
2222 C CB  . PHE B 137 ? 0.96947 0.75586 0.66464 0.10857  -0.03979 -0.05184 137 PHE B CB  
2223 C CG  . PHE B 137 ? 1.10409 0.90117 0.79323 0.11315  -0.05875 -0.05349 137 PHE B CG  
2224 C CD1 . PHE B 137 ? 1.06178 0.86451 0.77155 0.09475  -0.08999 -0.06691 137 PHE B CD1 
2225 C CD2 . PHE B 137 ? 1.07273 0.87719 0.74000 0.13488  -0.04610 -0.03850 137 PHE B CD2 
2226 C CE1 . PHE B 137 ? 1.04290 0.86132 0.75223 0.10155  -0.11096 -0.06791 137 PHE B CE1 
2227 C CE2 . PHE B 137 ? 1.15804 0.96908 0.81617 0.14242  -0.06601 -0.03890 137 PHE B CE2 
2228 C CZ  . PHE B 137 ? 0.96236 0.78198 0.64203 0.12751  -0.09978 -0.05488 137 PHE B CZ  
2229 N N   . ILE B 138 ? 0.98220 0.72212 0.62074 0.14668  -0.00449 -0.05220 138 ILE B N   
2230 C CA  . ILE B 138 ? 1.11189 0.84966 0.76606 0.14765  0.00857  -0.04836 138 ILE B CA  
2231 C C   . ILE B 138 ? 0.98219 0.76887 0.68195 0.14674  0.03611  -0.02336 138 ILE B C   
2232 O O   . ILE B 138 ? 0.99244 0.80332 0.68976 0.15989  0.05257  -0.00784 138 ILE B O   
2233 C CB  . ILE B 138 ? 1.16366 0.86005 0.75818 0.18262  0.00970  -0.06051 138 ILE B CB  
2234 C CG1 . ILE B 138 ? 1.16473 0.85477 0.77693 0.18435  0.01707  -0.05793 138 ILE B CG1 
2235 C CG2 . ILE B 138 ? 1.04550 0.75909 0.60546 0.22100  0.03457  -0.04939 138 ILE B CG2 
2236 C CD1 . ILE B 138 ? 1.10212 0.72905 0.65207 0.21272  0.00530  -0.07784 138 ILE B CD1 
2237 N N   . PHE B 139 ? 0.91634 0.71414 0.65636 0.12879  0.03825  -0.01821 139 PHE B N   
2238 C CA  . PHE B 139 ? 0.90883 0.74706 0.69585 0.12168  0.05509  0.00294  139 PHE B CA  
2239 C C   . PHE B 139 ? 0.95946 0.80247 0.75545 0.13494  0.06309  0.00778  139 PHE B C   
2240 O O   . PHE B 139 ? 0.92711 0.75892 0.73775 0.12057  0.05277  0.00351  139 PHE B O   
2241 C CB  . PHE B 139 ? 0.89185 0.73851 0.71514 0.09076  0.04583  0.00376  139 PHE B CB  
2242 C CG  . PHE B 139 ? 0.93572 0.78632 0.75859 0.08296  0.03973  0.00203  139 PHE B CG  
2243 C CD1 . PHE B 139 ? 0.98178 0.81635 0.79075 0.07535  0.02256  -0.01405 139 PHE B CD1 
2244 C CD2 . PHE B 139 ? 0.90759 0.77787 0.74711 0.08273  0.04891  0.01825  139 PHE B CD2 
2245 C CE1 . PHE B 139 ? 0.90573 0.75085 0.71980 0.07201  0.01506  -0.01493 139 PHE B CE1 
2246 C CE2 . PHE B 139 ? 0.93039 0.80004 0.76628 0.08048  0.04160  0.01697  139 PHE B CE2 
2247 C CZ  . PHE B 139 ? 1.01550 0.87604 0.83972 0.07738  0.02484  -0.00018 139 PHE B CZ  
2248 N N   . PRO B 140 ? 0.84874 0.71007 0.63479 0.16551  0.08228  0.01806  140 PRO B N   
2249 C CA  . PRO B 140 ? 0.95889 0.83015 0.75643 0.18463  0.08926  0.02261  140 PRO B CA  
2250 C C   . PRO B 140 ? 0.95135 0.87871 0.81537 0.17323  0.09909  0.04736  140 PRO B C   
2251 O O   . PRO B 140 ? 1.22350 1.16394 1.10803 0.18413  0.09836  0.05153  140 PRO B O   
2252 C CB  . PRO B 140 ? 0.91178 0.78022 0.66394 0.22914  0.10772  0.02163  140 PRO B CB  
2253 C CG  . PRO B 140 ? 0.91144 0.79995 0.65662 0.22767  0.12067  0.03336  140 PRO B CG  
2254 C CD  . PRO B 140 ? 0.88045 0.74680 0.63079 0.19093  0.09751  0.02290  140 PRO B CD  
2255 N N   . ASP B 141 ? 0.88792 0.84459 0.78551 0.15151  0.10419  0.06377  141 ASP B N   
2256 C CA  . ASP B 141 ? 0.98381 0.99380 0.94536 0.13960  0.11208  0.09051  141 ASP B CA  
2257 C C   . ASP B 141 ? 0.96930 0.97018 0.95907 0.10094  0.09204  0.09057  141 ASP B C   
2258 O O   . ASP B 141 ? 0.93688 0.95750 0.95745 0.08308  0.09498  0.10888  141 ASP B O   
2259 C CB  . ASP B 141 ? 0.96073 1.01313 0.93399 0.15378  0.14063  0.11674  141 ASP B CB  
2260 C CG  . ASP B 141 ? 1.27231 1.38977 1.32198 0.14231  0.15032  0.14927  141 ASP B CG  
2261 O OD1 . ASP B 141 ? 1.20183 1.33319 1.29008 0.13315  0.13398  0.14824  141 ASP B OD1 
2262 O OD2 . ASP B 141 ? 1.28660 1.44206 1.35867 0.14149  0.17292  0.17794  141 ASP B OD2 
2263 N N   . LEU B 142 ? 0.86480 0.82982 0.83831 0.08897  0.07168  0.07041  142 LEU B N   
2264 C CA  . LEU B 142 ? 0.81160 0.76287 0.80005 0.05999  0.05371  0.06705  142 LEU B CA  
2265 C C   . LEU B 142 ? 0.91753 0.87589 0.93077 0.05325  0.03818  0.06925  142 LEU B C   
2266 O O   . LEU B 142 ? 1.00176 0.94578 0.99629 0.06606  0.03388  0.06012  142 LEU B O   
2267 C CB  . LEU B 142 ? 0.84893 0.75966 0.79875 0.05270  0.04514  0.04546  142 LEU B CB  
2268 C CG  . LEU B 142 ? 0.87926 0.78114 0.80918 0.05353  0.05039  0.04111  142 LEU B CG  
2269 C CD1 . LEU B 142 ? 0.95254 0.82724 0.85655 0.04741  0.04099  0.02149  142 LEU B CD1 
2270 C CD2 . LEU B 142 ? 0.81822 0.72679 0.76926 0.04002  0.04913  0.05299  142 LEU B CD2 
2271 N N   . SER B 143 ? 0.98797 0.96024 1.03800 0.03249  0.02537  0.08049  143 SER B N   
2272 C CA  . SER B 143 ? 0.95117 0.92991 1.02459 0.02457  0.00374  0.08270  143 SER B CA  
2273 C C   . SER B 143 ? 0.95014 0.89476 1.01318 0.00072  -0.01943 0.07339  143 SER B C   
2274 O O   . SER B 143 ? 0.91945 0.85056 0.98082 -0.01192 -0.01882 0.07406  143 SER B O   
2275 C CB  . SER B 143 ? 1.01542 1.05364 1.15391 0.02463  0.00491  0.10863  143 SER B CB  
2276 O OG  . SER B 143 ? 1.12281 1.19666 1.26855 0.05040  0.03422  0.12037  143 SER B OG  
2277 N N   . VAL B 144 ? 0.97733 0.90281 1.02615 -0.00135 -0.04054 0.06441  144 VAL B N   
2278 C CA  . VAL B 144 ? 0.87308 0.75795 0.89527 -0.01644 -0.06327 0.05173  144 VAL B CA  
2279 C C   . VAL B 144 ? 0.96647 0.86364 1.02209 -0.02839 -0.09500 0.06008  144 VAL B C   
2280 O O   . VAL B 144 ? 0.96889 0.89109 1.04313 -0.01823 -0.10235 0.06697  144 VAL B O   
2281 C CB  . VAL B 144 ? 0.98790 0.83353 0.95107 -0.00744 -0.06076 0.03394  144 VAL B CB  
2282 C CG1 . VAL B 144 ? 0.94666 0.75060 0.87291 -0.01616 -0.07822 0.02047  144 VAL B CG1 
2283 C CG2 . VAL B 144 ? 0.93470 0.77783 0.87832 0.00126  -0.03379 0.02844  144 VAL B CG2 
2284 N N   . ARG B 145 ? 1.01690 0.89275 1.07881 -0.04901 -0.11762 0.05877  145 ARG B N   
2285 C CA  . ARG B 145 ? 1.10274 0.99124 1.20456 -0.06620 -0.15463 0.06782  145 ARG B CA  
2286 C C   . ARG B 145 ? 1.11175 0.96224 1.16686 -0.06088 -0.18518 0.05102  145 ARG B C   
2287 O O   . ARG B 145 ? 0.99583 0.87207 1.08403 -0.06352 -0.21214 0.05965  145 ARG B O   
2288 C CB  . ARG B 145 ? 1.26168 1.12806 1.38230 -0.09334 -0.17424 0.07200  145 ARG B CB  
2289 C CG  . ARG B 145 ? 1.46185 1.35675 1.64945 -0.11988 -0.21161 0.08990  145 ARG B CG  
2290 C CD  . ARG B 145 ? 1.60375 1.42901 1.76017 -0.14199 -0.25620 0.07425  145 ARG B CD  
2291 N NE  . ARG B 145 ? 1.64656 1.43313 1.79271 -0.15497 -0.24901 0.07510  145 ARG B NE  
2292 C CZ  . ARG B 145 ? 1.80279 1.51569 1.91302 -0.17028 -0.28449 0.05997  145 ARG B CZ  
2293 N NH1 . ARG B 145 ? 1.89615 1.56128 1.96597 -0.17248 -0.32864 0.03890  145 ARG B NH1 
2294 N NH2 . ARG B 145 ? 1.68274 1.36095 1.78720 -0.17952 -0.27659 0.06435  145 ARG B NH2 
2295 N N   . ASN B 146 ? 1.07414 0.86868 1.05339 -0.05083 -0.18041 0.02937  146 ASN B N   
2296 C CA  . ASN B 146 ? 1.12721 0.87846 1.04926 -0.04435 -0.20792 0.01464  146 ASN B CA  
2297 C C   . ASN B 146 ? 1.18453 0.92237 1.05318 -0.02256 -0.18240 0.00888  146 ASN B C   
2298 O O   . ASN B 146 ? 1.16923 0.91191 1.02840 -0.01573 -0.14662 0.00790  146 ASN B O   
2299 C CB  . ASN B 146 ? 1.34965 1.03711 1.21748 -0.05041 -0.22867 -0.00520 146 ASN B CB  
2300 C CG  . ASN B 146 ? 1.46355 1.14906 1.37881 -0.07614 -0.25483 0.00069  146 ASN B CG  
2301 O OD1 . ASN B 146 ? 1.47511 1.19898 1.45676 -0.09454 -0.27975 0.01761  146 ASN B OD1 
2302 N ND2 . ASN B 146 ? 1.48741 1.12927 1.37202 -0.07763 -0.24957 -0.01103 146 ASN B ND2 
2303 N N   . GLU B 147 ? 1.14633 0.86425 0.97916 -0.01351 -0.20431 0.00641  147 GLU B N   
2304 C CA  . GLU B 147 ? 1.21465 0.91191 0.99289 0.00377  -0.18314 0.00519  147 GLU B CA  
2305 C C   . GLU B 147 ? 1.17331 0.82691 0.88264 0.00812  -0.16461 -0.00917 147 GLU B C   
2306 O O   . GLU B 147 ? 1.30299 0.92641 0.98517 0.00515  -0.17985 -0.02275 147 GLU B O   
2307 C CB  . GLU B 147 ? 1.32220 1.00492 1.07440 0.01422  -0.21342 0.00917  147 GLU B CB  
2308 C CG  . GLU B 147 ? 1.51948 1.15423 1.21462 0.01334  -0.25132 -0.00447 147 GLU B CG  
2309 C CD  . GLU B 147 ? 1.75357 1.38012 1.43150 0.02377  -0.28910 0.00129  147 GLU B CD  
2310 O OE1 . GLU B 147 ? 1.65100 1.26146 1.28693 0.04058  -0.27539 0.00881  147 GLU B OE1 
2311 O OE2 . GLU B 147 ? 1.59492 1.22929 1.30205 0.01410  -0.33532 -0.00042 147 GLU B OE2 
2312 N N   . GLY B 148 ? 1.23706 0.88736 0.91947 0.01598  -0.13204 -0.00533 148 GLY B N   
2313 C CA  . GLY B 148 ? 1.21983 0.84330 0.84556 0.02194  -0.10854 -0.01358 148 GLY B CA  
2314 C C   . GLY B 148 ? 1.19654 0.84242 0.83816 0.01948  -0.07005 -0.00561 148 GLY B C   
2315 O O   . GLY B 148 ? 1.24115 0.91196 0.92595 0.01504  -0.06404 0.00307  148 GLY B O   
2316 N N   . SER B 149 ? 1.20851 0.84488 0.81264 0.02397  -0.04515 -0.00883 149 SER B N   
2317 C CA  . SER B 149 ? 1.22538 0.88676 0.84932 0.01776  -0.01179 -0.00122 149 SER B CA  
2318 C C   . SER B 149 ? 1.28835 0.97648 0.95012 0.01658  -0.00171 -0.01037 149 SER B C   
2319 O O   . SER B 149 ? 1.21405 0.89041 0.85511 0.02645  -0.00412 -0.02227 149 SER B O   
2320 C CB  . SER B 149 ? 1.19709 0.84569 0.76952 0.02223  0.01271  0.00659  149 SER B CB  
2321 O OG  . SER B 149 ? 1.49129 1.15684 1.08609 0.00838  0.03401  0.02177  149 SER B OG  
2322 N N   . TYR B 150 ? 1.14050 0.85774 0.85037 0.00755  0.00729  -0.00569 150 TYR B N   
2323 C CA  . TYR B 150 ? 1.08704 0.82789 0.83162 0.00782  0.01309  -0.01218 150 TYR B CA  
2324 C C   . TYR B 150 ? 1.10566 0.87493 0.87427 0.00131  0.03427  -0.00721 150 TYR B C   
2325 O O   . TYR B 150 ? 1.11207 0.88029 0.87703 -0.00774 0.04171  0.00188  150 TYR B O   
2326 C CB  . TYR B 150 ? 1.02922 0.77886 0.81184 0.00423  -0.00408 -0.01134 150 TYR B CB  
2327 C CG  . TYR B 150 ? 1.10025 0.82990 0.87626 0.00446  -0.03031 -0.01431 150 TYR B CG  
2328 C CD1 . TYR B 150 ? 1.17802 0.89276 0.95120 0.00567  -0.04111 -0.02285 150 TYR B CD1 
2329 C CD2 . TYR B 150 ? 0.99838 0.72189 0.77313 0.00310  -0.04838 -0.00818 150 TYR B CD2 
2330 C CE1 . TYR B 150 ? 1.06898 0.76076 0.83914 0.00048  -0.07163 -0.02548 150 TYR B CE1 
2331 C CE2 . TYR B 150 ? 1.15586 0.86643 0.93281 0.00000  -0.07820 -0.01003 150 TYR B CE2 
2332 C CZ  . TYR B 150 ? 1.08431 0.77808 0.85984 -0.00389 -0.09096 -0.01878 150 TYR B CZ  
2333 O OH  . TYR B 150 ? 1.26171 0.93787 1.04186 -0.01213 -0.12684 -0.02058 150 TYR B OH  
2334 N N   . ARG B 151 ? 1.03493 0.82585 0.82870 0.00498  0.03960  -0.01271 151 ARG B N   
2335 C CA  . ARG B 151 ? 0.94569 0.76770 0.76996 -0.00088 0.05148  -0.01001 151 ARG B CA  
2336 C C   . ARG B 151 ? 0.98352 0.81545 0.83424 0.00307  0.04267  -0.01393 151 ARG B C   
2337 O O   . ARG B 151 ? 1.14456 0.96386 0.99235 0.01024  0.03353  -0.01750 151 ARG B O   
2338 C CB  . ARG B 151 ? 1.08120 0.92839 0.90623 0.00488  0.07100  -0.00995 151 ARG B CB  
2339 C CG  . ARG B 151 ? 1.05726 0.92229 0.88898 -0.01033 0.08616  0.00262  151 ARG B CG  
2340 C CD  . ARG B 151 ? 0.99006 0.89764 0.83744 -0.00297 0.10875  0.00614  151 ARG B CD  
2341 N NE  . ARG B 151 ? 0.97914 0.89167 0.80477 -0.00737 0.13054  0.02018  151 ARG B NE  
2342 C CZ  . ARG B 151 ? 1.10799 1.04822 0.96120 -0.03012 0.14309  0.03802  151 ARG B CZ  
2343 N NH1 . ARG B 151 ? 1.01135 0.97284 0.91268 -0.05031 0.13129  0.04015  151 ARG B NH1 
2344 N NH2 . ARG B 151 ? 1.09079 1.03404 0.91977 -0.03372 0.16643  0.05524  151 ARG B NH2 
2345 N N   . PHE B 152 ? 0.84554 0.69542 0.71827 -0.00255 0.04353  -0.01219 152 PHE B N   
2346 C CA  . PHE B 152 ? 0.78218 0.64120 0.67159 0.00387  0.03753  -0.01389 152 PHE B CA  
2347 C C   . PHE B 152 ? 0.93357 0.82037 0.84062 0.00806  0.04217  -0.01685 152 PHE B C   
2348 O O   . PHE B 152 ? 0.92878 0.83598 0.84830 -0.00084 0.04737  -0.01553 152 PHE B O   
2349 C CB  . PHE B 152 ? 0.91706 0.77068 0.80809 0.00139  0.03139  -0.01170 152 PHE B CB  
2350 C CG  . PHE B 152 ? 0.94584 0.78814 0.83435 0.00670  0.02695  -0.00649 152 PHE B CG  
2351 C CD1 . PHE B 152 ? 0.87608 0.72050 0.77383 0.01071  0.02456  -0.00230 152 PHE B CD1 
2352 C CD2 . PHE B 152 ? 1.01428 0.84481 0.89478 0.00780  0.02413  -0.00402 152 PHE B CD2 
2353 C CE1 . PHE B 152 ? 0.85876 0.70386 0.76714 0.01143  0.02022  0.00680  152 PHE B CE1 
2354 C CE2 . PHE B 152 ? 0.98060 0.81392 0.86917 0.01517  0.02138  0.00329  152 PHE B CE2 
2355 C CZ  . PHE B 152 ? 1.01141 0.85727 0.91872 0.01488  0.01985  0.00999  152 PHE B CZ  
2356 N N   . SER B 153 ? 0.82684 0.71528 0.73785 0.02100  0.03917  -0.01862 153 SER B N   
2357 C CA  . SER B 153 ? 0.70768 0.62304 0.63666 0.03033  0.03921  -0.02073 153 SER B CA  
2358 C C   . SER B 153 ? 0.76616 0.67784 0.69554 0.03451  0.02875  -0.01823 153 SER B C   
2359 O O   . SER B 153 ? 0.75524 0.64495 0.67295 0.03780  0.02661  -0.01296 153 SER B O   
2360 C CB  . SER B 153 ? 0.84600 0.75852 0.76944 0.04888  0.04384  -0.02460 153 SER B CB  
2361 O OG  . SER B 153 ? 0.99648 0.94408 0.94257 0.06157  0.04520  -0.02589 153 SER B OG  
2362 N N   . PHE B 154 ? 0.73090 0.66379 0.67249 0.03239  0.02148  -0.02035 154 PHE B N   
2363 C CA  . PHE B 154 ? 0.78907 0.71557 0.71931 0.04012  0.01055  -0.01929 154 PHE B CA  
2364 C C   . PHE B 154 ? 0.77335 0.72200 0.71612 0.05444  0.00204  -0.02012 154 PHE B C   
2365 O O   . PHE B 154 ? 0.83969 0.82155 0.80900 0.05039  -0.00427 -0.02420 154 PHE B O   
2366 C CB  . PHE B 154 ? 0.76439 0.68439 0.68568 0.02944  0.00105  -0.02421 154 PHE B CB  
2367 C CG  . PHE B 154 ? 0.82129 0.71740 0.72852 0.02076  0.00787  -0.02310 154 PHE B CG  
2368 C CD1 . PHE B 154 ? 0.83393 0.71215 0.72251 0.03067  0.01359  -0.01745 154 PHE B CD1 
2369 C CD2 . PHE B 154 ? 0.83831 0.73301 0.75342 0.00367  0.00920  -0.02464 154 PHE B CD2 
2370 C CE1 . PHE B 154 ? 0.77136 0.63362 0.65182 0.02708  0.01803  -0.01584 154 PHE B CE1 
2371 C CE2 . PHE B 154 ? 0.75101 0.61967 0.64948 -0.00064 0.01279  -0.02283 154 PHE B CE2 
2372 C CZ  . PHE B 154 ? 0.80745 0.66133 0.68984 0.01276  0.01599  -0.01966 154 PHE B CZ  
2373 N N   . HIS B 155 ? 0.76862 0.70055 0.69542 0.07049  0.00087  -0.01370 155 HIS B N   
2374 C CA  . HIS B 155 ? 0.72876 0.67320 0.66087 0.08964  -0.00852 -0.01255 155 HIS B CA  
2375 C C   . HIS B 155 ? 0.75114 0.68800 0.65934 0.09829  -0.02247 -0.00918 155 HIS B C   
2376 O O   . HIS B 155 ? 0.84918 0.75901 0.72788 0.09922  -0.01667 -0.00076 155 HIS B O   
2377 C CB  . HIS B 155 ? 0.85427 0.77188 0.77614 0.10338  -0.00247 -0.00618 155 HIS B CB  
2378 C CG  . HIS B 155 ? 0.86710 0.77117 0.79117 0.09532  0.00924  -0.00999 155 HIS B CG  
2379 N ND1 . HIS B 155 ? 0.83651 0.75851 0.77404 0.10392  0.01571  -0.01852 155 HIS B ND1 
2380 C CD2 . HIS B 155 ? 0.88610 0.76316 0.79890 0.08109  0.01457  -0.00641 155 HIS B CD2 
2381 C CE1 . HIS B 155 ? 0.79776 0.69531 0.72181 0.09678  0.02338  -0.02152 155 HIS B CE1 
2382 N NE2 . HIS B 155 ? 0.90274 0.77365 0.81488 0.08126  0.02015  -0.01456 155 HIS B NE2 
2383 N N   . LEU B 156 ? 0.76260 0.72625 0.68322 0.10634  -0.04092 -0.01453 156 LEU B N   
2384 C CA  . LEU B 156 ? 0.81484 0.76853 0.70422 0.11685  -0.05988 -0.01442 156 LEU B CA  
2385 C C   . LEU B 156 ? 0.92486 0.86805 0.79644 0.14291  -0.06604 -0.00365 156 LEU B C   
2386 O O   . LEU B 156 ? 0.90878 0.87414 0.80853 0.15541  -0.07093 -0.00399 156 LEU B O   
2387 C CB  . LEU B 156 ? 0.85197 0.83723 0.76440 0.10719  -0.08515 -0.02710 156 LEU B CB  
2388 C CG  . LEU B 156 ? 0.91518 0.88451 0.78705 0.11933  -0.11274 -0.03162 156 LEU B CG  
2389 C CD1 . LEU B 156 ? 0.90470 0.82807 0.71959 0.11968  -0.10441 -0.03282 156 LEU B CD1 
2390 C CD2 . LEU B 156 ? 0.85903 0.86292 0.76547 0.10560  -0.14569 -0.04418 156 LEU B CD2 
2391 N N   . PHE B 157 ? 0.91681 0.82573 0.73955 0.15372  -0.06403 0.00769  157 PHE B N   
2392 C CA  . PHE B 157 ? 0.89986 0.78855 0.69351 0.17797  -0.07050 0.02245  157 PHE B CA  
2393 C C   . PHE B 157 ? 1.05213 0.93541 0.80215 0.19305  -0.09259 0.02022  157 PHE B C   
2394 O O   . PHE B 157 ? 0.97095 0.84094 0.68783 0.18822  -0.08981 0.01583  157 PHE B O   
2395 C CB  . PHE B 157 ? 0.98339 0.83371 0.75330 0.17642  -0.04687 0.04427  157 PHE B CB  
2396 C CG  . PHE B 157 ? 0.97883 0.82355 0.78268 0.16326  -0.03331 0.04473  157 PHE B CG  
2397 C CD1 . PHE B 157 ? 0.99329 0.83803 0.81635 0.17607  -0.04111 0.04054  157 PHE B CD1 
2398 C CD2 . PHE B 157 ? 0.94864 0.78680 0.76166 0.14186  -0.01500 0.04794  157 PHE B CD2 
2399 C CE1 . PHE B 157 ? 1.07261 0.90320 0.91420 0.16820  -0.03123 0.03732  157 PHE B CE1 
2400 C CE2 . PHE B 157 ? 0.97624 0.80361 0.81305 0.13055  -0.00845 0.04599  157 PHE B CE2 
2401 C CZ  . PHE B 157 ? 0.89228 0.71190 0.73863 0.14397  -0.01675 0.03957  157 PHE B CZ  
2402 N N   . GLU B 158 ? 0.97791 0.86874 0.72360 0.21469  -0.11637 0.02181  158 GLU B N   
2403 C CA  . GLU B 158 ? 1.03395 0.91624 0.73220 0.23278  -0.14450 0.01900  158 GLU B CA  
2404 C C   . GLU B 158 ? 1.22076 1.06403 0.86457 0.25961  -0.14045 0.04352  158 GLU B C   
2405 O O   . GLU B 158 ? 1.26876 1.10982 0.93066 0.27278  -0.14228 0.05404  158 GLU B O   
2406 C CB  . GLU B 158 ? 1.03253 0.96076 0.77361 0.23583  -0.18209 0.00265  158 GLU B CB  
2407 C CG  . GLU B 158 ? 1.16158 1.07869 0.85284 0.25651  -0.21983 -0.00117 158 GLU B CG  
2408 C CD  . GLU B 158 ? 1.28762 1.25964 1.03499 0.25467  -0.26141 -0.01612 158 GLU B CD  
2409 O OE1 . GLU B 158 ? 1.20385 1.22664 1.03007 0.23274  -0.25670 -0.02379 158 GLU B OE1 
2410 O OE2 . GLU B 158 ? 1.41108 1.37821 1.12420 0.27641  -0.29877 -0.01755 158 GLU B OE2 
2411 N N   . GLN B 159 ? 1.30140 1.11070 0.87512 0.26969  -0.13319 0.05399  159 GLN B N   
2412 C CA  . GLN B 159 ? 1.48981 1.25992 1.00196 0.29467  -0.12767 0.08207  159 GLN B CA  
2413 C C   . GLN B 159 ? 1.53907 1.30375 0.99809 0.32113  -0.16679 0.07258  159 GLN B C   
2414 O O   . GLN B 159 ? 1.72532 1.48128 1.13841 0.32408  -0.17520 0.05879  159 GLN B O   
2415 C CB  . GLN B 159 ? 1.62353 1.36617 1.09102 0.29106  -0.08913 0.10476  159 GLN B CB  
2416 C CG  . GLN B 159 ? 1.90697 1.61153 1.29092 0.31958  -0.08517 0.13275  159 GLN B CG  
2417 C CD  . GLN B 159 ? 2.04407 1.73275 1.41146 0.31115  -0.03950 0.16670  159 GLN B CD  
2418 O OE1 . GLN B 159 ? 1.99517 1.70443 1.39453 0.29074  -0.01481 0.16152  159 GLN B OE1 
2419 N NE2 . GLN B 159 ? 2.24319 1.89792 1.56973 0.32414  -0.02827 0.20433  159 GLN B NE2 
2420 N N   . ILE B 160 ? 1.72493 1.49220 1.18795 0.34268  -0.19458 0.07769  160 ILE B N   
2421 C CA  . ILE B 160 ? 1.98940 1.76304 1.41949 0.36566  -0.24269 0.06422  160 ILE B CA  
2422 C C   . ILE B 160 ? 2.09345 1.81284 1.41611 0.39680  -0.24291 0.08665  160 ILE B C   
2423 O O   . ILE B 160 ? 2.03158 1.71618 1.32476 0.40744  -0.21645 0.11947  160 ILE B O   
2424 C CB  . ILE B 160 ? 2.00571 1.81850 1.49792 0.37820  -0.27491 0.05910  160 ILE B CB  
2425 C CG1 . ILE B 160 ? 2.03804 1.89482 1.55484 0.37816  -0.32718 0.03189  160 ILE B CG1 
2426 C CG2 . ILE B 160 ? 2.04877 1.82498 1.49805 0.41358  -0.28090 0.08636  160 ILE B CG2 
2427 C CD1 . ILE B 160 ? 1.87889 1.80104 1.48939 0.38199  -0.35003 0.02508  160 ILE B CD1 
2428 N N   . LYS B 161 ? 2.73541 2.03890 1.26747 0.51849  -0.54686 -0.30404 161 LYS B N   
2429 C CA  . LYS B 161 ? 3.00907 2.38531 1.45762 0.59440  -0.54368 -0.29734 161 LYS B CA  
2430 C C   . LYS B 161 ? 3.34520 2.76299 1.78079 0.60721  -0.58995 -0.29166 161 LYS B C   
2431 O O   . LYS B 161 ? 3.37111 2.86299 1.74843 0.66484  -0.57653 -0.26612 161 LYS B O   
2432 C CB  . LYS B 161 ? 2.92181 2.27456 1.26594 0.64919  -0.58158 -0.36310 161 LYS B CB  
2433 C CG  . LYS B 161 ? 2.80929 2.13598 1.15199 0.65560  -0.53880 -0.37312 161 LYS B CG  
2434 C CD  . LYS B 161 ? 2.96285 2.28833 1.20193 0.72279  -0.57067 -0.43554 161 LYS B CD  
2435 C CE  . LYS B 161 ? 2.92361 2.15638 1.16601 0.70607  -0.60683 -0.49210 161 LYS B CE  
2436 N NZ  . LYS B 161 ? 3.00381 2.24920 1.22035 0.75356  -0.62899 -0.54304 161 LYS B NZ  
2437 N N   . ASP B 162 ? 3.95516 3.33064 2.44153 0.55595  -0.64436 -0.31487 162 ASP B N   
2438 C CA  . ASP B 162 ? 4.08831 3.50609 2.57146 0.56615  -0.69459 -0.31607 162 ASP B CA  
2439 C C   . ASP B 162 ? 4.10367 3.54148 2.70654 0.51013  -0.66611 -0.26276 162 ASP B C   
2440 O O   . ASP B 162 ? 4.04145 3.42194 2.72397 0.43945  -0.67137 -0.27495 162 ASP B O   
2441 C CB  . ASP B 162 ? 4.11280 3.47295 2.56179 0.55539  -0.78680 -0.39640 162 ASP B CB  
2442 C CG  . ASP B 162 ? 4.18949 3.58405 2.66980 0.54311  -0.84061 -0.40223 162 ASP B CG  
2443 O OD1 . ASP B 162 ? 4.28738 3.76741 2.74766 0.58622  -0.83092 -0.36256 162 ASP B OD1 
2444 O OD2 . ASP B 162 ? 4.06903 3.40570 2.59413 0.49089  -0.89355 -0.44627 162 ASP B OD2 
2445 N N   . PRO B 163 ? 3.62535 3.14309 2.24594 0.53907  -0.63416 -0.20262 163 PRO B N   
2446 C CA  . PRO B 163 ? 3.37535 2.91432 2.12269 0.48894  -0.59444 -0.14854 163 PRO B CA  
2447 C C   . PRO B 163 ? 3.25283 2.76618 2.07522 0.43060  -0.65106 -0.18004 163 PRO B C   
2448 O O   . PRO B 163 ? 3.01745 2.51835 1.95274 0.36723  -0.61745 -0.15800 163 PRO B O   
2449 C CB  . PRO B 163 ? 3.25074 2.87831 1.98173 0.54670  -0.56646 -0.08387 163 PRO B CB  
2450 C CG  . PRO B 163 ? 3.38851 3.03965 1.98592 0.62008  -0.56435 -0.09317 163 PRO B CG  
2451 C CD  . PRO B 163 ? 3.58845 3.18078 2.11372 0.61964  -0.63202 -0.17998 163 PRO B CD  
2452 N N   . LYS B 164 ? 3.35332 2.86316 2.12133 0.44821  -0.73408 -0.23394 164 LYS B N   
2453 C CA  . LYS B 164 ? 3.18755 2.68100 2.03553 0.39165  -0.78594 -0.26405 164 LYS B CA  
2454 C C   . LYS B 164 ? 2.99132 2.39135 1.88275 0.31605  -0.79479 -0.30623 164 LYS B C   
2455 O O   . LYS B 164 ? 2.76590 2.15019 1.74462 0.25383  -0.81780 -0.32140 164 LYS B O   
2456 C CB  . LYS B 164 ? 3.26032 2.78303 2.04318 0.43186  -0.87343 -0.31312 164 LYS B CB  
2457 C CG  . LYS B 164 ? 3.48199 2.97334 2.13585 0.47999  -0.91560 -0.37236 164 LYS B CG  
2458 C CD  . LYS B 164 ? 3.42970 2.91512 2.05585 0.48241  -1.01132 -0.44719 164 LYS B CD  
2459 C CE  . LYS B 164 ? 3.52214 2.96263 2.03544 0.52110  -1.05271 -0.51668 164 LYS B CE  
2460 N NZ  . LYS B 164 ? 3.46647 2.87882 2.00164 0.49549  -1.12574 -0.59144 164 LYS B NZ  
2461 N N   . ASP B 165 ? 3.02789 2.36787 1.86215 0.31986  -0.77696 -0.32396 165 ASP B N   
2462 C CA  . ASP B 165 ? 2.87634 2.12618 1.74831 0.24972  -0.77887 -0.35162 165 ASP B CA  
2463 C C   . ASP B 165 ? 2.66160 1.91475 1.64079 0.18663  -0.70794 -0.30301 165 ASP B C   
2464 O O   . ASP B 165 ? 2.49715 1.68400 1.51616 0.11979  -0.70761 -0.31973 165 ASP B O   
2465 C CB  . ASP B 165 ? 2.91808 2.10744 1.69897 0.27960  -0.78222 -0.38227 165 ASP B CB  
2466 C CG  . ASP B 165 ? 3.01887 2.18839 1.70356 0.32918  -0.85882 -0.44697 165 ASP B CG  
2467 O OD1 . ASP B 165 ? 2.94068 2.11457 1.64000 0.31647  -0.91971 -0.48090 165 ASP B OD1 
2468 O OD2 . ASP B 165 ? 3.01074 2.16436 1.60993 0.38085  -0.85797 -0.46818 165 ASP B OD2 
2469 N N   . ALA B 166 ? 2.66175 1.98945 1.68757 0.20597  -0.64799 -0.24408 166 ALA B N   
2470 C CA  . ALA B 166 ? 2.44406 1.78280 1.57554 0.15097  -0.57579 -0.20166 166 ALA B CA  
2471 C C   . ALA B 166 ? 2.34299 1.67303 1.57976 0.07361  -0.59314 -0.21403 166 ALA B C   
2472 O O   . ALA B 166 ? 2.35816 1.70113 1.60549 0.07219  -0.65202 -0.23981 166 ALA B O   
2473 C CB  . ALA B 166 ? 2.44881 1.86899 1.61352 0.19300  -0.51257 -0.13787 166 ALA B CB  
2474 N N   . THR B 167 ? 2.42283 1.73698 1.74035 0.00804  -0.53929 -0.19783 167 THR B N   
2475 C CA  . THR B 167 ? 2.37827 1.68563 1.79965 -0.07376 -0.54336 -0.20993 167 THR B CA  
2476 C C   . THR B 167 ? 2.35055 1.73839 1.86486 -0.06813 -0.53900 -0.18637 167 THR B C   
2477 O O   . THR B 167 ? 2.30771 1.74587 1.91135 -0.07985 -0.47499 -0.14539 167 THR B O   
2478 C CB  . THR B 167 ? 2.23829 1.52634 1.72352 -0.14053 -0.47692 -0.19414 167 THR B CB  
2479 O OG1 . THR B 167 ? 2.12358 1.34375 1.52206 -0.13641 -0.47911 -0.20924 167 THR B OG1 
2480 C CG2 . THR B 167 ? 2.10538 1.37811 1.68045 -0.22999 -0.48572 -0.21516 167 THR B CG2 
2481 N N   . PRO B 184 ? 3.06399 2.86080 2.30646 0.47576  0.38887  0.20795  184 PRO B N   
2482 C CA  . PRO B 184 ? 3.04615 2.79552 2.32543 0.42371  0.32940  0.18107  184 PRO B CA  
2483 C C   . PRO B 184 ? 3.12620 2.85749 2.33344 0.44697  0.25255  0.18548  184 PRO B C   
2484 O O   . PRO B 184 ? 3.24944 2.95318 2.50500 0.40405  0.21343  0.17764  184 PRO B O   
2485 C CB  . PRO B 184 ? 2.88384 2.65273 2.31534 0.37065  0.39378  0.21859  184 PRO B CB  
2486 C CG  . PRO B 184 ? 2.73132 2.54037 2.21123 0.37719  0.48067  0.23238  184 PRO B CG  
2487 C CD  . PRO B 184 ? 3.05651 2.89177 2.42282 0.45087  0.48465  0.25159  184 PRO B CD  
2488 N N   . GLN B 185 ? 2.92302 2.67520 2.01697 0.51344  0.23175  0.19481  185 GLN B N   
2489 C CA  . GLN B 185 ? 2.83760 2.57978 1.85806 0.53876  0.15470  0.19247  185 GLN B CA  
2490 C C   . GLN B 185 ? 2.78166 2.46413 1.74651 0.52089  0.06749  0.12004  185 GLN B C   
2491 O O   . GLN B 185 ? 2.72543 2.39003 1.66757 0.51752  0.00057  0.10903  185 GLN B O   
2492 C CB  . GLN B 185 ? 2.78792 2.57505 1.69528 0.61487  0.15716  0.21855  185 GLN B CB  
2493 C CG  . GLN B 185 ? 2.76874 2.61037 1.72498 0.63413  0.24148  0.30008  185 GLN B CG  
2494 C CD  . GLN B 185 ? 2.81829 2.70672 1.65985 0.70390  0.26539  0.32072  185 GLN B CD  
2495 O OE1 . GLN B 185 ? 2.81534 2.69964 1.54422 0.73886  0.22184  0.26732  185 GLN B OE1 
2496 N NE2 . GLN B 185 ? 2.84735 2.78057 1.71928 0.72385  0.33695  0.39831  185 GLN B NE2 
2497 N N   . GLU B 186 ? 2.66671 2.31810 1.61193 0.51058  0.06586  0.07111  186 GLU B N   
2498 C CA  . GLU B 186 ? 2.46015 2.04504 1.36327 0.48904  -0.01165 0.00645  186 GLU B CA  
2499 C C   . GLU B 186 ? 2.29942 1.84953 1.30900 0.41063  0.00027  0.00013  186 GLU B C   
2500 O O   . GLU B 186 ? 2.27202 1.84955 1.36917 0.38297  0.07212  0.02591  186 GLU B O   
2501 C CB  . GLU B 186 ? 2.44862 2.01773 1.26458 0.52892  -0.02598 -0.04322 186 GLU B CB  
2502 C CG  . GLU B 186 ? 2.66491 2.21678 1.35714 0.58179  -0.10228 -0.08604 186 GLU B CG  
2503 C CD  . GLU B 186 ? 2.60684 2.09377 1.28770 0.54960  -0.18996 -0.12435 186 GLU B CD  
2504 O OE1 . GLU B 186 ? 2.49059 1.94407 1.25523 0.48398  -0.19377 -0.11704 186 GLU B OE1 
2505 O OE2 . GLU B 186 ? 2.57307 2.04426 1.16098 0.58952  -0.25455 -0.16570 186 GLU B OE2 
2506 N N   . PHE B 187 ? 2.13663 1.62856 1.13956 0.37294  -0.06840 -0.03599 187 PHE B N   
2507 C CA  . PHE B 187 ? 2.05421 1.51650 1.15091 0.29538  -0.05878 -0.04085 187 PHE B CA  
2508 C C   . PHE B 187 ? 2.08208 1.46764 1.13038 0.27013  -0.12312 -0.09590 187 PHE B C   
2509 O O   . PHE B 187 ? 2.16648 1.51412 1.12431 0.30355  -0.19038 -0.13098 187 PHE B O   
2510 C CB  . PHE B 187 ? 2.02422 1.49892 1.19679 0.25683  -0.06649 -0.01422 187 PHE B CB  
2511 C CG  . PHE B 187 ? 2.10358 1.59685 1.40573 0.19128  -0.00614 0.00787  187 PHE B CG  
2512 C CD1 . PHE B 187 ? 1.86987 1.34970 1.20534 0.15372  0.02804  -0.00982 187 PHE B CD1 
2513 C CD2 . PHE B 187 ? 2.02673 1.55536 1.42011 0.16906  0.01543  0.04363  187 PHE B CD2 
2514 C CE1 . PHE B 187 ? 1.77370 1.27715 1.22726 0.09295  0.08358  0.00432  187 PHE B CE1 
2515 C CE2 . PHE B 187 ? 2.09400 1.64306 1.61211 0.10927  0.07228  0.05753  187 PHE B CE2 
2516 C CZ  . PHE B 187 ? 1.98666 1.52445 1.53321 0.07011  0.10728  0.03625  187 PHE B CZ  
2517 N N   . LEU B 188 ? 1.27851 0.83955 1.16879 0.09332  -0.03556 0.01691  188 LEU B N   
2518 C CA  . LEU B 188 ? 1.26150 0.85604 1.14583 0.10020  -0.02381 0.00995  188 LEU B CA  
2519 C C   . LEU B 188 ? 1.24449 0.87229 1.16692 0.11017  -0.03225 0.00061  188 LEU B C   
2520 O O   . LEU B 188 ? 1.32532 0.96995 1.28563 0.11883  -0.03496 -0.01412 188 LEU B O   
2521 C CB  . LEU B 188 ? 1.20656 0.82889 1.09801 0.10279  -0.00438 -0.00219 188 LEU B CB  
2522 C CG  . LEU B 188 ? 1.30981 0.93018 1.16405 0.10097  0.01291  0.00508  188 LEU B CG  
2523 C CD1 . LEU B 188 ? 1.34109 1.00039 1.21725 0.10551  0.02592  -0.00920 188 LEU B CD1 
2524 C CD2 . LEU B 188 ? 1.27510 0.88260 1.09305 0.10225  0.00726  0.01379  188 LEU B CD2 
2525 N N   . GLU B 189 ? 1.16753 0.80431 1.07990 0.11001  -0.03669 0.01023  189 GLU B N   
2526 C CA  . GLU B 189 ? 1.08602 0.76263 1.03765 0.11891  -0.04100 0.00804  189 GLU B CA  
2527 C C   . GLU B 189 ? 1.12419 0.84012 1.07014 0.12210  -0.02726 0.00448  189 GLU B C   
2528 O O   . GLU B 189 ? 0.99753 0.69882 0.90787 0.11405  -0.02871 0.01551  189 GLU B O   
2529 C CB  . GLU B 189 ? 1.21860 0.87722 1.17883 0.11322  -0.06428 0.02921  189 GLU B CB  
2530 C CG  . GLU B 189 ? 1.47231 1.08575 1.43369 0.10796  -0.08255 0.03585  189 GLU B CG  
2531 C CD  . GLU B 189 ? 1.64962 1.26866 1.65372 0.10980  -0.10478 0.04928  189 GLU B CD  
2532 O OE1 . GLU B 189 ? 1.69705 1.36911 1.74573 0.12096  -0.09820 0.04724  189 GLU B OE1 
2533 O OE2 . GLU B 189 ? 1.81661 1.38882 1.81131 0.10045  -0.12843 0.06354  189 GLU B OE2 
2534 N N   . PHE B 190 ? 1.01307 0.77446 0.98950 0.13499  -0.01531 -0.01137 190 PHE B N   
2535 C CA  . PHE B 190 ? 0.95071 0.75296 0.92456 0.13775  -0.00393 -0.01210 190 PHE B CA  
2536 C C   . PHE B 190 ? 0.94126 0.76490 0.93414 0.13461  -0.01383 0.01028  190 PHE B C   
2537 O O   . PHE B 190 ? 0.88671 0.71814 0.91553 0.13945  -0.02241 0.01792  190 PHE B O   
2538 C CB  . PHE B 190 ? 0.81549 0.65466 0.80810 0.15396  0.01136  -0.03573 190 PHE B CB  
2539 C CG  . PHE B 190 ? 0.86280 0.74719 0.85328 0.15783  0.02332  -0.03479 190 PHE B CG  
2540 C CD1 . PHE B 190 ? 0.78071 0.66435 0.74079 0.14926  0.02760  -0.03503 190 PHE B CD1 
2541 C CD2 . PHE B 190 ? 0.73839 0.66787 0.75886 0.17064  0.03097  -0.03160 190 PHE B CD2 
2542 C CE1 . PHE B 190 ? 0.83138 0.75399 0.78748 0.15084  0.03595  -0.03220 190 PHE B CE1 
2543 C CE2 . PHE B 190 ? 0.72766 0.70068 0.74376 0.17293  0.04341  -0.02714 190 PHE B CE2 
2544 C CZ  . PHE B 190 ? 0.78393 0.75122 0.76595 0.16165  0.04419  -0.02740 190 PHE B CZ  
2545 N N   . ARG B 191 ? 0.81303 0.64714 0.78664 0.12604  -0.01494 0.02284  191 ARG B N   
2546 C CA  . ARG B 191 ? 0.83488 0.68937 0.82914 0.11897  -0.02852 0.04928  191 ARG B CA  
2547 C C   . ARG B 191 ? 0.81916 0.73489 0.83206 0.12391  -0.01322 0.05174  191 ARG B C   
2548 O O   . ARG B 191 ? 0.88595 0.84813 0.94366 0.13151  -0.00777 0.06195  191 ARG B O   
2549 C CB  . ARG B 191 ? 0.96085 0.76618 0.91375 0.10221  -0.05142 0.06803  191 ARG B CB  
2550 C CG  . ARG B 191 ? 1.06505 0.80761 0.99377 0.09684  -0.06895 0.07189  191 ARG B CG  
2551 C CD  . ARG B 191 ? 0.99492 0.73861 0.96500 0.09374  -0.08977 0.09089  191 ARG B CD  
2552 N NE  . ARG B 191 ? 1.21878 0.90049 1.16386 0.08871  -0.10724 0.09343  191 ARG B NE  
2553 C CZ  . ARG B 191 ? 1.21671 0.89574 1.19537 0.09342  -0.11205 0.09143  191 ARG B CZ  
2554 N NH1 . ARG B 191 ? 1.23051 0.96473 1.27021 0.10657  -0.09986 0.08495  191 ARG B NH1 
2555 N NH2 . ARG B 191 ? 1.32382 0.94110 1.27103 0.08624  -0.12981 0.09617  191 ARG B NH2 
2556 N N   . LEU B 192 ? 0.82507 0.74382 0.80563 0.12060  -0.00525 0.04414  192 LEU B N   
2557 C CA  . LEU B 192 ? 0.71484 0.68742 0.70549 0.12278  0.00726  0.04912  192 LEU B CA  
2558 C C   . LEU B 192 ? 0.77826 0.74127 0.72931 0.12083  0.01438  0.03325  192 LEU B C   
2559 O O   . LEU B 192 ? 0.81579 0.73396 0.73649 0.11655  0.00854  0.02435  192 LEU B O   
2560 C CB  . LEU B 192 ? 0.76531 0.75658 0.77423 0.10811  -0.01005 0.08501  192 LEU B CB  
2561 C CG  . LEU B 192 ? 0.79963 0.75349 0.76985 0.09027  -0.03235 0.09905  192 LEU B CG  
2562 C CD1 . LEU B 192 ? 0.78513 0.76950 0.77996 0.07556  -0.04922 0.13520  192 LEU B CD1 
2563 C CD2 . LEU B 192 ? 0.74885 0.63225 0.68928 0.08474  -0.05319 0.09840  192 LEU B CD2 
2564 N N   . GLU B 193 ? 0.75620 0.76360 0.70879 0.12452  0.02747  0.03204  193 GLU B N   
2565 C CA  . GLU B 193 ? 0.83579 0.83925 0.75579 0.12217  0.03153  0.01933  193 GLU B CA  
2566 C C   . GLU B 193 ? 0.88580 0.91704 0.80147 0.11012  0.02495  0.04295  193 GLU B C   
2567 O O   . GLU B 193 ? 0.82452 0.89408 0.76784 0.10714  0.02530  0.06642  193 GLU B O   
2568 C CB  . GLU B 193 ? 0.70844 0.73003 0.62393 0.13820  0.05037  -0.00903 193 GLU B CB  
2569 C CG  . GLU B 193 ? 0.82469 0.90053 0.74685 0.14710  0.06607  -0.00518 193 GLU B CG  
2570 C CD  . GLU B 193 ? 1.16322 1.24957 1.08310 0.16996  0.08315  -0.03408 193 GLU B CD  
2571 O OE1 . GLU B 193 ? 1.29216 1.34631 1.21708 0.17754  0.07975  -0.05345 193 GLU B OE1 
2572 O OE2 . GLU B 193 ? 1.27849 1.40230 1.18782 0.18078  0.09870  -0.03683 193 GLU B OE2 
2573 N N   . VAL B 194 ? 0.70708 0.71967 0.59202 0.10259  0.01760  0.03921  194 VAL B N   
2574 C CA  . VAL B 194 ? 0.83123 0.86593 0.70759 0.09049  0.00896  0.05917  194 VAL B CA  
2575 C C   . VAL B 194 ? 0.72749 0.76691 0.57896 0.09449  0.01728  0.03917  194 VAL B C   
2576 O O   . VAL B 194 ? 0.78665 0.79337 0.62305 0.09888  0.01695  0.01817  194 VAL B O   
2577 C CB  . VAL B 194 ? 0.93310 0.92883 0.79530 0.07462  -0.02001 0.08058  194 VAL B CB  
2578 C CG1 . VAL B 194 ? 0.85682 0.79917 0.68606 0.07798  -0.02600 0.06154  194 VAL B CG1 
2579 C CG2 . VAL B 194 ? 0.91086 0.93241 0.77170 0.05981  -0.03324 0.10644  194 VAL B CG2 
2580 N N   . ILE B 195 ? 0.73951 0.82066 0.58807 0.09228  0.02405  0.04841  195 ILE B N   
2581 C CA  . ILE B 195 ? 0.73001 0.81767 0.55260 0.09632  0.03050  0.03050  195 ILE B CA  
2582 C C   . ILE B 195 ? 0.99816 1.07991 0.80295 0.07937  0.01069  0.04839  195 ILE B C   
2583 O O   . ILE B 195 ? 0.83347 0.93750 0.64643 0.06637  0.00169  0.07880  195 ILE B O   
2584 C CB  . ILE B 195 ? 0.79932 0.93308 0.62026 0.10946  0.05369  0.02511  195 ILE B CB  
2585 C CG1 . ILE B 195 ? 0.83879 0.96506 0.67050 0.13001  0.06904  -0.00160 195 ILE B CG1 
2586 C CG2 . ILE B 195 ? 0.77431 0.91219 0.55921 0.10894  0.05366  0.01444  195 ILE B CG2 
2587 C CD1 . ILE B 195 ? 0.86030 1.03293 0.70861 0.14618  0.09198  0.00304  195 ILE B CD1 
2588 N N   . SER B 196 ? 0.88837 0.94133 0.67327 0.07912  0.00203  0.03153  196 SER B N   
2589 C CA  . SER B 196 ? 0.93777 0.97671 0.70659 0.06566  -0.01983 0.04453  196 SER B CA  
2590 C C   . SER B 196 ? 1.00416 1.07660 0.75545 0.05950  -0.01859 0.05228  196 SER B C   
2591 O O   . SER B 196 ? 0.93887 1.04175 0.68389 0.06878  0.00152  0.04347  196 SER B O   
2592 C CB  . SER B 196 ? 0.95579 0.95399 0.71739 0.07043  -0.02807 0.02470  196 SER B CB  
2593 O OG  . SER B 196 ? 0.87984 0.88442 0.63312 0.07561  -0.02269 0.00482  196 SER B OG  
2594 N N   . ASN B 197 ? 0.83774 0.90102 0.57682 0.04475  -0.04144 0.06947  197 ASN B N   
2595 C CA  . ASN B 197 ? 0.92860 1.01503 0.64515 0.03629  -0.04529 0.07799  197 ASN B CA  
2596 C C   . ASN B 197 ? 0.95916 1.02627 0.65715 0.04449  -0.04603 0.04883  197 ASN B C   
2597 O O   . ASN B 197 ? 0.98369 1.01786 0.69237 0.05184  -0.05066 0.02959  197 ASN B O   
2598 C CB  . ASN B 197 ? 1.04690 1.12372 0.75914 0.01612  -0.07545 0.10757  197 ASN B CB  
2599 C CG  . ASN B 197 ? 1.14424 1.24476 0.87670 0.00351  -0.08000 0.14297  197 ASN B CG  
2600 O OD1 . ASN B 197 ? 1.24498 1.39201 0.99016 0.00602  -0.05695 0.15432  197 ASN B OD1 
2601 N ND2 . ASN B 197 ? 1.17799 1.24502 0.91499 -0.00879 -0.11126 0.16112  197 ASN B ND2 
2602 N N   . PRO B 198 ? 0.92856 1.01536 0.59849 0.04319  -0.04229 0.04706  198 PRO B N   
2603 C CA  . PRO B 198 ? 0.99030 1.05405 0.64211 0.04910  -0.04934 0.02088  198 PRO B CA  
2604 C C   . PRO B 198 ? 1.00716 1.03825 0.66636 0.03978  -0.07814 0.02256  198 PRO B C   
2605 O O   . PRO B 198 ? 1.01132 1.03955 0.67039 0.02615  -0.09687 0.04577  198 PRO B O   
2606 C CB  . PRO B 198 ? 0.88942 0.97788 0.49920 0.04735  -0.04339 0.02516  198 PRO B CB  
2607 C CG  . PRO B 198 ? 0.96552 1.09887 0.57900 0.04770  -0.02077 0.04808  198 PRO B CG  
2608 C CD  . PRO B 198 ? 0.85745 0.98841 0.50963 0.03681  -0.03110 0.07045  198 PRO B CD  
2609 N N   . PHE B 199 ? 0.95935 0.96542 0.62898 0.04806  -0.08289 -0.00125 199 PHE B N   
2610 C CA  . PHE B 199 ? 0.92076 0.90009 0.60405 0.04369  -0.10715 -0.00203 199 PHE B CA  
2611 C C   . PHE B 199 ? 1.02164 0.98975 0.69797 0.04550  -0.11769 -0.02044 199 PHE B C   
2612 O O   . PHE B 199 ? 1.10217 1.07279 0.76825 0.05373  -0.10564 -0.03811 199 PHE B O   
2613 C CB  . PHE B 199 ? 0.97360 0.93261 0.69198 0.05303  -0.10303 -0.00707 199 PHE B CB  
2614 C CG  . PHE B 199 ? 1.01819 0.97378 0.75748 0.06580  -0.08463 -0.02806 199 PHE B CG  
2615 C CD1 . PHE B 199 ? 0.92755 0.89526 0.66612 0.07225  -0.06267 -0.03242 199 PHE B CD1 
2616 C CD2 . PHE B 199 ? 1.08454 1.02583 0.84900 0.07040  -0.09159 -0.04082 199 PHE B CD2 
2617 C CE1 . PHE B 199 ? 0.99593 0.95684 0.75366 0.08249  -0.04976 -0.05026 199 PHE B CE1 
2618 C CE2 . PHE B 199 ? 0.93774 0.87588 0.72477 0.07906  -0.07807 -0.05595 199 PHE B CE2 
2619 C CZ  . PHE B 199 ? 0.99536 0.94100 0.77655 0.08483  -0.05800 -0.06127 199 PHE B CZ  
2620 N N   . ILE B 200 ? 0.86544 0.81704 0.54787 0.03814  -0.14415 -0.01600 200 ILE B N   
2621 C CA  . ILE B 200 ? 1.05895 0.99716 0.73267 0.03518  -0.16362 -0.02761 200 ILE B CA  
2622 C C   . ILE B 200 ? 1.03617 0.95792 0.76093 0.04227  -0.17112 -0.03831 200 ILE B C   
2623 O O   . ILE B 200 ? 0.95670 0.87301 0.71373 0.04529  -0.17489 -0.03014 200 ILE B O   
2624 C CB  . ILE B 200 ? 1.09132 1.02493 0.73605 0.01967  -0.19169 -0.01140 200 ILE B CB  
2625 C CG1 . ILE B 200 ? 1.25522 1.21010 0.84540 0.01293  -0.18099 -0.00081 200 ILE B CG1 
2626 C CG2 . ILE B 200 ? 1.20459 1.11576 0.85323 0.01599  -0.22008 -0.02143 200 ILE B CG2 
2627 C CD1 . ILE B 200 ? 1.26885 1.23536 0.84632 -0.00250 -0.19199 0.02926  200 ILE B CD1 
2628 N N   . VAL B 201 ? 1.01416 0.92752 0.74624 0.04611  -0.17334 -0.05546 201 VAL B N   
2629 C CA  . VAL B 201 ? 1.04114 0.94363 0.82708 0.04933  -0.18454 -0.06094 201 VAL B CA  
2630 C C   . VAL B 201 ? 1.06253 0.94807 0.83968 0.03885  -0.22043 -0.06208 201 VAL B C   
2631 O O   . VAL B 201 ? 1.04225 0.91579 0.77383 0.03516  -0.23019 -0.07255 201 VAL B O   
2632 C CB  . VAL B 201 ? 1.06326 0.96507 0.87153 0.05806  -0.16742 -0.07547 201 VAL B CB  
2633 C CG1 . VAL B 201 ? 0.96381 0.85812 0.83101 0.05749  -0.18317 -0.07621 201 VAL B CG1 
2634 C CG2 . VAL B 201 ? 1.05215 0.96684 0.87150 0.06754  -0.13527 -0.07254 201 VAL B CG2 
2635 N N   . TYR B 202 ? 1.01449 0.89606 0.83135 0.03566  -0.24125 -0.05156 202 TYR B N   
2636 C CA  . TYR B 202 ? 1.10425 0.96801 0.91650 0.02396  -0.28053 -0.04890 202 TYR B CA  
2637 C C   . TYR B 202 ? 1.06624 0.92621 0.94988 0.02578  -0.29629 -0.04984 202 TYR B C   
2638 O O   . TYR B 202 ? 1.05178 0.92787 0.99217 0.03674  -0.27469 -0.04761 202 TYR B O   
2639 C CB  . TYR B 202 ? 1.05065 0.91257 0.85182 0.01670  -0.29895 -0.03216 202 TYR B CB  
2640 C CG  . TYR B 202 ? 1.07959 0.95026 0.93492 0.02772  -0.29056 -0.02275 202 TYR B CG  
2641 C CD1 . TYR B 202 ? 1.02148 0.89042 0.94124 0.03257  -0.30808 -0.01860 202 TYR B CD1 
2642 C CD2 . TYR B 202 ? 1.03180 0.91091 0.87402 0.03534  -0.26532 -0.01796 202 TYR B CD2 
2643 C CE1 . TYR B 202 ? 0.94834 0.82421 0.91255 0.04823  -0.29668 -0.01193 202 TYR B CE1 
2644 C CE2 . TYR B 202 ? 1.01882 0.89710 0.89920 0.04907  -0.25870 -0.01226 202 TYR B CE2 
2645 C CZ  . TYR B 202 ? 0.91518 0.79217 0.85397 0.05733  -0.27216 -0.01040 202 TYR B CZ  
2646 O OH  . TYR B 202 ? 0.98294 0.85819 0.95441 0.07621  -0.26215 -0.00641 202 TYR B OH  
2647 N N   . SER B 203 ? 1.13810 0.97670 1.01867 0.01432  -0.33501 -0.05081 203 SER B N   
2648 C CA  . SER B 203 ? 1.28583 1.12164 1.24050 0.01226  -0.35774 -0.04680 203 SER B CA  
2649 C C   . SER B 203 ? 1.21328 1.04501 1.20127 0.00562  -0.39211 -0.03171 203 SER B C   
2650 O O   . SER B 203 ? 1.11307 0.92685 1.04676 -0.00463 -0.41559 -0.02895 203 SER B O   
2651 C CB  . SER B 203 ? 1.23849 1.04531 1.17073 0.00365  -0.38344 -0.05977 203 SER B CB  
2652 O OG  . SER B 203 ? 1.51221 1.29260 1.34944 -0.00273 -0.39664 -0.07006 203 SER B OG  
2653 N N   . ALA B 204 ? 1.19127 1.04136 1.27040 0.01203  -0.39448 -0.02018 204 ALA B N   
2654 C CA  . ALA B 204 ? 1.07098 0.92056 1.19846 0.00920  -0.42717 -0.00519 204 ALA B CA  
2655 C C   . ALA B 204 ? 1.09503 0.92702 1.25941 -0.00580 -0.47276 -0.00110 204 ALA B C   
2656 O O   . ALA B 204 ? 1.37896 1.22214 1.60109 -0.00514 -0.46895 0.00095  204 ALA B O   
2657 C CB  . ALA B 204 ? 1.15451 1.03740 1.36224 0.02960  -0.40039 0.00639  204 ALA B CB  
2658 N N   . LYS B 205 ? 1.10106 0.90312 1.23235 -0.02085 -0.51896 0.00230  205 LYS B N   
2659 C CA  . LYS B 205 ? 1.09340 0.87022 1.25456 -0.03695 -0.57102 0.00745  205 LYS B CA  
2660 C C   . LYS B 205 ? 1.06587 0.87292 1.35419 -0.03182 -0.58286 0.02872  205 LYS B C   
2661 O O   . LYS B 205 ? 1.17997 1.01971 1.51890 -0.01505 -0.55820 0.03850  205 LYS B O   
2662 C CB  . LYS B 205 ? 1.28247 1.01542 1.36662 -0.05445 -0.61828 0.00658  205 LYS B CB  
2663 C CG  . LYS B 205 ? 1.25253 0.95332 1.21301 -0.06012 -0.61216 -0.01287 205 LYS B CG  
2664 C CD  . LYS B 205 ? 1.56241 1.24468 1.43968 -0.06901 -0.62603 -0.00895 205 LYS B CD  
2665 C CE  . LYS B 205 ? 1.64207 1.27068 1.42401 -0.08455 -0.66644 -0.01799 205 LYS B CE  
2666 N NZ  . LYS B 205 ? 1.75577 1.37537 1.43363 -0.08968 -0.65780 -0.01682 205 LYS B NZ  
2667 N N   . LYS B 206 ? 1.19734 0.99179 1.53748 -0.04535 -0.62239 0.03663  206 LYS B N   
2668 C CA  . LYS B 206 ? 1.22611 1.05273 1.69701 -0.04319 -0.63847 0.06144  206 LYS B CA  
2669 C C   . LYS B 206 ? 1.31313 1.11073 1.79797 -0.05915 -0.70287 0.07354  206 LYS B C   
2670 O O   . LYS B 206 ? 1.37538 1.12042 1.79713 -0.08018 -0.75166 0.06635  206 LYS B O   
2671 C CB  . LYS B 206 ? 1.28373 1.12029 1.81996 -0.05020 -0.64237 0.06872  206 LYS B CB  
2672 C CG  . LYS B 206 ? 1.42093 1.31556 2.03103 -0.03013 -0.58192 0.07773  206 LYS B CG  
2673 C CD  . LYS B 206 ? 1.60209 1.50732 2.28519 -0.04120 -0.59201 0.09103  206 LYS B CD  
2674 C CE  . LYS B 206 ? 1.59851 1.57260 2.39584 -0.02341 -0.54417 0.11493  206 LYS B CE  
2675 N NZ  . LYS B 206 ? 1.43638 1.43741 2.19804 0.00426  -0.48060 0.10434  206 LYS B NZ  
2676 N N   . PHE B 207 ? 1.28972 1.11778 1.85263 -0.04734 -0.70382 0.09110  207 PHE B N   
2677 C CA  . PHE B 207 ? 1.34854 1.15401 1.93989 -0.06018 -0.76479 0.10568  207 PHE B CA  
2678 C C   . PHE B 207 ? 1.44340 1.29660 2.19136 -0.05185 -0.77235 0.13367  207 PHE B C   
2679 O O   . PHE B 207 ? 1.54537 1.44082 2.36165 -0.02752 -0.74431 0.14405  207 PHE B O   
2680 C CB  . PHE B 207 ? 1.21291 1.00765 1.74846 -0.05243 -0.76269 0.10146  207 PHE B CB  
2681 C CG  . PHE B 207 ? 1.17507 0.92744 1.56377 -0.06377 -0.75963 0.08088  207 PHE B CG  
2682 C CD1 . PHE B 207 ? 1.24620 0.94302 1.55542 -0.08884 -0.81401 0.07802  207 PHE B CD1 
2683 C CD2 . PHE B 207 ? 1.13898 0.90799 1.46938 -0.04877 -0.70190 0.06639  207 PHE B CD2 
2684 C CE1 . PHE B 207 ? 1.33164 0.99642 1.50740 -0.09692 -0.80541 0.06206  207 PHE B CE1 
2685 C CE2 . PHE B 207 ? 1.16801 0.90661 1.37381 -0.05862 -0.69643 0.05186  207 PHE B CE2 
2686 C CZ  . PHE B 207 ? 1.23797 0.92755 1.36717 -0.08179 -0.74546 0.05018  207 PHE B CZ  
2687 N N   . PRO B 208 ? 1.48436 1.33239 2.29438 -0.07018 -0.81007 0.14772  208 PRO B N   
2688 C CA  . PRO B 208 ? 1.49657 1.39878 2.46774 -0.06367 -0.81486 0.18014  208 PRO B CA  
2689 C C   . PRO B 208 ? 1.30517 1.20004 2.31624 -0.06120 -0.83353 0.19400  208 PRO B C   
2690 O O   . PRO B 208 ? 1.42234 1.25319 2.35885 -0.08070 -0.87517 0.18784  208 PRO B O   
2691 C CB  . PRO B 208 ? 1.61419 1.48310 2.59954 -0.09155 -0.84853 0.18864  208 PRO B CB  
2692 C CG  . PRO B 208 ? 1.68554 1.47428 2.51980 -0.11106 -0.88027 0.16084  208 PRO B CG  
2693 C CD  . PRO B 208 ? 1.62695 1.41267 2.35800 -0.09817 -0.85739 0.13583  208 PRO B CD  
2694 N N   . GLY B 209 ? 1.26219 1.22200 2.38838 -0.03476 -0.79871 0.21267  209 GLY B N   
2695 C CA  . GLY B 209 ? 1.22784 1.18714 2.39368 -0.02588 -0.80961 0.22229  209 GLY B CA  
2696 C C   . GLY B 209 ? 1.25750 1.20744 2.35118 -0.00476 -0.79542 0.20338  209 GLY B C   
2697 O O   . GLY B 209 ? 1.31154 1.26640 2.44242 0.00915  -0.79784 0.20954  209 GLY B O   
2698 N N   . LEU B 210 ? 1.23045 1.16411 2.22118 -0.00280 -0.78281 0.18119  210 LEU B N   
2699 C CA  . LEU B 210 ? 1.23735 1.15811 2.14772 0.01543  -0.76061 0.16365  210 LEU B CA  
2700 C C   . LEU B 210 ? 1.37391 1.32835 2.26356 0.04254  -0.68293 0.15024  210 LEU B C   
2701 O O   . LEU B 210 ? 1.39775 1.37298 2.30627 0.07426  -0.64898 0.14825  210 LEU B O   
2702 C CB  . LEU B 210 ? 1.28895 1.14340 2.05640 -0.01334 -0.79587 0.14632  210 LEU B CB  
2703 C CG  . LEU B 210 ? 1.32274 1.15173 2.00381 -0.00576 -0.79056 0.13485  210 LEU B CG  
2704 C CD1 . LEU B 210 ? 1.15106 0.97358 1.88876 0.00174  -0.81548 0.14771  210 LEU B CD1 
2705 C CD2 . LEU B 210 ? 1.17174 0.94599 1.71413 -0.03522 -0.81572 0.12171  210 LEU B CD2 
2706 N N   . THR B 211 ? 1.43300 1.38843 2.28135 0.03188  -0.65655 0.14043  211 THR B N   
2707 C CA  . THR B 211 ? 1.52481 1.50949 2.35383 0.05413  -0.58629 0.12936  211 THR B CA  
2708 C C   . THR B 211 ? 1.76044 1.79625 2.69186 0.06035  -0.55776 0.14643  211 THR B C   
2709 O O   . THR B 211 ? 1.84275 1.88821 2.74352 0.06151  -0.51743 0.13779  211 THR B O   
2710 C CB  . THR B 211 ? 1.54692 1.49425 2.24424 0.03890  -0.57348 0.10505  211 THR B CB  
2711 O OG1 . THR B 211 ? 1.54634 1.48645 2.24229 0.01719  -0.58539 0.10454  211 THR B OG1 
2712 C CG2 . THR B 211 ? 1.41566 1.31162 2.01738 0.02105  -0.61540 0.09556  211 THR B CG2 
2713 N N   . THR B 212 ? 1.77448 1.84485 2.83226 0.06319  -0.58004 0.17361  212 THR B N   
2714 C CA  . THR B 212 ? 1.81526 1.93960 2.98652 0.06488  -0.55972 0.19826  212 THR B CA  
2715 C C   . THR B 212 ? 1.75254 1.85091 2.88886 0.03178  -0.58135 0.19481  212 THR B C   
2716 O O   . THR B 212 ? 1.59127 1.67451 2.77430 0.00497  -0.63864 0.21032  212 THR B O   
2717 C CB  . THR B 212 ? 1.89563 2.07269 3.09514 0.10147  -0.47990 0.19978  212 THR B CB  
2718 O OG1 . THR B 212 ? 1.81204 2.00958 3.04610 0.13706  -0.46107 0.20211  212 THR B OG1 
2719 C CG2 . THR B 212 ? 1.85416 2.09057 3.17228 0.10017  -0.45871 0.23038  212 THR B CG2 
2720 N N   . GLY C 15  ? 1.57023 1.98058 1.40995 -0.38885 0.15191  -0.29190 15  GLY C N   
2721 C CA  . GLY C 15  ? 1.54118 2.04892 1.44579 -0.31714 0.12347  -0.31564 15  GLY C CA  
2722 C C   . GLY C 15  ? 1.59588 2.03814 1.50525 -0.26329 0.09070  -0.28709 15  GLY C C   
2723 O O   . GLY C 15  ? 1.61223 2.10045 1.55079 -0.20291 0.06650  -0.30010 15  GLY C O   
2724 N N   . ASN C 16  ? 1.41674 1.74357 1.28875 -0.28511 0.09045  -0.25092 16  ASN C N   
2725 C CA  . ASN C 16  ? 1.30902 1.57301 1.18796 -0.24161 0.06520  -0.22816 16  ASN C CA  
2726 C C   . ASN C 16  ? 1.21023 1.41230 1.07182 -0.19518 0.04429  -0.19034 16  ASN C C   
2727 O O   . ASN C 16  ? 1.06568 1.22153 0.93651 -0.16131 0.02806  -0.17672 16  ASN C O   
2728 C CB  . ASN C 16  ? 1.38577 1.55735 1.23683 -0.28051 0.07127  -0.21327 16  ASN C CB  
2729 C CG  . ASN C 16  ? 1.61089 1.82430 1.49885 -0.28531 0.07276  -0.24484 16  ASN C CG  
2730 O OD1 . ASN C 16  ? 1.62696 1.94538 1.55932 -0.26514 0.06977  -0.28330 16  ASN C OD1 
2731 N ND2 . ASN C 16  ? 1.59201 1.71921 1.45659 -0.30856 0.07373  -0.23150 16  ASN C ND2 
2732 N N   . SER C 17  ? 1.13067 1.33300 0.96849 -0.19638 0.04688  -0.17747 17  SER C N   
2733 C CA  . SER C 17  ? 1.24736 1.38517 1.06613 -0.16211 0.02815  -0.14362 17  SER C CA  
2734 C C   . SER C 17  ? 1.19082 1.38503 1.00928 -0.13826 0.02732  -0.14891 17  SER C C   
2735 O O   . SER C 17  ? 1.14330 1.42326 0.97329 -0.15017 0.04118  -0.17843 17  SER C O   
2736 C CB  . SER C 17  ? 1.22839 1.25952 0.99405 -0.19020 0.02461  -0.11227 17  SER C CB  
2737 O OG  . SER C 17  ? 1.40290 1.42966 1.12545 -0.21178 0.03404  -0.10398 17  SER C OG  
2738 N N   . ASN C 18  ? 1.02788 1.17751 0.83685 -0.10350 0.01063  -0.12549 18  ASN C N   
2739 C CA  . ASN C 18  ? 1.04764 1.22718 0.84496 -0.08122 0.00782  -0.12435 18  ASN C CA  
2740 C C   . ASN C 18  ? 0.89684 0.99924 0.67436 -0.06644 -0.00839 -0.09362 18  ASN C C   
2741 O O   . ASN C 18  ? 1.07190 1.11775 0.86071 -0.05770 -0.02039 -0.08250 18  ASN C O   
2742 C CB  . ASN C 18  ? 0.95734 1.19447 0.77287 -0.03606 0.00172  -0.14766 18  ASN C CB  
2743 C CG  . ASN C 18  ? 0.99348 1.27041 0.79228 -0.01449 -0.00004 -0.15432 18  ASN C CG  
2744 O OD1 . ASN C 18  ? 0.94524 1.24766 0.73239 -0.04134 0.01105  -0.15547 18  ASN C OD1 
2745 N ND2 . ASN C 18  ? 0.99210 1.26537 0.77959 0.03258  -0.01209 -0.16021 18  ASN C ND2 
2746 N N   . SER C 19  ? 0.93391 1.04162 0.68677 -0.06123 -0.00999 -0.08586 19  SER C N   
2747 C CA  . SER C 19  ? 1.14138 1.18492 0.87794 -0.04585 -0.02861 -0.06281 19  SER C CA  
2748 C C   . SER C 19  ? 1.23204 1.30368 0.95813 -0.02102 -0.03055 -0.06436 19  SER C C   
2749 O O   . SER C 19  ? 1.18920 1.31516 0.90166 -0.02689 -0.01804 -0.07636 19  SER C O   
2750 C CB  . SER C 19  ? 1.23419 1.20815 0.92246 -0.07664 -0.03479 -0.04262 19  SER C CB  
2751 O OG  . SER C 19  ? 1.54169 1.44539 1.22890 -0.05544 -0.06304 -0.02817 19  SER C OG  
2752 N N   . VAL C 20  ? 1.21942 1.25659 0.95390 0.00508  -0.04505 -0.05726 20  VAL C N   
2753 C CA  . VAL C 20  ? 1.22308 1.27044 0.94122 0.02709  -0.04775 -0.05775 20  VAL C CA  
2754 C C   . VAL C 20  ? 1.19785 1.19227 0.91255 0.03178  -0.06772 -0.04429 20  VAL C C   
2755 O O   . VAL C 20  ? 1.19506 1.15067 0.93093 0.02970  -0.08197 -0.04143 20  VAL C O   
2756 C CB  . VAL C 20  ? 1.17086 1.23303 0.89603 0.05632  -0.04107 -0.07394 20  VAL C CB  
2757 C CG1 . VAL C 20  ? 1.09250 1.10816 0.83903 0.06414  -0.04482 -0.07466 20  VAL C CG1 
2758 C CG2 . VAL C 20  ? 1.12596 1.21125 0.81670 0.07749  -0.03955 -0.08019 20  VAL C CG2 
2759 N N   . SER C 21  ? 1.25704 1.25338 0.94637 0.04208  -0.07188 -0.04090 21  SER C N   
2760 C CA  . SER C 21  ? 1.20195 1.15642 0.88604 0.04904  -0.09453 -0.03332 21  SER C CA  
2761 C C   . SER C 21  ? 1.20421 1.16727 0.88842 0.06873  -0.09231 -0.04298 21  SER C C   
2762 O O   . SER C 21  ? 1.20320 1.19342 0.86323 0.07742  -0.07722 -0.04763 21  SER C O   
2763 C CB  . SER C 21  ? 1.23263 1.15756 0.86245 0.03313  -0.10532 -0.01564 21  SER C CB  
2764 O OG  . SER C 21  ? 1.42282 1.38881 1.02126 0.01734  -0.08177 -0.01626 21  SER C OG  
2765 N N   . ARG C 22  ? 1.11585 1.05459 0.82607 0.07663  -0.10888 -0.05089 22  ARG C N   
2766 C CA  . ARG C 22  ? 1.20733 1.14518 0.91491 0.08719  -0.10574 -0.06310 22  ARG C CA  
2767 C C   . ARG C 22  ? 1.32347 1.24164 1.04328 0.09219  -0.13657 -0.06696 22  ARG C C   
2768 O O   . ARG C 22  ? 1.31032 1.20679 1.03381 0.09315  -0.16287 -0.06017 22  ARG C O   
2769 C CB  . ARG C 22  ? 1.12219 1.05851 0.85773 0.08711  -0.08374 -0.08504 22  ARG C CB  
2770 C CG  . ARG C 22  ? 1.15390 1.08778 0.95468 0.08142  -0.09133 -0.10639 22  ARG C CG  
2771 C CD  . ARG C 22  ? 1.24564 1.17197 1.06078 0.07188  -0.05923 -0.13142 22  ARG C CD  
2772 N NE  . ARG C 22  ? 1.25716 1.19529 1.14451 0.06370  -0.06091 -0.15930 22  ARG C NE  
2773 C CZ  . ARG C 22  ? 1.36213 1.31553 1.30094 0.05884  -0.06718 -0.19225 22  ARG C CZ  
2774 N NH1 . ARG C 22  ? 1.37627 1.32821 1.29832 0.05859  -0.07178 -0.19832 22  ARG C NH1 
2775 N NH2 . ARG C 22  ? 1.39633 1.37313 1.40966 0.05465  -0.06939 -0.22537 22  ARG C NH2 
2776 N N   . ILE C 23  ? 1.46168 1.38000 1.17994 0.09755  -0.13631 -0.08041 23  ILE C N   
2777 C CA  . ILE C 23  ? 1.40873 1.31635 1.14022 0.10589  -0.16893 -0.09098 23  ILE C CA  
2778 C C   . ILE C 23  ? 1.36043 1.28486 1.14962 0.10194  -0.16030 -0.12936 23  ILE C C   
2779 O O   . ILE C 23  ? 1.36127 1.28413 1.13526 0.09144  -0.12688 -0.13824 23  ILE C O   
2780 C CB  . ILE C 23  ? 1.25736 1.15190 0.92550 0.11066  -0.17741 -0.07425 23  ILE C CB  
2781 C CG1 . ILE C 23  ? 1.39262 1.25976 1.00849 0.10888  -0.19536 -0.04627 23  ILE C CG1 
2782 C CG2 . ILE C 23  ? 1.28313 1.17458 0.96995 0.11917  -0.20133 -0.09668 23  ILE C CG2 
2783 C CD1 . ILE C 23  ? 1.30810 1.17102 0.85387 0.10522  -0.18643 -0.02860 23  ILE C CD1 
2784 N N   . THR C 24  ? 1.46663 1.40304 1.31643 0.11000  -0.19011 -0.15671 24  THR C N   
2785 C CA  . THR C 24  ? 1.61079 1.57914 1.53244 0.10006  -0.17941 -0.20568 24  THR C CA  
2786 C C   . THR C 24  ? 1.65087 1.62654 1.57036 0.10118  -0.19275 -0.22588 24  THR C C   
2787 O O   . THR C 24  ? 1.57181 1.52382 1.43131 0.11332  -0.21291 -0.19935 24  THR C O   
2788 C CB  . THR C 24  ? 1.54439 1.53906 1.54742 0.11235  -0.20717 -0.23810 24  THR C CB  
2789 O OG1 . THR C 24  ? 1.54632 1.52345 1.53763 0.14352  -0.26586 -0.23236 24  THR C OG1 
2790 C CG2 . THR C 24  ? 1.41980 1.40466 1.42446 0.10799  -0.19025 -0.22072 24  THR C CG2 
2791 N N   . ARG C 25  ? 1.69394 1.70458 1.68012 0.08401  -0.17769 -0.27802 25  ARG C N   
2792 C CA  . ARG C 25  ? 1.68090 1.70620 1.67672 0.07969  -0.18794 -0.30758 25  ARG C CA  
2793 C C   . ARG C 25  ? 1.60504 1.64655 1.62763 0.11518  -0.25484 -0.31932 25  ARG C C   
2794 O O   . ARG C 25  ? 1.55202 1.58674 1.54648 0.12281  -0.27646 -0.32154 25  ARG C O   
2795 C CB  . ARG C 25  ? 1.71729 1.78011 1.78188 0.04346  -0.14908 -0.36955 25  ARG C CB  
2796 C CG  . ARG C 25  ? 1.91958 1.93447 1.91995 0.00690  -0.08329 -0.35840 25  ARG C CG  
2797 C CD  . ARG C 25  ? 2.13922 2.15604 2.14916 -0.03373 -0.04718 -0.40821 25  ARG C CD  
2798 N NE  . ARG C 25  ? 2.16431 2.19332 2.21944 -0.07698 0.00465  -0.45585 25  ARG C NE  
2799 C CZ  . ARG C 25  ? 2.18256 2.13920 2.15718 -0.11139 0.06398  -0.44773 25  ARG C CZ  
2800 N NH1 . ARG C 25  ? 2.23660 2.10871 2.08731 -0.10067 0.07409  -0.39649 25  ARG C NH1 
2801 N NH2 . ARG C 25  ? 2.22362 2.18844 2.23680 -0.15558 0.11324  -0.49567 25  ARG C NH2 
2802 N N   . GLU C 26  ? 1.47021 1.52286 1.53617 0.14039  -0.29121 -0.32756 26  GLU C N   
2803 C CA  . GLU C 26  ? 1.47727 1.52292 1.54728 0.18281  -0.36271 -0.33833 26  GLU C CA  
2804 C C   . GLU C 26  ? 1.60982 1.57609 1.56325 0.20119  -0.38810 -0.27388 26  GLU C C   
2805 O O   . GLU C 26  ? 1.52445 1.45539 1.44740 0.23706  -0.44848 -0.27439 26  GLU C O   
2806 C CB  . GLU C 26  ? 1.42935 1.50306 1.57769 0.20841  -0.39590 -0.37512 26  GLU C CB  
2807 C CG  . GLU C 26  ? 1.51784 1.66358 1.77180 0.17925  -0.35082 -0.42846 26  GLU C CG  
2808 C CD  . GLU C 26  ? 1.67581 1.84937 2.00448 0.20922  -0.38503 -0.46428 26  GLU C CD  
2809 O OE1 . GLU C 26  ? 1.66469 1.78762 1.95041 0.25463  -0.44585 -0.44323 26  GLU C OE1 
2810 O OE2 . GLU C 26  ? 1.62378 1.86075 2.04444 0.18674  -0.34987 -0.51441 26  GLU C OE2 
2811 N N   . GLY C 27  ? 1.58619 1.52124 1.46977 0.17778  -0.34403 -0.22365 27  GLY C N   
2812 C CA  . GLY C 27  ? 1.64383 1.51491 1.42105 0.18383  -0.35537 -0.17022 27  GLY C CA  
2813 C C   . GLY C 27  ? 1.64465 1.47222 1.38842 0.18888  -0.36489 -0.14169 27  GLY C C   
2814 O O   . GLY C 27  ? 1.71773 1.48655 1.36729 0.18594  -0.36963 -0.10146 27  GLY C O   
2815 N N   . LYS C 28  ? 1.64978 1.50125 1.46352 0.19236  -0.36456 -0.16406 28  LYS C N   
2816 C CA  . LYS C 28  ? 1.80320 1.60900 1.58433 0.19453  -0.37098 -0.13896 28  LYS C CA  
2817 C C   . LYS C 28  ? 1.61066 1.42901 1.37378 0.16119  -0.31364 -0.10929 28  LYS C C   
2818 O O   . LYS C 28  ? 1.52861 1.39835 1.34143 0.14481  -0.27336 -0.12386 28  LYS C O   
2819 C CB  . LYS C 28  ? 1.63219 1.45810 1.49613 0.21768  -0.39953 -0.17976 28  LYS C CB  
2820 C CG  . LYS C 28  ? 1.82276 1.64401 1.71188 0.26097  -0.46650 -0.21982 28  LYS C CG  
2821 C CD  . LYS C 28  ? 1.94932 1.83428 1.95868 0.28103  -0.48356 -0.28147 28  LYS C CD  
2822 C CE  . LYS C 28  ? 2.00815 1.89982 2.05002 0.33259  -0.55855 -0.33184 28  LYS C CE  
2823 N NZ  . LYS C 28  ? 1.93029 1.90752 2.10809 0.35235  -0.57334 -0.40638 28  LYS C NZ  
2824 N N   . LYS C 29  ? 1.55536 1.32125 1.23936 0.15033  -0.31031 -0.07130 29  LYS C N   
2825 C CA  . LYS C 29  ? 1.44530 1.23003 1.11889 0.12236  -0.26346 -0.05102 29  LYS C CA  
2826 C C   . LYS C 29  ? 1.34537 1.13964 1.07622 0.12294  -0.25997 -0.06465 29  LYS C C   
2827 O O   . LYS C 29  ? 1.37339 1.12592 1.10649 0.14093  -0.29694 -0.07201 29  LYS C O   
2828 C CB  . LYS C 29  ? 1.37444 1.10806 0.95025 0.10275  -0.25687 -0.01567 29  LYS C CB  
2829 C CG  . LYS C 29  ? 1.16763 0.93124 0.73975 0.07390  -0.21271 -0.00370 29  LYS C CG  
2830 C CD  . LYS C 29  ? 1.29626 1.07069 0.80523 0.05232  -0.18627 0.01244  29  LYS C CD  
2831 C CE  . LYS C 29  ? 1.65369 1.35539 1.07136 0.02654  -0.18884 0.03382  29  LYS C CE  
2832 N NZ  . LYS C 29  ? 1.79623 1.53542 1.17711 -0.00830 -0.14565 0.03831  29  LYS C NZ  
2833 N N   . ILE C 30  ? 1.11250 0.95427 0.88155 0.10705  -0.21841 -0.06968 30  ILE C N   
2834 C CA  . ILE C 30  ? 1.07573 0.92928 0.89664 0.10450  -0.20860 -0.08330 30  ILE C CA  
2835 C C   . ILE C 30  ? 1.11674 0.97822 0.90790 0.08196  -0.17421 -0.06216 30  ILE C C   
2836 O O   . ILE C 30  ? 1.16681 1.06044 0.94358 0.07369  -0.14496 -0.05797 30  ILE C O   
2837 C CB  . ILE C 30  ? 1.09427 0.99503 0.99460 0.10690  -0.19164 -0.12129 30  ILE C CB  
2838 C CG1 . ILE C 30  ? 1.16187 1.07021 1.11501 0.12931  -0.23011 -0.15655 30  ILE C CG1 
2839 C CG2 . ILE C 30  ? 0.91398 0.82774 0.85185 0.09708  -0.16727 -0.13097 30  ILE C CG2 
2840 C CD1 . ILE C 30  ? 1.25890 1.21536 1.30450 0.12615  -0.21393 -0.20511 30  ILE C CD1 
2841 N N   . THR C 31  ? 1.10220 0.93295 0.88221 0.07474  -0.18069 -0.05327 31  THR C N   
2842 C CA  . THR C 31  ? 1.13001 0.97022 0.88336 0.05013  -0.15210 -0.03846 31  THR C CA  
2843 C C   . THR C 31  ? 1.10528 0.96063 0.91033 0.04923  -0.14009 -0.05358 31  THR C C   
2844 O O   . THR C 31  ? 1.19221 1.01843 1.02501 0.06079  -0.16227 -0.06454 31  THR C O   
2845 C CB  . THR C 31  ? 1.27510 1.05476 0.95398 0.03093  -0.16265 -0.01546 31  THR C CB  
2846 O OG1 . THR C 31  ? 1.28519 1.02862 0.90918 0.03657  -0.18264 -0.00369 31  THR C OG1 
2847 C CG2 . THR C 31  ? 1.15473 0.96640 0.80866 -0.00224 -0.12611 -0.00832 31  THR C CG2 
2848 N N   . TYR C 32  ? 1.06441 0.96277 0.87815 0.03967  -0.10824 -0.05724 32  TYR C N   
2849 C CA  . TYR C 32  ? 0.91640 0.82617 0.76560 0.03645  -0.09335 -0.07019 32  TYR C CA  
2850 C C   . TYR C 32  ? 1.07282 0.98845 0.89308 0.01406  -0.08116 -0.05955 32  TYR C C   
2851 O O   . TYR C 32  ? 1.14178 1.09221 0.93421 0.00492  -0.06648 -0.05567 32  TYR C O   
2852 C CB  . TYR C 32  ? 0.91675 0.85698 0.78354 0.04471  -0.06867 -0.08691 32  TYR C CB  
2853 C CG  . TYR C 32  ? 0.96006 0.89761 0.84803 0.05574  -0.07063 -0.10215 32  TYR C CG  
2854 C CD1 . TYR C 32  ? 0.84324 0.78501 0.70105 0.06129  -0.07361 -0.09520 32  TYR C CD1 
2855 C CD2 . TYR C 32  ? 0.91831 0.85375 0.85911 0.05713  -0.06631 -0.12915 32  TYR C CD2 
2856 C CE1 . TYR C 32  ? 0.99506 0.93487 0.87255 0.06624  -0.07341 -0.11323 32  TYR C CE1 
2857 C CE2 . TYR C 32  ? 0.97013 0.91213 0.93687 0.05926  -0.06293 -0.15207 32  TYR C CE2 
2858 C CZ  . TYR C 32  ? 1.10767 1.04991 1.04143 0.06293  -0.06684 -0.14334 32  TYR C CZ  
2859 O OH  . TYR C 32  ? 1.15471 1.10402 1.11472 0.06022  -0.06153 -0.17013 32  TYR C OH  
2860 N N   . LYS C 33  ? 1.04018 0.92607 0.86993 0.00494  -0.08688 -0.06050 33  LYS C N   
2861 C CA  . LYS C 33  ? 0.99287 0.88101 0.79814 -0.02321 -0.07306 -0.05581 33  LYS C CA  
2862 C C   . LYS C 33  ? 0.94380 0.85032 0.78819 -0.02114 -0.06098 -0.07213 33  LYS C C   
2863 O O   . LYS C 33  ? 0.96739 0.84272 0.84128 -0.01005 -0.07196 -0.07973 33  LYS C O   
2864 C CB  . LYS C 33  ? 1.02362 0.83600 0.77875 -0.04216 -0.08994 -0.03983 33  LYS C CB  
2865 C CG  . LYS C 33  ? 1.16894 0.97842 0.88873 -0.08393 -0.06831 -0.03801 33  LYS C CG  
2866 C CD  . LYS C 33  ? 1.33389 1.04226 1.00239 -0.09986 -0.08428 -0.02677 33  LYS C CD  
2867 C CE  . LYS C 33  ? 1.35218 1.02930 0.94545 -0.15404 -0.06056 -0.01909 33  LYS C CE  
2868 N NZ  . LYS C 33  ? 1.48400 1.02350 0.98665 -0.16723 -0.08096 -0.00124 33  LYS C NZ  
2869 N N   . LEU C 34  ? 0.88439 0.84353 0.72861 -0.02867 -0.04072 -0.08197 34  LEU C N   
2870 C CA  . LEU C 34  ? 0.86568 0.84107 0.73314 -0.02795 -0.02990 -0.09808 34  LEU C CA  
2871 C C   . LEU C 34  ? 0.98909 0.97521 0.84328 -0.06110 -0.02194 -0.10099 34  LEU C C   
2872 O O   . LEU C 34  ? 1.00405 1.02156 0.83523 -0.08252 -0.01351 -0.10115 34  LEU C O   
2873 C CB  . LEU C 34  ? 0.94011 0.95947 0.80612 -0.00569 -0.01869 -0.11322 34  LEU C CB  
2874 C CG  . LEU C 34  ? 0.90413 0.89970 0.77378 0.01898  -0.01562 -0.11796 34  LEU C CG  
2875 C CD1 . LEU C 34  ? 0.91453 0.92808 0.75117 0.04059  -0.00653 -0.13163 34  LEU C CD1 
2876 C CD2 . LEU C 34  ? 0.82219 0.78238 0.72437 0.01685  -0.01307 -0.12629 34  LEU C CD2 
2877 N N   . ASN C 35  ? 0.90497 0.86555 0.77352 -0.06940 -0.02155 -0.10723 35  ASN C N   
2878 C CA  . ASN C 35  ? 1.03781 1.00334 0.89211 -0.10670 -0.01109 -0.11373 35  ASN C CA  
2879 C C   . ASN C 35  ? 0.92580 0.89413 0.80689 -0.10255 -0.00751 -0.13030 35  ASN C C   
2880 O O   . ASN C 35  ? 1.00371 0.92795 0.90222 -0.08408 -0.01616 -0.12830 35  ASN C O   
2881 C CB  . ASN C 35  ? 1.01519 0.89812 0.82425 -0.13426 -0.01924 -0.09395 35  ASN C CB  
2882 C CG  . ASN C 35  ? 1.25913 1.10994 1.04692 -0.17372 -0.00874 -0.10050 35  ASN C CG  
2883 O OD1 . ASN C 35  ? 1.46492 1.37965 1.27095 -0.19532 0.01044  -0.12270 35  ASN C OD1 
2884 N ND2 . ASN C 35  ? 1.61471 1.36182 1.35961 -0.18107 -0.02422 -0.08476 35  ASN C ND2 
2885 N N   . ILE C 36  ? 0.93029 0.95682 0.81795 -0.11869 0.00489  -0.15215 36  ILE C N   
2886 C CA  . ILE C 36  ? 0.90684 0.94324 0.81494 -0.11080 0.00687  -0.17133 36  ILE C CA  
2887 C C   . ILE C 36  ? 1.09753 1.07893 0.99723 -0.14510 0.00907  -0.16829 36  ILE C C   
2888 O O   . ILE C 36  ? 1.00334 0.98834 0.88221 -0.18825 0.01987  -0.17225 36  ILE C O   
2889 C CB  . ILE C 36  ? 1.00671 1.13141 0.92478 -0.10593 0.01151  -0.20273 36  ILE C CB  
2890 C CG1 . ILE C 36  ? 0.85572 1.01279 0.76522 -0.06390 0.00435  -0.20506 36  ILE C CG1 
2891 C CG2 . ILE C 36  ? 0.88743 1.01386 0.81706 -0.09950 0.01045  -0.22354 36  ILE C CG2 
2892 C CD1 . ILE C 36  ? 0.84699 1.08875 0.76005 -0.04566 -0.00091 -0.24076 36  ILE C CD1 
2893 N N   . MET C 37  ? 1.02412 0.95044 0.93530 -0.12840 0.00138  -0.16473 37  MET C N   
2894 C CA  . MET C 37  ? 1.01452 0.87823 0.91338 -0.15223 -0.00043 -0.16422 37  MET C CA  
2895 C C   . MET C 37  ? 1.01283 0.91198 0.92383 -0.16894 0.01074  -0.18947 37  MET C C   
2896 O O   . MET C 37  ? 1.22981 1.10527 1.11985 -0.20954 0.01807  -0.19488 37  MET C O   
2897 C CB  . MET C 37  ? 1.12910 0.92842 1.04295 -0.12201 -0.01600 -0.15772 37  MET C CB  
2898 C CG  . MET C 37  ? 1.18276 0.93427 1.08094 -0.10797 -0.03507 -0.13809 37  MET C CG  
2899 S SD  . MET C 37  ? 1.31543 1.05629 1.15324 -0.14348 -0.03203 -0.11792 37  MET C SD  
2900 C CE  . MET C 37  ? 1.37555 1.00348 1.14480 -0.18073 -0.03763 -0.10996 37  MET C CE  
2901 N N   . GLN C 38  ? 0.99988 0.94515 0.93450 -0.13950 0.01201  -0.20661 38  GLN C N   
2902 C CA  . GLN C 38  ? 0.96949 0.94322 0.91253 -0.14562 0.01650  -0.23321 38  GLN C CA  
2903 C C   . GLN C 38  ? 0.98671 1.04384 0.93362 -0.12364 0.01438  -0.25596 38  GLN C C   
2904 O O   . GLN C 38  ? 0.91501 0.96931 0.85196 -0.08382 0.00979  -0.25424 38  GLN C O   
2905 C CB  . GLN C 38  ? 0.97293 0.89420 0.92339 -0.12414 0.01522  -0.23566 38  GLN C CB  
2906 C CG  . GLN C 38  ? 0.98224 0.92364 0.93341 -0.12738 0.01799  -0.26268 38  GLN C CG  
2907 C CD  . GLN C 38  ? 1.02853 0.90399 0.98348 -0.13100 0.01993  -0.26447 38  GLN C CD  
2908 O OE1 . GLN C 38  ? 1.18462 1.02982 1.13416 -0.16292 0.02003  -0.26594 38  GLN C OE1 
2909 N NE2 . GLN C 38  ? 1.00084 0.84908 0.95961 -0.10100 0.02427  -0.26766 38  GLN C NE2 
2910 N N   . GLN C 39  ? 0.75947 0.85382 1.39298 -0.11011 0.13631  -0.38490 39  GLN C N   
2911 C CA  . GLN C 39  ? 0.75161 0.82913 1.39936 -0.10605 0.12119  -0.38925 39  GLN C CA  
2912 C C   . GLN C 39  ? 0.73623 0.80150 1.38142 -0.11308 0.11670  -0.39804 39  GLN C C   
2913 O O   . GLN C 39  ? 0.74001 0.82005 1.36899 -0.11725 0.12306  -0.40641 39  GLN C O   
2914 C CB  . GLN C 39  ? 0.71793 0.81470 1.37116 -0.09298 0.11247  -0.39625 39  GLN C CB  
2915 C CG  . GLN C 39  ? 0.76437 0.87093 1.42313 -0.08752 0.11555  -0.38904 39  GLN C CG  
2916 C CD  . GLN C 39  ? 0.78928 0.87462 1.46474 -0.08481 0.10658  -0.38535 39  GLN C CD  
2917 O OE1 . GLN C 39  ? 0.80727 0.87020 1.49412 -0.08570 0.09718  -0.38698 39  GLN C OE1 
2918 N NE2 . GLN C 39  ? 0.98615 1.07834 1.66494 -0.08159 0.10924  -0.38083 39  GLN C NE2 
2919 N N   . PRO C 40  ? 0.83521 0.87671 1.49147 -0.11212 0.10597  -0.39080 40  PRO C N   
2920 C CA  . PRO C 40  ? 0.71080 0.75849 1.33820 -0.10346 0.09812  -0.37459 40  PRO C CA  
2921 C C   . PRO C 40  ? 0.70905 0.77369 1.33442 -0.09204 0.08455  -0.39258 40  PRO C C   
2922 O O   . PRO C 40  ? 0.82595 0.88815 1.47798 -0.08727 0.07652  -0.40935 40  PRO C O   
2923 C CB  . PRO C 40  ? 0.79272 0.81587 1.42874 -0.09923 0.08982  -0.34957 40  PRO C CB  
2924 C CG  . PRO C 40  ? 0.78392 0.79185 1.45836 -0.10038 0.08617  -0.36319 40  PRO C CG  
2925 C CD  . PRO C 40  ? 0.74935 0.76606 1.43297 -0.11140 0.09964  -0.38416 40  PRO C CD  
2926 N N   . LYS C 41  ? 0.65020 0.73259 1.24452 -0.08758 0.08217  -0.38979 41  LYS C N   
2927 C CA  . LYS C 41  ? 0.74035 0.84202 1.33304 -0.07763 0.06944  -0.40893 41  LYS C CA  
2928 C C   . LYS C 41  ? 0.74758 0.85023 1.32001 -0.06499 0.05152  -0.39284 41  LYS C C   
2929 O O   . LYS C 41  ? 0.77461 0.87734 1.36403 -0.05455 0.03473  -0.40003 41  LYS C O   
2930 C CB  . LYS C 41  ? 0.83228 0.95900 1.40986 -0.08263 0.08022  -0.42724 41  LYS C CB  
2931 C CG  . LYS C 41  ? 0.75832 0.89041 1.36337 -0.09083 0.09252  -0.45036 41  LYS C CG  
2932 C CD  . LYS C 41  ? 0.78539 0.92126 1.41441 -0.07974 0.08195  -0.45091 41  LYS C CD  
2933 C CE  . LYS C 41  ? 1.07083 1.21618 1.70834 -0.07978 0.09392  -0.43492 41  LYS C CE  
2934 N NZ  . LYS C 41  ? 1.08901 1.22031 1.74627 -0.07355 0.08576  -0.42854 41  LYS C NZ  
2935 N N   . ARG C 42  ? 0.78098 0.88517 1.31747 -0.06528 0.05484  -0.37065 42  ARG C N   
2936 C CA  . ARG C 42  ? 0.76437 0.87394 1.27498 -0.05282 0.03788  -0.35532 42  ARG C CA  
2937 C C   . ARG C 42  ? 0.81993 0.91761 1.30195 -0.05428 0.04436  -0.32067 42  ARG C C   
2938 O O   . ARG C 42  ? 0.82813 0.91983 1.30374 -0.06554 0.06366  -0.31212 42  ARG C O   
2939 C CB  . ARG C 42  ? 0.74652 0.88499 1.23167 -0.04809 0.03230  -0.37366 42  ARG C CB  
2940 C CG  . ARG C 42  ? 1.03509 1.18730 1.48722 -0.05674 0.05030  -0.37424 42  ARG C CG  
2941 C CD  . ARG C 42  ? 1.04352 1.20063 1.44834 -0.05029 0.04575  -0.34967 42  ARG C CD  
2942 N NE  . ARG C 42  ? 0.81720 0.98020 1.19241 -0.05960 0.06684  -0.34288 42  ARG C NE  
2943 C CZ  . ARG C 42  ? 0.96749 1.15410 1.31277 -0.05953 0.07083  -0.35716 42  ARG C CZ  
2944 N NH1 . ARG C 42  ? 1.04300 1.25035 1.38423 -0.05111 0.05461  -0.38002 42  ARG C NH1 
2945 N NH2 . ARG C 42  ? 0.95778 1.14748 1.27948 -0.06833 0.09195  -0.34969 42  ARG C NH2 
2946 N N   . ALA C 43  ? 0.92134 1.01658 1.38713 -0.04233 0.02803  -0.29995 43  ALA C N   
2947 C CA  . ALA C 43  ? 0.97382 1.06129 1.40734 -0.04124 0.03300  -0.26496 43  ALA C CA  
2948 C C   . ALA C 43  ? 0.84983 0.94821 1.25563 -0.02577 0.01164  -0.25225 43  ALA C C   
2949 O O   . ALA C 43  ? 0.84586 0.94847 1.27040 -0.01601 -0.00839 -0.26431 43  ALA C O   
2950 C CB  . ALA C 43  ? 0.81292 0.87018 1.27339 -0.04565 0.03950  -0.24004 43  ALA C CB  
2951 N N   . ARG C 44  ? 0.99481 1.09813 1.35617 -0.02335 0.01617  -0.22727 44  ARG C N   
2952 C CA  . ARG C 44  ? 1.02606 1.13992 1.35469 -0.00843 -0.00361 -0.21012 44  ARG C CA  
2953 C C   . ARG C 44  ? 0.97747 1.06718 1.31196 -0.00350 -0.00606 -0.16917 44  ARG C C   
2954 O O   . ARG C 44  ? 0.98635 1.06068 1.31749 -0.01178 0.01339  -0.14673 44  ARG C O   
2955 C CB  . ARG C 44  ? 0.97039 1.10749 1.24165 -0.00778 0.00300  -0.20905 44  ARG C CB  
2956 C CG  . ARG C 44  ? 1.05338 1.20633 1.28524 0.00810  -0.01915 -0.19565 44  ARG C CG  
2957 C CD  . ARG C 44  ? 1.07291 1.24094 1.24444 0.00773  -0.00684 -0.18256 44  ARG C CD  
2958 N NE  . ARG C 44  ? 1.05052 1.24694 1.19869 0.00581  -0.00614 -0.21748 44  ARG C NE  
2959 C CZ  . ARG C 44  ? 1.09047 1.31138 1.19183 0.01588  -0.01975 -0.22104 44  ARG C CZ  
2960 N NH1 . ARG C 44  ? 1.14654 1.36821 1.21522 0.02887  -0.03489 -0.19016 44  ARG C NH1 
2961 N NH2 . ARG C 44  ? 1.07557 1.32124 1.16294 0.01300  -0.01822 -0.25630 44  ARG C NH2 
2962 N N   . ALA C 45  ? 0.99735 1.08351 1.34524 0.00981  -0.02960 -0.15964 45  ALA C N   
2963 C CA  . ALA C 45  ? 1.03145 1.09412 1.39200 0.01560  -0.03353 -0.12078 45  ALA C CA  
2964 C C   . ALA C 45  ? 1.07868 1.14054 1.39367 0.01545  -0.02024 -0.08466 45  ALA C C   
2965 O O   . ALA C 45  ? 1.22926 1.31363 1.49237 0.02098  -0.02327 -0.08215 45  ALA C O   
2966 C CB  . ALA C 45  ? 1.05481 1.12089 1.42532 0.03221  -0.06271 -0.11446 45  ALA C CB  
2967 N N   . CYS C 46  ? 1.08670 1.12271 1.42215 0.00950  -0.00552 -0.05673 46  CYS C N   
2968 C CA  . CYS C 46  ? 1.13020 1.16275 1.42860 0.00835  0.01070  -0.02029 46  CYS C CA  
2969 C C   . CYS C 46  ? 1.18715 1.21195 1.47444 0.02291  -0.00307 0.02181  46  CYS C C   
2970 O O   . CYS C 46  ? 1.30919 1.33102 1.56469 0.02406  0.00957  0.05688  46  CYS C O   
2971 C CB  . CYS C 46  ? 1.10780 1.11854 1.43416 -0.00754 0.03722  -0.01320 46  CYS C CB  
2972 S SG  . CYS C 46  ? 1.14645 1.12014 1.53944 -0.00961 0.03643  0.00677  46  CYS C SG  
2973 N N   . GLY C 47  ? 1.18936 1.21131 1.50312 0.03434  -0.02800 0.02002  47  GLY C N   
2974 C CA  . GLY C 47  ? 1.25048 1.26333 1.56269 0.04850  -0.04241 0.06059  47  GLY C CA  
2975 C C   . GLY C 47  ? 1.33375 1.36934 1.62216 0.06498  -0.07205 0.05543  47  GLY C C   
2976 O O   . GLY C 47  ? 1.44772 1.47797 1.73895 0.07855  -0.08881 0.08650  47  GLY C O   
2977 N N   . GLN C 48  ? 1.40513 1.46661 1.67241 0.06408  -0.07922 0.01660  48  GLN C N   
2978 C CA  . GLN C 48  ? 1.52296 1.60760 1.77402 0.07878  -0.10894 0.00522  48  GLN C CA  
2979 C C   . GLN C 48  ? 1.47001 1.58666 1.67125 0.07694  -0.10856 -0.02439 48  GLN C C   
2980 O O   . GLN C 48  ? 1.41379 1.53363 1.60890 0.06319  -0.08685 -0.04662 48  GLN C O   
2981 C CB  . GLN C 48  ? 1.44055 1.51914 1.75134 0.08118  -0.12620 -0.02237 48  GLN C CB  
2982 C CG  . GLN C 48  ? 1.59571 1.64459 1.96117 0.08500  -0.13100 0.00140  48  GLN C CG  
2983 C CD  . GLN C 48  ? 1.57953 1.62300 2.00349 0.08517  -0.14296 -0.03166 48  GLN C CD  
2984 O OE1 . GLN C 48  ? 1.32671 1.38779 1.75156 0.08150  -0.14568 -0.07141 48  GLN C OE1 
2985 N NE2 . GLN C 48  ? 1.65508 1.67427 2.12971 0.08971  -0.14934 -0.01531 48  GLN C NE2 
2986 N N   . GLY C 49  ? 1.32715 1.46794 1.49458 0.09125  -0.13361 -0.02453 49  GLY C N   
2987 C CA  . GLY C 49  ? 1.29309 1.46614 1.41642 0.09160  -0.13825 -0.05514 49  GLY C CA  
2988 C C   . GLY C 49  ? 1.32738 1.50978 1.38868 0.08706  -0.11693 -0.04018 49  GLY C C   
2989 O O   . GLY C 49  ? 1.40682 1.57626 1.44645 0.08906  -0.10562 0.00166  49  GLY C O   
2990 N N   . SER C 50  ? 1.31081 1.51666 1.34527 0.08114  -0.11095 -0.07566 50  SER C N   
2991 C CA  . SER C 50  ? 1.34023 1.55812 1.31616 0.07638  -0.08987 -0.06885 50  SER C CA  
2992 C C   . SER C 50  ? 1.43970 1.63132 1.43052 0.06284  -0.05678 -0.04713 50  SER C C   
2993 O O   . SER C 50  ? 1.32703 1.49906 1.37244 0.05173  -0.04607 -0.05972 50  SER C O   
2994 C CB  . SER C 50  ? 1.31262 1.55682 1.27300 0.07006  -0.08697 -0.11650 50  SER C CB  
2995 O OG  . SER C 50  ? 1.34204 1.59418 1.25613 0.06250  -0.06110 -0.11370 50  SER C OG  
2996 N N   . LYS C 51  ? 1.59600 1.78773 1.53846 0.06389  -0.04040 -0.01438 51  LYS C N   
2997 C CA  . LYS C 51  ? 1.53016 1.69914 1.48577 0.05077  -0.00791 0.00587  51  LYS C CA  
2998 C C   . LYS C 51  ? 1.50870 1.69195 1.43186 0.03932  0.01795  -0.01428 51  LYS C C   
2999 O O   . LYS C 51  ? 1.46117 1.63136 1.37889 0.03039  0.04594  0.00704  51  LYS C O   
3000 C CB  . LYS C 51  ? 1.72864 1.88236 1.66492 0.05862  -0.00308 0.06130  51  LYS C CB  
3001 C CG  . LYS C 51  ? 1.72707 1.86374 1.70272 0.06931  -0.02647 0.08379  51  LYS C CG  
3002 C CD  . LYS C 51  ? 1.81358 1.93020 1.78309 0.07447  -0.01670 0.13999  51  LYS C CD  
3003 C CE  . LYS C 51  ? 1.87269 1.96979 1.89103 0.08394  -0.03820 0.16102  51  LYS C CE  
3004 N NZ  . LYS C 51  ? 1.90960 1.98394 1.93327 0.08784  -0.02692 0.21614  51  LYS C NZ  
3005 N N   . SER C 52  ? 1.43109 1.64088 1.33622 0.03948  0.00922  -0.05520 52  SER C N   
3006 C CA  . SER C 52  ? 1.37276 1.59844 1.25161 0.02914  0.03163  -0.08022 52  SER C CA  
3007 C C   . SER C 52  ? 1.31724 1.53159 1.25382 0.01318  0.04568  -0.11047 52  SER C C   
3008 O O   . SER C 52  ? 1.27215 1.47097 1.26240 0.01184  0.03448  -0.11703 52  SER C O   
3009 C CB  . SER C 52  ? 1.34926 1.60947 1.18346 0.03755  0.01437  -0.11037 52  SER C CB  
3010 O OG  . SER C 52  ? 1.58481 1.85703 1.36312 0.05314  -0.00076 -0.08233 52  SER C OG  
3011 N N   . HIS C 53  ? 1.23542 1.45892 1.16053 0.00157  0.06992  -0.13001 53  HIS C N   
3012 C CA  . HIS C 53  ? 1.27528 1.49175 1.25084 -0.01339 0.08372  -0.15958 53  HIS C CA  
3013 C C   . HIS C 53  ? 1.13815 1.32279 1.16832 -0.01967 0.08829  -0.14016 53  HIS C C   
3014 O O   . HIS C 53  ? 1.09788 1.27415 1.17501 -0.02028 0.07446  -0.15658 53  HIS C O   
3015 C CB  . HIS C 53  ? 1.25777 1.49326 1.25260 -0.01155 0.06475  -0.20461 53  HIS C CB  
3016 C CG  . HIS C 53  ? 1.19079 1.45765 1.13517 -0.00323 0.05418  -0.22419 53  HIS C CG  
3017 N ND1 . HIS C 53  ? 1.17207 1.45699 1.09315 -0.01063 0.07280  -0.24761 53  HIS C ND1 
3018 C CD2 . HIS C 53  ? 1.22694 1.51100 1.14168 0.01181  0.02622  -0.22559 53  HIS C CD2 
3019 C CE1 . HIS C 53  ? 1.28574 1.59741 1.16370 -0.00066 0.05717  -0.26351 53  HIS C CE1 
3020 N NE2 . HIS C 53  ? 1.25318 1.56537 1.12576 0.01308  0.02813  -0.25053 53  HIS C NE2 
3021 N N   . THR C 54  ? 1.23869 1.72463 0.81936 -0.03961 0.13962  -0.15877 54  THR C N   
3022 C CA  . THR C 54  ? 1.13561 1.60018 0.77274 -0.01815 0.13552  -0.12008 54  THR C CA  
3023 C C   . THR C 54  ? 1.11160 1.50695 0.79304 -0.01485 0.12648  -0.13693 54  THR C C   
3024 O O   . THR C 54  ? 1.15832 1.53676 0.87265 -0.00721 0.11001  -0.11349 54  THR C O   
3025 C CB  . THR C 54  ? 1.13700 1.61402 0.79360 -0.00042 0.16161  -0.09635 54  THR C CB  
3026 O OG1 . THR C 54  ? 1.22222 1.67035 0.88691 0.00114  0.18447  -0.13012 54  THR C OG1 
3027 C CG2 . THR C 54  ? 1.08706 1.63404 0.69715 -0.00221 0.16962  -0.07234 54  THR C CG2 
3028 N N   . ASP C 55  ? 1.08653 1.44046 0.76959 -0.01869 0.13778  -0.17613 55  ASP C N   
3029 C CA  . ASP C 55  ? 1.10693 1.39734 0.83412 -0.01191 0.12895  -0.18592 55  ASP C CA  
3030 C C   . ASP C 55  ? 1.15740 1.43140 0.87607 -0.02617 0.10154  -0.18836 55  ASP C C   
3031 O O   . ASP C 55  ? 1.23093 1.45411 0.97906 -0.02277 0.09107  -0.19403 55  ASP C O   
3032 C CB  . ASP C 55  ? 1.09067 1.33885 0.82102 -0.01055 0.14693  -0.22599 55  ASP C CB  
3033 C CG  . ASP C 55  ? 1.31419 1.50751 1.10208 0.00618  0.14329  -0.22485 55  ASP C CG  
3034 O OD1 . ASP C 55  ? 1.45071 1.64087 1.27414 0.01492  0.12800  -0.19463 55  ASP C OD1 
3035 O OD2 . ASP C 55  ? 1.40318 1.55673 1.20005 0.01101  0.15542  -0.25450 55  ASP C OD2 
3036 N N   . ARG C 56  ? 1.14049 1.46132 0.81963 -0.04220 0.08978  -0.18275 56  ARG C N   
3037 C CA  . ARG C 56  ? 1.21066 1.52752 0.88451 -0.05632 0.06527  -0.18131 56  ARG C CA  
3038 C C   . ARG C 56  ? 1.11297 1.44768 0.81543 -0.04167 0.05174  -0.13889 56  ARG C C   
3039 O O   . ARG C 56  ? 1.09545 1.43076 0.79863 -0.04990 0.03292  -0.13338 56  ARG C O   
3040 C CB  . ARG C 56  ? 1.13945 1.50438 0.76007 -0.08296 0.05818  -0.19852 56  ARG C CB  
3041 C CG  . ARG C 56  ? 1.22157 1.56820 0.80625 -0.10145 0.07251  -0.24556 56  ARG C CG  
3042 C CD  . ARG C 56  ? 1.12671 1.45066 0.68948 -0.13153 0.05854  -0.27664 56  ARG C CD  
3043 N NE  . ARG C 56  ? 1.21201 1.52201 0.73328 -0.15299 0.07285  -0.32399 56  ARG C NE  
3044 C CZ  . ARG C 56  ? 1.23245 1.60036 0.70299 -0.17508 0.07333  -0.34028 56  ARG C CZ  
3045 N NH1 . ARG C 56  ? 1.38306 1.83157 0.83922 -0.17675 0.05936  -0.30963 56  ARG C NH1 
3046 N NH2 . ARG C 56  ? 1.26685 1.61173 0.69953 -0.19505 0.08852  -0.38860 56  ARG C NH2 
3047 N N   . ARG C 57  ? 1.09588 1.44280 0.82258 -0.02073 0.06297  -0.10977 57  ARG C N   
3048 C CA  . ARG C 57  ? 1.03195 1.39190 0.78433 -0.00573 0.05421  -0.07008 57  ARG C CA  
3049 C C   . ARG C 57  ? 0.94740 1.25045 0.74686 0.00559  0.04872  -0.06635 57  ARG C C   
3050 O O   . ARG C 57  ? 0.91829 1.21542 0.73067 0.00880  0.03385  -0.05060 57  ARG C O   
3051 C CB  . ARG C 57  ? 0.94249 1.34339 0.69295 0.00810  0.07036  -0.03950 57  ARG C CB  
3052 C CG  . ARG C 57  ? 1.18050 1.64193 0.87812 -0.00425 0.07438  -0.04496 57  ARG C CG  
3053 C CD  . ARG C 57  ? 1.07286 1.59287 0.75842 0.00741  0.07562  -0.00195 57  ARG C CD  
3054 N NE  . ARG C 57  ? 1.09915 1.61690 0.80308 0.02436  0.09783  0.02350  57  ARG C NE  
3055 C CZ  . ARG C 57  ? 1.30489 1.87173 0.97846 0.02714  0.11237  0.04149  57  ARG C CZ  
3056 N NH1 . ARG C 57  ? 1.36331 1.99064 0.98621 0.01587  0.10437  0.03960  57  ARG C NH1 
3057 N NH2 . ARG C 57  ? 1.22338 1.78190 0.91765 0.04029  0.13506  0.06341  57  ARG C NH2 
3058 N N   . PRO C 58  ? 0.83078 1.09695 0.65784 0.01306  0.06051  -0.07839 58  PRO C N   
3059 C CA  . PRO C 58  ? 0.80200 1.01976 0.67156 0.02164  0.05146  -0.07646 58  PRO C CA  
3060 C C   . PRO C 58  ? 0.81588 1.00832 0.67610 0.01107  0.03054  -0.08787 58  PRO C C   
3061 O O   . PRO C 58  ? 1.06852 1.25623 0.89954 -0.00452 0.02718  -0.11207 58  PRO C O   
3062 C CB  . PRO C 58  ? 0.81602 1.00725 0.70688 0.02687  0.06579  -0.09710 58  PRO C CB  
3063 C CG  . PRO C 58  ? 0.86811 1.09960 0.74295 0.02878  0.08795  -0.09271 58  PRO C CG  
3064 C CD  . PRO C 58  ? 0.85960 1.13046 0.68262 0.01503  0.08296  -0.09415 58  PRO C CD  
3065 N N   . VAL C 59  ? 0.82951 1.00446 0.71337 0.01804  0.01787  -0.07108 59  VAL C N   
3066 C CA  . VAL C 59  ? 0.84855 1.00154 0.72360 0.00856  -0.00032 -0.07860 59  VAL C CA  
3067 C C   . VAL C 59  ? 0.94420 1.05093 0.82226 0.00286  -0.00287 -0.10488 59  VAL C C   
3068 O O   . VAL C 59  ? 0.87364 0.95191 0.78277 0.01431  0.00040  -0.10758 59  VAL C O   
3069 C CB  . VAL C 59  ? 0.75685 0.89692 0.65629 0.01882  -0.01051 -0.05799 59  VAL C CB  
3070 C CG1 . VAL C 59  ? 0.86985 0.99510 0.75496 0.00832  -0.02688 -0.06402 59  VAL C CG1 
3071 C CG2 . VAL C 59  ? 0.89637 1.07491 0.79732 0.02883  -0.00407 -0.03018 59  VAL C CG2 
3072 N N   . ASP C 60  ? 1.04303 1.14295 0.89063 -0.01506 -0.00849 -0.12342 60  ASP C N   
3073 C CA  . ASP C 60  ? 0.88527 0.93586 0.73159 -0.02087 -0.00915 -0.14736 60  ASP C CA  
3074 C C   . ASP C 60  ? 0.93688 0.96127 0.77186 -0.03391 -0.02561 -0.14858 60  ASP C C   
3075 O O   . ASP C 60  ? 1.01454 1.06891 0.83060 -0.04633 -0.03329 -0.14079 60  ASP C O   
3076 C CB  . ASP C 60  ? 0.92865 0.98528 0.74526 -0.03392 0.00486  -0.17421 60  ASP C CB  
3077 C CG  . ASP C 60  ? 1.20703 1.21367 1.03660 -0.02675 0.01527  -0.19645 60  ASP C CG  
3078 O OD1 . ASP C 60  ? 1.20574 1.20887 1.06867 -0.00638 0.02421  -0.19029 60  ASP C OD1 
3079 O OD2 . ASP C 60  ? 1.23539 1.20759 1.04321 -0.04157 0.01621  -0.22025 60  ASP C OD2 
3080 N N   . PRO C 61  ? 0.88624 0.85767 0.73374 -0.03038 -0.03080 -0.15595 61  PRO C N   
3081 C CA  . PRO C 61  ? 0.95486 0.89481 0.83481 -0.01096 -0.02549 -0.15922 61  PRO C CA  
3082 C C   . PRO C 61  ? 0.92559 0.88192 0.84069 0.00691  -0.03029 -0.13707 61  PRO C C   
3083 O O   . PRO C 61  ? 0.84887 0.81716 0.76289 0.00533  -0.04167 -0.12082 61  PRO C O   
3084 C CB  . PRO C 61  ? 1.01091 0.89523 0.88892 -0.01426 -0.03540 -0.16585 61  PRO C CB  
3085 C CG  . PRO C 61  ? 0.96218 0.85304 0.81731 -0.03098 -0.04945 -0.15568 61  PRO C CG  
3086 C CD  . PRO C 61  ? 0.96820 0.90952 0.79866 -0.04595 -0.04314 -0.15884 61  PRO C CD  
3087 N N   . PRO C 62  ? 0.94242 0.90014 0.88932 0.02275  -0.02001 -0.13775 62  PRO C N   
3088 C CA  . PRO C 62  ? 0.76546 0.73825 0.74893 0.03589  -0.02319 -0.11898 62  PRO C CA  
3089 C C   . PRO C 62  ? 0.86942 0.81774 0.86470 0.03799  -0.04438 -0.10923 62  PRO C C   
3090 O O   . PRO C 62  ? 0.83385 0.74815 0.83500 0.04130  -0.05382 -0.11542 62  PRO C O   
3091 C CB  . PRO C 62  ? 0.79762 0.76928 0.81572 0.05005  -0.00930 -0.12647 62  PRO C CB  
3092 C CG  . PRO C 62  ? 0.81251 0.75103 0.81566 0.04885  -0.00478 -0.14848 62  PRO C CG  
3093 C CD  . PRO C 62  ? 0.88564 0.82891 0.83934 0.02905  -0.00373 -0.15752 62  PRO C CD  
3094 N N   . PRO C 63  ? 0.88003 0.84352 0.87548 0.03648  -0.05174 -0.09379 63  PRO C N   
3095 C CA  . PRO C 63  ? 0.79761 0.73947 0.79599 0.03637  -0.07118 -0.08723 63  PRO C CA  
3096 C C   . PRO C 63  ? 0.85039 0.77632 0.88700 0.04762  -0.07970 -0.08744 63  PRO C C   
3097 O O   . PRO C 63  ? 0.85297 0.79496 0.92400 0.05572  -0.07083 -0.08589 63  PRO C O   
3098 C CB  . PRO C 63  ? 0.70046 0.66409 0.69691 0.03572  -0.07091 -0.07306 63  PRO C CB  
3099 C CG  . PRO C 63  ? 0.76947 0.76563 0.75031 0.03305  -0.05467 -0.07007 63  PRO C CG  
3100 C CD  . PRO C 63  ? 0.71376 0.71330 0.70276 0.03547  -0.04162 -0.08143 63  PRO C CD  
3101 N N   . VAL C 64  ? 0.83908 0.73705 0.86971 0.04744  -0.09732 -0.08763 64  VAL C N   
3102 C CA  . VAL C 64  ? 0.85544 0.74177 0.91909 0.05820  -0.11100 -0.08554 64  VAL C CA  
3103 C C   . VAL C 64  ? 0.80990 0.68661 0.86207 0.05366  -0.13198 -0.07778 64  VAL C C   
3104 O O   . VAL C 64  ? 0.88014 0.74031 0.89517 0.04511  -0.13837 -0.07616 64  VAL C O   
3105 C CB  . VAL C 64  ? 0.86852 0.72756 0.93473 0.06622  -0.11151 -0.09227 64  VAL C CB  
3106 C CG1 . VAL C 64  ? 0.80586 0.65587 0.90185 0.07849  -0.13105 -0.08506 64  VAL C CG1 
3107 C CG2 . VAL C 64  ? 0.82323 0.69328 0.90587 0.07305  -0.08885 -0.10332 64  VAL C CG2 
3108 N N   . ILE C 65  ? 0.81334 0.70231 0.89660 0.05744  -0.14161 -0.07422 65  ILE C N   
3109 C CA  . ILE C 65  ? 0.74985 0.63293 0.82272 0.05226  -0.16094 -0.07040 65  ILE C CA  
3110 C C   . ILE C 65  ? 0.79834 0.68196 0.90171 0.05994  -0.18098 -0.06855 65  ILE C C   
3111 O O   . ILE C 65  ? 0.76821 0.67104 0.91693 0.06720  -0.17790 -0.06988 65  ILE C O   
3112 C CB  . ILE C 65  ? 0.86268 0.76026 0.93991 0.04591  -0.15473 -0.07004 65  ILE C CB  
3113 C CG1 . ILE C 65  ? 0.83502 0.73971 0.88688 0.04222  -0.13517 -0.06773 65  ILE C CG1 
3114 C CG2 . ILE C 65  ? 0.76772 0.65529 0.82783 0.03971  -0.17322 -0.07077 65  ILE C CG2 
3115 C CD1 . ILE C 65  ? 0.78431 0.70696 0.85127 0.04622  -0.11434 -0.06738 65  ILE C CD1 
3116 N N   . GLU C 66  ? 0.87607 0.74277 0.95465 0.05849  -0.20123 -0.06394 66  GLU C N   
3117 C CA  . GLU C 66  ? 0.77744 0.64702 0.87681 0.06636  -0.22487 -0.05855 66  GLU C CA  
3118 C C   . GLU C 66  ? 0.99394 0.87617 1.09049 0.05656  -0.24316 -0.06094 66  GLU C C   
3119 O O   . GLU C 66  ? 0.87167 0.74370 0.92934 0.04564  -0.24263 -0.06367 66  GLU C O   
3120 C CB  . GLU C 66  ? 0.92168 0.76144 0.98951 0.07139  -0.23520 -0.04898 66  GLU C CB  
3121 C CG  . GLU C 66  ? 1.28683 1.12788 1.35139 0.07513  -0.26455 -0.03878 66  GLU C CG  
3122 C CD  . GLU C 66  ? 1.31322 1.12093 1.34936 0.08239  -0.27213 -0.02456 66  GLU C CD  
3123 O OE1 . GLU C 66  ? 1.27759 1.07031 1.33433 0.09665  -0.26374 -0.02117 66  GLU C OE1 
3124 O OE2 . GLU C 66  ? 1.44691 1.24112 1.43934 0.07385  -0.28449 -0.01672 66  GLU C OE2 
3125 N N   . LEU C 67  ? 0.87109 0.77821 1.01087 0.05975  -0.25797 -0.06177 67  LEU C N   
3126 C CA  . LEU C 67  ? 0.89264 0.81473 1.03533 0.04734  -0.27563 -0.06859 67  LEU C CA  
3127 C C   . LEU C 67  ? 0.84425 0.78017 0.99463 0.05277  -0.30741 -0.06123 67  LEU C C   
3128 O O   . LEU C 67  ? 0.84950 0.80331 1.04142 0.06725  -0.31397 -0.05339 67  LEU C O   
3129 C CB  . LEU C 67  ? 0.76721 0.71374 0.95853 0.04024  -0.26498 -0.07777 67  LEU C CB  
3130 C CG  . LEU C 67  ? 0.78059 0.74510 0.98721 0.02502  -0.28468 -0.08804 67  LEU C CG  
3131 C CD1 . LEU C 67  ? 0.79718 0.73796 0.95111 0.01158  -0.28738 -0.09741 67  LEU C CD1 
3132 C CD2 . LEU C 67  ? 0.83903 0.82621 1.10099 0.01678  -0.27140 -0.09488 67  LEU C CD2 
3133 N N   . ASN C 68  ? 0.86595 0.79717 0.97720 0.04219  -0.32667 -0.06351 68  ASN C N   
3134 C CA  . ASN C 68  ? 0.86721 0.81836 0.98019 0.04440  -0.36022 -0.05656 68  ASN C CA  
3135 C C   . ASN C 68  ? 0.88059 0.84815 0.98494 0.02389  -0.37527 -0.07364 68  ASN C C   
3136 O O   . ASN C 68  ? 0.98699 0.93467 1.05885 0.01045  -0.36117 -0.08723 68  ASN C O   
3137 C CB  . ASN C 68  ? 0.91694 0.84318 0.97797 0.05210  -0.37167 -0.03958 68  ASN C CB  
3138 C CG  . ASN C 68  ? 1.04039 0.94838 1.11504 0.07251  -0.36185 -0.02290 68  ASN C CG  
3139 O OD1 . ASN C 68  ? 0.90989 0.83555 1.02396 0.08938  -0.37526 -0.01126 68  ASN C OD1 
3140 N ND2 . ASN C 68  ? 0.91698 0.79015 0.95994 0.07103  -0.33808 -0.02246 68  ASN C ND2 
3141 N N   . ILE C 69  ? 0.89801 0.90296 1.03221 0.02177  -0.40399 -0.07362 69  ILE C N   
3142 C CA  . ILE C 69  ? 0.91833 0.94270 1.04819 -0.00080 -0.42150 -0.09328 69  ILE C CA  
3143 C C   . ILE C 69  ? 0.96835 1.01405 1.07007 -0.00018 -0.45916 -0.08443 69  ILE C C   
3144 O O   . ILE C 69  ? 1.07623 1.14720 1.20502 0.01750  -0.47813 -0.06401 69  ILE C O   
3145 C CB  . ILE C 69  ? 0.92409 0.98448 1.12506 -0.01076 -0.42104 -0.10527 69  ILE C CB  
3146 C CG1 . ILE C 69  ? 0.86341 0.90376 1.08994 -0.00980 -0.38272 -0.10939 69  ILE C CG1 
3147 C CG2 . ILE C 69  ? 0.92995 1.00645 1.12510 -0.03850 -0.43927 -0.12918 69  ILE C CG2 
3148 C CD1 . ILE C 69  ? 0.91988 0.99784 1.22349 -0.00834 -0.37756 -0.10830 69  ILE C CD1 
3149 N N   . PHE C 70  ? 1.09465 1.13129 1.14175 -0.01810 -0.46931 -0.09920 70  PHE C N   
3150 C CA  . PHE C 70  ? 1.04097 1.09630 1.04682 -0.01942 -0.50381 -0.09074 70  PHE C CA  
3151 C C   . PHE C 70  ? 1.08018 1.16411 1.08064 -0.04624 -0.52588 -0.11810 70  PHE C C   
3152 O O   . PHE C 70  ? 1.14944 1.21202 1.13800 -0.06576 -0.50789 -0.14598 70  PHE C O   
3153 C CB  . PHE C 70  ? 1.12765 1.14290 1.05657 -0.01564 -0.49448 -0.08099 70  PHE C CB  
3154 C CG  . PHE C 70  ? 1.04032 1.02575 0.97005 0.00631  -0.47474 -0.05574 70  PHE C CG  
3155 C CD1 . PHE C 70  ? 1.20443 1.19565 1.13717 0.02636  -0.49236 -0.02563 70  PHE C CD1 
3156 C CD2 . PHE C 70  ? 1.00532 0.95672 0.93325 0.00663  -0.43863 -0.06223 70  PHE C CD2 
3157 C CE1 . PHE C 70  ? 1.04730 1.00444 0.98010 0.04396  -0.47242 -0.00589 70  PHE C CE1 
3158 C CE2 . PHE C 70  ? 1.09443 1.01954 1.02136 0.02270  -0.42113 -0.04292 70  PHE C CE2 
3159 C CZ  . PHE C 70  ? 1.01248 0.93732 0.94147 0.04017  -0.43712 -0.01649 70  PHE C CZ  
3160 N N   . GLU C 71  ? 1.10488 1.23707 1.11438 -0.04691 -0.56497 -0.11003 71  GLU C N   
3161 C CA  . GLU C 71  ? 1.14711 1.31234 1.14226 -0.07448 -0.59260 -0.13581 71  GLU C CA  
3162 C C   . GLU C 71  ? 1.20207 1.36227 1.11241 -0.07718 -0.61251 -0.13080 71  GLU C C   
3163 O O   . GLU C 71  ? 1.33529 1.49463 1.22109 -0.05505 -0.62295 -0.09738 71  GLU C O   
3164 C CB  . GLU C 71  ? 1.15076 1.38557 1.21357 -0.07644 -0.62628 -0.13111 71  GLU C CB  
3165 C CG  . GLU C 71  ? 1.25667 1.52126 1.34117 -0.11274 -0.63909 -0.16877 71  GLU C CG  
3166 C CD  . GLU C 71  ? 1.43842 1.77681 1.60596 -0.11563 -0.66652 -0.16385 71  GLU C CD  
3167 O OE1 . GLU C 71  ? 1.21129 1.59870 1.38853 -0.09750 -0.70014 -0.13666 71  GLU C OE1 
3168 O OE2 . GLU C 71  ? 1.55635 1.90530 1.78128 -0.13566 -0.65381 -0.18549 71  GLU C OE2 
3169 N N   . SER C 72  ? 1.30898 1.46344 1.17329 -0.10463 -0.61598 -0.16420 72  SER C N   
3170 C CA  . SER C 72  ? 1.41150 1.55929 1.18824 -0.10944 -0.62955 -0.16352 72  SER C CA  
3171 C C   . SER C 72  ? 1.53138 1.70098 1.27894 -0.14304 -0.64929 -0.20380 72  SER C C   
3172 O O   . SER C 72  ? 1.50375 1.67640 1.29349 -0.16437 -0.64317 -0.23567 72  SER C O   
3173 C CB  . SER C 72  ? 1.31536 1.40191 1.03821 -0.10148 -0.59098 -0.16159 72  SER C CB  
3174 O OG  . SER C 72  ? 1.60744 1.68530 1.24693 -0.11557 -0.59574 -0.17688 72  SER C OG  
3175 N N   . ASP C 73  ? 1.79778 1.98146 1.47094 -0.14884 -0.67242 -0.20209 73  ASP C N   
3176 C CA  . ASP C 73  ? 1.90127 2.09787 1.52529 -0.18080 -0.68423 -0.24282 73  ASP C CA  
3177 C C   . ASP C 73  ? 2.04163 2.17837 1.59073 -0.18584 -0.65165 -0.26407 73  ASP C C   
3178 O O   . ASP C 73  ? 2.08108 2.19695 1.58144 -0.16688 -0.64013 -0.23648 73  ASP C O   
3179 C CB  . ASP C 73  ? 2.00586 2.26906 1.59925 -0.18167 -0.71572 -0.22591 73  ASP C CB  
3180 C CG  . ASP C 73  ? 2.11646 2.44928 1.78604 -0.17804 -0.74792 -0.20880 73  ASP C CG  
3181 O OD1 . ASP C 73  ? 2.09564 2.42288 1.84227 -0.17104 -0.74452 -0.20415 73  ASP C OD1 
3182 O OD2 . ASP C 73  ? 2.15353 2.55093 1.80747 -0.18050 -0.77601 -0.20038 73  ASP C OD2 
3183 N N   . PRO C 74  ? 2.43646 1.81587 1.34019 -0.13441 -0.35978 -0.19453 74  PRO C N   
3184 C CA  . PRO C 74  ? 2.30841 1.68326 1.16928 -0.11458 -0.30653 -0.22891 74  PRO C CA  
3185 C C   . PRO C 74  ? 2.53090 1.85640 1.26961 -0.11948 -0.28479 -0.24447 74  PRO C C   
3186 O O   . PRO C 74  ? 2.42966 1.77665 1.14524 -0.10397 -0.22952 -0.26579 74  PRO C O   
3187 C CB  . PRO C 74  ? 2.27590 1.61069 1.13184 -0.10495 -0.32785 -0.25116 74  PRO C CB  
3188 C CG  . PRO C 74  ? 2.12503 1.45694 1.03634 -0.12433 -0.38874 -0.22474 74  PRO C CG  
3189 C CD  . PRO C 74  ? 2.22355 1.57123 1.14383 -0.14349 -0.41300 -0.19214 74  PRO C CD  
3190 N N   . HIS C 75  ? 2.65320 1.93127 1.33920 -0.13874 -0.32006 -0.22907 75  HIS C N   
3191 C CA  . HIS C 75  ? 2.90537 2.15335 1.50443 -0.14250 -0.29212 -0.23667 75  HIS C CA  
3192 C C   . HIS C 75  ? 2.92202 2.21281 1.51977 -0.14976 -0.25512 -0.22254 75  HIS C C   
3193 O O   . HIS C 75  ? 2.98767 2.28653 1.53574 -0.14619 -0.20632 -0.23653 75  HIS C O   
3194 C CB  . HIS C 75  ? 3.15222 2.33710 1.70318 -0.16154 -0.34145 -0.22091 75  HIS C CB  
3195 C CG  . HIS C 75  ? 3.35369 2.54993 1.94876 -0.18023 -0.38758 -0.18311 75  HIS C CG  
3196 N ND1 . HIS C 75  ? 3.35827 2.56124 1.93311 -0.19157 -0.38051 -0.16228 75  HIS C ND1 
3197 C CD2 . HIS C 75  ? 3.30465 2.50902 1.96572 -0.18813 -0.44170 -0.16160 75  HIS C CD2 
3198 C CE1 . HIS C 75  ? 3.24196 2.45404 1.86722 -0.20124 -0.42849 -0.13144 75  HIS C CE1 
3199 N NE2 . HIS C 75  ? 3.31438 2.53337 1.99599 -0.19943 -0.46504 -0.13005 75  HIS C NE2 
3200 N N   . ASP C 76  ? 2.77832 2.09848 1.43144 -0.16012 -0.27765 -0.19369 76  ASP C N   
3201 C CA  . ASP C 76  ? 2.74124 2.09309 1.39354 -0.16959 -0.24990 -0.17576 76  ASP C CA  
3202 C C   . ASP C 76  ? 2.53136 1.95662 1.28948 -0.15749 -0.22965 -0.16803 76  ASP C C   
3203 O O   . ASP C 76  ? 2.38745 1.83640 1.22689 -0.15475 -0.26261 -0.14644 76  ASP C O   
3204 C CB  . ASP C 76  ? 2.77715 2.09903 1.41447 -0.18754 -0.29251 -0.14319 76  ASP C CB  
3205 C CG  . ASP C 76  ? 2.60379 1.93804 1.21664 -0.19968 -0.26399 -0.12624 76  ASP C CG  
3206 O OD1 . ASP C 76  ? 2.52971 1.90296 1.14249 -0.19751 -0.21074 -0.13757 76  ASP C OD1 
3207 O OD2 . ASP C 76  ? 2.59088 1.89554 1.18659 -0.21207 -0.29637 -0.10042 76  ASP C OD2 
3208 N N   . ASP C 77  ? 2.59774 2.06980 1.37124 -0.14823 -0.17228 -0.18282 77  ASP C N   
3209 C CA  . ASP C 77  ? 2.51316 2.06018 1.39672 -0.13531 -0.14747 -0.17581 77  ASP C CA  
3210 C C   . ASP C 77  ? 2.42759 2.00199 1.32486 -0.14922 -0.13189 -0.15019 77  ASP C C   
3211 O O   . ASP C 77  ? 2.31239 1.94225 1.29237 -0.14129 -0.11322 -0.14217 77  ASP C O   
3212 C CB  . ASP C 77  ? 2.61745 2.20360 1.51904 -0.11629 -0.09831 -0.20505 77  ASP C CB  
3213 C CG  . ASP C 77  ? 2.64532 2.20824 1.55830 -0.09669 -0.11672 -0.22877 77  ASP C CG  
3214 O OD1 . ASP C 77  ? 2.61011 2.13940 1.53636 -0.10130 -0.16739 -0.21867 77  ASP C OD1 
3215 O OD2 . ASP C 77  ? 2.71322 2.29130 1.62170 -0.07679 -0.08198 -0.25668 77  ASP C OD2 
3216 N N   . SER C 78  ? 2.47649 2.00591 1.28833 -0.17096 -0.14174 -0.13676 78  SER C N   
3217 C CA  . SER C 78  ? 2.33339 1.87387 1.14245 -0.18693 -0.13092 -0.11197 78  SER C CA  
3218 C C   . SER C 78  ? 2.30607 1.83594 1.16245 -0.18369 -0.17586 -0.08351 78  SER C C   
3219 O O   . SER C 78  ? 2.39542 1.93239 1.26130 -0.19100 -0.16985 -0.06325 78  SER C O   
3220 C CB  . SER C 78  ? 2.36080 1.85271 1.04847 -0.21388 -0.12075 -0.10915 78  SER C CB  
3221 O OG  . SER C 78  ? 2.25863 1.78643 0.92598 -0.21508 -0.06480 -0.12981 78  SER C OG  
3222 N N   . ASN C 79  ? 2.24324 1.75658 1.12845 -0.17270 -0.22084 -0.08114 79  ASN C N   
3223 C CA  . ASN C 79  ? 2.16290 1.67606 1.10133 -0.16483 -0.26361 -0.05479 79  ASN C CA  
3224 C C   . ASN C 79  ? 1.95508 1.51866 1.00187 -0.14410 -0.27210 -0.05817 79  ASN C C   
3225 O O   . ASN C 79  ? 2.04431 1.60466 1.09567 -0.14144 -0.28125 -0.07537 79  ASN C O   
3226 C CB  . ASN C 79  ? 2.21983 1.66997 1.09199 -0.17567 -0.31658 -0.04188 79  ASN C CB  
3227 C CG  . ASN C 79  ? 2.40481 1.79481 1.14891 -0.20000 -0.30681 -0.04748 79  ASN C CG  
3228 O OD1 . ASN C 79  ? 2.46133 1.84760 1.16136 -0.20511 -0.27483 -0.07196 79  ASN C OD1 
3229 N ND2 . ASN C 79  ? 2.50545 1.85861 1.21255 -0.20986 -0.32700 -0.02380 79  ASN C ND2 
3230 N N   . LYS C 80  ? 1.89533 1.49973 1.02194 -0.13048 -0.26929 -0.04175 80  LYS C N   
3231 C CA  . LYS C 80  ? 1.79659 1.45170 1.02573 -0.11296 -0.27485 -0.04123 80  LYS C CA  
3232 C C   . LYS C 80  ? 1.69651 1.36672 0.98063 -0.09981 -0.30357 -0.01392 80  LYS C C   
3233 O O   . LYS C 80  ? 1.72445 1.36677 0.97124 -0.10051 -0.31183 0.00207  80  LYS C O   
3234 C CB  . LYS C 80  ? 1.74952 1.45262 1.03093 -0.10467 -0.22820 -0.05349 80  LYS C CB  
3235 C CG  . LYS C 80  ? 1.85842 1.55821 1.08828 -0.11357 -0.18763 -0.07701 80  LYS C CG  
3236 C CD  . LYS C 80  ? 2.15172 1.83766 1.32587 -0.12812 -0.16443 -0.06743 80  LYS C CD  
3237 C CE  . LYS C 80  ? 2.16080 1.87684 1.32457 -0.13427 -0.11445 -0.08410 80  LYS C CE  
3238 N NZ  . LYS C 80  ? 2.15202 1.84896 1.24892 -0.15686 -0.09717 -0.07192 80  LYS C NZ  
3239 N N   . THR C 81  ? 1.46277 1.17690 0.83456 -0.08698 -0.31849 -0.00829 81  THR C N   
3240 C CA  . THR C 81  ? 1.48078 1.22260 0.91676 -0.06958 -0.34234 0.01662  81  THR C CA  
3241 C C   . THR C 81  ? 1.29740 1.09818 0.82260 -0.05378 -0.31501 0.01674  81  THR C C   
3242 O O   . THR C 81  ? 1.38188 1.21061 0.94865 -0.05735 -0.30920 0.00572  81  THR C O   
3243 C CB  . THR C 81  ? 1.30226 1.04658 0.76057 -0.07246 -0.39444 0.02937  81  THR C CB  
3244 O OG1 . THR C 81  ? 1.40978 1.09091 0.77367 -0.09129 -0.41992 0.02514  81  THR C OG1 
3245 C CG2 . THR C 81  ? 1.27175 1.04687 0.79073 -0.05085 -0.41881 0.05665  81  THR C CG2 
3246 N N   . ASP C 82  ? 1.18615 0.99830 0.73366 -0.03668 -0.30035 0.02924  82  ASP C N   
3247 C CA  . ASP C 82  ? 1.22701 1.08942 0.85140 -0.02118 -0.27506 0.03062  82  ASP C CA  
3248 C C   . ASP C 82  ? 1.23953 1.15175 0.94661 -0.00872 -0.30109 0.04603  82  ASP C C   
3249 O O   . ASP C 82  ? 1.21406 1.13298 0.93947 0.00757  -0.32556 0.06520  82  ASP C O   
3250 C CB  . ASP C 82  ? 1.06515 0.91295 0.67481 -0.00688 -0.25408 0.03873  82  ASP C CB  
3251 C CG  . ASP C 82  ? 1.18459 1.07004 0.85034 0.00417  -0.22152 0.03565  82  ASP C CG  
3252 O OD1 . ASP C 82  ? 1.23022 1.16372 0.96667 0.01027  -0.22260 0.03680  82  ASP C OD1 
3253 O OD2 . ASP C 82  ? 1.43346 1.29732 1.06834 0.00375  -0.19650 0.03340  82  ASP C OD2 
3254 N N   . ILE C 83  ? 1.09468 1.04376 0.85318 -0.01631 -0.29647 0.03898  83  ILE C N   
3255 C CA  . ILE C 83  ? 1.04446 1.04752 0.88381 -0.01192 -0.32018 0.05543  83  ILE C CA  
3256 C C   . ILE C 83  ? 1.07194 1.12564 0.98096 -0.00192 -0.29037 0.05727  83  ILE C C   
3257 O O   . ILE C 83  ? 1.09330 1.19049 1.06315 -0.00973 -0.30091 0.06417  83  ILE C O   
3258 C CB  . ILE C 83  ? 1.09173 1.08651 0.92442 -0.03665 -0.35321 0.05049  83  ILE C CB  
3259 C CG1 . ILE C 83  ? 1.12486 1.09349 0.92320 -0.05149 -0.33086 0.02421  83  ILE C CG1 
3260 C CG2 . ILE C 83  ? 1.07643 1.02409 0.84477 -0.04521 -0.38954 0.05408  83  ILE C CG2 
3261 C CD1 . ILE C 83  ? 1.02019 0.97435 0.81183 -0.07324 -0.36248 0.01781  83  ILE C CD1 
3262 N N   . THR C 84  ? 1.00236 1.04675 0.89776 0.01187  -0.25484 0.05219  84  THR C N   
3263 C CA  . THR C 84  ? 0.98411 1.06401 0.92930 0.01766  -0.22500 0.05068  84  THR C CA  
3264 C C   . THR C 84  ? 0.98894 1.13098 1.01478 0.03304  -0.23119 0.07166  84  THR C C   
3265 O O   . THR C 84  ? 1.07023 1.25164 1.14763 0.02544  -0.22254 0.07377  84  THR C O   
3266 C CB  . THR C 84  ? 0.94825 1.00020 0.85681 0.02822  -0.19112 0.04369  84  THR C CB  
3267 O OG1 . THR C 84  ? 0.98685 0.98684 0.81906 0.01551  -0.19003 0.03134  84  THR C OG1 
3268 C CG2 . THR C 84  ? 1.00206 1.07200 0.93765 0.02325  -0.16263 0.03454  84  THR C CG2 
3269 N N   . PHE C 85  ? 1.07940 1.23262 1.11727 0.05540  -0.24550 0.08807  85  PHE C N   
3270 C CA  . PHE C 85  ? 1.07970 1.30227 1.19919 0.07515  -0.24751 0.10877  85  PHE C CA  
3271 C C   . PHE C 85  ? 1.04445 1.31483 1.21811 0.05877  -0.28587 0.12395  85  PHE C C   
3272 O O   . PHE C 85  ? 1.03474 1.37789 1.28800 0.06828  -0.28676 0.14289  85  PHE C O   
3273 C CB  . PHE C 85  ? 1.27125 1.48830 1.38518 0.11358  -0.24549 0.11981  85  PHE C CB  
3274 C CG  . PHE C 85  ? 1.26858 1.43509 1.32801 0.12935  -0.21155 0.10833  85  PHE C CG  
3275 C CD1 . PHE C 85  ? 1.41034 1.50538 1.38637 0.11287  -0.20779 0.09292  85  PHE C CD1 
3276 C CD2 . PHE C 85  ? 1.38212 1.57293 1.47157 0.15903  -0.18340 0.11381  85  PHE C CD2 
3277 C CE1 . PHE C 85  ? 1.57471 1.62424 1.50165 0.12196  -0.18065 0.08531  85  PHE C CE1 
3278 C CE2 . PHE C 85  ? 1.62779 1.76363 1.66010 0.17078  -0.15662 0.10391  85  PHE C CE2 
3279 C CZ  . PHE C 85  ? 1.57466 1.64010 1.52724 0.15028  -0.15725 0.09068  85  PHE C CZ  
3280 N N   . VAL C 86  ? 1.11004 1.34202 1.24082 0.03324  -0.31731 0.11691  86  VAL C N   
3281 C CA  . VAL C 86  ? 1.00936 1.27404 1.17945 0.01265  -0.36069 0.13155  86  VAL C CA  
3282 C C   . VAL C 86  ? 1.09777 1.36177 1.27445 -0.02173 -0.36479 0.12247  86  VAL C C   
3283 O O   . VAL C 86  ? 0.95940 1.27401 1.19714 -0.03966 -0.38852 0.13945  86  VAL C O   
3284 C CB  . VAL C 86  ? 1.04680 1.25937 1.15553 0.00710  -0.39976 0.13139  86  VAL C CB  
3285 C CG1 . VAL C 86  ? 1.22473 1.43229 1.33215 -0.02801 -0.44387 0.13443  86  VAL C CG1 
3286 C CG2 . VAL C 86  ? 1.06945 1.30860 1.20720 0.03881  -0.41601 0.15251  86  VAL C CG2 
3287 N N   . TYR C 87  ? 1.04517 1.25293 1.16041 -0.03103 -0.34274 0.09680  87  TYR C N   
3288 C CA  . TYR C 87  ? 0.91764 1.11232 1.02951 -0.05772 -0.34516 0.08463  87  TYR C CA  
3289 C C   . TYR C 87  ? 1.01046 1.26752 1.19969 -0.06048 -0.32902 0.09837  87  TYR C C   
3290 O O   . TYR C 87  ? 1.08566 1.35578 1.28697 -0.04299 -0.29004 0.09504  87  TYR C O   
3291 C CB  . TYR C 87  ? 0.93287 1.06642 0.97343 -0.05723 -0.31753 0.05509  87  TYR C CB  
3292 C CG  . TYR C 87  ? 0.93475 1.03757 0.95443 -0.07957 -0.32577 0.03805  87  TYR C CG  
3293 C CD1 . TYR C 87  ? 1.08042 1.14109 1.05662 -0.09927 -0.36307 0.03102  87  TYR C CD1 
3294 C CD2 . TYR C 87  ? 0.99409 1.10283 1.03173 -0.07978 -0.29895 0.02875  87  TYR C CD2 
3295 C CE1 . TYR C 87  ? 1.13487 1.15709 1.08396 -0.11570 -0.37218 0.01360  87  TYR C CE1 
3296 C CE2 . TYR C 87  ? 1.08595 1.16003 1.10160 -0.09624 -0.30932 0.01271  87  TYR C CE2 
3297 C CZ  . TYR C 87  ? 1.07958 1.10902 1.05001 -0.11274 -0.34541 0.00444  87  TYR C CZ  
3298 O OH  . TYR C 87  ? 1.29382 1.27873 1.23446 -0.12535 -0.35732 -0.01331 87  TYR C OH  
3299 N N   . ASN C 88  ? 0.98915 1.28157 1.22592 -0.08557 -0.35967 0.11478  88  ASN C N   
3300 C CA  . ASN C 88  ? 1.05862 1.41801 1.37168 -0.09326 -0.34709 0.13321  88  ASN C CA  
3301 C C   . ASN C 88  ? 1.12086 1.44320 1.41116 -0.11734 -0.34248 0.11827  88  ASN C C   
3302 O O   . ASN C 88  ? 1.23831 1.53451 1.51468 -0.14784 -0.37810 0.11766  88  ASN C O   
3303 C CB  . ASN C 88  ? 1.15633 1.58443 1.54072 -0.11024 -0.38393 0.16435  88  ASN C CB  
3304 C CG  . ASN C 88  ? 1.23090 1.73640 1.69557 -0.12211 -0.36898 0.18641  88  ASN C CG  
3305 O OD1 . ASN C 88  ? 1.19948 1.73589 1.68769 -0.09872 -0.32552 0.18725  88  ASN C OD1 
3306 N ND2 . ASN C 88  ? 1.14223 1.67647 1.64439 -0.16115 -0.40587 0.20546  88  ASN C ND2 
3307 N N   . ALA C 89  ? 1.08444 1.39870 1.36680 -0.10306 -0.30149 0.10642  89  ALA C N   
3308 C CA  . ALA C 89  ? 0.97715 1.26030 1.24413 -0.12086 -0.29518 0.09414  89  ALA C CA  
3309 C C   . ALA C 89  ? 0.97746 1.28046 1.26156 -0.10338 -0.25061 0.09365  89  ALA C C   
3310 O O   . ALA C 89  ? 1.01355 1.32998 1.29678 -0.07532 -0.22359 0.09373  89  ALA C O   
3311 C CB  . ALA C 89  ? 0.99477 1.19643 1.18376 -0.12281 -0.30357 0.06334  89  ALA C CB  
3312 N N   . ASN C 90  ? 0.82111 1.11756 1.11357 -0.12115 -0.24609 0.09331  90  ASN C N   
3313 C CA  . ASN C 90  ? 0.87345 1.17658 1.17127 -0.10873 -0.20774 0.09145  90  ASN C CA  
3314 C C   . ASN C 90  ? 0.87981 1.11828 1.11858 -0.09844 -0.19529 0.06247  90  ASN C C   
3315 O O   . ASN C 90  ? 0.91537 1.10655 1.11881 -0.10913 -0.21671 0.04549  90  ASN C O   
3316 C CB  . ASN C 90  ? 0.94825 1.27686 1.28300 -0.13490 -0.20979 0.10843  90  ASN C CB  
3317 C CG  . ASN C 90  ? 1.23752 1.65011 1.64078 -0.13899 -0.20429 0.13971  90  ASN C CG  
3318 O OD1 . ASN C 90  ? 1.35203 1.80382 1.77607 -0.11194 -0.18799 0.14656  90  ASN C OD1 
3319 N ND2 . ASN C 90  ? 1.24848 1.68996 1.68706 -0.17242 -0.21792 0.15965  90  ASN C ND2 
3320 N N   . PHE C 91  ? 0.81650 1.05333 1.04369 -0.07682 -0.16120 0.05700  91  PHE C N   
3321 C CA  . PHE C 91  ? 0.74067 0.92887 0.92005 -0.06719 -0.14787 0.03283  91  PHE C CA  
3322 C C   . PHE C 91  ? 0.74326 0.92946 0.92683 -0.06475 -0.12282 0.03371  91  PHE C C   
3323 O O   . PHE C 91  ? 0.88619 1.10339 1.09271 -0.05786 -0.10319 0.04953  91  PHE C O   
3324 C CB  . PHE C 91  ? 0.86115 1.03758 1.00763 -0.04681 -0.13585 0.02452  91  PHE C CB  
3325 C CG  . PHE C 91  ? 0.83418 0.99224 0.95460 -0.05028 -0.16066 0.01673  91  PHE C CG  
3326 C CD1 . PHE C 91  ? 0.81042 0.92703 0.89206 -0.05718 -0.17185 -0.00494 91  PHE C CD1 
3327 C CD2 . PHE C 91  ? 0.72962 0.90956 0.86079 -0.04431 -0.17294 0.03065  91  PHE C CD2 
3328 C CE1 . PHE C 91  ? 0.79954 0.89262 0.84674 -0.06065 -0.19359 -0.01305 91  PHE C CE1 
3329 C CE2 . PHE C 91  ? 0.73952 0.89630 0.83945 -0.04965 -0.19865 0.02442  91  PHE C CE2 
3330 C CZ  . PHE C 91  ? 0.85904 0.97008 0.91325 -0.05903 -0.20820 0.00225  91  PHE C CZ  
3331 N N   . PHE C 92  ? 0.68558 0.83417 0.84493 -0.06856 -0.12401 0.01646  92  PHE C N   
3332 C CA  . PHE C 92  ? 0.77682 0.91607 0.93392 -0.06708 -0.10490 0.01622  92  PHE C CA  
3333 C C   . PHE C 92  ? 0.77280 0.88018 0.89611 -0.05639 -0.09696 -0.00556 92  PHE C C   
3334 O O   . PHE C 92  ? 0.78973 0.87839 0.89427 -0.05441 -0.10950 -0.02249 92  PHE C O   
3335 C CB  . PHE C 92  ? 0.72795 0.86019 0.90180 -0.08760 -0.11963 0.02342  92  PHE C CB  
3336 C CG  . PHE C 92  ? 0.90855 1.07885 1.11948 -0.10489 -0.13015 0.04680  92  PHE C CG  
3337 C CD1 . PHE C 92  ? 0.91505 1.08519 1.13442 -0.12077 -0.16157 0.04896  92  PHE C CD1 
3338 C CD2 . PHE C 92  ? 0.88163 1.08937 1.11780 -0.10613 -0.10853 0.06735  92  PHE C CD2 
3339 C CE1 . PHE C 92  ? 0.85856 1.07198 1.11842 -0.14099 -0.17344 0.07376  92  PHE C CE1 
3340 C CE2 . PHE C 92  ? 1.03192 1.28760 1.30981 -0.12278 -0.11535 0.09091  92  PHE C CE2 
3341 C CZ  . PHE C 92  ? 0.93877 1.20084 1.23238 -0.14190 -0.14891 0.09543  92  PHE C CZ  
3342 N N   . LEU C 93  ? 0.65500 0.75737 0.76975 -0.05032 -0.07612 -0.00452 93  LEU C N   
3343 C CA  . LEU C 93  ? 0.56308 0.64542 0.65450 -0.04360 -0.06838 -0.02102 93  LEU C CA  
3344 C C   . LEU C 93  ? 0.69761 0.76580 0.79417 -0.04929 -0.06758 -0.01992 93  LEU C C   
3345 O O   . LEU C 93  ? 0.76610 0.83612 0.86496 -0.05304 -0.05657 -0.00539 93  LEU C O   
3346 C CB  . LEU C 93  ? 0.69396 0.77787 0.76192 -0.03395 -0.04869 -0.01962 93  LEU C CB  
3347 C CG  . LEU C 93  ? 0.74281 0.81783 0.78702 -0.03071 -0.04315 -0.03561 93  LEU C CG  
3348 C CD1 . LEU C 93  ? 0.67030 0.74560 0.70599 -0.02859 -0.05467 -0.04951 93  LEU C CD1 
3349 C CD2 . LEU C 93  ? 0.75928 0.82847 0.77560 -0.02763 -0.02642 -0.02891 93  LEU C CD2 
3350 N N   . PHE C 94  ? 0.78412 0.83615 0.87948 -0.04799 -0.07963 -0.03557 94  PHE C N   
3351 C CA  . PHE C 94  ? 0.65210 0.68612 0.75297 -0.05232 -0.08662 -0.03563 94  PHE C CA  
3352 C C   . PHE C 94  ? 0.69834 0.73311 0.79195 -0.04336 -0.07697 -0.04654 94  PHE C C   
3353 O O   . PHE C 94  ? 0.67156 0.71596 0.76108 -0.03322 -0.07425 -0.06219 94  PHE C O   
3354 C CB  . PHE C 94  ? 0.62820 0.64026 0.73574 -0.05593 -0.11346 -0.04372 94  PHE C CB  
3355 C CG  . PHE C 94  ? 0.73164 0.71785 0.84181 -0.05821 -0.12633 -0.04478 94  PHE C CG  
3356 C CD1 . PHE C 94  ? 0.73111 0.71068 0.84130 -0.07164 -0.12247 -0.02656 94  PHE C CD1 
3357 C CD2 . PHE C 94  ? 0.70839 0.67335 0.81747 -0.04523 -0.14361 -0.06421 94  PHE C CD2 
3358 C CE1 . PHE C 94  ? 0.78856 0.73860 0.89645 -0.07521 -0.13835 -0.02621 94  PHE C CE1 
3359 C CE2 . PHE C 94  ? 0.70315 0.64112 0.81516 -0.04478 -0.15996 -0.06460 94  PHE C CE2 
3360 C CZ  . PHE C 94  ? 0.79139 0.72068 0.90232 -0.06152 -0.15896 -0.04474 94  PHE C CZ  
3361 N N   . ALA C 95  ? 0.70665 0.73281 0.79740 -0.04894 -0.07201 -0.03721 95  ALA C N   
3362 C CA  . ALA C 95  ? 0.60982 0.64075 0.69692 -0.04583 -0.06536 -0.04238 95  ALA C CA  
3363 C C   . ALA C 95  ? 0.67836 0.69800 0.78219 -0.04305 -0.08395 -0.04918 95  ALA C C   
3364 O O   . ALA C 95  ? 0.69583 0.69074 0.79943 -0.05129 -0.09722 -0.04003 95  ALA C O   
3365 C CB  . ALA C 95  ? 0.67137 0.69270 0.73619 -0.05474 -0.05122 -0.02683 95  ALA C CB  
3366 N N   . THR C 96  ? 0.63483 0.67387 0.75276 -0.03093 -0.08466 -0.06434 96  THR C N   
3367 C CA  . THR C 96  ? 0.70622 0.74142 0.84516 -0.02265 -0.10198 -0.07127 96  THR C CA  
3368 C C   . THR C 96  ? 0.67604 0.73983 0.82632 -0.02448 -0.09379 -0.06907 96  THR C C   
3369 O O   . THR C 96  ? 0.68034 0.77224 0.82490 -0.02722 -0.07468 -0.07006 96  THR C O   
3370 C CB  . THR C 96  ? 0.58529 0.62141 0.73807 -0.00068 -0.11369 -0.09335 96  THR C CB  
3371 O OG1 . THR C 96  ? 0.80661 0.87417 0.95661 0.00956  -0.09485 -0.10690 96  THR C OG1 
3372 C CG2 . THR C 96  ? 0.67455 0.67210 0.81407 -0.00454 -0.13133 -0.09271 96  THR C CG2 
3373 N N   . LEU C 97  ? 0.71214 0.76663 0.87684 -0.02587 -0.11133 -0.06406 97  LEU C N   
3374 C CA  . LEU C 97  ? 0.63645 0.71681 0.81538 -0.03262 -0.11067 -0.05763 97  LEU C CA  
3375 C C   . LEU C 97  ? 0.71442 0.83503 0.93807 -0.00977 -0.11819 -0.07375 97  LEU C C   
3376 O O   . LEU C 97  ? 0.85347 0.95619 1.09347 0.00699  -0.13983 -0.08184 97  LEU C O   
3377 C CB  . LEU C 97  ? 0.64756 0.68982 0.81094 -0.04987 -0.12814 -0.03969 97  LEU C CB  
3378 C CG  . LEU C 97  ? 0.82305 0.88047 0.99200 -0.06437 -0.13341 -0.02813 97  LEU C CG  
3379 C CD1 . LEU C 97  ? 0.77095 0.83590 0.91043 -0.08085 -0.11065 -0.02036 97  LEU C CD1 
3380 C CD2 . LEU C 97  ? 0.87909 0.88793 1.02633 -0.07935 -0.15609 -0.01252 97  LEU C CD2 
3381 N N   . GLU C 98  ? 0.74839 0.92292 0.99029 -0.00860 -0.10023 -0.07781 98  GLU C N   
3382 C CA  . GLU C 98  ? 0.76437 0.99234 1.05353 0.01554  -0.10006 -0.09307 98  GLU C CA  
3383 C C   . GLU C 98  ? 0.66020 0.93190 0.98080 0.00111  -0.10431 -0.07880 98  GLU C C   
3384 O O   . GLU C 98  ? 0.76167 1.05221 1.06718 -0.02442 -0.08904 -0.06594 98  GLU C O   
3385 C CB  . GLU C 98  ? 0.83956 1.10514 1.12705 0.02903  -0.07274 -0.11025 98  GLU C CB  
3386 C CG  . GLU C 98  ? 0.95367 1.17661 1.20544 0.03835  -0.07008 -0.12256 98  GLU C CG  
3387 C CD  . GLU C 98  ? 1.39617 1.65237 1.64132 0.05282  -0.04578 -0.14080 98  GLU C CD  
3388 O OE1 . GLU C 98  ? 1.20237 1.51024 1.45659 0.04330  -0.02424 -0.13692 98  GLU C OE1 
3389 O OE2 . GLU C 98  ? 1.34041 1.56789 1.56652 0.07106  -0.04933 -0.15803 98  GLU C OE2 
3390 N N   . PRO C 99  ? 0.79844 1.08398 1.16039 0.01458  -0.12798 -0.07885 99  PRO C N   
3391 C CA  . PRO C 99  ? 0.70255 1.04187 1.10381 0.00048  -0.13439 -0.06447 99  PRO C CA  
3392 C C   . PRO C 99  ? 0.79052 1.21420 1.22489 0.00511  -0.10502 -0.07169 99  PRO C C   
3393 O O   . PRO C 99  ? 0.92020 1.37149 1.36882 0.03576  -0.08740 -0.09396 99  PRO C O   
3394 C CB  . PRO C 99  ? 0.68882 1.02938 1.13398 0.02486  -0.16682 -0.06808 99  PRO C CB  
3395 C CG  . PRO C 99  ? 0.79532 1.05768 1.20411 0.03874  -0.18191 -0.07727 99  PRO C CG  
3396 C CD  . PRO C 99  ? 0.73893 0.98859 1.11222 0.04207  -0.15375 -0.09050 99  PRO C CD  
3397 N N   . GLU C 100 ? 0.89667 1.22916 1.29202 -0.12489 0.19251  -0.17532 100 GLU C N   
3398 C CA  . GLU C 100 ? 1.09728 1.43286 1.49129 -0.14128 0.23290  -0.19830 100 GLU C CA  
3399 C C   . GLU C 100 ? 1.14775 1.57437 1.62759 -0.13659 0.22496  -0.21726 100 GLU C C   
3400 O O   . GLU C 100 ? 1.27118 1.70205 1.77217 -0.11557 0.23633  -0.22608 100 GLU C O   
3401 C CB  . GLU C 100 ? 1.08056 1.39022 1.42524 -0.18797 0.26794  -0.20989 100 GLU C CB  
3402 C CG  . GLU C 100 ? 1.04923 1.25801 1.30432 -0.18984 0.30319  -0.20459 100 GLU C CG  
3403 C CD  . GLU C 100 ? 1.26858 1.45463 1.51381 -0.17784 0.33051  -0.21570 100 GLU C CD  
3404 O OE1 . GLU C 100 ? 1.35208 1.54210 1.58818 -0.20954 0.36891  -0.23800 100 GLU C OE1 
3405 O OE2 . GLU C 100 ? 1.28091 1.44310 1.52404 -0.13948 0.31499  -0.20323 100 GLU C OE2 
3406 N N   . ARG C 101 ? 1.23570 1.73746 1.76633 -0.15451 0.20443  -0.22434 101 ARG C N   
3407 C CA  . ARG C 101 ? 1.61383 2.21245 2.23492 -0.14456 0.19093  -0.24185 101 ARG C CA  
3408 C C   . ARG C 101 ? 1.76331 2.43636 2.43237 -0.15350 0.15112  -0.23982 101 ARG C C   
3409 O O   . ARG C 101 ? 1.72754 2.46025 2.42286 -0.19127 0.16151  -0.26043 101 ARG C O   
3410 C CB  . ARG C 101 ? 1.66224 2.29259 2.30109 -0.17460 0.23747  -0.27390 101 ARG C CB  
3411 C CG  . ARG C 101 ? 1.63349 2.33858 2.35657 -0.14917 0.23619  -0.29228 101 ARG C CG  
3412 C CD  . ARG C 101 ? 1.59309 2.29000 2.30722 -0.17073 0.29184  -0.31945 101 ARG C CD  
3413 N NE  . ARG C 101 ? 1.71422 2.47686 2.50714 -0.14247 0.29354  -0.33730 101 ARG C NE  
3414 C CZ  . ARG C 101 ? 1.78419 2.56636 2.59367 -0.15916 0.33971  -0.36629 101 ARG C CZ  
3415 N NH1 . ARG C 101 ? 1.89826 2.63393 2.64580 -0.20522 0.38851  -0.38007 101 ARG C NH1 
3416 N NH2 . ARG C 101 ? 1.70783 2.55324 2.59435 -0.12899 0.33898  -0.38233 101 ARG C NH2 
3417 N N   . PRO C 102 ? 1.72991 2.40016 2.40764 -0.12206 0.10529  -0.21608 102 PRO C N   
3418 C CA  . PRO C 102 ? 1.78168 2.52265 2.50414 -0.12522 0.06275  -0.21310 102 PRO C CA  
3419 C C   . PRO C 102 ? 1.81769 2.65828 2.63590 -0.10153 0.04251  -0.22882 102 PRO C C   
3420 O O   . PRO C 102 ? 1.84546 2.75052 2.70443 -0.09956 0.00285  -0.22648 102 PRO C O   
3421 C CB  . PRO C 102 ? 1.66320 2.34831 2.34841 -0.09800 0.02586  -0.18085 102 PRO C CB  
3422 C CG  . PRO C 102 ? 1.55319 2.17445 2.21528 -0.06563 0.03988  -0.17199 102 PRO C CG  
3423 C CD  . PRO C 102 ? 1.46563 2.05913 2.10030 -0.08790 0.09158  -0.19025 102 PRO C CD  
3424 N N   . ILE C 103 ? 1.78650 2.64048 2.63977 -0.08218 0.06797  -0.24482 103 ILE C N   
3425 C CA  . ILE C 103 ? 1.88963 2.83797 2.83841 -0.05450 0.05389  -0.26220 103 ILE C CA  
3426 C C   . ILE C 103 ? 1.97201 2.93387 2.94938 -0.00699 -0.00289 -0.23944 103 ILE C C   
3427 O O   . ILE C 103 ? 1.99936 2.95928 3.00836 0.03852  -0.01131 -0.23693 103 ILE C O   
3428 C CB  . ILE C 103 ? 1.87128 2.92567 2.88103 -0.09272 0.06212  -0.29223 103 ILE C CB  
3429 C CG1 . ILE C 103 ? 1.81745 2.85260 2.79683 -0.14020 0.12414  -0.31738 103 ILE C CG1 
3430 C CG2 . ILE C 103 ? 1.70164 2.86424 2.81954 -0.05777 0.04117  -0.30943 103 ILE C CG2 
3431 C CD1 . ILE C 103 ? 1.66599 2.80175 2.69971 -0.18668 0.13799  -0.34990 103 ILE C CD1 
3432 N N   . GLY C 113 ? 1.39678 1.36328 1.56928 0.00872  -0.22094 0.09063  113 GLY C N   
3433 C CA  . GLY C 113 ? 1.65874 1.64890 1.81707 -0.01513 -0.22370 0.09204  113 GLY C CA  
3434 C C   . GLY C 113 ? 1.80008 1.80562 1.95681 -0.04116 -0.18872 0.07994  113 GLY C C   
3435 O O   . GLY C 113 ? 1.74679 1.72849 1.89180 -0.04955 -0.16603 0.07677  113 GLY C O   
3436 N N   . SER C 114 ? 1.88022 1.92596 2.04850 -0.05366 -0.18461 0.07235  114 SER C N   
3437 C CA  . SER C 114 ? 1.91832 1.97211 2.07907 -0.07692 -0.15087 0.06105  114 SER C CA  
3438 C C   . SER C 114 ? 1.86667 1.95786 2.07137 -0.06312 -0.13094 0.04464  114 SER C C   
3439 O O   . SER C 114 ? 1.85032 1.97918 2.09269 -0.04683 -0.14390 0.03920  114 SER C O   
3440 C CB  . SER C 114 ? 1.99383 2.05512 2.12441 -0.10721 -0.15390 0.06213  114 SER C CB  
3441 O OG  . SER C 114 ? 2.01484 2.12389 2.17477 -0.10183 -0.17424 0.05766  114 SER C OG  
3442 N N   . PRO C 115 ? 1.64595 1.72665 1.84511 -0.06866 -0.09922 0.03630  115 PRO C N   
3443 C CA  . PRO C 115 ? 1.56447 1.66772 1.79339 -0.05550 -0.07858 0.02210  115 PRO C CA  
3444 C C   . PRO C 115 ? 1.39552 1.52173 1.62148 -0.07570 -0.06175 0.01136  115 PRO C C   
3445 O O   . PRO C 115 ? 1.41851 1.54148 1.61694 -0.10171 -0.06279 0.01377  115 PRO C O   
3446 C CB  . PRO C 115 ? 1.35650 1.43170 1.57209 -0.05150 -0.05632 0.02044  115 PRO C CB  
3447 C CG  . PRO C 115 ? 1.45675 1.50758 1.63436 -0.07614 -0.05073 0.02718  115 PRO C CG  
3448 C CD  . PRO C 115 ? 1.52389 1.57031 1.68761 -0.08597 -0.08020 0.03920  115 PRO C CD  
3449 N N   . VAL C 116 ? 1.24252 1.38754 1.49216 -0.06595 -0.04424 -0.00160 116 VAL C N   
3450 C CA  . VAL C 116 ? 1.13106 1.29178 1.37421 -0.08756 -0.02284 -0.01415 116 VAL C CA  
3451 C C   . VAL C 116 ? 0.99064 1.11375 1.19846 -0.09490 0.01189  -0.01835 116 VAL C C   
3452 O O   . VAL C 116 ? 0.93616 1.04785 1.11357 -0.12047 0.02961  -0.02290 116 VAL C O   
3453 C CB  . VAL C 116 ? 1.04399 1.24572 1.32928 -0.07722 -0.02060 -0.02760 116 VAL C CB  
3454 C CG1 . VAL C 116 ? 1.06758 1.31692 1.38756 -0.07604 -0.05348 -0.02638 116 VAL C CG1 
3455 C CG2 . VAL C 116 ? 1.20854 1.39970 1.51268 -0.04627 -0.01550 -0.02920 116 VAL C CG2 
3456 N N   . LEU C 117 ? 0.93049 1.03271 1.13976 -0.07186 0.02152  -0.01745 117 LEU C N   
3457 C CA  . LEU C 117 ? 0.86583 0.93284 1.04310 -0.07143 0.04989  -0.01972 117 LEU C CA  
3458 C C   . LEU C 117 ? 0.86707 0.91432 1.02670 -0.07514 0.04482  -0.00972 117 LEU C C   
3459 O O   . LEU C 117 ? 0.92798 0.97708 1.10304 -0.06196 0.02629  -0.00250 117 LEU C O   
3460 C CB  . LEU C 117 ? 0.72503 0.78227 0.91061 -0.04450 0.05994  -0.02409 117 LEU C CB  
3461 C CG  . LEU C 117 ? 0.81915 0.83992 0.96963 -0.03932 0.08773  -0.02650 117 LEU C CG  
3462 C CD1 . LEU C 117 ? 0.82476 0.82964 0.94448 -0.06119 0.11433  -0.03486 117 LEU C CD1 
3463 C CD2 . LEU C 117 ? 0.84362 0.85333 0.99749 -0.01102 0.09154  -0.02891 117 LEU C CD2 
3464 N N   . THR C 118 ? 0.88000 0.90624 1.00556 -0.09497 0.06378  -0.01079 118 THR C N   
3465 C CA  . THR C 118 ? 0.90971 0.91785 1.01702 -0.10210 0.06568  -0.00428 118 THR C CA  
3466 C C   . THR C 118 ? 0.88645 0.86813 0.97228 -0.09403 0.09645  -0.00943 118 THR C C   
3467 O O   . THR C 118 ? 0.86788 0.83466 0.93801 -0.09050 0.11771  -0.01667 118 THR C O   
3468 C CB  . THR C 118 ? 0.90211 0.90719 0.98461 -0.13396 0.05878  -0.00053 118 THR C CB  
3469 O OG1 . THR C 118 ? 1.01773 1.02721 1.08632 -0.15289 0.06915  -0.00879 118 THR C OG1 
3470 C CG2 . THR C 118 ? 0.92963 0.95194 1.02867 -0.13453 0.02303  0.00964  118 THR C CG2 
3471 N N   . GLY C 119 ? 0.92263 0.89732 1.00669 -0.09084 0.09954  -0.00618 119 GLY C N   
3472 C CA  . GLY C 119 ? 0.79854 0.75510 0.87024 -0.07673 0.12564  -0.01121 119 GLY C CA  
3473 C C   . GLY C 119 ? 0.88690 0.85829 0.98811 -0.04662 0.11764  -0.01111 119 GLY C C   
3474 O O   . GLY C 119 ? 0.91789 0.90918 1.04477 -0.04445 0.09464  -0.00694 119 GLY C O   
3475 N N   . VAL C 120 ? 0.92340 0.88273 1.01789 -0.02308 0.13539  -0.01578 120 VAL C N   
3476 C CA  . VAL C 120 ? 0.90949 0.88601 1.03001 0.00644  0.12616  -0.01688 120 VAL C CA  
3477 C C   . VAL C 120 ? 0.81898 0.78674 0.93545 0.02688  0.12205  -0.01784 120 VAL C C   
3478 O O   . VAL C 120 ? 0.82309 0.76114 0.90955 0.03796  0.14189  -0.02041 120 VAL C O   
3479 C CB  . VAL C 120 ? 0.85477 0.82799 0.97236 0.02335  0.14531  -0.02137 120 VAL C CB  
3480 C CG1 . VAL C 120 ? 0.90194 0.89877 1.04719 0.05522  0.13200  -0.02354 120 VAL C CG1 
3481 C CG2 . VAL C 120 ? 1.00561 0.98916 1.12854 0.00058  0.15265  -0.02259 120 VAL C CG2 
3482 N N   . PRO C 121 ? 0.89555 0.88173 1.03553 0.03147  0.09943  -0.01635 121 PRO C N   
3483 C CA  . PRO C 121 ? 0.74901 0.72522 0.88263 0.04780  0.09804  -0.01872 121 PRO C CA  
3484 C C   . PRO C 121 ? 0.74478 0.72134 0.88142 0.07859  0.09227  -0.02056 121 PRO C C   
3485 O O   . PRO C 121 ? 0.74964 0.71607 0.87831 0.09122  0.08922  -0.02256 121 PRO C O   
3486 C CB  . PRO C 121 ? 0.71989 0.71630 0.87849 0.03683  0.07671  -0.01710 121 PRO C CB  
3487 C CG  . PRO C 121 ? 0.70572 0.72090 0.88601 0.02910  0.06022  -0.01303 121 PRO C CG  
3488 C CD  . PRO C 121 ? 0.71922 0.72870 0.88589 0.01803  0.07653  -0.01256 121 PRO C CD  
3489 N N   . VAL C 122 ? 0.74400 0.73494 0.89277 0.08997  0.09010  -0.02106 122 VAL C N   
3490 C CA  . VAL C 122 ? 0.77075 0.76973 0.92493 0.11985  0.08065  -0.02355 122 VAL C CA  
3491 C C   . VAL C 122 ? 0.82622 0.81016 0.96090 0.14047  0.09843  -0.02427 122 VAL C C   
3492 O O   . VAL C 122 ? 0.88594 0.87951 1.02937 0.13209  0.10990  -0.02539 122 VAL C O   
3493 C CB  . VAL C 122 ? 0.72401 0.76383 0.91825 0.11734  0.05842  -0.02616 122 VAL C CB  
3494 C CG1 . VAL C 122 ? 0.86363 0.91698 1.06340 0.14698  0.04594  -0.03030 122 VAL C CG1 
3495 C CG2 . VAL C 122 ? 0.83019 0.87469 1.03757 0.09956  0.04217  -0.02472 122 VAL C CG2 
3496 N N   . ALA C 123 ? 0.81016 0.76603 0.91446 0.16831  0.10180  -0.02365 123 ALA C N   
3497 C CA  . ALA C 123 ? 0.94493 0.87793 1.02425 0.19576  0.11696  -0.02308 123 ALA C CA  
3498 C C   . ALA C 123 ? 0.85856 0.81301 0.94985 0.23150  0.09584  -0.02434 123 ALA C C   
3499 O O   . ALA C 123 ? 0.85777 0.81070 0.94280 0.23891  0.07839  -0.02413 123 ALA C O   
3500 C CB  . ALA C 123 ? 0.89826 0.76554 0.91635 0.19913  0.14163  -0.02012 123 ALA C CB  
3501 N N   . GLY C 124 ? 0.87025 0.84653 0.97896 0.25388  0.09743  -0.02679 124 GLY C N   
3502 C CA  . GLY C 124 ? 0.88716 0.88602 1.00547 0.29215  0.07633  -0.02839 124 GLY C CA  
3503 C C   . GLY C 124 ? 0.95172 0.88964 1.00908 0.32889  0.08570  -0.02182 124 GLY C C   
3504 O O   . GLY C 124 ? 1.08005 0.95882 1.09016 0.32452  0.11352  -0.01752 124 GLY C O   
3505 N N   . VAL C 125 ? 0.71035 1.08644 1.03206 0.05460  -0.09574 -0.09113 125 VAL C N   
3506 C CA  . VAL C 125 ? 0.67244 1.01806 0.97798 0.07790  -0.12036 -0.09526 125 VAL C CA  
3507 C C   . VAL C 125 ? 0.78732 1.17833 1.12737 0.11629  -0.12211 -0.10202 125 VAL C C   
3508 O O   . VAL C 125 ? 0.63176 1.10123 1.02798 0.11912  -0.11198 -0.10130 125 VAL C O   
3509 C CB  . VAL C 125 ? 0.64454 0.98053 0.94902 0.05878  -0.14773 -0.09031 125 VAL C CB  
3510 C CG1 . VAL C 125 ? 0.76182 1.17291 1.12761 0.04705  -0.15671 -0.08692 125 VAL C CG1 
3511 C CG2 . VAL C 125 ? 0.79832 1.08991 1.07165 0.08007  -0.17301 -0.09174 125 VAL C CG2 
3512 N N   . ALA C 126 ? 0.77202 1.11303 1.07696 0.14651  -0.13422 -0.10819 126 ALA C N   
3513 C CA  . ALA C 126 ? 0.74675 1.11184 1.07189 0.19168  -0.14299 -0.11655 126 ALA C CA  
3514 C C   . ALA C 126 ? 0.79198 1.10374 1.08746 0.20542  -0.17915 -0.11476 126 ALA C C   
3515 O O   . ALA C 126 ? 0.93015 1.16139 1.16594 0.19532  -0.18738 -0.11162 126 ALA C O   
3516 C CB  . ALA C 126 ? 0.61353 0.95215 0.90899 0.22134  -0.12328 -0.12769 126 ALA C CB  
3517 N N   . TYR C 127 ? 0.76402 1.12319 1.10148 0.22649  -0.20138 -0.11493 127 TYR C N   
3518 C CA  . TYR C 127 ? 0.93486 1.24374 1.24182 0.23983  -0.23971 -0.11128 127 TYR C CA  
3519 C C   . TYR C 127 ? 0.95067 1.21607 1.22930 0.29093  -0.25052 -0.12033 127 TYR C C   
3520 O O   . TYR C 127 ? 0.97424 1.29614 1.29508 0.33098  -0.24210 -0.13068 127 TYR C O   
3521 C CB  . TYR C 127 ? 0.80867 1.18590 1.17172 0.23745  -0.26536 -0.10661 127 TYR C CB  
3522 C CG  . TYR C 127 ? 0.79682 1.19090 1.16889 0.18525  -0.26372 -0.09823 127 TYR C CG  
3523 C CD1 . TYR C 127 ? 0.95162 1.27424 1.26436 0.15926  -0.28120 -0.09147 127 TYR C CD1 
3524 C CD2 . TYR C 127 ? 0.61849 1.09517 1.05238 0.16217  -0.24416 -0.09691 127 TYR C CD2 
3525 C CE1 . TYR C 127 ? 0.89074 1.21862 1.20220 0.11720  -0.28060 -0.08686 127 TYR C CE1 
3526 C CE2 . TYR C 127 ? 0.81623 1.29333 1.24876 0.11486  -0.24648 -0.09009 127 TYR C CE2 
3527 C CZ  . TYR C 127 ? 0.85417 1.25419 1.22378 0.09535  -0.26549 -0.08673 127 TYR C CZ  
3528 O OH  . TYR C 127 ? 0.82920 1.22017 1.18851 0.05388  -0.26880 -0.08290 127 TYR C OH  
3529 N N   . LEU C 128 ? 1.10911 1.27265 1.31352 0.28958  -0.26835 -0.11615 128 LEU C N   
3530 C CA  . LEU C 128 ? 1.14384 1.23944 1.30271 0.33193  -0.28114 -0.12409 128 LEU C CA  
3531 C C   . LEU C 128 ? 1.18088 1.19454 1.28375 0.33616  -0.32131 -0.11368 128 LEU C C   
3532 O O   . LEU C 128 ? 1.04504 1.03771 1.12636 0.29847  -0.33101 -0.09994 128 LEU C O   
3533 C CB  . LEU C 128 ? 1.15420 1.18818 1.26270 0.31940  -0.25909 -0.12849 128 LEU C CB  
3534 C CG  . LEU C 128 ? 1.09861 1.19220 1.24145 0.31663  -0.22011 -0.13832 128 LEU C CG  
3535 C CD1 . LEU C 128 ? 1.14240 1.16018 1.22436 0.30319  -0.20925 -0.14148 128 LEU C CD1 
3536 C CD2 . LEU C 128 ? 1.00844 1.16885 1.19738 0.36912  -0.21097 -0.15312 128 LEU C CD2 
3537 N N   . ASP C 129 ? 1.41042 1.37255 1.48309 0.38489  -0.34481 -0.12047 129 ASP C N   
3538 C CA  . ASP C 129 ? 1.34978 1.21867 1.35705 0.39187  -0.38557 -0.10908 129 ASP C CA  
3539 C C   . ASP C 129 ? 1.32890 1.07515 1.24580 0.37501  -0.38936 -0.10329 129 ASP C C   
3540 O O   . ASP C 129 ? 1.46912 1.13123 1.32196 0.36138  -0.41723 -0.08765 129 ASP C O   
3541 C CB  . ASP C 129 ? 1.43019 1.30620 1.45310 0.45771  -0.41822 -0.11754 129 ASP C CB  
3542 C CG  . ASP C 129 ? 1.52777 1.54396 1.65589 0.48160  -0.40926 -0.12656 129 ASP C CG  
3543 O OD1 . ASP C 129 ? 1.56239 1.63886 1.73165 0.45145  -0.41691 -0.11660 129 ASP C OD1 
3544 O OD2 . ASP C 129 ? 1.51281 1.57874 1.68047 0.52986  -0.39505 -0.14336 129 ASP C OD2 
3545 N N   . LYS C 130 ? 1.35608 1.08945 1.26380 0.37233  -0.36359 -0.11401 130 LYS C N   
3546 C CA  . LYS C 130 ? 1.37922 1.00240 1.20728 0.35061  -0.36887 -0.10872 130 LYS C CA  
3547 C C   . LYS C 130 ? 1.46598 1.11741 1.30691 0.30338  -0.33360 -0.10741 130 LYS C C   
3548 O O   . LYS C 130 ? 1.45939 1.19456 1.35721 0.30847  -0.30436 -0.11912 130 LYS C O   
3549 C CB  . LYS C 130 ? 1.46632 1.01638 1.24987 0.40280  -0.38488 -0.12560 130 LYS C CB  
3550 C CG  . LYS C 130 ? 1.48614 0.94678 1.21367 0.43689  -0.43053 -0.11976 130 LYS C CG  
3551 C CD  . LYS C 130 ? 1.73955 1.13482 1.41446 0.38344  -0.44913 -0.09166 130 LYS C CD  
3552 C CE  . LYS C 130 ? 1.68951 0.94573 1.27074 0.40131  -0.49384 -0.08226 130 LYS C CE  
3553 N NZ  . LYS C 130 ? 1.70912 0.96081 1.29798 0.47946  -0.52135 -0.09862 130 LYS C NZ  
3554 N N   . PRO C 131 ? 1.58136 1.16638 1.37076 0.25670  -0.33613 -0.09185 131 PRO C N   
3555 C CA  . PRO C 131 ? 1.46010 0.94302 1.17608 0.23971  -0.36686 -0.07340 131 PRO C CA  
3556 C C   . PRO C 131 ? 1.57791 1.07939 1.29714 0.22598  -0.37788 -0.05661 131 PRO C C   
3557 O O   . PRO C 131 ? 1.56867 0.99244 1.22962 0.22820  -0.40854 -0.04283 131 PRO C O   
3558 C CB  . PRO C 131 ? 1.53392 0.98043 1.21948 0.18575  -0.35370 -0.06210 131 PRO C CB  
3559 C CG  . PRO C 131 ? 1.45237 1.00260 1.20543 0.16529  -0.31628 -0.06694 131 PRO C CG  
3560 C CD  . PRO C 131 ? 1.41247 1.02882 1.21784 0.21309  -0.30610 -0.08921 131 PRO C CD  
3561 N N   . ASN C 132 ? 1.57211 1.16939 1.35227 0.21207  -0.35526 -0.05775 132 ASN C N   
3562 C CA  . ASN C 132 ? 1.46766 1.08822 1.25201 0.20261  -0.36637 -0.04625 132 ASN C CA  
3563 C C   . ASN C 132 ? 1.36463 1.08548 1.22675 0.22892  -0.36162 -0.06041 132 ASN C C   
3564 O O   . ASN C 132 ? 1.29976 1.08518 1.21619 0.23827  -0.33723 -0.07491 132 ASN C O   
3565 C CB  . ASN C 132 ? 1.50388 1.13319 1.27417 0.14855  -0.34447 -0.03069 132 ASN C CB  
3566 C CG  . ASN C 132 ? 1.53364 1.08558 1.24193 0.11394  -0.34267 -0.01437 132 ASN C CG  
3567 O OD1 . ASN C 132 ? 1.74349 1.20996 1.39722 0.12382  -0.36846 -0.00832 132 ASN C OD1 
3568 N ND2 . ASN C 132 ? 1.58844 1.17092 1.30626 0.07299  -0.31322 -0.00682 132 ASN C ND2 
3569 N N   . ARG C 133 ? 1.27713 1.01003 1.14199 0.23812  -0.38676 -0.05457 133 ARG C N   
3570 C CA  . ARG C 133 ? 1.38941 1.22063 1.33072 0.25552  -0.38803 -0.06472 133 ARG C CA  
3571 C C   . ARG C 133 ? 1.25570 1.13810 1.22137 0.21098  -0.36259 -0.06170 133 ARG C C   
3572 O O   . ARG C 133 ? 1.24976 1.11116 1.18224 0.18669  -0.37329 -0.05083 133 ARG C O   
3573 C CB  . ARG C 133 ? 1.43963 1.26121 1.37350 0.28386  -0.43189 -0.05999 133 ARG C CB  
3574 C CG  . ARG C 133 ? 1.40705 1.16975 1.31174 0.33510  -0.46058 -0.06376 133 ARG C CG  
3575 C CD  . ARG C 133 ? 1.52375 1.25780 1.40398 0.35970  -0.50914 -0.05486 133 ARG C CD  
3576 N NE  . ARG C 133 ? 1.73293 1.57306 1.70084 0.39275  -0.52380 -0.06543 133 ARG C NE  
3577 C CZ  . ARG C 133 ? 1.66864 1.55410 1.68777 0.44972  -0.53138 -0.07993 133 ARG C CZ  
3578 N NH1 . ARG C 133 ? 1.49907 1.32103 1.48152 0.48483  -0.52808 -0.08834 133 ARG C NH1 
3579 N NH2 . ARG C 133 ? 1.58942 1.58725 1.69784 0.47237  -0.54327 -0.08639 133 ARG C NH2 
3580 N N   . ALA C 134 ? 1.15248 1.09522 1.16845 0.20226  -0.32951 -0.07168 134 ALA C N   
3581 C CA  . ALA C 134 ? 1.15117 1.12978 1.18315 0.16275  -0.30433 -0.06985 134 ALA C CA  
3582 C C   . ALA C 134 ? 1.12240 1.17356 1.21752 0.16523  -0.27608 -0.08138 134 ALA C C   
3583 O O   . ALA C 134 ? 1.03252 1.10793 1.15595 0.19693  -0.27260 -0.09079 134 ALA C O   
3584 C CB  . ALA C 134 ? 0.83737 0.75719 0.81249 0.13063  -0.28753 -0.05992 134 ALA C CB  
3585 N N   . GLY C 135 ? 1.01422 1.09494 1.12451 0.13296  -0.25531 -0.08042 135 GLY C N   
3586 C CA  . GLY C 135 ? 0.80063 0.93504 0.95536 0.12743  -0.22639 -0.08750 135 GLY C CA  
3587 C C   . GLY C 135 ? 0.78235 0.87810 0.90584 0.11951  -0.20349 -0.08795 135 GLY C C   
3588 O O   . GLY C 135 ? 0.86699 0.90828 0.94335 0.10391  -0.20490 -0.08056 135 GLY C O   
3589 N N   . TYR C 136 ? 0.75285 0.88118 0.90330 0.12877  -0.18229 -0.09574 136 TYR C N   
3590 C CA  . TYR C 136 ? 0.81254 0.90452 0.93335 0.12461  -0.16598 -0.09764 136 TYR C CA  
3591 C C   . TYR C 136 ? 0.70229 0.83733 0.85000 0.11348  -0.13868 -0.10115 136 TYR C C   
3592 O O   . TYR C 136 ? 0.72934 0.92269 0.91950 0.12267  -0.12924 -0.10528 136 TYR C O   
3593 C CB  . TYR C 136 ? 0.79933 0.85490 0.89773 0.15824  -0.17536 -0.10552 136 TYR C CB  
3594 C CG  . TYR C 136 ? 0.83864 0.82540 0.89073 0.16383  -0.20339 -0.09901 136 TYR C CG  
3595 C CD1 . TYR C 136 ? 0.89655 0.81748 0.89834 0.14201  -0.20682 -0.09092 136 TYR C CD1 
3596 C CD2 . TYR C 136 ? 0.95463 0.94373 1.01341 0.18812  -0.22803 -0.09869 136 TYR C CD2 
3597 C CE1 . TYR C 136 ? 1.00934 0.86315 0.96343 0.14125  -0.23160 -0.08139 136 TYR C CE1 
3598 C CE2 . TYR C 136 ? 1.10860 1.02537 1.11580 0.19222  -0.25548 -0.09039 136 TYR C CE2 
3599 C CZ  . TYR C 136 ? 1.17469 1.02131 1.12699 0.16701  -0.25598 -0.08101 136 TYR C CZ  
3600 O OH  . TYR C 136 ? 1.24288 1.01350 1.13881 0.16592  -0.28262 -0.06942 136 TYR C OH  
3601 N N   . PHE C 137 ? 0.60841 0.71703 0.73186 0.09267  -0.12674 -0.09774 137 PHE C N   
3602 C CA  . PHE C 137 ? 0.54907 0.68116 0.68332 0.08329  -0.10412 -0.09970 137 PHE C CA  
3603 C C   . PHE C 137 ? 0.68249 0.77435 0.78286 0.08827  -0.10058 -0.10334 137 PHE C C   
3604 O O   . PHE C 137 ? 0.77959 0.82667 0.85014 0.07953  -0.11240 -0.09894 137 PHE C O   
3605 C CB  . PHE C 137 ? 0.58718 0.72415 0.72286 0.05485  -0.09729 -0.09242 137 PHE C CB  
3606 C CG  . PHE C 137 ? 0.68136 0.84275 0.83799 0.04467  -0.10579 -0.08945 137 PHE C CG  
3607 C CD1 . PHE C 137 ? 0.70661 0.84328 0.84470 0.04108  -0.12326 -0.08587 137 PHE C CD1 
3608 C CD2 . PHE C 137 ? 0.72226 0.92661 0.91111 0.03463  -0.09752 -0.08897 137 PHE C CD2 
3609 C CE1 . PHE C 137 ? 0.67452 0.82573 0.82314 0.03102  -0.13529 -0.08444 137 PHE C CE1 
3610 C CE2 . PHE C 137 ? 0.59218 0.81314 0.79695 0.02032  -0.11057 -0.08627 137 PHE C CE2 
3611 C CZ  . PHE C 137 ? 0.65485 0.84748 0.83799 0.01998  -0.13087 -0.08524 137 PHE C CZ  
3612 N N   . ILE C 138 ? 0.57269 0.68032 0.67499 0.09953  -0.08493 -0.11036 138 ILE C N   
3613 C CA  . ILE C 138 ? 0.67210 0.73834 0.73635 0.10449  -0.08444 -0.11570 138 ILE C CA  
3614 C C   . ILE C 138 ? 0.72965 0.81407 0.79383 0.09170  -0.06569 -0.11391 138 ILE C C   
3615 O O   . ILE C 138 ? 0.67765 0.80691 0.76636 0.09229  -0.04795 -0.11324 138 ILE C O   
3616 C CB  . ILE C 138 ? 0.80267 0.85011 0.84754 0.14000  -0.08755 -0.12926 138 ILE C CB  
3617 C CG1 . ILE C 138 ? 0.87949 0.87211 0.87404 0.14235  -0.09154 -0.13622 138 ILE C CG1 
3618 C CG2 . ILE C 138 ? 0.64250 0.75226 0.72073 0.16108  -0.06597 -0.13552 138 ILE C CG2 
3619 C CD1 . ILE C 138 ? 0.75773 0.68679 0.71015 0.16689  -0.11239 -0.14643 138 ILE C CD1 
3620 N N   . PHE C 139 ? 0.62381 0.67342 0.65975 0.07871  -0.07148 -0.11162 139 PHE C N   
3621 C CA  . PHE C 139 ? 0.79936 0.85534 0.82715 0.06753  -0.05996 -0.10852 139 PHE C CA  
3622 C C   . PHE C 139 ? 0.72638 0.74370 0.71082 0.07785  -0.06485 -0.11694 139 PHE C C   
3623 O O   . PHE C 139 ? 0.81640 0.80126 0.78072 0.06531  -0.08149 -0.11443 139 PHE C O   
3624 C CB  . PHE C 139 ? 0.76530 0.82045 0.80146 0.04466  -0.06581 -0.09788 139 PHE C CB  
3625 C CG  . PHE C 139 ? 0.72529 0.80919 0.79071 0.03510  -0.05977 -0.09164 139 PHE C CG  
3626 C CD1 . PHE C 139 ? 0.75961 0.86296 0.83363 0.02771  -0.04679 -0.08780 139 PHE C CD1 
3627 C CD2 . PHE C 139 ? 0.77901 0.86178 0.85477 0.03152  -0.06929 -0.08901 139 PHE C CD2 
3628 C CE1 . PHE C 139 ? 0.71974 0.83771 0.81233 0.01682  -0.04583 -0.08328 139 PHE C CE1 
3629 C CE2 . PHE C 139 ? 0.77904 0.87952 0.87176 0.02311  -0.06684 -0.08517 139 PHE C CE2 
3630 C CZ  . PHE C 139 ? 0.72368 0.84015 0.82490 0.01564  -0.05632 -0.08320 139 PHE C CZ  
3631 N N   . PRO C 140 ? 0.80813 0.82987 0.77616 0.10030  -0.05094 -0.12707 140 PRO C N   
3632 C CA  . PRO C 140 ? 0.87225 0.84561 0.78598 0.11371  -0.05774 -0.13822 140 PRO C CA  
3633 C C   . PRO C 140 ? 0.80685 0.77616 0.69290 0.10542  -0.04862 -0.13552 140 PRO C C   
3634 O O   . PRO C 140 ? 1.09500 1.01834 0.92825 0.11413  -0.05786 -0.14481 140 PRO C O   
3635 C CB  . PRO C 140 ? 0.76258 0.74447 0.66883 0.14973  -0.04430 -0.15240 140 PRO C CB  
3636 C CG  . PRO C 140 ? 0.83280 0.88914 0.79361 0.14754  -0.02003 -0.14466 140 PRO C CG  
3637 C CD  . PRO C 140 ? 0.76002 0.83061 0.75838 0.11775  -0.03145 -0.13036 140 PRO C CD  
3638 N N   . ASP C 141 ? 0.89037 0.89737 0.80234 0.08925  -0.03382 -0.12329 141 ASP C N   
3639 C CA  . ASP C 141 ? 0.95823 0.95963 0.83863 0.08399  -0.02283 -0.11886 141 ASP C CA  
3640 C C   . ASP C 141 ? 0.91937 0.92004 0.81299 0.06048  -0.03427 -0.10493 141 ASP C C   
3641 O O   . ASP C 141 ? 1.13696 1.15375 1.03517 0.05019  -0.02094 -0.09456 141 ASP C O   
3642 C CB  . ASP C 141 ? 1.10051 1.14469 0.98947 0.09059  0.01026  -0.11668 141 ASP C CB  
3643 C CG  . ASP C 141 ? 1.36255 1.39295 1.20583 0.08492  0.02365  -0.11052 141 ASP C CG  
3644 O OD1 . ASP C 141 ? 1.42759 1.40907 1.22232 0.08585  0.00561  -0.11373 141 ASP C OD1 
3645 O OD2 . ASP C 141 ? 1.49014 1.55750 1.34435 0.07688  0.05022  -0.10094 141 ASP C OD2 
3646 N N   . LEU C 142 ? 0.90266 0.88468 0.80234 0.05208  -0.05934 -0.10384 142 LEU C N   
3647 C CA  . LEU C 142 ? 0.89958 0.88632 0.81438 0.03708  -0.07080 -0.09254 142 LEU C CA  
3648 C C   . LEU C 142 ? 0.82588 0.78151 0.70637 0.03476  -0.09322 -0.09284 142 LEU C C   
3649 O O   . LEU C 142 ? 1.06113 0.99222 0.92558 0.03421  -0.11197 -0.09992 142 LEU C O   
3650 C CB  . LEU C 142 ? 0.81258 0.81795 0.76983 0.02828  -0.07958 -0.08868 142 LEU C CB  
3651 C CG  . LEU C 142 ? 0.81798 0.85064 0.80709 0.02852  -0.06425 -0.08764 142 LEU C CG  
3652 C CD1 . LEU C 142 ? 0.75653 0.79812 0.77257 0.02074  -0.07415 -0.08413 142 LEU C CD1 
3653 C CD2 . LEU C 142 ? 0.79384 0.84065 0.78908 0.02328  -0.05002 -0.08039 142 LEU C CD2 
3654 N N   . SER C 143 ? 0.92999 0.88217 0.79707 0.03215  -0.09529 -0.08443 143 SER C N   
3655 C CA  . SER C 143 ? 0.87907 0.80511 0.71450 0.03069  -0.12053 -0.08312 143 SER C CA  
3656 C C   . SER C 143 ? 0.88100 0.82672 0.74628 0.02653  -0.13376 -0.07135 143 SER C C   
3657 O O   . SER C 143 ? 1.01341 0.97441 0.89809 0.02817  -0.11919 -0.06446 143 SER C O   
3658 C CB  . SER C 143 ? 0.87336 0.76492 0.64417 0.03881  -0.11346 -0.08531 143 SER C CB  
3659 O OG  . SER C 143 ? 1.18950 1.06226 0.92787 0.04920  -0.10275 -0.09910 143 SER C OG  
3660 N N   . VAL C 144 ? 0.88056 0.82580 0.74975 0.02193  -0.16341 -0.06966 144 VAL C N   
3661 C CA  . VAL C 144 ? 0.72111 0.69493 0.62541 0.02328  -0.17930 -0.05964 144 VAL C CA  
3662 C C   . VAL C 144 ? 0.95698 0.90422 0.82114 0.02793  -0.20571 -0.05631 144 VAL C C   
3663 O O   . VAL C 144 ? 1.10349 1.02439 0.93419 0.02118  -0.22659 -0.06214 144 VAL C O   
3664 C CB  . VAL C 144 ? 0.89201 0.90841 0.85267 0.01167  -0.19152 -0.05744 144 VAL C CB  
3665 C CG1 . VAL C 144 ? 0.86512 0.92432 0.86893 0.01975  -0.20124 -0.04783 144 VAL C CG1 
3666 C CG2 . VAL C 144 ? 0.68929 0.72087 0.67552 0.00765  -0.16697 -0.06030 144 VAL C CG2 
3667 N N   . ARG C 145 ? 1.04786 0.99503 0.90976 0.04034  -0.20829 -0.04721 145 ARG C N   
3668 C CA  . ARG C 145 ? 1.15110 1.06439 0.96457 0.04780  -0.23339 -0.04215 145 ARG C CA  
3669 C C   . ARG C 145 ? 1.13216 1.07287 0.97503 0.04519  -0.27386 -0.03984 145 ARG C C   
3670 O O   . ARG C 145 ? 1.30167 1.21030 1.09926 0.04127  -0.30188 -0.04161 145 ARG C O   
3671 C CB  . ARG C 145 ? 1.26607 1.16216 1.06402 0.06270  -0.22540 -0.03179 145 ARG C CB  
3672 C CG  . ARG C 145 ? 1.38899 1.27114 1.16884 0.07775  -0.25976 -0.02277 145 ARG C CG  
3673 C CD  . ARG C 145 ? 1.49060 1.32269 1.21986 0.08918  -0.25146 -0.01220 145 ARG C CD  
3674 N NE  . ARG C 145 ? 1.65801 1.43280 1.30537 0.07924  -0.24136 -0.00960 145 ARG C NE  
3675 C CZ  . ARG C 145 ? 1.75438 1.48670 1.33850 0.08344  -0.26740 -0.00469 145 ARG C CZ  
3676 N NH1 . ARG C 145 ? 1.69489 1.43676 1.29239 0.09701  -0.30967 -0.00150 145 ARG C NH1 
3677 N NH2 . ARG C 145 ? 1.82159 1.50427 1.32704 0.07439  -0.25069 -0.00246 145 ARG C NH2 
3678 N N   . ASN C 146 ? 1.10084 1.10326 1.01828 0.04637  -0.27791 -0.03561 146 ASN C N   
3679 C CA  . ASN C 146 ? 1.09754 1.14487 1.05821 0.04457  -0.31497 -0.02978 146 ASN C CA  
3680 C C   . ASN C 146 ? 0.93403 1.03442 0.95566 0.02108  -0.31588 -0.03051 146 ASN C C   
3681 O O   . ASN C 146 ? 0.89948 1.01683 0.94655 0.01617  -0.28534 -0.03283 146 ASN C O   
3682 C CB  . ASN C 146 ? 1.24629 1.33173 1.24624 0.07201  -0.32061 -0.02089 146 ASN C CB  
3683 C CG  . ASN C 146 ? 1.25383 1.27774 1.18953 0.09394  -0.32021 -0.01727 146 ASN C CG  
3684 O OD1 . ASN C 146 ? 1.21347 1.23176 1.15305 0.11310  -0.30086 -0.01477 146 ASN C OD1 
3685 N ND2 . ASN C 146 ? 1.35548 1.32677 1.22505 0.09035  -0.34396 -0.01626 146 ASN C ND2 
3686 N N   . GLU C 147 ? 0.87831 1.00343 0.92132 0.00403  -0.35373 -0.02681 147 GLU C N   
3687 C CA  . GLU C 147 ? 0.91942 1.09072 1.01596 -0.02599 -0.35867 -0.02387 147 GLU C CA  
3688 C C   . GLU C 147 ? 0.85255 1.11305 1.03495 -0.01860 -0.33957 -0.01427 147 GLU C C   
3689 O O   . GLU C 147 ? 0.93131 1.22867 1.14192 0.01059  -0.33899 -0.00963 147 GLU C O   
3690 C CB  . GLU C 147 ? 1.00491 1.18088 1.10348 -0.05120 -0.40861 -0.02047 147 GLU C CB  
3691 C CG  . GLU C 147 ? 1.15706 1.34027 1.24904 -0.03174 -0.44309 -0.01565 147 GLU C CG  
3692 C CD  . GLU C 147 ? 1.28926 1.50395 1.40909 -0.05948 -0.49658 -0.00917 147 GLU C CD  
3693 O OE1 . GLU C 147 ? 1.27915 1.52142 1.43575 -0.09673 -0.50416 -0.00574 147 GLU C OE1 
3694 O OE2 . GLU C 147 ? 1.27335 1.48278 1.37631 -0.04615 -0.53370 -0.00620 147 GLU C OE2 
3695 N N   . GLY C 148 ? 0.74226 1.03341 0.96055 -0.04346 -0.32446 -0.01127 148 GLY C N   
3696 C CA  . GLY C 148 ? 0.64028 1.01799 0.93462 -0.03937 -0.30305 -0.00182 148 GLY C CA  
3697 C C   . GLY C 148 ? 0.73549 1.11137 1.03485 -0.06223 -0.27532 -0.00106 148 GLY C C   
3698 O O   . GLY C 148 ? 0.76819 1.07821 1.01790 -0.08104 -0.27727 -0.00758 148 GLY C O   
3699 N N   . SER C 149 ? 0.61076 1.05626 0.96505 -0.05522 -0.24857 0.00624  149 SER C N   
3700 C CA  . SER C 149 ? 0.61591 1.06261 0.97249 -0.07228 -0.21951 0.00877  149 SER C CA  
3701 C C   . SER C 149 ? 0.68365 1.10486 1.01469 -0.03886 -0.18479 -0.00107 149 SER C C   
3702 O O   . SER C 149 ? 0.71034 1.16428 1.06145 -0.00560 -0.17317 -0.00269 149 SER C O   
3703 C CB  . SER C 149 ? 0.61851 1.16226 1.04883 -0.09333 -0.21240 0.02571  149 SER C CB  
3704 O OG  . SER C 149 ? 0.89544 1.42281 1.31563 -0.13092 -0.20347 0.03314  149 SER C OG  
3705 N N   . TYR C 150 ? 0.73091 1.09058 1.01586 -0.04667 -0.17160 -0.00808 150 TYR C N   
3706 C CA  . TYR C 150 ? 0.66781 0.99383 0.92276 -0.02086 -0.14581 -0.01793 150 TYR C CA  
3707 C C   . TYR C 150 ? 0.76519 1.08086 1.01122 -0.03474 -0.12508 -0.01696 150 TYR C C   
3708 O O   . TYR C 150 ? 0.78314 1.09486 1.03000 -0.06437 -0.13265 -0.01007 150 TYR C O   
3709 C CB  . TYR C 150 ? 0.66126 0.91682 0.86175 -0.01038 -0.15318 -0.02888 150 TYR C CB  
3710 C CG  . TYR C 150 ? 0.76732 1.01853 0.96062 0.00624  -0.17274 -0.02933 150 TYR C CG  
3711 C CD1 . TYR C 150 ? 0.77179 1.02145 0.96071 0.03644  -0.16433 -0.03129 150 TYR C CD1 
3712 C CD2 . TYR C 150 ? 0.58332 0.82179 0.76533 -0.00813 -0.20294 -0.02784 150 TYR C CD2 
3713 C CE1 . TYR C 150 ? 0.66957 0.90653 0.84429 0.05262  -0.18528 -0.02993 150 TYR C CE1 
3714 C CE2 . TYR C 150 ? 0.75623 0.98573 0.92450 0.00722  -0.22404 -0.02736 150 TYR C CE2 
3715 C CZ  . TYR C 150 ? 0.73066 0.96000 0.89577 0.03798  -0.21504 -0.02751 150 TYR C CZ  
3716 O OH  . TYR C 150 ? 0.79145 1.00398 0.93586 0.05368  -0.23954 -0.02527 150 TYR C OH  
3717 N N   . ARG C 151 ? 0.71071 1.01427 0.94203 -0.01361 -0.10225 -0.02359 151 ARG C N   
3718 C CA  . ARG C 151 ? 0.64336 0.92394 0.85419 -0.02131 -0.08591 -0.02508 151 ARG C CA  
3719 C C   . ARG C 151 ? 0.68332 0.91068 0.85593 -0.00558 -0.08136 -0.03724 151 ARG C C   
3720 O O   . ARG C 151 ? 0.73585 0.95195 0.90008 0.01318  -0.08268 -0.04250 151 ARG C O   
3721 C CB  . ARG C 151 ? 0.67869 1.00320 0.90882 -0.01392 -0.06219 -0.02031 151 ARG C CB  
3722 C CG  . ARG C 151 ? 0.79455 1.16964 1.05641 -0.04087 -0.05895 -0.00457 151 ARG C CG  
3723 C CD  . ARG C 151 ? 0.70914 1.12520 0.97970 -0.03023 -0.02931 -0.00075 151 ARG C CD  
3724 N NE  . ARG C 151 ? 0.78587 1.26845 1.09566 -0.05615 -0.02154 0.01758  151 ARG C NE  
3725 C CZ  . ARG C 151 ? 0.81389 1.28851 1.10926 -0.08796 -0.01557 0.03036  151 ARG C CZ  
3726 N NH1 . ARG C 151 ? 0.85527 1.25799 1.09857 -0.09360 -0.01878 0.02555  151 ARG C NH1 
3727 N NH2 . ARG C 151 ? 0.81892 1.36123 1.15383 -0.11552 -0.00715 0.05001  151 ARG C NH2 
3728 N N   . PHE C 152 ? 0.68147 0.87713 0.83155 -0.01457 -0.07759 -0.04007 152 PHE C N   
3729 C CA  . PHE C 152 ? 0.67752 0.83658 0.80140 -0.00370 -0.07227 -0.04961 152 PHE C CA  
3730 C C   . PHE C 152 ? 0.67615 0.83696 0.79426 0.00163  -0.05771 -0.05098 152 PHE C C   
3731 O O   . PHE C 152 ? 0.66253 0.83309 0.78178 -0.00871 -0.05336 -0.04523 152 PHE C O   
3732 C CB  . PHE C 152 ? 0.71777 0.84313 0.82188 -0.01177 -0.08102 -0.05370 152 PHE C CB  
3733 C CG  . PHE C 152 ? 0.85002 0.95639 0.94000 -0.00739 -0.09000 -0.05860 152 PHE C CG  
3734 C CD1 . PHE C 152 ? 0.70615 0.80949 0.78960 0.00447  -0.08519 -0.06098 152 PHE C CD1 
3735 C CD2 . PHE C 152 ? 0.73452 0.81747 0.80841 -0.01490 -0.10392 -0.06082 152 PHE C CD2 
3736 C CE1 . PHE C 152 ? 0.65811 0.74120 0.71994 0.00761  -0.09156 -0.06384 152 PHE C CE1 
3737 C CE2 . PHE C 152 ? 0.81340 0.87461 0.86408 -0.00858 -0.11062 -0.06666 152 PHE C CE2 
3738 C CZ  . PHE C 152 ? 0.80910 0.87326 0.85405 0.00213  -0.10309 -0.06738 152 PHE C CZ  
3739 N N   . SER C 153 ? 0.65974 0.80476 0.76495 0.01562  -0.05204 -0.05782 153 SER C N   
3740 C CA  . SER C 153 ? 0.58134 0.71381 0.66990 0.02032  -0.04339 -0.06209 153 SER C CA  
3741 C C   . SER C 153 ? 0.60709 0.71082 0.68180 0.01505  -0.04902 -0.06744 153 SER C C   
3742 O O   . SER C 153 ? 0.63831 0.72960 0.70983 0.01669  -0.05161 -0.06961 153 SER C O   
3743 C CB  . SER C 153 ? 0.77017 0.90241 0.85123 0.04016  -0.03557 -0.06630 153 SER C CB  
3744 O OG  . SER C 153 ? 0.81585 0.93171 0.87268 0.04491  -0.02833 -0.07156 153 SER C OG  
3745 N N   . PHE C 154 ? 0.66630 0.76338 0.73421 0.00788  -0.05142 -0.06782 154 PHE C N   
3746 C CA  . PHE C 154 ? 0.74392 0.82819 0.80937 0.00370  -0.05808 -0.07198 154 PHE C CA  
3747 C C   . PHE C 154 ? 0.72699 0.79589 0.77508 0.00352  -0.05953 -0.07624 154 PHE C C   
3748 O O   . PHE C 154 ? 0.76119 0.82528 0.79363 0.00408  -0.05928 -0.07555 154 PHE C O   
3749 C CB  . PHE C 154 ? 0.57795 0.66268 0.64746 -0.00024 -0.06602 -0.07003 154 PHE C CB  
3750 C CG  . PHE C 154 ? 0.70281 0.78942 0.77839 -0.00123 -0.06876 -0.06761 154 PHE C CG  
3751 C CD1 . PHE C 154 ? 0.74081 0.82703 0.82010 0.00303  -0.06855 -0.07163 154 PHE C CD1 
3752 C CD2 . PHE C 154 ? 0.69866 0.78486 0.77154 -0.00905 -0.07210 -0.06058 154 PHE C CD2 
3753 C CE1 . PHE C 154 ? 0.55458 0.63318 0.62910 0.00283  -0.07430 -0.07147 154 PHE C CE1 
3754 C CE2 . PHE C 154 ? 0.65601 0.73632 0.72975 -0.01389 -0.08006 -0.05883 154 PHE C CE2 
3755 C CZ  . PHE C 154 ? 0.58868 0.66189 0.66042 -0.00626 -0.08242 -0.06567 154 PHE C CZ  
3756 N N   . HIS C 155 ? 0.60070 0.65778 0.64627 -0.00003 -0.06235 -0.07975 155 HIS C N   
3757 C CA  . HIS C 155 ? 0.55624 0.58874 0.57959 -0.00385 -0.06881 -0.08470 155 HIS C CA  
3758 C C   . HIS C 155 ? 0.62688 0.66773 0.66457 -0.01749 -0.08122 -0.08490 155 HIS C C   
3759 O O   . HIS C 155 ? 0.61017 0.66961 0.67169 -0.02481 -0.08003 -0.08218 155 HIS C O   
3760 C CB  . HIS C 155 ? 0.71169 0.71649 0.71688 -0.00133 -0.06702 -0.08707 155 HIS C CB  
3761 C CG  . HIS C 155 ? 0.73154 0.74028 0.73577 0.01577  -0.05688 -0.08570 155 HIS C CG  
3762 N ND1 . HIS C 155 ? 0.79949 0.80378 0.78669 0.03376  -0.04978 -0.08958 155 HIS C ND1 
3763 C CD2 . HIS C 155 ? 0.75653 0.77786 0.77585 0.01904  -0.05366 -0.08078 155 HIS C CD2 
3764 C CE1 . HIS C 155 ? 0.68577 0.70666 0.68593 0.04757  -0.04365 -0.08655 155 HIS C CE1 
3765 N NE2 . HIS C 155 ? 0.75774 0.78528 0.77493 0.03789  -0.04819 -0.08115 155 HIS C NE2 
3766 N N   . LEU C 156 ? 0.59145 0.62162 0.61397 -0.02025 -0.09303 -0.08774 156 LEU C N   
3767 C CA  . LEU C 156 ? 0.65602 0.70208 0.69776 -0.03107 -0.10952 -0.08752 156 LEU C CA  
3768 C C   . LEU C 156 ? 0.74113 0.76786 0.77258 -0.04877 -0.12262 -0.09041 156 LEU C C   
3769 O O   . LEU C 156 ? 0.73703 0.72068 0.72564 -0.04867 -0.12843 -0.09623 156 LEU C O   
3770 C CB  . LEU C 156 ? 0.62547 0.66734 0.65333 -0.02499 -0.12126 -0.08734 156 LEU C CB  
3771 C CG  . LEU C 156 ? 0.66267 0.72339 0.71150 -0.03136 -0.14399 -0.08722 156 LEU C CG  
3772 C CD1 . LEU C 156 ? 0.67544 0.78157 0.77358 -0.02557 -0.14057 -0.08431 156 LEU C CD1 
3773 C CD2 . LEU C 156 ? 0.80821 0.84815 0.82610 -0.02481 -0.15928 -0.08642 156 LEU C CD2 
3774 N N   . PHE C 157 ? 0.75204 0.81028 0.82063 -0.06452 -0.12744 -0.08627 157 PHE C N   
3775 C CA  . PHE C 157 ? 0.78002 0.82640 0.84700 -0.09052 -0.14278 -0.08551 157 PHE C CA  
3776 C C   . PHE C 157 ? 0.83877 0.92683 0.94267 -0.10217 -0.16371 -0.08372 157 PHE C C   
3777 O O   . PHE C 157 ? 0.81184 0.95577 0.96244 -0.09338 -0.15817 -0.08005 157 PHE C O   
3778 C CB  . PHE C 157 ? 0.83143 0.88603 0.91365 -0.10578 -0.12956 -0.07810 157 PHE C CB  
3779 C CG  . PHE C 157 ? 0.93569 0.94376 0.97883 -0.09435 -0.11615 -0.07943 157 PHE C CG  
3780 C CD1 . PHE C 157 ? 0.89548 0.84056 0.88640 -0.09062 -0.12517 -0.08667 157 PHE C CD1 
3781 C CD2 . PHE C 157 ? 0.73125 0.75716 0.78664 -0.08321 -0.09635 -0.07469 157 PHE C CD2 
3782 C CE1 . PHE C 157 ? 0.90635 0.81404 0.86568 -0.07371 -0.11418 -0.08844 157 PHE C CE1 
3783 C CE2 . PHE C 157 ? 0.90071 0.88827 0.92393 -0.07046 -0.08838 -0.07533 157 PHE C CE2 
3784 C CZ  . PHE C 157 ? 1.01694 0.94889 0.99585 -0.06417 -0.09700 -0.08193 157 PHE C CZ  
3785 N N   . GLU C 158 ? 0.85549 0.91461 0.93591 -0.11889 -0.18981 -0.08737 158 GLU C N   
3786 C CA  . GLU C 158 ? 0.80341 0.90250 0.91952 -0.13233 -0.21685 -0.08532 158 GLU C CA  
3787 C C   . GLU C 158 ? 0.93272 1.03950 1.06778 -0.17208 -0.23244 -0.07983 158 GLU C C   
3788 O O   . GLU C 158 ? 1.10831 1.14865 1.19248 -0.18952 -0.24144 -0.08329 158 GLU C O   
3789 C CB  . GLU C 158 ? 0.83484 0.89377 0.90516 -0.12366 -0.24186 -0.09280 158 GLU C CB  
3790 C CG  . GLU C 158 ? 0.94075 1.03907 1.04650 -0.13721 -0.27693 -0.09047 158 GLU C CG  
3791 C CD  . GLU C 158 ? 1.06786 1.12052 1.11898 -0.12749 -0.30388 -0.09692 158 GLU C CD  
3792 O OE1 . GLU C 158 ? 1.07723 1.07850 1.06897 -0.10728 -0.28892 -0.10179 158 GLU C OE1 
3793 O OE2 . GLU C 158 ? 1.08648 1.15707 1.15349 -0.14137 -0.34043 -0.09616 158 GLU C OE2 
3794 N N   . GLN C 159 ? 0.95538 1.14277 1.16254 -0.18597 -0.23541 -0.07090 159 GLN C N   
3795 C CA  . GLN C 159 ? 0.88943 1.10421 1.12992 -0.23056 -0.25184 -0.06164 159 GLN C CA  
3796 C C   . GLN C 159 ? 1.00831 1.26579 1.28448 -0.23892 -0.28956 -0.06221 159 GLN C C   
3797 O O   . GLN C 159 ? 0.98168 1.31732 1.31828 -0.21822 -0.28811 -0.05988 159 GLN C O   
3798 C CB  . GLN C 159 ? 0.95508 1.24282 1.25593 -0.24074 -0.22180 -0.04876 159 GLN C CB  
3799 C CG  . GLN C 159 ? 1.08795 1.40228 1.41960 -0.29380 -0.23138 -0.03468 159 GLN C CG  
3800 C CD  . GLN C 159 ? 1.17649 1.52073 1.52715 -0.30436 -0.19356 -0.02173 159 GLN C CD  
3801 O OE1 . GLN C 159 ? 1.16272 1.59135 1.56995 -0.28647 -0.16759 -0.01727 159 GLN C OE1 
3802 N NE2 . GLN C 159 ? 1.23729 1.50618 1.53336 -0.33096 -0.19093 -0.01604 159 GLN C NE2 
3803 N N   . ILE C 160 ? 1.34391 1.54695 1.57969 -0.26700 -0.32594 -0.06601 160 ILE C N   
3804 C CA  . ILE C 160 ? 1.31187 1.53526 1.56177 -0.27171 -0.36893 -0.06886 160 ILE C CA  
3805 C C   . ILE C 160 ? 1.31905 1.63856 1.65930 -0.31044 -0.38822 -0.05535 160 ILE C C   
3806 O O   . ILE C 160 ? 1.25984 1.57957 1.61161 -0.35521 -0.38752 -0.04572 160 ILE C O   
3807 C CB  . ILE C 160 ? 1.47158 1.58616 1.62675 -0.28297 -0.40164 -0.08093 160 ILE C CB  
3808 C CG1 . ILE C 160 ? 1.36593 1.42196 1.45217 -0.23706 -0.39003 -0.09299 160 ILE C CG1 
3809 C CG2 . ILE C 160 ? 1.64970 1.78266 1.82330 -0.31433 -0.45558 -0.07972 160 ILE C CG2 
3810 C CD1 . ILE C 160 ? 1.51679 1.47428 1.50683 -0.24022 -0.42054 -0.10619 160 ILE C CD1 
3811 N N   . LYS C 161 ? 1.33558 1.73892 1.74109 -0.29305 -0.40570 -0.05329 161 LYS C N   
3812 C CA  . LYS C 161 ? 1.44743 1.96317 1.95282 -0.32366 -0.42593 -0.04042 161 LYS C CA  
3813 C C   . LYS C 161 ? 1.58697 2.09483 2.08954 -0.35088 -0.48786 -0.04206 161 LYS C C   
3814 O O   . LYS C 161 ? 1.58950 2.15337 2.14576 -0.39205 -0.50265 -0.03265 161 LYS C O   
3815 C CB  . LYS C 161 ? 1.19936 1.82812 1.79074 -0.28076 -0.40517 -0.03716 161 LYS C CB  
3816 C CG  . LYS C 161 ? 1.06990 1.71179 1.66557 -0.25308 -0.34715 -0.03632 161 LYS C CG  
3817 C CD  . LYS C 161 ? 1.05324 1.81942 1.74357 -0.22019 -0.32823 -0.03208 161 LYS C CD  
3818 C CE  . LYS C 161 ? 1.23738 1.97540 1.89591 -0.16202 -0.29525 -0.04220 161 LYS C CE  
3819 N NZ  . LYS C 161 ? 1.28322 2.12628 2.02036 -0.11973 -0.28382 -0.04247 161 LYS C NZ  
3820 N N   . ASP C 162 ? 1.73731 2.17055 2.16801 -0.32345 -0.51475 -0.05514 162 ASP C N   
3821 C CA  . ASP C 162 ? 1.88669 2.29282 2.29005 -0.33976 -0.56558 -0.05970 162 ASP C CA  
3822 C C   . ASP C 162 ? 1.98669 2.25025 2.26767 -0.35798 -0.57864 -0.07146 162 ASP C C   
3823 O O   . ASP C 162 ? 2.01160 2.19077 2.21172 -0.33134 -0.56933 -0.08239 162 ASP C O   
3824 C CB  . ASP C 162 ? 1.89678 2.32100 2.30056 -0.29326 -0.58794 -0.06435 162 ASP C CB  
3825 C CG  . ASP C 162 ? 1.98241 2.54249 2.49970 -0.28257 -0.59633 -0.05537 162 ASP C CG  
3826 O OD1 . ASP C 162 ? 2.08831 2.71985 2.67243 -0.31940 -0.59629 -0.04795 162 ASP C OD1 
3827 O OD2 . ASP C 162 ? 1.87371 2.46672 2.41095 -0.23549 -0.60250 -0.05621 162 ASP C OD2 
3828 N N   . PRO C 163 ? 2.13398 2.36536 2.39553 -0.39999 -0.59951 -0.07045 163 PRO C N   
3829 C CA  . PRO C 163 ? 2.26312 2.35159 2.40242 -0.41156 -0.61012 -0.08286 163 PRO C CA  
3830 C C   . PRO C 163 ? 2.23829 2.24421 2.28319 -0.37799 -0.63171 -0.09772 163 PRO C C   
3831 O O   . PRO C 163 ? 2.17803 2.06666 2.11502 -0.37114 -0.62841 -0.11082 163 PRO C O   
3832 C CB  . PRO C 163 ? 2.35205 2.43823 2.50487 -0.46269 -0.63462 -0.07586 163 PRO C CB  
3833 C CG  . PRO C 163 ? 2.31287 2.54614 2.60040 -0.48282 -0.62402 -0.05837 163 PRO C CG  
3834 C CD  . PRO C 163 ? 2.15621 2.47912 2.50511 -0.43658 -0.61475 -0.05847 163 PRO C CD  
3835 N N   . LYS C 164 ? 2.02779 2.08903 2.10544 -0.35472 -0.65235 -0.09575 164 LYS C N   
3836 C CA  . LYS C 164 ? 1.96608 1.94855 1.94958 -0.32229 -0.66924 -0.10670 164 LYS C CA  
3837 C C   . LYS C 164 ? 1.97548 1.91351 1.90612 -0.28331 -0.63768 -0.11381 164 LYS C C   
3838 O O   . LYS C 164 ? 1.88183 1.73818 1.71545 -0.25904 -0.64248 -0.12337 164 LYS C O   
3839 C CB  . LYS C 164 ? 1.75857 1.80990 1.79050 -0.30807 -0.70177 -0.10022 164 LYS C CB  
3840 C CG  . LYS C 164 ? 1.74359 1.92550 1.89515 -0.28813 -0.68978 -0.08855 164 LYS C CG  
3841 C CD  . LYS C 164 ? 1.83057 1.99525 1.95584 -0.24056 -0.66918 -0.09047 164 LYS C CD  
3842 C CE  . LYS C 164 ? 1.67775 1.94127 1.88766 -0.20716 -0.67708 -0.08133 164 LYS C CE  
3843 N NZ  . LYS C 164 ? 1.82098 2.07702 2.02415 -0.16612 -0.64978 -0.08171 164 LYS C NZ  
3844 N N   . ASP C 165 ? 1.68282 1.67293 1.67266 -0.27786 -0.60496 -0.10881 165 ASP C N   
3845 C CA  . ASP C 165 ? 1.77653 1.73045 1.72242 -0.23797 -0.55731 -0.11325 165 ASP C CA  
3846 C C   . ASP C 165 ? 1.83937 1.70140 1.70509 -0.24233 -0.53019 -0.12386 165 ASP C C   
3847 O O   . ASP C 165 ? 1.72434 1.55927 1.55433 -0.20961 -0.48750 -0.12715 165 ASP C O   
3848 C CB  . ASP C 165 ? 1.65120 1.70140 1.69332 -0.21862 -0.51599 -0.10180 165 ASP C CB  
3849 C CG  . ASP C 165 ? 1.58202 1.71530 1.69380 -0.19741 -0.53550 -0.09377 165 ASP C CG  
3850 O OD1 . ASP C 165 ? 1.56398 1.66679 1.63318 -0.18564 -0.57244 -0.09641 165 ASP C OD1 
3851 O OD2 . ASP C 165 ? 1.32879 1.55449 1.53303 -0.18951 -0.51395 -0.08516 165 ASP C OD2 
3852 N N   . ALA C 166 ? 2.05322 1.86721 1.89131 -0.28136 -0.55527 -0.12872 166 ALA C N   
3853 C CA  . ALA C 166 ? 2.05043 1.77448 1.81402 -0.28121 -0.53130 -0.13909 166 ALA C CA  
3854 C C   . ALA C 166 ? 2.06228 1.68931 1.70804 -0.24603 -0.52463 -0.15601 166 ALA C C   
3855 O O   . ALA C 166 ? 2.02580 1.62852 1.62545 -0.23813 -0.55422 -0.16115 166 ALA C O   
3856 C CB  . ALA C 166 ? 2.18740 1.86914 1.93788 -0.32894 -0.56081 -0.13904 166 ALA C CB  
3857 N N   . THR C 167 ? 1.85979 1.43384 1.45596 -0.22367 -0.48499 -0.16401 167 THR C N   
3858 C CA  . THR C 167 ? 1.87861 1.37075 1.36729 -0.18713 -0.46920 -0.17987 167 THR C CA  
3859 C C   . THR C 167 ? 2.10599 1.48804 1.48732 -0.20144 -0.51195 -0.19818 167 THR C C   
3860 O O   . THR C 167 ? 2.22074 1.52897 1.54906 -0.20206 -0.50611 -0.20815 167 THR C O   
3861 C CB  . THR C 167 ? 1.86292 1.33828 1.33685 -0.15706 -0.41651 -0.18362 167 THR C CB  
3862 O OG1 . THR C 167 ? 1.61251 1.18000 1.18937 -0.15802 -0.38696 -0.16691 167 THR C OG1 
3863 C CG2 . THR C 167 ? 1.87985 1.32679 1.28471 -0.11323 -0.38587 -0.19195 167 THR C CG2 
3864 N N   . PRO C 184 ? 2.07172 2.41149 2.45892 -0.83561 -0.20039 0.18024  184 PRO C N   
3865 C CA  . PRO C 184 ? 2.09098 2.36048 2.44694 -0.81938 -0.25054 0.15498  184 PRO C CA  
3866 C C   . PRO C 184 ? 1.96861 2.13577 2.24738 -0.77198 -0.25929 0.13037  184 PRO C C   
3867 O O   . PRO C 184 ? 1.65146 1.75037 1.86942 -0.76470 -0.23852 0.13506  184 PRO C O   
3868 C CB  . PRO C 184 ? 1.99564 2.41433 2.46565 -0.80199 -0.25120 0.14784  184 PRO C CB  
3869 C CG  . PRO C 184 ? 1.86962 2.39147 2.41214 -0.84753 -0.22743 0.17615  184 PRO C CG  
3870 C CD  . PRO C 184 ? 1.95779 2.44060 2.45000 -0.86321 -0.18599 0.19714  184 PRO C CD  
3871 N N   . GLN C 185 ? 2.39661 2.55280 2.67591 -0.74007 -0.28993 0.10497  185 GLN C N   
3872 C CA  . GLN C 185 ? 2.43730 2.49867 2.64416 -0.69489 -0.30004 0.08016  185 GLN C CA  
3873 C C   . GLN C 185 ? 2.18424 2.31108 2.43764 -0.64909 -0.31124 0.05817  185 GLN C C   
3874 O O   . GLN C 185 ? 2.16516 2.38858 2.49569 -0.66118 -0.32523 0.06109  185 GLN C O   
3875 C CB  . GLN C 185 ? 2.55341 2.44351 2.64244 -0.70064 -0.33553 0.06918  185 GLN C CB  
3876 C CG  . GLN C 185 ? 2.58523 2.45269 2.66884 -0.73687 -0.37358 0.07232  185 GLN C CG  
3877 C CD  . GLN C 185 ? 2.47989 2.39956 2.60399 -0.71687 -0.40073 0.05381  185 GLN C CD  
3878 O OE1 . GLN C 185 ? 2.49337 2.35121 2.56549 -0.67499 -0.41592 0.02881  185 GLN C OE1 
3879 N NE2 . GLN C 185 ? 2.38124 2.41491 2.59626 -0.74518 -0.40665 0.06625  185 GLN C NE2 
3880 N N   . GLU C 186 ? 1.97404 2.04459 2.17487 -0.58268 -0.29909 0.03536  186 GLU C N   
3881 C CA  . GLU C 186 ? 1.94098 2.04986 2.16461 -0.53344 -0.30738 0.01470  186 GLU C CA  
3882 C C   . GLU C 186 ? 1.91735 1.90637 2.04302 -0.48530 -0.31027 -0.00825 186 GLU C C   
3883 O O   . GLU C 186 ? 1.99118 1.87753 2.04084 -0.48781 -0.30758 -0.00884 186 GLU C O   
3884 C CB  . GLU C 186 ? 1.76769 2.00460 2.07569 -0.49578 -0.26822 0.01762  186 GLU C CB  
3885 C CG  . GLU C 186 ? 1.73348 2.08157 2.12823 -0.49293 -0.28662 0.01628  186 GLU C CG  
3886 C CD  . GLU C 186 ? 1.67917 1.97018 2.03271 -0.47341 -0.32806 -0.00351 186 GLU C CD  
3887 O OE1 . GLU C 186 ? 1.56101 1.79508 1.86036 -0.42229 -0.31809 -0.02066 186 GLU C OE1 
3888 O OE2 . GLU C 186 ? 1.80793 2.11268 2.18219 -0.51120 -0.37115 -0.00088 186 GLU C OE2 
3889 N N   . PHE C 187 ? 1.57415 1.57764 1.70108 -0.44021 -0.31545 -0.02620 187 PHE C N   
3890 C CA  . PHE C 187 ? 1.49566 1.40131 1.53680 -0.39535 -0.31663 -0.04727 187 PHE C CA  
3891 C C   . PHE C 187 ? 1.40003 1.35240 1.46226 -0.33817 -0.28125 -0.05425 187 PHE C C   
3892 O O   . PHE C 187 ? 1.22931 1.26652 1.35245 -0.32312 -0.27864 -0.05398 187 PHE C O   
3893 C CB  . PHE C 187 ? 1.33892 1.19332 1.33698 -0.39870 -0.36019 -0.06262 187 PHE C CB  
3894 C CG  . PHE C 187 ? 1.72597 1.47773 1.65655 -0.44350 -0.39855 -0.06400 187 PHE C CG  
3895 C CD1 . PHE C 187 ? 1.93728 1.69330 1.89037 -0.50090 -0.40554 -0.04410 187 PHE C CD1 
3896 C CD2 . PHE C 187 ? 1.75642 1.40177 1.59418 -0.42912 -0.42782 -0.08496 187 PHE C CD2 
3897 C CE1 . PHE C 187 ? 1.86833 1.51958 1.75299 -0.54333 -0.44293 -0.04439 187 PHE C CE1 
3898 C CE2 . PHE C 187 ? 2.05881 1.59605 1.82377 -0.46851 -0.46664 -0.08866 187 PHE C CE2 
3899 C CZ  . PHE C 187 ? 1.93424 1.47891 1.72591 -0.51808 -0.46815 -0.06656 187 PHE C CZ  
3900 N N   . LEU C 188 ? 1.37875 1.00933 1.45541 -0.06750 -0.22221 0.05424  188 LEU C N   
3901 C CA  . LEU C 188 ? 1.09797 0.76712 1.18919 -0.04608 -0.18891 0.04074  188 LEU C CA  
3902 C C   . LEU C 188 ? 1.08836 0.73013 1.13712 -0.02729 -0.18408 0.01177  188 LEU C C   
3903 O O   . LEU C 188 ? 1.13201 0.73528 1.15200 -0.01478 -0.19457 -0.00662 188 LEU C O   
3904 C CB  . LEU C 188 ? 0.97725 0.66972 1.09036 -0.03732 -0.17281 0.04226  188 LEU C CB  
3905 C CG  . LEU C 188 ? 1.10163 0.83848 1.23681 -0.01989 -0.14072 0.03341  188 LEU C CG  
3906 C CD1 . LEU C 188 ? 0.94851 0.73220 1.12341 -0.02811 -0.13115 0.04803  188 LEU C CD1 
3907 C CD2 . LEU C 188 ? 1.05732 0.80245 1.20045 -0.01068 -0.13068 0.03116  188 LEU C CD2 
3908 N N   . GLU C 189 ? 1.08630 0.75022 1.13148 -0.02542 -0.16941 0.00685  189 GLU C N   
3909 C CA  . GLU C 189 ? 1.02415 0.67612 1.02715 -0.01406 -0.16167 -0.01912 189 GLU C CA  
3910 C C   . GLU C 189 ? 1.03939 0.73482 1.05579 -0.00182 -0.13090 -0.02734 189 GLU C C   
3911 O O   . GLU C 189 ? 0.96854 0.69296 1.01122 -0.01010 -0.12242 -0.01078 189 GLU C O   
3912 C CB  . GLU C 189 ? 1.14901 0.78473 1.12337 -0.03253 -0.17688 -0.01372 189 GLU C CB  
3913 C CG  . GLU C 189 ? 1.32747 0.90936 1.25828 -0.03788 -0.20483 -0.02432 189 GLU C CG  
3914 C CD  . GLU C 189 ? 1.59923 1.16687 1.49023 -0.05504 -0.21628 -0.02428 189 GLU C CD  
3915 O OE1 . GLU C 189 ? 1.46264 1.02920 1.37003 -0.07665 -0.23450 0.00219  189 GLU C OE1 
3916 O OE2 . GLU C 189 ? 1.59082 1.15233 1.43454 -0.04756 -0.20757 -0.05115 189 GLU C OE2 
3917 N N   . PHE C 190 ? 0.95833 0.65799 0.95803 0.01818  -0.11718 -0.05382 190 PHE C N   
3918 C CA  . PHE C 190 ? 0.93180 0.67508 0.93844 0.02550  -0.08960 -0.06247 190 PHE C CA  
3919 C C   . PHE C 190 ? 0.92049 0.67528 0.89326 0.01059  -0.08402 -0.06579 190 PHE C C   
3920 O O   . PHE C 190 ? 1.02522 0.75829 0.95660 0.00744  -0.09356 -0.08046 190 PHE C O   
3921 C CB  . PHE C 190 ? 0.90336 0.65589 0.90835 0.05165  -0.07815 -0.09056 190 PHE C CB  
3922 C CG  . PHE C 190 ? 0.93748 0.74041 0.94547 0.05654  -0.05065 -0.10234 190 PHE C CG  
3923 C CD1 . PHE C 190 ? 0.83486 0.66838 0.87662 0.05404  -0.03659 -0.08708 190 PHE C CD1 
3924 C CD2 . PHE C 190 ? 0.91823 0.74132 0.89390 0.06164  -0.03926 -0.12935 190 PHE C CD2 
3925 C CE1 . PHE C 190 ? 0.82138 0.69987 0.86511 0.05388  -0.01482 -0.09499 190 PHE C CE1 
3926 C CE2 . PHE C 190 ? 0.90274 0.78096 0.88230 0.06048  -0.01388 -0.13754 190 PHE C CE2 
3927 C CZ  . PHE C 190 ? 0.85430 0.75786 0.86821 0.05524  -0.00323 -0.11853 190 PHE C CZ  
3928 N N   . ARG C 191 ? 0.89220 0.67853 0.87779 -0.00051 -0.07077 -0.05228 191 ARG C N   
3929 C CA  . ARG C 191 ? 0.93408 0.72869 0.88427 -0.02234 -0.06991 -0.04826 191 ARG C CA  
3930 C C   . ARG C 191 ? 0.93403 0.77360 0.87144 -0.02215 -0.04409 -0.06289 191 ARG C C   
3931 O O   . ARG C 191 ? 0.96095 0.81511 0.85677 -0.02649 -0.03540 -0.08287 191 ARG C O   
3932 C CB  . ARG C 191 ? 0.95266 0.73926 0.92157 -0.04226 -0.08538 -0.01676 191 ARG C CB  
3933 C CG  . ARG C 191 ? 0.96854 0.72149 0.94766 -0.04819 -0.11222 -0.00191 191 ARG C CG  
3934 C CD  . ARG C 191 ? 0.98239 0.70704 0.90937 -0.06435 -0.12877 -0.00607 191 ARG C CD  
3935 N NE  . ARG C 191 ? 1.17854 0.87177 1.11687 -0.07053 -0.15628 0.00749  191 ARG C NE  
3936 C CZ  . ARG C 191 ? 1.19838 0.85959 1.10843 -0.06975 -0.17012 -0.00425 191 ARG C CZ  
3937 N NH1 . ARG C 191 ? 1.31180 0.96615 1.18085 -0.05803 -0.15938 -0.03415 191 ARG C NH1 
3938 N NH2 . ARG C 191 ? 1.28234 0.91914 1.20711 -0.08038 -0.19725 0.01292  191 ARG C NH2 
3939 N N   . LEU C 192 ? 0.87773 0.74423 0.84949 -0.01786 -0.03116 -0.05516 192 LEU C N   
3940 C CA  . LEU C 192 ? 0.88577 0.80012 0.84936 -0.02209 -0.00838 -0.06561 192 LEU C CA  
3941 C C   . LEU C 192 ? 0.82885 0.76235 0.83719 -0.00933 0.00141  -0.06062 192 LEU C C   
3942 O O   . LEU C 192 ? 0.79860 0.70981 0.83951 0.00137  -0.00793 -0.04966 192 LEU C O   
3943 C CB  . LEU C 192 ? 0.90647 0.83135 0.83615 -0.05788 -0.01101 -0.04786 192 LEU C CB  
3944 C CG  . LEU C 192 ? 0.92889 0.84355 0.87779 -0.07687 -0.02356 -0.01645 192 LEU C CG  
3945 C CD1 . LEU C 192 ? 0.92932 0.86039 0.83650 -0.11515 -0.02510 -0.00194 192 LEU C CD1 
3946 C CD2 . LEU C 192 ? 0.88042 0.74817 0.84914 -0.07504 -0.05045 0.00237  192 LEU C CD2 
3947 N N   . GLU C 193 ? 0.82555 0.80505 0.83318 -0.01437 0.02019  -0.06766 193 GLU C N   
3948 C CA  . GLU C 193 ? 0.78699 0.78976 0.83165 -0.00290 0.03031  -0.06709 193 GLU C CA  
3949 C C   . GLU C 193 ? 0.84425 0.88074 0.88131 -0.03041 0.03774  -0.05341 193 GLU C C   
3950 O O   . GLU C 193 ? 0.85895 0.92136 0.86106 -0.05405 0.04409  -0.05419 193 GLU C O   
3951 C CB  . GLU C 193 ? 0.78207 0.80988 0.84127 0.02728  0.04324  -0.09705 193 GLU C CB  
3952 C CG  . GLU C 193 ? 0.83399 0.90914 0.91973 0.03298  0.05874  -0.10301 193 GLU C CG  
3953 C CD  . GLU C 193 ? 1.03542 1.15090 1.12746 0.05889  0.07184  -0.13818 193 GLU C CD  
3954 O OE1 . GLU C 193 ? 1.00234 1.15745 1.06968 0.05208  0.08495  -0.15601 193 GLU C OE1 
3955 O OE2 . GLU C 193 ? 0.93319 1.04200 1.05441 0.08641  0.06758  -0.14923 193 GLU C OE2 
3956 N N   . VAL C 194 ? 0.76205 0.79560 0.82777 -0.03079 0.03449  -0.03939 194 VAL C N   
3957 C CA  . VAL C 194 ? 0.76908 0.82810 0.83011 -0.05762 0.03660  -0.02470 194 VAL C CA  
3958 C C   . VAL C 194 ? 0.73572 0.81975 0.83197 -0.04163 0.04663  -0.03180 194 VAL C C   
3959 O O   . VAL C 194 ? 0.70674 0.76630 0.83031 -0.01770 0.04202  -0.03443 194 VAL C O   
3960 C CB  . VAL C 194 ? 0.78346 0.79757 0.83645 -0.08067 0.01110  0.00427  194 VAL C CB  
3961 C CG1 . VAL C 194 ? 0.75188 0.72718 0.84072 -0.05742 -0.00184 0.00828  194 VAL C CG1 
3962 C CG2 . VAL C 194 ? 0.88899 0.92144 0.92825 -0.11476 0.00705  0.02212  194 VAL C CG2 
3963 N N   . ILE C 195 ? 0.74319 0.88123 0.83764 -0.05662 0.06064  -0.03523 195 ILE C N   
3964 C CA  . ILE C 195 ? 0.71652 0.88741 0.84392 -0.04326 0.06998  -0.04357 195 ILE C CA  
3965 C C   . ILE C 195 ? 0.78124 0.94818 0.90911 -0.07232 0.05883  -0.01922 195 ILE C C   
3966 O O   . ILE C 195 ? 0.83309 1.01217 0.93354 -0.10959 0.05439  -0.00228 195 ILE C O   
3967 C CB  . ILE C 195 ? 0.76316 1.00714 0.89709 -0.03514 0.09284  -0.06921 195 ILE C CB  
3968 C CG1 . ILE C 195 ? 0.83697 1.07316 0.97036 -0.00105 0.09764  -0.09733 195 ILE C CG1 
3969 C CG2 . ILE C 195 ? 0.69808 0.97917 0.86879 -0.02560 0.09844  -0.07417 195 ILE C CG2 
3970 C CD1 . ILE C 195 ? 0.75863 1.05370 0.87260 -0.00335 0.11627  -0.12190 195 ILE C CD1 
3971 N N   . SER C 196 ? 0.69588 0.84302 0.85063 -0.05758 0.05173  -0.01704 196 SER C N   
3972 C CA  . SER C 196 ? 0.70464 0.83457 0.86023 -0.07960 0.03593  0.00279  196 SER C CA  
3973 C C   . SER C 196 ? 0.82363 1.01483 0.98614 -0.10033 0.04588  0.00412  196 SER C C   
3974 O O   . SER C 196 ? 0.79941 1.05110 0.97660 -0.08896 0.06678  -0.01473 196 SER C O   
3975 C CB  . SER C 196 ? 0.68034 0.76850 0.85857 -0.05449 0.02569  0.00029  196 SER C CB  
3976 O OG  . SER C 196 ? 0.65580 0.77582 0.85862 -0.03592 0.03753  -0.01368 196 SER C OG  
3977 N N   . ASN C 197 ? 0.79479 0.96946 0.94898 -0.13037 0.02766  0.02587  197 ASN C N   
3978 C CA  . ASN C 197 ? 0.73743 0.96463 0.90285 -0.15237 0.03182  0.03101  197 ASN C CA  
3979 C C   . ASN C 197 ? 0.80312 1.03807 1.00473 -0.11957 0.03687  0.01470  197 ASN C C   
3980 O O   . ASN C 197 ? 0.75842 0.94296 0.96820 -0.08961 0.03013  0.00725  197 ASN C O   
3981 C CB  . ASN C 197 ? 0.85922 1.05026 1.00308 -0.19391 0.00303  0.06062  197 ASN C CB  
3982 C CG  . ASN C 197 ? 0.87040 1.06168 0.97428 -0.23710 -0.00566 0.08234  197 ASN C CG  
3983 O OD1 . ASN C 197 ? 0.95306 1.20361 1.04575 -0.24740 0.01717  0.07563  197 ASN C OD1 
3984 N ND2 . ASN C 197 ? 1.08595 1.20915 1.16566 -0.26294 -0.04134 0.10759  197 ASN C ND2 
3985 N N   . PRO C 198 ? 0.84626 1.14909 1.07036 -0.12544 0.04869  0.00871  198 PRO C N   
3986 C CA  . PRO C 198 ? 0.76126 1.06850 1.01796 -0.09646 0.04877  -0.00455 198 PRO C CA  
3987 C C   . PRO C 198 ? 0.75255 0.99717 1.00293 -0.10236 0.02429  0.00939  198 PRO C C   
3988 O O   . PRO C 198 ? 0.79973 1.01677 1.02879 -0.13552 0.00547  0.03019  198 PRO C O   
3989 C CB  . PRO C 198 ? 0.66556 1.06456 0.94835 -0.10991 0.06203  -0.00978 198 PRO C CB  
3990 C CG  . PRO C 198 ? 0.74085 1.19413 1.00671 -0.13427 0.07865  -0.00926 198 PRO C CG  
3991 C CD  . PRO C 198 ? 0.71427 1.09977 0.93669 -0.15943 0.06255  0.01321  198 PRO C CD  
3992 N N   . PHE C 199 ? 0.65079 0.86909 0.91627 -0.07007 0.02216  -0.00304 199 PHE C N   
3993 C CA  . PHE C 199 ? 0.69774 0.86442 0.95730 -0.07061 0.00191  0.00320  199 PHE C CA  
3994 C C   . PHE C 199 ? 0.82035 1.00988 1.10394 -0.05227 0.00378  -0.00755 199 PHE C C   
3995 O O   . PHE C 199 ? 0.76214 0.99242 1.06770 -0.03142 0.01789  -0.02126 199 PHE C O   
3996 C CB  . PHE C 199 ? 0.77508 0.87376 1.01874 -0.05149 -0.00574 -0.00020 199 PHE C CB  
3997 C CG  . PHE C 199 ? 0.77786 0.87381 1.03228 -0.01656 0.00770  -0.01635 199 PHE C CG  
3998 C CD1 . PHE C 199 ? 0.74757 0.86118 1.00417 -0.00557 0.02213  -0.02291 199 PHE C CD1 
3999 C CD2 . PHE C 199 ? 0.81183 0.88544 1.06951 0.00186  0.00352  -0.02392 199 PHE C CD2 
4000 C CE1 . PHE C 199 ? 0.74192 0.84627 1.00532 0.02208  0.02891  -0.03463 199 PHE C CE1 
4001 C CE2 . PHE C 199 ? 0.79018 0.86011 1.05313 0.02684  0.01248  -0.03400 199 PHE C CE2 
4002 C CZ  . PHE C 199 ? 0.70293 0.78596 0.96956 0.03641  0.02358  -0.03830 199 PHE C CZ  
4003 N N   . ILE C 200 ? 0.80083 0.95780 1.07809 -0.05883 -0.01434 -0.00235 200 ILE C N   
4004 C CA  . ILE C 200 ? 0.75981 0.93692 1.05528 -0.05068 -0.01878 -0.00763 200 ILE C CA  
4005 C C   . ILE C 200 ? 0.76927 0.89312 1.05147 -0.02650 -0.02495 -0.01678 200 ILE C C   
4006 O O   . ILE C 200 ? 0.83618 0.90670 1.09474 -0.02819 -0.03558 -0.01602 200 ILE C O   
4007 C CB  . ILE C 200 ? 0.83036 1.02286 1.12709 -0.08449 -0.03613 0.00684  200 ILE C CB  
4008 C CG1 . ILE C 200 ? 0.82435 1.09117 1.13826 -0.11133 -0.02540 0.01567  200 ILE C CG1 
4009 C CG2 . ILE C 200 ? 0.96420 1.16428 1.27514 -0.07593 -0.04624 0.00215  200 ILE C CG2 
4010 C CD1 . ILE C 200 ? 0.94149 1.21103 1.24278 -0.15851 -0.04477 0.03854  200 ILE C CD1 
4011 N N   . VAL C 201 ? 0.84719 0.98719 1.14412 -0.00403 -0.01952 -0.02641 201 VAL C N   
4012 C CA  . VAL C 201 ? 0.88549 0.98681 1.16741 0.01179  -0.02616 -0.03231 201 VAL C CA  
4013 C C   . VAL C 201 ? 0.88725 1.00367 1.17781 0.00502  -0.04090 -0.02998 201 VAL C C   
4014 O O   . VAL C 201 ? 0.82903 0.99345 1.14962 0.00817  -0.04064 -0.03062 201 VAL C O   
4015 C CB  . VAL C 201 ? 0.79198 0.89126 1.07733 0.03657  -0.01566 -0.04001 201 VAL C CB  
4016 C CG1 . VAL C 201 ? 0.81674 0.87930 1.07951 0.04537  -0.02139 -0.04281 201 VAL C CG1 
4017 C CG2 . VAL C 201 ? 0.69295 0.78526 0.97415 0.04045  -0.00262 -0.04116 201 VAL C CG2 
4018 N N   . TYR C 202 ? 0.86410 0.94125 1.12973 -0.00299 -0.05534 -0.02941 202 TYR C N   
4019 C CA  . TYR C 202 ? 0.92083 1.00462 1.18843 -0.01424 -0.07362 -0.02566 202 TYR C CA  
4020 C C   . TYR C 202 ? 0.85000 0.90128 1.09303 -0.00122 -0.07995 -0.03251 202 TYR C C   
4021 O O   . TYR C 202 ? 0.84481 0.86468 1.06372 0.01077  -0.07093 -0.04028 202 TYR C O   
4022 C CB  . TYR C 202 ? 0.73586 0.79827 0.98867 -0.04136 -0.09104 -0.01824 202 TYR C CB  
4023 C CG  . TYR C 202 ? 0.74960 0.74870 0.96617 -0.03741 -0.09608 -0.02649 202 TYR C CG  
4024 C CD1 . TYR C 202 ? 0.84970 0.80809 1.03629 -0.02935 -0.10624 -0.03821 202 TYR C CD1 
4025 C CD2 . TYR C 202 ? 0.74930 0.73230 0.96228 -0.03966 -0.09111 -0.02493 202 TYR C CD2 
4026 C CE1 . TYR C 202 ? 0.80482 0.71383 0.96357 -0.02027 -0.10969 -0.05205 202 TYR C CE1 
4027 C CE2 . TYR C 202 ? 0.91109 0.83947 1.09848 -0.03087 -0.09853 -0.03581 202 TYR C CE2 
4028 C CZ  . TYR C 202 ? 0.80410 0.69850 0.96684 -0.01917 -0.10677 -0.05142 202 TYR C CZ  
4029 O OH  . TYR C 202 ? 0.94881 0.79662 1.09089 -0.00552 -0.11335 -0.06819 202 TYR C OH  
4030 N N   . SER C 203 ? 0.88817 0.95174 1.13719 -0.00621 -0.09629 -0.02881 203 SER C N   
4031 C CA  . SER C 203 ? 1.01740 1.05143 1.23699 -0.00077 -0.10648 -0.03219 203 SER C CA  
4032 C C   . SER C 203 ? 1.03329 1.03679 1.22373 -0.01849 -0.12597 -0.03342 203 SER C C   
4033 O O   . SER C 203 ? 1.06821 1.08840 1.27546 -0.03660 -0.14119 -0.02544 203 SER C O   
4034 C CB  . SER C 203 ? 1.04141 1.10307 1.28504 0.00785  -0.11710 -0.02682 203 SER C CB  
4035 O OG  . SER C 203 ? 1.22470 1.25859 1.43670 0.00318  -0.13511 -0.02501 203 SER C OG  
4036 N N   . ALA C 204 ? 1.04945 1.01118 1.19565 -0.01443 -0.12578 -0.04454 204 ALA C N   
4037 C CA  . ALA C 204 ? 1.02836 0.95428 1.13866 -0.02735 -0.14578 -0.05122 204 ALA C CA  
4038 C C   . ALA C 204 ? 1.07214 0.99913 1.16613 -0.03208 -0.16135 -0.04637 204 ALA C C   
4039 O O   . ALA C 204 ? 1.28428 1.20480 1.35400 -0.02357 -0.15324 -0.04962 204 ALA C O   
4040 C CB  . ALA C 204 ? 1.12317 1.00872 1.19455 -0.01739 -0.13700 -0.07181 204 ALA C CB  
4041 N N   . LYS C 205 ? 1.16329 1.09921 1.26944 -0.04895 -0.18607 -0.03643 205 LYS C N   
4042 C CA  . LYS C 205 ? 1.09316 1.02948 1.18706 -0.05492 -0.20671 -0.02936 205 LYS C CA  
4043 C C   . LYS C 205 ? 1.09381 0.98344 1.12096 -0.05892 -0.21237 -0.04245 205 LYS C C   
4044 O O   . LYS C 205 ? 1.25329 1.10902 1.24791 -0.06085 -0.21118 -0.05896 205 LYS C O   
4045 C CB  . LYS C 205 ? 0.99832 0.95718 1.12176 -0.07400 -0.23413 -0.01661 205 LYS C CB  
4046 C CG  . LYS C 205 ? 1.05474 1.07212 1.23908 -0.06697 -0.23811 -0.00375 205 LYS C CG  
4047 C CD  . LYS C 205 ? 1.21195 1.26654 1.43411 -0.08758 -0.26194 0.00774  205 LYS C CD  
4048 C CE  . LYS C 205 ? 1.13353 1.20045 1.36940 -0.10537 -0.25466 0.00991  205 LYS C CE  
4049 N NZ  . LYS C 205 ? 1.09951 1.23303 1.39175 -0.12414 -0.26898 0.02382  205 LYS C NZ  
4050 N N   . LYS C 206 ? 1.20555 1.09344 1.21077 -0.06002 -0.22041 -0.03608 206 LYS C N   
4051 C CA  . LYS C 206 ? 1.24691 1.09966 1.18387 -0.06837 -0.22584 -0.04704 206 LYS C CA  
4052 C C   . LYS C 206 ? 1.29551 1.12729 1.21155 -0.08821 -0.25974 -0.04475 206 LYS C C   
4053 O O   . LYS C 206 ? 1.17867 1.03002 1.12871 -0.09711 -0.28415 -0.02618 206 LYS C O   
4054 C CB  . LYS C 206 ? 1.19957 1.05670 1.11408 -0.06861 -0.22373 -0.03654 206 LYS C CB  
4055 C CG  . LYS C 206 ? 1.35867 1.22968 1.27978 -0.05381 -0.19185 -0.03998 206 LYS C CG  
4056 C CD  . LYS C 206 ? 1.38538 1.26928 1.32540 -0.05190 -0.19944 -0.01864 206 LYS C CD  
4057 C CE  . LYS C 206 ? 1.37070 1.24839 1.26386 -0.05810 -0.18378 -0.01760 206 LYS C CE  
4058 N NZ  . LYS C 206 ? 1.36017 1.24318 1.27592 -0.05436 -0.19084 0.00275  206 LYS C NZ  
4059 N N   . PHE C 207 ? 1.30589 1.09907 1.16826 -0.09361 -0.26281 -0.06587 207 PHE C N   
4060 C CA  . PHE C 207 ? 1.45690 1.21955 1.28735 -0.11369 -0.29684 -0.06741 207 PHE C CA  
4061 C C   . PHE C 207 ? 1.57680 1.30712 1.32639 -0.11777 -0.29601 -0.08742 207 PHE C C   
4062 O O   . PHE C 207 ? 1.61210 1.31164 1.32149 -0.11091 -0.28894 -0.11701 207 PHE C O   
4063 C CB  . PHE C 207 ? 1.26573 1.00618 1.10919 -0.11883 -0.30896 -0.07584 207 PHE C CB  
4064 C CG  . PHE C 207 ? 1.17149 0.95081 1.08737 -0.12636 -0.31627 -0.05233 207 PHE C CG  
4065 C CD1 . PHE C 207 ? 1.17568 0.97789 1.11964 -0.14605 -0.34595 -0.03089 207 PHE C CD1 
4066 C CD2 . PHE C 207 ? 1.12261 0.92131 1.07864 -0.11501 -0.29359 -0.05228 207 PHE C CD2 
4067 C CE1 . PHE C 207 ? 1.13079 0.98311 1.14395 -0.15375 -0.34935 -0.01205 207 PHE C CE1 
4068 C CE2 . PHE C 207 ? 1.08095 0.92384 1.09897 -0.12504 -0.29749 -0.03203 207 PHE C CE2 
4069 C CZ  . PHE C 207 ? 1.08447 0.95853 1.13225 -0.14419 -0.32365 -0.01300 207 PHE C CZ  
4070 N N   . PRO C 208 ? 1.57621 1.31272 1.29849 -0.12938 -0.30556 -0.07304 208 PRO C N   
4071 C CA  . PRO C 208 ? 1.63997 1.35392 1.27850 -0.13883 -0.30281 -0.09008 208 PRO C CA  
4072 C C   . PRO C 208 ? 1.55672 1.22762 1.15013 -0.15200 -0.33132 -0.10704 208 PRO C C   
4073 O O   . PRO C 208 ? 1.45579 1.11664 1.06381 -0.16938 -0.36769 -0.08828 208 PRO C O   
4074 C CB  . PRO C 208 ? 1.63634 1.36236 1.26356 -0.15514 -0.31850 -0.06072 208 PRO C CB  
4075 C CG  . PRO C 208 ? 1.40673 1.15408 1.11166 -0.15256 -0.33969 -0.03282 208 PRO C CG  
4076 C CD  . PRO C 208 ? 1.40499 1.16675 1.17098 -0.13694 -0.32721 -0.04069 208 PRO C CD  
4077 N N   . GLY C 209 ? 1.65817 1.30487 1.19715 -0.14273 -0.31634 -0.14467 209 GLY C N   
4078 C CA  . GLY C 209 ? 1.80752 1.40432 1.29952 -0.14984 -0.34294 -0.16889 209 GLY C CA  
4079 C C   . GLY C 209 ? 1.79427 1.36611 1.31182 -0.12990 -0.34001 -0.19290 209 GLY C C   
4080 O O   . GLY C 209 ? 1.74652 1.27459 1.21365 -0.12260 -0.34886 -0.22963 209 GLY C O   
4081 N N   . LEU C 210 ? 1.73984 1.33584 1.33211 -0.12117 -0.33066 -0.17357 210 LEU C N   
4082 C CA  . LEU C 210 ? 1.82175 1.39411 1.44181 -0.10573 -0.33037 -0.18929 210 LEU C CA  
4083 C C   . LEU C 210 ? 1.79533 1.39710 1.43646 -0.07686 -0.28793 -0.20442 210 LEU C C   
4084 O O   . LEU C 210 ? 1.83369 1.41459 1.44455 -0.05506 -0.27631 -0.24283 210 LEU C O   
4085 C CB  . LEU C 210 ? 1.57941 1.16374 1.26633 -0.12147 -0.35000 -0.15494 210 LEU C CB  
4086 C CG  . LEU C 210 ? 1.61625 1.17571 1.30214 -0.15193 -0.39554 -0.13739 210 LEU C CG  
4087 C CD1 . LEU C 210 ? 1.44005 1.04247 1.20466 -0.16396 -0.39844 -0.10298 210 LEU C CD1 
4088 C CD2 . LEU C 210 ? 1.61756 1.10331 1.25471 -0.15413 -0.42456 -0.16604 210 LEU C CD2 
4089 N N   . THR C 211 ? 1.79287 1.44390 1.48758 -0.07502 -0.26662 -0.17648 211 THR C N   
4090 C CA  . THR C 211 ? 1.82034 1.49945 1.54101 -0.05062 -0.22966 -0.18643 211 THR C CA  
4091 C C   . THR C 211 ? 1.98728 1.67896 1.65734 -0.03765 -0.20287 -0.21608 211 THR C C   
4092 O O   . THR C 211 ? 2.01288 1.71132 1.68807 -0.01334 -0.18006 -0.24281 211 THR C O   
4093 C CB  . THR C 211 ? 1.55393 1.28075 1.33155 -0.05304 -0.21461 -0.15212 211 THR C CB  
4094 O OG1 . THR C 211 ? 1.67265 1.41808 1.43377 -0.06879 -0.22053 -0.13208 211 THR C OG1 
4095 C CG2 . THR C 211 ? 1.28681 1.01507 1.11933 -0.06196 -0.23264 -0.12988 211 THR C CG2 
4096 N N   . THR C 212 ? 2.22164 1.91990 1.84244 -0.05529 -0.20675 -0.21178 212 THR C N   
4097 C CA  . THR C 212 ? 2.26178 1.98107 1.82451 -0.05252 -0.18181 -0.23668 212 THR C CA  
4098 C C   . THR C 212 ? 2.21966 1.98205 1.80377 -0.02984 -0.14045 -0.25267 212 THR C C   
4099 O O   . THR C 212 ? 2.18312 1.98655 1.78365 -0.03707 -0.12026 -0.22917 212 THR C O   
4100 C CB  . THR C 212 ? 2.27816 1.95813 1.77616 -0.04775 -0.19535 -0.27962 212 THR C CB  
4101 O OG1 . THR C 212 ? 2.18519 1.82426 1.65661 -0.07235 -0.23598 -0.26480 212 THR C OG1 
4102 C CG2 . THR C 212 ? 2.34251 2.05687 1.77804 -0.04761 -0.16650 -0.30705 212 THR C CG2 
4103 N N   . GLY D 15  ? 1.68844 1.90002 1.47081 0.14534  0.09051  0.07713  15  GLY D N   
4104 C CA  . GLY D 15  ? 1.69546 1.81673 1.46021 0.15186  0.11700  0.08909  15  GLY D CA  
4105 C C   . GLY D 15  ? 1.71080 1.83345 1.53178 0.13208  0.13976  0.08036  15  GLY D C   
4106 O O   . GLY D 15  ? 1.71173 1.89581 1.57942 0.10619  0.13820  0.06653  15  GLY D O   
4107 N N   . ASN D 16  ? 1.50116 1.55284 1.31494 0.14214  0.15870  0.08959  16  ASN D N   
4108 C CA  . ASN D 16  ? 1.32414 1.36692 1.18817 0.12549  0.18058  0.08282  16  ASN D CA  
4109 C C   . ASN D 16  ? 1.18307 1.17221 1.04023 0.09194  0.21373  0.08964  16  ASN D C   
4110 O O   . ASN D 16  ? 1.17951 1.15544 1.07739 0.07637  0.23291  0.08453  16  ASN D O   
4111 C CB  . ASN D 16  ? 1.37016 1.36988 1.23594 0.15656  0.17843  0.08686  16  ASN D CB  
4112 C CG  . ASN D 16  ? 1.60771 1.68165 1.52533 0.17799  0.15666  0.06625  16  ASN D CG  
4113 O OD1 . ASN D 16  ? 1.52665 1.68866 1.48081 0.16444  0.14609  0.05035  16  ASN D OD1 
4114 N ND2 . ASN D 16  ? 1.58486 1.62435 1.50369 0.21059  0.14831  0.06579  16  ASN D ND2 
4115 N N   . SER D 17  ? 1.19191 1.15543 1.00132 0.08083  0.22006  0.09823  17  SER D N   
4116 C CA  . SER D 17  ? 1.11013 1.02371 0.90851 0.05444  0.25241  0.10222  17  SER D CA  
4117 C C   . SER D 17  ? 1.11150 1.04487 0.88830 0.03557  0.24957  0.09598  17  SER D C   
4118 O O   . SER D 17  ? 1.13972 1.10609 0.89135 0.04506  0.22406  0.09614  17  SER D O   
4119 C CB  . SER D 17  ? 1.19128 1.02354 0.93611 0.06427  0.27066  0.12365  17  SER D CB  
4120 O OG  . SER D 17  ? 1.20731 1.01515 0.88459 0.06598  0.26931  0.13511  17  SER D OG  
4121 N N   . ASN D 18  ? 1.04939 0.96134 0.83635 0.01000  0.27462  0.08895  18  ASN D N   
4122 C CA  . ASN D 18  ? 1.15402 1.07401 0.91960 -0.00677 0.27373  0.07959  18  ASN D CA  
4123 C C   . ASN D 18  ? 1.25321 1.12999 1.01349 -0.02362 0.30957  0.07576  18  ASN D C   
4124 O O   . ASN D 18  ? 1.18721 1.04802 0.98750 -0.03273 0.33051  0.07278  18  ASN D O   
4125 C CB  . ASN D 18  ? 0.98738 0.96502 0.79811 -0.02485 0.24948  0.06083  18  ASN D CB  
4126 C CG  . ASN D 18  ? 1.19628 1.18067 0.97756 -0.03738 0.23728  0.05142  18  ASN D CG  
4127 O OD1 . ASN D 18  ? 1.26009 1.22788 0.98354 -0.02543 0.23459  0.06032  18  ASN D OD1 
4128 N ND2 . ASN D 18  ? 0.96941 0.97408 0.78767 -0.06145 0.22668  0.03290  18  ASN D ND2 
4129 N N   . SER D 19  ? 1.25088 1.11115 0.96050 -0.02680 0.31697  0.07530  19  SER D N   
4130 C CA  . SER D 19  ? 1.37452 1.20380 1.07410 -0.04150 0.35243  0.06912  19  SER D CA  
4131 C C   . SER D 19  ? 1.38302 1.22908 1.06926 -0.05137 0.34713  0.04787  19  SER D C   
4132 O O   . SER D 19  ? 1.41840 1.28401 1.07694 -0.04479 0.31832  0.04657  19  SER D O   
4133 C CB  . SER D 19  ? 1.32601 1.10723 0.96129 -0.03465 0.37458  0.09251  19  SER D CB  
4134 O OG  . SER D 19  ? 1.64517 1.40950 1.27135 -0.01625 0.36051  0.11375  19  SER D OG  
4135 N N   . VAL D 20  ? 1.17795 1.01718 0.88576 -0.06630 0.37321  0.02931  20  VAL D N   
4136 C CA  . VAL D 20  ? 1.36879 1.21998 1.06573 -0.07272 0.36979  0.00370  20  VAL D CA  
4137 C C   . VAL D 20  ? 1.38322 1.21811 1.07105 -0.08126 0.41270  -0.00596 20  VAL D C   
4138 O O   . VAL D 20  ? 1.33301 1.15539 1.05144 -0.08963 0.44043  -0.00077 20  VAL D O   
4139 C CB  . VAL D 20  ? 1.33389 1.21192 1.08920 -0.08346 0.34131  -0.02195 20  VAL D CB  
4140 C CG1 . VAL D 20  ? 1.28091 1.15507 1.09910 -0.09658 0.36302  -0.03853 20  VAL D CG1 
4141 C CG2 . VAL D 20  ? 1.34651 1.23323 1.07495 -0.08372 0.31997  -0.04440 20  VAL D CG2 
4142 N N   . SER D 21  ? 1.65092 1.48945 1.29562 -0.07979 0.41794  -0.02092 21  SER D N   
4143 C CA  . SER D 21  ? 1.58675 1.42218 1.21610 -0.08827 0.45946  -0.03326 21  SER D CA  
4144 C C   . SER D 21  ? 1.60141 1.46218 1.26008 -0.08998 0.45458  -0.07670 21  SER D C   
4145 O O   . SER D 21  ? 1.72428 1.59471 1.38092 -0.08275 0.41683  -0.09264 21  SER D O   
4146 C CB  . SER D 21  ? 1.69259 1.51070 1.23458 -0.08444 0.47499  -0.01389 21  SER D CB  
4147 O OG  . SER D 21  ? 1.91144 1.69911 1.42932 -0.09084 0.49925  0.01938  21  SER D OG  
4148 N N   . ARG D 22  ? 1.52072 1.39218 1.20696 -0.09966 0.49046  -0.09684 22  ARG D N   
4149 C CA  . ARG D 22  ? 1.53433 1.43127 1.24695 -0.09731 0.48804  -0.14299 22  ARG D CA  
4150 C C   . ARG D 22  ? 1.47250 1.38752 1.17012 -0.10525 0.53855  -0.15601 22  ARG D C   
4151 O O   . ARG D 22  ? 1.63758 1.54122 1.31031 -0.11757 0.57323  -0.12670 22  ARG D O   
4152 C CB  . ARG D 22  ? 1.52387 1.42664 1.31957 -0.10129 0.46605  -0.16620 22  ARG D CB  
4153 C CG  . ARG D 22  ? 1.40876 1.32220 1.26257 -0.11278 0.50170  -0.18070 22  ARG D CG  
4154 C CD  . ARG D 22  ? 1.41406 1.32820 1.34412 -0.11548 0.47208  -0.20510 22  ARG D CD  
4155 N NE  . ARG D 22  ? 1.42585 1.33615 1.41266 -0.12845 0.49621  -0.19749 22  ARG D NE  
4156 C CZ  . ARG D 22  ? 1.43871 1.36713 1.46031 -0.13501 0.53129  -0.21924 22  ARG D CZ  
4157 N NH1 . ARG D 22  ? 1.51284 1.47031 1.52026 -0.12901 0.54888  -0.25216 22  ARG D NH1 
4158 N NH2 . ARG D 22  ? 1.48115 1.40217 1.55400 -0.14768 0.54872  -0.20947 22  ARG D NH2 
4159 N N   . ILE D 23  ? 1.66542 1.61011 1.37711 -0.09891 0.54057  -0.20146 23  ILE D N   
4160 C CA  . ILE D 23  ? 1.65220 1.62988 1.35460 -0.10620 0.58829  -0.22254 23  ILE D CA  
4161 C C   . ILE D 23  ? 1.61690 1.62450 1.40120 -0.10503 0.59088  -0.26897 23  ILE D C   
4162 O O   . ILE D 23  ? 1.59448 1.60286 1.41120 -0.09024 0.55019  -0.30224 23  ILE D O   
4163 C CB  . ILE D 23  ? 1.40777 1.40219 1.03795 -0.09546 0.59174  -0.23873 23  ILE D CB  
4164 C CG1 . ILE D 23  ? 1.45789 1.41922 1.00462 -0.09822 0.59073  -0.19048 23  ILE D CG1 
4165 C CG2 . ILE D 23  ? 1.58499 1.62756 1.21337 -0.10373 0.64114  -0.26860 23  ILE D CG2 
4166 C CD1 . ILE D 23  ? 1.51711 1.48301 0.99164 -0.08423 0.57734  -0.20221 23  ILE D CD1 
4167 N N   . THR D 24  ? 1.72646 1.75626 1.54262 -0.12165 0.63558  -0.27094 24  THR D N   
4168 C CA  . THR D 24  ? 1.81586 1.87539 1.71461 -0.12143 0.64064  -0.31327 24  THR D CA  
4169 C C   . THR D 24  ? 1.88828 2.00331 1.78425 -0.11093 0.65948  -0.36638 24  THR D C   
4170 O O   . THR D 24  ? 1.81938 1.94989 1.64720 -0.10599 0.67140  -0.36863 24  THR D O   
4171 C CB  . THR D 24  ? 1.79653 1.85558 1.73548 -0.14511 0.67768  -0.29026 24  THR D CB  
4172 O OG1 . THR D 24  ? 1.84704 1.93312 1.86994 -0.14266 0.67087  -0.32868 24  THR D OG1 
4173 C CG2 . THR D 24  ? 1.76422 1.84110 1.65236 -0.16153 0.71154  -0.26226 24  THR D CG2 
4174 N N   . ARG D 25  ? 1.88711 2.03366 1.85923 -0.10576 0.65831  -0.41076 25  ARG D N   
4175 C CA  . ARG D 25  ? 1.96798 2.17107 1.94955 -0.09019 0.65972  -0.45831 25  ARG D CA  
4176 C C   . ARG D 25  ? 2.03346 2.27800 1.97934 -0.10659 0.70097  -0.43585 25  ARG D C   
4177 O O   . ARG D 25  ? 2.13531 2.42516 2.05204 -0.09488 0.70949  -0.46351 25  ARG D O   
4178 C CB  . ARG D 25  ? 1.84969 2.07134 1.92363 -0.08031 0.63665  -0.50050 25  ARG D CB  
4179 C CG  . ARG D 25  ? 1.80631 1.98714 1.91450 -0.06362 0.58722  -0.52956 25  ARG D CG  
4180 C CD  . ARG D 25  ? 1.86823 2.07583 2.01377 -0.03543 0.55030  -0.59261 25  ARG D CD  
4181 N NE  . ARG D 25  ? 1.89293 2.05835 2.02211 -0.01553 0.49717  -0.62064 25  ARG D NE  
4182 C CZ  . ARG D 25  ? 1.85032 2.02772 1.95905 0.01231  0.46436  -0.66501 25  ARG D CZ  
4183 N NH1 . ARG D 25  ? 1.69285 1.92864 1.79671 0.02598  0.48358  -0.68944 25  ARG D NH1 
4184 N NH2 . ARG D 25  ? 1.83259 1.95882 1.92228 0.02518  0.40150  -0.67437 25  ARG D NH2 
4185 N N   . GLU D 26  ? 2.18419 2.41255 2.12994 -0.13364 0.72373  -0.38680 26  GLU D N   
4186 C CA  . GLU D 26  ? 2.31884 2.58256 2.23519 -0.15442 0.75898  -0.36414 26  GLU D CA  
4187 C C   . GLU D 26  ? 2.30938 2.55419 2.12784 -0.16474 0.77542  -0.32445 26  GLU D C   
4188 O O   . GLU D 26  ? 2.16054 2.42840 1.94443 -0.18562 0.80292  -0.30061 26  GLU D O   
4189 C CB  . GLU D 26  ? 2.35550 2.60564 2.31669 -0.17910 0.76917  -0.33263 26  GLU D CB  
4190 C CG  . GLU D 26  ? 2.41406 2.68433 2.46948 -0.17149 0.75386  -0.37078 26  GLU D CG  
4191 C CD  . GLU D 26  ? 2.55232 2.81793 2.64618 -0.19630 0.76639  -0.34419 26  GLU D CD  
4192 O OE1 . GLU D 26  ? 2.50182 2.73122 2.55564 -0.21721 0.77827  -0.29292 26  GLU D OE1 
4193 O OE2 . GLU D 26  ? 2.63072 2.92668 2.79297 -0.19396 0.76148  -0.37576 26  GLU D OE2 
4194 N N   . GLY D 27  ? 2.16830 2.37066 1.93919 -0.15210 0.75753  -0.31662 27  GLY D N   
4195 C CA  . GLY D 27  ? 2.07316 2.25674 1.74704 -0.15754 0.76751  -0.28539 27  GLY D CA  
4196 C C   . GLY D 27  ? 2.10879 2.22987 1.74000 -0.17608 0.76890  -0.22293 27  GLY D C   
4197 O O   . GLY D 27  ? 2.04451 2.14439 1.59153 -0.18226 0.77491  -0.19290 27  GLY D O   
4198 N N   . LYS D 28  ? 2.05836 2.14745 1.74318 -0.18349 0.76055  -0.20319 28  LYS D N   
4199 C CA  . LYS D 28  ? 1.98840 2.01725 1.63778 -0.19694 0.75767  -0.14664 28  LYS D CA  
4200 C C   . LYS D 28  ? 1.79557 1.77773 1.43095 -0.17972 0.73194  -0.13846 28  LYS D C   
4201 O O   . LYS D 28  ? 1.69865 1.68805 1.38960 -0.16288 0.70712  -0.16982 28  LYS D O   
4202 C CB  . LYS D 28  ? 1.93097 1.94948 1.64150 -0.21359 0.76104  -0.12815 28  LYS D CB  
4203 C CG  . LYS D 28  ? 2.02135 2.09792 1.79470 -0.22095 0.77552  -0.16132 28  LYS D CG  
4204 C CD  . LYS D 28  ? 2.05988 2.11947 1.90995 -0.22729 0.76600  -0.15648 28  LYS D CD  
4205 C CE  . LYS D 28  ? 2.02923 2.14397 1.93552 -0.23655 0.78041  -0.18504 28  LYS D CE  
4206 N NZ  . LYS D 28  ? 1.98106 2.07869 1.96503 -0.23858 0.76618  -0.18837 28  LYS D NZ  
4207 N N   . LYS D 29  ? 1.87477 1.80914 1.43735 -0.18279 0.72794  -0.09421 29  LYS D N   
4208 C CA  . LYS D 29  ? 1.80941 1.70500 1.36845 -0.16173 0.67948  -0.07540 29  LYS D CA  
4209 C C   . LYS D 29  ? 1.68028 1.54368 1.28830 -0.16686 0.67111  -0.04895 29  LYS D C   
4210 O O   . LYS D 29  ? 1.75428 1.58847 1.33753 -0.18418 0.69213  -0.01420 29  LYS D O   
4211 C CB  . LYS D 29  ? 1.94641 1.81001 1.41002 -0.15692 0.66836  -0.04272 29  LYS D CB  
4212 C CG  . LYS D 29  ? 1.71552 1.55433 1.17434 -0.13306 0.61703  -0.03128 29  LYS D CG  
4213 C CD  . LYS D 29  ? 1.99302 1.80458 1.35742 -0.12664 0.60543  -0.00423 29  LYS D CD  
4214 C CE  . LYS D 29  ? 1.90223 1.67387 1.25691 -0.11345 0.56922  0.03111  29  LYS D CE  
4215 N NZ  . LYS D 29  ? 1.89942 1.66346 1.19790 -0.09494 0.53490  0.03626  29  LYS D NZ  
4216 N N   . ILE D 30  ? 1.64890 1.51535 1.32242 -0.15301 0.63821  -0.06520 30  ILE D N   
4217 C CA  . ILE D 30  ? 1.58568 1.42955 1.31434 -0.15622 0.62875  -0.04801 30  ILE D CA  
4218 C C   . ILE D 30  ? 1.54247 1.36323 1.25887 -0.13814 0.58444  -0.02796 30  ILE D C   
4219 O O   . ILE D 30  ? 1.57127 1.40788 1.29203 -0.12459 0.55200  -0.04703 30  ILE D O   
4220 C CB  . ILE D 30  ? 1.38533 1.25648 1.20388 -0.15929 0.62883  -0.08483 30  ILE D CB  
4221 C CG1 . ILE D 30  ? 1.56552 1.45598 1.40492 -0.18069 0.67644  -0.09383 30  ILE D CG1 
4222 C CG2 . ILE D 30  ? 1.39594 1.24561 1.26815 -0.15608 0.60229  -0.07199 30  ILE D CG2 
4223 C CD1 . ILE D 30  ? 1.52311 1.43101 1.45391 -0.18393 0.67186  -0.12118 30  ILE D CD1 
4224 N N   . THR D 31  ? 1.55518 1.34017 1.25618 -0.13816 0.58114  0.00915  31  THR D N   
4225 C CA  . THR D 31  ? 1.46217 1.23157 1.14920 -0.11981 0.54189  0.02875  31  THR D CA  
4226 C C   . THR D 31  ? 1.31717 1.07974 1.06873 -0.11866 0.52932  0.03443  31  THR D C   
4227 O O   . THR D 31  ? 1.53736 1.27664 1.30412 -0.12901 0.55086  0.04913  31  THR D O   
4228 C CB  . THR D 31  ? 1.56777 1.29998 1.17283 -0.11441 0.54166  0.06536  31  THR D CB  
4229 O OG1 . THR D 31  ? 1.65144 1.39298 1.19442 -0.11024 0.53980  0.05930  31  THR D OG1 
4230 C CG2 . THR D 31  ? 1.36685 1.08396 0.97350 -0.09450 0.50426  0.08554  31  THR D CG2 
4231 N N   . TYR D 32  ? 1.27726 1.06091 1.06414 -0.10825 0.49366  0.02272  32  TYR D N   
4232 C CA  . TYR D 32  ? 1.19733 0.98199 1.04082 -0.10608 0.47666  0.02660  32  TYR D CA  
4233 C C   . TYR D 32  ? 1.29384 1.07172 1.10784 -0.08734 0.44860  0.05084  32  TYR D C   
4234 O O   . TYR D 32  ? 1.30898 1.10180 1.08657 -0.07653 0.42488  0.05157  32  TYR D O   
4235 C CB  . TYR D 32  ? 1.16942 0.98652 1.07293 -0.11169 0.45387  -0.00355 32  TYR D CB  
4236 C CG  . TYR D 32  ? 1.25074 1.07842 1.18650 -0.12484 0.47240  -0.03487 32  TYR D CG  
4237 C CD1 . TYR D 32  ? 1.26884 1.10980 1.17233 -0.12297 0.47385  -0.05477 32  TYR D CD1 
4238 C CD2 . TYR D 32  ? 1.24169 1.06755 1.24125 -0.13698 0.48645  -0.04712 32  TYR D CD2 
4239 C CE1 . TYR D 32  ? 1.32468 1.18016 1.26029 -0.13057 0.48834  -0.08850 32  TYR D CE1 
4240 C CE2 . TYR D 32  ? 1.23937 1.07859 1.27227 -0.14607 0.50079  -0.07921 32  TYR D CE2 
4241 C CZ  . TYR D 32  ? 1.30812 1.16388 1.30973 -0.14169 0.50145  -0.10111 32  TYR D CZ  
4242 O OH  . TYR D 32  ? 1.19959 1.07338 1.23645 -0.14647 0.51345  -0.13813 32  TYR D OH  
4243 N N   . LYS D 33  ? 1.18721 0.94342 1.01728 -0.08213 0.44981  0.06883  33  LYS D N   
4244 C CA  . LYS D 33  ? 1.10305 0.85611 0.91354 -0.06024 0.42202  0.08735  33  LYS D CA  
4245 C C   . LYS D 33  ? 1.13233 0.90358 1.00744 -0.05720 0.40755  0.08119  33  LYS D C   
4246 O O   . LYS D 33  ? 1.19055 0.93986 1.09988 -0.06542 0.42561  0.08278  33  LYS D O   
4247 C CB  . LYS D 33  ? 1.37171 1.07167 1.12474 -0.05133 0.43235  0.11698  33  LYS D CB  
4248 C CG  . LYS D 33  ? 1.52217 1.21533 1.22727 -0.02441 0.40094  0.13406  33  LYS D CG  
4249 C CD  . LYS D 33  ? 1.83904 1.50329 1.46067 -0.02088 0.40260  0.15064  33  LYS D CD  
4250 C CE  . LYS D 33  ? 1.85597 1.52195 1.44462 0.00925  0.36410  0.16217  33  LYS D CE  
4251 N NZ  . LYS D 33  ? 1.86188 1.56944 1.43175 0.01556  0.34308  0.15161  33  LYS D NZ  
4252 N N   . LEU D 34  ? 1.06182 0.87532 0.95117 -0.04673 0.37482  0.07459  34  LEU D N   
4253 C CA  . LEU D 34  ? 1.04247 0.88393 0.98593 -0.04280 0.35766  0.06856  34  LEU D CA  
4254 C C   . LEU D 34  ? 1.09942 0.94666 1.01630 -0.01389 0.33500  0.08289  34  LEU D C   
4255 O O   . LEU D 34  ? 1.09561 0.96027 0.97204 -0.00184 0.31629  0.08712  34  LEU D O   
4256 C CB  . LEU D 34  ? 0.97416 0.86916 0.95791 -0.05844 0.33595  0.04736  34  LEU D CB  
4257 C CG  . LEU D 34  ? 1.02150 0.91470 1.04894 -0.08470 0.34760  0.02754  34  LEU D CG  
4258 C CD1 . LEU D 34  ? 0.80195 0.74237 0.85501 -0.09973 0.31550  0.01115  34  LEU D CD1 
4259 C CD2 . LEU D 34  ? 1.05280 0.92362 1.12705 -0.09039 0.36647  0.02720  34  LEU D CD2 
4260 N N   . ASN D 35  ? 1.04134 0.87284 0.97993 -0.00082 0.33459  0.08874  35  ASN D N   
4261 C CA  . ASN D 35  ? 1.00085 0.83955 0.91840 0.03149  0.30926  0.09728  35  ASN D CA  
4262 C C   . ASN D 35  ? 1.00467 0.87541 0.97977 0.03961  0.29788  0.08558  35  ASN D C   
4263 O O   . ASN D 35  ? 1.02674 0.86982 1.03515 0.02911  0.31534  0.08421  35  ASN D O   
4264 C CB  . ASN D 35  ? 1.11255 0.87812 0.97131 0.04757  0.31649  0.12090  35  ASN D CB  
4265 C CG  . ASN D 35  ? 1.12445 0.88431 0.97201 0.08423  0.28826  0.12643  35  ASN D CG  
4266 O OD1 . ASN D 35  ? 1.37282 1.15004 1.18579 0.10686  0.26317  0.12905  35  ASN D OD1 
4267 N ND2 . ASN D 35  ? 1.43730 1.17192 1.31378 0.09236  0.28983  0.12653  35  ASN D ND2 
4268 N N   . ILE D 36  ? 0.99586 0.92913 0.98296 0.05724  0.26893  0.07597  36  ILE D N   
4269 C CA  . ILE D 36  ? 0.96910 0.95019 1.01103 0.06350  0.25699  0.06075  36  ILE D CA  
4270 C C   . ILE D 36  ? 1.03633 0.97978 1.06727 0.09982  0.24900  0.06717  36  ILE D C   
4271 O O   . ILE D 36  ? 0.96362 0.91215 0.96144 0.13206  0.22645  0.07066  36  ILE D O   
4272 C CB  . ILE D 36  ? 0.83219 0.90695 0.89262 0.06305  0.23013  0.04582  36  ILE D CB  
4273 C CG1 . ILE D 36  ? 0.95019 1.04897 1.01633 0.02489  0.23303  0.04085  36  ILE D CG1 
4274 C CG2 . ILE D 36  ? 0.78513 0.91677 0.90035 0.06707  0.22001  0.02875  36  ILE D CG2 
4275 C CD1 . ILE D 36  ? 0.76587 0.95097 0.84014 0.01712  0.20494  0.03060  36  ILE D CD1 
4276 N N   . MET D 37  ? 1.01729 0.91887 1.07500 0.09528  0.26451  0.06802  37  MET D N   
4277 C CA  . MET D 37  ? 1.06463 0.91979 1.11270 0.12784  0.25452  0.07350  37  MET D CA  
4278 C C   . MET D 37  ? 0.96497 0.88804 1.05062 0.15617  0.22823  0.05181  37  MET D C   
4279 O O   . MET D 37  ? 1.04307 0.95095 1.10854 0.19661  0.20491  0.05101  37  MET D O   
4280 C CB  . MET D 37  ? 1.16937 0.95704 1.23402 0.10983  0.27961  0.08183  37  MET D CB  
4281 C CG  . MET D 37  ? 1.18273 0.89982 1.20670 0.08596  0.30642  0.10348  37  MET D CG  
4282 S SD  . MET D 37  ? 1.50873 1.20394 1.45241 0.10026  0.29513  0.12128  37  MET D SD  
4283 C CE  . MET D 37  ? 1.39051 1.00056 1.28547 0.13487  0.27441  0.14074  37  MET D CE  
4284 N N   . GLN D 38  ? 0.86858 0.86617 1.00746 0.13527  0.23000  0.03292  38  GLN D N   
4285 C CA  . GLN D 38  ? 0.81626 0.88955 0.99605 0.15532  0.20993  0.00968  38  GLN D CA  
4286 C C   . GLN D 38  ? 0.84161 1.01757 1.04554 0.13194  0.20120  -0.00461 38  GLN D C   
4287 O O   . GLN D 38  ? 0.77468 0.96754 1.00548 0.09076  0.21434  -0.00709 38  GLN D O   
4288 C CB  . GLN D 38  ? 0.81456 0.86730 1.03735 0.14787  0.22170  0.00195  38  GLN D CB  
4289 C CG  . GLN D 38  ? 0.83075 0.96557 1.09670 0.16547  0.20404  -0.02444 38  GLN D CG  
4290 C CD  . GLN D 38  ? 0.97342 1.06006 1.25947 0.18350  0.20598  -0.02953 38  GLN D CD  
4291 O OE1 . GLN D 38  ? 1.15309 1.22045 1.42548 0.22863  0.18606  -0.03549 38  GLN D OE1 
4292 N NE2 . GLN D 38  ? 0.81896 0.88123 1.13660 0.14918  0.22715  -0.02793 38  GLN D NE2 
4293 N N   . GLN D 39  ? 1.04801 0.82338 1.14701 0.03840  0.15614  0.04561  39  GLN D N   
4294 C CA  . GLN D 39  ? 1.07721 0.83095 1.17066 0.07337  0.17841  0.02969  39  GLN D CA  
4295 C C   . GLN D 39  ? 1.11418 0.85682 1.20133 0.08340  0.15959  0.01911  39  GLN D C   
4296 O O   . GLN D 39  ? 1.05192 0.78079 1.12684 0.06205  0.12637  0.01217  39  GLN D O   
4297 C CB  . GLN D 39  ? 1.09781 0.79037 1.15611 0.07567  0.18423  0.00633  39  GLN D CB  
4298 C CG  . GLN D 39  ? 1.14662 0.84793 1.20088 0.06651  0.20707  0.01410  39  GLN D CG  
4299 C CD  . GLN D 39  ? 1.27177 0.98116 1.33665 0.09489  0.25010  0.00462  39  GLN D CD  
4300 O OE1 . GLN D 39  ? 1.21242 0.90670 1.28136 0.12132  0.26104  -0.00964 39  GLN D OE1 
4301 N NE2 . GLN D 39  ? 1.20053 0.93237 1.26892 0.08727  0.27725  0.01077  39  GLN D NE2 
4302 N N   . PRO D 40  ? 1.23605 0.98263 1.32971 0.11373  0.18192  0.01699  40  PRO D N   
4303 C CA  . PRO D 40  ? 1.17345 0.89588 1.24728 0.12109  0.16889  0.00131  40  PRO D CA  
4304 C C   . PRO D 40  ? 1.01269 0.66823 1.05527 0.12352  0.17003  -0.03499 40  PRO D C   
4305 O O   . PRO D 40  ? 1.13030 0.76253 1.16914 0.13550  0.19381  -0.04596 40  PRO D O   
4306 C CB  . PRO D 40  ? 1.18142 0.93045 1.27341 0.15230  0.19635  0.01781  40  PRO D CB  
4307 C CG  . PRO D 40  ? 1.03320 0.78880 1.14689 0.16771  0.23266  0.02310  40  PRO D CG  
4308 C CD  . PRO D 40  ? 1.05171 0.82487 1.17241 0.14101  0.22178  0.02931  40  PRO D CD  
4309 N N   . LYS D 41  ? 1.07201 0.70001 1.09506 0.11070  0.14358  -0.05664 41  LYS D N   
4310 C CA  . LYS D 41  ? 1.25661 0.82585 1.25849 0.11249  0.14023  -0.09503 41  LYS D CA  
4311 C C   . LYS D 41  ? 1.32130 0.87439 1.31096 0.13009  0.15862  -0.11573 41  LYS D C   
4312 O O   . LYS D 41  ? 1.30479 0.82769 1.28908 0.14612  0.18215  -0.13734 41  LYS D O   
4313 C CB  . LYS D 41  ? 1.27198 0.81555 1.26601 0.08636  0.10112  -0.11169 41  LYS D CB  
4314 C CG  . LYS D 41  ? 1.45470 1.01146 1.45734 0.06334  0.08187  -0.08778 41  LYS D CG  
4315 C CD  . LYS D 41  ? 1.27645 0.84518 1.28280 0.03645  0.04966  -0.08642 41  LYS D CD  
4316 C CE  . LYS D 41  ? 1.64462 1.22634 1.66032 0.01033  0.03424  -0.06150 41  LYS D CE  
4317 N NZ  . LYS D 41  ? 1.82543 1.34665 1.82700 0.00050  0.01783  -0.07336 41  LYS D NZ  
4318 N N   A ARG D 42  ? 1.27536 0.85002 1.25834 0.12486  0.14901  -0.10929 42  ARG D N   
4319 N N   B ARG D 42  ? 1.29847 0.87138 1.28074 0.12413  0.14802  -0.11094 42  ARG D N   
4320 C CA  A ARG D 42  ? 1.24995 0.80929 1.21381 0.13641  0.16663  -0.12559 42  ARG D CA  
4321 C CA  B ARG D 42  ? 1.18103 0.73950 1.14425 0.13576  0.16584  -0.12675 42  ARG D CA  
4322 C C   A ARG D 42  ? 1.24267 0.84599 1.20110 0.13428  0.15949  -0.09590 42  ARG D C   
4323 C C   B ARG D 42  ? 1.29851 0.90106 1.25621 0.13360  0.15878  -0.09700 42  ARG D C   
4324 O O   A ARG D 42  ? 1.21683 0.86065 1.18735 0.11938  0.13440  -0.07357 42  ARG D O   
4325 O O   B ARG D 42  ? 1.22794 0.86982 1.19662 0.11778  0.13278  -0.07612 42  ARG D O   
4326 C CB  A ARG D 42  ? 1.33059 0.84743 1.27734 0.12323  0.15307  -0.17300 42  ARG D CB  
4327 C CB  B ARG D 42  ? 1.41504 0.93065 1.36099 0.12324  0.15341  -0.17450 42  ARG D CB  
4328 C CG  A ARG D 42  ? 1.39913 0.87097 1.34712 0.13566  0.17140  -0.20872 42  ARG D CG  
4329 C CG  B ARG D 42  ? 1.37843 0.84984 1.32622 0.13606  0.17216  -0.20913 42  ARG D CG  
4330 C CD  A ARG D 42  ? 1.44106 0.87833 1.39137 0.12053  0.14342  -0.24963 42  ARG D CD  
4331 C CD  B ARG D 42  ? 1.43490 0.87083 1.38340 0.12177  0.14695  -0.25284 42  ARG D CD  
4332 N NE  A ARG D 42  ? 1.42171 0.85505 1.38520 0.10998  0.11533  -0.23689 42  ARG D NE  
4333 N NE  B ARG D 42  ? 1.41735 0.83948 1.37307 0.13237  0.14645  -0.27446 42  ARG D NE  
4334 C CZ  A ARG D 42  ? 1.44265 0.87017 1.41002 0.08838  0.08110  -0.24201 42  ARG D CZ  
4335 C CZ  B ARG D 42  ? 1.35389 0.77056 1.30753 0.12595  0.10957  -0.29204 42  ARG D CZ  
4336 N NH1 A ARG D 42  ? 1.50223 0.93140 1.46285 0.07450  0.07014  -0.26316 42  ARG D NH1 
4337 N NH1 B ARG D 42  ? 1.27855 0.67284 1.23193 0.10927  0.08696  -0.30726 42  ARG D NH1 
4338 N NH2 A ARG D 42  ? 1.28311 0.70203 1.25924 0.07809  0.05886  -0.22560 42  ARG D NH2 
4339 N NH2 B ARG D 42  ? 1.28391 0.71220 1.22911 0.13627  0.09808  -0.29142 42  ARG D NH2 
4340 N N   . ALA D 43  ? 1.24402 0.84000 1.18367 0.14852  0.18159  -0.09439 43  ALA D N   
4341 C CA  . ALA D 43  ? 1.18767 0.82301 1.11619 0.14920  0.17383  -0.06238 43  ALA D CA  
4342 C C   . ALA D 43  ? 1.25233 0.85799 1.14047 0.14986  0.18979  -0.08015 43  ALA D C   
4343 O O   . ALA D 43  ? 1.29415 0.85356 1.17290 0.15601  0.21531  -0.11217 43  ALA D O   
4344 C CB  . ALA D 43  ? 1.29818 0.97035 1.25710 0.17474  0.18962  -0.01595 43  ALA D CB  
4345 N N   . ARG D 44  ? 1.21346 0.84896 1.07662 0.14185  0.17503  -0.05871 44  ARG D N   
4346 C CA  . ARG D 44  ? 1.20995 0.82220 1.02565 0.13770  0.18945  -0.06913 44  ARG D CA  
4347 C C   . ARG D 44  ? 1.32705 0.94578 1.13803 0.16495  0.21116  -0.02248 44  ARG D C   
4348 O O   . ARG D 44  ? 1.22792 0.89449 1.05778 0.17581  0.19414  0.02323  44  ARG D O   
4349 C CB  . ARG D 44  ? 1.22970 0.86756 1.01068 0.10634  0.15777  -0.07892 44  ARG D CB  
4350 C CG  . ARG D 44  ? 1.36249 0.98480 1.08537 0.09749  0.17147  -0.08326 44  ARG D CG  
4351 C CD  . ARG D 44  ? 1.47853 1.14229 1.16669 0.06717  0.13701  -0.08135 44  ARG D CD  
4352 N NE  . ARG D 44  ? 1.47089 1.13617 1.09975 0.06268  0.14521  -0.06087 44  ARG D NE  
4353 C CZ  . ARG D 44  ? 1.66798 1.33179 1.24245 0.03016  0.14008  -0.09044 44  ARG D CZ  
4354 N NH1 . ARG D 44  ? 1.57099 1.23186 1.14910 0.00102  0.12722  -0.14478 44  ARG D NH1 
4355 N NH2 . ARG D 44  ? 1.55018 1.21396 1.06450 0.02597  0.14865  -0.06495 44  ARG D NH2 
4356 N N   . ALA D 45  ? 1.23623 0.80666 1.02656 0.17617  0.24863  -0.03470 45  ALA D N   
4357 C CA  . ALA D 45  ? 1.26841 0.83199 1.05325 0.20241  0.27242  0.00872  45  ALA D CA  
4358 C C   . ALA D 45  ? 1.32338 0.91937 1.06885 0.19483  0.24790  0.04724  45  ALA D C   
4359 O O   . ALA D 45  ? 1.39565 0.98903 1.09109 0.16604  0.23545  0.02564  45  ALA D O   
4360 C CB  . ALA D 45  ? 1.28369 0.78416 1.04656 0.20780  0.31776  -0.01763 45  ALA D CB  
4361 N N   . CYS D 46  ? 1.33875 0.96802 1.10833 0.22063  0.24036  0.10323  46  CYS D N   
4362 C CA  . CYS D 46  ? 1.39596 1.06179 1.13185 0.21799  0.21237  0.14747  46  CYS D CA  
4363 C C   . CYS D 46  ? 1.58030 1.20185 1.26930 0.23054  0.23847  0.17472  46  CYS D C   
4364 O O   . CYS D 46  ? 1.93090 1.57527 1.57797 0.22599  0.21527  0.21248  46  CYS D O   
4365 C CB  . CYS D 46  ? 1.38399 1.11674 1.17589 0.23983  0.18449  0.19551  46  CYS D CB  
4366 S SG  . CYS D 46  ? 1.57479 1.29580 1.43674 0.28929  0.21911  0.22827  46  CYS D SG  
4367 N N   . GLY D 47  ? 1.59635 1.15509 1.28890 0.24408  0.28523  0.15706  47  GLY D N   
4368 C CA  . GLY D 47  ? 1.85139 1.35942 1.49874 0.25298  0.31448  0.18145  47  GLY D CA  
4369 C C   . GLY D 47  ? 2.05739 1.58349 1.72540 0.28883  0.30504  0.25331  47  GLY D C   
4370 O O   . GLY D 47  ? 1.97121 1.54139 1.70621 0.31443  0.29000  0.27747  47  GLY D O   
4371 N N   . GLN D 48  ? 2.40632 1.89785 2.01566 0.28975  0.31380  0.28800  48  GLN D N   
4372 C CA  . GLN D 48  ? 2.49625 1.99993 2.11642 0.32373  0.29963  0.36138  48  GLN D CA  
4373 C C   . GLN D 48  ? 2.87664 2.38254 2.40748 0.30230  0.27433  0.39525  48  GLN D C   
4374 O O   . GLN D 48  ? 2.86153 2.36444 2.32630 0.25981  0.26988  0.35788  48  GLN D O   
4375 C CB  . GLN D 48  ? 2.33119 1.76893 1.98313 0.35937  0.34844  0.37982  48  GLN D CB  
4376 C CG  . GLN D 48  ? 2.36692 1.72472 1.98043 0.34001  0.40171  0.33247  48  GLN D CG  
4377 C CD  . GLN D 48  ? 2.24087 1.59364 1.90854 0.33714  0.42737  0.26924  48  GLN D CD  
4378 O OE1 . GLN D 48  ? 1.96682 1.34875 1.70902 0.36310  0.42581  0.27292  48  GLN D OE1 
4379 N NE2 . GLN D 48  ? 2.25771 1.57609 1.88826 0.30474  0.45054  0.21025  48  GLN D NE2 
4380 N N   . GLY D 49  ? 3.27960 2.79170 2.80925 0.33202  0.25724  0.46629  49  GLY D N   
4381 C CA  . GLY D 49  ? 3.59683 3.10819 3.03673 0.31482  0.23201  0.50862  49  GLY D CA  
4382 C C   . GLY D 49  ? 3.58905 3.19421 3.02500 0.30547  0.16664  0.53395  49  GLY D C   
4383 O O   . GLY D 49  ? 3.47245 3.14524 2.98315 0.31659  0.13994  0.52615  49  GLY D O   
4384 N N   . SER D 50  ? 3.31919 2.92886 2.66178 0.28116  0.14148  0.56411  50  SER D N   
4385 C CA  . SER D 50  ? 3.19907 2.89874 2.52654 0.27007  0.07687  0.59317  50  SER D CA  
4386 C C   . SER D 50  ? 3.14813 2.90922 2.49460 0.23370  0.05607  0.52943  50  SER D C   
4387 O O   . SER D 50  ? 3.10129 2.94531 2.50039 0.24034  0.01150  0.54166  50  SER D O   
4388 C CB  . SER D 50  ? 3.17050 2.85635 2.37896 0.24311  0.05884  0.63010  50  SER D CB  
4389 O OG  . SER D 50  ? 3.06017 2.73292 2.18958 0.18571  0.07280  0.56809  50  SER D OG  
4390 N N   . LYS D 51  ? 3.09183 2.81345 2.39990 0.19493  0.08777  0.46046  51  LYS D N   
4391 C CA  . LYS D 51  ? 2.94263 2.71281 2.26909 0.16060  0.06905  0.39925  51  LYS D CA  
4392 C C   . LYS D 51  ? 3.02155 2.81893 2.45751 0.18613  0.06963  0.38173  51  LYS D C   
4393 O O   . LYS D 51  ? 2.95030 2.81170 2.41926 0.16948  0.03608  0.36082  51  LYS D O   
4394 C CB  . LYS D 51  ? 2.78446 2.50127 2.05468 0.11854  0.10543  0.32863  51  LYS D CB  
4395 C CG  . LYS D 51  ? 2.63893 2.38680 1.82278 0.06657  0.08023  0.30534  51  LYS D CG  
4396 C CD  . LYS D 51  ? 2.59511 2.31786 1.67958 0.05729  0.08185  0.35296  51  LYS D CD  
4397 C CE  . LYS D 51  ? 2.45726 2.19372 1.44561 -0.00189 0.07441  0.31259  51  LYS D CE  
4398 N NZ  . LYS D 51  ? 2.33403 2.03290 1.21444 -0.01667 0.08602  0.35336  51  LYS D NZ  
4399 N N   . SER D 52  ? 3.30807 3.05716 2.79858 0.22320  0.10888  0.38828  52  SER D N   
4400 C CA  . SER D 52  ? 3.16710 2.93751 2.75370 0.24348  0.11511  0.36791  52  SER D CA  
4401 C C   . SER D 52  ? 3.16116 3.01681 2.81314 0.26568  0.07157  0.41106  52  SER D C   
4402 O O   . SER D 52  ? 2.94024 2.83761 2.65642 0.26353  0.06190  0.38715  52  SER D O   
4403 C CB  . SER D 52  ? 2.92844 2.63131 2.55417 0.27736  0.16757  0.36723  52  SER D CB  
4404 O OG  . SER D 52  ? 2.94039 2.63675 2.58458 0.31835  0.16908  0.43248  52  SER D OG  
4405 N N   . HIS D 53  ? 3.02319 2.90659 2.66123 0.28646  0.04449  0.47484  53  HIS D N   
4406 C CA  . HIS D 53  ? 2.91821 2.88645 2.62833 0.31285  0.00380  0.51809  53  HIS D CA  
4407 C C   . HIS D 53  ? 2.85006 2.90500 2.55329 0.27685  -0.04824 0.50385  53  HIS D C   
4408 O O   . HIS D 53  ? 2.70777 2.84225 2.48077 0.29273  -0.08132 0.52831  53  HIS D O   
4409 C CB  . HIS D 53  ? 2.90899 2.87751 2.61000 0.35038  -0.01165 0.59357  53  HIS D CB  
4410 C CG  . HIS D 53  ? 2.90385 2.79173 2.62826 0.39082  0.03795  0.61337  53  HIS D CG  
4411 N ND1 . HIS D 53  ? 2.79921 2.68327 2.62124 0.42575  0.06720  0.60578  53  HIS D ND1 
4412 C CD2 . HIS D 53  ? 2.95891 2.76627 2.62117 0.39949  0.06512  0.63939  53  HIS D CD2 
4413 C CE1 . HIS D 53  ? 2.76698 2.57178 2.58875 0.45479  0.11020  0.62358  53  HIS D CE1 
4414 N NE2 . HIS D 53  ? 2.89751 2.65265 2.62389 0.43972  0.10990  0.64532  53  HIS D NE2 
4415 N N   . THR D 54  ? 2.96388 2.98227 2.53173 0.08991  0.18487  0.04901  54  THR D N   
4416 C CA  . THR D 54  ? 2.88407 2.86952 2.41475 0.12334  0.17649  0.00046  54  THR D CA  
4417 C C   . THR D 54  ? 2.79975 2.82096 2.33887 0.15321  0.21490  -0.01871 54  THR D C   
4418 O O   . THR D 54  ? 2.78265 2.77328 2.28720 0.18293  0.21031  -0.06067 54  THR D O   
4419 C CB  . THR D 54  ? 2.89480 2.85418 2.32466 0.13635  0.16171  -0.00494 54  THR D CB  
4420 O OG1 . THR D 54  ? 2.92229 2.92327 2.30660 0.12492  0.18822  0.04156  54  THR D OG1 
4421 C CG2 . THR D 54  ? 2.84422 2.74399 2.27045 0.12323  0.10724  -0.01438 54  THR D CG2 
4422 N N   . ASP D 55  ? 2.73497 2.81832 2.32133 0.14759  0.24974  0.00850  55  ASP D N   
4423 C CA  . ASP D 55  ? 2.63182 2.75495 2.23206 0.18013  0.28551  -0.00734 55  ASP D CA  
4424 C C   . ASP D 55  ? 2.52510 2.68134 2.21716 0.16964  0.29459  0.00639  55  ASP D C   
4425 O O   . ASP D 55  ? 2.43460 2.65707 2.15480 0.18118  0.32892  0.02117  55  ASP D O   
4426 C CB  . ASP D 55  ? 2.64326 2.83027 2.19271 0.19402  0.32728  0.01163  55  ASP D CB  
4427 C CG  . ASP D 55  ? 2.66185 2.87318 2.19849 0.24150  0.35853  -0.02156 55  ASP D CG  
4428 O OD1 . ASP D 55  ? 2.71311 2.88650 2.28314 0.26197  0.34617  -0.05531 55  ASP D OD1 
4429 O OD2 . ASP D 55  ? 2.55854 2.82602 2.05160 0.25867  0.39627  -0.01375 55  ASP D OD2 
4430 N N   . ARG D 56  ? 2.48413 2.59948 2.22420 0.14839  0.26378  0.00110  56  ARG D N   
4431 C CA  . ARG D 56  ? 2.16115 2.30272 1.97954 0.13675  0.26786  0.01335  56  ARG D CA  
4432 C C   . ARG D 56  ? 1.86888 1.97260 1.70882 0.16121  0.26205  -0.01994 56  ARG D C   
4433 O O   . ARG D 56  ? 1.79908 1.84612 1.60260 0.17881  0.24780  -0.05457 56  ARG D O   
4434 C CB  . ARG D 56  ? 2.01621 2.14344 1.87352 0.09495  0.24150  0.03207  56  ARG D CB  
4435 C CG  . ARG D 56  ? 2.05674 2.11417 1.89332 0.08545  0.20433  0.00954  56  ARG D CG  
4436 C CD  . ARG D 56  ? 1.92502 1.96375 1.82301 0.06058  0.18285  0.00669  56  ARG D CD  
4437 N NE  . ARG D 56  ? 1.85165 1.83367 1.74144 0.05214  0.14827  -0.01633 56  ARG D NE  
4438 C CZ  . ARG D 56  ? 1.66073 1.61936 1.59753 0.03738  0.12991  -0.03170 56  ARG D CZ  
4439 N NH1 . ARG D 56  ? 1.43995 1.42055 1.42626 0.02897  0.14161  -0.02587 56  ARG D NH1 
4440 N NH2 . ARG D 56  ? 1.70547 1.62183 1.63927 0.03139  0.09905  -0.05345 56  ARG D NH2 
4441 N N   . ARG D 57  ? 1.64516 1.77908 1.54443 0.16066  0.27129  -0.00783 57  ARG D N   
4442 C CA  . ARG D 57  ? 1.36338 1.46481 1.28436 0.18452  0.26943  -0.03021 57  ARG D CA  
4443 C C   . ARG D 57  ? 1.23306 1.33056 1.21159 0.15836  0.25488  -0.01689 57  ARG D C   
4444 O O   . ARG D 57  ? 1.11321 1.26909 1.13162 0.14571  0.26427  0.01179  57  ARG D O   
4445 C CB  . ARG D 57  ? 1.24128 1.38959 1.16518 0.22476  0.30068  -0.02966 57  ARG D CB  
4446 C CG  . ARG D 57  ? 1.36082 1.45597 1.26283 0.26621  0.30169  -0.06658 57  ARG D CG  
4447 C CD  . ARG D 57  ? 1.37869 1.52817 1.29734 0.30869  0.33223  -0.06391 57  ARG D CD  
4448 N NE  . ARG D 57  ? 1.47558 1.65719 1.45903 0.30923  0.33316  -0.04038 57  ARG D NE  
4449 C CZ  . ARG D 57  ? 1.44810 1.62113 1.45317 0.34877  0.33935  -0.04942 57  ARG D CZ  
4450 N NH1 . ARG D 57  ? 1.31474 1.44410 1.28548 0.39129  0.34621  -0.08466 57  ARG D NH1 
4451 N NH2 . ARG D 57  ? 1.35081 1.55644 1.41137 0.34690  0.33606  -0.02344 57  ARG D NH2 
4452 N N   . PRO D 58  ? 1.13217 1.16711 1.11698 0.14832  0.23277  -0.03715 58  PRO D N   
4453 C CA  . PRO D 58  ? 1.10396 1.13776 1.13574 0.12027  0.22087  -0.02503 58  PRO D CA  
4454 C C   . PRO D 58  ? 1.09060 1.15029 1.15511 0.13577  0.23357  -0.00982 58  PRO D C   
4455 O O   . PRO D 58  ? 1.26230 1.31948 1.31787 0.17195  0.24699  -0.01632 58  PRO D O   
4456 C CB  . PRO D 58  ? 0.99562 0.95875 1.02284 0.11014  0.19935  -0.05366 58  PRO D CB  
4457 C CG  . PRO D 58  ? 1.14533 1.07441 1.12329 0.12728  0.19329  -0.08006 58  PRO D CG  
4458 C CD  . PRO D 58  ? 1.19791 1.16415 1.14640 0.15933  0.21751  -0.07337 58  PRO D CD  
4459 N N   . VAL D 59  ? 1.12448 1.20877 1.22616 0.10967  0.22720  0.00961  59  VAL D N   
4460 C CA  . VAL D 59  ? 1.09790 1.20536 1.22810 0.12200  0.23324  0.02657  59  VAL D CA  
4461 C C   . VAL D 59  ? 1.13872 1.17944 1.25935 0.14136  0.22972  0.01065  59  VAL D C   
4462 O O   . VAL D 59  ? 1.03831 1.02074 1.14899 0.12512  0.21759  -0.00868 59  VAL D O   
4463 C CB  . VAL D 59  ? 0.82893 0.96616 0.99099 0.08730  0.22288  0.04502  59  VAL D CB  
4464 C CG1 . VAL D 59  ? 0.93309 1.11064 1.12105 0.10130  0.22707  0.06746  59  VAL D CG1 
4465 C CG2 . VAL D 59  ? 1.04739 1.22882 1.21732 0.06098  0.22087  0.05520  59  VAL D CG2 
4466 N N   . ASP D 60  ? 1.08654 1.13583 1.21462 0.17598  0.23943  0.01934  60  ASP D N   
4467 C CA  . ASP D 60  ? 1.08918 1.06911 1.20855 0.19765  0.23597  0.00803  60  ASP D CA  
4468 C C   . ASP D 60  ? 1.04936 1.05014 1.19384 0.21389  0.23654  0.03584  60  ASP D C   
4469 O O   . ASP D 60  ? 1.15949 1.23048 1.32431 0.23319  0.24519  0.05325  60  ASP D O   
4470 C CB  . ASP D 60  ? 1.43106 1.37787 1.52163 0.23714  0.24454  -0.01944 60  ASP D CB  
4471 C CG  . ASP D 60  ? 1.45387 1.30782 1.53183 0.24939  0.23548  -0.03937 60  ASP D CG  
4472 O OD1 . ASP D 60  ? 1.41781 1.22033 1.48923 0.21846  0.22217  -0.05402 60  ASP D OD1 
4473 O OD2 . ASP D 60  ? 1.42234 1.25442 1.50015 0.29017  0.24115  -0.04158 60  ASP D OD2 
4474 N N   . PRO D 61  ? 1.07496 1.01986 1.21964 0.20502  0.22675  0.04267  61  PRO D N   
4475 C CA  . PRO D 61  ? 1.04093 0.91221 1.17212 0.17661  0.21802  0.02551  61  PRO D CA  
4476 C C   . PRO D 61  ? 1.03584 0.93538 1.17596 0.12954  0.21231  0.02637  61  PRO D C   
4477 O O   . PRO D 61  ? 0.95850 0.91929 1.11445 0.11587  0.21207  0.04709  61  PRO D O   
4478 C CB  . PRO D 61  ? 1.04241 0.86382 1.17551 0.18404  0.21370  0.04493  61  PRO D CB  
4479 C CG  . PRO D 61  ? 0.93175 0.82087 1.08235 0.19550  0.21394  0.07887  61  PRO D CG  
4480 C CD  . PRO D 61  ? 1.06412 1.01941 1.22455 0.22343  0.22351  0.07224  61  PRO D CD  
4481 N N   . PRO D 62  ? 1.05344 0.91040 1.18661 0.10584  0.20590  0.00138  62  PRO D N   
4482 C CA  . PRO D 62  ? 0.89588 0.77812 1.04171 0.06595  0.19964  -0.00256 62  PRO D CA  
4483 C C   . PRO D 62  ? 0.86580 0.76204 1.02564 0.04208  0.20011  0.01920  62  PRO D C   
4484 O O   . PRO D 62  ? 1.00108 0.85571 1.15699 0.04256  0.20227  0.02903  62  PRO D O   
4485 C CB  . PRO D 62  ? 0.86143 0.68781 1.00236 0.05204  0.19101  -0.03479 62  PRO D CB  
4486 C CG  . PRO D 62  ? 0.97858 0.74041 1.10818 0.07301  0.19274  -0.04093 62  PRO D CG  
4487 C CD  . PRO D 62  ? 1.02013 0.80270 1.13772 0.11492  0.20163  -0.02693 62  PRO D CD  
4488 N N   . PRO D 63  ? 0.84503 0.79629 1.01769 0.02037  0.19772  0.02741  63  PRO D N   
4489 C CA  . PRO D 63  ? 0.75029 0.71826 0.92904 -0.00266 0.19802  0.04404  63  PRO D CA  
4490 C C   . PRO D 63  ? 0.83274 0.75709 1.01375 -0.02967 0.20001  0.02986  63  PRO D C   
4491 O O   . PRO D 63  ? 0.79836 0.70451 0.98938 -0.04291 0.19623  0.00267  63  PRO D O   
4492 C CB  . PRO D 63  ? 0.76250 0.79150 0.95510 -0.02126 0.19254  0.04416  63  PRO D CB  
4493 C CG  . PRO D 63  ? 0.69726 0.75073 0.89105 -0.00138 0.19224  0.04328  63  PRO D CG  
4494 C CD  . PRO D 63  ? 0.83542 0.83594 1.01417 0.01762  0.19474  0.02444  63  PRO D CD  
4495 N N   . VAL D 64  ? 0.88301 0.79240 1.05503 -0.03724 0.20577  0.05039  64  VAL D N   
4496 C CA  . VAL D 64  ? 0.80244 0.67797 0.97701 -0.06653 0.21299  0.04432  64  VAL D CA  
4497 C C   . VAL D 64  ? 0.86313 0.77938 1.03024 -0.08892 0.21820  0.06139  64  VAL D C   
4498 O O   . VAL D 64  ? 0.90639 0.84018 1.05434 -0.07623 0.21633  0.09108  64  VAL D O   
4499 C CB  . VAL D 64  ? 0.94280 0.74835 1.10504 -0.05669 0.21736  0.05639  64  VAL D CB  
4500 C CG1 . VAL D 64  ? 0.87317 0.65030 1.04172 -0.09375 0.22804  0.05421  64  VAL D CG1 
4501 C CG2 . VAL D 64  ? 1.00202 0.76529 1.16678 -0.03227 0.21082  0.03432  64  VAL D CG2 
4502 N N   . ILE D 65  ? 0.81779 0.75160 0.99975 -0.12003 0.22352  0.04073  65  ILE D N   
4503 C CA  . ILE D 65  ? 0.85571 0.82946 1.02708 -0.14255 0.23046  0.04895  65  ILE D CA  
4504 C C   . ILE D 65  ? 0.85358 0.80512 1.02839 -0.17236 0.24808  0.04336  65  ILE D C   
4505 O O   . ILE D 65  ? 0.85894 0.79417 1.06430 -0.18484 0.25087  0.01535  65  ILE D O   
4506 C CB  . ILE D 65  ? 0.77523 0.80255 0.96370 -0.15134 0.22215  0.02583  65  ILE D CB  
4507 C CG1 . ILE D 65  ? 0.69467 0.75332 0.87882 -0.12910 0.20753  0.03942  65  ILE D CG1 
4508 C CG2 . ILE D 65  ? 0.76598 0.82800 0.94418 -0.17702 0.23149  0.02268  65  ILE D CG2 
4509 C CD1 . ILE D 65  ? 0.70458 0.74999 0.90440 -0.10886 0.19918  0.02890  65  ILE D CD1 
4510 N N   . GLU D 66  ? 0.84202 0.79470 0.98538 -0.18383 0.25945  0.07192  66  GLU D N   
4511 C CA  . GLU D 66  ? 0.93942 0.87589 1.07909 -0.21547 0.28132  0.07574  66  GLU D CA  
4512 C C   . GLU D 66  ? 0.98713 0.98379 1.12297 -0.23967 0.29305  0.06036  66  GLU D C   
4513 O O   . GLU D 66  ? 0.92989 0.96506 1.03753 -0.23304 0.28567  0.07053  66  GLU D O   
4514 C CB  . GLU D 66  ? 0.99849 0.89013 1.09739 -0.21273 0.28743  0.12207  66  GLU D CB  
4515 C CG  . GLU D 66  ? 1.11635 0.97364 1.21570 -0.24685 0.31099  0.13067  66  GLU D CG  
4516 C CD  . GLU D 66  ? 1.31331 1.11315 1.36968 -0.24344 0.31416  0.18136  66  GLU D CD  
4517 O OE1 . GLU D 66  ? 1.51949 1.25544 1.58111 -0.22204 0.30260  0.19153  66  GLU D OE1 
4518 O OE2 . GLU D 66  ? 1.42590 1.24165 1.44046 -0.26136 0.32764  0.21069  66  GLU D OE2 
4519 N N   . LEU D 67  ? 0.97487 0.98263 1.14255 -0.26634 0.30993  0.03214  67  LEU D N   
4520 C CA  . LEU D 67  ? 0.90254 0.96728 1.07197 -0.28838 0.32541  0.01021  67  LEU D CA  
4521 C C   . LEU D 67  ? 0.92786 0.98986 1.08294 -0.32073 0.35751  0.02559  67  LEU D C   
4522 O O   . LEU D 67  ? 0.98811 1.01660 1.17272 -0.33620 0.36882  0.02492  67  LEU D O   
4523 C CB  . LEU D 67  ? 0.95953 1.05126 1.18631 -0.29018 0.31948  -0.03999 67  LEU D CB  
4524 C CG  . LEU D 67  ? 0.88755 1.03336 1.13078 -0.31352 0.34080  -0.07089 67  LEU D CG  
4525 C CD1 . LEU D 67  ? 0.77893 0.96674 0.97961 -0.31097 0.33926  -0.07005 67  LEU D CD1 
4526 C CD2 . LEU D 67  ? 0.84870 1.01204 1.15820 -0.31209 0.33276  -0.11906 67  LEU D CD2 
4527 N N   . ASN D 68  ? 0.94273 1.04210 1.05216 -0.33321 0.37226  0.03824  68  ASN D N   
4528 C CA  . ASN D 68  ? 1.06861 1.17599 1.15657 -0.36697 0.40750  0.05405  68  ASN D CA  
4529 C C   . ASN D 68  ? 1.10610 1.28576 1.18739 -0.38163 0.42585  0.02188  68  ASN D C   
4530 O O   . ASN D 68  ? 1.12573 1.33696 1.17672 -0.36646 0.41005  0.01356  68  ASN D O   
4531 C CB  . ASN D 68  ? 1.07417 1.14789 1.08889 -0.36709 0.41007  0.11339  68  ASN D CB  
4532 C CG  . ASN D 68  ? 1.28092 1.27562 1.29967 -0.35874 0.40098  0.14763  68  ASN D CG  
4533 O OD1 . ASN D 68  ? 1.19600 1.16173 1.26681 -0.34921 0.38918  0.12587  68  ASN D OD1 
4534 N ND2 . ASN D 68  ? 1.43362 1.38968 1.39367 -0.36045 0.40426  0.20127  68  ASN D ND2 
4535 N N   . ILE D 69  ? 1.15826 1.36604 1.27171 -0.41102 0.45891  0.00093  69  ILE D N   
4536 C CA  . ILE D 69  ? 1.13780 1.41738 1.25070 -0.42449 0.48236  -0.03552 69  ILE D CA  
4537 C C   . ILE D 69  ? 1.24120 1.53171 1.30200 -0.45022 0.51547  -0.00259 69  ILE D C   
4538 O O   . ILE D 69  ? 1.31972 1.57995 1.39809 -0.46641 0.52781  0.02154  69  ILE D O   
4539 C CB  . ILE D 69  ? 1.25540 1.56508 1.45438 -0.42227 0.48177  -0.09128 69  ILE D CB  
4540 C CG1 . ILE D 69  ? 1.08925 1.36582 1.34070 -0.40030 0.44832  -0.10867 69  ILE D CG1 
4541 C CG2 . ILE D 69  ? 1.23041 1.60649 1.42991 -0.41814 0.49020  -0.13708 69  ILE D CG2 
4542 C CD1 . ILE D 69  ? 1.10626 1.40205 1.43916 -0.39529 0.44070  -0.15668 69  ILE D CD1 
4543 N N   . PHE D 70  ? 1.29935 1.63139 1.29490 -0.45226 0.52567  -0.00137 70  PHE D N   
4544 C CA  . PHE D 70  ? 1.41239 1.75461 1.34415 -0.47135 0.55273  0.03426  70  PHE D CA  
4545 C C   . PHE D 70  ? 1.43879 1.85260 1.37316 -0.47557 0.57462  -0.01056 70  PHE D C   
4546 O O   . PHE D 70  ? 1.41471 1.86862 1.34078 -0.46221 0.56501  -0.05236 70  PHE D O   
4547 C CB  . PHE D 70  ? 1.40828 1.73015 1.24125 -0.46880 0.54364  0.08430  70  PHE D CB  
4548 C CG  . PHE D 70  ? 1.56893 1.81541 1.39606 -0.45901 0.52048  0.13193  70  PHE D CG  
4549 C CD1 . PHE D 70  ? 1.58171 1.77089 1.40685 -0.47750 0.53554  0.17805  70  PHE D CD1 
4550 C CD2 . PHE D 70  ? 1.46884 1.69760 1.30142 -0.42185 0.47512  0.12844  70  PHE D CD2 
4551 C CE1 . PHE D 70  ? 1.69837 1.81076 1.52152 -0.45946 0.50851  0.21723  70  PHE D CE1 
4552 C CE2 . PHE D 70  ? 1.46184 1.62324 1.29544 -0.40177 0.44921  0.16795  70  PHE D CE2 
4553 C CZ  . PHE D 70  ? 1.73058 1.83175 1.55852 -0.41841 0.46513  0.21063  70  PHE D CZ  
4554 N N   . GLU D 71  ? 1.43061 1.86068 1.37835 -0.49468 0.60437  -0.00311 71  GLU D N   
4555 C CA  . GLU D 71  ? 1.48111 1.97932 1.42062 -0.49973 0.63111  -0.03877 71  GLU D CA  
4556 C C   . GLU D 71  ? 1.54455 2.05043 1.37937 -0.51117 0.65073  0.00455  71  GLU D C   
4557 O O   . GLU D 71  ? 1.65136 2.11133 1.44518 -0.52440 0.65601  0.06730  71  GLU D O   
4558 C CB  . GLU D 71  ? 1.46102 1.98374 1.47789 -0.51440 0.65451  -0.05714 71  GLU D CB  
4559 C CG  . GLU D 71  ? 1.38286 1.97739 1.39116 -0.52164 0.68881  -0.08757 71  GLU D CG  
4560 C CD  . GLU D 71  ? 1.61204 2.22858 1.68320 -0.54343 0.71701  -0.08458 71  GLU D CD  
4561 O OE1 . GLU D 71  ? 1.47396 2.09252 1.63700 -0.53919 0.70465  -0.11689 71  GLU D OE1 
4562 O OE2 . GLU D 71  ? 1.71469 2.34826 1.74313 -0.56521 0.75088  -0.04932 71  GLU D OE2 
4563 N N   . SER D 72  ? 1.48484 2.04488 1.27400 -0.50476 0.65921  -0.02937 72  SER D N   
4564 C CA  . SER D 72  ? 1.75494 2.32965 1.44207 -0.51467 0.67918  0.00551  72  SER D CA  
4565 C C   . SER D 72  ? 1.96777 2.61549 1.64520 -0.51184 0.70162  -0.05070 72  SER D C   
4566 O O   . SER D 72  ? 1.83575 2.51598 1.57015 -0.49715 0.69187  -0.11592 72  SER D O   
4567 C CB  . SER D 72  ? 1.75140 2.29560 1.34812 -0.50429 0.64950  0.04103  72  SER D CB  
4568 O OG  . SER D 72  ? 1.79828 2.37197 1.39472 -0.48590 0.62357  -0.01107 72  SER D OG  
4569 N N   . ASP D 73  ? 2.48262 3.15290 2.08692 -0.52476 0.73168  -0.02470 73  ASP D N   
4570 C CA  . ASP D 73  ? 2.67016 3.40532 2.23513 -0.51884 0.74943  -0.07317 73  ASP D CA  
4571 C C   . ASP D 73  ? 2.74751 3.48081 2.21833 -0.50443 0.71942  -0.07673 73  ASP D C   
4572 O O   . ASP D 73  ? 2.76850 3.46243 2.16061 -0.50778 0.70543  -0.01672 73  ASP D O   
4573 C CB  . ASP D 73  ? 2.75143 3.51658 2.27855 -0.53900 0.79741  -0.04589 73  ASP D CB  
4574 C CG  . ASP D 73  ? 2.94511 3.67986 2.35189 -0.54792 0.80095  0.02349  73  ASP D CG  
4575 O OD1 . ASP D 73  ? 2.95154 3.71078 2.26741 -0.53867 0.79646  0.01114  73  ASP D OD1 
4576 O OD2 . ASP D 73  ? 3.11267 3.79616 2.51539 -0.56337 0.80593  0.09006  73  ASP D OD2 
4577 N N   . PRO D 74  ? 2.40105 2.62022 2.64681 -0.15449 0.67752  0.23675  74  PRO D N   
4578 C CA  . PRO D 74  ? 2.30520 2.53343 2.52220 -0.15661 0.66237  0.25409  74  PRO D CA  
4579 C C   . PRO D 74  ? 2.49151 2.70434 2.66586 -0.16780 0.67280  0.27939  74  PRO D C   
4580 O O   . PRO D 74  ? 2.30667 2.51813 2.45956 -0.17081 0.66169  0.29917  74  PRO D O   
4581 C CB  . PRO D 74  ? 2.07957 2.33311 2.28721 -0.15657 0.64837  0.23827  74  PRO D CB  
4582 C CG  . PRO D 74  ? 1.98868 2.24715 2.22683 -0.15231 0.65265  0.21320  74  PRO D CG  
4583 C CD  . PRO D 74  ? 2.20667 2.44184 2.46064 -0.15387 0.67393  0.21324  74  PRO D CD  
4584 N N   . HIS D 75  ? 2.91734 3.11610 3.07757 -0.17473 0.69363  0.28023  75  HIS D N   
4585 C CA  . HIS D 75  ? 2.94033 3.12088 3.05707 -0.18636 0.70447  0.30600  75  HIS D CA  
4586 C C   . HIS D 75  ? 2.92242 3.08225 3.04925 -0.18495 0.70782  0.32790  75  HIS D C   
4587 O O   . HIS D 75  ? 2.91095 3.05801 3.00869 -0.18981 0.70385  0.35485  75  HIS D O   
4588 C CB  . HIS D 75  ? 3.00530 3.17362 3.10823 -0.19266 0.72803  0.30011  75  HIS D CB  
4589 C CG  . HIS D 75  ? 3.02459 3.20878 3.14018 -0.18958 0.72881  0.27294  75  HIS D CG  
4590 N ND1 . HIS D 75  ? 3.03004 3.21422 3.19023 -0.18212 0.73489  0.24986  75  HIS D ND1 
4591 C CD2 . HIS D 75  ? 3.01409 3.21280 3.10390 -0.19350 0.72420  0.26600  75  HIS D CD2 
4592 C CE1 . HIS D 75  ? 3.03633 3.23375 3.19857 -0.18171 0.73339  0.23080  75  HIS D CE1 
4593 N NE2 . HIS D 75  ? 2.92605 3.13269 3.04744 -0.18765 0.72769  0.23967  75  HIS D NE2 
4594 N N   . ASP D 76  ? 2.71313 2.86306 2.88306 -0.17664 0.71860  0.31855  76  ASP D N   
4595 C CA  . ASP D 76  ? 2.59274 2.72216 2.78003 -0.17347 0.72463  0.33717  76  ASP D CA  
4596 C C   . ASP D 76  ? 2.47953 2.61612 2.71629 -0.15974 0.71429  0.32393  76  ASP D C   
4597 O O   . ASP D 76  ? 2.38068 2.51759 2.65147 -0.15403 0.72134  0.30164  76  ASP D O   
4598 C CB  . ASP D 76  ? 2.54211 2.64842 2.73426 -0.17700 0.75079  0.33963  76  ASP D CB  
4599 C CG  . ASP D 76  ? 2.39875 2.48221 2.60266 -0.17534 0.75825  0.36334  76  ASP D CG  
4600 O OD1 . ASP D 76  ? 2.37006 2.45003 2.57715 -0.17007 0.74699  0.38184  76  ASP D OD1 
4601 O OD2 . ASP D 76  ? 2.08656 2.15033 2.30126 -0.17663 0.77972  0.36509  76  ASP D OD2 
4602 N N   . ASP D 77  ? 2.47703 2.61680 2.71669 -0.15518 0.69790  0.33832  77  ASP D N   
4603 C CA  . ASP D 77  ? 2.46485 2.60819 2.74917 -0.14182 0.68887  0.32959  77  ASP D CA  
4604 C C   . ASP D 77  ? 2.47625 2.59616 2.78774 -0.13662 0.70054  0.34544  77  ASP D C   
4605 O O   . ASP D 77  ? 2.37272 2.49159 2.72293 -0.12548 0.69639  0.33855  77  ASP D O   
4606 C CB  . ASP D 77  ? 2.53989 2.69915 2.81843 -0.13764 0.66534  0.33519  77  ASP D CB  
4607 C CG  . ASP D 77  ? 2.43596 2.62095 2.71239 -0.13619 0.65215  0.30997  77  ASP D CG  
4608 O OD1 . ASP D 77  ? 2.41233 2.60334 2.67930 -0.14158 0.66030  0.29345  77  ASP D OD1 
4609 O OD2 . ASP D 77  ? 2.38239 2.58069 2.66856 -0.12913 0.63397  0.30734  77  ASP D OD2 
4610 N N   . SER D 78  ? 2.54176 2.64050 2.83458 -0.14378 0.71679  0.36717  78  SER D N   
4611 C CA  . SER D 78  ? 2.53490 2.60829 2.85806 -0.13731 0.73238  0.38303  78  SER D CA  
4612 C C   . SER D 78  ? 2.45646 2.52562 2.81540 -0.13417 0.74537  0.35800  78  SER D C   
4613 O O   . SER D 78  ? 2.44612 2.49866 2.83872 -0.12729 0.75473  0.36376  78  SER D O   
4614 C CB  . SER D 78  ? 2.54109 2.58791 2.83511 -0.14412 0.75049  0.41542  78  SER D CB  
4615 O OG  . SER D 78  ? 2.61602 2.65505 2.88851 -0.14252 0.74187  0.44788  78  SER D OG  
4616 N N   . ASN D 79  ? 2.36476 2.44386 2.72080 -0.13751 0.74930  0.33212  79  ASN D N   
4617 C CA  . ASN D 79  ? 2.25217 2.32321 2.64348 -0.13419 0.76255  0.30825  79  ASN D CA  
4618 C C   . ASN D 79  ? 2.14881 2.23892 2.55839 -0.12874 0.74643  0.28164  79  ASN D C   
4619 O O   . ASN D 79  ? 2.08457 2.19429 2.47465 -0.13218 0.73551  0.26990  79  ASN D O   
4620 C CB  . ASN D 79  ? 2.24928 2.31234 2.62663 -0.14311 0.78147  0.30043  79  ASN D CB  
4621 C CG  . ASN D 79  ? 2.27814 2.31927 2.63752 -0.14899 0.79954  0.32634  79  ASN D CG  
4622 O OD1 . ASN D 79  ? 2.26620 2.29683 2.62741 -0.14640 0.79827  0.35043  79  ASN D OD1 
4623 N ND2 . ASN D 79  ? 2.15679 2.18970 2.49938 -0.15700 0.81670  0.32232  79  ASN D ND2 
4624 N N   . LYS D 80  ? 2.00728 2.09047 2.45330 -0.12074 0.74543  0.27261  80  LYS D N   
4625 C CA  . LYS D 80  ? 1.78538 1.88298 2.24832 -0.11636 0.73068  0.24870  80  LYS D CA  
4626 C C   . LYS D 80  ? 1.63134 1.71510 2.12523 -0.11726 0.74360  0.22691  80  LYS D C   
4627 O O   . LYS D 80  ? 1.69476 1.75580 2.20702 -0.11687 0.76168  0.23283  80  LYS D O   
4628 C CB  . LYS D 80  ? 1.77705 1.87899 2.25197 -0.10667 0.71501  0.25745  80  LYS D CB  
4629 C CG  . LYS D 80  ? 1.83017 1.94816 2.27643 -0.10632 0.69878  0.27585  80  LYS D CG  
4630 C CD  . LYS D 80  ? 1.81880 1.93870 2.28283 -0.09574 0.68477  0.28451  80  LYS D CD  
4631 C CE  . LYS D 80  ? 1.87897 2.01417 2.31595 -0.09612 0.66796  0.30248  80  LYS D CE  
4632 N NZ  . LYS D 80  ? 1.90802 2.04377 2.36660 -0.08476 0.65497  0.31207  80  LYS D NZ  
4633 N N   . THR D 81  ? 1.55318 1.65048 2.05304 -0.11915 0.73401  0.20200  81  THR D N   
4634 C CA  . THR D 81  ? 1.46716 1.55358 1.99341 -0.12266 0.74399  0.17940  81  THR D CA  
4635 C C   . THR D 81  ? 1.31360 1.41173 1.85269 -0.11990 0.72705  0.16085  81  THR D C   
4636 O O   . THR D 81  ? 1.28456 1.40555 1.80992 -0.12051 0.70979  0.15251  81  THR D O   
4637 C CB  . THR D 81  ? 1.39890 1.48764 1.91875 -0.13168 0.75363  0.16668  81  THR D CB  
4638 O OG1 . THR D 81  ? 1.38708 1.45950 1.89759 -0.13464 0.77322  0.18320  81  THR D OG1 
4639 C CG2 . THR D 81  ? 1.18868 1.26934 1.73691 -0.13643 0.76053  0.14186  81  THR D CG2 
4640 N N   . ASP D 82  ? 1.30529 1.38700 1.87010 -0.11727 0.73282  0.15442  82  ASP D N   
4641 C CA  . ASP D 82  ? 1.17927 1.26846 1.75546 -0.11631 0.71956  0.13583  82  ASP D CA  
4642 C C   . ASP D 82  ? 1.24885 1.34664 1.82945 -0.12599 0.71900  0.11090  82  ASP D C   
4643 O O   . ASP D 82  ? 1.27687 1.35930 1.87298 -0.13259 0.73593  0.10138  82  ASP D O   
4644 C CB  . ASP D 82  ? 1.12351 1.18918 1.72529 -0.11222 0.72952  0.13536  82  ASP D CB  
4645 C CG  . ASP D 82  ? 1.20784 1.28003 1.81590 -0.10912 0.71481  0.12290  82  ASP D CG  
4646 O OD1 . ASP D 82  ? 1.27084 1.35655 1.87685 -0.11561 0.70575  0.10196  82  ASP D OD1 
4647 O OD2 . ASP D 82  ? 1.04510 1.10853 1.66097 -0.10025 0.71277  0.13465  82  ASP D OD2 
4648 N N   . ILE D 83  ? 1.21584 1.33816 1.78505 -0.12684 0.69967  0.10070  83  ILE D N   
4649 C CA  . ILE D 83  ? 1.20417 1.33824 1.77825 -0.13567 0.69668  0.07903  83  ILE D CA  
4650 C C   . ILE D 83  ? 1.21649 1.35881 1.80055 -0.13714 0.68364  0.06111  83  ILE D C   
4651 O O   . ILE D 83  ? 1.26997 1.43039 1.85374 -0.14264 0.67344  0.04597  83  ILE D O   
4652 C CB  . ILE D 83  ? 1.18078 1.33748 1.73453 -0.13691 0.68664  0.08094  83  ILE D CB  
4653 C CG1 . ILE D 83  ? 1.13037 1.30279 1.66319 -0.12845 0.66934  0.09559  83  ILE D CG1 
4654 C CG2 . ILE D 83  ? 1.08298 1.22902 1.63113 -0.14078 0.70481  0.08938  83  ILE D CG2 
4655 C CD1 . ILE D 83  ? 1.18725 1.38023 1.69907 -0.12969 0.66088  0.09797  83  ILE D CD1 
4656 N N   . THR D 84  ? 0.99273 1.12173 1.58583 -0.13240 0.68441  0.06315  84  THR D N   
4657 C CA  . THR D 84  ? 1.17711 1.31502 1.77355 -0.13269 0.67057  0.04921  84  THR D CA  
4658 C C   . THR D 84  ? 1.21980 1.36079 1.82919 -0.14446 0.67297  0.02496  84  THR D C   
4659 O O   . THR D 84  ? 1.32691 1.48840 1.93202 -0.14747 0.65718  0.01277  84  THR D O   
4660 C CB  . THR D 84  ? 1.10826 1.22588 1.71481 -0.12614 0.67571  0.05514  84  THR D CB  
4661 O OG1 . THR D 84  ? 1.08391 1.19576 1.68371 -0.11599 0.67718  0.07964  84  THR D OG1 
4662 C CG2 . THR D 84  ? 0.99726 1.12645 1.60052 -0.12420 0.65911  0.04558  84  THR D CG2 
4663 N N   . PHE D 85  ? 1.26136 1.38282 1.88760 -0.15147 0.69260  0.01811  85  PHE D N   
4664 C CA  . PHE D 85  ? 1.21634 1.33995 1.85763 -0.16375 0.69603  -0.00519 85  PHE D CA  
4665 C C   . PHE D 85  ? 1.17723 1.32157 1.81631 -0.16983 0.69025  -0.01184 85  PHE D C   
4666 O O   . PHE D 85  ? 1.15297 1.31111 1.80034 -0.17847 0.68329  -0.02992 85  PHE D O   
4667 C CB  . PHE D 85  ? 1.30002 1.39483 1.96223 -0.16924 0.71995  -0.01054 85  PHE D CB  
4668 C CG  . PHE D 85  ? 1.38517 1.46146 2.05779 -0.16939 0.72588  -0.01774 85  PHE D CG  
4669 C CD1 . PHE D 85  ? 1.37914 1.44219 2.04777 -0.15815 0.72690  -0.00146 85  PHE D CD1 
4670 C CD2 . PHE D 85  ? 1.53996 1.61144 2.22748 -0.18122 0.73148  -0.04096 85  PHE D CD2 
4671 C CE1 . PHE D 85  ? 1.44376 1.48723 2.12366 -0.15806 0.73437  -0.00849 85  PHE D CE1 
4672 C CE2 . PHE D 85  ? 1.55821 1.61070 2.25404 -0.18224 0.73892  -0.04890 85  PHE D CE2 
4673 C CZ  . PHE D 85  ? 1.48084 1.51826 2.17319 -0.17034 0.74097  -0.03275 85  PHE D CZ  
4674 N N   . VAL D 86  ? 1.06120 1.20818 1.68976 -0.16585 0.69333  0.00240  86  VAL D N   
4675 C CA  . VAL D 86  ? 1.06559 1.22796 1.69506 -0.17171 0.69164  -0.00422 86  VAL D CA  
4676 C C   . VAL D 86  ? 1.26744 1.45847 1.88014 -0.16769 0.66933  -0.00253 86  VAL D C   
4677 O O   . VAL D 86  ? 1.25659 1.46496 1.87565 -0.17362 0.66238  -0.01455 86  VAL D O   
4678 C CB  . VAL D 86  ? 1.11151 1.25974 1.73869 -0.17111 0.70966  0.00815  86  VAL D CB  
4679 C CG1 . VAL D 86  ? 1.03190 1.17402 1.63875 -0.16061 0.70971  0.03158  86  VAL D CG1 
4680 C CG2 . VAL D 86  ? 1.10800 1.27169 1.73336 -0.17548 0.70783  0.00353  86  VAL D CG2 
4681 N N   . TYR D 87  ? 1.09684 1.29322 1.69049 -0.15770 0.65825  0.01224  87  TYR D N   
4682 C CA  . TYR D 87  ? 1.12806 1.35072 1.70601 -0.15319 0.63731  0.01435  87  TYR D CA  
4683 C C   . TYR D 87  ? 1.32041 1.56028 1.90747 -0.15817 0.62321  -0.00333 87  TYR D C   
4684 O O   . TYR D 87  ? 1.28420 1.51998 1.87542 -0.15809 0.61921  -0.00908 87  TYR D O   
4685 C CB  . TYR D 87  ? 1.30575 1.52877 1.86643 -0.14227 0.62830  0.03123  87  TYR D CB  
4686 C CG  . TYR D 87  ? 1.23832 1.48631 1.78089 -0.13686 0.60924  0.03661  87  TYR D CG  
4687 C CD1 . TYR D 87  ? 1.19168 1.45823 1.73334 -0.13527 0.59052  0.02817  87  TYR D CD1 
4688 C CD2 . TYR D 87  ? 1.21099 1.46367 1.73682 -0.13387 0.61076  0.04988  87  TYR D CD2 
4689 C CE1 . TYR D 87  ? 1.16429 1.45298 1.69100 -0.13011 0.57371  0.03286  87  TYR D CE1 
4690 C CE2 . TYR D 87  ? 1.14397 1.41886 1.65387 -0.12954 0.59423  0.05358  87  TYR D CE2 
4691 C CZ  . TYR D 87  ? 1.18181 1.47452 1.69329 -0.12731 0.57564  0.04504  87  TYR D CZ  
4692 O OH  . TYR D 87  ? 1.21052 1.52479 1.70756 -0.12276 0.55968  0.04858  87  TYR D OH  
4693 N N   . ASN D 88  ? 1.33531 1.59424 1.92552 -0.16258 0.61625  -0.01141 88  ASN D N   
4694 C CA  . ASN D 88  ? 1.42219 1.69816 2.02494 -0.16936 0.60515  -0.02842 88  ASN D CA  
4695 C C   . ASN D 88  ? 1.32621 1.62595 1.91431 -0.16248 0.58270  -0.02487 88  ASN D C   
4696 O O   . ASN D 88  ? 1.35448 1.67177 1.93770 -0.16071 0.57411  -0.02286 88  ASN D O   
4697 C CB  . ASN D 88  ? 1.54931 1.83108 2.16970 -0.17846 0.61211  -0.03911 88  ASN D CB  
4698 C CG  . ASN D 88  ? 1.70431 2.01083 2.33593 -0.18409 0.59684  -0.05292 88  ASN D CG  
4699 O OD1 . ASN D 88  ? 1.68064 1.99446 2.31229 -0.18536 0.58632  -0.05959 88  ASN D OD1 
4700 N ND2 . ASN D 88  ? 1.66102 1.98012 2.30302 -0.18770 0.59643  -0.05694 88  ASN D ND2 
4701 N N   . ALA D 89  ? 1.10643 1.78604 2.04613 -0.06557 0.37136  -0.03240 89  ALA D N   
4702 C CA  . ALA D 89  ? 0.94863 1.61749 1.82454 -0.03505 0.32717  -0.05935 89  ALA D CA  
4703 C C   . ALA D 89  ? 0.64800 1.26467 1.48215 -0.05369 0.26994  -0.07671 89  ALA D C   
4704 O O   . ALA D 89  ? 0.87572 1.44427 1.68449 -0.07740 0.27245  -0.06717 89  ALA D O   
4705 C CB  . ALA D 89  ? 0.97744 1.61433 1.74137 0.00674  0.35399  -0.05552 89  ALA D CB  
4706 N N   . ASN D 90  ? 0.72908 1.35225 1.55296 -0.04028 0.22087  -0.10106 90  ASN D N   
4707 C CA  . ASN D 90  ? 0.80974 1.38289 1.58087 -0.05022 0.17024  -0.11714 90  ASN D CA  
4708 C C   . ASN D 90  ? 0.77622 1.29236 1.43027 -0.02769 0.17575  -0.11511 90  ASN D C   
4709 O O   . ASN D 90  ? 0.80720 1.32864 1.42001 0.00251  0.19554  -0.11327 90  ASN D O   
4710 C CB  . ASN D 90  ? 0.87745 1.47657 1.67760 -0.04248 0.11841  -0.13979 90  ASN D CB  
4711 C CG  . ASN D 90  ? 1.04359 1.68844 1.95394 -0.06996 0.09398  -0.14656 90  ASN D CG  
4712 O OD1 . ASN D 90  ? 1.17181 1.83481 2.10755 -0.06600 0.04649  -0.16423 90  ASN D OD1 
4713 N ND2 . ASN D 90  ? 1.13294 1.79531 2.11077 -0.09838 0.12480  -0.13164 90  ASN D ND2 
4714 N N   . PHE D 91  ? 0.69725 1.15879 1.29987 -0.04145 0.15759  -0.11653 91  PHE D N   
4715 C CA  . PHE D 91  ? 0.64634 1.05874 1.14940 -0.02188 0.15907  -0.11445 91  PHE D CA  
4716 C C   . PHE D 91  ? 0.64614 1.02616 1.11278 -0.02532 0.11360  -0.13075 91  PHE D C   
4717 O O   . PHE D 91  ? 0.73128 1.09907 1.22417 -0.04843 0.09010  -0.13827 91  PHE D O   
4718 C CB  . PHE D 91  ? 0.74397 1.11654 1.20935 -0.02838 0.19432  -0.09347 91  PHE D CB  
4719 C CG  . PHE D 91  ? 0.66626 1.05554 1.12390 -0.01154 0.24356  -0.07423 91  PHE D CG  
4720 C CD1 . PHE D 91  ? 0.81584 1.19965 1.20552 0.02276  0.25108  -0.07579 91  PHE D CD1 
4721 C CD2 . PHE D 91  ? 0.75669 1.16560 1.27439 -0.02978 0.28257  -0.05458 91  PHE D CD2 
4722 C CE1 . PHE D 91  ? 0.79605 1.18961 1.16502 0.04284  0.29562  -0.05992 91  PHE D CE1 
4723 C CE2 . PHE D 91  ? 0.92681 1.34882 1.42887 -0.01073 0.33330  -0.03429 91  PHE D CE2 
4724 C CZ  . PHE D 91  ? 0.85920 1.27150 1.28033 0.02780  0.33932  -0.03788 91  PHE D CZ  
4725 N N   . PHE D 92  ? 0.69676 1.06196 1.10305 -0.00202 0.10155  -0.13644 92  PHE D N   
4726 C CA  . PHE D 92  ? 0.69465 1.02770 1.05809 -0.00142 0.06777  -0.14686 92  PHE D CA  
4727 C C   . PHE D 92  ? 0.65668 0.95782 0.94854 0.01589  0.07787  -0.14030 92  PHE D C   
4728 O O   . PHE D 92  ? 0.73320 1.04365 1.00623 0.03359  0.09684  -0.13481 92  PHE D O   
4729 C CB  . PHE D 92  ? 0.64897 1.00397 1.02778 0.00824  0.03559  -0.16045 92  PHE D CB  
4730 C CG  . PHE D 92  ? 0.65800 1.05249 1.11315 -0.00374 0.02046  -0.16782 92  PHE D CG  
4731 C CD1 . PHE D 92  ? 0.73932 1.12356 1.21264 -0.02244 -0.01098 -0.17755 92  PHE D CD1 
4732 C CD2 . PHE D 92  ? 0.69714 1.13981 1.20642 0.00594  0.03633  -0.16634 92  PHE D CD2 
4733 C CE1 . PHE D 92  ? 0.67153 1.09677 1.22215 -0.03342 -0.03092 -0.18570 92  PHE D CE1 
4734 C CE2 . PHE D 92  ? 0.73679 1.22406 1.32776 -0.00355 0.02177  -0.17245 92  PHE D CE2 
4735 C CZ  . PHE D 92  ? 0.71407 1.19461 1.32908 -0.02437 -0.01418 -0.18214 92  PHE D CZ  
4736 N N   . LEU D 93  ? 0.61416 0.87819 0.86623 0.01267  0.06394  -0.14205 93  LEU D N   
4737 C CA  . LEU D 93  ? 0.57860 0.81832 0.77341 0.02907  0.06966  -0.13611 93  LEU D CA  
4738 C C   . LEU D 93  ? 0.64390 0.87467 0.81582 0.03509  0.04390  -0.14416 93  LEU D C   
4739 O O   . LEU D 93  ? 0.72159 0.93596 0.89124 0.02550  0.02660  -0.15090 93  LEU D O   
4740 C CB  . LEU D 93  ? 0.66824 0.87003 0.83506 0.02442  0.08653  -0.12558 93  LEU D CB  
4741 C CG  . LEU D 93  ? 0.75197 0.93792 0.86951 0.04514  0.09887  -0.11530 93  LEU D CG  
4742 C CD1 . LEU D 93  ? 0.55885 0.76502 0.67141 0.05941  0.11767  -0.10778 93  LEU D CD1 
4743 C CD2 . LEU D 93  ? 0.58782 0.72998 0.67768 0.04256  0.11076  -0.10576 93  LEU D CD2 
4744 N N   . PHE D 94  ? 0.64561 0.88472 0.79916 0.05104  0.04159  -0.14322 94  PHE D N   
4745 C CA  . PHE D 94  ? 0.55285 0.78710 0.69157 0.05636  0.02266  -0.14635 94  PHE D CA  
4746 C C   . PHE D 94  ? 0.63018 0.84974 0.73547 0.06652  0.02967  -0.13872 94  PHE D C   
4747 O O   . PHE D 94  ? 0.68157 0.90727 0.77889 0.07635  0.03975  -0.13465 94  PHE D O   
4748 C CB  . PHE D 94  ? 0.65714 0.91428 0.81633 0.06365  0.01116  -0.15189 94  PHE D CB  
4749 C CG  . PHE D 94  ? 0.68705 0.93576 0.83419 0.06738  -0.00529 -0.15095 94  PHE D CG  
4750 C CD1 . PHE D 94  ? 0.67209 0.90409 0.80574 0.06229  -0.01694 -0.14989 94  PHE D CD1 
4751 C CD2 . PHE D 94  ? 0.65003 0.90428 0.79770 0.07611  -0.00913 -0.15088 94  PHE D CD2 
4752 C CE1 . PHE D 94  ? 0.72136 0.94319 0.84015 0.06678  -0.02608 -0.14419 94  PHE D CE1 
4753 C CE2 . PHE D 94  ? 0.61365 0.85871 0.75707 0.07645  -0.02067 -0.14626 94  PHE D CE2 
4754 C CZ  . PHE D 94  ? 0.68694 0.91637 0.81512 0.07224  -0.02620 -0.14064 94  PHE D CZ  
4755 N N   . ALA D 95  ? 0.59601 0.79727 0.68093 0.06662  0.02420  -0.13682 95  ALA D N   
4756 C CA  . ALA D 95  ? 0.56461 0.75724 0.62684 0.07749  0.03269  -0.12857 95  ALA D CA  
4757 C C   . ALA D 95  ? 0.69843 0.90468 0.76793 0.08186  0.02402  -0.12527 95  ALA D C   
4758 O O   . ALA D 95  ? 0.67158 0.87285 0.74011 0.07763  0.01439  -0.12618 95  ALA D O   
4759 C CB  . ALA D 95  ? 0.65997 0.82043 0.69316 0.07791  0.03915  -0.12751 95  ALA D CB  
4760 N N   . THR D 96  ? 0.61909 0.84044 0.69616 0.09021  0.02636  -0.12035 96  THR D N   
4761 C CA  . THR D 96  ? 0.75871 0.99349 0.85266 0.09117  0.02033  -0.11485 96  THR D CA  
4762 C C   . THR D 96  ? 0.74609 0.98741 0.83921 0.10109  0.03126  -0.10488 96  THR D C   
4763 O O   . THR D 96  ? 0.68755 0.92639 0.76873 0.11053  0.03807  -0.10410 96  THR D O   
4764 C CB  . THR D 96  ? 0.63924 0.89161 0.75860 0.09014  0.00569  -0.12157 96  THR D CB  
4765 O OG1 . THR D 96  ? 0.71222 0.97138 0.82496 0.09883  0.00612  -0.12694 96  THR D OG1 
4766 C CG2 . THR D 96  ? 0.53888 0.78666 0.66534 0.08388  -0.00460 -0.12957 96  THR D CG2 
4767 N N   . LEU D 97  ? 0.74287 0.99283 0.85078 0.10028  0.03470  -0.09511 97  LEU D N   
4768 C CA  . LEU D 97  ? 0.68118 0.94589 0.80045 0.11071  0.04791  -0.08363 97  LEU D CA  
4769 C C   . LEU D 97  ? 0.70377 1.00247 0.87232 0.10771  0.03548  -0.08132 97  LEU D C   
4770 O O   . LEU D 97  ? 0.82616 1.13067 1.02075 0.09521  0.02660  -0.07977 97  LEU D O   
4771 C CB  . LEU D 97  ? 0.74896 1.00218 0.85339 0.11292  0.06576  -0.07190 97  LEU D CB  
4772 C CG  . LEU D 97  ? 0.87597 1.13600 0.97765 0.12991  0.08819  -0.06115 97  LEU D CG  
4773 C CD1 . LEU D 97  ? 0.70294 0.93655 0.76604 0.14226  0.09292  -0.06944 97  LEU D CD1 
4774 C CD2 . LEU D 97  ? 0.84790 1.09595 0.93003 0.13362  0.10871  -0.04865 97  LEU D CD2 
4775 N N   . GLU D 98  ? 0.73109 1.04899 0.91248 0.11945  0.03207  -0.08147 98  GLU D N   
4776 C CA  . GLU D 98  ? 0.76168 1.11303 0.99198 0.11716  0.01286  -0.08310 98  GLU D CA  
4777 C C   . GLU D 98  ? 0.60900 0.99257 0.87557 0.12831  0.02285  -0.06980 98  GLU D C   
4778 O O   . GLU D 98  ? 0.79700 1.18011 1.04413 0.14770  0.02935  -0.06787 98  GLU D O   
4779 C CB  . GLU D 98  ? 0.94129 1.29038 1.15471 0.12450  -0.00871 -0.09822 98  GLU D CB  
4780 C CG  . GLU D 98  ? 0.99733 1.31942 1.17718 0.11810  -0.01288 -0.11058 98  GLU D CG  
4781 C CD  . GLU D 98  ? 1.32021 1.64552 1.49685 0.12254  -0.03704 -0.12649 98  GLU D CD  
4782 O OE1 . GLU D 98  ? 1.30816 1.63867 1.46771 0.13873  -0.04408 -0.12853 98  GLU D OE1 
4783 O OE2 . GLU D 98  ? 1.44200 1.76061 1.62764 0.11280  -0.04955 -0.13727 98  GLU D OE2 
4784 N N   . PRO D 99  ? 0.78223 1.19421 1.10474 0.11775  0.02641  -0.05859 99  PRO D N   
4785 C CA  . PRO D 99  ? 0.79774 1.25118 1.16948 0.12914  0.03762  -0.04477 99  PRO D CA  
4786 C C   . PRO D 99  ? 0.88448 1.36580 1.28040 0.14155  0.00921  -0.05434 99  PRO D C   
4787 O O   . PRO D 99  ? 1.01449 1.49731 1.41941 0.13280  -0.02357 -0.06977 99  PRO D O   
4788 C CB  . PRO D 99  ? 0.82476 1.30404 1.26208 0.10835  0.04298  -0.03141 99  PRO D CB  
4789 C CG  . PRO D 99  ? 0.82381 1.26087 1.22151 0.09271  0.04684  -0.03291 99  PRO D CG  
4790 C CD  . PRO D 99  ? 0.72248 1.12917 1.06904 0.09544  0.02348  -0.05522 99  PRO D CD  
4791 N N   . GLU D 100 ? 0.89387 1.39378 1.29470 0.16559  0.02068  -0.04590 100 GLU D N   
4792 C CA  . GLU D 100 ? 1.05659 1.58712 1.48358 0.18161  -0.00868 -0.05211 100 GLU D CA  
4793 C C   . GLU D 100 ? 1.15288 1.73832 1.67371 0.16637  -0.03327 -0.05217 100 GLU D C   
4794 O O   . GLU D 100 ? 1.16834 1.76951 1.70672 0.16797  -0.07416 -0.06699 100 GLU D O   
4795 C CB  . GLU D 100 ? 0.99645 1.53431 1.41261 0.21367  0.00965  -0.04092 100 GLU D CB  
4796 C CG  . GLU D 100 ? 1.03679 1.52480 1.36903 0.23355  0.00947  -0.04681 100 GLU D CG  
4797 C CD  . GLU D 100 ? 1.16256 1.64697 1.47431 0.23847  -0.02893 -0.06043 100 GLU D CD  
4798 O OE1 . GLU D 100 ? 1.17616 1.64569 1.47322 0.21860  -0.04492 -0.07385 100 GLU D OE1 
4799 O OE2 . GLU D 100 ? 1.08209 1.57589 1.38727 0.26575  -0.04292 -0.05758 100 GLU D OE2 
4800 N N   . ARG D 101 ? 1.13837 1.75192 1.71977 0.15190  -0.00896 -0.03534 101 ARG D N   
4801 C CA  . ARG D 101 ? 1.32076 1.98270 2.00114 0.12910  -0.02855 -0.03298 101 ARG D CA  
4802 C C   . ARG D 101 ? 1.43481 2.06296 2.10754 0.09759  -0.03252 -0.03785 101 ARG D C   
4803 O O   . ARG D 101 ? 1.35315 1.95858 2.00496 0.08937  0.00353  -0.02231 101 ARG D O   
4804 C CB  . ARG D 101 ? 1.45340 2.16953 2.21370 0.13195  0.00588  -0.00684 101 ARG D CB  
4805 C CG  . ARG D 101 ? 1.49674 2.26622 2.30287 0.16167  -0.00016 -0.00242 101 ARG D CG  
4806 C CD  . ARG D 101 ? 1.49223 2.22381 2.20681 0.19809  0.01489  -0.00461 101 ARG D CD  
4807 N NE  . ARG D 101 ? 1.49559 2.26073 2.23971 0.22642  0.05126  0.01466  101 ARG D NE  
4808 C CZ  . ARG D 101 ? 1.43586 2.17015 2.11337 0.26061  0.06882  0.01568  101 ARG D CZ  
4809 N NH1 . ARG D 101 ? 1.40838 2.08038 1.99112 0.26817  0.05464  0.00116  101 ARG D NH1 
4810 N NH2 . ARG D 101 ? 1.34803 2.11338 2.05718 0.28836  0.10333  0.03240  101 ARG D NH2 
4811 N N   . PRO D 102 ? 1.54364 2.16283 2.22684 0.08238  -0.07610 -0.05954 102 PRO D N   
4812 C CA  . PRO D 102 ? 1.54225 2.12300 2.21537 0.05598  -0.08068 -0.06515 102 PRO D CA  
4813 C C   . PRO D 102 ? 1.62955 2.22837 2.37702 0.02959  -0.05809 -0.04180 102 PRO D C   
4814 O O   . PRO D 102 ? 1.58251 2.14731 2.32725 0.00786  -0.06098 -0.04253 102 PRO D O   
4815 C CB  . PRO D 102 ? 1.43357 2.00851 2.11431 0.05028  -0.13494 -0.09488 102 PRO D CB  
4816 C CG  . PRO D 102 ? 1.42996 2.01452 2.06873 0.08122  -0.15132 -0.10621 102 PRO D CG  
4817 C CD  . PRO D 102 ? 1.53895 2.16893 2.21792 0.09577  -0.12321 -0.08266 102 PRO D CD  
4818 N N   . ILE D 103 ? 1.55761 2.20933 2.37288 0.03301  -0.03383 -0.01937 103 ILE D N   
4819 C CA  . ILE D 103 ? 1.53287 2.20366 2.41093 0.01345  0.00366  0.01123  103 ILE D CA  
4820 C C   . ILE D 103 ? 1.47906 2.09202 2.27939 0.01113  0.03839  0.02422  103 ILE D C   
4821 O O   . ILE D 103 ? 1.27153 1.85051 2.07298 -0.01210 0.03053  0.02487  103 ILE D O   
4822 C CB  . ILE D 103 ? 1.43312 2.16542 2.36774 0.03101  0.03801  0.03462  103 ILE D CB  
4823 C CG1 . ILE D 103 ? 1.37096 2.14013 2.40200 0.00667  0.07162  0.06696  103 ILE D CG1 
4824 C CG2 . ILE D 103 ? 1.31494 2.01930 2.15493 0.06383  0.07729  0.04172  103 ILE D CG2 
4825 C CD1 . ILE D 103 ? 1.17785 2.01774 2.28075 0.02475  0.10747  0.09068  103 ILE D CD1 
4826 N N   . PRO D 115 ? 1.55060 1.67458 1.55887 0.08800  0.07385  0.01732  115 PRO D N   
4827 C CA  . PRO D 115 ? 1.55899 1.68425 1.53668 0.09690  0.06551  -0.00667 115 PRO D CA  
4828 C C   . PRO D 115 ? 1.60581 1.74767 1.58216 0.10527  0.09404  -0.00307 115 PRO D C   
4829 O O   . PRO D 115 ? 1.62381 1.74314 1.54355 0.12113  0.11333  0.00419  115 PRO D O   
4830 C CB  . PRO D 115 ? 1.54877 1.63337 1.45211 0.11012  0.05441  -0.00874 115 PRO D CB  
4831 C CG  . PRO D 115 ? 1.55673 1.62527 1.46582 0.10620  0.04042  0.00419  115 PRO D CG  
4832 C CD  . PRO D 115 ? 1.70129 1.78537 1.66137 0.09484  0.06428  0.02857  115 PRO D CD  
4833 N N   . VAL D 116 ? 1.30636 1.48467 1.33964 0.09823  0.09518  -0.00909 116 VAL D N   
4834 C CA  . VAL D 116 ? 1.02844 1.22513 1.06592 0.10968  0.11936  -0.00624 116 VAL D CA  
4835 C C   . VAL D 116 ? 1.03690 1.21438 1.02991 0.12052  0.11187  -0.02800 116 VAL D C   
4836 O O   . VAL D 116 ? 1.01871 1.18579 0.97884 0.13735  0.13306  -0.02643 116 VAL D O   
4837 C CB  . VAL D 116 ? 0.98638 1.22963 1.10261 0.10017  0.11898  -0.00322 116 VAL D CB  
4838 C CG1 . VAL D 116 ? 1.01520 1.26668 1.15421 0.09051  0.08668  -0.02571 116 VAL D CG1 
4839 C CG2 . VAL D 116 ? 1.07009 1.33696 1.19726 0.11578  0.14352  0.00223  116 VAL D CG2 
4840 N N   . LEU D 117 ? 0.99218 1.16206 0.98420 0.11169  0.08397  -0.04770 117 LEU D N   
4841 C CA  . LEU D 117 ? 0.90493 1.05081 0.85867 0.11656  0.07513  -0.06679 117 LEU D CA  
4842 C C   . LEU D 117 ? 1.02316 1.13576 0.93185 0.11551  0.05664  -0.07497 117 LEU D C   
4843 O O   . LEU D 117 ? 1.06505 1.18216 0.99060 0.10647  0.03802  -0.07483 117 LEU D O   
4844 C CB  . LEU D 117 ? 0.78205 0.94571 0.77079 0.10741  0.06010  -0.08086 117 LEU D CB  
4845 C CG  . LEU D 117 ? 0.94663 1.08488 0.90598 0.10827  0.05408  -0.09727 117 LEU D CG  
4846 C CD1 . LEU D 117 ? 0.78052 0.90510 0.71661 0.12340  0.07467  -0.09524 117 LEU D CD1 
4847 C CD2 . LEU D 117 ? 0.89053 1.04449 0.88237 0.09722  0.04072  -0.10743 117 LEU D CD2 
4848 N N   . THR D 118 ? 0.99912 1.07632 0.84976 0.12678  0.05908  -0.08358 118 THR D N   
4849 C CA  . THR D 118 ? 1.10317 1.14567 0.90299 0.12922  0.03742  -0.09305 118 THR D CA  
4850 C C   . THR D 118 ? 1.09463 1.11288 0.87497 0.12554  0.01888  -0.11805 118 THR D C   
4851 O O   . THR D 118 ? 1.08492 1.10113 0.87311 0.12605  0.03073  -0.12435 118 THR D O   
4852 C CB  . THR D 118 ? 1.21653 1.22846 0.94963 0.14894  0.05569  -0.07941 118 THR D CB  
4853 O OG1 . THR D 118 ? 1.57946 1.54912 1.24777 0.15583  0.02979  -0.09479 118 THR D OG1 
4854 C CG2 . THR D 118 ? 1.11042 1.11668 0.82356 0.16511  0.08913  -0.07533 118 THR D CG2 
4855 N N   . GLY D 119 ? 1.06532 1.06429 0.82372 0.12150  -0.01231 -0.13153 119 GLY D N   
4856 C CA  . GLY D 119 ? 1.09600 1.07403 0.84843 0.11253  -0.03574 -0.15615 119 GLY D CA  
4857 C C   . GLY D 119 ? 1.11613 1.12649 0.93345 0.09254  -0.06031 -0.16452 119 GLY D C   
4858 O O   . GLY D 119 ? 1.11809 1.15138 0.95924 0.09141  -0.07184 -0.15687 119 GLY D O   
4859 N N   . VAL D 120 ? 1.07001 1.08109 0.91771 0.07783  -0.06594 -0.17874 120 VAL D N   
4860 C CA  . VAL D 120 ? 0.87005 0.91701 0.78618 0.05959  -0.08098 -0.18448 120 VAL D CA  
4861 C C   . VAL D 120 ? 0.87534 0.94937 0.83329 0.05454  -0.05285 -0.17417 120 VAL D C   
4862 O O   . VAL D 120 ? 0.87620 0.93335 0.83056 0.05069  -0.03861 -0.17658 120 VAL D O   
4863 C CB  . VAL D 120 ? 0.89587 0.92688 0.82427 0.04396  -0.10810 -0.20594 120 VAL D CB  
4864 C CG1 . VAL D 120 ? 0.84477 0.92145 0.85541 0.02553  -0.11317 -0.20743 120 VAL D CG1 
4865 C CG2 . VAL D 120 ? 0.89761 0.90327 0.78165 0.05162  -0.14392 -0.21845 120 VAL D CG2 
4866 N N   . PRO D 121 ? 0.81388 0.92383 0.80549 0.05662  -0.04561 -0.16301 121 PRO D N   
4867 C CA  . PRO D 121 ? 0.66074 0.79269 0.68018 0.05613  -0.02269 -0.15467 121 PRO D CA  
4868 C C   . PRO D 121 ? 0.63177 0.78872 0.70006 0.04408  -0.02244 -0.15947 121 PRO D C   
4869 O O   . PRO D 121 ? 0.64048 0.81405 0.72401 0.04687  -0.00485 -0.15265 121 PRO D O   
4870 C CB  . PRO D 121 ? 0.75052 0.90240 0.77681 0.06499  -0.01943 -0.14320 121 PRO D CB  
4871 C CG  . PRO D 121 ? 0.70361 0.85732 0.73384 0.06435  -0.04301 -0.14685 121 PRO D CG  
4872 C CD  . PRO D 121 ? 0.74789 0.87104 0.74231 0.06316  -0.05872 -0.15691 121 PRO D CD  
4873 N N   . VAL D 122 ? 0.72035 0.88235 0.81413 0.03237  -0.04133 -0.17040 122 VAL D N   
4874 C CA  . VAL D 122 ? 0.71949 0.91126 0.86896 0.02064  -0.03685 -0.17280 122 VAL D CA  
4875 C C   . VAL D 122 ? 0.79748 0.96930 0.95831 0.00278  -0.03885 -0.18023 122 VAL D C   
4876 O O   . VAL D 122 ? 0.77259 0.92021 0.91740 -0.00308 -0.06328 -0.19248 122 VAL D O   
4877 C CB  . VAL D 122 ? 0.69240 0.91818 0.88352 0.02145  -0.05708 -0.17821 122 VAL D CB  
4878 C CG1 . VAL D 122 ? 0.64597 0.90648 0.90106 0.00986  -0.04825 -0.18020 122 VAL D CG1 
4879 C CG2 . VAL D 122 ? 0.67954 0.91790 0.86253 0.03760  -0.05352 -0.17104 122 VAL D CG2 
4880 N N   . ALA D 123 ? 0.68357 0.85992 0.86705 -0.00519 -0.01379 -0.17265 123 ALA D N   
4881 C CA  . ALA D 123 ? 0.72317 0.87765 0.92606 -0.02567 -0.01097 -0.17620 123 ALA D CA  
4882 C C   . ALA D 123 ? 0.62612 0.82160 0.90129 -0.04056 0.00167  -0.17129 123 ALA D C   
4883 O O   . ALA D 123 ? 0.75833 0.98126 1.04397 -0.03027 0.02672  -0.15908 123 ALA D O   
4884 C CB  . ALA D 123 ? 0.69111 0.80342 0.85123 -0.02106 0.01354  -0.16639 123 ALA D CB  
4885 N N   . GLY D 124 ? 0.73857 0.93889 1.06414 -0.06373 -0.01613 -0.18156 124 GLY D N   
4886 C CA  . GLY D 124 ? 0.75678 0.99600 1.16092 -0.08149 0.00193  -0.17401 124 GLY D CA  
4887 C C   . GLY D 124 ? 0.70216 0.90923 1.10660 -0.09637 0.03444  -0.15957 124 GLY D C   
4888 O O   . GLY D 124 ? 0.85835 1.00859 1.21026 -0.09701 0.03338  -0.16093 124 GLY D O   
4889 N N   . VAL D 125 ? 0.76290 1.00448 1.22563 -0.10623 0.06630  -0.14393 125 VAL D N   
4890 C CA  . VAL D 125 ? 0.80304 1.01253 1.26247 -0.11785 0.10404  -0.12363 125 VAL D CA  
4891 C C   . VAL D 125 ? 0.88752 1.07356 1.40166 -0.15515 0.09056  -0.13036 125 VAL D C   
4892 O O   . VAL D 125 ? 0.80517 1.02682 1.39243 -0.17520 0.06275  -0.14530 125 VAL D O   
4893 C CB  . VAL D 125 ? 0.79564 1.04697 1.28453 -0.10983 0.14999  -0.10059 125 VAL D CB  
4894 C CG1 . VAL D 125 ? 0.76568 1.07796 1.36135 -0.13108 0.15290  -0.10126 125 VAL D CG1 
4895 C CG2 . VAL D 125 ? 0.72654 0.93405 1.18256 -0.11164 0.19168  -0.07478 125 VAL D CG2 
4896 N N   . ALA D 126 ? 0.84024 0.96354 1.32019 -0.16399 0.10753  -0.12002 126 ALA D N   
4897 C CA  . ALA D 126 ? 0.81391 0.90444 1.34721 -0.20216 0.10353  -0.12164 126 ALA D CA  
4898 C C   . ALA D 126 ? 0.88987 0.95540 1.42717 -0.20968 0.15711  -0.08791 126 ALA D C   
4899 O O   . ALA D 126 ? 0.95641 0.97626 1.41301 -0.18595 0.17887  -0.07322 126 ALA D O   
4900 C CB  . ALA D 126 ? 0.92228 0.94021 1.40030 -0.20569 0.06577  -0.14569 126 ALA D CB  
4901 N N   . TYR D 127 ? 0.86945 0.96613 1.50223 -0.24144 0.17878  -0.07392 127 TYR D N   
4902 C CA  . TYR D 127 ? 1.05169 1.12902 1.69516 -0.25001 0.23607  -0.03644 127 TYR D CA  
4903 C C   . TYR D 127 ? 1.10717 1.10009 1.74818 -0.27915 0.23190  -0.03469 127 TYR D C   
4904 O O   . TYR D 127 ? 1.13762 1.12358 1.84747 -0.31596 0.19861  -0.05515 127 TYR D O   
4905 C CB  . TYR D 127 ? 0.97122 1.12511 1.72406 -0.26979 0.26783  -0.01905 127 TYR D CB  
4906 C CG  . TYR D 127 ? 0.86490 1.09347 1.61259 -0.23611 0.27629  -0.02038 127 TYR D CG  
4907 C CD1 . TYR D 127 ? 0.86695 1.09799 1.54905 -0.20152 0.32188  0.00439  127 TYR D CD1 
4908 C CD2 . TYR D 127 ? 0.81062 1.10100 1.61281 -0.23637 0.23549  -0.04781 127 TYR D CD2 
4909 C CE1 . TYR D 127 ? 0.79443 1.08495 1.46733 -0.17000 0.32713  -0.00043 127 TYR D CE1 
4910 C CE2 . TYR D 127 ? 0.74412 1.09436 1.53935 -0.20402 0.24275  -0.04969 127 TYR D CE2 
4911 C CZ  . TYR D 127 ? 0.74052 1.08902 1.47165 -0.17183 0.28870  -0.02722 127 TYR D CZ  
4912 O OH  . TYR D 127 ? 0.83575 1.23567 1.55647 -0.13928 0.29380  -0.03244 127 TYR D OH  
4913 N N   . LEU D 128 ? 1.16848 1.09483 1.73000 -0.26146 0.26269  -0.01144 128 LEU D N   
4914 C CA  . LEU D 128 ? 1.29077 1.12341 1.83233 -0.28122 0.25890  -0.00991 128 LEU D CA  
4915 C C   . LEU D 128 ? 1.28402 1.07314 1.80233 -0.27867 0.31833  0.03590  128 LEU D C   
4916 O O   . LEU D 128 ? 1.21732 1.03665 1.69676 -0.24836 0.35673  0.06250  128 LEU D O   
4917 C CB  . LEU D 128 ? 1.26940 1.04230 1.71079 -0.25215 0.22267  -0.03549 128 LEU D CB  
4918 C CG  . LEU D 128 ? 1.08183 0.87281 1.52558 -0.25321 0.16333  -0.08000 128 LEU D CG  
4919 C CD1 . LEU D 128 ? 1.11063 0.84232 1.44819 -0.21860 0.14273  -0.09689 128 LEU D CD1 
4920 C CD2 . LEU D 128 ? 1.12462 0.90106 1.65154 -0.30094 0.13039  -0.10220 128 LEU D CD2 
4921 N N   . ASP D 129 ? 1.45964 1.17152 1.99735 -0.30974 0.32470  0.04499  129 ASP D N   
4922 C CA  . ASP D 129 ? 1.45830 1.11580 1.97164 -0.30912 0.38132  0.09181  129 ASP D CA  
4923 C C   . ASP D 129 ? 1.45033 1.01226 1.84845 -0.27541 0.38031  0.09769  129 ASP D C   
4924 O O   . ASP D 129 ? 1.58891 1.11393 1.93555 -0.25555 0.42588  0.13837  129 ASP D O   
4925 C CB  . ASP D 129 ? 1.52269 1.15125 2.14040 -0.36762 0.39748  0.10640  129 ASP D CB  
4926 C CG  . ASP D 129 ? 1.59870 1.32193 2.34927 -0.40585 0.38725  0.09373  129 ASP D CG  
4927 O OD1 . ASP D 129 ? 1.59972 1.41393 2.35989 -0.38311 0.39025  0.08953  129 ASP D OD1 
4928 O OD2 . ASP D 129 ? 1.79558 1.50238 2.64461 -0.45818 0.37311  0.08626  129 ASP D OD2 
4929 N N   . LYS D 130 ? 1.37664 0.89804 1.73253 -0.26602 0.33096  0.05936  130 LYS D N   
4930 C CA  . LYS D 130 ? 1.53683 0.97214 1.78986 -0.23068 0.32707  0.06070  130 LYS D CA  
4931 C C   . LYS D 130 ? 1.60409 1.07107 1.78910 -0.18735 0.29261  0.03083  130 LYS D C   
4932 O O   . LYS D 130 ? 1.41840 0.93062 1.63321 -0.19696 0.25332  -0.00531 130 LYS D O   
4933 C CB  . LYS D 130 ? 1.61670 0.95108 1.87913 -0.25987 0.30558  0.04403  130 LYS D CB  
4934 C CG  . LYS D 130 ? 1.62256 0.94934 1.99483 -0.32093 0.31959  0.05632  130 LYS D CG  
4935 C CD  . LYS D 130 ? 1.67353 0.90568 2.03319 -0.33227 0.36368  0.09873  130 LYS D CD  
4936 C CE  . LYS D 130 ? 1.89659 1.09819 2.36905 -0.39956 0.36520  0.10121  130 LYS D CE  
4937 N NZ  . LYS D 130 ? 2.01277 1.30531 2.58522 -0.42867 0.40683  0.13337  130 LYS D NZ  
4938 N N   . PRO D 131 ? 1.57937 1.02360 1.67594 -0.13964 0.30513  0.04572  131 PRO D N   
4939 C CA  . PRO D 131 ? 1.53091 0.91212 1.57300 -0.11817 0.34433  0.08681  131 PRO D CA  
4940 C C   . PRO D 131 ? 1.62214 1.04854 1.67619 -0.11571 0.39032  0.12766  131 PRO D C   
4941 O O   . PRO D 131 ? 1.76960 1.14251 1.78891 -0.10629 0.42819  0.16725  131 PRO D O   
4942 C CB  . PRO D 131 ? 1.53186 0.90158 1.48525 -0.06375 0.32811  0.07807  131 PRO D CB  
4943 C CG  . PRO D 131 ? 1.49652 0.95940 1.46381 -0.05413 0.30112  0.05021  131 PRO D CG  
4944 C CD  . PRO D 131 ? 1.53468 1.02042 1.57958 -0.10038 0.27748  0.02190  131 PRO D CD  
4945 N N   . ASN D 132 ? 1.56830 1.08943 1.66575 -0.12103 0.38805  0.11851  132 ASN D N   
4946 C CA  . ASN D 132 ? 1.55938 1.12857 1.66847 -0.11686 0.43173  0.15202  132 ASN D CA  
4947 C C   . ASN D 132 ? 1.43929 1.08994 1.64936 -0.15272 0.42925  0.13775  132 ASN D C   
4948 O O   . ASN D 132 ? 1.39074 1.07613 1.64177 -0.16710 0.38625  0.09918  132 ASN D O   
4949 C CB  . ASN D 132 ? 1.47576 1.08137 1.50420 -0.06353 0.43282  0.15727  132 ASN D CB  
4950 C CG  . ASN D 132 ? 1.64684 1.18082 1.58059 -0.02371 0.43551  0.17493  132 ASN D CG  
4951 O OD1 . ASN D 132 ? 1.70471 1.16816 1.61440 -0.02546 0.46753  0.20940  132 ASN D OD1 
4952 N ND2 . ASN D 132 ? 1.49185 1.04423 1.37538 0.01296  0.40236  0.15310  132 ASN D ND2 
4953 N N   . ARG D 133 ? 1.49634 1.17724 1.74454 -0.16412 0.47749  0.17099  133 ARG D N   
4954 C CA  . ARG D 133 ? 1.50004 1.26714 1.84934 -0.19247 0.48246  0.16241  133 ARG D CA  
4955 C C   . ARG D 133 ? 1.43053 1.27223 1.74560 -0.15466 0.46861  0.14484  133 ARG D C   
4956 O O   . ARG D 133 ? 1.46695 1.32744 1.73155 -0.12277 0.50318  0.16829  133 ARG D O   
4957 C CB  . ARG D 133 ? 1.53335 1.30743 1.93599 -0.21470 0.54597  0.20706  133 ARG D CB  
4958 C CG  . ARG D 133 ? 1.90866 1.59770 2.33885 -0.25129 0.56687  0.23222  133 ARG D CG  
4959 C CD  . ARG D 133 ? 1.95524 1.65927 2.44314 -0.27310 0.63683  0.28132  133 ARG D CD  
4960 N NE  . ARG D 133 ? 1.97493 1.78732 2.56099 -0.28811 0.64735  0.27350  133 ARG D NE  
4961 C CZ  . ARG D 133 ? 1.93346 1.79400 2.64720 -0.33482 0.62024  0.24865  133 ARG D CZ  
4962 N NH1 . ARG D 133 ? 1.88867 1.69610 2.64617 -0.37400 0.57946  0.22689  133 ARG D NH1 
4963 N NH2 . ARG D 133 ? 1.86841 1.83142 2.66656 -0.34001 0.63198  0.24395  133 ARG D NH2 
4964 N N   . ALA D 134 ? 1.10565 1.02189 1.60997 -0.30750 0.57797  0.01040  134 ALA D N   
4965 C CA  . ALA D 134 ? 1.12572 1.09919 1.61027 -0.26920 0.53755  0.00998  134 ALA D CA  
4966 C C   . ALA D 134 ? 0.93927 1.00336 1.51228 -0.26187 0.48400  -0.03025 134 ALA D C   
4967 O O   . ALA D 134 ? 0.99057 1.07373 1.63449 -0.28403 0.47413  -0.05784 134 ALA D O   
4968 C CB  . ALA D 134 ? 1.10257 1.01574 1.47493 -0.22895 0.50638  0.04829  134 ALA D CB  
4969 N N   . GLY D 135 ? 0.98846 1.10182 1.54939 -0.22997 0.44837  -0.03351 135 GLY D N   
4970 C CA  . GLY D 135 ? 0.73619 0.91647 1.35043 -0.21414 0.39211  -0.06287 135 GLY D CA  
4971 C C   . GLY D 135 ? 0.77531 0.91999 1.32643 -0.18762 0.34745  -0.04550 135 GLY D C   
4972 O O   . GLY D 135 ? 0.94268 1.03305 1.40967 -0.16968 0.34995  -0.01170 135 GLY D O   
4973 N N   . TYR D 136 ? 0.81895 0.99665 1.41171 -0.18435 0.30601  -0.07073 136 TYR D N   
4974 C CA  . TYR D 136 ? 0.84299 0.99080 1.38653 -0.16349 0.26953  -0.05987 136 TYR D CA  
4975 C C   . TYR D 136 ? 0.74713 0.94697 1.30711 -0.14383 0.21996  -0.08086 136 TYR D C   
4976 O O   . TYR D 136 ? 0.68355 0.93585 1.30977 -0.15190 0.20502  -0.11315 136 TYR D O   
4977 C CB  . TYR D 136 ? 0.79196 0.89637 1.34805 -0.18271 0.27713  -0.06608 136 TYR D CB  
4978 C CG  . TYR D 136 ? 0.93277 0.96165 1.44805 -0.19566 0.32273  -0.03733 136 TYR D CG  
4979 C CD1 . TYR D 136 ? 0.80571 0.77447 1.23917 -0.17040 0.31974  -0.00225 136 TYR D CD1 
4980 C CD2 . TYR D 136 ? 0.99200 1.00833 1.54930 -0.23220 0.36919  -0.04499 136 TYR D CD2 
4981 C CE1 . TYR D 136 ? 1.08122 0.97163 1.46607 -0.17652 0.35737  0.02667  136 TYR D CE1 
4982 C CE2 . TYR D 136 ? 1.04242 0.97548 1.54876 -0.24388 0.41372  -0.01505 136 TYR D CE2 
4983 C CZ  . TYR D 136 ? 1.17242 1.03887 1.58729 -0.21349 0.40557  0.02209  136 TYR D CZ  
4984 O OH  . TYR D 136 ? 1.17178 0.94623 1.52521 -0.21954 0.44574  0.05434  136 TYR D OH  
4985 N N   . PHE D 137 ? 0.62204 0.80574 1.12107 -0.11784 0.19434  -0.06282 137 PHE D N   
4986 C CA  . PHE D 137 ? 0.75197 0.96610 1.24815 -0.10012 0.15115  -0.07731 137 PHE D CA  
4987 C C   . PHE D 137 ? 0.75410 0.93634 1.21671 -0.09302 0.13353  -0.07339 137 PHE D C   
4988 O O   . PHE D 137 ? 0.80112 0.94546 1.21913 -0.08437 0.14374  -0.04867 137 PHE D O   
4989 C CB  . PHE D 137 ? 0.50620 0.73297 0.96306 -0.07840 0.13941  -0.06352 137 PHE D CB  
4990 C CG  . PHE D 137 ? 0.67111 0.92395 1.15155 -0.08101 0.16051  -0.06671 137 PHE D CG  
4991 C CD1 . PHE D 137 ? 0.69761 0.92350 1.14733 -0.08528 0.19622  -0.04446 137 PHE D CD1 
4992 C CD2 . PHE D 137 ? 0.61066 0.91291 1.14081 -0.07641 0.14457  -0.09294 137 PHE D CD2 
4993 C CE1 . PHE D 137 ? 0.73944 0.98725 1.20614 -0.08762 0.22078  -0.04927 137 PHE D CE1 
4994 C CE2 . PHE D 137 ? 0.57758 0.90734 1.13507 -0.07628 0.16706  -0.09903 137 PHE D CE2 
4995 C CZ  . PHE D 137 ? 0.64769 0.95032 1.17300 -0.08335 0.20792  -0.07772 137 PHE D CZ  
4996 N N   . ILE D 138 ? 0.73198 0.93025 1.21536 -0.09455 0.10651  -0.09942 138 ILE D N   
4997 C CA  . ILE D 138 ? 0.74955 0.92056 1.20070 -0.08759 0.09076  -0.10193 138 ILE D CA  
4998 C C   . ILE D 138 ? 0.62573 0.81258 1.04186 -0.06831 0.05935  -0.10389 138 ILE D C   
4999 O O   . ILE D 138 ? 0.79291 1.01154 1.22474 -0.06369 0.03910  -0.11763 138 ILE D O   
5000 C CB  . ILE D 138 ? 0.69280 0.85718 1.18081 -0.10616 0.08641  -0.13166 138 ILE D CB  
5001 C CG1 . ILE D 138 ? 0.88062 0.99787 1.33279 -0.10201 0.08921  -0.12887 138 ILE D CG1 
5002 C CG2 . ILE D 138 ? 0.96038 1.16579 1.47575 -0.10543 0.05038  -0.16407 138 ILE D CG2 
5003 C CD1 . ILE D 138 ? 0.89765 0.97536 1.32052 -0.09423 0.11638  -0.09739 138 ILE D CD1 
5004 N N   . PHE D 139 ? 0.55477 0.71754 0.92431 -0.05655 0.05687  -0.09062 139 PHE D N   
5005 C CA  . PHE D 139 ? 0.66374 0.83011 0.99292 -0.04310 0.03409  -0.09177 139 PHE D CA  
5006 C C   . PHE D 139 ? 0.64633 0.78759 0.95035 -0.04182 0.03026  -0.10245 139 PHE D C   
5007 O O   . PHE D 139 ? 0.68233 0.80791 0.96061 -0.03453 0.04216  -0.08896 139 PHE D O   
5008 C CB  . PHE D 139 ? 0.67963 0.84717 0.97778 -0.03253 0.03968  -0.06680 139 PHE D CB  
5009 C CG  . PHE D 139 ? 0.59532 0.78299 0.90467 -0.03103 0.04044  -0.05993 139 PHE D CG  
5010 C CD1 . PHE D 139 ? 0.58037 0.76778 0.90581 -0.03559 0.06287  -0.04691 139 PHE D CD1 
5011 C CD2 . PHE D 139 ? 0.63573 0.83567 0.93286 -0.02333 0.02021  -0.06665 139 PHE D CD2 
5012 C CE1 . PHE D 139 ? 0.65155 0.85518 0.98230 -0.03365 0.06741  -0.04293 139 PHE D CE1 
5013 C CE2 . PHE D 139 ? 0.49485 0.71084 0.80227 -0.01938 0.02259  -0.06315 139 PHE D CE2 
5014 C CZ  . PHE D 139 ? 0.64369 0.86395 0.96897 -0.02515 0.04739  -0.05245 139 PHE D CZ  
5015 N N   . PRO D 140 ? 0.59243 0.73168 0.90409 -0.04766 0.01288  -0.12948 140 PRO D N   
5016 C CA  . PRO D 140 ? 0.77120 0.88072 1.05254 -0.04673 0.01154  -0.14320 140 PRO D CA  
5017 C C   . PRO D 140 ? 0.96441 1.06342 1.18538 -0.03513 -0.00501 -0.14573 140 PRO D C   
5018 O O   . PRO D 140 ? 1.08433 1.15622 1.27041 -0.03313 -0.00105 -0.15619 140 PRO D O   
5019 C CB  . PRO D 140 ? 0.64069 0.75150 0.95835 -0.06131 -0.00114 -0.17439 140 PRO D CB  
5020 C CG  . PRO D 140 ? 0.61473 0.76604 0.96758 -0.06264 -0.02149 -0.18196 140 PRO D CG  
5021 C CD  . PRO D 140 ? 0.58248 0.74871 0.94073 -0.05690 -0.00341 -0.15196 140 PRO D CD  
5022 N N   . ASP D 141 ? 0.94944 1.06221 1.15184 -0.02751 -0.02022 -0.13659 141 ASP D N   
5023 C CA  . ASP D 141 ? 0.89675 0.98854 1.03379 -0.01809 -0.03739 -0.13937 141 ASP D CA  
5024 C C   . ASP D 141 ? 0.95389 1.04434 1.06315 -0.01365 -0.02556 -0.11370 141 ASP D C   
5025 O O   . ASP D 141 ? 1.02804 1.11174 1.10605 -0.00649 -0.04244 -0.10890 141 ASP D O   
5026 C CB  . ASP D 141 ? 0.92916 1.02797 1.06324 -0.01131 -0.07564 -0.15881 141 ASP D CB  
5027 C CG  . ASP D 141 ? 1.27013 1.33099 1.32023 0.00046  -0.09652 -0.16366 141 ASP D CG  
5028 O OD1 . ASP D 141 ? 1.38151 1.41463 1.37692 0.00148  -0.07751 -0.14608 141 ASP D OD1 
5029 O OD2 . ASP D 141 ? 1.53081 1.58888 1.56838 0.00855  -0.13250 -0.18589 141 ASP D OD2 
5030 N N   . LEU D 142 ? 0.86398 0.96022 0.98716 -0.01726 0.00196  -0.09804 142 LEU D N   
5031 C CA  . LEU D 142 ? 0.81998 0.92011 0.92557 -0.01704 0.01319  -0.07804 142 LEU D CA  
5032 C C   . LEU D 142 ? 0.93694 1.02039 1.00739 -0.01920 0.03268  -0.07760 142 LEU D C   
5033 O O   . LEU D 142 ? 1.14260 1.22406 1.22601 -0.01821 0.04772  -0.08539 142 LEU D O   
5034 C CB  . LEU D 142 ? 0.76175 0.88824 0.91278 -0.01801 0.02636  -0.06242 142 LEU D CB  
5035 C CG  . LEU D 142 ? 0.62042 0.76379 0.80177 -0.01749 0.01672  -0.05961 142 LEU D CG  
5036 C CD1 . LEU D 142 ? 0.76900 0.92777 0.96998 -0.01707 0.03042  -0.04128 142 LEU D CD1 
5037 C CD2 . LEU D 142 ? 0.89421 1.03290 1.04974 -0.01309 -0.00359 -0.06222 142 LEU D CD2 
5038 N N   . SER D 143 ? 0.98636 1.05509 1.01287 -0.02270 0.03572  -0.06948 143 SER D N   
5039 C CA  . SER D 143 ? 0.91131 0.96777 0.90783 -0.02878 0.06141  -0.06930 143 SER D CA  
5040 C C   . SER D 143 ? 0.89096 0.95538 0.88304 -0.03909 0.07311  -0.05413 143 SER D C   
5041 O O   . SER D 143 ? 0.95217 1.00906 0.93226 -0.04008 0.05704  -0.04565 143 SER D O   
5042 C CB  . SER D 143 ? 1.07734 1.08740 1.00031 -0.02759 0.05785  -0.08128 143 SER D CB  
5043 O OG  . SER D 143 ? 1.31430 1.31659 1.23983 -0.01927 0.03535  -0.09868 143 SER D OG  
5044 N N   . VAL D 144 ? 0.91980 1.00074 0.92591 -0.04698 0.10177  -0.05362 144 VAL D N   
5045 C CA  . VAL D 144 ? 0.70836 0.80459 0.72284 -0.06185 0.11608  -0.04411 144 VAL D CA  
5046 C C   . VAL D 144 ? 0.96404 1.03243 0.92977 -0.07624 0.14605  -0.04799 144 VAL D C   
5047 O O   . VAL D 144 ? 0.98740 1.05557 0.94985 -0.07289 0.16692  -0.05924 144 VAL D O   
5048 C CB  . VAL D 144 ? 0.78105 0.93468 0.87127 -0.05938 0.12290  -0.04216 144 VAL D CB  
5049 C CG1 . VAL D 144 ? 0.70828 0.88269 0.81346 -0.07681 0.12946  -0.03622 144 VAL D CG1 
5050 C CG2 . VAL D 144 ? 0.66496 0.83293 0.78854 -0.04400 0.09911  -0.03736 144 VAL D CG2 
5051 N N   . ARG D 145 ? 0.96259 1.00174 0.88643 -0.09291 0.15165  -0.03911 145 ARG D N   
5052 C CA  . ARG D 145 ? 1.02389 1.02048 0.88396 -0.10931 0.18386  -0.04010 145 ARG D CA  
5053 C C   . ARG D 145 ? 0.96849 1.00979 0.87997 -0.12913 0.22464  -0.04585 145 ARG D C   
5054 O O   . ARG D 145 ? 0.96371 0.99331 0.85065 -0.13632 0.26019  -0.05426 145 ARG D O   
5055 C CB  . ARG D 145 ? 1.29313 1.22436 1.07538 -0.11942 0.17631  -0.02702 145 ARG D CB  
5056 C CG  . ARG D 145 ? 1.43079 1.30732 1.14359 -0.09740 0.14074  -0.02495 145 ARG D CG  
5057 C CD  . ARG D 145 ? 1.56898 1.38031 1.21085 -0.10135 0.12929  -0.01044 145 ARG D CD  
5058 N NE  . ARG D 145 ? 1.74546 1.47847 1.28123 -0.08681 0.11417  -0.00726 145 ARG D NE  
5059 C CZ  . ARG D 145 ? 1.71595 1.44283 1.23313 -0.06064 0.07965  -0.01705 145 ARG D CZ  
5060 N NH1 . ARG D 145 ? 1.69915 1.48980 1.29731 -0.04857 0.06051  -0.03025 145 ARG D NH1 
5061 N NH2 . ARG D 145 ? 1.98209 1.63360 1.39394 -0.04682 0.06320  -0.01410 145 ARG D NH2 
5062 N N   . ASN D 146 ? 0.88422 0.97980 0.86876 -0.13718 0.21997  -0.04409 146 ASN D N   
5063 C CA  . ASN D 146 ? 0.88085 1.02686 0.92405 -0.15846 0.25356  -0.05226 146 ASN D CA  
5064 C C   . ASN D 146 ? 0.82216 1.04896 0.96495 -0.14097 0.24262  -0.06068 146 ASN D C   
5065 O O   . ASN D 146 ? 0.85746 1.09765 1.02232 -0.12096 0.20721  -0.05470 146 ASN D O   
5066 C CB  . ASN D 146 ? 1.02302 1.16016 1.06306 -0.18769 0.25607  -0.04592 146 ASN D CB  
5067 C CG  . ASN D 146 ? 1.08815 1.13209 1.02134 -0.20051 0.26106  -0.03343 146 ASN D CG  
5068 O OD1 . ASN D 146 ? 1.05883 1.05067 0.92076 -0.20109 0.28315  -0.03232 146 ASN D OD1 
5069 N ND2 . ASN D 146 ? 1.12370 1.14044 1.03866 -0.20809 0.23913  -0.02415 146 ASN D ND2 
5070 N N   . GLU D 147 ? 0.86904 1.14754 1.07002 -0.14751 0.27494  -0.07468 147 GLU D N   
5071 C CA  . GLU D 147 ? 0.82373 1.17695 1.11779 -0.12554 0.26413  -0.08346 147 GLU D CA  
5072 C C   . GLU D 147 ? 0.74271 1.14139 1.09020 -0.13068 0.23462  -0.07985 147 GLU D C   
5073 O O   . GLU D 147 ? 0.90814 1.29106 1.23534 -0.15800 0.23331  -0.07602 147 GLU D O   
5074 C CB  . GLU D 147 ? 0.77251 1.17604 1.12325 -0.12915 0.30660  -0.10275 147 GLU D CB  
5075 C CG  . GLU D 147 ? 0.99728 1.39527 1.33388 -0.16938 0.35142  -0.10951 147 GLU D CG  
5076 C CD  . GLU D 147 ? 1.25386 1.70053 1.64478 -0.17118 0.40060  -0.13113 147 GLU D CD  
5077 O OE1 . GLU D 147 ? 1.08547 1.59990 1.56199 -0.14286 0.39223  -0.14348 147 GLU D OE1 
5078 O OE2 . GLU D 147 ? 1.24953 1.66427 1.59573 -0.19968 0.44923  -0.13575 147 GLU D OE2 
5079 N N   . GLY D 148 ? 0.72855 1.17660 1.13741 -0.10271 0.20969  -0.08127 148 GLY D N   
5080 C CA  . GLY D 148 ? 0.60484 1.09971 1.06274 -0.10305 0.17922  -0.08054 148 GLY D CA  
5081 C C   . GLY D 148 ? 0.64460 1.13959 1.10656 -0.06825 0.14138  -0.06889 148 GLY D C   
5082 O O   . GLY D 148 ? 0.68642 1.14709 1.12126 -0.04621 0.14102  -0.06223 148 GLY D O   
5083 N N   . SER D 149 ? 0.62157 1.15086 1.11326 -0.06471 0.11050  -0.06726 149 SER D N   
5084 C CA  . SER D 149 ? 0.75526 1.27831 1.24026 -0.03343 0.07649  -0.05397 149 SER D CA  
5085 C C   . SER D 149 ? 0.77567 1.24953 1.19779 -0.04420 0.05875  -0.04097 149 SER D C   
5086 O O   . SER D 149 ? 0.85372 1.33413 1.27134 -0.06719 0.05088  -0.04564 149 SER D O   
5087 C CB  . SER D 149 ? 0.69286 1.28452 1.24496 -0.01597 0.05078  -0.06152 149 SER D CB  
5088 O OG  . SER D 149 ? 1.02317 1.59908 1.54585 -0.00012 0.01465  -0.04789 149 SER D OG  
5089 N N   . TYR D 150 ? 0.74438 1.17007 1.12239 -0.02834 0.05401  -0.02721 150 TYR D N   
5090 C CA  . TYR D 150 ? 0.73929 1.12067 1.06324 -0.03593 0.04242  -0.01741 150 TYR D CA  
5091 C C   . TYR D 150 ? 0.75486 1.12203 1.06549 -0.01140 0.02428  -0.00374 150 TYR D C   
5092 O O   . TYR D 150 ? 0.74311 1.12086 1.07584 0.01200  0.02152  0.00087  150 TYR D O   
5093 C CB  . TYR D 150 ? 0.56822 0.89988 0.84702 -0.04612 0.05875  -0.01647 150 TYR D CB  
5094 C CG  . TYR D 150 ? 0.79874 1.12425 1.06831 -0.06960 0.08137  -0.02596 150 TYR D CG  
5095 C CD1 . TYR D 150 ? 0.67564 1.01050 0.96123 -0.06829 0.10549  -0.03409 150 TYR D CD1 
5096 C CD2 . TYR D 150 ? 0.83821 1.13941 1.07502 -0.09296 0.08181  -0.02648 150 TYR D CD2 
5097 C CE1 . TYR D 150 ? 0.78646 1.10834 1.05313 -0.09127 0.13197  -0.04148 150 TYR D CE1 
5098 C CE2 . TYR D 150 ? 0.73059 1.01340 0.94751 -0.11613 0.10660  -0.03214 150 TYR D CE2 
5099 C CZ  . TYR D 150 ? 0.77861 1.07227 1.00884 -0.11606 0.13294  -0.03907 150 TYR D CZ  
5100 O OH  . TYR D 150 ? 0.79555 1.06469 0.99668 -0.14059 0.16334  -0.04362 150 TYR D OH  
5101 N N   . ARG D 151 ? 0.66815 1.00545 0.93851 -0.01674 0.01494  0.00277  151 ARG D N   
5102 C CA  . ARG D 151 ? 0.64378 0.95484 0.88934 -0.00016 0.00795  0.01590  151 ARG D CA  
5103 C C   . ARG D 151 ? 0.70075 0.97411 0.91509 -0.00929 0.01701  0.01612  151 ARG D C   
5104 O O   . ARG D 151 ? 0.79744 1.06097 0.99659 -0.02532 0.01902  0.00878  151 ARG D O   
5105 C CB  . ARG D 151 ? 0.54575 0.86398 0.77452 0.00569  -0.01307 0.02090  151 ARG D CB  
5106 C CG  . ARG D 151 ? 0.72480 1.07403 0.97756 0.02636  -0.03026 0.02434  151 ARG D CG  
5107 C CD  . ARG D 151 ? 0.78961 1.14277 1.01464 0.03094  -0.05556 0.02630  151 ARG D CD  
5108 N NE  . ARG D 151 ? 1.01018 1.39827 1.25933 0.05353  -0.08014 0.02696  151 ARG D NE  
5109 C CZ  . ARG D 151 ? 0.85212 1.21886 1.07385 0.08308  -0.09205 0.04388  151 ARG D CZ  
5110 N NH1 . ARG D 151 ? 0.92924 1.24004 1.10044 0.08898  -0.07628 0.06152  151 ARG D NH1 
5111 N NH2 . ARG D 151 ? 0.76151 1.16287 1.00745 0.10760  -0.12010 0.04266  151 ARG D NH2 
5112 N N   . PHE D 152 ? 0.54965 0.80082 0.75610 0.00142  0.02235  0.02387  152 PHE D N   
5113 C CA  . PHE D 152 ? 0.52248 0.74854 0.71200 -0.00439 0.02796  0.02132  152 PHE D CA  
5114 C C   . PHE D 152 ? 0.60532 0.82229 0.77257 -0.00151 0.02407  0.02756  152 PHE D C   
5115 O O   . PHE D 152 ? 0.69458 0.90969 0.85358 0.00909  0.02288  0.03863  152 PHE D O   
5116 C CB  . PHE D 152 ? 0.71481 0.92557 0.91781 0.00019  0.03964  0.02079  152 PHE D CB  
5117 C CG  . PHE D 152 ? 0.75144 0.95832 0.95976 -0.00603 0.04361  0.00841  152 PHE D CG  
5118 C CD1 . PHE D 152 ? 0.76985 0.96934 0.95845 -0.01550 0.03804  -0.00009 152 PHE D CD1 
5119 C CD2 . PHE D 152 ? 0.72090 0.92370 0.94542 -0.00037 0.05281  0.00520  152 PHE D CD2 
5120 C CE1 . PHE D 152 ? 0.82698 1.01443 1.00544 -0.01956 0.04085  -0.01030 152 PHE D CE1 
5121 C CE2 . PHE D 152 ? 0.66459 0.85889 0.88354 -0.00565 0.05731  -0.00801 152 PHE D CE2 
5122 C CZ  . PHE D 152 ? 0.77031 0.95656 0.96297 -0.01542 0.05096  -0.01511 152 PHE D CZ  
5123 N N   . SER D 153 ? 0.65918 0.86663 0.81057 -0.00867 0.02180  0.02036  153 SER D N   
5124 C CA  . SER D 153 ? 0.63604 0.83304 0.76636 -0.00521 0.02329  0.02235  153 SER D CA  
5125 C C   . SER D 153 ? 0.61205 0.80124 0.75575 -0.00462 0.03403  0.01614  153 SER D C   
5126 O O   . SER D 153 ? 0.68925 0.87647 0.84012 -0.00750 0.02845  0.00578  153 SER D O   
5127 C CB  . SER D 153 ? 0.73946 0.93222 0.84474 -0.01125 0.01171  0.01538  153 SER D CB  
5128 O OG  . SER D 153 ? 0.91520 1.09685 0.99468 -0.00548 0.01460  0.01641  153 SER D OG  
5129 N N   . PHE D 154 ? 0.64895 0.83327 0.79631 -0.00099 0.04941  0.02194  154 PHE D N   
5130 C CA  . PHE D 154 ? 0.56203 0.74891 0.73659 -0.00325 0.06230  0.01279  154 PHE D CA  
5131 C C   . PHE D 154 ? 0.63720 0.82247 0.79884 0.00005  0.07257  0.00920  154 PHE D C   
5132 O O   . PHE D 154 ? 0.74573 0.91861 0.87871 0.00236  0.08496  0.02031  154 PHE D O   
5133 C CB  . PHE D 154 ? 0.50715 0.68741 0.70256 -0.00685 0.08000  0.01954  154 PHE D CB  
5134 C CG  . PHE D 154 ? 0.59587 0.77440 0.80346 -0.00748 0.07237  0.02005  154 PHE D CG  
5135 C CD1 . PHE D 154 ? 0.57110 0.75705 0.80233 -0.01218 0.06441  0.00439  154 PHE D CD1 
5136 C CD2 . PHE D 154 ? 0.59968 0.76846 0.79245 -0.00040 0.07176  0.03460  154 PHE D CD2 
5137 C CE1 . PHE D 154 ? 0.52384 0.70446 0.75976 -0.01224 0.06089  0.00271  154 PHE D CE1 
5138 C CE2 . PHE D 154 ? 0.64091 0.80947 0.84815 0.00167  0.06806  0.03253  154 PHE D CE2 
5139 C CZ  . PHE D 154 ? 0.57942 0.75243 0.80631 -0.00549 0.06505  0.01627  154 PHE D CZ  
5140 N N   . HIS D 155 ? 0.49495 0.68961 0.67313 0.00309  0.06706  -0.00675 155 HIS D N   
5141 C CA  . HIS D 155 ? 0.63614 0.83107 0.80631 0.00979  0.07699  -0.01472 155 HIS D CA  
5142 C C   . HIS D 155 ? 0.59412 0.81256 0.81683 0.00925  0.09503  -0.02819 155 HIS D C   
5143 O O   . HIS D 155 ? 0.64683 0.88324 0.90963 0.01025  0.08170  -0.04144 155 HIS D O   
5144 C CB  . HIS D 155 ? 0.62069 0.80551 0.77024 0.01783  0.05572  -0.02458 155 HIS D CB  
5145 C CG  . HIS D 155 ? 0.54921 0.71825 0.66751 0.01175  0.03650  -0.01679 155 HIS D CG  
5146 N ND1 . HIS D 155 ? 0.73342 0.88991 0.81347 0.00804  0.03282  -0.01035 155 HIS D ND1 
5147 C CD2 . HIS D 155 ? 0.62304 0.78867 0.74439 0.00722  0.02171  -0.01672 155 HIS D CD2 
5148 C CE1 . HIS D 155 ? 0.72225 0.87463 0.79392 -0.00047 0.01787  -0.00784 155 HIS D CE1 
5149 N NE2 . HIS D 155 ? 0.66586 0.82094 0.75874 -0.00123 0.01389  -0.01043 155 HIS D NE2 
5150 N N   . LEU D 156 ? 0.56355 0.78279 0.78535 0.00761  0.12501  -0.02711 156 LEU D N   
5151 C CA  . LEU D 156 ? 0.59183 0.83983 0.87320 0.00256  0.14971  -0.04198 156 LEU D CA  
5152 C C   . LEU D 156 ? 0.71854 0.98708 1.02016 0.01779  0.14975  -0.06296 156 LEU D C   
5153 O O   . LEU D 156 ? 0.74381 0.99328 0.99997 0.02697  0.15664  -0.06109 156 LEU D O   
5154 C CB  . LEU D 156 ? 0.70749 0.94031 0.97601 -0.01042 0.19108  -0.02853 156 LEU D CB  
5155 C CG  . LEU D 156 ? 0.63923 0.90289 0.97642 -0.02342 0.22573  -0.04453 156 LEU D CG  
5156 C CD1 . LEU D 156 ? 0.52150 0.80755 0.92142 -0.03557 0.21231  -0.05523 156 LEU D CD1 
5157 C CD2 . LEU D 156 ? 0.72366 0.95837 1.02955 -0.03703 0.27415  -0.02836 156 LEU D CD2 
5158 N N   . PHE D 157 ? 0.72839 1.03534 1.09838 0.02248  0.14011  -0.08501 157 PHE D N   
5159 C CA  . PHE D 157 ? 0.64712 0.98173 1.05322 0.04177  0.13910  -0.10858 157 PHE D CA  
5160 C C   . PHE D 157 ? 0.67749 1.06236 1.16666 0.03264  0.17197  -0.12807 157 PHE D C   
5161 O O   . PHE D 157 ? 0.66350 1.07441 1.20763 0.01687  0.17071  -0.13501 157 PHE D O   
5162 C CB  . PHE D 157 ? 0.73686 1.07704 1.15580 0.06120  0.09301  -0.12119 157 PHE D CB  
5163 C CG  . PHE D 157 ? 0.88716 1.17712 1.22901 0.06801  0.06629  -0.10532 157 PHE D CG  
5164 C CD1 . PHE D 157 ? 0.80091 1.05941 1.09030 0.07761  0.07153  -0.10168 157 PHE D CD1 
5165 C CD2 . PHE D 157 ? 0.69388 0.96663 1.01533 0.06211  0.03918  -0.09601 157 PHE D CD2 
5166 C CE1 . PHE D 157 ? 0.66169 0.87501 0.88677 0.07826  0.04936  -0.08971 157 PHE D CE1 
5167 C CE2 . PHE D 157 ? 0.72806 0.95689 0.98415 0.06362  0.02104  -0.08266 157 PHE D CE2 
5168 C CZ  . PHE D 157 ? 0.78359 0.98392 0.99491 0.07005  0.02586  -0.07973 157 PHE D CZ  
5169 N N   . GLU D 158 ? 0.67874 1.07681 1.17810 0.04065  0.20367  -0.13913 158 GLU D N   
5170 C CA  . GLU D 158 ? 0.62965 1.08208 1.21569 0.03171  0.24190  -0.16168 158 GLU D CA  
5171 C C   . GLU D 158 ? 0.67966 1.18084 1.33123 0.06154  0.22360  -0.19414 158 GLU D C   
5172 O O   . GLU D 158 ? 0.78540 1.26302 1.39289 0.08799  0.21228  -0.19603 158 GLU D O   
5173 C CB  . GLU D 158 ? 0.60401 1.03554 1.15323 0.01833  0.30092  -0.15126 158 GLU D CB  
5174 C CG  . GLU D 158 ? 0.63626 1.12215 1.27643 0.00151  0.35141  -0.17344 158 GLU D CG  
5175 C CD  . GLU D 158 ? 0.80024 1.25336 1.38749 -0.01313 0.41501  -0.15997 158 GLU D CD  
5176 O OE1 . GLU D 158 ? 0.87520 1.26045 1.35514 -0.01570 0.41577  -0.12892 158 GLU D OE1 
5177 O OE2 . GLU D 158 ? 0.82186 1.31765 1.47343 -0.02071 0.46400  -0.18168 158 GLU D OE2 
5178 N N   . GLN D 159 ? 0.76274 1.32996 1.51959 0.05871  0.21772  -0.22119 159 GLN D N   
5179 C CA  . GLN D 159 ? 0.75842 1.38356 1.59403 0.09048  0.19922  -0.25589 159 GLN D CA  
5180 C C   . GLN D 159 ? 0.79974 1.49129 1.73261 0.07507  0.25566  -0.28116 159 GLN D C   
5181 O O   . GLN D 159 ? 0.69543 1.43087 1.70445 0.05038  0.26017  -0.29416 159 GLN D O   
5182 C CB  . GLN D 159 ? 0.56556 1.21889 1.44689 0.10374  0.13849  -0.27091 159 GLN D CB  
5183 C CG  . GLN D 159 ? 0.83433 1.53621 1.78068 0.14667  0.10463  -0.30343 159 GLN D CG  
5184 C CD  . GLN D 159 ? 0.94839 1.63240 1.87096 0.17097  0.03377  -0.30386 159 GLN D CD  
5185 O OE1 . GLN D 159 ? 0.95050 1.65138 1.89906 0.15395  0.00950  -0.30793 159 GLN D OE1 
5186 N NE2 . GLN D 159 ? 0.86243 1.50432 1.72770 0.21069  0.00163  -0.29975 159 GLN D NE2 
5187 N N   . ILE D 160 ? 0.92640 1.61125 1.83866 0.08610  0.29808  -0.28461 160 ILE D N   
5188 C CA  . ILE D 160 ? 0.95403 1.67464 1.91866 0.06649  0.35417  -0.29672 160 ILE D CA  
5189 C C   . ILE D 160 ? 1.02448 1.81501 2.09361 0.07686  0.32651  -0.32719 160 ILE D C   
5190 O O   . ILE D 160 ? 1.01426 1.82667 2.10979 0.11592  0.27565  -0.34459 160 ILE D O   
5191 C CB  . ILE D 160 ? 1.13149 1.82484 2.04045 0.08137  0.40081  -0.29575 160 ILE D CB  
5192 C CG1 . ILE D 160 ? 1.16904 1.88095 2.09749 0.13162  0.36977  -0.32030 160 ILE D CG1 
5193 C CG2 . ILE D 160 ? 1.07092 1.68117 1.85317 0.07149  0.41538  -0.26194 160 ILE D CG2 
5194 C CD1 . ILE D 160 ? 1.04882 1.81016 2.04323 0.14103  0.39717  -0.34385 160 ILE D CD1 
5195 N N   . LYS D 161 ? 1.06588 1.85452 2.07501 -0.09801 0.42414  -0.13981 161 LYS D N   
5196 C CA  . LYS D 161 ? 1.04946 1.94537 2.20317 -0.10775 0.42181  -0.13947 161 LYS D CA  
5197 C C   . LYS D 161 ? 1.13154 2.07318 2.35063 -0.10387 0.49485  -0.14597 161 LYS D C   
5198 O O   . LYS D 161 ? 0.99133 2.03242 2.34650 -0.10527 0.49998  -0.14619 161 LYS D O   
5199 C CB  . LYS D 161 ? 0.99692 1.91876 2.17605 -0.15897 0.39060  -0.13216 161 LYS D CB  
5200 C CG  . LYS D 161 ? 1.31738 2.35476 2.64674 -0.17640 0.37471  -0.13056 161 LYS D CG  
5201 C CD  . LYS D 161 ? 1.46210 2.51251 2.80078 -0.23355 0.34892  -0.12678 161 LYS D CD  
5202 C CE  . LYS D 161 ? 1.40172 2.54930 2.85407 -0.24554 0.30506  -0.11885 161 LYS D CE  
5203 N NZ  . LYS D 161 ? 1.07976 2.29454 2.61607 -0.23269 0.34319  -0.11346 161 LYS D NZ  
5204 N N   . ASP D 162 ? 1.16123 2.03427 2.28750 -0.09760 0.55096  -0.15086 162 ASP D N   
5205 C CA  . ASP D 162 ? 1.16755 2.06902 2.33400 -0.09288 0.62867  -0.15843 162 ASP D CA  
5206 C C   . ASP D 162 ? 1.29255 2.12528 2.37217 -0.04999 0.66104  -0.17053 162 ASP D C   
5207 O O   . ASP D 162 ? 1.31529 2.05050 2.25604 -0.04850 0.65006  -0.16914 162 ASP D O   
5208 C CB  . ASP D 162 ? 1.30911 2.17976 2.42284 -0.13943 0.66869  -0.14944 162 ASP D CB  
5209 C CG  . ASP D 162 ? 1.38696 2.31740 2.57378 -0.14990 0.70524  -0.14444 162 ASP D CG  
5210 O OD1 . ASP D 162 ? 1.44050 2.38067 2.64035 -0.11785 0.74620  -0.15237 162 ASP D OD1 
5211 O OD2 . ASP D 162 ? 1.43815 2.40373 2.66756 -0.19138 0.69410  -0.13355 162 ASP D OD2 
5212 N N   . PRO D 163 ? 1.37602 2.25074 2.52558 -0.01432 0.69519  -0.18146 163 PRO D N   
5213 C CA  . PRO D 163 ? 1.39010 2.19704 2.46086 0.02654  0.72930  -0.19850 163 PRO D CA  
5214 C C   . PRO D 163 ? 1.55095 2.26929 2.48201 0.01077  0.78585  -0.20187 163 PRO D C   
5215 O O   . PRO D 163 ? 1.58790 2.21945 2.40169 0.03238  0.78928  -0.21177 163 PRO D O   
5216 C CB  . PRO D 163 ? 1.23064 2.10029 2.40280 0.06264  0.74702  -0.20372 163 PRO D CB  
5217 C CG  . PRO D 163 ? 1.14552 2.12006 2.45647 0.04842  0.69902  -0.18809 163 PRO D CG  
5218 C CD  . PRO D 163 ? 1.24440 2.21747 2.52773 -0.00794 0.69259  -0.17558 163 PRO D CD  
5219 N N   . LYS D 164 ? 1.77011 2.49752 2.69377 -0.02664 0.81671  -0.18974 164 LYS D N   
5220 C CA  . LYS D 164 ? 1.75599 2.39644 2.54220 -0.04369 0.86619  -0.18814 164 LYS D CA  
5221 C C   . LYS D 164 ? 1.76973 2.31998 2.42451 -0.05496 0.84069  -0.18330 164 LYS D C   
5222 O O   . LYS D 164 ? 1.84585 2.30760 2.36564 -0.04961 0.86640  -0.18678 164 LYS D O   
5223 C CB  . LYS D 164 ? 1.76963 2.43666 2.57916 -0.08564 0.89408  -0.17208 164 LYS D CB  
5224 C CG  . LYS D 164 ? 1.71811 2.43849 2.60496 -0.12156 0.84873  -0.15723 164 LYS D CG  
5225 C CD  . LYS D 164 ? 1.74437 2.42644 2.57221 -0.16916 0.87126  -0.14008 164 LYS D CD  
5226 C CE  . LYS D 164 ? 1.58214 2.29261 2.45924 -0.20529 0.82219  -0.12841 164 LYS D CE  
5227 N NZ  . LYS D 164 ? 1.55153 2.19187 2.33803 -0.24642 0.83764  -0.11186 164 LYS D NZ  
5228 N N   . ASP D 165 ? 1.64186 2.20242 2.31484 -0.06921 0.77070  -0.17021 165 ASP D N   
5229 C CA  . ASP D 165 ? 1.61470 2.08779 2.16000 -0.07849 0.72523  -0.15814 165 ASP D CA  
5230 C C   . ASP D 165 ? 1.58017 2.00118 2.05694 -0.04201 0.68485  -0.16786 165 ASP D C   
5231 O O   . ASP D 165 ? 1.61956 1.97097 1.99325 -0.04665 0.64690  -0.15852 165 ASP D O   
5232 C CB  . ASP D 165 ? 1.47978 1.98104 2.07077 -0.10707 0.67108  -0.14316 165 ASP D CB  
5233 C CG  . ASP D 165 ? 1.45910 1.99118 2.09403 -0.15088 0.70764  -0.13248 165 ASP D CG  
5234 O OD1 . ASP D 165 ? 1.35427 1.85761 1.94243 -0.16366 0.77090  -0.13009 165 ASP D OD1 
5235 O OD2 . ASP D 165 ? 1.38882 1.96997 2.10032 -0.17508 0.67357  -0.12675 165 ASP D OD2 
5236 N N   . ALA D 166 ? 1.63958 2.09273 2.17551 -0.00634 0.69171  -0.18557 166 ALA D N   
5237 C CA  . ALA D 166 ? 1.53576 1.93622 2.00992 0.02642  0.65618  -0.19630 166 ALA D CA  
5238 C C   . ALA D 166 ? 1.68033 1.98156 2.00057 0.02813  0.68438  -0.20254 166 ALA D C   
5239 O O   . ALA D 166 ? 1.69412 1.97294 1.96536 0.01236  0.74302  -0.20210 166 ALA D O   
5240 C CB  . ALA D 166 ? 1.50627 1.95694 2.07913 0.06542  0.66606  -0.21374 166 ALA D CB  
5241 N N   . THR D 167 ? 1.66561 1.90602 1.90634 0.04489  0.64061  -0.20760 167 THR D N   
5242 C CA  . THR D 167 ? 1.77396 1.91830 1.86203 0.04374  0.65280  -0.21265 167 THR D CA  
5243 C C   . THR D 167 ? 1.70886 1.82690 1.76484 0.06384  0.72021  -0.23790 167 THR D C   
5244 O O   . THR D 167 ? 1.56240 1.66609 1.62572 0.09449  0.71755  -0.25890 167 THR D O   
5245 C CB  . THR D 167 ? 1.57707 1.66989 1.59956 0.05416  0.58561  -0.21293 167 THR D CB  
5246 O OG1 . THR D 167 ? 1.50751 1.62774 1.56704 0.03798  0.52808  -0.19166 167 THR D OG1 
5247 C CG2 . THR D 167 ? 1.56721 1.56557 1.43140 0.04594  0.58893  -0.21413 167 THR D CG2 
5248 N N   . PRO D 184 ? 1.60763 2.74894 3.26564 0.21392  -0.10737 -0.02966 184 PRO D N   
5249 C CA  . PRO D 184 ? 1.73161 2.83621 3.34627 0.21215  -0.02927 -0.05578 184 PRO D CA  
5250 C C   . PRO D 184 ? 1.74169 2.72257 3.20345 0.21475  -0.01479 -0.06789 184 PRO D C   
5251 O O   . PRO D 184 ? 1.66428 2.59236 3.04237 0.19880  -0.06238 -0.05812 184 PRO D O   
5252 C CB  . PRO D 184 ? 1.61357 2.76510 3.23456 0.15445  -0.01874 -0.06116 184 PRO D CB  
5253 C CG  . PRO D 184 ? 1.52592 2.75774 3.21952 0.13189  -0.08460 -0.03940 184 PRO D CG  
5254 C CD  . PRO D 184 ? 1.47862 2.70802 3.19668 0.17593  -0.13234 -0.01846 184 PRO D CD  
5255 N N   . GLN D 185 ? 1.90570 2.84266 3.33185 0.23292  0.05083  -0.08900 185 GLN D N   
5256 C CA  . GLN D 185 ? 1.81210 2.63632 3.09996 0.23617  0.06713  -0.10207 185 GLN D CA  
5257 C C   . GLN D 185 ? 1.67831 2.46956 2.87833 0.19442  0.10068  -0.11499 185 GLN D C   
5258 O O   . GLN D 185 ? 1.63547 2.36115 2.75762 0.20217  0.14466  -0.13176 185 GLN D O   
5259 C CB  . GLN D 185 ? 1.91979 2.70244 3.21135 0.28630  0.11244  -0.11730 185 GLN D CB  
5260 C CG  . GLN D 185 ? 2.07720 2.87214 3.44433 0.33441  0.08169  -0.10415 185 GLN D CG  
5261 C CD  . GLN D 185 ? 2.01851 2.91807 3.54606 0.36285  0.10196  -0.09972 185 GLN D CD  
5262 O OE1 . GLN D 185 ? 1.97821 2.94283 3.56138 0.34394  0.14253  -0.10799 185 GLN D OE1 
5263 N NE2 . GLN D 185 ? 1.88908 2.80562 3.49555 0.40891  0.07455  -0.08523 185 GLN D NE2 
5264 N N   . GLU D 186 ? 1.49435 2.32704 2.70377 0.15000  0.07975  -0.10705 186 GLU D N   
5265 C CA  . GLU D 186 ? 1.28787 2.09440 2.42693 0.11022  0.11071  -0.11596 186 GLU D CA  
5266 C C   . GLU D 186 ? 1.16878 1.87184 2.17281 0.11177  0.12322  -0.12500 186 GLU D C   
5267 O O   . GLU D 186 ? 1.12974 1.78098 2.07690 0.12168  0.08568  -0.12004 186 GLU D O   
5268 C CB  . GLU D 186 ? 1.18092 2.01743 2.32121 0.06401  0.06850  -0.10487 186 GLU D CB  
5269 C CG  . GLU D 186 ? 1.29863 2.23110 2.54820 0.03950  0.07712  -0.10230 186 GLU D CG  
5270 C CD  . GLU D 186 ? 1.27371 2.20006 2.49972 0.00977  0.13393  -0.11317 186 GLU D CD  
5271 O OE1 . GLU D 186 ? 1.24900 2.12746 2.42399 0.02714  0.18534  -0.12415 186 GLU D OE1 
5272 O OE2 . GLU D 186 ? 1.22554 2.18993 2.47825 -0.03294 0.12646  -0.11044 186 GLU D OE2 
5273 N N   . PHE D 187 ? 1.09474 1.76928 2.04892 0.10064  0.17577  -0.13699 187 PHE D N   
5274 C CA  . PHE D 187 ? 1.06519 1.64760 1.89485 0.10094  0.18985  -0.14518 187 PHE D CA  
5275 C C   . PHE D 187 ? 0.92568 1.47914 1.68399 0.06109  0.17177  -0.13788 187 PHE D C   
5276 O O   . PHE D 187 ? 0.91502 1.50967 1.70756 0.03050  0.17567  -0.13281 187 PHE D O   
5277 C CB  . PHE D 187 ? 1.06438 1.62166 1.86540 0.11337  0.25615  -0.16113 187 PHE D CB  
5278 C CG  . PHE D 187 ? 1.23137 1.83804 2.12836 0.14707  0.29205  -0.17004 187 PHE D CG  
5279 C CD1 . PHE D 187 ? 1.23903 1.86818 2.20375 0.18141  0.26278  -0.16675 187 PHE D CD1 
5280 C CD2 . PHE D 187 ? 1.10939 1.73736 2.02865 0.14571  0.35782  -0.18073 187 PHE D CD2 
5281 C CE1 . PHE D 187 ? 1.22728 1.90284 2.28841 0.21691  0.29756  -0.17424 187 PHE D CE1 
5282 C CE2 . PHE D 187 ? 1.05684 1.73324 2.07109 0.17865  0.39649  -0.18996 187 PHE D CE2 
5283 C CZ  . PHE D 187 ? 1.03060 1.73230 2.11970 0.21602  0.36603  -0.18692 187 PHE D CZ  
5284 N N   . LEU D 188 ? 0.80100 1.28210 1.46241 0.06164  0.15296  -0.13782 188 LEU D N   
5285 C CA  . LEU D 188 ? 0.80110 1.24534 1.38934 0.03094  0.14128  -0.13156 188 LEU D CA  
5286 C C   . LEU D 188 ? 0.77133 1.14210 1.25982 0.03786  0.16099  -0.13782 188 LEU D C   
5287 O O   . LEU D 188 ? 0.90361 1.23298 1.35299 0.05813  0.14597  -0.14256 188 LEU D O   
5288 C CB  . LEU D 188 ? 0.63879 1.07849 1.21799 0.02022  0.08644  -0.12123 188 LEU D CB  
5289 C CG  . LEU D 188 ? 0.67819 1.08731 1.19697 -0.01036 0.07722  -0.11527 188 LEU D CG  
5290 C CD1 . LEU D 188 ? 0.79360 1.23448 1.34193 -0.03708 0.10466  -0.11480 188 LEU D CD1 
5291 C CD2 . LEU D 188 ? 0.58288 0.99104 1.09674 -0.02143 0.02924  -0.10703 188 LEU D CD2 
5292 N N   . GLU D 189 ? 0.71634 1.06793 1.16063 0.01894  0.19132  -0.13654 189 GLU D N   
5293 C CA  . GLU D 189 ? 0.76404 1.04960 1.11221 0.02330  0.21062  -0.14041 189 GLU D CA  
5294 C C   . GLU D 189 ? 0.84231 1.09226 1.12771 0.00133  0.18988  -0.12784 189 GLU D C   
5295 O O   . GLU D 189 ? 0.88373 1.14887 1.18197 -0.02159 0.19924  -0.11930 189 GLU D O   
5296 C CB  . GLU D 189 ? 0.81518 1.10129 1.15593 0.02301  0.26858  -0.14712 189 GLU D CB  
5297 C CG  . GLU D 189 ? 1.00738 1.32658 1.41033 0.04806  0.30008  -0.16138 189 GLU D CG  
5298 C CD  . GLU D 189 ? 1.29521 1.56462 1.62682 0.06006  0.34803  -0.17465 189 GLU D CD  
5299 O OE1 . GLU D 189 ? 1.26062 1.47652 1.53066 0.07842  0.33745  -0.18491 189 GLU D OE1 
5300 O OE2 . GLU D 189 ? 1.35982 1.64050 1.69284 0.04863  0.39726  -0.17533 189 GLU D OE2 
5301 N N   . PHE D 190 ? 0.96871 1.17105 1.19020 0.00835  0.16275  -0.12687 190 PHE D N   
5302 C CA  . PHE D 190 ? 0.75838 0.92536 0.92003 -0.00709 0.14700  -0.11454 190 PHE D CA  
5303 C C   . PHE D 190 ? 0.81456 0.94765 0.91509 -0.01250 0.18199  -0.11111 190 PHE D C   
5304 O O   . PHE D 190 ? 0.99765 1.10961 1.06427 -0.00063 0.20823  -0.12135 190 PHE D O   
5305 C CB  . PHE D 190 ? 0.75605 0.88825 0.87428 0.00102  0.10926  -0.11429 190 PHE D CB  
5306 C CG  . PHE D 190 ? 0.77688 0.87531 0.83730 -0.01027 0.09412  -0.10123 190 PHE D CG  
5307 C CD1 . PHE D 190 ? 0.74169 0.85334 0.82295 -0.02452 0.07693  -0.08940 190 PHE D CD1 
5308 C CD2 . PHE D 190 ? 0.81646 0.86946 0.80200 -0.00616 0.09639  -0.10078 190 PHE D CD2 
5309 C CE1 . PHE D 190 ? 0.73037 0.81445 0.76929 -0.03050 0.06475  -0.07621 190 PHE D CE1 
5310 C CE2 . PHE D 190 ? 0.83163 0.85995 0.77310 -0.01433 0.07818  -0.08557 190 PHE D CE2 
5311 C CZ  . PHE D 190 ? 0.77927 0.82520 0.75290 -0.02452 0.06349  -0.07269 190 PHE D CZ  
5312 N N   . ARG D 191 ? 0.81225 0.93486 0.89403 -0.03045 0.18392  -0.09634 191 ARG D N   
5313 C CA  . ARG D 191 ? 0.87162 0.95830 0.89259 -0.03753 0.21521  -0.08778 191 ARG D CA  
5314 C C   . ARG D 191 ? 0.89435 0.93265 0.84162 -0.03821 0.19000  -0.07275 191 ARG D C   
5315 O O   . ARG D 191 ? 0.95389 0.95133 0.82775 -0.03187 0.19416  -0.07206 191 ARG D O   
5316 C CB  . ARG D 191 ? 0.93312 1.04234 0.99341 -0.05818 0.24445  -0.08018 191 ARG D CB  
5317 C CG  . ARG D 191 ? 0.97019 1.12624 1.09527 -0.05986 0.28071  -0.09259 191 ARG D CG  
5318 C CD  . ARG D 191 ? 0.99027 1.12363 1.07019 -0.04823 0.32039  -0.10084 191 ARG D CD  
5319 N NE  . ARG D 191 ? 1.03733 1.22402 1.19433 -0.04492 0.35549  -0.11416 191 ARG D NE  
5320 C CZ  . ARG D 191 ? 1.20738 1.40187 1.37576 -0.02200 0.37144  -0.13096 191 ARG D CZ  
5321 N NH1 . ARG D 191 ? 1.34771 1.49456 1.44787 -0.00330 0.35533  -0.13870 191 ARG D NH1 
5322 N NH2 . ARG D 191 ? 1.12240 1.37338 1.37517 -0.01812 0.40530  -0.14071 191 ARG D NH2 
5323 N N   . LEU D 192 ? 0.85419 0.89636 0.81930 -0.04575 0.16378  -0.06084 192 LEU D N   
5324 C CA  . LEU D 192 ? 0.87533 0.87967 0.78547 -0.04441 0.14090  -0.04374 192 LEU D CA  
5325 C C   . LEU D 192 ? 0.81868 0.83953 0.77037 -0.04833 0.11244  -0.03769 192 LEU D C   
5326 O O   . LEU D 192 ? 0.81365 0.86840 0.82430 -0.05546 0.11200  -0.04619 192 LEU D O   
5327 C CB  . LEU D 192 ? 1.04285 1.01153 0.90332 -0.05195 0.16728  -0.02601 192 LEU D CB  
5328 C CG  . LEU D 192 ? 1.02753 0.99770 0.91940 -0.06634 0.18213  -0.01331 192 LEU D CG  
5329 C CD1 . LEU D 192 ? 1.04624 0.96561 0.87263 -0.06865 0.19528  0.01064  192 LEU D CD1 
5330 C CD2 . LEU D 192 ? 0.91969 0.92583 0.86953 -0.08038 0.21481  -0.02635 192 LEU D CD2 
5331 N N   . GLU D 193 ? 0.90347 0.89973 0.82270 -0.04434 0.08995  -0.02197 193 GLU D N   
5332 C CA  . GLU D 193 ? 0.82482 0.83257 0.77665 -0.04483 0.06453  -0.01630 193 GLU D CA  
5333 C C   . GLU D 193 ? 0.90070 0.87993 0.82898 -0.04257 0.06315  0.00662  193 GLU D C   
5334 O O   . GLU D 193 ? 0.93306 0.88214 0.80698 -0.03699 0.06312  0.02039  193 GLU D O   
5335 C CB  . GLU D 193 ? 0.76750 0.78384 0.71748 -0.03715 0.02999  -0.02292 193 GLU D CB  
5336 C CG  . GLU D 193 ? 0.93925 0.95890 0.90292 -0.03517 0.00251  -0.01161 193 GLU D CG  
5337 C CD  . GLU D 193 ? 1.22411 1.24188 1.16708 -0.03033 -0.02995 -0.01394 193 GLU D CD  
5338 O OE1 . GLU D 193 ? 1.08633 1.08138 0.97770 -0.02686 -0.03335 -0.01488 193 GLU D OE1 
5339 O OE2 . GLU D 193 ? 1.17010 1.20593 1.14423 -0.03252 -0.05069 -0.01546 193 GLU D OE2 
5340 N N   . VAL D 194 ? 0.78804 0.77303 0.75430 -0.04672 0.06384  0.01095  194 VAL D N   
5341 C CA  . VAL D 194 ? 0.94690 0.90499 0.90320 -0.04022 0.06280  0.03294  194 VAL D CA  
5342 C C   . VAL D 194 ? 0.82009 0.79636 0.81595 -0.03515 0.04157  0.03293  194 VAL D C   
5343 O O   . VAL D 194 ? 0.78128 0.78114 0.81386 -0.04437 0.04256  0.01631  194 VAL D O   
5344 C CB  . VAL D 194 ? 0.84080 0.77426 0.79995 -0.05072 0.09745  0.03876  194 VAL D CB  
5345 C CG1 . VAL D 194 ? 0.79849 0.75360 0.80745 -0.06710 0.11010  0.01981  194 VAL D CG1 
5346 C CG2 . VAL D 194 ? 0.88082 0.77761 0.82523 -0.03898 0.09634  0.06458  194 VAL D CG2 
5347 N N   . ILE D 195 ? 0.85267 0.81939 0.84136 -0.02093 0.02227  0.05260  195 ILE D N   
5348 C CA  . ILE D 195 ? 0.85850 0.84743 0.88789 -0.01447 0.00299  0.05433  195 ILE D CA  
5349 C C   . ILE D 195 ? 0.87446 0.84364 0.92669 -0.00545 0.01859  0.06947  195 ILE D C   
5350 O O   . ILE D 195 ? 0.93654 0.87549 0.96514 0.00557  0.02212  0.09153  195 ILE D O   
5351 C CB  . ILE D 195 ? 0.97639 0.97948 0.99401 -0.00546 -0.03422 0.06402  195 ILE D CB  
5352 C CG1 . ILE D 195 ? 0.97950 0.99811 0.98181 -0.01519 -0.04743 0.04388  195 ILE D CG1 
5353 C CG2 . ILE D 195 ? 0.80348 0.83125 0.87166 0.00201  -0.04921 0.07129  195 ILE D CG2 
5354 C CD1 . ILE D 195 ? 1.35424 1.36522 1.31180 -0.01173 -0.07617 0.05049  195 ILE D CD1 
5355 N N   . SER D 196 ? 0.74597 0.72694 0.83960 -0.00984 0.02933  0.05784  196 SER D N   
5356 C CA  . SER D 196 ? 0.90039 0.85734 1.01727 -0.00177 0.05106  0.06616  196 SER D CA  
5357 C C   . SER D 196 ? 0.94910 0.91843 1.09681 0.02125  0.03290  0.08685  196 SER D C   
5358 O O   . SER D 196 ? 0.88362 0.88559 1.03884 0.02592  0.00164  0.09211  196 SER D O   
5359 C CB  . SER D 196 ? 0.86915 0.82943 1.00969 -0.01824 0.07240  0.04218  196 SER D CB  
5360 O OG  . SER D 196 ? 0.75751 0.74940 0.92990 -0.01581 0.05983  0.03609  196 SER D OG  
5361 N N   . ASN D 197 ? 0.92644 0.86863 1.09546 0.03548  0.05331  0.09879  197 ASN D N   
5362 C CA  . ASN D 197 ? 0.91339 0.87249 1.12927 0.05986  0.04203  0.11754  197 ASN D CA  
5363 C C   . ASN D 197 ? 0.90956 0.90755 1.17025 0.05322  0.04466  0.09868  197 ASN D C   
5364 O O   . ASN D 197 ? 0.86581 0.86129 1.11735 0.03185  0.06299  0.07251  197 ASN D O   
5365 C CB  . ASN D 197 ? 1.01212 0.92602 1.24286 0.07930  0.06949  0.13325  197 ASN D CB  
5366 C CG  . ASN D 197 ? 0.94276 0.81575 1.13052 0.08961  0.06369  0.16033  197 ASN D CG  
5367 O OD1 . ASN D 197 ? 1.14102 1.02913 1.30450 0.09521  0.02962  0.17870  197 ASN D OD1 
5368 N ND2 . ASN D 197 ? 1.00672 0.82236 1.18000 0.09066  0.09739  0.16347  197 ASN D ND2 
5369 N N   . PRO D 198 ? 1.00421 1.04101 1.31209 0.06883  0.02422  0.11254  198 PRO D N   
5370 C CA  . PRO D 198 ? 0.81332 0.88615 1.16431 0.06109  0.03142  0.09643  198 PRO D CA  
5371 C C   . PRO D 198 ? 0.76227 0.80604 1.13064 0.06233  0.07736  0.08195  198 PRO D C   
5372 O O   . PRO D 198 ? 0.97099 0.97819 1.34797 0.08115  0.09891  0.09320  198 PRO D O   
5373 C CB  . PRO D 198 ? 0.74290 0.86160 1.15041 0.08068  0.00370  0.11980  198 PRO D CB  
5374 C CG  . PRO D 198 ? 0.82160 0.93184 1.20082 0.09285  -0.02960 0.14543  198 PRO D CG  
5375 C CD  . PRO D 198 ? 0.85509 0.90611 1.18025 0.09261  -0.00709 0.14508  198 PRO D CD  
5376 N N   . PHE D 199 ? 0.82059 0.87432 1.18726 0.04101  0.09253  0.05666  199 PHE D N   
5377 C CA  . PHE D 199 ? 0.80579 0.83118 1.18035 0.03747  0.13616  0.03855  199 PHE D CA  
5378 C C   . PHE D 199 ? 0.89014 0.95292 1.29534 0.02850  0.14238  0.02718  199 PHE D C   
5379 O O   . PHE D 199 ? 0.82523 0.92530 1.22744 0.01448  0.11414  0.02623  199 PHE D O   
5380 C CB  . PHE D 199 ? 0.98174 0.96277 1.29920 0.01179  0.15469  0.01535  199 PHE D CB  
5381 C CG  . PHE D 199 ? 0.85901 0.86037 1.14497 -0.01819 0.13919  -0.00401 199 PHE D CG  
5382 C CD1 . PHE D 199 ? 0.83947 0.86702 1.10917 -0.02388 0.10330  0.00224  199 PHE D CD1 
5383 C CD2 . PHE D 199 ? 0.91018 0.89885 1.17812 -0.04032 0.16106  -0.02831 199 PHE D CD2 
5384 C CE1 . PHE D 199 ? 0.82067 0.86367 1.06585 -0.04744 0.08923  -0.01355 199 PHE D CE1 
5385 C CE2 . PHE D 199 ? 0.77662 0.78205 1.01517 -0.06607 0.14320  -0.04217 199 PHE D CE2 
5386 C CZ  . PHE D 199 ? 0.72584 0.75917 0.95718 -0.06789 0.10719  -0.03390 199 PHE D CZ  
5387 N N   . ILE D 200 ? 0.93020 0.97813 1.36287 0.03645  0.18267  0.01846  200 ILE D N   
5388 C CA  . ILE D 200 ? 0.92177 1.00470 1.39342 0.03292  0.19785  0.01159  200 ILE D CA  
5389 C C   . ILE D 200 ? 0.87125 0.92059 1.29275 0.00384  0.22965  -0.01959 200 ILE D C   
5390 O O   . ILE D 200 ? 0.83616 0.83134 1.22613 0.00079  0.26095  -0.03482 200 ILE D O   
5391 C CB  . ILE D 200 ? 0.94061 1.03612 1.48851 0.06731  0.22372  0.02632  200 ILE D CB  
5392 C CG1 . ILE D 200 ? 0.88413 1.03552 1.49207 0.09011  0.18219  0.05879  200 ILE D CG1 
5393 C CG2 . ILE D 200 ? 0.85599 0.96530 1.43184 0.06025  0.26398  0.00933  200 ILE D CG2 
5394 C CD1 . ILE D 200 ? 0.82573 1.03931 1.45990 0.07301  0.15592  0.06054  200 ILE D CD1 
5395 N N   . VAL D 201 ? 0.85250 0.92947 1.26053 -0.01991 0.21926  -0.02851 201 VAL D N   
5396 C CA  . VAL D 201 ? 0.88701 0.93551 1.24404 -0.04895 0.24556  -0.05493 201 VAL D CA  
5397 C C   . VAL D 201 ? 0.88489 0.95244 1.28155 -0.04555 0.28101  -0.05846 201 VAL D C   
5398 O O   . VAL D 201 ? 0.81434 0.93421 1.25715 -0.04286 0.26509  -0.04423 201 VAL D O   
5399 C CB  . VAL D 201 ? 0.81574 0.87503 1.12274 -0.07857 0.20974  -0.06042 201 VAL D CB  
5400 C CG1 . VAL D 201 ? 0.83381 0.86954 1.08928 -0.10871 0.23167  -0.08250 201 VAL D CG1 
5401 C CG2 . VAL D 201 ? 0.74133 0.78240 1.01310 -0.08234 0.18311  -0.06010 201 VAL D CG2 
5402 N N   . TYR D 202 ? 0.86083 0.88495 1.24050 -0.04685 0.33141  -0.07824 202 TYR D N   
5403 C CA  . TYR D 202 ? 0.93195 0.96960 1.35032 -0.04136 0.37594  -0.08391 202 TYR D CA  
5404 C C   . TYR D 202 ? 0.94468 0.95717 1.29037 -0.07984 0.39577  -0.10805 202 TYR D C   
5405 O O   . TYR D 202 ? 0.95900 0.93377 1.22524 -0.10710 0.38057  -0.12281 202 TYR D O   
5406 C CB  . TYR D 202 ? 0.90714 0.90968 1.36082 -0.01125 0.42603  -0.08928 202 TYR D CB  
5407 C CG  . TYR D 202 ? 0.97942 0.90069 1.35814 -0.02413 0.45142  -0.11478 202 TYR D CG  
5408 C CD1 . TYR D 202 ? 1.02845 0.90375 1.33228 -0.05684 0.48448  -0.14609 202 TYR D CD1 
5409 C CD2 . TYR D 202 ? 1.03983 0.92764 1.41745 -0.00722 0.44091  -0.10723 202 TYR D CD2 
5410 C CE1 . TYR D 202 ? 1.13871 0.93954 1.37204 -0.07346 0.50400  -0.17093 202 TYR D CE1 
5411 C CE2 . TYR D 202 ? 1.20731 1.02016 1.51825 -0.02365 0.46347  -0.13112 202 TYR D CE2 
5412 C CZ  . TYR D 202 ? 1.25353 1.02429 1.49387 -0.05746 0.49367  -0.16387 202 TYR D CZ  
5413 O OH  . TYR D 202 ? 1.24233 0.93780 1.41444 -0.07826 0.51323  -0.18933 202 TYR D OH  
5414 N N   . SER D 203 ? 1.25101 0.94244 1.58097 0.30010  0.40843  0.26886  203 SER D N   
5415 C CA  . SER D 203 ? 1.26787 0.93951 1.52480 0.28961  0.40852  0.26866  203 SER D CA  
5416 C C   . SER D 203 ? 1.30949 0.98395 1.54606 0.28005  0.38198  0.21928  203 SER D C   
5417 O O   . SER D 203 ? 1.15823 0.84483 1.40267 0.27702  0.39380  0.17124  203 SER D O   
5418 C CB  . SER D 203 ? 1.27661 0.92598 1.46612 0.28098  0.46765  0.26248  203 SER D CB  
5419 O OG  . SER D 203 ? 1.55755 1.17570 1.67736 0.28229  0.47198  0.29229  203 SER D OG  
5420 N N   . ALA D 204 ? 1.38471 1.05099 1.59500 0.27732  0.34547  0.23019  204 ALA D N   
5421 C CA  . ALA D 204 ? 1.31861 0.98015 1.49753 0.26709  0.32088  0.18522  204 ALA D CA  
5422 C C   . ALA D 204 ? 1.42115 1.05745 1.50835 0.25807  0.35818  0.15885  204 ALA D C   
5423 O O   . ALA D 204 ? 1.49041 1.10378 1.51745 0.26111  0.37164  0.18804  204 ALA D O   
5424 C CB  . ALA D 204 ? 1.27682 0.94320 1.46482 0.26595  0.26552  0.20363  204 ALA D CB  
5425 N N   . LYS D 205 ? 1.25557 0.89419 1.32983 0.24939  0.37791  0.10413  205 LYS D N   
5426 C CA  . LYS D 205 ? 1.27925 0.89298 1.27083 0.23761  0.42030  0.07340  205 LYS D CA  
5427 C C   . LYS D 205 ? 1.36129 0.94318 1.27722 0.23618  0.39641  0.07833  205 LYS D C   
5428 O O   . LYS D 205 ? 1.41965 1.00852 1.35202 0.23844  0.34308  0.07923  205 LYS D O   
5429 C CB  . LYS D 205 ? 1.26646 0.89891 1.26865 0.22989  0.43950  0.01023  205 LYS D CB  
5430 C CG  . LYS D 205 ? 1.26508 0.93244 1.32162 0.23211  0.47437  -0.00299 205 LYS D CG  
5431 C CD  . LYS D 205 ? 1.38844 1.08487 1.45310 0.22807  0.49298  -0.06883 205 LYS D CD  
5432 C CE  . LYS D 205 ? 1.27630 1.00844 1.41680 0.24855  0.45993  -0.08110 205 LYS D CE  
5433 N NZ  . LYS D 205 ? 1.39665 1.17138 1.59089 0.25854  0.48536  -0.08735 205 LYS D NZ  
5434 N N   . LYS D 206 ? 1.69444 1.23817 1.52272 0.23249  0.43863  0.08025  206 LYS D N   
5435 C CA  . LYS D 206 ? 1.76429 1.27154 1.50451 0.23755  0.42191  0.08956  206 LYS D CA  
5436 C C   . LYS D 206 ? 1.67934 1.16481 1.36175 0.22445  0.43508  0.03271  206 LYS D C   
5437 O O   . LYS D 206 ? 1.72764 1.19848 1.38069 0.21164  0.49252  -0.00025 206 LYS D O   
5438 C CB  . LYS D 206 ? 1.72654 1.19146 1.39025 0.24803  0.46359  0.13087  206 LYS D CB  
5439 C CG  . LYS D 206 ? 1.98430 1.43561 1.64644 0.23690  0.53624  0.12544  206 LYS D CG  
5440 C CD  . LYS D 206 ? 2.20422 1.59027 1.75906 0.24409  0.58990  0.15373  206 LYS D CD  
5441 C CE  . LYS D 206 ? 2.02643 1.36216 1.47514 0.23909  0.61014  0.12105  206 LYS D CE  
5442 N NZ  . LYS D 206 ? 2.28446 1.55127 1.61629 0.26045  0.63769  0.16198  206 LYS D NZ  
5443 N N   . PHE D 207 ? 1.60573 1.09122 1.27529 0.22585  0.38312  0.01889  207 PHE D N   
5444 C CA  . PHE D 207 ? 1.79070 1.24891 1.39562 0.21628  0.38939  -0.03082 207 PHE D CA  
5445 C C   . PHE D 207 ? 1.92100 1.34081 1.43020 0.22743  0.36624  -0.01046 207 PHE D C   
5446 O O   . PHE D 207 ? 1.99220 1.42965 1.51743 0.23314  0.30345  0.00052  207 PHE D O   
5447 C CB  . PHE D 207 ? 1.63547 1.12170 1.30176 0.20985  0.34895  -0.06865 207 PHE D CB  
5448 C CG  . PHE D 207 ? 1.54514 1.07145 1.30239 0.20803  0.36591  -0.08580 207 PHE D CG  
5449 C CD1 . PHE D 207 ? 1.53763 1.07033 1.28982 0.20039  0.41466  -0.13157 207 PHE D CD1 
5450 C CD2 . PHE D 207 ? 1.47205 1.03198 1.31871 0.21589  0.33474  -0.05675 207 PHE D CD2 
5451 C CE1 . PHE D 207 ? 1.45920 1.03675 1.29248 0.20421  0.42684  -0.14915 207 PHE D CE1 
5452 C CE2 . PHE D 207 ? 1.39776 0.99110 1.31886 0.22015  0.35012  -0.07142 207 PHE D CE2 
5453 C CZ  . PHE D 207 ? 1.39139 0.99633 1.30496 0.21614  0.39399  -0.11783 207 PHE D CZ  
5454 N N   . PRO D 208 ? 2.04112 1.40780 1.44724 0.23158  0.41620  -0.00631 208 PRO D N   
5455 C CA  . PRO D 208 ? 2.18940 1.51811 1.49688 0.25267  0.39694  0.02472  208 PRO D CA  
5456 C C   . PRO D 208 ? 2.13911 1.47065 1.41794 0.25482  0.33440  0.00331  208 PRO D C   
5457 O O   . PRO D 208 ? 2.22263 1.57908 1.50868 0.26988  0.27639  0.03269  208 PRO D O   
5458 C CB  . PRO D 208 ? 2.38699 1.64429 1.58117 0.25231  0.47435  0.01528  208 PRO D CB  
5459 C CG  . PRO D 208 ? 2.25533 1.52331 1.49693 0.22457  0.52780  -0.03167 208 PRO D CG  
5460 C CD  . PRO D 208 ? 1.96577 1.30523 1.34218 0.21828  0.49635  -0.02846 208 PRO D CD  
5461 N N   . GLY D 209 ? 2.03177 1.34148 1.27979 0.23940  0.34543  -0.04960 209 GLY D N   
5462 C CA  . GLY D 209 ? 2.09048 1.39583 1.30328 0.23971  0.28926  -0.07259 209 GLY D CA  
5463 C C   . GLY D 209 ? 2.02051 1.37999 1.33854 0.22749  0.22767  -0.08552 209 GLY D C   
5464 O O   . GLY D 209 ? 2.06990 1.42852 1.36490 0.22441  0.17742  -0.10464 209 GLY D O   
5465 N N   . LEU D 210 ? 1.91444 1.31613 1.34240 0.22048  0.23272  -0.07642 210 LEU D N   
5466 C CA  . LEU D 210 ? 1.85164 1.29256 1.37756 0.20905  0.18728  -0.09102 210 LEU D CA  
5467 C C   . LEU D 210 ? 1.86233 1.34710 1.45783 0.21418  0.13728  -0.04791 210 LEU D C   
5468 O O   . LEU D 210 ? 1.82978 1.33168 1.44814 0.20599  0.08209  -0.05731 210 LEU D O   
5469 C CB  . LEU D 210 ? 1.76954 1.22749 1.36970 0.20241  0.22521  -0.11154 210 LEU D CB  
5470 C CG  . LEU D 210 ? 1.72500 1.20111 1.39933 0.19421  0.19745  -0.14197 210 LEU D CG  
5471 C CD1 . LEU D 210 ? 1.80233 1.24521 1.41572 0.18547  0.18017  -0.18798 210 LEU D CD1 
5472 C CD2 . LEU D 210 ? 1.65005 1.14651 1.38433 0.19737  0.23974  -0.15821 210 LEU D CD2 
5473 N N   . THR D 211 ? 1.89250 1.39622 1.52374 0.22578  0.15808  -0.00271 211 THR D N   
5474 C CA  . THR D 211 ? 1.83942 1.38747 1.53855 0.23248  0.11549  0.04059  211 THR D CA  
5475 C C   . THR D 211 ? 2.13616 1.68902 1.76882 0.24834  0.07907  0.06518  211 THR D C   
5476 O O   . THR D 211 ? 2.05261 1.65172 1.73904 0.24866  0.02620  0.08331  211 THR D O   
5477 C CB  . THR D 211 ? 1.77981 1.34298 1.53424 0.24198  0.15237  0.08109  211 THR D CB  
5478 O OG1 . THR D 211 ? 1.88920 1.41306 1.56462 0.25100  0.21222  0.08760  211 THR D OG1 
5479 C CG2 . THR D 211 ? 1.55934 1.13852 1.40596 0.23038  0.16519  0.06193  211 THR D CG2 
5480 N N   . THR D 212 ? 2.33751 1.84483 1.85353 0.26297  0.10767  0.06492  212 THR D N   
5481 C CA  . THR D 212 ? 2.38024 1.88575 1.81268 0.28692  0.07642  0.08750  212 THR D CA  
5482 C C   . THR D 212 ? 2.33707 1.88896 1.81452 0.30939  0.05600  0.14553  212 THR D C   
5483 O O   . THR D 212 ? 2.34713 1.87801 1.74681 0.34054  0.07543  0.18265  212 THR D O   
5484 C CB  . THR D 212 ? 2.38696 1.91055 1.80573 0.27598  0.01117  0.05174  212 THR D CB  
5485 O OG1 . THR D 212 ? 2.17873 1.65302 1.54379 0.25890  0.03204  -0.00060 212 THR D OG1 
5486 C CG2 . THR D 212 ? 2.35782 1.88879 1.68825 0.30604  -0.02487 0.07395  212 THR D CG2 
# 
