data_9FC2
# 
_entry.id   9FC2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FC2         pdb_00009fc2 10.2210/pdb9fc2/pdb 
WWPDB D_1292133195 ?            ?                   
# 
_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       2025-06-11 
_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                        9FC2 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_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              jcasasnovas@cnb.csic.es 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Casasnovas 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2873-6410 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Casasnovas, J.M.' 1 0000-0002-2873-6410 
'Fernandez, L.A.'  2 0000-0001-5920-0638 
'Silva, K.'        3 ?                   
# 
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 
? ? ? ? ? ? ? US ? ? primary Mabs            ? ? 1942-0870 ? ? 17 ? 2499595 2499595 
;Integrating immune library probing with structure-based computational design to develop potent neutralizing nanobodies against emerging SARS-CoV-2 variants.
;
2025 ? 10.1080/19420862.2025.2499595 40329514 ? ? 
? ? ? ? ? ? ? CH ? ? 1       'Front Immunol' ? ? 1664-3224 ? ? 13 ? 863831  ?       
;Nanobodies Protecting From Lethal SARS-CoV-2 Infection Target Receptor Binding Epitopes Preserved in Virus Variants Other Than Omicron.
;
2022 ? 10.1038/s41586-021-04017-w    35547740 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cerdan, L.'           1  0000-0003-4938-5848 
primary 'Silva, K.'            2  ?                   
primary 'Rodriguez-Martin, D.' 3  0000-0002-6838-6355 
primary 'Perez, P.'            4  0000-0001-8983-6784 
primary 'Noriega, M.A.'        5  ?                   
primary 'Esteban Martin, A.'   6  ?                   
primary 'Gutierrez-Adan, A.'   7  ?                   
primary 'Margolles, Y.'        8  0000-0003-1413-060X 
primary 'Corbera, J.A.'        9  ?                   
primary 'Martin-Acebes, M.A.'  10 ?                   
primary 'Garcia-Arriaza, J.'   11 0000-0002-5167-5724 
primary 'Fernandez-Recio, J.'  12 0000-0002-3986-7686 
primary 'Fernandez, L.A.'      13 0000-0001-5920-0638 
primary 'Casasnovas, J.M.'     14 0000-0002-2873-6410 
1       'Casasnovas, J.M.'     15 ?                   
1       'Margolles, Y.'        16 ?                   
1       'Noriega, M.A.'        17 ?                   
1       'Guzman, M.'           18 ?                   
1       'Arranz, R.'           19 ?                   
1       'Melero, R.'           20 ?                   
1       'Casanova, M.'         21 ?                   
1       'Corbera, J.A.'        22 ?                   
1       'Jimenez-de-Oya, N.'   23 ?                   
1       'Gastaminza, P.'       24 ?                   
1       'Garaigorta, U.'       25 ?                   
1       'Saiz, J.C.'           26 ?                   
1       'Martin-Acebes, M.A.'  27 ?                   
1       'Fernandez, L.A.'      28 ?                   
# 
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 'Spike protein S1'                       23158.027 1   ? ? ? ? 
2 polymer     man 'Nanobody 4'                             13337.723 1   ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                           62.068    2   ? ? ? ? 
5 non-polymer syn 'ACETATE ION'                            59.044    1   ? ? ? ? 
6 water       nat water                                    18.015    364 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVPR
;
;GSITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVPR
;
A ? 
2 'polypeptide(L)' no no 
;QVQLVESGGGSVQAGGSLRLSCAASGDTGRTCNLVWYRQAPGKELEFVSSISDGSTNYAGSVKGRFTISQDNAKNTVYLQ
MNSLKPEDTAVYYCAATISRTGSLWCEEYWGQGTQVTVSSALVPR
;
;QVQLVESGGGSVQAGGSLRLSCAASGDTGRTCNLVWYRQAPGKELEFVSSISDGSTNYAGSVKGRFTISQDNAKNTVYLQ
MNSLKPEDTAVYYCAATISRTGSLWCEEYWGQGTQVTVSSALVPR
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
4 1,2-ETHANEDIOL                           EDO 
5 'ACETATE ION'                            ACT 
6 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ILE n 
1 4   THR n 
1 5   ASN n 
1 6   LEU n 
1 7   CYS n 
1 8   PRO n 
1 9   PHE n 
1 10  GLY n 
1 11  GLU n 
1 12  VAL n 
1 13  PHE n 
1 14  ASN n 
1 15  ALA n 
1 16  THR n 
1 17  ARG n 
1 18  PHE n 
1 19  ALA n 
1 20  SER n 
1 21  VAL n 
1 22  TYR n 
1 23  ALA n 
1 24  TRP n 
1 25  ASN n 
1 26  ARG n 
1 27  LYS n 
1 28  ARG n 
1 29  ILE n 
1 30  SER n 
1 31  ASN n 
1 32  CYS n 
1 33  VAL n 
1 34  ALA n 
1 35  ASP n 
1 36  TYR n 
1 37  SER n 
1 38  VAL n 
1 39  LEU n 
1 40  TYR n 
1 41  ASN n 
1 42  SER n 
1 43  ALA n 
1 44  SER n 
1 45  PHE n 
1 46  SER n 
1 47  THR n 
1 48  PHE n 
1 49  LYS n 
1 50  CYS n 
1 51  TYR n 
1 52  GLY n 
1 53  VAL n 
1 54  SER n 
1 55  PRO n 
1 56  THR n 
1 57  LYS n 
1 58  LEU n 
1 59  ASN n 
1 60  ASP n 
1 61  LEU n 
1 62  CYS n 
1 63  PHE n 
1 64  THR n 
1 65  ASN n 
1 66  VAL n 
1 67  TYR n 
1 68  ALA n 
1 69  ASP n 
1 70  SER n 
1 71  PHE n 
1 72  VAL n 
1 73  ILE n 
1 74  ARG n 
1 75  GLY n 
1 76  ASP n 
1 77  GLU n 
1 78  VAL n 
1 79  ARG n 
1 80  GLN n 
1 81  ILE n 
1 82  ALA n 
1 83  PRO n 
1 84  GLY n 
1 85  GLN n 
1 86  THR n 
1 87  GLY n 
1 88  LYS n 
1 89  ILE n 
1 90  ALA n 
1 91  ASP n 
1 92  TYR n 
1 93  ASN n 
1 94  TYR n 
1 95  LYS n 
1 96  LEU n 
1 97  PRO n 
1 98  ASP n 
1 99  ASP n 
1 100 PHE n 
1 101 THR n 
1 102 GLY n 
1 103 CYS n 
1 104 VAL n 
1 105 ILE n 
1 106 ALA n 
1 107 TRP n 
1 108 ASN n 
1 109 SER n 
1 110 ASN n 
1 111 ASN n 
1 112 LEU n 
1 113 ASP n 
1 114 SER n 
1 115 LYS n 
1 116 VAL n 
1 117 GLY n 
1 118 GLY n 
1 119 ASN n 
1 120 TYR n 
1 121 ASN n 
1 122 TYR n 
1 123 LEU n 
1 124 TYR n 
1 125 ARG n 
1 126 LEU n 
1 127 PHE n 
1 128 ARG n 
1 129 LYS n 
1 130 SER n 
1 131 ASN n 
1 132 LEU n 
1 133 LYS n 
1 134 PRO n 
1 135 PHE n 
1 136 GLU n 
1 137 ARG n 
1 138 ASP n 
1 139 ILE n 
1 140 SER n 
1 141 THR n 
1 142 GLU n 
1 143 ILE n 
1 144 TYR n 
1 145 GLN n 
1 146 ALA n 
1 147 GLY n 
1 148 SER n 
1 149 THR n 
1 150 PRO n 
1 151 CYS n 
1 152 ASN n 
1 153 GLY n 
1 154 VAL n 
1 155 GLU n 
1 156 GLY n 
1 157 PHE n 
1 158 ASN n 
1 159 CYS n 
1 160 TYR n 
1 161 PHE n 
1 162 PRO n 
1 163 LEU n 
1 164 GLN n 
1 165 SER n 
1 166 TYR n 
1 167 GLY n 
1 168 PHE n 
1 169 GLN n 
1 170 PRO n 
1 171 THR n 
1 172 ASN n 
1 173 GLY n 
1 174 VAL n 
1 175 GLY n 
1 176 TYR n 
1 177 GLN n 
1 178 PRO n 
1 179 TYR n 
1 180 ARG n 
1 181 VAL n 
1 182 VAL n 
1 183 VAL n 
1 184 LEU n 
1 185 SER n 
1 186 PHE n 
1 187 GLU n 
1 188 LEU n 
1 189 LEU n 
1 190 HIS n 
1 191 ALA n 
1 192 PRO n 
1 193 ALA n 
1 194 THR n 
1 195 VAL n 
1 196 CYS n 
1 197 GLY n 
1 198 PRO n 
1 199 LYS n 
1 200 LYS n 
1 201 SER n 
1 202 THR n 
1 203 ASN n 
1 204 LEU n 
1 205 VAL n 
1 206 PRO n 
1 207 ARG n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  SER n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  ASP n 
2 28  THR n 
2 29  GLY n 
2 30  ARG n 
2 31  THR n 
2 32  CYS n 
2 33  ASN n 
2 34  LEU n 
2 35  VAL n 
2 36  TRP n 
2 37  TYR n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLU n 
2 45  LEU n 
2 46  GLU n 
2 47  PHE n 
2 48  VAL n 
2 49  SER n 
2 50  SER n 
2 51  ILE n 
2 52  SER n 
2 53  ASP n 
2 54  GLY n 
2 55  SER n 
2 56  THR n 
2 57  ASN n 
2 58  TYR n 
2 59  ALA n 
2 60  GLY n 
2 61  SER n 
2 62  VAL n 
2 63  LYS n 
2 64  GLY n 
2 65  ARG n 
2 66  PHE n 
2 67  THR n 
2 68  ILE n 
2 69  SER n 
2 70  GLN n 
2 71  ASP n 
2 72  ASN n 
2 73  ALA n 
2 74  LYS n 
2 75  ASN n 
2 76  THR n 
2 77  VAL n 
2 78  TYR n 
2 79  LEU n 
2 80  GLN n 
2 81  MET n 
2 82  ASN n 
2 83  SER n 
2 84  LEU n 
2 85  LYS n 
2 86  PRO n 
2 87  GLU n 
2 88  ASP n 
2 89  THR n 
2 90  ALA n 
2 91  VAL n 
2 92  TYR n 
2 93  TYR n 
2 94  CYS n 
2 95  ALA n 
2 96  ALA n 
2 97  THR n 
2 98  ILE n 
2 99  SER n 
2 100 ARG n 
2 101 THR n 
2 102 GLY n 
2 103 SER n 
2 104 LEU n 
2 105 TRP n 
2 106 CYS n 
2 107 GLU n 
2 108 GLU n 
2 109 TYR n 
2 110 TRP n 
2 111 GLY n 
2 112 GLN n 
2 113 GLY n 
2 114 THR n 
2 115 GLN n 
2 116 VAL n 
2 117 THR n 
2 118 VAL n 
2 119 SER n 
2 120 SER n 
2 121 ALA n 
2 122 LEU n 
2 123 VAL n 
2 124 PRO n 
2 125 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 207 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Cricetulus griseus' 10029 ? ? ?      ? Ovary  ? ? ? 'CHO Lec. 3.2.8.1' ?        ? Epithelial ? ? plasmid ? ? ? pBJ5-GS ? ? 
2 1 sample 'Biological sequence' 1 125 ? ? ?      ? ? ? ? ? ? 'Camelus dromedarius'                             9838    ? ? ? ? ? 
? ? ? 'Homo sapiens'       9606  ? ? kidney ? Embryo ? ? ? HEK293F            CRL-1573 ? epithelial ? ? plasmid ? ? ? 
Flag-MCS-pcDNA3.1 ? ? 
# 
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 
ACT non-polymer                  . 'ACETATE ION'                            ? 'C2 H3 O2 -1'    59.044  
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 
EDO non-polymer                  . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   GLY 1   330 ?   ?   ?   A . n 
A 1 2   SER 2   331 ?   ?   ?   A . n 
A 1 3   ILE 3   332 ?   ?   ?   A . n 
A 1 4   THR 4   333 333 THR THR A . n 
A 1 5   ASN 5   334 334 ASN ASN A . n 
A 1 6   LEU 6   335 335 LEU LEU A . n 
A 1 7   CYS 7   336 336 CYS CYS A . n 
A 1 8   PRO 8   337 337 PRO PRO A . n 
A 1 9   PHE 9   338 338 PHE PHE A . n 
A 1 10  GLY 10  339 339 GLY GLY A . n 
A 1 11  GLU 11  340 340 GLU GLU A . n 
A 1 12  VAL 12  341 341 VAL VAL A . n 
A 1 13  PHE 13  342 342 PHE PHE A . n 
A 1 14  ASN 14  343 343 ASN ASN A . n 
A 1 15  ALA 15  344 344 ALA ALA A . n 
A 1 16  THR 16  345 345 THR THR A . n 
A 1 17  ARG 17  346 346 ARG ARG A . n 
A 1 18  PHE 18  347 347 PHE PHE A . n 
A 1 19  ALA 19  348 348 ALA ALA A . n 
A 1 20  SER 20  349 349 SER SER A . n 
A 1 21  VAL 21  350 350 VAL VAL A . n 
A 1 22  TYR 22  351 351 TYR TYR A . n 
A 1 23  ALA 23  352 352 ALA ALA A . n 
A 1 24  TRP 24  353 353 TRP TRP A . n 
A 1 25  ASN 25  354 354 ASN ASN A . n 
A 1 26  ARG 26  355 355 ARG ARG A . n 
A 1 27  LYS 27  356 356 LYS LYS A . n 
A 1 28  ARG 28  357 357 ARG ARG A . n 
A 1 29  ILE 29  358 358 ILE ILE A . n 
A 1 30  SER 30  359 359 SER SER A . n 
A 1 31  ASN 31  360 360 ASN ASN A . n 
A 1 32  CYS 32  361 361 CYS CYS A . n 
A 1 33  VAL 33  362 362 VAL VAL A . n 
A 1 34  ALA 34  363 363 ALA ALA A . n 
A 1 35  ASP 35  364 364 ASP ASP A . n 
A 1 36  TYR 36  365 365 TYR TYR A . n 
A 1 37  SER 37  366 366 SER SER A . n 
A 1 38  VAL 38  367 367 VAL VAL A . n 
A 1 39  LEU 39  368 368 LEU LEU A . n 
A 1 40  TYR 40  369 369 TYR TYR A . n 
A 1 41  ASN 41  370 370 ASN ASN A . n 
A 1 42  SER 42  371 371 SER SER A . n 
A 1 43  ALA 43  372 372 ALA ALA A . n 
A 1 44  SER 44  373 373 SER SER A . n 
A 1 45  PHE 45  374 374 PHE PHE A . n 
A 1 46  SER 46  375 375 SER SER A . n 
A 1 47  THR 47  376 376 THR THR A . n 
A 1 48  PHE 48  377 377 PHE PHE A . n 
A 1 49  LYS 49  378 378 LYS LYS A . n 
A 1 50  CYS 50  379 379 CYS CYS A . n 
A 1 51  TYR 51  380 380 TYR TYR A . n 
A 1 52  GLY 52  381 381 GLY GLY A . n 
A 1 53  VAL 53  382 382 VAL VAL A . n 
A 1 54  SER 54  383 383 SER SER A . n 
A 1 55  PRO 55  384 384 PRO PRO A . n 
A 1 56  THR 56  385 385 THR THR A . n 
A 1 57  LYS 57  386 386 LYS LYS A . n 
A 1 58  LEU 58  387 387 LEU LEU A . n 
A 1 59  ASN 59  388 388 ASN ASN A . n 
A 1 60  ASP 60  389 389 ASP ASP A . n 
A 1 61  LEU 61  390 390 LEU LEU A . n 
A 1 62  CYS 62  391 391 CYS CYS A . n 
A 1 63  PHE 63  392 392 PHE PHE A . n 
A 1 64  THR 64  393 393 THR THR A . n 
A 1 65  ASN 65  394 394 ASN ASN A . n 
A 1 66  VAL 66  395 395 VAL VAL A . n 
A 1 67  TYR 67  396 396 TYR TYR A . n 
A 1 68  ALA 68  397 397 ALA ALA A . n 
A 1 69  ASP 69  398 398 ASP ASP A . n 
A 1 70  SER 70  399 399 SER SER A . n 
A 1 71  PHE 71  400 400 PHE PHE A . n 
A 1 72  VAL 72  401 401 VAL VAL A . n 
A 1 73  ILE 73  402 402 ILE ILE A . n 
A 1 74  ARG 74  403 403 ARG ARG A . n 
A 1 75  GLY 75  404 404 GLY GLY A . n 
A 1 76  ASP 76  405 405 ASP ASP A . n 
A 1 77  GLU 77  406 406 GLU GLU A . n 
A 1 78  VAL 78  407 407 VAL VAL A . n 
A 1 79  ARG 79  408 408 ARG ARG A . n 
A 1 80  GLN 80  409 409 GLN GLN A . n 
A 1 81  ILE 81  410 410 ILE ILE A . n 
A 1 82  ALA 82  411 411 ALA ALA A . n 
A 1 83  PRO 83  412 412 PRO PRO A . n 
A 1 84  GLY 84  413 413 GLY GLY A . n 
A 1 85  GLN 85  414 414 GLN GLN A . n 
A 1 86  THR 86  415 415 THR THR A . n 
A 1 87  GLY 87  416 416 GLY GLY A . n 
A 1 88  LYS 88  417 417 LYS LYS A . n 
A 1 89  ILE 89  418 418 ILE ILE A . n 
A 1 90  ALA 90  419 419 ALA ALA A . n 
A 1 91  ASP 91  420 420 ASP ASP A . n 
A 1 92  TYR 92  421 421 TYR TYR A . n 
A 1 93  ASN 93  422 422 ASN ASN A . n 
A 1 94  TYR 94  423 423 TYR TYR A . n 
A 1 95  LYS 95  424 424 LYS LYS A . n 
A 1 96  LEU 96  425 425 LEU LEU A . n 
A 1 97  PRO 97  426 426 PRO PRO A . n 
A 1 98  ASP 98  427 427 ASP ASP A . n 
A 1 99  ASP 99  428 428 ASP ASP A . n 
A 1 100 PHE 100 429 429 PHE PHE A . n 
A 1 101 THR 101 430 430 THR THR A . n 
A 1 102 GLY 102 431 431 GLY GLY A . n 
A 1 103 CYS 103 432 432 CYS CYS A . n 
A 1 104 VAL 104 433 433 VAL VAL A . n 
A 1 105 ILE 105 434 434 ILE ILE A . n 
A 1 106 ALA 106 435 435 ALA ALA A . n 
A 1 107 TRP 107 436 436 TRP TRP A . n 
A 1 108 ASN 108 437 437 ASN ASN A . n 
A 1 109 SER 109 438 438 SER SER A . n 
A 1 110 ASN 110 439 439 ASN ASN A . n 
A 1 111 ASN 111 440 440 ASN ASN A . n 
A 1 112 LEU 112 441 441 LEU LEU A . n 
A 1 113 ASP 113 442 442 ASP ASP A . n 
A 1 114 SER 114 443 443 SER SER A . n 
A 1 115 LYS 115 444 444 LYS LYS A . n 
A 1 116 VAL 116 445 445 VAL VAL A . n 
A 1 117 GLY 117 446 446 GLY GLY A . n 
A 1 118 GLY 118 447 447 GLY GLY A . n 
A 1 119 ASN 119 448 448 ASN ASN A . n 
A 1 120 TYR 120 449 449 TYR TYR A . n 
A 1 121 ASN 121 450 450 ASN ASN A . n 
A 1 122 TYR 122 451 451 TYR TYR A . n 
A 1 123 LEU 123 452 452 LEU LEU A . n 
A 1 124 TYR 124 453 453 TYR TYR A . n 
A 1 125 ARG 125 454 454 ARG ARG A . n 
A 1 126 LEU 126 455 455 LEU LEU A . n 
A 1 127 PHE 127 456 456 PHE PHE A . n 
A 1 128 ARG 128 457 457 ARG ARG A . n 
A 1 129 LYS 129 458 458 LYS LYS A . n 
A 1 130 SER 130 459 459 SER SER A . n 
A 1 131 ASN 131 460 460 ASN ASN A . n 
A 1 132 LEU 132 461 461 LEU LEU A . n 
A 1 133 LYS 133 462 462 LYS LYS A . n 
A 1 134 PRO 134 463 463 PRO PRO A . n 
A 1 135 PHE 135 464 464 PHE PHE A . n 
A 1 136 GLU 136 465 465 GLU GLU A . n 
A 1 137 ARG 137 466 466 ARG ARG A . n 
A 1 138 ASP 138 467 467 ASP ASP A . n 
A 1 139 ILE 139 468 468 ILE ILE A . n 
A 1 140 SER 140 469 469 SER SER A . n 
A 1 141 THR 141 470 470 THR THR A . n 
A 1 142 GLU 142 471 471 GLU GLU A . n 
A 1 143 ILE 143 472 472 ILE ILE A . n 
A 1 144 TYR 144 473 473 TYR TYR A . n 
A 1 145 GLN 145 474 474 GLN GLN A . n 
A 1 146 ALA 146 475 475 ALA ALA A . n 
A 1 147 GLY 147 476 476 GLY GLY A . n 
A 1 148 SER 148 477 477 SER SER A . n 
A 1 149 THR 149 478 478 THR THR A . n 
A 1 150 PRO 150 479 479 PRO PRO A . n 
A 1 151 CYS 151 480 480 CYS CYS A . n 
A 1 152 ASN 152 481 481 ASN ASN A . n 
A 1 153 GLY 153 482 482 GLY GLY A . n 
A 1 154 VAL 154 483 483 VAL VAL A . n 
A 1 155 GLU 155 484 484 GLU GLU A . n 
A 1 156 GLY 156 485 485 GLY GLY A . n 
A 1 157 PHE 157 486 486 PHE PHE A . n 
A 1 158 ASN 158 487 487 ASN ASN A . n 
A 1 159 CYS 159 488 488 CYS CYS A . n 
A 1 160 TYR 160 489 489 TYR TYR A . n 
A 1 161 PHE 161 490 490 PHE PHE A . n 
A 1 162 PRO 162 491 491 PRO PRO A . n 
A 1 163 LEU 163 492 492 LEU LEU A . n 
A 1 164 GLN 164 493 493 GLN GLN A . n 
A 1 165 SER 165 494 494 SER SER A . n 
A 1 166 TYR 166 495 495 TYR TYR A . n 
A 1 167 GLY 167 496 496 GLY GLY A . n 
A 1 168 PHE 168 497 497 PHE PHE A . n 
A 1 169 GLN 169 498 498 GLN GLN A . n 
A 1 170 PRO 170 499 499 PRO PRO A . n 
A 1 171 THR 171 500 500 THR THR A . n 
A 1 172 ASN 172 501 501 ASN ASN A . n 
A 1 173 GLY 173 502 502 GLY GLY A . n 
A 1 174 VAL 174 503 503 VAL VAL A . n 
A 1 175 GLY 175 504 504 GLY GLY A . n 
A 1 176 TYR 176 505 505 TYR TYR A . n 
A 1 177 GLN 177 506 506 GLN GLN A . n 
A 1 178 PRO 178 507 507 PRO PRO A . n 
A 1 179 TYR 179 508 508 TYR TYR A . n 
A 1 180 ARG 180 509 509 ARG ARG A . n 
A 1 181 VAL 181 510 510 VAL VAL A . n 
A 1 182 VAL 182 511 511 VAL VAL A . n 
A 1 183 VAL 183 512 512 VAL VAL A . n 
A 1 184 LEU 184 513 513 LEU LEU A . n 
A 1 185 SER 185 514 514 SER SER A . n 
A 1 186 PHE 186 515 515 PHE PHE A . n 
A 1 187 GLU 187 516 516 GLU GLU A . n 
A 1 188 LEU 188 517 517 LEU LEU A . n 
A 1 189 LEU 189 518 518 LEU LEU A . n 
A 1 190 HIS 190 519 519 HIS HIS A . n 
A 1 191 ALA 191 520 520 ALA ALA A . n 
A 1 192 PRO 192 521 521 PRO PRO A . n 
A 1 193 ALA 193 522 522 ALA ALA A . n 
A 1 194 THR 194 523 523 THR THR A . n 
A 1 195 VAL 195 524 524 VAL VAL A . n 
A 1 196 CYS 196 525 525 CYS CYS A . n 
A 1 197 GLY 197 526 526 GLY GLY A . n 
A 1 198 PRO 198 527 527 PRO PRO A . n 
A 1 199 LYS 199 528 ?   ?   ?   A . n 
A 1 200 LYS 200 529 ?   ?   ?   A . n 
A 1 201 SER 201 530 ?   ?   ?   A . n 
A 1 202 THR 202 531 ?   ?   ?   A . n 
A 1 203 ASN 203 532 ?   ?   ?   A . n 
A 1 204 LEU 204 533 ?   ?   ?   A . n 
A 1 205 VAL 205 534 ?   ?   ?   A . n 
A 1 206 PRO 206 535 ?   ?   ?   A . n 
A 1 207 ARG 207 536 ?   ?   ?   A . n 
B 2 1   GLN 1   1   1   GLN GLN B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  SER 11  11  11  SER SER B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  ALA 14  14  14  ALA ALA B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  ARG 19  19  19  ARG ARG B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  ALA 23  23  23  ALA ALA B . n 
B 2 24  ALA 24  24  24  ALA ALA B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  ASP 27  27  27  ASP ASP B . n 
B 2 28  THR 28  28  28  THR THR B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ARG 30  30  30  ARG ARG B . n 
B 2 31  THR 31  31  31  THR THR B . n 
B 2 32  CYS 32  32  32  CYS CYS B . n 
B 2 33  ASN 33  33  33  ASN ASN B . n 
B 2 34  LEU 34  34  34  LEU LEU B . n 
B 2 35  VAL 35  35  35  VAL VAL B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLU 44  44  44  GLU GLU B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  PHE 47  47  47  PHE PHE B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  SER 49  49  49  SER SER B . n 
B 2 50  SER 50  50  50  SER SER B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  SER 52  52  52  SER SER B . n 
B 2 53  ASP 53  53  53  ASP ASP B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  SER 55  55  55  SER SER B . n 
B 2 56  THR 56  56  56  THR THR B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  TYR 58  58  58  TYR TYR B . n 
B 2 59  ALA 59  59  59  ALA ALA B . n 
B 2 60  GLY 60  60  60  GLY GLY B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  VAL 62  62  62  VAL VAL B . n 
B 2 63  LYS 63  63  63  LYS LYS B . n 
B 2 64  GLY 64  64  64  GLY GLY B . n 
B 2 65  ARG 65  65  65  ARG ARG B . n 
B 2 66  PHE 66  66  66  PHE PHE B . n 
B 2 67  THR 67  67  67  THR THR B . n 
B 2 68  ILE 68  68  68  ILE ILE B . n 
B 2 69  SER 69  69  69  SER SER B . n 
B 2 70  GLN 70  70  70  GLN GLN B . n 
B 2 71  ASP 71  71  71  ASP ASP B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  ALA 73  73  73  ALA ALA B . n 
B 2 74  LYS 74  74  74  LYS LYS B . n 
B 2 75  ASN 75  75  75  ASN ASN B . n 
B 2 76  THR 76  76  76  THR THR B . n 
B 2 77  VAL 77  77  77  VAL VAL B . n 
B 2 78  TYR 78  78  78  TYR TYR B . n 
B 2 79  LEU 79  79  79  LEU LEU B . n 
B 2 80  GLN 80  80  80  GLN GLN B . n 
B 2 81  MET 81  81  81  MET MET B . n 
B 2 82  ASN 82  82  82  ASN ASN B . n 
B 2 83  SER 83  83  83  SER SER B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  LYS 85  85  85  LYS LYS B . n 
B 2 86  PRO 86  86  86  PRO PRO B . n 
B 2 87  GLU 87  87  87  GLU GLU B . n 
B 2 88  ASP 88  88  88  ASP ASP B . n 
B 2 89  THR 89  89  89  THR THR B . n 
B 2 90  ALA 90  90  90  ALA ALA B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  TYR 92  92  92  TYR TYR B . n 
B 2 93  TYR 93  93  93  TYR TYR B . n 
B 2 94  CYS 94  94  94  CYS CYS B . n 
B 2 95  ALA 95  95  95  ALA ALA B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  THR 97  97  97  THR THR B . n 
B 2 98  ILE 98  98  98  ILE ILE B . n 
B 2 99  SER 99  99  99  SER SER B . n 
B 2 100 ARG 100 100 100 ARG ARG B . n 
B 2 101 THR 101 101 101 THR THR B . n 
B 2 102 GLY 102 102 102 GLY GLY B . n 
B 2 103 SER 103 103 103 SER SER B . n 
B 2 104 LEU 104 104 104 LEU LEU B . n 
B 2 105 TRP 105 105 105 TRP TRP B . n 
B 2 106 CYS 106 106 106 CYS CYS B . n 
B 2 107 GLU 107 107 107 GLU GLU B . n 
B 2 108 GLU 108 108 108 GLU GLU B . n 
B 2 109 TYR 109 109 109 TYR TYR B . n 
B 2 110 TRP 110 110 110 TRP TRP B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 GLN 112 112 112 GLN GLN B . n 
B 2 113 GLY 113 113 113 GLY GLY B . n 
B 2 114 THR 114 114 114 THR THR B . n 
B 2 115 GLN 115 115 115 GLN GLN B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 THR 117 117 117 THR THR B . n 
B 2 118 VAL 118 118 118 VAL VAL B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 SER 120 120 120 SER SER B . n 
B 2 121 ALA 121 121 ?   ?   ?   B . n 
B 2 122 LEU 122 122 ?   ?   ?   B . n 
B 2 123 VAL 123 123 ?   ?   ?   B . n 
B 2 124 PRO 124 124 ?   ?   ?   B . n 
B 2 125 ARG 125 125 ?   ?   ?   B . 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 
C 3 NAG 1   601 3430 NAG NAG A . 
D 4 EDO 1   602 3    EDO EDO A . 
E 5 ACT 1   201 1    ACT ACT B . 
F 4 EDO 1   202 2    EDO EDO B . 
G 6 HOH 1   701 323  HOH HOH A . 
G 6 HOH 2   702 356  HOH HOH A . 
G 6 HOH 3   703 93   HOH HOH A . 
G 6 HOH 4   704 337  HOH HOH A . 
G 6 HOH 5   705 392  HOH HOH A . 
G 6 HOH 6   706 266  HOH HOH A . 
G 6 HOH 7   707 248  HOH HOH A . 
G 6 HOH 8   708 251  HOH HOH A . 
G 6 HOH 9   709 196  HOH HOH A . 
G 6 HOH 10  710 393  HOH HOH A . 
G 6 HOH 11  711 296  HOH HOH A . 
G 6 HOH 12  712 121  HOH HOH A . 
G 6 HOH 13  713 85   HOH HOH A . 
G 6 HOH 14  714 31   HOH HOH A . 
G 6 HOH 15  715 83   HOH HOH A . 
G 6 HOH 16  716 319  HOH HOH A . 
G 6 HOH 17  717 220  HOH HOH A . 
G 6 HOH 18  718 252  HOH HOH A . 
G 6 HOH 19  719 46   HOH HOH A . 
G 6 HOH 20  720 376  HOH HOH A . 
G 6 HOH 21  721 287  HOH HOH A . 
G 6 HOH 22  722 133  HOH HOH A . 
G 6 HOH 23  723 225  HOH HOH A . 
G 6 HOH 24  724 52   HOH HOH A . 
G 6 HOH 25  725 77   HOH HOH A . 
G 6 HOH 26  726 34   HOH HOH A . 
G 6 HOH 27  727 155  HOH HOH A . 
G 6 HOH 28  728 45   HOH HOH A . 
G 6 HOH 29  729 69   HOH HOH A . 
G 6 HOH 30  730 378  HOH HOH A . 
G 6 HOH 31  731 15   HOH HOH A . 
G 6 HOH 32  732 99   HOH HOH A . 
G 6 HOH 33  733 12   HOH HOH A . 
G 6 HOH 34  734 181  HOH HOH A . 
G 6 HOH 35  735 112  HOH HOH A . 
G 6 HOH 36  736 9    HOH HOH A . 
G 6 HOH 37  737 2    HOH HOH A . 
G 6 HOH 38  738 82   HOH HOH A . 
G 6 HOH 39  739 291  HOH HOH A . 
G 6 HOH 40  740 237  HOH HOH A . 
G 6 HOH 41  741 49   HOH HOH A . 
G 6 HOH 42  742 147  HOH HOH A . 
G 6 HOH 43  743 60   HOH HOH A . 
G 6 HOH 44  744 131  HOH HOH A . 
G 6 HOH 45  745 199  HOH HOH A . 
G 6 HOH 46  746 365  HOH HOH A . 
G 6 HOH 47  747 3    HOH HOH A . 
G 6 HOH 48  748 161  HOH HOH A . 
G 6 HOH 49  749 139  HOH HOH A . 
G 6 HOH 50  750 341  HOH HOH A . 
G 6 HOH 51  751 79   HOH HOH A . 
G 6 HOH 52  752 16   HOH HOH A . 
G 6 HOH 53  753 30   HOH HOH A . 
G 6 HOH 54  754 65   HOH HOH A . 
G 6 HOH 55  755 317  HOH HOH A . 
G 6 HOH 56  756 145  HOH HOH A . 
G 6 HOH 57  757 320  HOH HOH A . 
G 6 HOH 58  758 115  HOH HOH A . 
G 6 HOH 59  759 135  HOH HOH A . 
G 6 HOH 60  760 95   HOH HOH A . 
G 6 HOH 61  761 24   HOH HOH A . 
G 6 HOH 62  762 307  HOH HOH A . 
G 6 HOH 63  763 40   HOH HOH A . 
G 6 HOH 64  764 26   HOH HOH A . 
G 6 HOH 65  765 391  HOH HOH A . 
G 6 HOH 66  766 105  HOH HOH A . 
G 6 HOH 67  767 23   HOH HOH A . 
G 6 HOH 68  768 8    HOH HOH A . 
G 6 HOH 69  769 47   HOH HOH A . 
G 6 HOH 70  770 81   HOH HOH A . 
G 6 HOH 71  771 43   HOH HOH A . 
G 6 HOH 72  772 20   HOH HOH A . 
G 6 HOH 73  773 275  HOH HOH A . 
G 6 HOH 74  774 163  HOH HOH A . 
G 6 HOH 75  775 194  HOH HOH A . 
G 6 HOH 76  776 182  HOH HOH A . 
G 6 HOH 77  777 116  HOH HOH A . 
G 6 HOH 78  778 7    HOH HOH A . 
G 6 HOH 79  779 35   HOH HOH A . 
G 6 HOH 80  780 257  HOH HOH A . 
G 6 HOH 81  781 113  HOH HOH A . 
G 6 HOH 82  782 216  HOH HOH A . 
G 6 HOH 83  783 353  HOH HOH A . 
G 6 HOH 84  784 108  HOH HOH A . 
G 6 HOH 85  785 114  HOH HOH A . 
G 6 HOH 86  786 37   HOH HOH A . 
G 6 HOH 87  787 244  HOH HOH A . 
G 6 HOH 88  788 6    HOH HOH A . 
G 6 HOH 89  789 17   HOH HOH A . 
G 6 HOH 90  790 185  HOH HOH A . 
G 6 HOH 91  791 44   HOH HOH A . 
G 6 HOH 92  792 11   HOH HOH A . 
G 6 HOH 93  793 137  HOH HOH A . 
G 6 HOH 94  794 21   HOH HOH A . 
G 6 HOH 95  795 5    HOH HOH A . 
G 6 HOH 96  796 119  HOH HOH A . 
G 6 HOH 97  797 55   HOH HOH A . 
G 6 HOH 98  798 51   HOH HOH A . 
G 6 HOH 99  799 146  HOH HOH A . 
G 6 HOH 100 800 107  HOH HOH A . 
G 6 HOH 101 801 96   HOH HOH A . 
G 6 HOH 102 802 103  HOH HOH A . 
G 6 HOH 103 803 193  HOH HOH A . 
G 6 HOH 104 804 14   HOH HOH A . 
G 6 HOH 105 805 176  HOH HOH A . 
G 6 HOH 106 806 231  HOH HOH A . 
G 6 HOH 107 807 369  HOH HOH A . 
G 6 HOH 108 808 329  HOH HOH A . 
G 6 HOH 109 809 245  HOH HOH A . 
G 6 HOH 110 810 190  HOH HOH A . 
G 6 HOH 111 811 18   HOH HOH A . 
G 6 HOH 112 812 169  HOH HOH A . 
G 6 HOH 113 813 100  HOH HOH A . 
G 6 HOH 114 814 62   HOH HOH A . 
G 6 HOH 115 815 159  HOH HOH A . 
G 6 HOH 116 816 27   HOH HOH A . 
G 6 HOH 117 817 10   HOH HOH A . 
G 6 HOH 118 818 123  HOH HOH A . 
G 6 HOH 119 819 278  HOH HOH A . 
G 6 HOH 120 820 281  HOH HOH A . 
G 6 HOH 121 821 56   HOH HOH A . 
G 6 HOH 122 822 89   HOH HOH A . 
G 6 HOH 123 823 267  HOH HOH A . 
G 6 HOH 124 824 269  HOH HOH A . 
G 6 HOH 125 825 282  HOH HOH A . 
G 6 HOH 126 826 128  HOH HOH A . 
G 6 HOH 127 827 272  HOH HOH A . 
G 6 HOH 128 828 92   HOH HOH A . 
G 6 HOH 129 829 226  HOH HOH A . 
G 6 HOH 130 830 242  HOH HOH A . 
G 6 HOH 131 831 75   HOH HOH A . 
G 6 HOH 132 832 109  HOH HOH A . 
G 6 HOH 133 833 380  HOH HOH A . 
G 6 HOH 134 834 86   HOH HOH A . 
G 6 HOH 135 835 28   HOH HOH A . 
G 6 HOH 136 836 351  HOH HOH A . 
G 6 HOH 137 837 138  HOH HOH A . 
G 6 HOH 138 838 304  HOH HOH A . 
G 6 HOH 139 839 57   HOH HOH A . 
G 6 HOH 140 840 70   HOH HOH A . 
G 6 HOH 141 841 63   HOH HOH A . 
G 6 HOH 142 842 286  HOH HOH A . 
G 6 HOH 143 843 200  HOH HOH A . 
G 6 HOH 144 844 377  HOH HOH A . 
G 6 HOH 145 845 187  HOH HOH A . 
G 6 HOH 146 846 68   HOH HOH A . 
G 6 HOH 147 847 268  HOH HOH A . 
G 6 HOH 148 848 168  HOH HOH A . 
G 6 HOH 149 849 201  HOH HOH A . 
G 6 HOH 150 850 271  HOH HOH A . 
G 6 HOH 151 851 74   HOH HOH A . 
G 6 HOH 152 852 32   HOH HOH A . 
G 6 HOH 153 853 212  HOH HOH A . 
G 6 HOH 154 854 259  HOH HOH A . 
G 6 HOH 155 855 274  HOH HOH A . 
G 6 HOH 156 856 215  HOH HOH A . 
G 6 HOH 157 857 67   HOH HOH A . 
G 6 HOH 158 858 247  HOH HOH A . 
G 6 HOH 159 859 171  HOH HOH A . 
G 6 HOH 160 860 330  HOH HOH A . 
G 6 HOH 161 861 294  HOH HOH A . 
G 6 HOH 162 862 167  HOH HOH A . 
G 6 HOH 163 863 209  HOH HOH A . 
G 6 HOH 164 864 339  HOH HOH A . 
G 6 HOH 165 865 210  HOH HOH A . 
G 6 HOH 166 866 142  HOH HOH A . 
G 6 HOH 167 867 213  HOH HOH A . 
G 6 HOH 168 868 309  HOH HOH A . 
G 6 HOH 169 869 264  HOH HOH A . 
G 6 HOH 170 870 270  HOH HOH A . 
G 6 HOH 171 871 308  HOH HOH A . 
G 6 HOH 172 872 295  HOH HOH A . 
G 6 HOH 173 873 202  HOH HOH A . 
G 6 HOH 174 874 283  HOH HOH A . 
G 6 HOH 175 875 273  HOH HOH A . 
G 6 HOH 176 876 358  HOH HOH A . 
G 6 HOH 177 877 357  HOH HOH A . 
G 6 HOH 178 878 149  HOH HOH A . 
G 6 HOH 179 879 243  HOH HOH A . 
G 6 HOH 180 880 284  HOH HOH A . 
G 6 HOH 181 881 208  HOH HOH A . 
G 6 HOH 182 882 223  HOH HOH A . 
G 6 HOH 183 883 261  HOH HOH A . 
G 6 HOH 184 884 315  HOH HOH A . 
G 6 HOH 185 885 338  HOH HOH A . 
G 6 HOH 186 886 340  HOH HOH A . 
G 6 HOH 187 887 151  HOH HOH A . 
G 6 HOH 188 888 290  HOH HOH A . 
G 6 HOH 189 889 217  HOH HOH A . 
G 6 HOH 190 890 118  HOH HOH A . 
G 6 HOH 191 891 303  HOH HOH A . 
G 6 HOH 192 892 140  HOH HOH A . 
G 6 HOH 193 893 327  HOH HOH A . 
G 6 HOH 194 894 255  HOH HOH A . 
G 6 HOH 195 895 227  HOH HOH A . 
G 6 HOH 196 896 367  HOH HOH A . 
G 6 HOH 197 897 143  HOH HOH A . 
G 6 HOH 198 898 141  HOH HOH A . 
G 6 HOH 199 899 324  HOH HOH A . 
G 6 HOH 200 900 206  HOH HOH A . 
G 6 HOH 201 901 250  HOH HOH A . 
G 6 HOH 202 902 285  HOH HOH A . 
G 6 HOH 203 903 364  HOH HOH A . 
G 6 HOH 204 904 214  HOH HOH A . 
G 6 HOH 205 905 241  HOH HOH A . 
G 6 HOH 206 906 344  HOH HOH A . 
G 6 HOH 207 907 302  HOH HOH A . 
G 6 HOH 208 908 222  HOH HOH A . 
G 6 HOH 209 909 326  HOH HOH A . 
G 6 HOH 210 910 352  HOH HOH A . 
G 6 HOH 211 911 297  HOH HOH A . 
G 6 HOH 212 912 348  HOH HOH A . 
G 6 HOH 213 913 354  HOH HOH A . 
G 6 HOH 214 914 262  HOH HOH A . 
G 6 HOH 215 915 316  HOH HOH A . 
G 6 HOH 216 916 180  HOH HOH A . 
G 6 HOH 217 917 239  HOH HOH A . 
G 6 HOH 218 918 335  HOH HOH A . 
G 6 HOH 219 919 126  HOH HOH A . 
G 6 HOH 220 920 236  HOH HOH A . 
G 6 HOH 221 921 179  HOH HOH A . 
G 6 HOH 222 922 117  HOH HOH A . 
G 6 HOH 223 923 379  HOH HOH A . 
G 6 HOH 224 924 189  HOH HOH A . 
G 6 HOH 225 925 41   HOH HOH A . 
G 6 HOH 226 926 375  HOH HOH A . 
G 6 HOH 227 927 381  HOH HOH A . 
G 6 HOH 228 928 366  HOH HOH A . 
G 6 HOH 229 929 301  HOH HOH A . 
G 6 HOH 230 930 288  HOH HOH A . 
G 6 HOH 231 931 359  HOH HOH A . 
G 6 HOH 232 932 229  HOH HOH A . 
G 6 HOH 233 933 388  HOH HOH A . 
G 6 HOH 234 934 153  HOH HOH A . 
G 6 HOH 235 935 322  HOH HOH A . 
H 6 HOH 1   301 260  HOH HOH B . 
H 6 HOH 2   302 345  HOH HOH B . 
H 6 HOH 3   303 59   HOH HOH B . 
H 6 HOH 4   304 233  HOH HOH B . 
H 6 HOH 5   305 279  HOH HOH B . 
H 6 HOH 6   306 390  HOH HOH B . 
H 6 HOH 7   307 173  HOH HOH B . 
H 6 HOH 8   308 300  HOH HOH B . 
H 6 HOH 9   309 129  HOH HOH B . 
H 6 HOH 10  310 73   HOH HOH B . 
H 6 HOH 11  311 195  HOH HOH B . 
H 6 HOH 12  312 22   HOH HOH B . 
H 6 HOH 13  313 384  HOH HOH B . 
H 6 HOH 14  314 191  HOH HOH B . 
H 6 HOH 15  315 61   HOH HOH B . 
H 6 HOH 16  316 76   HOH HOH B . 
H 6 HOH 17  317 258  HOH HOH B . 
H 6 HOH 18  318 385  HOH HOH B . 
H 6 HOH 19  319 154  HOH HOH B . 
H 6 HOH 20  320 110  HOH HOH B . 
H 6 HOH 21  321 66   HOH HOH B . 
H 6 HOH 22  322 228  HOH HOH B . 
H 6 HOH 23  323 292  HOH HOH B . 
H 6 HOH 24  324 38   HOH HOH B . 
H 6 HOH 25  325 177  HOH HOH B . 
H 6 HOH 26  326 299  HOH HOH B . 
H 6 HOH 27  327 136  HOH HOH B . 
H 6 HOH 28  328 78   HOH HOH B . 
H 6 HOH 29  329 311  HOH HOH B . 
H 6 HOH 30  330 50   HOH HOH B . 
H 6 HOH 31  331 234  HOH HOH B . 
H 6 HOH 32  332 42   HOH HOH B . 
H 6 HOH 33  333 97   HOH HOH B . 
H 6 HOH 34  334 19   HOH HOH B . 
H 6 HOH 35  335 88   HOH HOH B . 
H 6 HOH 36  336 188  HOH HOH B . 
H 6 HOH 37  337 84   HOH HOH B . 
H 6 HOH 38  338 106  HOH HOH B . 
H 6 HOH 39  339 87   HOH HOH B . 
H 6 HOH 40  340 29   HOH HOH B . 
H 6 HOH 41  341 186  HOH HOH B . 
H 6 HOH 42  342 219  HOH HOH B . 
H 6 HOH 43  343 71   HOH HOH B . 
H 6 HOH 44  344 120  HOH HOH B . 
H 6 HOH 45  345 4    HOH HOH B . 
H 6 HOH 46  346 162  HOH HOH B . 
H 6 HOH 47  347 25   HOH HOH B . 
H 6 HOH 48  348 58   HOH HOH B . 
H 6 HOH 49  349 230  HOH HOH B . 
H 6 HOH 50  350 192  HOH HOH B . 
H 6 HOH 51  351 101  HOH HOH B . 
H 6 HOH 52  352 246  HOH HOH B . 
H 6 HOH 53  353 224  HOH HOH B . 
H 6 HOH 54  354 39   HOH HOH B . 
H 6 HOH 55  355 305  HOH HOH B . 
H 6 HOH 56  356 175  HOH HOH B . 
H 6 HOH 57  357 368  HOH HOH B . 
H 6 HOH 58  358 125  HOH HOH B . 
H 6 HOH 59  359 238  HOH HOH B . 
H 6 HOH 60  360 150  HOH HOH B . 
H 6 HOH 61  361 94   HOH HOH B . 
H 6 HOH 62  362 254  HOH HOH B . 
H 6 HOH 63  363 48   HOH HOH B . 
H 6 HOH 64  364 235  HOH HOH B . 
H 6 HOH 65  365 174  HOH HOH B . 
H 6 HOH 66  366 277  HOH HOH B . 
H 6 HOH 67  367 253  HOH HOH B . 
H 6 HOH 68  368 184  HOH HOH B . 
H 6 HOH 69  369 298  HOH HOH B . 
H 6 HOH 70  370 54   HOH HOH B . 
H 6 HOH 71  371 33   HOH HOH B . 
H 6 HOH 72  372 36   HOH HOH B . 
H 6 HOH 73  373 389  HOH HOH B . 
H 6 HOH 74  374 90   HOH HOH B . 
H 6 HOH 75  375 232  HOH HOH B . 
H 6 HOH 76  376 102  HOH HOH B . 
H 6 HOH 77  377 203  HOH HOH B . 
H 6 HOH 78  378 383  HOH HOH B . 
H 6 HOH 79  379 80   HOH HOH B . 
H 6 HOH 80  380 165  HOH HOH B . 
H 6 HOH 81  381 98   HOH HOH B . 
H 6 HOH 82  382 130  HOH HOH B . 
H 6 HOH 83  383 276  HOH HOH B . 
H 6 HOH 84  384 314  HOH HOH B . 
H 6 HOH 85  385 204  HOH HOH B . 
H 6 HOH 86  386 306  HOH HOH B . 
H 6 HOH 87  387 111  HOH HOH B . 
H 6 HOH 88  388 256  HOH HOH B . 
H 6 HOH 89  389 144  HOH HOH B . 
H 6 HOH 90  390 374  HOH HOH B . 
H 6 HOH 91  391 372  HOH HOH B . 
H 6 HOH 92  392 218  HOH HOH B . 
H 6 HOH 93  393 240  HOH HOH B . 
H 6 HOH 94  394 265  HOH HOH B . 
H 6 HOH 95  395 104  HOH HOH B . 
H 6 HOH 96  396 346  HOH HOH B . 
H 6 HOH 97  397 156  HOH HOH B . 
H 6 HOH 98  398 127  HOH HOH B . 
H 6 HOH 99  399 334  HOH HOH B . 
H 6 HOH 100 400 321  HOH HOH B . 
H 6 HOH 101 401 312  HOH HOH B . 
H 6 HOH 102 402 170  HOH HOH B . 
H 6 HOH 103 403 386  HOH HOH B . 
H 6 HOH 104 404 293  HOH HOH B . 
H 6 HOH 105 405 350  HOH HOH B . 
H 6 HOH 106 406 1    HOH HOH B . 
H 6 HOH 107 407 207  HOH HOH B . 
H 6 HOH 108 408 342  HOH HOH B . 
H 6 HOH 109 409 198  HOH HOH B . 
H 6 HOH 110 410 373  HOH HOH B . 
H 6 HOH 111 411 249  HOH HOH B . 
H 6 HOH 112 412 332  HOH HOH B . 
H 6 HOH 113 413 361  HOH HOH B . 
H 6 HOH 114 414 132  HOH HOH B . 
H 6 HOH 115 415 349  HOH HOH B . 
H 6 HOH 116 416 183  HOH HOH B . 
H 6 HOH 117 417 336  HOH HOH B . 
H 6 HOH 118 418 362  HOH HOH B . 
H 6 HOH 119 419 325  HOH HOH B . 
H 6 HOH 120 420 211  HOH HOH B . 
H 6 HOH 121 421 328  HOH HOH B . 
H 6 HOH 122 422 370  HOH HOH B . 
H 6 HOH 123 423 333  HOH HOH B . 
H 6 HOH 124 424 313  HOH HOH B . 
H 6 HOH 125 425 280  HOH HOH B . 
H 6 HOH 126 426 347  HOH HOH B . 
H 6 HOH 127 427 355  HOH HOH B . 
H 6 HOH 128 428 343  HOH HOH B . 
H 6 HOH 129 429 382  HOH HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FC2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     97.664 
_cell.length_a_esd                 ? 
_cell.length_b                     97.664 
_cell.length_b_esd                 ? 
_cell.length_c                     64.350 
_cell.length_c_esd                 ? 
_cell.volume                       531554.988 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9FC2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
_symmetry.space_group_name_Hall            'P 61' 
_symmetry.space_group_name_H-M             'P 61' 
_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                   9FC2 
_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          44.5 
_exptl_crystal.description                  Monoclinic 
_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              4.5 
_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    '22,5 % PEG 8000, 100mM NaAc pH 4.5, 200mM NaCl' 
_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 PILATUS3 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         2023-07-14 
_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   0.97926 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97926 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          14.87 
_reflns.entry_id                                       9FC2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.210 
_reflns.d_resolution_low                               48.832 
_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                                     103166 
_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                           97.22 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.89 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.245 
_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                                0.046 
_reflns.pdbx_Rpim_I_all                                0.015 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.044 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.210 
_reflns_shell.d_res_low                                     1.231 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.212 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5301 
_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                               8.33 
_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                               0.868 
_reflns_shell.pdbx_Rpim_I_all                               0.300 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.8234 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.814 
_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               ? 
# 
_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                               23.71 
_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                                 9FC2 
_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                            1.21 
_refine.ls_d_res_low                             42.29 
_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                     103164 
_refine.ls_number_reflns_R_free                  5193 
_refine.ls_number_reflns_R_work                  97971 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.22 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1534 
_refine.ls_R_factor_R_free                       0.1696 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1525 
_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                          1.36 
_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                 16.8112 
_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                            0.1225 
_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                       1.21 
_refine_hist.d_res_low                        42.29 
_refine_hist.number_atoms_solvent             364 
_refine_hist.number_atoms_total               2829 
_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        2439 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_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' ? 0.0115 ? 2679 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2159 ? 3670 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1015 ? 397  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0129 ? 486  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.9675 ? 403  ? 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' 1.21 1.22  . . 181 3336 100.00 . . . . 0.2167 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 1.22 1.24  . . 177 3367 100.00 . . . . 0.2109 . . . . . . . . . . . 0.2910 
'X-RAY DIFFRACTION' 1.24 1.25  . . 157 2913 95.76  . . . . 0.2067 . . . . . . . . . . . 0.2571 
'X-RAY DIFFRACTION' 1.26 1.27  . . 69  951  100.00 . . . . 0.1871 . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 1.27 1.29  . . 166 3369 100.00 . . . . 0.1780 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 1.29 1.30  . . 180 3322 100.00 . . . . 0.1634 . . . . . . . . . . . 0.1831 
'X-RAY DIFFRACTION' 1.30 1.32  . . 145 3375 100.00 . . . . 0.1572 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 1.32 1.34  . . 211 3325 100.00 . . . . 0.1467 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 1.34 1.36  . . 177 3333 100.00 . . . . 0.1539 . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 1.36 1.39  . . 150 3337 100.00 . . . . 0.1524 . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 1.39 1.41  . . 178 3391 100.00 . . . . 0.1436 . . . . . . . . . . . 0.1936 
'X-RAY DIFFRACTION' 1.41 1.44  . . 182 3348 100.00 . . . . 0.1476 . . . . . . . . . . . 0.1766 
'X-RAY DIFFRACTION' 1.44 1.46  . . 173 3367 100.00 . . . . 0.1465 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 1.46 1.49  . . 184 3330 100.00 . . . . 0.1411 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 1.49 1.53  . . 171 3349 100.00 . . . . 0.1473 . . . . . . . . . . . 0.1663 
'X-RAY DIFFRACTION' 1.53 1.56  . . 185 3349 100.00 . . . . 0.1380 . . . . . . . . . . . 0.1552 
'X-RAY DIFFRACTION' 1.56 1.60  . . 193 3343 100.00 . . . . 0.1321 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.60 1.64  . . 186 3342 100.00 . . . . 0.1357 . . . . . . . . . . . 0.1680 
'X-RAY DIFFRACTION' 1.64 1.69  . . 195 3340 100.00 . . . . 0.1368 . . . . . . . . . . . 0.1746 
'X-RAY DIFFRACTION' 1.69 1.75  . . 181 3372 100.00 . . . . 0.1412 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 1.75 1.81  . . 166 3355 100.00 . . . . 0.1422 . . . . . . . . . . . 0.1739 
'X-RAY DIFFRACTION' 1.81 1.88  . . 186 3353 100.00 . . . . 0.1461 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.88 1.97  . . 170 3354 100.00 . . . . 0.1486 . . . . . . . . . . . 0.1719 
'X-RAY DIFFRACTION' 1.97 2.07  . . 188 3360 100.00 . . . . 0.1391 . . . . . . . . . . . 0.1567 
'X-RAY DIFFRACTION' 2.07 2.20  . . 179 3362 100.00 . . . . 0.1472 . . . . . . . . . . . 0.1627 
'X-RAY DIFFRACTION' 2.20 2.37  . . 159 3401 100.00 . . . . 0.1545 . . . . . . . . . . . 0.1564 
'X-RAY DIFFRACTION' 2.37 2.61  . . 165 3391 100.00 . . . . 0.1629 . . . . . . . . . . . 0.1733 
'X-RAY DIFFRACTION' 2.61 2.98  . . 176 3382 100.00 . . . . 0.1618 . . . . . . . . . . . 0.1793 
'X-RAY DIFFRACTION' 2.98 3.76  . . 187 3404 100.00 . . . . 0.1589 . . . . . . . . . . . 0.1623 
'X-RAY DIFFRACTION' 3.76 42.29 . . 176 3450 100.00 . . . . 0.1495 . . . . . . . . . . . 0.1526 
# 
_struct.entry_id                     9FC2 
_struct.title                        
'The crystal structure of the SARS-CoV-2 receptor binding domain in complex with the neutralizing nanobody 4.' 
_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        9FC2 
_struct_keywords.text            
'coronavirus, COVID-19, RBD, SARS-CoV-2, spike, nanobodies, neutralization, VIRAL PROTEIN, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 4 ? 
G N N 6 ? 
H N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPIKE_SARS2 P0DTC2 ? 1 
;ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLV
;
332 
2 PDB 9FC2        9FC2   ? 2 ? 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 9FC2 A 3 ? 205 ? P0DTC2 332 ? 534 ? 332 534 
2 2 9FC2 B 1 ? 125 ? 9FC2   1   ? 125 ? 1   125 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FC2 GLY A 1   ? UNP P0DTC2 ? ? 'expression tag' 330 1 
1 9FC2 SER A 2   ? UNP P0DTC2 ? ? 'expression tag' 331 2 
1 9FC2 PRO A 206 ? UNP P0DTC2 ? ? 'expression tag' 535 3 
1 9FC2 ARG A 207 ? UNP P0DTC2 ? ? 'expression tag' 536 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 2910  ? 
1 MORE         1     ? 
1 'SSA (A^2)'  14630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 PRO A 8   ? ASN A 14  ? PRO A 337 ASN A 343 1 ? 7 
HELX_P HELX_P2 AA2 SER A 20  ? TRP A 24  ? SER A 349 TRP A 353 5 ? 5 
HELX_P HELX_P3 AA3 ASP A 35  ? SER A 42  ? ASP A 364 SER A 371 1 ? 8 
HELX_P HELX_P4 AA4 SER A 54  ? ASP A 60  ? SER A 383 ASP A 389 5 ? 7 
HELX_P HELX_P5 AA5 ASP A 76  ? ILE A 81  ? ASP A 405 ILE A 410 5 ? 6 
HELX_P HELX_P6 AA6 GLY A 87  ? ASN A 93  ? GLY A 416 ASN A 422 1 ? 7 
HELX_P HELX_P7 AA7 SER A 109 ? SER A 114 ? SER A 438 SER A 443 1 ? 6 
HELX_P HELX_P8 AA8 GLY A 173 ? TYR A 176 ? GLY A 502 TYR A 505 5 ? 4 
HELX_P HELX_P9 AA9 LYS B 85  ? THR B 89  ? LYS B 85  THR B 89  5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 7   SG  ? ? ? 1_555 A CYS 32  SG ? ? A CYS 336 A CYS 361 1_555 ? ? ? ? ? ? ? 2.046 ? ?               
disulf2 disulf ?   ? A CYS 50  SG  ? ? ? 1_555 A CYS 103 SG ? ? A CYS 379 A CYS 432 1_555 ? ? ? ? ? ? ? 2.065 ? ?               
disulf3 disulf ?   ? A CYS 62  SG  ? ? ? 1_555 A CYS 196 SG ? ? A CYS 391 A CYS 525 1_555 ? ? ? ? ? ? ? 2.049 ? ?               
disulf4 disulf ?   ? A CYS 151 SG  ? ? ? 1_555 A CYS 159 SG ? ? A CYS 480 A CYS 488 1_555 ? ? ? ? ? ? ? 2.051 ? ?               
disulf5 disulf ?   ? B CYS 22  SG  ? ? ? 1_555 B CYS 94  SG ? ? B CYS 22  B CYS 94  1_555 ? ? ? ? ? ? ? 2.069 ? ?               
disulf6 disulf ?   ? B CYS 32  SG  ? ? ? 1_555 B CYS 106 SG ? ? B CYS 32  B CYS 106 1_555 ? ? ? ? ? ? ? 2.023 ? ?               
covale1 covale one ? A ASN 14  ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 343 A NAG 601 1_555 ? ? ? ? ? ? ? 1.433 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG C .   ? ASN A 14  ? NAG A 601 ? 1_555 ASN A 343 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 7   ? CYS A 32  ? CYS A 336 ? 1_555 CYS A 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 50  ? CYS A 103 ? CYS A 379 ? 1_555 CYS A 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS A 62  ? CYS A 196 ? CYS A 391 ? 1_555 CYS A 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS A 151 ? CYS A 159 ? CYS A 480 ? 1_555 CYS A 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS B 22  ? CYS B 94  ? CYS B 22  ? 1_555 CYS B 94  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS B 32  ? CYS B 106 ? CYS B 32  ? 1_555 CYS B 106 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
# 
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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? 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 ASN A 25  ? ILE A 29  ? ASN A 354 ILE A 358 
AA1 2 ASN A 65  ? ARG A 74  ? ASN A 394 ARG A 403 
AA1 3 PRO A 178 ? GLU A 187 ? PRO A 507 GLU A 516 
AA1 4 GLY A 102 ? ASN A 108 ? GLY A 431 ASN A 437 
AA1 5 THR A 47  ? TYR A 51  ? THR A 376 TYR A 380 
AA2 1 CYS A 32  ? VAL A 33  ? CYS A 361 VAL A 362 
AA2 2 VAL A 195 ? CYS A 196 ? VAL A 524 CYS A 525 
AA2 3 CYS A 62  ? PHE A 63  ? CYS A 391 PHE A 392 
AA3 1 LEU A 123 ? ARG A 125 ? LEU A 452 ARG A 454 
AA3 2 LEU A 163 ? SER A 165 ? LEU A 492 SER A 494 
AA4 1 TYR A 144 ? GLN A 145 ? TYR A 473 GLN A 474 
AA4 2 CYS A 159 ? TYR A 160 ? CYS A 488 TYR A 489 
AA5 1 VAL A 154 ? GLU A 155 ? VAL A 483 GLU A 484 
AA5 2 SER B 55  ? ALA B 59  ? SER B 55  ALA B 59  
AA5 3 GLU B 46  ? SER B 52  ? GLU B 46  SER B 52  
AA5 4 THR B 28  ? GLN B 39  ? THR B 28  GLN B 39  
AA5 5 ALA B 90  ? ARG B 100 ? ALA B 90  ARG B 100 
AA5 6 THR B 114 ? SER B 119 ? THR B 114 SER B 119 
AA5 7 GLY B 10  ? GLN B 13  ? GLY B 10  GLN B 13  
AA6 1 VAL A 154 ? GLU A 155 ? VAL A 483 GLU A 484 
AA6 2 SER B 55  ? ALA B 59  ? SER B 55  ALA B 59  
AA6 3 GLU B 46  ? SER B 52  ? GLU B 46  SER B 52  
AA6 4 THR B 28  ? GLN B 39  ? THR B 28  GLN B 39  
AA6 5 ALA B 90  ? ARG B 100 ? ALA B 90  ARG B 100 
AA6 6 GLU B 107 ? TRP B 110 ? GLU B 107 TRP B 110 
AA7 1 VAL B 2   ? SER B 7   ? VAL B 2   SER B 7   
AA7 2 LEU B 18  ? GLY B 26  ? LEU B 18  GLY B 26  
AA7 3 THR B 76  ? MET B 81  ? THR B 76  MET B 81  
AA7 4 PHE B 66  ? GLN B 70  ? PHE B 66  GLN B 70  
# 
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 ILE A 29  ? N ILE A 358 O VAL A 66  ? O VAL A 395 
AA1 2 3 N ASP A 69  ? N ASP A 398 O VAL A 183 ? O VAL A 512 
AA1 3 4 O LEU A 184 ? O LEU A 513 N CYS A 103 ? N CYS A 432 
AA1 4 5 O GLY A 102 ? O GLY A 431 N TYR A 51  ? N TYR A 380 
AA2 1 2 N CYS A 32  ? N CYS A 361 O CYS A 196 ? O CYS A 525 
AA2 2 3 O VAL A 195 ? O VAL A 524 N PHE A 63  ? N PHE A 392 
AA3 1 2 N TYR A 124 ? N TYR A 453 O GLN A 164 ? O GLN A 493 
AA4 1 2 N TYR A 144 ? N TYR A 473 O TYR A 160 ? O TYR A 489 
AA5 1 2 N GLU A 155 ? N GLU A 484 O TYR B 58  ? O TYR B 58  
AA5 2 3 O ALA B 59  ? O ALA B 59  N VAL B 48  ? N VAL B 48  
AA5 3 4 O SER B 49  ? O SER B 49  N TRP B 36  ? N TRP B 36  
AA5 4 5 N VAL B 35  ? N VAL B 35  O ALA B 95  ? O ALA B 95  
AA5 5 6 N TYR B 92  ? N TYR B 92  O THR B 114 ? O THR B 114 
AA5 6 7 O THR B 117 ? O THR B 117 N VAL B 12  ? N VAL B 12  
AA6 1 2 N GLU A 155 ? N GLU A 484 O TYR B 58  ? O TYR B 58  
AA6 2 3 O ALA B 59  ? O ALA B 59  N VAL B 48  ? N VAL B 48  
AA6 3 4 O SER B 49  ? O SER B 49  N TRP B 36  ? N TRP B 36  
AA6 4 5 N VAL B 35  ? N VAL B 35  O ALA B 95  ? O ALA B 95  
AA6 5 6 N ILE B 98  ? N ILE B 98  O GLU B 107 ? O GLU B 107 
AA7 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA7 2 3 N LEU B 18  ? N LEU B 18  O MET B 81  ? O MET B 81  
AA7 3 4 O GLN B 80  ? O GLN B 80  N THR B 67  ? N THR B 67  
# 
_pdbx_entry_details.entry_id                   9FC2 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 890 ? ? O A HOH 902 ? ? 1.88 
2  1 O   B HOH 322 ? ? O B HOH 404 ? ? 1.90 
3  1 O   B HOH 384 ? ? O B HOH 391 ? ? 1.93 
4  1 O   A HOH 862 ? ? O A HOH 867 ? ? 1.95 
5  1 ND2 B ASN 72  ? B O B HOH 301 ? ? 2.01 
6  1 O   A HOH 897 ? ? O B HOH 395 ? ? 2.04 
7  1 O   A HOH 824 ? ? O A HOH 907 ? ? 2.09 
8  1 O   A HOH 707 ? ? O A HOH 910 ? ? 2.10 
9  1 O   A HOH 840 ? ? O A HOH 918 ? ? 2.12 
10 1 O   A HOH 834 ? ? O A HOH 904 ? ? 2.15 
11 1 O   A HOH 706 ? ? O A HOH 918 ? ? 2.15 
12 1 O   B HOH 382 ? ? O B HOH 400 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     850 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     881 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   5_554 
_pdbx_validate_symm_contact.dist              2.08 
# 
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 ALA A 352 ? ? -109.71 43.34  
2 1 ASN A 422 ? ? -125.05 -53.93 
3 1 ASN A 487 ? ? 57.25   19.64  
4 1 ASN B 75  ? ? 35.17   52.00  
5 1 ALA B 90  ? ? 176.35  170.15 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 x-y,x,z+1/6   
3 y,-x+y,z+5/6  
4 -y,x-y,z+1/3  
5 -x+y,-x,z+2/3 
6 -x,-y,z+1/2   
# 
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 GLY 330 ? A GLY 1   
2  1 Y 1 A SER 331 ? A SER 2   
3  1 Y 1 A ILE 332 ? A ILE 3   
4  1 Y 1 A LYS 528 ? A LYS 199 
5  1 Y 1 A LYS 529 ? A LYS 200 
6  1 Y 1 A SER 530 ? A SER 201 
7  1 Y 1 A THR 531 ? A THR 202 
8  1 Y 1 A ASN 532 ? A ASN 203 
9  1 Y 1 A LEU 533 ? A LEU 204 
10 1 Y 1 A VAL 534 ? A VAL 205 
11 1 Y 1 A PRO 535 ? A PRO 206 
12 1 Y 1 A ARG 536 ? A ARG 207 
13 1 Y 1 B ALA 121 ? B ALA 121 
14 1 Y 1 B LEU 122 ? B LEU 122 
15 1 Y 1 B VAL 123 ? B VAL 123 
16 1 Y 1 B PRO 124 ? B PRO 124 
17 1 Y 1 B ARG 125 ? B ARG 125 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
EDO C1   C N N 95  
EDO O1   O N N 96  
EDO C2   C N N 97  
EDO O2   O N N 98  
EDO H11  H N N 99  
EDO H12  H N N 100 
EDO HO1  H N N 101 
EDO H21  H N N 102 
EDO H22  H N N 103 
EDO HO2  H N N 104 
GLN N    N N N 105 
GLN CA   C N S 106 
GLN C    C N N 107 
GLN O    O N N 108 
GLN CB   C N N 109 
GLN CG   C N N 110 
GLN CD   C N N 111 
GLN OE1  O N N 112 
GLN NE2  N N N 113 
GLN OXT  O N N 114 
GLN H    H N N 115 
GLN H2   H N N 116 
GLN HA   H N N 117 
GLN HB2  H N N 118 
GLN HB3  H N N 119 
GLN HG2  H N N 120 
GLN HG3  H N N 121 
GLN HE21 H N N 122 
GLN HE22 H N N 123 
GLN HXT  H N N 124 
GLU N    N N N 125 
GLU CA   C N S 126 
GLU C    C N N 127 
GLU O    O N N 128 
GLU CB   C N N 129 
GLU CG   C N N 130 
GLU CD   C N N 131 
GLU OE1  O N N 132 
GLU OE2  O N N 133 
GLU OXT  O N N 134 
GLU H    H N N 135 
GLU H2   H N N 136 
GLU HA   H N N 137 
GLU HB2  H N N 138 
GLU HB3  H N N 139 
GLU HG2  H N N 140 
GLU HG3  H N N 141 
GLU HE2  H N N 142 
GLU HXT  H N N 143 
GLY N    N N N 144 
GLY CA   C N N 145 
GLY C    C N N 146 
GLY O    O N N 147 
GLY OXT  O N N 148 
GLY H    H N N 149 
GLY H2   H N N 150 
GLY HA2  H N N 151 
GLY HA3  H N N 152 
GLY HXT  H N N 153 
HIS N    N N N 154 
HIS CA   C N S 155 
HIS C    C N N 156 
HIS O    O N N 157 
HIS CB   C N N 158 
HIS CG   C Y N 159 
HIS ND1  N Y N 160 
HIS CD2  C Y N 161 
HIS CE1  C Y N 162 
HIS NE2  N Y N 163 
HIS OXT  O N N 164 
HIS H    H N N 165 
HIS H2   H N N 166 
HIS HA   H N N 167 
HIS HB2  H N N 168 
HIS HB3  H N N 169 
HIS HD1  H N N 170 
HIS HD2  H N N 171 
HIS HE1  H N N 172 
HIS HE2  H N N 173 
HIS HXT  H N N 174 
HOH O    O N N 175 
HOH H1   H N N 176 
HOH H2   H N N 177 
ILE N    N N N 178 
ILE CA   C N S 179 
ILE C    C N N 180 
ILE O    O N N 181 
ILE CB   C N S 182 
ILE CG1  C N N 183 
ILE CG2  C N N 184 
ILE CD1  C N N 185 
ILE OXT  O N N 186 
ILE H    H N N 187 
ILE H2   H N N 188 
ILE HA   H N N 189 
ILE HB   H N N 190 
ILE HG12 H N N 191 
ILE HG13 H N N 192 
ILE HG21 H N N 193 
ILE HG22 H N N 194 
ILE HG23 H N N 195 
ILE HD11 H N N 196 
ILE HD12 H N N 197 
ILE HD13 H N N 198 
ILE HXT  H N N 199 
LEU N    N N N 200 
LEU CA   C N S 201 
LEU C    C N N 202 
LEU O    O N N 203 
LEU CB   C N N 204 
LEU CG   C N N 205 
LEU CD1  C N N 206 
LEU CD2  C N N 207 
LEU OXT  O N N 208 
LEU H    H N N 209 
LEU H2   H N N 210 
LEU HA   H N N 211 
LEU HB2  H N N 212 
LEU HB3  H N N 213 
LEU HG   H N N 214 
LEU HD11 H N N 215 
LEU HD12 H N N 216 
LEU HD13 H N N 217 
LEU HD21 H N N 218 
LEU HD22 H N N 219 
LEU HD23 H N N 220 
LEU HXT  H N N 221 
LYS N    N N N 222 
LYS CA   C N S 223 
LYS C    C N N 224 
LYS O    O N N 225 
LYS CB   C N N 226 
LYS CG   C N N 227 
LYS CD   C N N 228 
LYS CE   C N N 229 
LYS NZ   N N N 230 
LYS OXT  O N N 231 
LYS H    H N N 232 
LYS H2   H N N 233 
LYS HA   H N N 234 
LYS HB2  H N N 235 
LYS HB3  H N N 236 
LYS HG2  H N N 237 
LYS HG3  H N N 238 
LYS HD2  H N N 239 
LYS HD3  H N N 240 
LYS HE2  H N N 241 
LYS HE3  H N N 242 
LYS HZ1  H N N 243 
LYS HZ2  H N N 244 
LYS HZ3  H N N 245 
LYS HXT  H N N 246 
MET N    N N N 247 
MET CA   C N S 248 
MET C    C N N 249 
MET O    O N N 250 
MET CB   C N N 251 
MET CG   C N N 252 
MET SD   S N N 253 
MET CE   C N N 254 
MET OXT  O N N 255 
MET H    H N N 256 
MET H2   H N N 257 
MET HA   H N N 258 
MET HB2  H N N 259 
MET HB3  H N N 260 
MET HG2  H N N 261 
MET HG3  H N N 262 
MET HE1  H N N 263 
MET HE2  H N N 264 
MET HE3  H N N 265 
MET HXT  H N N 266 
NAG C1   C N R 267 
NAG C2   C N R 268 
NAG C3   C N R 269 
NAG C4   C N S 270 
NAG C5   C N R 271 
NAG C6   C N N 272 
NAG C7   C N N 273 
NAG C8   C N N 274 
NAG N2   N N N 275 
NAG O1   O N N 276 
NAG O3   O N N 277 
NAG O4   O N N 278 
NAG O5   O N N 279 
NAG O6   O N N 280 
NAG O7   O N N 281 
NAG H1   H N N 282 
NAG H2   H N N 283 
NAG H3   H N N 284 
NAG H4   H N N 285 
NAG H5   H N N 286 
NAG H61  H N N 287 
NAG H62  H N N 288 
NAG H81  H N N 289 
NAG H82  H N N 290 
NAG H83  H N N 291 
NAG HN2  H N N 292 
NAG HO1  H N N 293 
NAG HO3  H N N 294 
NAG HO4  H N N 295 
NAG HO6  H N N 296 
PHE N    N N N 297 
PHE CA   C N S 298 
PHE C    C N N 299 
PHE O    O N N 300 
PHE CB   C N N 301 
PHE CG   C Y N 302 
PHE CD1  C Y N 303 
PHE CD2  C Y N 304 
PHE CE1  C Y N 305 
PHE CE2  C Y N 306 
PHE CZ   C Y N 307 
PHE OXT  O N N 308 
PHE H    H N N 309 
PHE H2   H N N 310 
PHE HA   H N N 311 
PHE HB2  H N N 312 
PHE HB3  H N N 313 
PHE HD1  H N N 314 
PHE HD2  H N N 315 
PHE HE1  H N N 316 
PHE HE2  H N N 317 
PHE HZ   H N N 318 
PHE HXT  H N N 319 
PRO N    N N N 320 
PRO CA   C N S 321 
PRO C    C N N 322 
PRO O    O N N 323 
PRO CB   C N N 324 
PRO CG   C N N 325 
PRO CD   C N N 326 
PRO OXT  O N N 327 
PRO H    H N N 328 
PRO HA   H N N 329 
PRO HB2  H N N 330 
PRO HB3  H N N 331 
PRO HG2  H N N 332 
PRO HG3  H N N 333 
PRO HD2  H N N 334 
PRO HD3  H N N 335 
PRO HXT  H N N 336 
SER N    N N N 337 
SER CA   C N S 338 
SER C    C N N 339 
SER O    O N N 340 
SER CB   C N N 341 
SER OG   O N N 342 
SER OXT  O N N 343 
SER H    H N N 344 
SER H2   H N N 345 
SER HA   H N N 346 
SER HB2  H N N 347 
SER HB3  H N N 348 
SER HG   H N N 349 
SER HXT  H N N 350 
THR N    N N N 351 
THR CA   C N S 352 
THR C    C N N 353 
THR O    O N N 354 
THR CB   C N R 355 
THR OG1  O N N 356 
THR CG2  C N N 357 
THR OXT  O N N 358 
THR H    H N N 359 
THR H2   H N N 360 
THR HA   H N N 361 
THR HB   H N N 362 
THR HG1  H N N 363 
THR HG21 H N N 364 
THR HG22 H N N 365 
THR HG23 H N N 366 
THR HXT  H N N 367 
TRP N    N N N 368 
TRP CA   C N S 369 
TRP C    C N N 370 
TRP O    O N N 371 
TRP CB   C N N 372 
TRP CG   C Y N 373 
TRP CD1  C Y N 374 
TRP CD2  C Y N 375 
TRP NE1  N Y N 376 
TRP CE2  C Y N 377 
TRP CE3  C Y N 378 
TRP CZ2  C Y N 379 
TRP CZ3  C Y N 380 
TRP CH2  C Y N 381 
TRP OXT  O N N 382 
TRP H    H N N 383 
TRP H2   H N N 384 
TRP HA   H N N 385 
TRP HB2  H N N 386 
TRP HB3  H N N 387 
TRP HD1  H N N 388 
TRP HE1  H N N 389 
TRP HE3  H N N 390 
TRP HZ2  H N N 391 
TRP HZ3  H N N 392 
TRP HH2  H N N 393 
TRP HXT  H N N 394 
TYR N    N N N 395 
TYR CA   C N S 396 
TYR C    C N N 397 
TYR O    O N N 398 
TYR CB   C N N 399 
TYR CG   C Y N 400 
TYR CD1  C Y N 401 
TYR CD2  C Y N 402 
TYR CE1  C Y N 403 
TYR CE2  C Y N 404 
TYR CZ   C Y N 405 
TYR OH   O N N 406 
TYR OXT  O N N 407 
TYR H    H N N 408 
TYR H2   H N N 409 
TYR HA   H N N 410 
TYR HB2  H N N 411 
TYR HB3  H N N 412 
TYR HD1  H N N 413 
TYR HD2  H N N 414 
TYR HE1  H N N 415 
TYR HE2  H N N 416 
TYR HH   H N N 417 
TYR HXT  H N N 418 
VAL N    N N N 419 
VAL CA   C N S 420 
VAL C    C N N 421 
VAL O    O N N 422 
VAL CB   C N N 423 
VAL CG1  C N N 424 
VAL CG2  C N N 425 
VAL OXT  O N N 426 
VAL H    H N N 427 
VAL H2   H N N 428 
VAL HA   H N N 429 
VAL HB   H N N 430 
VAL HG11 H N N 431 
VAL HG12 H N N 432 
VAL HG13 H N N 433 
VAL HG21 H N N 434 
VAL HG22 H N N 435 
VAL HG23 H N N 436 
VAL HXT  H N N 437 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
EDO C1  O1   sing N N 89  
EDO C1  C2   sing N N 90  
EDO C1  H11  sing N N 91  
EDO C1  H12  sing N N 92  
EDO O1  HO1  sing N N 93  
EDO C2  O2   sing N N 94  
EDO C2  H21  sing N N 95  
EDO C2  H22  sing N N 96  
EDO O2  HO2  sing N N 97  
GLN N   CA   sing N N 98  
GLN N   H    sing N N 99  
GLN N   H2   sing N N 100 
GLN CA  C    sing N N 101 
GLN CA  CB   sing N N 102 
GLN CA  HA   sing N N 103 
GLN C   O    doub N N 104 
GLN C   OXT  sing N N 105 
GLN CB  CG   sing N N 106 
GLN CB  HB2  sing N N 107 
GLN CB  HB3  sing N N 108 
GLN CG  CD   sing N N 109 
GLN CG  HG2  sing N N 110 
GLN CG  HG3  sing N N 111 
GLN CD  OE1  doub N N 112 
GLN CD  NE2  sing N N 113 
GLN NE2 HE21 sing N N 114 
GLN NE2 HE22 sing N N 115 
GLN OXT HXT  sing N N 116 
GLU N   CA   sing N N 117 
GLU N   H    sing N N 118 
GLU N   H2   sing N N 119 
GLU CA  C    sing N N 120 
GLU CA  CB   sing N N 121 
GLU CA  HA   sing N N 122 
GLU C   O    doub N N 123 
GLU C   OXT  sing N N 124 
GLU CB  CG   sing N N 125 
GLU CB  HB2  sing N N 126 
GLU CB  HB3  sing N N 127 
GLU CG  CD   sing N N 128 
GLU CG  HG2  sing N N 129 
GLU CG  HG3  sing N N 130 
GLU CD  OE1  doub N N 131 
GLU CD  OE2  sing N N 132 
GLU OE2 HE2  sing N N 133 
GLU OXT HXT  sing N N 134 
GLY N   CA   sing N N 135 
GLY N   H    sing N N 136 
GLY N   H2   sing N N 137 
GLY CA  C    sing N N 138 
GLY CA  HA2  sing N N 139 
GLY CA  HA3  sing N N 140 
GLY C   O    doub N N 141 
GLY C   OXT  sing N N 142 
GLY OXT HXT  sing N N 143 
HIS N   CA   sing N N 144 
HIS N   H    sing N N 145 
HIS N   H2   sing N N 146 
HIS CA  C    sing N N 147 
HIS CA  CB   sing N N 148 
HIS CA  HA   sing N N 149 
HIS C   O    doub N N 150 
HIS C   OXT  sing N N 151 
HIS CB  CG   sing N N 152 
HIS CB  HB2  sing N N 153 
HIS CB  HB3  sing N N 154 
HIS CG  ND1  sing Y N 155 
HIS CG  CD2  doub Y N 156 
HIS ND1 CE1  doub Y N 157 
HIS ND1 HD1  sing N N 158 
HIS CD2 NE2  sing Y N 159 
HIS CD2 HD2  sing N N 160 
HIS CE1 NE2  sing Y N 161 
HIS CE1 HE1  sing N N 162 
HIS NE2 HE2  sing N N 163 
HIS OXT HXT  sing N N 164 
HOH O   H1   sing N N 165 
HOH O   H2   sing N N 166 
ILE N   CA   sing N N 167 
ILE N   H    sing N N 168 
ILE N   H2   sing N N 169 
ILE CA  C    sing N N 170 
ILE CA  CB   sing N N 171 
ILE CA  HA   sing N N 172 
ILE C   O    doub N N 173 
ILE C   OXT  sing N N 174 
ILE CB  CG1  sing N N 175 
ILE CB  CG2  sing N N 176 
ILE CB  HB   sing N N 177 
ILE CG1 CD1  sing N N 178 
ILE CG1 HG12 sing N N 179 
ILE CG1 HG13 sing N N 180 
ILE CG2 HG21 sing N N 181 
ILE CG2 HG22 sing N N 182 
ILE CG2 HG23 sing N N 183 
ILE CD1 HD11 sing N N 184 
ILE CD1 HD12 sing N N 185 
ILE CD1 HD13 sing N N 186 
ILE OXT HXT  sing N N 187 
LEU N   CA   sing N N 188 
LEU N   H    sing N N 189 
LEU N   H2   sing N N 190 
LEU CA  C    sing N N 191 
LEU CA  CB   sing N N 192 
LEU CA  HA   sing N N 193 
LEU C   O    doub N N 194 
LEU C   OXT  sing N N 195 
LEU CB  CG   sing N N 196 
LEU CB  HB2  sing N N 197 
LEU CB  HB3  sing N N 198 
LEU CG  CD1  sing N N 199 
LEU CG  CD2  sing N N 200 
LEU CG  HG   sing N N 201 
LEU CD1 HD11 sing N N 202 
LEU CD1 HD12 sing N N 203 
LEU CD1 HD13 sing N N 204 
LEU CD2 HD21 sing N N 205 
LEU CD2 HD22 sing N N 206 
LEU CD2 HD23 sing N N 207 
LEU OXT HXT  sing N N 208 
LYS N   CA   sing N N 209 
LYS N   H    sing N N 210 
LYS N   H2   sing N N 211 
LYS CA  C    sing N N 212 
LYS CA  CB   sing N N 213 
LYS CA  HA   sing N N 214 
LYS C   O    doub N N 215 
LYS C   OXT  sing N N 216 
LYS CB  CG   sing N N 217 
LYS CB  HB2  sing N N 218 
LYS CB  HB3  sing N N 219 
LYS CG  CD   sing N N 220 
LYS CG  HG2  sing N N 221 
LYS CG  HG3  sing N N 222 
LYS CD  CE   sing N N 223 
LYS CD  HD2  sing N N 224 
LYS CD  HD3  sing N N 225 
LYS CE  NZ   sing N N 226 
LYS CE  HE2  sing N N 227 
LYS CE  HE3  sing N N 228 
LYS NZ  HZ1  sing N N 229 
LYS NZ  HZ2  sing N N 230 
LYS NZ  HZ3  sing N N 231 
LYS OXT HXT  sing N N 232 
MET N   CA   sing N N 233 
MET N   H    sing N N 234 
MET N   H2   sing N N 235 
MET CA  C    sing N N 236 
MET CA  CB   sing N N 237 
MET CA  HA   sing N N 238 
MET C   O    doub N N 239 
MET C   OXT  sing N N 240 
MET CB  CG   sing N N 241 
MET CB  HB2  sing N N 242 
MET CB  HB3  sing N N 243 
MET CG  SD   sing N N 244 
MET CG  HG2  sing N N 245 
MET CG  HG3  sing N N 246 
MET SD  CE   sing N N 247 
MET CE  HE1  sing N N 248 
MET CE  HE2  sing N N 249 
MET CE  HE3  sing N N 250 
MET OXT HXT  sing N N 251 
NAG C1  C2   sing N N 252 
NAG C1  O1   sing N N 253 
NAG C1  O5   sing N N 254 
NAG C1  H1   sing N N 255 
NAG C2  C3   sing N N 256 
NAG C2  N2   sing N N 257 
NAG C2  H2   sing N N 258 
NAG C3  C4   sing N N 259 
NAG C3  O3   sing N N 260 
NAG C3  H3   sing N N 261 
NAG C4  C5   sing N N 262 
NAG C4  O4   sing N N 263 
NAG C4  H4   sing N N 264 
NAG C5  C6   sing N N 265 
NAG C5  O5   sing N N 266 
NAG C5  H5   sing N N 267 
NAG C6  O6   sing N N 268 
NAG C6  H61  sing N N 269 
NAG C6  H62  sing N N 270 
NAG C7  C8   sing N N 271 
NAG C7  N2   sing N N 272 
NAG C7  O7   doub N N 273 
NAG C8  H81  sing N N 274 
NAG C8  H82  sing N N 275 
NAG C8  H83  sing N N 276 
NAG N2  HN2  sing N N 277 
NAG O1  HO1  sing N N 278 
NAG O3  HO3  sing N N 279 
NAG O4  HO4  sing N N 280 
NAG O6  HO6  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
_pdbx_audit_support.funding_organization   'Ministerio de Ciencia e Innovacion (MCIN)' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           202020E079 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' Other ?    'RBD structure from the authors' 
2 ? 'experimental model' PDB   6h71 ?                                
# 
_space_group.name_H-M_alt     'P 61' 
_space_group.name_Hall        'P 61' 
_space_group.IT_number        169 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FC2 
_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]   0.010239 
_atom_sites.fract_transf_matrix[1][2]   0.005912 
_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]   0.011823 
_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]   0.015540 
_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.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 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   . THR A 1 4   ? -0.19594  -20.09060 -28.69567 1.000 82.57278  ? 333 THR A N   1 
ATOM   2    C CA  . THR A 1 4   ? -1.23883  -21.04331 -28.33378 1.000 80.62114  ? 333 THR A CA  1 
ATOM   3    C C   . THR A 1 4   ? -0.76212  -22.49284 -28.36236 1.000 73.76802  ? 333 THR A C   1 
ATOM   4    O O   . THR A 1 4   ? -1.39413  -23.33203 -29.00562 1.000 75.22621  ? 333 THR A O   1 
ATOM   5    C CB  . THR A 1 4   ? -2.45044  -20.95624 -29.28688 1.000 84.05284  ? 333 THR A CB  1 
ATOM   6    O OG1 . THR A 1 4   ? -2.32387  -19.80616 -30.13124 1.000 85.52133  ? 333 THR A OG1 1 
ATOM   7    C CG2 . THR A 1 4   ? -3.75598  -20.87973 -28.50292 1.000 84.78263  ? 333 THR A CG2 1 
ATOM   8    N N   . ASN A 1 5   ? 0.33974   -22.80945 -27.68695 1.000 64.11015  ? 334 ASN A N   1 
ATOM   9    C CA  . ASN A 1 5   ? 0.67051   -24.21546 -27.51870 1.000 55.23942  ? 334 ASN A CA  1 
ATOM   10   C C   . ASN A 1 5   ? -0.30940  -24.82938 -26.52605 1.000 48.09710  ? 334 ASN A C   1 
ATOM   11   O O   . ASN A 1 5   ? -0.76730  -24.16498 -25.59455 1.000 43.41408  ? 334 ASN A O   1 
ATOM   12   C CB  . ASN A 1 5   ? 2.10903   -24.40855 -27.02682 1.000 55.22076  ? 334 ASN A CB  1 
ATOM   13   C CG  . ASN A 1 5   ? 2.46054   -23.52177 -25.84116 1.000 56.45930  ? 334 ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 5   ? 2.31860   -22.29695 -25.89645 1.000 57.46530  ? 334 ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 5   ? 2.92227   -24.14496 -24.75449 1.000 56.59587  ? 334 ASN A ND2 1 
ATOM   16   N N   . LEU A 1 6   ? -0.66144  -26.08708 -26.74910 1.000 47.51032  ? 335 LEU A N   1 
ATOM   17   C CA  . LEU A 1 6   ? -1.56123  -26.77555 -25.83479 1.000 48.53023  ? 335 LEU A CA  1 
ATOM   18   C C   . LEU A 1 6   ? -0.80450  -27.33297 -24.63492 1.000 43.78663  ? 335 LEU A C   1 
ATOM   19   O O   . LEU A 1 6   ? 0.33162   -27.80543 -24.74173 1.000 42.13465  ? 335 LEU A O   1 
ATOM   20   C CB  . LEU A 1 6   ? -2.28188  -27.91243 -26.54743 1.000 53.08048  ? 335 LEU A CB  1 
ATOM   21   C CG  . LEU A 1 6   ? -1.29992  -28.96394 -27.05234 1.000 56.68089  ? 335 LEU A CG  1 
ATOM   22   C CD1 . LEU A 1 6   ? -1.25146  -30.18231 -26.13918 1.000 57.17473  ? 335 LEU A CD1 1 
ATOM   23   C CD2 . LEU A 1 6   ? -1.67781  -29.34877 -28.47981 1.000 58.70915  ? 335 LEU A CD2 1 
ATOM   24   N N   . CYS A 1 7   ? -1.45966  -27.29010 -23.48404 1.000 36.49066  ? 336 CYS A N   1 
ATOM   25   C CA  . CYS A 1 7   ? -0.80829  -27.73728 -22.26750 1.000 31.71652  ? 336 CYS A CA  1 
ATOM   26   C C   . CYS A 1 7   ? -0.48811  -29.23173 -22.34157 1.000 30.48423  ? 336 CYS A C   1 
ATOM   27   O O   . CYS A 1 7   ? -1.32095  -30.02792 -22.79523 1.000 30.24969  ? 336 CYS A O   1 
ATOM   28   C CB  . CYS A 1 7   ? -1.69354  -27.42726 -21.06822 1.000 28.96231  ? 336 CYS A CB  1 
ATOM   29   S SG  . CYS A 1 7   ? -1.99607  -25.67665 -20.81328 1.000 28.31312  ? 336 CYS A SG  1 
ATOM   30   N N   . PRO A 1 8   ? 0.71224   -29.64933 -21.87333 1.000 28.66797  ? 337 PRO A N   1 
ATOM   31   C CA  . PRO A 1 8   ? 1.16759   -31.05214 -21.99532 1.000 28.42444  ? 337 PRO A CA  1 
ATOM   32   C C   . PRO A 1 8   ? 0.61361   -31.95976 -20.90040 1.000 26.70020  ? 337 PRO A C   1 
ATOM   33   O O   . PRO A 1 8   ? 1.36031   -32.62125 -20.17927 1.000 27.21459  ? 337 PRO A O   1 
ATOM   34   C CB  . PRO A 1 8   ? 2.69480   -30.92431 -21.86551 1.000 30.21103  ? 337 PRO A CB  1 
ATOM   35   C CG  . PRO A 1 8   ? 2.96644   -29.61581 -21.30533 1.000 31.27012  ? 337 PRO A CG  1 
ATOM   36   C CD  . PRO A 1 8   ? 1.75094   -28.75541 -21.34399 1.000 29.72459  ? 337 PRO A CD  1 
ATOM   37   N N   . PHE A 1 9   ? -0.71325  -32.01083 -20.77190 1.000 26.23337  ? 338 PHE A N   1 
ATOM   38   C CA  . PHE A 1 9   ? -1.30089  -32.81914 -19.70586 1.000 25.58517  ? 338 PHE A CA  1 
ATOM   39   C C   . PHE A 1 9   ? -1.12419  -34.29954 -19.98143 1.000 24.64803  ? 338 PHE A C   1 
ATOM   40   O O   . PHE A 1 9   ? -1.11573  -35.10460 -19.04676 1.000 24.36529  ? 338 PHE A O   1 
ATOM   41   C CB  . PHE A 1 9   ? -2.78332  -32.50435 -19.61726 1.000 25.67228  ? 338 PHE A CB  1 
ATOM   42   C CG  . PHE A 1 9   ? -3.08605  -31.28107 -18.82046 1.000 27.17606  ? 338 PHE A CG  1 
ATOM   43   C CD1 . PHE A 1 9   ? -2.57876  -31.10763 -17.53723 1.000 27.91823  ? 338 PHE A CD1 1 
ATOM   44   C CD2 . PHE A 1 9   ? -3.78206  -30.23529 -19.41435 1.000 30.53428  ? 338 PHE A CD2 1 
ATOM   45   C CE1 . PHE A 1 9   ? -2.85266  -29.94770 -16.82674 1.000 28.72247  ? 338 PHE A CE1 1 
ATOM   46   C CE2 . PHE A 1 9   ? -4.05073  -29.06525 -18.71966 1.000 30.35217  ? 338 PHE A CE2 1 
ATOM   47   C CZ  . PHE A 1 9   ? -3.57699  -28.90883 -17.43424 1.000 30.61289  ? 338 PHE A CZ  1 
ATOM   48   N N   . GLY A 1 10  ? -0.99677  -34.67842 -21.25597 1.000 27.00759  ? 339 GLY A N   1 
ATOM   49   C CA  . GLY A 1 10  ? -0.77895  -36.07351 -21.58660 1.000 27.11511  ? 339 GLY A CA  1 
ATOM   50   C C   . GLY A 1 10  ? 0.44470   -36.65501 -20.92061 1.000 25.01034  ? 339 GLY A C   1 
ATOM   51   O O   . GLY A 1 10  ? 0.45506   -37.83220 -20.55301 1.000 25.64650  ? 339 GLY A O   1 
ATOM   52   N N   . GLU A 1 11  ? 1.49772   -35.85365 -20.76536 1.000 25.82764  ? 340 GLU A N   1 
ATOM   53   C CA  . GLU A 1 11  ? 2.69483   -36.38014 -20.12965 1.000 27.94963  ? 340 GLU A CA  1 
ATOM   54   C C   . GLU A 1 11  ? 2.40464   -36.79711 -18.70534 1.000 25.82947  ? 340 GLU A C   1 
ATOM   55   O O   . GLU A 1 11  ? 3.07791   -37.68999 -18.17523 1.000 27.73458  ? 340 GLU A O   1 
ATOM   56   C CB  . GLU A 1 11  ? 3.80395   -35.33392 -20.11977 1.000 33.23418  ? 340 GLU A CB  1 
ATOM   57   C CG  . GLU A 1 11  ? 4.58416   -35.25939 -21.41260 1.000 41.96051  ? 340 GLU A CG  1 
ATOM   58   C CD  . GLU A 1 11  ? 5.15002   -33.88308 -21.65105 1.000 47.61386  ? 340 GLU A CD  1 
ATOM   59   O OE1 . GLU A 1 11  ? 5.78154   -33.34462 -20.71744 1.000 50.08066  ? 340 GLU A OE1 1 
ATOM   60   O OE2 . GLU A 1 11  ? 4.97777   -33.34556 -22.76810 1.000 50.04760  ? 340 GLU A OE2 1 
ATOM   61   N N   . VAL A 1 12  ? 1.44683   -36.13520 -18.05195 1.000 22.99379  ? 341 VAL A N   1 
ATOM   62   C CA  . VAL A 1 12  ? 1.12163   -36.48916 -16.67649 1.000 20.86135  ? 341 VAL A CA  1 
ATOM   63   C C   . VAL A 1 12  ? 0.14893   -37.64569 -16.66857 1.000 19.48045  ? 341 VAL A C   1 
ATOM   64   O O   . VAL A 1 12  ? 0.39055   -38.68072 -16.03474 1.000 19.41701  ? 341 VAL A O   1 
ATOM   65   C CB  . VAL A 1 12  ? 0.54986   -35.26144 -15.94581 1.000 23.33211  ? 341 VAL A CB  1 
ATOM   66   C CG1 . VAL A 1 12  ? 0.15792   -35.60320 -14.49979 1.000 23.51818  ? 341 VAL A CG1 1 
ATOM   67   C CG2 . VAL A 1 12  ? 1.53686   -34.10683 -16.01295 1.000 24.23732  ? 341 VAL A CG2 1 
ATOM   68   N N   . PHE A 1 13  ? -0.97306  -37.49917 -17.38009 1.000 18.61275  ? 342 PHE A N   1 
ATOM   69   C CA  . PHE A 1 13  ? -2.02125  -38.49850 -17.24766 1.000 17.86960  ? 342 PHE A CA  1 
ATOM   70   C C   . PHE A 1 13  ? -1.61515  -39.82853 -17.84432 1.000 20.16472  ? 342 PHE A C   1 
ATOM   71   O O   . PHE A 1 13  ? -2.05668  -40.87878 -17.36581 1.000 20.88753  ? 342 PHE A O   1 
ATOM   72   C CB  . PHE A 1 13  ? -3.33195  -38.01325 -17.87996 1.000 19.06841  ? 342 PHE A CB  1 
ATOM   73   C CG  . PHE A 1 13  ? -4.03184  -36.97301 -17.06449 1.000 17.23345  ? 342 PHE A CG  1 
ATOM   74   C CD1 . PHE A 1 13  ? -3.73025  -35.62415 -17.20982 1.000 18.72300  ? 342 PHE A CD1 1 
ATOM   75   C CD2 . PHE A 1 13  ? -4.94117  -37.33987 -16.08520 1.000 16.43537  ? 342 PHE A CD2 1 
ATOM   76   C CE1 . PHE A 1 13  ? -4.36511  -34.67778 -16.46061 1.000 18.90917  ? 342 PHE A CE1 1 
ATOM   77   C CE2 . PHE A 1 13  ? -5.58200  -36.38931 -15.33021 1.000 18.10449  ? 342 PHE A CE2 1 
ATOM   78   C CZ  . PHE A 1 13  ? -5.28122  -35.05668 -15.50365 1.000 18.36512  ? 342 PHE A CZ  1 
ATOM   79   N N   . ASN A 1 14  ? -0.79055  -39.80694 -18.88819 1.000 20.75278  ? 343 ASN A N   1 
ATOM   80   C CA  . ASN A 1 14  ? -0.46808  -41.01377 -19.62757 1.000 21.22162  ? 343 ASN A CA  1 
ATOM   81   C C   . ASN A 1 14  ? 0.91432   -41.55021 -19.32139 1.000 22.87377  ? 343 ASN A C   1 
ATOM   82   O O   . ASN A 1 14  ? 1.40936   -42.40571 -20.05564 1.000 25.32837  ? 343 ASN A O   1 
ATOM   83   C CB  . ASN A 1 14  ? -0.62424  -40.77485 -21.10109 1.000 24.55127  ? 343 ASN A CB  1 
ATOM   84   C CG  . ASN A 1 14  ? -2.05757  -40.81504 -21.50667 1.000 28.85736  ? 343 ASN A CG  1 
ATOM   85   O OD1 . ASN A 1 14  ? -2.87269  -41.57417 -20.93038 1.000 29.12803  ? 343 ASN A OD1 1 
ATOM   86   N ND2 . ASN A 1 14  ? -2.39285  -40.01891 -22.50407 1.000 31.65542  ? 343 ASN A ND2 1 
ATOM   87   N N   . ALA A 1 15  ? 1.55711   -41.07182 -18.26981 1.000 22.37019  ? 344 ALA A N   1 
ATOM   88   C CA  . ALA A 1 15  ? 2.88116   -41.60646 -17.93400 1.000 23.23277  ? 344 ALA A CA  1 
ATOM   89   C C   . ALA A 1 15  ? 2.75927   -43.10883 -17.69304 1.000 21.54599  ? 344 ALA A C   1 
ATOM   90   O O   . ALA A 1 15  ? 1.79023   -43.57981 -17.08822 1.000 23.94161  ? 344 ALA A O   1 
ATOM   91   C CB  . ALA A 1 15  ? 3.38906   -40.91132 -16.66820 1.000 23.78618  ? 344 ALA A CB  1 
ATOM   92   N N   . THR A 1 16  ? 3.75172   -43.89075 -18.14831 1.000 25.40595  ? 345 THR A N   1 
ATOM   93   C CA  A THR A 1 16  ? 3.66284   -45.34347 -17.99402 0.500 27.38612  ? 345 THR A CA  1 
ATOM   94   C CA  B THR A 1 16  ? 3.66219   -45.34342 -17.99463 0.500 27.38282  ? 345 THR A CA  1 
ATOM   95   C C   . THR A 1 16  ? 3.77150   -45.75907 -16.53476 1.000 26.28372  ? 345 THR A C   1 
ATOM   96   O O   . THR A 1 16  ? 3.03889   -46.65409 -16.07857 1.000 25.22704  ? 345 THR A O   1 
ATOM   97   C CB  A THR A 1 16  ? 4.73729   -46.04348 -18.82502 0.500 30.81659  ? 345 THR A CB  1 
ATOM   98   C CB  B THR A 1 16  ? 4.75057   -46.04231 -18.80349 0.500 30.61319  ? 345 THR A CB  1 
ATOM   99   O OG1 A THR A 1 16  ? 5.99384   -45.38607 -18.63170 0.500 32.20052  ? 345 THR A OG1 1 
ATOM   100  O OG1 B THR A 1 16  ? 4.58284   -45.73684 -20.19455 0.500 30.13873  ? 345 THR A OG1 1 
ATOM   101  C CG2 A THR A 1 16  ? 4.37309   -46.02863 -20.30344 0.500 32.84948  ? 345 THR A CG2 1 
ATOM   102  C CG2 B THR A 1 16  ? 4.65474   -47.54844 -18.60120 0.500 32.84648  ? 345 THR A CG2 1 
ATOM   103  N N   . ARG A 1 17  ? 4.67644   -45.13837 -15.78607 1.000 25.87381  ? 346 ARG A N   1 
ATOM   104  C CA  A ARG A 1 17  ? 4.75474   -45.38264 -14.35661 0.500 27.24016  ? 346 ARG A CA  1 
ATOM   105  C CA  B ARG A 1 17  ? 4.76326   -45.37403 -14.35556 0.500 27.24925  ? 346 ARG A CA  1 
ATOM   106  C C   . ARG A 1 17  ? 4.44440   -44.09541 -13.59934 1.000 25.56061  ? 346 ARG A C   1 
ATOM   107  O O   . ARG A 1 17  ? 4.79169   -42.98101 -14.03522 1.000 24.70455  ? 346 ARG A O   1 
ATOM   108  C CB  A ARG A 1 17  ? 6.10810   -45.96926 -13.89690 0.500 32.82078  ? 346 ARG A CB  1 
ATOM   109  C CB  B ARG A 1 17  ? 6.11929   -45.89467 -13.86470 0.500 32.95109  ? 346 ARG A CB  1 
ATOM   110  C CG  A ARG A 1 17  ? 6.07347   -46.37991 -12.40322 0.500 40.15848  ? 346 ARG A CG  1 
ATOM   111  C CG  B ARG A 1 17  ? 6.02672   -46.13053 -12.34546 0.500 40.38448  ? 346 ARG A CG  1 
ATOM   112  C CD  A ARG A 1 17  ? 7.37100   -46.99983 -11.85964 0.500 46.18334  ? 346 ARG A CD  1 
ATOM   113  C CD  B ARG A 1 17  ? 7.26897   -46.65342 -11.65958 0.500 46.55713  ? 346 ARG A CD  1 
ATOM   114  N NE  A ARG A 1 17  ? 8.54779   -46.17344 -12.10415 0.500 51.29654  ? 346 ARG A NE  1 
ATOM   115  N NE  B ARG A 1 17  ? 6.99760   -46.83179 -10.23577 0.500 51.58157  ? 346 ARG A NE  1 
ATOM   116  C CZ  A ARG A 1 17  ? 9.12620   -45.40659 -11.18689 0.500 54.82000  ? 346 ARG A CZ  1 
ATOM   117  C CZ  B ARG A 1 17  ? 7.10349   -45.89437 -9.30179  0.500 55.10001  ? 346 ARG A CZ  1 
ATOM   118  N NH1 A ARG A 1 17  ? 8.65879   -45.33164 -9.95068  0.500 55.94931  ? 346 ARG A NH1 1 
ATOM   119  N NH1 B ARG A 1 17  ? 7.52083   -44.67363 -9.58826  0.500 56.04057  ? 346 ARG A NH1 1 
ATOM   120  N NH2 A ARG A 1 17  ? 10.19248  -44.68849 -11.52076 0.500 55.33470  ? 346 ARG A NH2 1 
ATOM   121  N NH2 B ARG A 1 17  ? 6.78666   -46.19627 -8.04461  0.500 55.75815  ? 346 ARG A NH2 1 
ATOM   122  N N   . PHE A 1 18  ? 3.77074   -44.26170 -12.49653 1.000 21.48015  ? 347 PHE A N   1 
ATOM   123  C CA  . PHE A 1 18  ? 3.45631   -43.17234 -11.59886 1.000 16.18079  ? 347 PHE A CA  1 
ATOM   124  C C   . PHE A 1 18  ? 4.34192   -43.30718 -10.36799 1.000 14.67303  ? 347 PHE A C   1 
ATOM   125  O O   . PHE A 1 18  ? 4.90092   -44.37958 -10.11466 1.000 15.17607  ? 347 PHE A O   1 
ATOM   126  C CB  . PHE A 1 18  ? 1.97575   -43.31236 -11.25427 1.000 16.23961  ? 347 PHE A CB  1 
ATOM   127  C CG  . PHE A 1 18  ? 1.07426   -42.42179 -12.08644 1.000 16.60178  ? 347 PHE A CG  1 
ATOM   128  C CD1 . PHE A 1 18  ? 1.16501   -42.42234 -13.46650 1.000 17.40734  ? 347 PHE A CD1 1 
ATOM   129  C CD2 . PHE A 1 18  ? 0.07345   -41.65986 -11.48940 1.000 16.69226  ? 347 PHE A CD2 1 
ATOM   130  C CE1 . PHE A 1 18  ? 0.29373   -41.62247 -14.23340 1.000 18.03431  ? 347 PHE A CE1 1 
ATOM   131  C CE2 . PHE A 1 18  ? -0.77294  -40.86615 -12.23249 1.000 17.33880  ? 347 PHE A CE2 1 
ATOM   132  C CZ  . PHE A 1 18  ? -0.65830  -40.84044 -13.62448 1.000 18.64076  ? 347 PHE A CZ  1 
ATOM   133  N N   . ALA A 1 19  ? 4.43092   -42.22016 -9.59498  1.000 13.64590  ? 348 ALA A N   1 
ATOM   134  C CA  . ALA A 1 19  ? 5.18273   -42.20207 -8.34893  1.000 13.05737  ? 348 ALA A CA  1 
ATOM   135  C C   . ALA A 1 19  ? 4.41838   -42.87917 -7.21325  1.000 11.99265  ? 348 ALA A C   1 
ATOM   136  O O   . ALA A 1 19  ? 3.18997   -42.77435 -7.09943  1.000 12.34731  ? 348 ALA A O   1 
ATOM   137  C CB  . ALA A 1 19  ? 5.41909   -40.74642 -7.94146  1.000 16.10802  ? 348 ALA A CB  1 
ATOM   138  N N   . SER A 1 20  ? 5.17258   -43.48358 -6.28905  1.000 11.66698  ? 349 SER A N   1 
ATOM   139  C CA  . SER A 1 20  ? 4.62787   -43.73026 -4.95235  1.000 11.15490  ? 349 SER A CA  1 
ATOM   140  C C   . SER A 1 20  ? 4.16034   -42.42107 -4.32938  1.000 11.37539  ? 349 SER A C   1 
ATOM   141  O O   . SER A 1 20  ? 4.80906   -41.38147 -4.49154  1.000 11.95120  ? 349 SER A O   1 
ATOM   142  C CB  . SER A 1 20  ? 5.69490   -44.28361 -4.01883  1.000 12.22208  ? 349 SER A CB  1 
ATOM   143  O OG  . SER A 1 20  ? 6.04900   -45.60093 -4.36733  1.000 12.00687  ? 349 SER A OG  1 
ATOM   144  N N   . VAL A 1 21  ? 3.07653   -42.50051 -3.55675  1.000 11.62098  ? 350 VAL A N   1 
ATOM   145  C CA  . VAL A 1 21  ? 2.51516   -41.28621 -2.96775  1.000 11.00880  ? 350 VAL A CA  1 
ATOM   146  C C   . VAL A 1 21  ? 3.50787   -40.55326 -2.05446  1.000 10.88345  ? 350 VAL A C   1 
ATOM   147  O O   . VAL A 1 21  ? 3.51905   -39.32298 -2.01649  1.000 11.85090  ? 350 VAL A O   1 
ATOM   148  C CB  . VAL A 1 21  ? 1.18104   -41.60945 -2.25857  1.000 11.53662  ? 350 VAL A CB  1 
ATOM   149  C CG1 . VAL A 1 21  ? 1.37212   -42.57916 -1.08010  1.000 11.49814  ? 350 VAL A CG1 1 
ATOM   150  C CG2 . VAL A 1 21  ? 0.46921   -40.32522 -1.86371  1.000 12.74991  ? 350 VAL A CG2 1 
ATOM   151  N N   . TYR A 1 22  ? 4.34999   -41.27932 -1.30418  1.000 11.25057  ? 351 TYR A N   1 
ATOM   152  C CA  . TYR A 1 22  ? 5.27780   -40.58268 -0.40515  1.000 11.89831  ? 351 TYR A CA  1 
ATOM   153  C C   . TYR A 1 22  ? 6.24224   -39.71667 -1.20917  1.000 11.74104  ? 351 TYR A C   1 
ATOM   154  O O   . TYR A 1 22  ? 6.73222   -38.68326 -0.72165  1.000 12.99243  ? 351 TYR A O   1 
ATOM   155  C CB  . TYR A 1 22  ? 5.99164   -41.57351 0.53417   1.000 12.20576  ? 351 TYR A CB  1 
ATOM   156  C CG  . TYR A 1 22  ? 7.23166   -42.16182 -0.07928  1.000 12.29819  ? 351 TYR A CG  1 
ATOM   157  C CD1 . TYR A 1 22  ? 7.16584   -43.29164 -0.86171  1.000 12.82572  ? 351 TYR A CD1 1 
ATOM   158  C CD2 . TYR A 1 22  ? 8.48210   -41.53568 0.08914   1.000 14.64590  ? 351 TYR A CD2 1 
ATOM   159  C CE1 . TYR A 1 22  ? 8.32838   -43.79781 -1.49372  1.000 15.19767  ? 351 TYR A CE1 1 
ATOM   160  C CE2 . TYR A 1 22  ? 9.61387   -42.03500 -0.47040  1.000 18.33256  ? 351 TYR A CE2 1 
ATOM   161  C CZ  . TYR A 1 22  ? 9.54359   -43.13186 -1.27757  1.000 17.46459  ? 351 TYR A CZ  1 
ATOM   162  O OH  . TYR A 1 22  ? 10.71416  -43.56361 -1.84137  1.000 20.86806  ? 351 TYR A OH  1 
ATOM   163  N N   . ALA A 1 23  ? 6.54784   -40.15168 -2.43541  1.000 11.92386  ? 352 ALA A N   1 
ATOM   164  C CA  . ALA A 1 23  ? 7.45822   -39.47987 -3.36360  1.000 12.40413  ? 352 ALA A CA  1 
ATOM   165  C C   . ALA A 1 23  ? 6.66671   -38.88838 -4.52601  1.000 11.88650  ? 352 ALA A C   1 
ATOM   166  O O   . ALA A 1 23  ? 7.07995   -38.96180 -5.68490  1.000 12.65874  ? 352 ALA A O   1 
ATOM   167  C CB  . ALA A 1 23  ? 8.53541   -40.46041 -3.85887  1.000 13.23322  ? 352 ALA A CB  1 
ATOM   168  N N   . TRP A 1 24  ? 5.53295   -38.26158 -4.21730  1.000 11.89196  ? 353 TRP A N   1 
ATOM   169  C CA  . TRP A 1 24  ? 4.63843   -37.78531 -5.25830  1.000 12.34691  ? 353 TRP A CA  1 
ATOM   170  C C   . TRP A 1 24  ? 5.36842   -36.87847 -6.25422  1.000 12.19456  ? 353 TRP A C   1 
ATOM   171  O O   . TRP A 1 24  ? 6.26614   -36.12008 -5.89427  1.000 13.16983  ? 353 TRP A O   1 
ATOM   172  C CB  . TRP A 1 24  ? 3.46485   -37.07995 -4.60681  1.000 12.10318  ? 353 TRP A CB  1 
ATOM   173  C CG  . TRP A 1 24  ? 3.74243   -36.02863 -3.58273  1.000 12.47283  ? 353 TRP A CG  1 
ATOM   174  C CD1 . TRP A 1 24  ? 3.87952   -36.20787 -2.21465  1.000 12.19864  ? 353 TRP A CD1 1 
ATOM   175  C CD2 . TRP A 1 24  ? 3.82814   -34.61516 -3.81571  1.000 12.22110  ? 353 TRP A CD2 1 
ATOM   176  N NE1 . TRP A 1 24  ? 4.02582   -34.99412 -1.58787  1.000 12.80281  ? 353 TRP A NE1 1 
ATOM   177  C CE2 . TRP A 1 24  ? 4.01467   -34.00033 -2.54849  1.000 12.60910  ? 353 TRP A CE2 1 
ATOM   178  C CE3 . TRP A 1 24  ? 3.75128   -33.80790 -4.96301  1.000 12.62236  ? 353 TRP A CE3 1 
ATOM   179  C CZ2 . TRP A 1 24  ? 4.07032   -32.61594 -2.39928  1.000 14.11113  ? 353 TRP A CZ2 1 
ATOM   180  C CZ3 . TRP A 1 24  ? 3.80412   -32.43030 -4.81479  1.000 14.49376  ? 353 TRP A CZ3 1 
ATOM   181  C CH2 . TRP A 1 24  ? 3.97910   -31.84815 -3.54025  1.000 14.80881  ? 353 TRP A CH2 1 
ATOM   182  N N   . ASN A 1 25  ? 4.95837   -36.93581 -7.51167  1.000 13.61162  ? 354 ASN A N   1 
ATOM   183  C CA  A ASN A 1 25  ? 5.58352   -36.14076 -8.54976  0.500 13.73055  ? 354 ASN A CA  1 
ATOM   184  C CA  B ASN A 1 25  ? 5.57910   -36.14050 -8.55468  0.500 13.72360  ? 354 ASN A CA  1 
ATOM   185  C C   . ASN A 1 25  ? 4.79545   -34.85306 -8.76156  1.000 13.86331  ? 354 ASN A C   1 
ATOM   186  O O   . ASN A 1 25  ? 3.59267   -34.76682 -8.47024  1.000 14.14151  ? 354 ASN A O   1 
ATOM   187  C CB  A ASN A 1 25  ? 5.65952   -36.94014 -9.85375  0.500 16.76791  ? 354 ASN A CB  1 
ATOM   188  C CB  B ASN A 1 25  ? 5.63396   -36.91538 -9.87326  0.500 16.41332  ? 354 ASN A CB  1 
ATOM   189  C CG  A ASN A 1 25  ? 6.76013   -36.45103 -10.78483 0.500 21.23772  ? 354 ASN A CG  1 
ATOM   190  C CG  B ASN A 1 25  ? 6.82165   -37.83024 -9.96033  0.500 18.40021  ? 354 ASN A CG  1 
ATOM   191  O OD1 A ASN A 1 25  ? 7.59069   -35.59240 -10.42317 0.500 24.12608  ? 354 ASN A OD1 1 
ATOM   192  O OD1 B ASN A 1 25  ? 7.88435   -37.54368 -9.41747  0.500 19.32609  ? 354 ASN A OD1 1 
ATOM   193  N ND2 A ASN A 1 25  ? 6.80581   -37.03590 -11.97890 0.500 25.12495  ? 354 ASN A ND2 1 
ATOM   194  N ND2 B ASN A 1 25  ? 6.64550   -38.95018 -10.64274 0.500 18.85872  ? 354 ASN A ND2 1 
ATOM   195  N N   . ARG A 1 26  ? 5.48251   -33.83358 -9.29461  1.000 14.39401  ? 355 ARG A N   1 
ATOM   196  C CA  . ARG A 1 26  ? 4.84774   -32.57800 -9.65933  1.000 14.87019  ? 355 ARG A CA  1 
ATOM   197  C C   . ARG A 1 26  ? 5.36472   -32.13849 -11.02127 1.000 14.99207  ? 355 ARG A C   1 
ATOM   198  O O   . ARG A 1 26  ? 6.56969   -32.17873 -11.27877 1.000 17.22862  ? 355 ARG A O   1 
ATOM   199  C CB  . ARG A 1 26  ? 5.19129   -31.47104 -8.65481  1.000 15.13491  ? 355 ARG A CB  1 
ATOM   200  C CG  . ARG A 1 26  ? 4.77022   -30.06781 -9.10325  1.000 16.59240  ? 355 ARG A CG  1 
ATOM   201  C CD  . ARG A 1 26  ? 4.79808   -29.10484 -7.93233  1.000 18.02780  ? 355 ARG A CD  1 
ATOM   202  N NE  . ARG A 1 26  ? 3.66413   -29.38729 -7.06290  1.000 16.42345  ? 355 ARG A NE  1 
ATOM   203  C CZ  . ARG A 1 26  ? 3.32294   -28.60673 -6.04781  1.000 17.50149  ? 355 ARG A CZ  1 
ATOM   204  N NH1 . ARG A 1 26  ? 4.05359   -27.55203 -5.71996  1.000 20.09818  ? 355 ARG A NH1 1 
ATOM   205  N NH2 . ARG A 1 26  ? 2.24750   -28.90350 -5.32650  1.000 18.19644  ? 355 ARG A NH2 1 
ATOM   206  N N   . LYS A 1 27  ? 4.45453   -31.68840 -11.87717 1.000 16.31154  ? 356 LYS A N   1 
ATOM   207  C CA  . LYS A 1 27  ? 4.82378   -31.05548 -13.13188 1.000 18.47213  ? 356 LYS A CA  1 
ATOM   208  C C   . LYS A 1 27  ? 4.20873   -29.66906 -13.16351 1.000 18.75772  ? 356 LYS A C   1 
ATOM   209  O O   . LYS A 1 27  ? 3.02168   -29.50861 -12.88928 1.000 20.11477  ? 356 LYS A O   1 
ATOM   210  C CB  . LYS A 1 27  ? 4.28501   -31.83714 -14.32069 1.000 20.38195  ? 356 LYS A CB  1 
ATOM   211  C CG  . LYS A 1 27  ? 4.69395   -31.13425 -15.60300 1.000 25.10339  ? 356 LYS A CG  1 
ATOM   212  C CD  . LYS A 1 27  ? 4.27710   -31.85639 -16.86604 1.000 29.48518  ? 356 LYS A CD  1 
ATOM   213  C CE  . LYS A 1 27  ? 4.81366   -31.10645 -18.12064 1.000 31.06558  ? 356 LYS A CE  1 
ATOM   214  N NZ  . LYS A 1 27  ? 6.26929   -31.37325 -18.38845 1.000 34.44460  ? 356 LYS A NZ  1 
ATOM   215  N N   . ARG A 1 28  ? 5.02169   -28.66965 -13.48610 1.000 21.31855  ? 357 ARG A N   1 
ATOM   216  C CA  . ARG A 1 28  ? 4.53118   -27.31624 -13.66495 1.000 23.52039  ? 357 ARG A CA  1 
ATOM   217  C C   . ARG A 1 28  ? 4.01760   -27.15166 -15.08548 1.000 25.10730  ? 357 ARG A C   1 
ATOM   218  O O   . ARG A 1 28  ? 4.70629   -27.50016 -16.05049 1.000 27.20137  ? 357 ARG A O   1 
ATOM   219  C CB  . ARG A 1 28  ? 5.64453   -26.30355 -13.41007 1.000 26.92757  ? 357 ARG A CB  1 
ATOM   220  C CG  . ARG A 1 28  ? 5.09491   -24.89730 -13.10957 1.000 33.97047  ? 357 ARG A CG  1 
ATOM   221  C CD  . ARG A 1 28  ? 6.18674   -23.88882 -12.78509 1.000 38.53229  ? 357 ARG A CD  1 
ATOM   222  N NE  . ARG A 1 28  ? 7.15948   -23.83740 -13.86517 1.000 43.61348  ? 357 ARG A NE  1 
ATOM   223  C CZ  . ARG A 1 28  ? 7.19517   -22.89686 -14.80179 1.000 47.81639  ? 357 ARG A CZ  1 
ATOM   224  N NH1 . ARG A 1 28  ? 6.35347   -21.87500 -14.79288 1.000 48.75410  ? 357 ARG A NH1 1 
ATOM   225  N NH2 . ARG A 1 28  ? 8.10130   -22.98321 -15.77216 1.000 49.44297  ? 357 ARG A NH2 1 
ATOM   226  N N   . ILE A 1 29  ? 2.81615   -26.59525 -15.20809 1.000 25.14452  ? 358 ILE A N   1 
ATOM   227  C CA  . ILE A 1 29  ? 2.18171   -26.32436 -16.49508 1.000 25.31518  ? 358 ILE A CA  1 
ATOM   228  C C   . ILE A 1 29  ? 2.06529   -24.81381 -16.64576 1.000 26.16893  ? 358 ILE A C   1 
ATOM   229  O O   . ILE A 1 29  ? 1.56504   -24.12734 -15.74422 1.000 27.26526  ? 358 ILE A O   1 
ATOM   230  C CB  . ILE A 1 29  ? 0.79077   -26.98298 -16.57199 1.000 26.20396  ? 358 ILE A CB  1 
ATOM   231  C CG1 . ILE A 1 29  ? 0.89946   -28.50437 -16.35542 1.000 28.90444  ? 358 ILE A CG1 1 
ATOM   232  C CG2 . ILE A 1 29  ? 0.03857   -26.56716 -17.85763 1.000 26.44913  ? 358 ILE A CG2 1 
ATOM   233  C CD1 . ILE A 1 29  ? 1.25674   -29.26509 -17.60408 1.000 29.98067  ? 358 ILE A CD1 1 
ATOM   234  N N   . SER A 1 30  ? 2.54519   -24.28486 -17.76759 1.000 26.98460  ? 359 SER A N   1 
ATOM   235  C CA  . SER A 1 30  ? 2.48422   -22.84303 -17.96019 1.000 29.92077  ? 359 SER A CA  1 
ATOM   236  C C   . SER A 1 30  ? 2.52115   -22.50455 -19.44527 1.000 28.28497  ? 359 SER A C   1 
ATOM   237  O O   . SER A 1 30  ? 2.90276   -23.32718 -20.28638 1.000 29.64014  ? 359 SER A O   1 
ATOM   238  C CB  . SER A 1 30  ? 3.62929   -22.14403 -17.22561 1.000 34.15742  ? 359 SER A CB  1 
ATOM   239  O OG  . SER A 1 30  ? 4.84113   -22.44833 -17.87360 1.000 37.80542  ? 359 SER A OG  1 
ATOM   240  N N   . ASN A 1 31  ? 2.09031   -21.27897 -19.74892 1.000 28.93233  ? 360 ASN A N   1 
ATOM   241  C CA  . ASN A 1 31  ? 2.18874   -20.70695 -21.08706 1.000 29.60397  ? 360 ASN A CA  1 
ATOM   242  C C   . ASN A 1 31  ? 1.55361   -21.61946 -22.12950 1.000 28.25601  ? 360 ASN A C   1 
ATOM   243  O O   . ASN A 1 31  ? 2.17872   -22.00279 -23.11755 1.000 29.41997  ? 360 ASN A O   1 
ATOM   244  C CB  . ASN A 1 31  ? 3.64406   -20.40102 -21.44097 1.000 33.28263  ? 360 ASN A CB  1 
ATOM   245  C CG  . ASN A 1 31  ? 4.31862   -19.50464 -20.42011 1.000 39.80038  ? 360 ASN A CG  1 
ATOM   246  O OD1 . ASN A 1 31  ? 3.93229   -18.34243 -20.23507 1.000 42.98272  ? 360 ASN A OD1 1 
ATOM   247  N ND2 . ASN A 1 31  ? 5.34432   -20.03574 -19.75924 1.000 42.30867  ? 360 ASN A ND2 1 
ATOM   248  N N   . CYS A 1 32  ? 0.30024   -22.00569 -21.89058 1.000 27.61304  ? 361 CYS A N   1 
ATOM   249  C CA  . CYS A 1 32  ? -0.32287  -22.94889 -22.80391 1.000 27.85751  ? 361 CYS A CA  1 
ATOM   250  C C   . CYS A 1 32  ? -1.83157  -22.83429 -22.64196 1.000 27.83340  ? 361 CYS A C   1 
ATOM   251  O O   . CYS A 1 32  ? -2.33382  -22.18374 -21.72822 1.000 28.80453  ? 361 CYS A O   1 
ATOM   252  C CB  . CYS A 1 32  ? 0.12749   -24.38235 -22.51643 1.000 28.07165  ? 361 CYS A CB  1 
ATOM   253  S SG  . CYS A 1 32  ? -0.11874  -24.86399 -20.79515 1.000 28.39586  ? 361 CYS A SG  1 
ATOM   254  N N   . VAL A 1 33  ? -2.55240  -23.46266 -23.55390 1.000 28.95203  ? 362 VAL A N   1 
ATOM   255  C CA  . VAL A 1 33  ? -4.00963  -23.44797 -23.52921 1.000 30.97126  ? 362 VAL A CA  1 
ATOM   256  C C   . VAL A 1 33  ? -4.45415  -24.85905 -23.17436 1.000 32.68406  ? 362 VAL A C   1 
ATOM   257  O O   . VAL A 1 33  ? -3.94795  -25.84215 -23.73517 1.000 31.58798  ? 362 VAL A O   1 
ATOM   258  C CB  . VAL A 1 33  ? -4.59821  -22.98493 -24.87394 1.000 32.35867  ? 362 VAL A CB  1 
ATOM   259  C CG1 . VAL A 1 33  ? -6.03780  -23.46685 -25.03128 1.000 33.11697  ? 362 VAL A CG1 1 
ATOM   260  C CG2 . VAL A 1 33  ? -4.51105  -21.46368 -25.00193 1.000 36.10293  ? 362 VAL A CG2 1 
ATOM   261  N N   . ALA A 1 34  ? -5.37001  -24.96441 -22.22307 1.000 33.84670  ? 363 ALA A N   1 
ATOM   262  C CA  . ALA A 1 34  ? -5.89400  -26.25129 -21.79577 1.000 38.54455  ? 363 ALA A CA  1 
ATOM   263  C C   . ALA A 1 34  ? -7.39158  -26.29136 -22.04497 1.000 37.78689  ? 363 ALA A C   1 
ATOM   264  O O   . ALA A 1 34  ? -8.11081  -25.35058 -21.69223 1.000 40.76933  ? 363 ALA A O   1 
ATOM   265  C CB  . ALA A 1 34  ? -5.62948  -26.47850 -20.31091 1.000 40.30073  ? 363 ALA A CB  1 
ATOM   266  N N   . ASP A 1 35  ? -7.85616  -27.37765 -22.64854 1.000 30.95241  ? 364 ASP A N   1 
ATOM   267  C CA  . ASP A 1 35  ? -9.28884  -27.69271 -22.69741 1.000 28.46723  ? 364 ASP A CA  1 
ATOM   268  C C   . ASP A 1 35  ? -9.62315  -28.66051 -21.57125 1.000 22.97958  ? 364 ASP A C   1 
ATOM   269  O O   . ASP A 1 35  ? -9.53224  -29.88362 -21.73442 1.000 22.59580  ? 364 ASP A O   1 
ATOM   270  C CB  . ASP A 1 35  ? -9.70467  -28.22554 -24.06164 1.000 30.91516  ? 364 ASP A CB  1 
ATOM   271  C CG  . ASP A 1 35  ? -11.21246 -28.40934 -24.18619 1.000 33.01932  ? 364 ASP A CG  1 
ATOM   272  O OD1 . ASP A 1 35  ? -11.93978 -28.21293 -23.18300 1.000 26.92567  ? 364 ASP A OD1 1 
ATOM   273  O OD2 . ASP A 1 35  ? -11.67658 -28.69305 -25.31214 1.000 34.94656  ? 364 ASP A OD2 1 
ATOM   274  N N   . TYR A 1 36  ? -10.08138 -28.11453 -20.42915 1.000 20.66824  ? 365 TYR A N   1 
ATOM   275  C CA  . TYR A 1 36  ? -10.41599 -28.96474 -19.29716 1.000 17.90914  ? 365 TYR A CA  1 
ATOM   276  C C   . TYR A 1 36  ? -11.62682 -29.83826 -19.56923 1.000 15.97594  ? 365 TYR A C   1 
ATOM   277  O O   . TYR A 1 36  ? -11.84707 -30.81125 -18.83893 1.000 16.04912  ? 365 TYR A O   1 
ATOM   278  C CB  . TYR A 1 36  ? -10.62993 -28.11425 -18.04159 1.000 18.82127  ? 365 TYR A CB  1 
ATOM   279  C CG  . TYR A 1 36  ? -9.35119  -27.43195 -17.64516 1.000 20.04242  ? 365 TYR A CG  1 
ATOM   280  C CD1 . TYR A 1 36  ? -8.34776  -28.12337 -16.98270 1.000 21.45811  ? 365 TYR A CD1 1 
ATOM   281  C CD2 . TYR A 1 36  ? -9.08370  -26.13963 -18.05066 1.000 23.32898  ? 365 TYR A CD2 1 
ATOM   282  C CE1 . TYR A 1 36  ? -7.14987  -27.50840 -16.63084 1.000 23.48075  ? 365 TYR A CE1 1 
ATOM   283  C CE2 . TYR A 1 36  ? -7.88682  -25.52340 -17.73968 1.000 25.96930  ? 365 TYR A CE2 1 
ATOM   284  C CZ  . TYR A 1 36  ? -6.91838  -26.21428 -17.02630 1.000 24.42662  ? 365 TYR A CZ  1 
ATOM   285  O OH  . TYR A 1 36  ? -5.71720  -25.60160 -16.69834 1.000 28.63311  ? 365 TYR A OH  1 
ATOM   286  N N   . SER A 1 37  ? -12.44560 -29.49971 -20.57702 1.000 16.87680  ? 366 SER A N   1 
ATOM   287  C CA  . SER A 1 37  ? -13.63265 -30.31052 -20.83469 1.000 17.16868  ? 366 SER A CA  1 
ATOM   288  C C   . SER A 1 37  ? -13.24015 -31.71469 -21.27264 1.000 17.38287  ? 366 SER A C   1 
ATOM   289  O O   . SER A 1 37  ? -13.95327 -32.67863 -20.98603 1.000 17.02739  ? 366 SER A O   1 
ATOM   290  C CB  . SER A 1 37  ? -14.57853 -29.63009 -21.84940 1.000 19.53375  ? 366 SER A CB  1 
ATOM   291  O OG  . SER A 1 37  ? -14.12458 -29.81642 -23.17606 1.000 20.89787  ? 366 SER A OG  1 
ATOM   292  N N   . VAL A 1 38  ? -12.09624 -31.86438 -21.94617 1.000 17.88491  ? 367 VAL A N   1 
ATOM   293  C CA  . VAL A 1 38  ? -11.65599 -33.19254 -22.33182 1.000 19.03800  ? 367 VAL A CA  1 
ATOM   294  C C   . VAL A 1 38  ? -11.41104 -34.06144 -21.11569 1.000 17.99859  ? 367 VAL A C   1 
ATOM   295  O O   . VAL A 1 38  ? -11.70991 -35.26173 -21.12136 1.000 20.10933  ? 367 VAL A O   1 
ATOM   296  C CB  . VAL A 1 38  ? -10.42163 -33.13241 -23.24078 1.000 22.72980  ? 367 VAL A CB  1 
ATOM   297  C CG1 . VAL A 1 38  ? -10.09406 -34.51587 -23.72430 1.000 26.14062  ? 367 VAL A CG1 1 
ATOM   298  C CG2 . VAL A 1 38  ? -10.73146 -32.26082 -24.49474 1.000 24.73423  ? 367 VAL A CG2 1 
ATOM   299  N N   . LEU A 1 39  ? -10.81149 -33.48948 -20.07445 1.000 17.20629  ? 368 LEU A N   1 
ATOM   300  C CA  . LEU A 1 39  ? -10.58445 -34.26115 -18.85853 1.000 15.96877  ? 368 LEU A CA  1 
ATOM   301  C C   . LEU A 1 39  ? -11.91206 -34.52773 -18.16056 1.000 15.63643  ? 368 LEU A C   1 
ATOM   302  O O   . LEU A 1 39  ? -12.17944 -35.64756 -17.70531 1.000 15.82064  ? 368 LEU A O   1 
ATOM   303  C CB  . LEU A 1 39  ? -9.62890  -33.48505 -17.94764 1.000 16.51711  ? 368 LEU A CB  1 
ATOM   304  C CG  . LEU A 1 39  ? -8.26145  -33.14228 -18.55259 1.000 19.73108  ? 368 LEU A CG  1 
ATOM   305  C CD1 . LEU A 1 39  ? -7.43980  -32.38071 -17.53621 1.000 20.92987  ? 368 LEU A CD1 1 
ATOM   306  C CD2 . LEU A 1 39  ? -7.52114  -34.43978 -18.92265 1.000 21.09538  ? 368 LEU A CD2 1 
ATOM   307  N N   . TYR A 1 40  ? -12.74165 -33.49058 -18.01092 1.000 14.81704  ? 369 TYR A N   1 
ATOM   308  C CA  . TYR A 1 40  ? -13.99540 -33.62167 -17.28049 1.000 13.68737  ? 369 TYR A CA  1 
ATOM   309  C C   . TYR A 1 40  ? -14.90172 -34.66321 -17.91506 1.000 14.88619  ? 369 TYR A C   1 
ATOM   310  O O   . TYR A 1 40  ? -15.59342 -35.41820 -17.21029 1.000 14.81916  ? 369 TYR A O   1 
ATOM   311  C CB  . TYR A 1 40  ? -14.69171 -32.27552 -17.28187 1.000 14.81134  ? 369 TYR A CB  1 
ATOM   312  C CG  . TYR A 1 40  ? -15.93533 -32.19665 -16.41711 1.000 13.57669  ? 369 TYR A CG  1 
ATOM   313  C CD1 . TYR A 1 40  ? -15.83954 -32.20466 -15.02354 1.000 15.26563  ? 369 TYR A CD1 1 
ATOM   314  C CD2 . TYR A 1 40  ? -17.20811 -32.12214 -16.98487 1.000 15.19450  ? 369 TYR A CD2 1 
ATOM   315  C CE1 . TYR A 1 40  ? -16.96732 -32.10523 -14.22525 1.000 15.46548  ? 369 TYR A CE1 1 
ATOM   316  C CE2 . TYR A 1 40  ? -18.33366 -32.01621 -16.20574 1.000 16.35067  ? 369 TYR A CE2 1 
ATOM   317  C CZ  . TYR A 1 40  ? -18.21677 -31.98267 -14.82885 1.000 15.83992  ? 369 TYR A CZ  1 
ATOM   318  O OH  . TYR A 1 40  ? -19.37755 -31.89279 -14.05984 1.000 18.16328  ? 369 TYR A OH  1 
ATOM   319  N N   . ASN A 1 41  ? -14.91051 -34.72276 -19.24737 1.000 13.62289  ? 370 ASN A N   1 
ATOM   320  C CA  . ASN A 1 41  ? -15.83986 -35.60552 -19.92790 1.000 15.37225  ? 370 ASN A CA  1 
ATOM   321  C C   . ASN A 1 41  ? -15.27939 -36.98977 -20.16402 1.000 17.76488  ? 370 ASN A C   1 
ATOM   322  O O   . ASN A 1 41  ? -16.00738 -37.84659 -20.66129 1.000 22.68470  ? 370 ASN A O   1 
ATOM   323  C CB  . ASN A 1 41  ? -16.31584 -34.97905 -21.22719 1.000 15.69461  ? 370 ASN A CB  1 
ATOM   324  C CG  . ASN A 1 41  ? -17.17996 -33.76617 -20.96721 1.000 15.86059  ? 370 ASN A CG  1 
ATOM   325  O OD1 . ASN A 1 41  ? -18.00636 -33.84408 -20.05555 1.000 16.50550  ? 370 ASN A OD1 1 
ATOM   326  N ND2 . ASN A 1 41  ? -17.10555 -32.73393 -21.80361 1.000 16.96979  ? 370 ASN A ND2 1 
ATOM   327  N N   . SER A 1 42  ? -14.02839 -37.22854 -19.81773 1.000 16.72550  ? 371 SER A N   1 
ATOM   328  C CA  . SER A 1 42  ? -13.45638 -38.55336 -20.04600 1.000 16.66958  ? 371 SER A CA  1 
ATOM   329  C C   . SER A 1 42  ? -14.11039 -39.63221 -19.18154 1.000 16.43546  ? 371 SER A C   1 
ATOM   330  O O   . SER A 1 42  ? -14.09872 -39.54637 -17.95540 1.000 18.96553  ? 371 SER A O   1 
ATOM   331  C CB  . SER A 1 42  ? -11.96576 -38.52749 -19.73902 1.000 19.63120  ? 371 SER A CB  1 
ATOM   332  O OG  . SER A 1 42  ? -11.47763 -39.81194 -19.97884 1.000 23.26115  ? 371 SER A OG  1 
ATOM   333  N N   . ALA A 1 43  ? -14.57877 -40.71435 -19.81556 1.000 16.94665  ? 372 ALA A N   1 
ATOM   334  C CA  . ALA A 1 43  ? -15.14516 -41.84274 -19.09359 1.000 18.54344  ? 372 ALA A CA  1 
ATOM   335  C C   . ALA A 1 43  ? -14.09972 -42.58486 -18.28366 1.000 16.78110  ? 372 ALA A C   1 
ATOM   336  O O   . ALA A 1 43  ? -14.45609 -43.39220 -17.43044 1.000 22.21482  ? 372 ALA A O   1 
ATOM   337  C CB  . ALA A 1 43  ? -15.83524 -42.79923 -20.05254 1.000 21.69359  ? 372 ALA A CB  1 
ATOM   338  N N   . SER A 1 44  ? -12.82576 -42.32417 -18.51260 1.000 17.05304  ? 373 SER A N   1 
ATOM   339  C CA  A SER A 1 44  ? -11.77334 -43.02915 -17.78697 0.500 19.83987  ? 373 SER A CA  1 
ATOM   340  C CA  B SER A 1 44  ? -11.78700 -43.04561 -17.78108 0.500 19.94146  ? 373 SER A CA  1 
ATOM   341  C C   . SER A 1 44  ? -11.67808 -42.61907 -16.32296 1.000 18.78177  ? 373 SER A C   1 
ATOM   342  O O   . SER A 1 44  ? -11.14464 -43.36880 -15.51646 1.000 23.61125  ? 373 SER A O   1 
ATOM   343  C CB  A SER A 1 44  ? -10.43605 -42.78329 -18.47877 0.500 22.94714  ? 373 SER A CB  1 
ATOM   344  C CB  B SER A 1 44  ? -10.43003 -42.86283 -18.45944 0.500 23.96165  ? 373 SER A CB  1 
ATOM   345  O OG  A SER A 1 44  ? -10.47762 -43.29205 -19.80740 0.500 24.65356  ? 373 SER A OG  1 
ATOM   346  O OG  B SER A 1 44  ? -9.99782  -41.52122 -18.43351 0.500 28.61318  ? 373 SER A OG  1 
ATOM   347  N N   . PHE A 1 45  ? -12.15506 -41.43426 -15.96291 1.000 15.64116  ? 374 PHE A N   1 
ATOM   348  C CA  . PHE A 1 45  ? -11.88508 -40.90790 -14.62757 1.000 15.49817  ? 374 PHE A CA  1 
ATOM   349  C C   . PHE A 1 45  ? -13.10785 -41.11571 -13.75848 1.000 17.64207  ? 374 PHE A C   1 
ATOM   350  O O   . PHE A 1 45  ? -14.18045 -40.61925 -14.08017 1.000 22.34782  ? 374 PHE A O   1 
ATOM   351  C CB  . PHE A 1 45  ? -11.50773 -39.43237 -14.65946 1.000 15.70996  ? 374 PHE A CB  1 
ATOM   352  C CG  . PHE A 1 45  ? -10.32600 -39.13169 -15.51803 1.000 15.06159  ? 374 PHE A CG  1 
ATOM   353  C CD1 . PHE A 1 45  ? -9.15031  -39.88900 -15.43548 1.000 16.78754  ? 374 PHE A CD1 1 
ATOM   354  C CD2 . PHE A 1 45  ? -10.36535 -38.06343 -16.40364 1.000 18.26075  ? 374 PHE A CD2 1 
ATOM   355  C CE1 . PHE A 1 45  ? -8.06021  -39.59202 -16.24024 1.000 16.79666  ? 374 PHE A CE1 1 
ATOM   356  C CE2 . PHE A 1 45  ? -9.26234  -37.77787 -17.20750 1.000 19.79055  ? 374 PHE A CE2 1 
ATOM   357  C CZ  . PHE A 1 45  ? -8.10479  -38.56456 -17.12655 1.000 17.43825  ? 374 PHE A CZ  1 
ATOM   358  N N   . SER A 1 46  ? -12.95679 -41.87722 -12.69348 1.000 16.36520  ? 375 SER A N   1 
ATOM   359  C CA  . SER A 1 46  ? -14.06387 -42.12430 -11.78276 1.000 18.21526  ? 375 SER A CA  1 
ATOM   360  C C   . SER A 1 46  ? -14.17405 -41.10063 -10.66776 1.000 16.95015  ? 375 SER A C   1 
ATOM   361  O O   . SER A 1 46  ? -15.24610 -40.98120 -10.06037 1.000 20.05244  ? 375 SER A O   1 
ATOM   362  C CB  . SER A 1 46  ? -13.97925 -43.53927 -11.22757 1.000 19.16941  ? 375 SER A CB  1 
ATOM   363  O OG  . SER A 1 46  ? -12.69512 -43.75685 -10.68771 1.000 18.82815  ? 375 SER A OG  1 
ATOM   364  N N   . THR A 1 47  ? -13.11932 -40.33966 -10.39687 1.000 14.58102  ? 376 THR A N   1 
ATOM   365  C CA  . THR A 1 47  ? -13.19441 -39.19238 -9.50430  1.000 14.00204  ? 376 THR A CA  1 
ATOM   366  C C   . THR A 1 47  ? -12.82048 -37.95609 -10.31394 1.000 13.46600  ? 376 THR A C   1 
ATOM   367  O O   . THR A 1 47  ? -11.79781 -37.96391 -11.01764 1.000 13.64833  ? 376 THR A O   1 
ATOM   368  C CB  . THR A 1 47  ? -12.17488 -39.35343 -8.36923  1.000 15.25585  ? 376 THR A CB  1 
ATOM   369  O OG1 . THR A 1 47  ? -12.60008 -40.41170 -7.51651  1.000 17.09206  ? 376 THR A OG1 1 
ATOM   370  C CG2 . THR A 1 47  ? -12.10558 -38.08923 -7.50651  1.000 16.79285  ? 376 THR A CG2 1 
ATOM   371  N N   . PHE A 1 48  ? -13.61605 -36.89646 -10.20002 1.000 13.60321  ? 377 PHE A N   1 
ATOM   372  C CA  . PHE A 1 48  ? -13.27381 -35.58691 -10.75677 1.000 13.47018  ? 377 PHE A CA  1 
ATOM   373  C C   . PHE A 1 48  ? -13.96687 -34.58321 -9.84266  1.000 13.13745  ? 377 PHE A C   1 
ATOM   374  O O   . PHE A 1 48  ? -15.16839 -34.34335 -9.97010  1.000 15.25656  ? 377 PHE A O   1 
ATOM   375  C CB  . PHE A 1 48  ? -13.73010 -35.44342 -12.20635 1.000 15.74876  ? 377 PHE A CB  1 
ATOM   376  C CG  . PHE A 1 48  ? -13.05505 -34.32467 -12.93029 1.000 15.48483  ? 377 PHE A CG  1 
ATOM   377  C CD1 . PHE A 1 48  ? -13.19003 -33.00408 -12.48843 1.000 17.49677  ? 377 PHE A CD1 1 
ATOM   378  C CD2 . PHE A 1 48  ? -12.27480 -34.57311 -14.04349 1.000 18.07499  ? 377 PHE A CD2 1 
ATOM   379  C CE1 . PHE A 1 48  ? -12.55624 -31.96888 -13.12084 1.000 18.97543  ? 377 PHE A CE1 1 
ATOM   380  C CE2 . PHE A 1 48  ? -11.63230 -33.52247 -14.67339 1.000 20.40061  ? 377 PHE A CE2 1 
ATOM   381  C CZ  . PHE A 1 48  ? -11.78309 -32.23904 -14.22302 1.000 20.14187  ? 377 PHE A CZ  1 
ATOM   382  N N   . LYS A 1 49  ? -13.21639 -34.08681 -8.85850  1.000 12.99102  ? 378 LYS A N   1 
ATOM   383  C CA  . LYS A 1 49  ? -13.78940 -33.25051 -7.81863  1.000 14.50690  ? 378 LYS A CA  1 
ATOM   384  C C   . LYS A 1 49  ? -12.98446 -31.96042 -7.71690  1.000 13.50237  ? 378 LYS A C   1 
ATOM   385  O O   . LYS A 1 49  ? -11.75262 -31.99986 -7.57383  1.000 15.50761  ? 378 LYS A O   1 
ATOM   386  C CB  . LYS A 1 49  ? -13.73969 -33.99802 -6.48471  1.000 15.14614  ? 378 LYS A CB  1 
ATOM   387  C CG  . LYS A 1 49  ? -14.83734 -35.03543 -6.33633  1.000 18.72131  ? 378 LYS A CG  1 
ATOM   388  C CD  . LYS A 1 49  ? -14.67903 -35.89246 -5.09333  1.000 23.07546  ? 378 LYS A CD  1 
ATOM   389  C CE  . LYS A 1 49  ? -15.62795 -37.09042 -5.10920  1.000 26.06747  ? 378 LYS A CE  1 
ATOM   390  N NZ  . LYS A 1 49  ? -15.69746 -37.68864 -3.73581  1.000 30.70207  ? 378 LYS A NZ  1 
ATOM   391  N N   . CYS A 1 50  ? -13.66833 -30.81574 -7.73250  1.000 14.27798  ? 379 CYS A N   1 
ATOM   392  C CA  . CYS A 1 50  ? -12.96260 -29.54084 -7.67789  1.000 15.42198  ? 379 CYS A CA  1 
ATOM   393  C C   . CYS A 1 50  ? -13.31016 -28.78345 -6.40764  1.000 15.53535  ? 379 CYS A C   1 
ATOM   394  O O   . CYS A 1 50  ? -14.35877 -28.98754 -5.81270  1.000 16.60751  ? 379 CYS A O   1 
ATOM   395  C CB  . CYS A 1 50  ? -13.29899 -28.65876 -8.87920  1.000 17.97307  ? 379 CYS A CB  1 
ATOM   396  S SG  . CYS A 1 50  ? -12.82231 -29.43007 -10.45003 1.000 18.11790  ? 379 CYS A SG  1 
ATOM   397  N N   . TYR A 1 51  ? -12.37624 -27.93344 -6.00083  1.000 15.35587  ? 380 TYR A N   1 
ATOM   398  C CA  . TYR A 1 51  ? -12.45244 -27.19782 -4.74997  1.000 16.55036  ? 380 TYR A CA  1 
ATOM   399  C C   . TYR A 1 51  ? -12.04230 -25.76351 -5.01647  1.000 17.53130  ? 380 TYR A C   1 
ATOM   400  O O   . TYR A 1 51  ? -11.08683 -25.52960 -5.76289  1.000 17.85039  ? 380 TYR A O   1 
ATOM   401  C CB  . TYR A 1 51  ? -11.53385 -27.82890 -3.67353  1.000 16.83825  ? 380 TYR A CB  1 
ATOM   402  C CG  . TYR A 1 51  ? -11.84800 -29.28847 -3.45000  1.000 16.05069  ? 380 TYR A CG  1 
ATOM   403  C CD1 . TYR A 1 51  ? -11.24522 -30.30273 -4.21243  1.000 15.06097  ? 380 TYR A CD1 1 
ATOM   404  C CD2 . TYR A 1 51  ? -12.84284 -29.64973 -2.53254  1.000 17.03915  ? 380 TYR A CD2 1 
ATOM   405  C CE1 . TYR A 1 51  ? -11.59460 -31.62339 -4.03099  1.000 15.30621  ? 380 TYR A CE1 1 
ATOM   406  C CE2 . TYR A 1 51  ? -13.19589 -30.96270 -2.33494  1.000 16.32234  ? 380 TYR A CE2 1 
ATOM   407  C CZ  . TYR A 1 51  ? -12.56626 -31.95560 -3.09480  1.000 14.94243  ? 380 TYR A CZ  1 
ATOM   408  O OH  . TYR A 1 51  ? -12.91222 -33.29102 -2.92825  1.000 16.07746  ? 380 TYR A OH  1 
ATOM   409  N N   . GLY A 1 52  ? -12.80026 -24.80151 -4.46560  1.000 18.01036  ? 381 GLY A N   1 
ATOM   410  C CA  . GLY A 1 52  ? -12.43565 -23.40812 -4.66661  1.000 19.07180  ? 381 GLY A CA  1 
ATOM   411  C C   . GLY A 1 52  ? -12.73916 -22.87332 -6.04388  1.000 20.72318  ? 381 GLY A C   1 
ATOM   412  O O   . GLY A 1 52  ? -12.51148 -21.67995 -6.30365  1.000 23.30753  ? 381 GLY A O   1 
ATOM   413  N N   . VAL A 1 53  ? -13.28593 -23.70242 -6.92444  1.000 20.34102  ? 382 VAL A N   1 
ATOM   414  C CA  . VAL A 1 53  ? -13.61090 -23.30516 -8.28712  1.000 19.39714  ? 382 VAL A CA  1 
ATOM   415  C C   . VAL A 1 53  ? -14.63358 -24.31299 -8.75857  1.000 19.59259  ? 382 VAL A C   1 
ATOM   416  O O   . VAL A 1 53  ? -14.59190 -25.46954 -8.35886  1.000 20.92025  ? 382 VAL A O   1 
ATOM   417  C CB  . VAL A 1 53  ? -12.35010 -23.30381 -9.18828  1.000 21.00410  ? 382 VAL A CB  1 
ATOM   418  C CG1 . VAL A 1 53  ? -11.71910 -24.67266 -9.23972  1.000 21.63006  ? 382 VAL A CG1 1 
ATOM   419  C CG2 . VAL A 1 53  ? -12.65829 -22.80354 -10.60433 1.000 24.28537  ? 382 VAL A CG2 1 
ATOM   420  N N   . SER A 1 54  ? -15.56536 -23.86734 -9.61503  1.000 21.56108  ? 383 SER A N   1 
ATOM   421  C CA  . SER A 1 54  ? -16.54668 -24.80702 -10.13358 1.000 22.27088  ? 383 SER A CA  1 
ATOM   422  C C   . SER A 1 54  ? -16.04024 -25.35285 -11.46930 1.000 19.07080  ? 383 SER A C   1 
ATOM   423  O O   . SER A 1 54  ? -15.45302 -24.61150 -12.25775 1.000 18.95694  ? 383 SER A O   1 
ATOM   424  C CB  . SER A 1 54  ? -17.90601 -24.11201 -10.36375 1.000 24.51134  ? 383 SER A CB  1 
ATOM   425  O OG  . SER A 1 54  ? -18.63915 -24.68682 -11.43758 1.000 28.60491  ? 383 SER A OG  1 
ATOM   426  N N   . PRO A 1 55  ? -16.26172 -26.63214 -11.77781 1.000 18.70634  ? 384 PRO A N   1 
ATOM   427  C CA  . PRO A 1 55  ? -15.90821 -27.11970 -13.11377 1.000 19.13622  ? 384 PRO A CA  1 
ATOM   428  C C   . PRO A 1 55  ? -16.45684 -26.29190 -14.23920 1.000 18.07166  ? 384 PRO A C   1 
ATOM   429  O O   . PRO A 1 55  ? -15.78437 -26.18414 -15.27236 1.000 18.73947  ? 384 PRO A O   1 
ATOM   430  C CB  . PRO A 1 55  ? -16.36778 -28.58581 -13.12270 1.000 21.74479  ? 384 PRO A CB  1 
ATOM   431  C CG  . PRO A 1 55  ? -17.06090 -28.82546 -11.83494 1.000 25.13538  ? 384 PRO A CG  1 
ATOM   432  C CD  . PRO A 1 55  ? -16.87240 -27.65152 -10.91335 1.000 19.91485  ? 384 PRO A CD  1 
ATOM   433  N N   . THR A 1 56  ? -17.65658 -25.71356 -14.08272 1.000 17.32969  ? 385 THR A N   1 
ATOM   434  C CA  . THR A 1 56  ? -18.25748 -24.99584 -15.18740 1.000 18.90554  ? 385 THR A CA  1 
ATOM   435  C C   . THR A 1 56  ? -17.40457 -23.81411 -15.60568 1.000 20.31545  ? 385 THR A C   1 
ATOM   436  O O   . THR A 1 56  ? -17.60364 -23.30002 -16.71173 1.000 23.74904  ? 385 THR A O   1 
ATOM   437  C CB  . THR A 1 56  ? -19.62111 -24.43367 -14.79117 1.000 19.51020  ? 385 THR A CB  1 
ATOM   438  O OG1 . THR A 1 56  ? -19.52110 -23.73948 -13.55183 1.000 22.86671  ? 385 THR A OG1 1 
ATOM   439  C CG2 . THR A 1 56  ? -20.60894 -25.55607 -14.61283 1.000 21.18085  ? 385 THR A CG2 1 
ATOM   440  N N   . LYS A 1 57  ? -16.47807 -23.35372 -14.74713 1.000 20.83808  ? 386 LYS A N   1 
ATOM   441  C CA  . LYS A 1 57  ? -15.69122 -22.16938 -15.05806 1.000 23.46562  ? 386 LYS A CA  1 
ATOM   442  C C   . LYS A 1 57  ? -14.29535 -22.48723 -15.60048 1.000 22.77119  ? 386 LYS A C   1 
ATOM   443  O O   . LYS A 1 57  ? -13.58729 -21.56659 -16.02382 1.000 25.29991  ? 386 LYS A O   1 
ATOM   444  C CB  . LYS A 1 57  ? -15.55625 -21.29406 -13.80570 1.000 29.31113  ? 386 LYS A CB  1 
ATOM   445  C CG  . LYS A 1 57  ? -16.79938 -20.50519 -13.48442 1.000 35.57183  ? 386 LYS A CG  1 
ATOM   446  C CD  . LYS A 1 57  ? -16.49980 -19.32504 -12.56303 1.000 39.51964  ? 386 LYS A CD  1 
ATOM   447  C CE  . LYS A 1 57  ? -17.53019 -18.21149 -12.70711 1.000 41.17628  ? 386 LYS A CE  1 
ATOM   448  N NZ  . LYS A 1 57  ? -17.28475 -17.34063 -13.90311 1.000 41.88015  ? 386 LYS A NZ  1 
ATOM   449  N N   . LEU A 1 58  ? -13.87922 -23.75451 -15.62295 1.000 20.25689  ? 387 LEU A N   1 
ATOM   450  C CA  . LEU A 1 58  ? -12.46112 -24.05596 -15.85941 1.000 21.48882  ? 387 LEU A CA  1 
ATOM   451  C C   . LEU A 1 58  ? -12.00495 -23.59069 -17.24077 1.000 23.56183  ? 387 LEU A C   1 
ATOM   452  O O   . LEU A 1 58  ? -10.83023 -23.23810 -17.41374 1.000 26.98463  ? 387 LEU A O   1 
ATOM   453  C CB  . LEU A 1 58  ? -12.27565 -25.56927 -15.72356 1.000 20.01163  ? 387 LEU A CB  1 
ATOM   454  C CG  . LEU A 1 58  ? -12.36545 -26.14772 -14.31986 1.000 21.73360  ? 387 LEU A CG  1 
ATOM   455  C CD1 . LEU A 1 58  ? -11.89161 -27.53464 -14.28477 1.000 23.18444  ? 387 LEU A CD1 1 
ATOM   456  C CD2 . LEU A 1 58  ? -11.43533 -25.34332 -13.38894 1.000 24.83049  ? 387 LEU A CD2 1 
ATOM   457  N N   . ASN A 1 59  ? -12.88662 -23.62519 -18.25265 1.000 22.92994  ? 388 ASN A N   1 
ATOM   458  C CA  . ASN A 1 59  ? -12.49275 -23.18439 -19.58398 1.000 25.25477  ? 388 ASN A CA  1 
ATOM   459  C C   . ASN A 1 59  ? -12.62232 -21.68643 -19.76537 1.000 26.72727  ? 388 ASN A C   1 
ATOM   460  O O   . ASN A 1 59  ? -12.26847 -21.17977 -20.83215 1.000 28.93863  ? 388 ASN A O   1 
ATOM   461  C CB  . ASN A 1 59  ? -13.26743 -23.94864 -20.65944 1.000 25.23646  ? 388 ASN A CB  1 
ATOM   462  C CG  . ASN A 1 59  ? -12.53769 -25.22516 -21.09211 1.000 24.00980  ? 388 ASN A CG  1 
ATOM   463  O OD1 . ASN A 1 59  ? -11.49351 -25.57977 -20.53915 1.000 27.75912  ? 388 ASN A OD1 1 
ATOM   464  N ND2 . ASN A 1 59  ? -13.12261 -25.94653 -22.04577 1.000 23.97356  ? 388 ASN A ND2 1 
ATOM   465  N N   . ASP A 1 60  ? -13.04562 -20.97090 -18.72504 1.000 28.23385  ? 389 ASP A N   1 
ATOM   466  C CA  . ASP A 1 60  ? -13.21871 -19.53339 -18.81632 1.000 31.65174  ? 389 ASP A CA  1 
ATOM   467  C C   . ASP A 1 60  ? -12.23081 -18.76434 -17.96498 1.000 33.02876  ? 389 ASP A C   1 
ATOM   468  O O   . ASP A 1 60  ? -12.29907 -17.53402 -17.91697 1.000 36.89724  ? 389 ASP A O   1 
ATOM   469  C CB  . ASP A 1 60  ? -14.63692 -19.12965 -18.40675 1.000 37.56283  ? 389 ASP A CB  1 
ATOM   470  C CG  . ASP A 1 60  ? -15.68307 -19.76045 -19.27458 1.000 42.42440  ? 389 ASP A CG  1 
ATOM   471  O OD1 . ASP A 1 60  ? -15.79236 -19.35964 -20.44568 1.000 45.05157  ? 389 ASP A OD1 1 
ATOM   472  O OD2 . ASP A 1 60  ? -16.40367 -20.65276 -18.77757 1.000 45.30619  ? 389 ASP A OD2 1 
ATOM   473  N N   . LEU A 1 61  ? -11.30831 -19.43875 -17.30684 1.000 32.27924  ? 390 LEU A N   1 
ATOM   474  C CA  . LEU A 1 61  ? -10.41638 -18.78745 -16.37155 1.000 31.57907  ? 390 LEU A CA  1 
ATOM   475  C C   . LEU A 1 61  ? -8.98990  -18.88893 -16.87778 1.000 31.66931  ? 390 LEU A C   1 
ATOM   476  O O   . LEU A 1 61  ? -8.64116  -19.78926 -17.65004 1.000 32.17828  ? 390 LEU A O   1 
ATOM   477  C CB  . LEU A 1 61  ? -10.51152 -19.44605 -14.99670 1.000 32.48568  ? 390 LEU A CB  1 
ATOM   478  C CG  . LEU A 1 61  ? -11.84896 -19.25272 -14.27346 1.000 34.76115  ? 390 LEU A CG  1 
ATOM   479  C CD1 . LEU A 1 61  ? -11.91349 -20.14407 -13.04267 1.000 34.75855  ? 390 LEU A CD1 1 
ATOM   480  C CD2 . LEU A 1 61  ? -12.03733 -17.80472 -13.88286 1.000 35.35673  ? 390 LEU A CD2 1 
ATOM   481  N N   . CYS A 1 62  ? -8.15772  -17.96970 -16.41306 1.000 29.62548  ? 391 CYS A N   1 
ATOM   482  C CA  . CYS A 1 62  ? -6.72929  -18.02811 -16.67004 1.000 30.34437  ? 391 CYS A CA  1 
ATOM   483  C C   . CYS A 1 62  ? -6.01902  -18.01783 -15.32953 1.000 29.85632  ? 391 CYS A C   1 
ATOM   484  O O   . CYS A 1 62  ? -6.46425  -17.35087 -14.38843 1.000 30.96042  ? 391 CYS A O   1 
ATOM   485  C CB  . CYS A 1 62  ? -6.27273  -16.80558 -17.44548 1.000 33.17315  ? 391 CYS A CB  1 
ATOM   486  S SG  . CYS A 1 62  ? -6.80902  -16.76801 -19.18120 1.000 37.50240  ? 391 CYS A SG  1 
ATOM   487  N N   . PHE A 1 63  ? -4.91504  -18.75913 -15.24345 1.000 27.56861  ? 392 PHE A N   1 
ATOM   488  C CA  . PHE A 1 63  ? -4.12429  -18.86125 -14.02466 1.000 27.78393  ? 392 PHE A CA  1 
ATOM   489  C C   . PHE A 1 63  ? -2.66543  -18.55580 -14.33052 1.000 28.57357  ? 392 PHE A C   1 
ATOM   490  O O   . PHE A 1 63  ? -2.21944  -18.66805 -15.47316 1.000 30.40937  ? 392 PHE A O   1 
ATOM   491  C CB  . PHE A 1 63  ? -4.30555  -20.24552 -13.39633 1.000 26.71044  ? 392 PHE A CB  1 
ATOM   492  C CG  . PHE A 1 63  ? -5.65812  -20.42390 -12.81776 1.000 26.58974  ? 392 PHE A CG  1 
ATOM   493  C CD1 . PHE A 1 63  ? -5.98353  -19.80177 -11.61226 1.000 28.20799  ? 392 PHE A CD1 1 
ATOM   494  C CD2 . PHE A 1 63  ? -6.64710  -21.10853 -13.51077 1.000 26.43044  ? 392 PHE A CD2 1 
ATOM   495  C CE1 . PHE A 1 63  ? -7.25267  -19.92067 -11.06865 1.000 28.53273  ? 392 PHE A CE1 1 
ATOM   496  C CE2 . PHE A 1 63  ? -7.92761  -21.22662 -12.97781 1.000 26.29884  ? 392 PHE A CE2 1 
ATOM   497  C CZ  . PHE A 1 63  ? -8.22158  -20.63564 -11.75029 1.000 27.81157  ? 392 PHE A CZ  1 
ATOM   498  N N   . THR A 1 64  ? -1.92750  -18.15579 -13.28644 1.000 29.35527  ? 393 THR A N   1 
ATOM   499  C CA  . THR A 1 64  ? -0.50002  -17.87716 -13.44667 1.000 31.51284  ? 393 THR A CA  1 
ATOM   500  C C   . THR A 1 64  ? 0.27346   -19.15998 -13.76071 1.000 29.53517  ? 393 THR A C   1 
ATOM   501  O O   . THR A 1 64  ? 1.11611   -19.19907 -14.67045 1.000 31.11838  ? 393 THR A O   1 
ATOM   502  C CB  . THR A 1 64  ? 0.03721   -17.23693 -12.16355 1.000 35.92524  ? 393 THR A CB  1 
ATOM   503  O OG1 . THR A 1 64  ? -0.87478  -16.22618 -11.69700 1.000 38.32641  ? 393 THR A OG1 1 
ATOM   504  C CG2 . THR A 1 64  ? 1.40411   -16.59596 -12.43033 1.000 37.03022  ? 393 THR A CG2 1 
ATOM   505  N N   . ASN A 1 65  ? -0.01685  -20.22952 -13.01969 1.000 29.52507  ? 394 ASN A N   1 
ATOM   506  C CA  . ASN A 1 65  ? 0.57089   -21.54399 -13.22927 1.000 27.80710  ? 394 ASN A CA  1 
ATOM   507  C C   . ASN A 1 65  ? -0.47715  -22.58155 -12.86633 1.000 25.27505  ? 394 ASN A C   1 
ATOM   508  O O   . ASN A 1 65  ? -1.37858  -22.32390 -12.06390 1.000 25.01129  ? 394 ASN A O   1 
ATOM   509  C CB  . ASN A 1 65  ? 1.78586   -21.77234 -12.31013 1.000 29.69768  ? 394 ASN A CB  1 
ATOM   510  C CG  . ASN A 1 65  ? 2.90987   -20.78446 -12.55547 1.000 34.16425  ? 394 ASN A CG  1 
ATOM   511  O OD1 . ASN A 1 65  ? 3.50179   -20.75651 -13.63774 1.000 36.28718  ? 394 ASN A OD1 1 
ATOM   512  N ND2 . ASN A 1 65  ? 3.16924   -19.93215 -11.56911 1.000 35.53645  ? 394 ASN A ND2 1 
ATOM   513  N N   . VAL A 1 66  ? -0.33761  -23.76961 -13.43422 1.000 23.83089  ? 395 VAL A N   1 
ATOM   514  C CA  . VAL A 1 66  ? -1.05379  -24.94001 -12.94846 1.000 21.33594  ? 395 VAL A CA  1 
ATOM   515  C C   . VAL A 1 66  ? 0.00429   -25.95110 -12.55579 1.000 20.54476  ? 395 VAL A C   1 
ATOM   516  O O   . VAL A 1 66  ? 1.02050   -26.09904 -13.23875 1.000 23.36111  ? 395 VAL A O   1 
ATOM   517  C CB  . VAL A 1 66  ? -2.02107  -25.50318 -14.01761 1.000 22.67217  ? 395 VAL A CB  1 
ATOM   518  C CG1 . VAL A 1 66  ? -2.69636  -26.79201 -13.54731 1.000 23.86252  ? 395 VAL A CG1 1 
ATOM   519  C CG2 . VAL A 1 66  ? -3.07829  -24.44818 -14.35739 1.000 24.13607  ? 395 VAL A CG2 1 
ATOM   520  N N   . TYR A 1 67  ? -0.18629  -26.59833 -11.41971 1.000 18.00628  ? 396 TYR A N   1 
ATOM   521  C CA  . TYR A 1 67  ? 0.66772   -27.71108 -11.03202 1.000 18.09475  ? 396 TYR A CA  1 
ATOM   522  C C   . TYR A 1 67  ? -0.13191  -28.99655 -11.13832 1.000 17.60769  ? 396 TYR A C   1 
ATOM   523  O O   . TYR A 1 67  ? -1.32141  -29.03031 -10.79858 1.000 18.81794  ? 396 TYR A O   1 
ATOM   524  C CB  . TYR A 1 67  ? 1.20000   -27.53974 -9.60503  1.000 20.91271  ? 396 TYR A CB  1 
ATOM   525  C CG  . TYR A 1 67  ? 1.99009   -26.27072 -9.47871  1.000 24.74077  ? 396 TYR A CG  1 
ATOM   526  C CD1 . TYR A 1 67  ? 3.31267   -26.19690 -9.87670  1.000 28.44172  ? 396 TYR A CD1 1 
ATOM   527  C CD2 . TYR A 1 67  ? 1.36608   -25.11211 -9.03302  1.000 28.88892  ? 396 TYR A CD2 1 
ATOM   528  C CE1 . TYR A 1 67  ? 4.02379   -24.97961 -9.78725  1.000 30.58525  ? 396 TYR A CE1 1 
ATOM   529  C CE2 . TYR A 1 67  ? 2.04390   -23.91279 -8.93507  1.000 32.39439  ? 396 TYR A CE2 1 
ATOM   530  C CZ  . TYR A 1 67  ? 3.36536   -23.84504 -9.31239  1.000 32.67516  ? 396 TYR A CZ  1 
ATOM   531  O OH  . TYR A 1 67  ? 4.01534   -22.62251 -9.21261  1.000 36.40063  ? 396 TYR A OH  1 
ATOM   532  N N   . ALA A 1 68  ? 0.52166   -30.04790 -11.61282 1.000 16.75123  ? 397 ALA A N   1 
ATOM   533  C CA  . ALA A 1 68  ? -0.12015  -31.35185 -11.70431 1.000 15.35349  ? 397 ALA A CA  1 
ATOM   534  C C   . ALA A 1 68  ? 0.70739   -32.31306 -10.87360 1.000 13.96431  ? 397 ALA A C   1 
ATOM   535  O O   . ALA A 1 68  ? 1.83837   -32.63619 -11.25118 1.000 15.74493  ? 397 ALA A O   1 
ATOM   536  C CB  . ALA A 1 68  ? -0.19812  -31.82257 -13.15113 1.000 17.05762  ? 397 ALA A CB  1 
ATOM   537  N N   . ASP A 1 69  ? 0.16245   -32.72782 -9.72591  1.000 13.25284  ? 398 ASP A N   1 
ATOM   538  C CA  . ASP A 1 69  ? 0.82587   -33.67351 -8.85345  1.000 13.39243  ? 398 ASP A CA  1 
ATOM   539  C C   . ASP A 1 69  ? 0.23609   -35.04937 -9.10915  1.000 13.58936  ? 398 ASP A C   1 
ATOM   540  O O   . ASP A 1 69  ? -0.95804  -35.16756 -9.36222  1.000 14.97348  ? 398 ASP A O   1 
ATOM   541  C CB  . ASP A 1 69  ? 0.56860   -33.25916 -7.41260  1.000 13.00802  ? 398 ASP A CB  1 
ATOM   542  C CG  . ASP A 1 69  ? 1.18548   -31.90363 -7.07604  1.000 14.53128  ? 398 ASP A CG  1 
ATOM   543  O OD1 . ASP A 1 69  ? 2.13818   -31.49091 -7.76524  1.000 15.32091  ? 398 ASP A OD1 1 
ATOM   544  O OD2 . ASP A 1 69  ? 0.69914   -31.26498 -6.10908  1.000 14.37757  ? 398 ASP A OD2 1 
ATOM   545  N N   . SER A 1 70  ? 1.06210   -36.09078 -9.08643  1.000 13.28220  ? 399 SER A N   1 
ATOM   546  C CA  . SER A 1 70  ? 0.50989   -37.40041 -9.42344  1.000 13.03797  ? 399 SER A CA  1 
ATOM   547  C C   . SER A 1 70  ? 1.19643   -38.50927 -8.64449  1.000 12.32521  ? 399 SER A C   1 
ATOM   548  O O   . SER A 1 70  ? 2.36337   -38.38899 -8.25063  1.000 12.67591  ? 399 SER A O   1 
ATOM   549  C CB  . SER A 1 70  ? 0.60461   -37.66788 -10.92453 1.000 14.96082  ? 399 SER A CB  1 
ATOM   550  O OG  . SER A 1 70  ? 1.94367   -37.64343 -11.38982 1.000 14.58702  ? 399 SER A OG  1 
ATOM   551  N N   . PHE A 1 71  ? 0.42051   -39.58150 -8.39691  1.000 11.67404  ? 400 PHE A N   1 
ATOM   552  C CA  . PHE A 1 71  ? 0.87103   -40.65911 -7.51542  1.000 11.93879  ? 400 PHE A CA  1 
ATOM   553  C C   . PHE A 1 71  ? -0.18415  -41.76195 -7.53102  1.000 11.16733  ? 400 PHE A C   1 
ATOM   554  O O   . PHE A 1 71  ? -1.26728  -41.60456 -8.10336  1.000 11.62424  ? 400 PHE A O   1 
ATOM   555  C CB  . PHE A 1 71  ? 1.08776   -40.14082 -6.08758  1.000 12.15448  ? 400 PHE A CB  1 
ATOM   556  C CG  . PHE A 1 71  ? -0.08358  -39.35288 -5.54518  1.000 11.73231  ? 400 PHE A CG  1 
ATOM   557  C CD1 . PHE A 1 71  ? -1.21950  -39.98895 -5.00124  1.000 11.39755  ? 400 PHE A CD1 1 
ATOM   558  C CD2 . PHE A 1 71  ? -0.05928  -37.96603 -5.53414  1.000 12.75888  ? 400 PHE A CD2 1 
ATOM   559  C CE1 . PHE A 1 71  ? -2.26381  -39.25099 -4.50385  1.000 12.21709  ? 400 PHE A CE1 1 
ATOM   560  C CE2 . PHE A 1 71  ? -1.09760  -37.21988 -5.02019  1.000 13.35468  ? 400 PHE A CE2 1 
ATOM   561  C CZ  . PHE A 1 71  ? -2.21267  -37.86491 -4.47494  1.000 13.00026  ? 400 PHE A CZ  1 
ATOM   562  N N   . VAL A 1 72  ? 0.15082   -42.88193 -6.87537  1.000 11.08626  ? 401 VAL A N   1 
ATOM   563  C CA  . VAL A 1 72  ? -0.75955  -44.00814 -6.70897  1.000 11.04045  ? 401 VAL A CA  1 
ATOM   564  C C   . VAL A 1 72  ? -1.07473  -44.20187 -5.23180  1.000 11.31460  ? 401 VAL A C   1 
ATOM   565  O O   . VAL A 1 72  ? -0.16908  -44.15252 -4.38498  1.000 11.88958  ? 401 VAL A O   1 
ATOM   566  C CB  . VAL A 1 72  ? -0.16180  -45.29052 -7.32502  1.000 12.47593  ? 401 VAL A CB  1 
ATOM   567  C CG1 . VAL A 1 72  ? -0.84142  -46.53991 -6.83187  1.000 13.84372  ? 401 VAL A CG1 1 
ATOM   568  C CG2 . VAL A 1 72  ? -0.21281  -45.20596 -8.83563  1.000 15.41157  ? 401 VAL A CG2 1 
ATOM   569  N N   . ILE A 1 73  ? -2.33502  -44.44631 -4.92777  1.000 10.85333  ? 402 ILE A N   1 
ATOM   570  C CA  . ILE A 1 73  ? -2.78000  -44.82599 -3.58514  1.000 11.37286  ? 402 ILE A CA  1 
ATOM   571  C C   . ILE A 1 73  ? -3.80861  -45.94086 -3.74824  1.000 11.82965  ? 402 ILE A C   1 
ATOM   572  O O   . ILE A 1 73  ? -4.13788  -46.34023 -4.86399  1.000 13.74038  ? 402 ILE A O   1 
ATOM   573  C CB  . ILE A 1 73  ? -3.39032  -43.64010 -2.81940  1.000 11.88008  ? 402 ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 73  ? -4.48393  -42.97067 -3.66912  1.000 12.73031  ? 402 ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 73  ? -2.28769  -42.68196 -2.40652  1.000 11.94560  ? 402 ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 73  ? -5.16584  -41.84110 -2.94296  1.000 13.76510  ? 402 ILE A CD1 1 
ATOM   577  N N   . ARG A 1 74  ? -4.34124  -46.45094 -2.63715  1.000 12.44434  ? 403 ARG A N   1 
ATOM   578  C CA  . ARG A 1 74  ? -5.38496  -47.46200 -2.78151  1.000 13.54149  ? 403 ARG A CA  1 
ATOM   579  C C   . ARG A 1 74  ? -6.76145  -46.80231 -2.82848  1.000 13.16329  ? 403 ARG A C   1 
ATOM   580  O O   . ARG A 1 74  ? -6.94708  -45.66108 -2.40719  1.000 14.15996  ? 403 ARG A O   1 
ATOM   581  C CB  . ARG A 1 74  ? -5.25741  -48.54287 -1.68876  1.000 20.46005  ? 403 ARG A CB  1 
ATOM   582  C CG  . ARG A 1 74  ? -5.44374  -48.15796 -0.30115  1.000 23.14099  ? 403 ARG A CG  1 
ATOM   583  C CD  . ARG A 1 74  ? -5.33805  -49.38482 0.61814   1.000 22.03751  ? 403 ARG A CD  1 
ATOM   584  N NE  . ARG A 1 74  ? -6.13241  -49.17825 1.82522   1.000 28.46533  ? 403 ARG A NE  1 
ATOM   585  C CZ  . ARG A 1 74  ? -5.82868  -49.69777 3.00634   1.000 35.03461  ? 403 ARG A CZ  1 
ATOM   586  N NH1 . ARG A 1 74  ? -4.75207  -50.44287 3.16715   1.000 35.90188  ? 403 ARG A NH1 1 
ATOM   587  N NH2 . ARG A 1 74  ? -6.60425  -49.42757 4.05748   1.000 37.17590  ? 403 ARG A NH2 1 
ATOM   588  N N   . GLY A 1 75  ? -7.72643  -47.52564 -3.40031  1.000 15.83187  ? 404 GLY A N   1 
ATOM   589  C CA  . GLY A 1 75  ? -9.02456  -46.92389 -3.67299  1.000 17.18618  ? 404 GLY A CA  1 
ATOM   590  C C   . GLY A 1 75  ? -9.67217  -46.28409 -2.46300  1.000 16.47966  ? 404 GLY A C   1 
ATOM   591  O O   . GLY A 1 75  ? -10.27999 -45.21408 -2.57374  1.000 16.56536  ? 404 GLY A O   1 
ATOM   592  N N   . ASP A 1 76  ? -9.62263  -46.95141 -1.30542  1.000 16.82971  ? 405 ASP A N   1 
ATOM   593  C CA  . ASP A 1 76  ? -10.33135 -46.38578 -0.15802  1.000 16.94128  ? 405 ASP A CA  1 
ATOM   594  C C   . ASP A 1 76  ? -9.61444  -45.17546 0.43678   1.000 14.88783  ? 405 ASP A C   1 
ATOM   595  O O   . ASP A 1 76  ? -10.12551 -44.57091 1.38842   1.000 14.99264  ? 405 ASP A O   1 
ATOM   596  C CB  . ASP A 1 76  ? -10.60749 -47.45076 0.89464   1.000 22.60399  ? 405 ASP A CB  1 
ATOM   597  C CG  . ASP A 1 76  ? -9.37383  -48.01418 1.50091   1.000 25.72564  ? 405 ASP A CG  1 
ATOM   598  O OD1 . ASP A 1 76  ? -9.52885  -48.96985 2.29854   1.000 32.11916  ? 405 ASP A OD1 1 
ATOM   599  O OD2 . ASP A 1 76  ? -8.26555  -47.51586 1.24447   1.000 27.02936  ? 405 ASP A OD2 1 
ATOM   600  N N   . GLU A 1 77  ? -8.46745  -44.78692 -0.12416  1.000 13.24937  ? 406 GLU A N   1 
ATOM   601  C CA  . GLU A 1 77  ? -7.74772  -43.59944 0.28705   1.000 12.44484  ? 406 GLU A CA  1 
ATOM   602  C C   . GLU A 1 77  ? -7.98446  -42.38964 -0.60435  1.000 11.49818  ? 406 GLU A C   1 
ATOM   603  O O   . GLU A 1 77  ? -7.55903  -41.28217 -0.24719  1.000 12.04554  ? 406 GLU A O   1 
ATOM   604  C CB  . GLU A 1 77  ? -6.23149  -43.85081 0.36479   1.000 12.41762  ? 406 GLU A CB  1 
ATOM   605  C CG  . GLU A 1 77  ? -5.89152  -44.92596 1.41398   1.000 13.85819  ? 406 GLU A CG  1 
ATOM   606  C CD  . GLU A 1 77  ? -4.46376  -45.40321 1.31125   1.000 13.16760  ? 406 GLU A CD  1 
ATOM   607  O OE1 . GLU A 1 77  ? -3.91241  -45.37902 0.19566   1.000 12.87756  ? 406 GLU A OE1 1 
ATOM   608  O OE2 . GLU A 1 77  ? -3.91038  -45.89066 2.31823   1.000 16.52640  ? 406 GLU A OE2 1 
ATOM   609  N N   . VAL A 1 78  ? -8.64810  -42.56688 -1.74874  1.000 12.29053  ? 407 VAL A N   1 
ATOM   610  C CA  . VAL A 1 78  ? -8.86744  -41.42259 -2.61786  1.000 12.34501  ? 407 VAL A CA  1 
ATOM   611  C C   . VAL A 1 78  ? -9.60104  -40.32390 -1.89045  1.000 11.94217  ? 407 VAL A C   1 
ATOM   612  O O   . VAL A 1 78  ? -9.34514  -39.13894 -2.11965  1.000 13.23480  ? 407 VAL A O   1 
ATOM   613  C CB  . VAL A 1 78  ? -9.56457  -41.88017 -3.91188  1.000 15.17251  ? 407 VAL A CB  1 
ATOM   614  C CG1 . VAL A 1 78  ? -9.93949  -40.67527 -4.78545  1.000 16.83298  ? 407 VAL A CG1 1 
ATOM   615  C CG2 . VAL A 1 78  ? -8.65425  -42.85718 -4.69178  1.000 16.08629  ? 407 VAL A CG2 1 
ATOM   616  N N   A ARG A 1 79  ? -10.51131 -40.68924 -0.98707  0.500 12.16465  ? 408 ARG A N   1 
ATOM   617  N N   B ARG A 1 79  ? -10.48413 -40.68165 -0.96065  0.500 12.12067  ? 408 ARG A N   1 
ATOM   618  C CA  A ARG A 1 79  ? -11.25451 -39.68762 -0.23567  0.500 13.12994  ? 408 ARG A CA  1 
ATOM   619  C CA  B ARG A 1 79  ? -11.24520 -39.65698 -0.26147  0.500 13.01526  ? 408 ARG A CA  1 
ATOM   620  C C   A ARG A 1 79  ? -10.34645 -38.82258 0.63391   0.500 12.54885  ? 408 ARG A C   1 
ATOM   621  C C   B ARG A 1 79  ? -10.35469 -38.82320 0.65489   0.500 12.51023  ? 408 ARG A C   1 
ATOM   622  O O   A ARG A 1 79  ? -10.75025 -37.72501 1.02704   0.500 13.96782  ? 408 ARG A O   1 
ATOM   623  O O   B ARG A 1 79  ? -10.77170 -37.74803 1.09240   0.500 13.97818  ? 408 ARG A O   1 
ATOM   624  C CB  A ARG A 1 79  ? -12.30702 -40.36275 0.64294   0.500 14.48839  ? 408 ARG A CB  1 
ATOM   625  C CB  B ARG A 1 79  ? -12.37767 -40.31102 0.53008   0.500 14.51704  ? 408 ARG A CB  1 
ATOM   626  C CG  A ARG A 1 79  ? -11.79018 -41.41357 1.61529   0.500 16.09738  ? 408 ARG A CG  1 
ATOM   627  C CG  B ARG A 1 79  ? -11.96213 -41.31040 1.59268   0.500 14.98450  ? 408 ARG A CG  1 
ATOM   628  C CD  A ARG A 1 79  ? -12.69196 -41.54811 2.84408   0.500 21.70786  ? 408 ARG A CD  1 
ATOM   629  C CD  B ARG A 1 79  ? -13.16916 -41.85983 2.38080   0.500 18.18592  ? 408 ARG A CD  1 
ATOM   630  N NE  A ARG A 1 79  ? -13.12215 -40.20921 3.20420   0.500 25.33479  ? 408 ARG A NE  1 
ATOM   631  N NE  B ARG A 1 79  ? -12.78099 -43.02577 3.16943   0.500 23.63856  ? 408 ARG A NE  1 
ATOM   632  C CZ  A ARG A 1 79  ? -12.43151 -39.32016 3.91943   0.500 25.87816  ? 408 ARG A CZ  1 
ATOM   633  C CZ  B ARG A 1 79  ? -12.71768 -44.28130 2.73433   0.500 27.33052  ? 408 ARG A CZ  1 
ATOM   634  N NH1 A ARG A 1 79  ? -11.28435 -39.63834 4.57371   0.500 16.01876  ? 408 ARG A NH1 1 
ATOM   635  N NH1 B ARG A 1 79  ? -13.15299 -44.63371 1.54143   0.500 20.78482  ? 408 ARG A NH1 1 
ATOM   636  N NH2 A ARG A 1 79  ? -12.83748 -38.05649 3.89238   0.500 25.49190  ? 408 ARG A NH2 1 
ATOM   637  N NH2 B ARG A 1 79  ? -12.29921 -45.23029 3.56664   0.500 30.86635  ? 408 ARG A NH2 1 
ATOM   638  N N   . GLN A 1 80  ? -9.13429  -39.28170 0.95070   1.000 11.85506  ? 409 GLN A N   1 
ATOM   639  C CA  . GLN A 1 80  ? -8.23363  -38.45867 1.75505   1.000 12.18697  ? 409 GLN A CA  1 
ATOM   640  C C   . GLN A 1 80  ? -7.61209  -37.32976 0.93488   1.000 11.43729  ? 409 GLN A C   1 
ATOM   641  O O   . GLN A 1 80  ? -7.00282  -36.41561 1.50393   1.000 12.07045  ? 409 GLN A O   1 
ATOM   642  C CB  . GLN A 1 80  ? -7.10838  -39.31499 2.33464   1.000 11.50052  ? 409 GLN A CB  1 
ATOM   643  C CG  . GLN A 1 80  ? -7.63247  -40.25918 3.42764   1.000 11.59089  ? 409 GLN A CG  1 
ATOM   644  C CD  . GLN A 1 80  ? -6.53562  -41.03767 4.10928   1.000 11.45999  ? 409 GLN A CD  1 
ATOM   645  O OE1 . GLN A 1 80  ? -5.44411  -40.48307 4.37869   1.000 11.65259  ? 409 GLN A OE1 1 
ATOM   646  N NE2 . GLN A 1 80  ? -6.80397  -42.28145 4.49503   1.000 12.41557  ? 409 GLN A NE2 1 
ATOM   647  N N   . ILE A 1 81  ? -7.70259  -37.39612 -0.40571  1.000 11.74432  ? 410 ILE A N   1 
ATOM   648  C CA  . ILE A 1 81  ? -7.08082  -36.37804 -1.25979  1.000 11.35665  ? 410 ILE A CA  1 
ATOM   649  C C   . ILE A 1 81  ? -8.12711  -35.28764 -1.46687  1.000 11.90602  ? 410 ILE A C   1 
ATOM   650  O O   . ILE A 1 81  ? -8.72077  -35.15900 -2.54185  1.000 12.52676  ? 410 ILE A O   1 
ATOM   651  C CB  . ILE A 1 81  ? -6.59473  -36.96892 -2.59821  1.000 11.78091  ? 410 ILE A CB  1 
ATOM   652  C CG1 . ILE A 1 81  ? -5.72673  -38.23453 -2.37434  1.000 12.34792  ? 410 ILE A CG1 1 
ATOM   653  C CG2 . ILE A 1 81  ? -5.77722  -35.90902 -3.34327  1.000 12.72741  ? 410 ILE A CG2 1 
ATOM   654  C CD1 . ILE A 1 81  ? -4.56866  -38.04917 -1.42445  1.000 13.68423  ? 410 ILE A CD1 1 
ATOM   655  N N   . ALA A 1 82  ? -8.37199  -34.50846 -0.42881  1.000 13.19307  ? 411 ALA A N   1 
ATOM   656  C CA  . ALA A 1 82  ? -9.38171  -33.45058 -0.44543  1.000 12.80770  ? 411 ALA A CA  1 
ATOM   657  C C   . ALA A 1 82  ? -9.04041  -32.52976 0.71537   1.000 12.95683  ? 411 ALA A C   1 
ATOM   658  O O   . ALA A 1 82  ? -8.46699  -32.99450 1.71033   1.000 13.66977  ? 411 ALA A O   1 
ATOM   659  C CB  . ALA A 1 82  ? -10.80346 -34.01716 -0.28104  1.000 14.07903  ? 411 ALA A CB  1 
ATOM   660  N N   . PRO A 1 83  ? -9.40497  -31.25043 0.65314   1.000 13.82095  ? 412 PRO A N   1 
ATOM   661  C CA  . PRO A 1 83  ? -9.15707  -30.35549 1.79778   1.000 15.05000  ? 412 PRO A CA  1 
ATOM   662  C C   . PRO A 1 83  ? -9.80684  -30.87832 3.06828   1.000 14.41950  ? 412 PRO A C   1 
ATOM   663  O O   . PRO A 1 83  ? -10.91726 -31.41391 3.03830   1.000 15.45030  ? 412 PRO A O   1 
ATOM   664  C CB  . PRO A 1 83  ? -9.79920  -29.02936 1.37523   1.000 16.58043  ? 412 PRO A CB  1 
ATOM   665  C CG  . PRO A 1 83  ? -9.98455  -29.11867 -0.08361  1.000 19.47581  ? 412 PRO A CG  1 
ATOM   666  C CD  . PRO A 1 83  ? -10.04439 -30.56396 -0.48303  1.000 15.86682  ? 412 PRO A CD  1 
ATOM   667  N N   . GLY A 1 84  ? -9.10869  -30.69099 4.19360   1.000 14.29624  ? 413 GLY A N   1 
ATOM   668  C CA  . GLY A 1 84  ? -9.71576  -30.97147 5.48760   1.000 15.96004  ? 413 GLY A CA  1 
ATOM   669  C C   . GLY A 1 84  ? -9.70584  -32.41576 5.91439   1.000 14.31668  ? 413 GLY A C   1 
ATOM   670  O O   . GLY A 1 84  ? -10.26643 -32.72615 6.97282   1.000 16.15797  ? 413 GLY A O   1 
ATOM   671  N N   . GLN A 1 85  ? -9.07489  -33.31783 5.17410   1.000 13.50457  ? 414 GLN A N   1 
ATOM   672  C CA  . GLN A 1 85  ? -9.15110  -34.74007 5.46823   1.000 12.79280  ? 414 GLN A CA  1 
ATOM   673  C C   . GLN A 1 85  ? -7.93034  -35.21616 6.24675   1.000 13.40754  ? 414 GLN A C   1 
ATOM   674  O O   . GLN A 1 85  ? -6.93650  -34.49702 6.41141   1.000 14.83087  ? 414 GLN A O   1 
ATOM   675  C CB  . GLN A 1 85  ? -9.38137  -35.53867 4.18873   1.000 13.71160  ? 414 GLN A CB  1 
ATOM   676  C CG  . GLN A 1 85  ? -10.61604 -35.08886 3.35709   1.000 15.15434  ? 414 GLN A CG  1 
ATOM   677  C CD  . GLN A 1 85  ? -11.83667 -34.89486 4.24925   1.000 15.71847  ? 414 GLN A CD  1 
ATOM   678  O OE1 . GLN A 1 85  ? -12.34735 -35.84239 4.81249   1.000 17.25287  ? 414 GLN A OE1 1 
ATOM   679  N NE2 . GLN A 1 85  ? -12.35180 -33.67102 4.30880   1.000 18.61267  ? 414 GLN A NE2 1 
ATOM   680  N N   . THR A 1 86  ? -8.01710  -36.47391 6.70233   1.000 12.30289  ? 415 THR A N   1 
ATOM   681  C CA  . THR A 1 86  ? -6.99197  -37.03858 7.55167   1.000 12.94961  ? 415 THR A CA  1 
ATOM   682  C C   . THR A 1 86  ? -6.92465  -38.54053 7.29918   1.000 11.98126  ? 415 THR A C   1 
ATOM   683  O O   . THR A 1 86  ? -7.76698  -39.12587 6.61443   1.000 12.60562  ? 415 THR A O   1 
ATOM   684  C CB  . THR A 1 86  ? -7.28586  -36.69457 9.02137   1.000 13.16698  ? 415 THR A CB  1 
ATOM   685  O OG1 . THR A 1 86  ? -6.14663  -37.01362 9.83027   1.000 13.97241  ? 415 THR A OG1 1 
ATOM   686  C CG2 . THR A 1 86  ? -8.49636  -37.47874 9.53664   1.000 14.97035  ? 415 THR A CG2 1 
ATOM   687  N N   . GLY A 1 87  ? -5.89834  -39.15922 7.87204   1.000 12.67715  ? 416 GLY A N   1 
ATOM   688  C CA  . GLY A 1 87  ? -5.56780  -40.55441 7.67127   1.000 12.28366  ? 416 GLY A CA  1 
ATOM   689  C C   . GLY A 1 87  ? -4.10263  -40.68079 7.29945   1.000 11.71817  ? 416 GLY A C   1 
ATOM   690  O O   . GLY A 1 87  ? -3.37670  -39.69662 7.22033   1.000 12.02159  ? 416 GLY A O   1 
ATOM   691  N N   . LYS A 1 88  ? -3.66504  -41.91673 7.02691   1.000 11.76414  ? 417 LYS A N   1 
ATOM   692  C CA  . LYS A 1 88  ? -2.23248  -42.09355 6.77328   1.000 12.19933  ? 417 LYS A CA  1 
ATOM   693  C C   . LYS A 1 88  ? -1.78067  -41.28058 5.57391   1.000 11.00849  ? 417 LYS A C   1 
ATOM   694  O O   . LYS A 1 88  ? -0.63081  -40.81516 5.52983   1.000 11.57363  ? 417 LYS A O   1 
ATOM   695  C CB  . LYS A 1 88  ? -1.87088  -43.56188 6.55751   1.000 15.66840  ? 417 LYS A CB  1 
ATOM   696  C CG  . LYS A 1 88  ? -2.19273  -44.47648 7.73647   1.000 18.03577  ? 417 LYS A CG  1 
ATOM   697  C CD  . LYS A 1 88  ? -1.60232  -44.06159 9.04006   1.000 24.11599  ? 417 LYS A CD  1 
ATOM   698  C CE  . LYS A 1 88  ? -1.66714  -45.20156 10.11105  1.000 25.22402  ? 417 LYS A CE  1 
ATOM   699  N NZ  . LYS A 1 88  ? -3.04185  -45.43126 10.74738  1.000 24.09937  ? 417 LYS A NZ  1 
ATOM   700  N N   . ILE A 1 89  ? -2.63470  -41.16477 4.54599   1.000 11.21397  ? 418 ILE A N   1 
ATOM   701  C CA  . ILE A 1 89  ? -2.18899  -40.49742 3.32809   1.000 11.93370  ? 418 ILE A CA  1 
ATOM   702  C C   . ILE A 1 89  ? -2.17440  -38.99339 3.52632   1.000 10.95495  ? 418 ILE A C   1 
ATOM   703  O O   . ILE A 1 89  ? -1.15388  -38.34441 3.30171   1.000 11.95054  ? 418 ILE A O   1 
ATOM   704  C CB  . ILE A 1 89  ? -3.03898  -40.92734 2.11985   1.000 11.70530  ? 418 ILE A CB  1 
ATOM   705  C CG1 . ILE A 1 89  ? -2.95410  -42.45408 1.95120   1.000 13.46225  ? 418 ILE A CG1 1 
ATOM   706  C CG2 . ILE A 1 89  ? -2.51820  -40.20112 0.87488   1.000 13.83649  ? 418 ILE A CG2 1 
ATOM   707  C CD1 . ILE A 1 89  ? -1.54552  -43.04774 1.96140   1.000 15.17087  ? 418 ILE A CD1 1 
ATOM   708  N N   . ALA A 1 90  ? -3.29099  -38.40784 3.97878   1.000 11.54981  ? 419 ALA A N   1 
ATOM   709  C CA  . ALA A 1 90  ? -3.32403  -36.96091 4.20520   1.000 11.43723  ? 419 ALA A CA  1 
ATOM   710  C C   . ALA A 1 90  ? -2.35190  -36.54702 5.29329   1.000 11.64075  ? 419 ALA A C   1 
ATOM   711  O O   . ALA A 1 90  ? -1.75315  -35.47422 5.20781   1.000 12.84615  ? 419 ALA A O   1 
ATOM   712  C CB  . ALA A 1 90  ? -4.73910  -36.51802 4.56315   1.000 13.08687  ? 419 ALA A CB  1 
ATOM   713  N N   . ASP A 1 91  ? -2.19434  -37.36570 6.32504   1.000 11.49613  ? 420 ASP A N   1 
ATOM   714  C CA  . ASP A 1 91  ? -1.33957  -36.94292 7.43485   1.000 11.85845  ? 420 ASP A CA  1 
ATOM   715  C C   . ASP A 1 91  ? 0.14857   -37.10151 7.13211   1.000 11.88760  ? 420 ASP A C   1 
ATOM   716  O O   . ASP A 1 91  ? 0.95900   -36.26021 7.55769   1.000 12.93840  ? 420 ASP A O   1 
ATOM   717  C CB  . ASP A 1 91  ? -1.62463  -37.74039 8.70060   1.000 12.36132  ? 420 ASP A CB  1 
ATOM   718  C CG  . ASP A 1 91  ? -3.00826  -37.51367 9.27543   1.000 12.41058  ? 420 ASP A CG  1 
ATOM   719  O OD1 . ASP A 1 91  ? -3.74339  -36.61181 8.82537   1.000 13.23900  ? 420 ASP A OD1 1 
ATOM   720  O OD2 . ASP A 1 91  ? -3.36962  -38.26818 10.21806  1.000 12.97529  ? 420 ASP A OD2 1 
ATOM   721  N N   . TYR A 1 92  ? 0.54963   -38.15871 6.42061   1.000 11.23821  ? 421 TYR A N   1 
ATOM   722  C CA  . TYR A 1 92  ? 1.97397   -38.46450 6.30932   1.000 11.17379  ? 421 TYR A CA  1 
ATOM   723  C C   . TYR A 1 92  ? 2.52132   -38.43613 4.88863   1.000 11.30239  ? 421 TYR A C   1 
ATOM   724  O O   . TYR A 1 92  ? 3.74580   -38.54008 4.75181   1.000 12.51241  ? 421 TYR A O   1 
ATOM   725  C CB  . TYR A 1 92  ? 2.30142   -39.86259 6.86115   1.000 12.10536  ? 421 TYR A CB  1 
ATOM   726  C CG  . TYR A 1 92  ? 1.75404   -40.18528 8.23885   1.000 11.73147  ? 421 TYR A CG  1 
ATOM   727  C CD1 . TYR A 1 92  ? 1.62969   -39.20803 9.21653   1.000 13.06695  ? 421 TYR A CD1 1 
ATOM   728  C CD2 . TYR A 1 92  ? 1.37947   -41.48770 8.54740   1.000 13.82134  ? 421 TYR A CD2 1 
ATOM   729  C CE1 . TYR A 1 92  ? 1.13007   -39.52669 10.49077  1.000 14.64055  ? 421 TYR A CE1 1 
ATOM   730  C CE2 . TYR A 1 92  ? 0.86350   -41.80386 9.79903   1.000 15.87057  ? 421 TYR A CE2 1 
ATOM   731  C CZ  . TYR A 1 92  ? 0.73240   -40.81807 10.75903  1.000 15.88126  ? 421 TYR A CZ  1 
ATOM   732  O OH  . TYR A 1 92  ? 0.20338   -41.14001 11.98575  1.000 19.45117  ? 421 TYR A OH  1 
ATOM   733  N N   . ASN A 1 93  ? 1.65802   -38.31886 3.83564   1.000 11.75557  ? 422 ASN A N   1 
ATOM   734  C CA  . ASN A 1 93  ? 2.11113   -38.51990 2.45858   1.000 11.03312  ? 422 ASN A CA  1 
ATOM   735  C C   . ASN A 1 93  ? 1.80997   -37.35214 1.54229   1.000 11.23538  ? 422 ASN A C   1 
ATOM   736  O O   . ASN A 1 93  ? 2.73013   -36.87889 0.86933   1.000 12.16517  ? 422 ASN A O   1 
ATOM   737  C CB  . ASN A 1 93  ? 1.46421   -39.79776 1.89422   1.000 11.64558  ? 422 ASN A CB  1 
ATOM   738  C CG  . ASN A 1 93  ? 2.06510   -41.05477 2.51805   1.000 10.76095  ? 422 ASN A CG  1 
ATOM   739  O OD1 . ASN A 1 93  ? 3.04189   -41.62273 2.00232   1.000 11.70660  ? 422 ASN A OD1 1 
ATOM   740  N ND2 . ASN A 1 93  ? 1.50842   -41.48015 3.66080   1.000 11.45347  ? 422 ASN A ND2 1 
ATOM   741  N N   . TYR A 1 94  ? 0.55380   -36.91325 1.46554   1.000 11.45147  ? 423 TYR A N   1 
ATOM   742  C CA  . TYR A 1 94  ? 0.19429   -35.85196 0.52646   1.000 11.33313  ? 423 TYR A CA  1 
ATOM   743  C C   . TYR A 1 94  ? -0.97218  -35.09572 1.13250   1.000 11.83401  ? 423 TYR A C   1 
ATOM   744  O O   . TYR A 1 94  ? -2.04209  -35.67797 1.33891   1.000 11.66417  ? 423 TYR A O   1 
ATOM   745  C CB  . TYR A 1 94  ? -0.19351  -36.40799 -0.85524  1.000 11.98135  ? 423 TYR A CB  1 
ATOM   746  C CG  . TYR A 1 94  ? -0.47213  -35.31168 -1.84809  1.000 11.07758  ? 423 TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 94  ? 0.55420   -34.73348 -2.57417  1.000 11.98429  ? 423 TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 94  ? -1.77420  -34.81140 -2.01430  1.000 12.08098  ? 423 TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 94  ? 0.31738   -33.71483 -3.48347  1.000 12.71414  ? 423 TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 94  ? -2.02092  -33.80222 -2.92616  1.000 12.91824  ? 423 TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 94  ? -0.98459  -33.25132 -3.66773  1.000 12.83137  ? 423 TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 94  ? -1.26343  -32.27125 -4.58439  1.000 13.84759  ? 423 TYR A OH  1 
ATOM   753  N N   . LYS A 1 95  ? -0.77642  -33.80334 1.41988   1.000 12.60491  ? 424 LYS A N   1 
ATOM   754  C CA  . LYS A 1 95  ? -1.73228  -33.00159 2.18271   1.000 12.65156  ? 424 LYS A CA  1 
ATOM   755  C C   . LYS A 1 95  ? -2.17937  -31.79650 1.36101   1.000 13.11936  ? 424 LYS A C   1 
ATOM   756  O O   . LYS A 1 95  ? -1.35686  -30.95519 0.98813   1.000 13.75520  ? 424 LYS A O   1 
ATOM   757  C CB  . LYS A 1 95  ? -1.08523  -32.52393 3.48686   1.000 13.47512  ? 424 LYS A CB  1 
ATOM   758  C CG  . LYS A 1 95  ? -1.97858  -31.63487 4.34905   1.000 13.43182  ? 424 LYS A CG  1 
ATOM   759  C CD  . LYS A 1 95  ? -3.29405  -32.33016 4.70690   1.000 13.70801  ? 424 LYS A CD  1 
ATOM   760  C CE  . LYS A 1 95  ? -4.10167  -31.50904 5.70889   1.000 14.21489  ? 424 LYS A CE  1 
ATOM   761  N NZ  . LYS A 1 95  ? -5.35547  -32.24482 5.99871   1.000 15.65857  ? 424 LYS A NZ  1 
ATOM   762  N N   . LEU A 1 96  ? -3.49316  -31.69808 1.10662   1.000 13.01411  ? 425 LEU A N   1 
ATOM   763  C CA  . LEU A 1 96  ? -4.04078  -30.49783 0.49620   1.000 13.96115  ? 425 LEU A CA  1 
ATOM   764  C C   . LEU A 1 96  ? -4.39282  -29.45350 1.56220   1.000 14.75980  ? 425 LEU A C   1 
ATOM   765  O O   . LEU A 1 96  ? -4.80723  -29.80135 2.66710   1.000 16.49458  ? 425 LEU A O   1 
ATOM   766  C CB  . LEU A 1 96  ? -5.30496  -30.84277 -0.29384  1.000 14.03351  ? 425 LEU A CB  1 
ATOM   767  C CG  . LEU A 1 96  ? -5.04173  -31.64640 -1.56873  1.000 13.93588  ? 425 LEU A CG  1 
ATOM   768  C CD1 . LEU A 1 96  ? -6.35556  -32.06255 -2.16027  1.000 16.64330  ? 425 LEU A CD1 1 
ATOM   769  C CD2 . LEU A 1 96  ? -4.20220  -30.83476 -2.55638  1.000 16.37691  ? 425 LEU A CD2 1 
ATOM   770  N N   . PRO A 1 97  ? -4.26442  -28.16866 1.22896   1.000 16.67610  ? 426 PRO A N   1 
ATOM   771  C CA  . PRO A 1 97  ? -4.59490  -27.10409 2.18486   1.000 17.20133  ? 426 PRO A CA  1 
ATOM   772  C C   . PRO A 1 97  ? -6.09323  -26.88407 2.27228   1.000 17.38035  ? 426 PRO A C   1 
ATOM   773  O O   . PRO A 1 97  ? -6.84737  -27.19794 1.34443   1.000 17.46519  ? 426 PRO A O   1 
ATOM   774  C CB  . PRO A 1 97  ? -3.91783  -25.86661 1.57555   1.000 17.95150  ? 426 PRO A CB  1 
ATOM   775  C CG  . PRO A 1 97  ? -3.94792  -26.14960 0.07310   1.000 17.57236  ? 426 PRO A CG  1 
ATOM   776  C CD  . PRO A 1 97  ? -3.70997  -27.65354 -0.04111  1.000 16.85425  ? 426 PRO A CD  1 
ATOM   777  N N   . ASP A 1 98  ? -6.52143  -26.27721 3.39063   1.000 19.76092  ? 427 ASP A N   1 
ATOM   778  C CA  . ASP A 1 98  ? -7.93643  -25.93369 3.52092   1.000 19.69996  ? 427 ASP A CA  1 
ATOM   779  C C   . ASP A 1 98  ? -8.42044  -25.05554 2.37589   1.000 20.79677  ? 427 ASP A C   1 
ATOM   780  O O   . ASP A 1 98  ? -9.55730  -25.19946 1.91021   1.000 22.70824  ? 427 ASP A O   1 
ATOM   781  C CB  . ASP A 1 98  ? -8.22442  -25.19993 4.83158   1.000 24.02653  ? 427 ASP A CB  1 
ATOM   782  C CG  . ASP A 1 98  ? -7.96465  -26.03221 6.04797   1.000 27.52568  ? 427 ASP A CG  1 
ATOM   783  O OD1 . ASP A 1 98  ? -7.91745  -27.27371 5.93410   1.000 25.66605  ? 427 ASP A OD1 1 
ATOM   784  O OD2 . ASP A 1 98  ? -7.92490  -25.41768 7.14661   1.000 30.29786  ? 427 ASP A OD2 1 
ATOM   785  N N   . ASP A 1 99  ? -7.58951  -24.11613 1.93433   1.000 19.99936  ? 428 ASP A N   1 
ATOM   786  C CA  . ASP A 1 99  ? -8.01706  -23.15765 0.92892   1.000 22.37876  ? 428 ASP A CA  1 
ATOM   787  C C   . ASP A 1 99  ? -7.68470  -23.62082 -0.48785  1.000 20.40700  ? 428 ASP A C   1 
ATOM   788  O O   . ASP A 1 99  ? -7.52979  -22.78744 -1.39105  1.000 22.34912  ? 428 ASP A O   1 
ATOM   789  C CB  . ASP A 1 99  ? -7.40530  -21.78137 1.20782   1.000 24.96846  ? 428 ASP A CB  1 
ATOM   790  C CG  . ASP A 1 99  ? -5.88595  -21.74536 1.02661   1.000 28.66240  ? 428 ASP A CG  1 
ATOM   791  O OD1 . ASP A 1 99  ? -5.24510  -22.80008 0.83459   1.000 28.45914  ? 428 ASP A OD1 1 
ATOM   792  O OD2 . ASP A 1 99  ? -5.30466  -20.62899 1.12765   1.000 33.00809  ? 428 ASP A OD2 1 
ATOM   793  N N   . PHE A 1 100 ? -7.55234  -24.92620 -0.69581  1.000 19.15905  ? 429 PHE A N   1 
ATOM   794  C CA  . PHE A 1 100 ? -7.16031  -25.44901 -1.99315  1.000 18.48832  ? 429 PHE A CA  1 
ATOM   795  C C   . PHE A 1 100 ? -8.05679  -24.93635 -3.11050  1.000 17.67615  ? 429 PHE A C   1 
ATOM   796  O O   . PHE A 1 100 ? -9.28124  -24.92982 -2.98588  1.000 19.29594  ? 429 PHE A O   1 
ATOM   797  C CB  . PHE A 1 100 ? -7.24715  -26.97502 -1.91311  1.000 17.28974  ? 429 PHE A CB  1 
ATOM   798  C CG  . PHE A 1 100 ? -6.95140  -27.68103 -3.21370  1.000 16.50818  ? 429 PHE A CG  1 
ATOM   799  C CD1 . PHE A 1 100 ? -5.73793  -27.48206 -3.84678  1.000 17.07787  ? 429 PHE A CD1 1 
ATOM   800  C CD2 . PHE A 1 100 ? -7.81736  -28.65013 -3.72350  1.000 15.28298  ? 429 PHE A CD2 1 
ATOM   801  C CE1 . PHE A 1 100 ? -5.41926  -28.17987 -5.02455  1.000 16.46003  ? 429 PHE A CE1 1 
ATOM   802  C CE2 . PHE A 1 100 ? -7.51555  -29.33454 -4.91221  1.000 15.30911  ? 429 PHE A CE2 1 
ATOM   803  C CZ  . PHE A 1 100 ? -6.29952  -29.11259 -5.54328  1.000 15.40452  ? 429 PHE A CZ  1 
ATOM   804  N N   . THR A 1 101 ? -7.43848  -24.49259 -4.20495  1.000 17.64964  ? 430 THR A N   1 
ATOM   805  C CA  . THR A 1 101 ? -8.15084  -24.20331 -5.44520  1.000 18.21637  ? 430 THR A CA  1 
ATOM   806  C C   . THR A 1 101 ? -7.60277  -25.14539 -6.49830  1.000 16.18460  ? 430 THR A C   1 
ATOM   807  O O   . THR A 1 101 ? -6.45611  -24.99527 -6.92930  1.000 18.07935  ? 430 THR A O   1 
ATOM   808  C CB  . THR A 1 101 ? -7.95620  -22.74486 -5.87402  1.000 20.35009  ? 430 THR A CB  1 
ATOM   809  O OG1 . THR A 1 101 ? -8.34740  -21.87160 -4.80678  1.000 22.54713  ? 430 THR A OG1 1 
ATOM   810  C CG2 . THR A 1 101 ? -8.77861  -22.44056 -7.12319  1.000 20.67137  ? 430 THR A CG2 1 
ATOM   811  N N   . GLY A 1 102 ? -8.42071  -26.10292 -6.92333  1.000 16.24160  ? 431 GLY A N   1 
ATOM   812  C CA  . GLY A 1 102 ? -7.94681  -27.10919 -7.84262  1.000 15.50725  ? 431 GLY A CA  1 
ATOM   813  C C   . GLY A 1 102 ? -8.92152  -28.26193 -7.95302  1.000 14.45422  ? 431 GLY A C   1 
ATOM   814  O O   . GLY A 1 102 ? -10.02091 -28.23379 -7.38987  1.000 15.81291  ? 431 GLY A O   1 
ATOM   815  N N   . CYS A 1 103 ? -8.48052  -29.28395 -8.69369  1.000 13.78243  ? 432 CYS A N   1 
ATOM   816  C CA  . CYS A 1 103 ? -9.29950  -30.45572 -8.91860  1.000 13.83806  ? 432 CYS A CA  1 
ATOM   817  C C   . CYS A 1 103 ? -8.48215  -31.71924 -8.67062  1.000 13.03579  ? 432 CYS A C   1 
ATOM   818  O O   . CYS A 1 103 ? -7.26846  -31.76741 -8.95291  1.000 15.97717  ? 432 CYS A O   1 
ATOM   819  C CB  . CYS A 1 103 ? -9.89288  -30.49447 -10.34526 1.000 16.39785  ? 432 CYS A CB  1 
ATOM   820  S SG  . CYS A 1 103 ? -10.83193 -29.00293 -10.79748 1.000 17.61169  ? 432 CYS A SG  1 
ATOM   821  N N   . VAL A 1 104 ? -9.17792  -32.75390 -8.19878  1.000 12.18060  ? 433 VAL A N   1 
ATOM   822  C CA  . VAL A 1 104 ? -8.59255  -34.06456 -7.91823  1.000 12.15902  ? 433 VAL A CA  1 
ATOM   823  C C   . VAL A 1 104 ? -9.25188  -35.04995 -8.87504  1.000 12.11677  ? 433 VAL A C   1 
ATOM   824  O O   . VAL A 1 104 ? -10.48620 -35.14777 -8.92749  1.000 12.60267  ? 433 VAL A O   1 
ATOM   825  C CB  . VAL A 1 104 ? -8.82850  -34.46717 -6.45207  1.000 12.81336  ? 433 VAL A CB  1 
ATOM   826  C CG1 . VAL A 1 104 ? -8.27180  -35.85891 -6.20678  1.000 13.49550  ? 433 VAL A CG1 1 
ATOM   827  C CG2 . VAL A 1 104 ? -8.18359  -33.43931 -5.51982  1.000 13.30958  ? 433 VAL A CG2 1 
ATOM   828  N N   . ILE A 1 105 ? -8.42866  -35.76087 -9.63668  1.000 11.90632  ? 434 ILE A N   1 
ATOM   829  C CA  . ILE A 1 105 ? -8.89251  -36.67585 -10.67292 1.000 12.11420  ? 434 ILE A CA  1 
ATOM   830  C C   . ILE A 1 105 ? -8.28098  -38.03155 -10.35583 1.000 12.14535  ? 434 ILE A C   1 
ATOM   831  O O   . ILE A 1 105 ? -7.08960  -38.11577 -10.04847 1.000 14.23329  ? 434 ILE A O   1 
ATOM   832  C CB  . ILE A 1 105 ? -8.40182  -36.16296 -12.04007 1.000 12.85540  ? 434 ILE A CB  1 
ATOM   833  C CG1 . ILE A 1 105 ? -8.95250  -34.73918 -12.28317 1.000 14.26233  ? 434 ILE A CG1 1 
ATOM   834  C CG2 . ILE A 1 105 ? -8.78838  -37.11549 -13.13415 1.000 14.24049  ? 434 ILE A CG2 1 
ATOM   835  C CD1 . ILE A 1 105 ? -8.26814  -34.04021 -13.43997 1.000 16.54329  ? 434 ILE A CD1 1 
ATOM   836  N N   . ALA A 1 106 ? -9.07426  -39.09343 -10.40427 1.000 12.00805  ? 435 ALA A N   1 
ATOM   837  C CA  . ALA A 1 106 ? -8.50629  -40.41736 -10.12098 1.000 12.46882  ? 435 ALA A CA  1 
ATOM   838  C C   . ALA A 1 106 ? -9.17056  -41.48731 -10.97062 1.000 12.90558  ? 435 ALA A C   1 
ATOM   839  O O   . ALA A 1 106 ? -10.32326 -41.32523 -11.41872 1.000 14.62943  ? 435 ALA A O   1 
ATOM   840  C CB  . ALA A 1 106 ? -8.64413  -40.77186 -8.62655  1.000 15.04184  ? 435 ALA A CB  1 
ATOM   841  N N   . TRP A 1 107 ? -8.46031  -42.60789 -11.13196 1.000 13.63950  ? 436 TRP A N   1 
ATOM   842  C CA  . TRP A 1 107 ? -9.00250  -43.73862 -11.85882 1.000 13.69011  ? 436 TRP A CA  1 
ATOM   843  C C   . TRP A 1 107 ? -8.34642  -45.01855 -11.38806 1.000 13.38737  ? 436 TRP A C   1 
ATOM   844  O O   . TRP A 1 107 ? -7.18601  -45.02432 -10.96537 1.000 13.86662  ? 436 TRP A O   1 
ATOM   845  C CB  . TRP A 1 107 ? -8.81637  -43.53177 -13.36014 1.000 15.04259  ? 436 TRP A CB  1 
ATOM   846  C CG  . TRP A 1 107 ? -7.39528  -43.48882 -13.86873 1.000 15.23539  ? 436 TRP A CG  1 
ATOM   847  C CD1 . TRP A 1 107 ? -6.70776  -44.48400 -14.50762 1.000 17.09550  ? 436 TRP A CD1 1 
ATOM   848  C CD2 . TRP A 1 107 ? -6.51037  -42.33862 -13.84990 1.000 14.82224  ? 436 TRP A CD2 1 
ATOM   849  N NE1 . TRP A 1 107 ? -5.46203  -44.01847 -14.89004 1.000 17.55870  ? 436 TRP A NE1 1 
ATOM   850  C CE2 . TRP A 1 107 ? -5.31719  -42.71115 -14.49254 1.000 15.53937  ? 436 TRP A CE2 1 
ATOM   851  C CE3 . TRP A 1 107 ? -6.62584  -41.03494 -13.35322 1.000 14.86507  ? 436 TRP A CE3 1 
ATOM   852  C CZ2 . TRP A 1 107 ? -4.24454  -41.82015 -14.66355 1.000 16.33466  ? 436 TRP A CZ2 1 
ATOM   853  C CZ3 . TRP A 1 107 ? -5.56222  -40.15349 -13.50849 1.000 15.61696  ? 436 TRP A CZ3 1 
ATOM   854  C CH2 . TRP A 1 107 ? -4.39659  -40.53970 -14.16130 1.000 16.96931  ? 436 TRP A CH2 1 
ATOM   855  N N   . ASN A 1 108 ? -9.09459  -46.10772 -11.49921 1.000 14.43104  ? 437 ASN A N   1 
ATOM   856  C CA  . ASN A 1 108 ? -8.59278  -47.41154 -11.09876 1.000 14.96837  ? 437 ASN A CA  1 
ATOM   857  C C   . ASN A 1 108 ? -7.46507  -47.83737 -12.03632 1.000 15.30488  ? 437 ASN A C   1 
ATOM   858  O O   . ASN A 1 108 ? -7.60935  -47.80268 -13.26045 1.000 16.67920  ? 437 ASN A O   1 
ATOM   859  C CB  . ASN A 1 108 ? -9.76047  -48.40485 -11.14536 1.000 16.95156  ? 437 ASN A CB  1 
ATOM   860  C CG  . ASN A 1 108 ? -9.38103  -49.78130 -10.65435 1.000 16.57338  ? 437 ASN A CG  1 
ATOM   861  O OD1 . ASN A 1 108 ? -8.55189  -50.47173 -11.26793 1.000 17.85870  ? 437 ASN A OD1 1 
ATOM   862  N ND2 . ASN A 1 108 ? -9.99605  -50.19726 -9.55092  1.000 18.46939  ? 437 ASN A ND2 1 
ATOM   863  N N   . SER A 1 109 ? -6.34849  -48.28572 -11.47797 1.000 14.17918  ? 438 SER A N   1 
ATOM   864  C CA  . SER A 1 109 ? -5.20360  -48.69709 -12.28040 1.000 15.01162  ? 438 SER A CA  1 
ATOM   865  C C   . SER A 1 109 ? -4.78199  -50.11934 -11.97474 1.000 14.04532  ? 438 SER A C   1 
ATOM   866  O O   . SER A 1 109 ? -3.61781  -50.48415 -12.19779 1.000 15.61259  ? 438 SER A O   1 
ATOM   867  C CB  . SER A 1 109 ? -4.02960  -47.73624 -12.10076 1.000 15.01708  ? 438 SER A CB  1 
ATOM   868  O OG  . SER A 1 109 ? -3.63951  -47.69598 -10.74361 1.000 14.02702  ? 438 SER A OG  1 
ATOM   869  N N   . ASN A 1 110 ? -5.74744  -50.96719 -11.55932 1.000 15.27250  ? 439 ASN A N   1 
ATOM   870  C CA  . ASN A 1 110 ? -5.43557  -52.37391 -11.28637 1.000 15.29480  ? 439 ASN A CA  1 
ATOM   871  C C   . ASN A 1 110 ? -4.72896  -53.06032 -12.45619 1.000 16.45607  ? 439 ASN A C   1 
ATOM   872  O O   . ASN A 1 110 ? -3.86447  -53.91980 -12.24341 1.000 18.32770  ? 439 ASN A O   1 
ATOM   873  C CB  . ASN A 1 110 ? -6.71590  -53.10871 -10.87876 1.000 16.23203  ? 439 ASN A CB  1 
ATOM   874  C CG  . ASN A 1 110 ? -6.43580  -54.36712 -10.10362 1.000 17.20707  ? 439 ASN A CG  1 
ATOM   875  O OD1 . ASN A 1 110 ? -5.55929  -54.39608 -9.25239  1.000 18.06675  ? 439 ASN A OD1 1 
ATOM   876  N ND2 . ASN A 1 110 ? -7.21731  -55.41506 -10.34891 1.000 19.76619  ? 439 ASN A ND2 1 
ATOM   877  N N   . ASN A 1 111 ? -5.08822  -52.70918 -13.69748 1.000 18.06889  ? 440 ASN A N   1 
ATOM   878  C CA  . ASN A 1 111 ? -4.51343  -53.37502 -14.85834 1.000 19.17209  ? 440 ASN A CA  1 
ATOM   879  C C   . ASN A 1 111 ? -3.03751  -53.04126 -15.05589 1.000 20.17813  ? 440 ASN A C   1 
ATOM   880  O O   . ASN A 1 111 ? -2.33497  -53.78676 -15.74726 1.000 24.31431  ? 440 ASN A O   1 
ATOM   881  C CB  . ASN A 1 111 ? -5.29379  -52.97294 -16.13253 1.000 23.65731  ? 440 ASN A CB  1 
ATOM   882  C CG  . ASN A 1 111 ? -5.19598  -51.46428 -16.44757 1.000 26.70040  ? 440 ASN A CG  1 
ATOM   883  O OD1 . ASN A 1 111 ? -5.40680  -50.62230 -15.58097 1.000 28.08985  ? 440 ASN A OD1 1 
ATOM   884  N ND2 . ASN A 1 111 ? -4.93707  -51.12889 -17.72250 1.000 28.60870  ? 440 ASN A ND2 1 
ATOM   885  N N   . LEU A 1 112 ? -2.56926  -51.91233 -14.52986 1.000 17.98228  ? 441 LEU A N   1 
ATOM   886  C CA  . LEU A 1 112 ? -1.19359  -51.47926 -14.71304 1.000 18.32756  ? 441 LEU A CA  1 
ATOM   887  C C   . LEU A 1 112 ? -0.35845  -51.64668 -13.46076 1.000 16.89402  ? 441 LEU A C   1 
ATOM   888  O O   . LEU A 1 112 ? 0.84732   -51.90278 -13.56005 1.000 19.57997  ? 441 LEU A O   1 
ATOM   889  C CB  . LEU A 1 112 ? -1.18502  -49.98152 -15.02244 1.000 20.08947  ? 441 LEU A CB  1 
ATOM   890  C CG  . LEU A 1 112 ? -1.89798  -49.50585 -16.28459 1.000 24.82804  ? 441 LEU A CG  1 
ATOM   891  C CD1 . LEU A 1 112 ? -1.64981  -48.01760 -16.45833 1.000 26.29096  ? 441 LEU A CD1 1 
ATOM   892  C CD2 . LEU A 1 112 ? -1.49381  -50.29144 -17.52146 1.000 27.60872  ? 441 LEU A CD2 1 
ATOM   893  N N   . ASP A 1 113 ? -0.97445  -51.49228 -12.27661 1.000 14.58762  ? 442 ASP A N   1 
ATOM   894  C CA  . ASP A 1 113 ? -0.25771  -51.26040 -11.04104 1.000 13.95715  ? 442 ASP A CA  1 
ATOM   895  C C   . ASP A 1 113 ? -0.34364  -52.39515 -10.03324 1.000 14.89989  ? 442 ASP A C   1 
ATOM   896  O O   . ASP A 1 113 ? 0.23990   -52.28135 -8.94083  1.000 15.22037  ? 442 ASP A O   1 
ATOM   897  C CB  . ASP A 1 113 ? -0.65396  -49.91601 -10.40506 1.000 14.11352  ? 442 ASP A CB  1 
ATOM   898  C CG  . ASP A 1 113 ? -0.27677  -48.75387 -11.27173 1.000 13.56432  ? 442 ASP A CG  1 
ATOM   899  O OD1 . ASP A 1 113 ? 0.80436   -48.82345 -11.91354 1.000 13.32255  ? 442 ASP A OD1 1 
ATOM   900  O OD2 . ASP A 1 113 ? -0.97483  -47.72239 -11.23521 1.000 14.02796  ? 442 ASP A OD2 1 
ATOM   901  N N   . SER A 1 114 ? -1.04330  -53.47556 -10.35126 1.000 14.93851  ? 443 SER A N   1 
ATOM   902  C CA  . SER A 1 114 ? -0.95508  -54.66752 -9.53116  1.000 14.64548  ? 443 SER A CA  1 
ATOM   903  C C   . SER A 1 114 ? -0.03748  -55.67699 -10.20865 1.000 15.02443  ? 443 SER A C   1 
ATOM   904  O O   . SER A 1 114 ? 0.20970   -55.60021 -11.40791 1.000 18.62851  ? 443 SER A O   1 
ATOM   905  C CB  . SER A 1 114 ? -2.33426  -55.29129 -9.35134  1.000 16.91136  ? 443 SER A CB  1 
ATOM   906  O OG  . SER A 1 114 ? -2.82781  -55.81508 -10.57865 1.000 19.38219  ? 443 SER A OG  1 
ATOM   907  N N   . LYS A 1 115 ? 0.48950   -56.58629 -9.41683  1.000 14.12281  ? 444 LYS A N   1 
ATOM   908  C CA  . LYS A 1 115 ? 1.28592   -57.68200 -9.92387  1.000 14.75056  ? 444 LYS A CA  1 
ATOM   909  C C   . LYS A 1 115 ? 0.87200   -58.95117 -9.20046  1.000 13.99760  ? 444 LYS A C   1 
ATOM   910  O O   . LYS A 1 115 ? 0.60057   -58.93850 -7.99510  1.000 14.15454  ? 444 LYS A O   1 
ATOM   911  C CB  . LYS A 1 115 ? 2.81839   -57.49275 -9.74584  1.000 15.52641  ? 444 LYS A CB  1 
ATOM   912  C CG  . LYS A 1 115 ? 3.44963   -56.31404 -10.50837 1.000 17.50003  ? 444 LYS A CG  1 
ATOM   913  C CD  . LYS A 1 115 ? 4.96556   -56.26354 -10.32169 1.000 19.49475  ? 444 LYS A CD  1 
ATOM   914  C CE  . LYS A 1 115 ? 5.63959   -55.48914 -11.44814 1.000 22.67535  ? 444 LYS A CE  1 
ATOM   915  N NZ  . LYS A 1 115 ? 5.39807   -54.06002 -11.20073 1.000 23.81518  ? 444 LYS A NZ  1 
ATOM   916  N N   . VAL A 1 116 ? 0.89664   -60.07788 -9.90970  1.000 14.72842  ? 445 VAL A N   1 
ATOM   917  C CA  . VAL A 1 116 ? 0.74980   -61.35861 -9.22869  1.000 14.86982  ? 445 VAL A CA  1 
ATOM   918  C C   . VAL A 1 116 ? 1.89540   -61.48138 -8.22605  1.000 14.69955  ? 445 VAL A C   1 
ATOM   919  O O   . VAL A 1 116 ? 3.03860   -61.13573 -8.51702  1.000 16.06384  ? 445 VAL A O   1 
ATOM   920  C CB  . VAL A 1 116 ? 0.81235   -62.50778 -10.24242 1.000 15.84630  ? 445 VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 116 ? 0.88965   -63.86953 -9.53607  1.000 16.34306  ? 445 VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 116 ? -0.36262  -62.42245 -11.18902 1.000 19.39940  ? 445 VAL A CG2 1 
ATOM   923  N N   . GLY A 1 117 ? 1.58717   -61.93149 -7.02509  1.000 15.48425  ? 446 GLY A N   1 
ATOM   924  C CA  . GLY A 1 117 ? 2.55946   -61.98312 -5.94854  1.000 16.85574  ? 446 GLY A CA  1 
ATOM   925  C C   . GLY A 1 117 ? 2.77574   -60.67187 -5.23511  1.000 15.55520  ? 446 GLY A C   1 
ATOM   926  O O   . GLY A 1 117 ? 3.54047   -60.63769 -4.26423  1.000 17.90058  ? 446 GLY A O   1 
ATOM   927  N N   . GLY A 1 118 ? 2.11302   -59.59489 -5.66482  1.000 14.47949  ? 447 GLY A N   1 
ATOM   928  C CA  . GLY A 1 118 ? 2.13711   -58.30467 -4.98871  1.000 15.30789  ? 447 GLY A CA  1 
ATOM   929  C C   . GLY A 1 118 ? 3.10653   -57.34216 -5.63455  1.000 14.51663  ? 447 GLY A C   1 
ATOM   930  O O   . GLY A 1 118 ? 4.30025   -57.64482 -5.75668  1.000 16.70129  ? 447 GLY A O   1 
ATOM   931  N N   . ASN A 1 119 ? 2.64497   -56.17567 -6.03533  1.000 13.94086  ? 448 ASN A N   1 
ATOM   932  C CA  . ASN A 1 119 ? 3.57424   -55.20118 -6.57225  1.000 14.17595  ? 448 ASN A CA  1 
ATOM   933  C C   . ASN A 1 119 ? 4.45413   -54.64434 -5.45498  1.000 13.58989  ? 448 ASN A C   1 
ATOM   934  O O   . ASN A 1 119 ? 3.99748   -54.37017 -4.34576  1.000 16.81275  ? 448 ASN A O   1 
ATOM   935  C CB  . ASN A 1 119 ? 2.79714   -54.12327 -7.31448  1.000 15.59623  ? 448 ASN A CB  1 
ATOM   936  C CG  . ASN A 1 119 ? 3.68862   -53.25686 -8.20755  1.000 16.01657  ? 448 ASN A CG  1 
ATOM   937  O OD1 . ASN A 1 119 ? 4.89399   -53.55344 -8.39175  1.000 16.34761  ? 448 ASN A OD1 1 
ATOM   938  N ND2 . ASN A 1 119 ? 3.06362   -52.36192 -8.92013  1.000 16.15607  ? 448 ASN A ND2 1 
ATOM   939  N N   . TYR A 1 120 ? 5.72209   -54.47804 -5.76598  1.000 15.58915  ? 449 TYR A N   1 
ATOM   940  C CA  . TYR A 1 120 ? 6.66491   -53.87616 -4.83387  1.000 16.63725  ? 449 TYR A CA  1 
ATOM   941  C C   . TYR A 1 120 ? 6.88563   -52.38604 -5.08609  1.000 15.73145  ? 449 TYR A C   1 
ATOM   942  O O   . TYR A 1 120 ? 7.48356   -51.71714 -4.24199  1.000 18.73342  ? 449 TYR A O   1 
ATOM   943  C CB  . TYR A 1 120 ? 8.02054   -54.56525 -4.96696  1.000 20.48123  ? 449 TYR A CB  1 
ATOM   944  C CG  . TYR A 1 120 ? 8.45625   -54.67643 -6.39614  1.000 20.23830  ? 449 TYR A CG  1 
ATOM   945  C CD1 . TYR A 1 120 ? 8.08275   -55.77260 -7.19092  1.000 22.49977  ? 449 TYR A CD1 1 
ATOM   946  C CD2 . TYR A 1 120 ? 9.23956   -53.66576 -6.96116  1.000 20.33292  ? 449 TYR A CD2 1 
ATOM   947  C CE1 . TYR A 1 120 ? 8.48716   -55.83652 -8.49884  1.000 22.57064  ? 449 TYR A CE1 1 
ATOM   948  C CE2 . TYR A 1 120 ? 9.64019   -53.71773 -8.25607  1.000 22.92931  ? 449 TYR A CE2 1 
ATOM   949  C CZ  . TYR A 1 120 ? 9.25123   -54.80097 -9.03114  1.000 22.92582  ? 449 TYR A CZ  1 
ATOM   950  O OH  . TYR A 1 120 ? 9.67642   -54.83436 -10.33267 1.000 25.67355  ? 449 TYR A OH  1 
ATOM   951  N N   . ASN A 1 121 ? 6.39914   -51.85577 -6.21832  1.000 14.25422  ? 450 ASN A N   1 
ATOM   952  C CA  A ASN A 1 121 ? 6.82117   -50.52176 -6.65499  0.500 15.76900  ? 450 ASN A CA  1 
ATOM   953  C CA  B ASN A 1 121 ? 6.77815   -50.53484 -6.70129  0.500 16.74932  ? 450 ASN A CA  1 
ATOM   954  C C   . ASN A 1 121 ? 6.19015   -49.38489 -5.87510  1.000 14.65773  ? 450 ASN A C   1 
ATOM   955  O O   . ASN A 1 121 ? 6.80477   -48.32826 -5.75594  1.000 19.64494  ? 450 ASN A O   1 
ATOM   956  C CB  A ASN A 1 121 ? 6.51152   -50.25486 -8.15726  0.500 21.55215  ? 450 ASN A CB  1 
ATOM   957  C CB  B ASN A 1 121 ? 6.25118   -50.49073 -8.14841  0.500 22.20218  ? 450 ASN A CB  1 
ATOM   958  C CG  A ASN A 1 121 ? 7.36740   -51.06159 -9.11793  0.500 30.18018  ? 450 ASN A CG  1 
ATOM   959  C CG  B ASN A 1 121 ? 6.70177   -49.31512 -8.89634  0.500 30.20206  ? 450 ASN A CG  1 
ATOM   960  O OD1 A ASN A 1 121 ? 6.85404   -51.71859 -10.02815 0.500 30.93363  ? 450 ASN A OD1 1 
ATOM   961  O OD1 B ASN A 1 121 ? 7.11770   -48.31864 -8.31699  0.500 33.23611  ? 450 ASN A OD1 1 
ATOM   962  N ND2 A ASN A 1 121 ? 8.67912   -50.98054 -8.95073  0.500 32.63174  ? 450 ASN A ND2 1 
ATOM   963  N ND2 B ASN A 1 121 ? 6.60124   -49.39432 -10.21921 0.500 32.30834  ? 450 ASN A ND2 1 
ATOM   964  N N   . TYR A 1 122 ? 4.98719   -49.55570 -5.34572  1.000 12.66278  ? 451 TYR A N   1 
ATOM   965  C CA  . TYR A 1 122 ? 4.22003   -48.45012 -4.77712  1.000 11.58103  ? 451 TYR A CA  1 
ATOM   966  C C   . TYR A 1 122 ? 4.22991   -48.55291 -3.26224  1.000 10.62631  ? 451 TYR A C   1 
ATOM   967  O O   . TYR A 1 122 ? 3.70463   -49.52503 -2.68370  1.000 11.89859  ? 451 TYR A O   1 
ATOM   968  C CB  . TYR A 1 122 ? 2.80961   -48.49095 -5.33727  1.000 12.39468  ? 451 TYR A CB  1 
ATOM   969  C CG  . TYR A 1 122 ? 2.77417   -48.15616 -6.79271  1.000 11.39671  ? 451 TYR A CG  1 
ATOM   970  C CD1 . TYR A 1 122 ? 3.14790   -46.88998 -7.23622  1.000 13.27064  ? 451 TYR A CD1 1 
ATOM   971  C CD2 . TYR A 1 122 ? 2.42833   -49.11126 -7.74169  1.000 12.15608  ? 451 TYR A CD2 1 
ATOM   972  C CE1 . TYR A 1 122 ? 3.11198   -46.57648 -8.58796  1.000 15.25540  ? 451 TYR A CE1 1 
ATOM   973  C CE2 . TYR A 1 122 ? 2.38949   -48.78909 -9.10825  1.000 13.67983  ? 451 TYR A CE2 1 
ATOM   974  C CZ  . TYR A 1 122 ? 2.73834   -47.53157 -9.50337  1.000 14.01574  ? 451 TYR A CZ  1 
ATOM   975  O OH  . TYR A 1 122 ? 2.70722   -47.18472 -10.84866 1.000 16.79622  ? 451 TYR A OH  1 
ATOM   976  N N   . LEU A 1 123 ? 4.80706   -47.53498 -2.63274  1.000 11.28049  ? 452 LEU A N   1 
ATOM   977  C CA  . LEU A 1 123 ? 4.94534   -47.46928 -1.18920  1.000 11.86026  ? 452 LEU A CA  1 
ATOM   978  C C   . LEU A 1 123 ? 4.17875   -46.27638 -0.63096  1.000 11.32142  ? 452 LEU A C   1 
ATOM   979  O O   . LEU A 1 123 ? 3.86965   -45.31552 -1.33108  1.000 11.51278  ? 452 LEU A O   1 
ATOM   980  C CB  . LEU A 1 123 ? 6.42343   -47.29652 -0.78023  1.000 12.88836  ? 452 LEU A CB  1 
ATOM   981  C CG  . LEU A 1 123 ? 7.46854   -48.12699 -1.54782  1.000 12.21258  ? 452 LEU A CG  1 
ATOM   982  C CD1 . LEU A 1 123 ? 8.85347   -47.80629 -1.05628  1.000 15.04356  ? 452 LEU A CD1 1 
ATOM   983  C CD2 . LEU A 1 123 ? 7.14981   -49.59902 -1.41966  1.000 14.48184  ? 452 LEU A CD2 1 
ATOM   984  N N   . TYR A 1 124 ? 3.90020   -46.31713 0.67352   1.000 11.64601  ? 453 TYR A N   1 
ATOM   985  C CA  . TYR A 1 124 ? 3.39062   -45.14715 1.37353   1.000 11.57851  ? 453 TYR A CA  1 
ATOM   986  C C   . TYR A 1 124 ? 4.09517   -45.04542 2.71815   1.000 11.14319  ? 453 TYR A C   1 
ATOM   987  O O   . TYR A 1 124 ? 4.58213   -46.04264 3.26224   1.000 12.32394  ? 453 TYR A O   1 
ATOM   988  C CB  . TYR A 1 124 ? 1.86106   -45.19009 1.57677   1.000 11.85271  ? 453 TYR A CB  1 
ATOM   989  C CG  . TYR A 1 124 ? 1.39728   -46.36176 2.41080   1.000 12.41586  ? 453 TYR A CG  1 
ATOM   990  C CD1 . TYR A 1 124 ? 1.30364   -47.65035 1.88281   1.000 13.37860  ? 453 TYR A CD1 1 
ATOM   991  C CD2 . TYR A 1 124 ? 1.05095   -46.18745 3.75416   1.000 15.94301  ? 453 TYR A CD2 1 
ATOM   992  C CE1 . TYR A 1 124 ? 0.89443   -48.75007 2.64457   1.000 16.74206  ? 453 TYR A CE1 1 
ATOM   993  C CE2 . TYR A 1 124 ? 0.64505   -47.27124 4.53306   1.000 19.12774  ? 453 TYR A CE2 1 
ATOM   994  C CZ  . TYR A 1 124 ? 0.57182   -48.54533 3.97197   1.000 21.00894  ? 453 TYR A CZ  1 
ATOM   995  O OH  . TYR A 1 124 ? 0.14372   -49.60202 4.76088   1.000 26.57545  ? 453 TYR A OH  1 
ATOM   996  N N   . ARG A 1 125 ? 4.13550   -43.83176 3.27000   1.000 10.90126  ? 454 ARG A N   1 
ATOM   997  C CA  . ARG A 1 125 ? 4.68375   -43.62854 4.59590   1.000 10.97246  ? 454 ARG A CA  1 
ATOM   998  C C   . ARG A 1 125 ? 3.62291   -43.98580 5.63484   1.000 11.49492  ? 454 ARG A C   1 
ATOM   999  O O   . ARG A 1 125 ? 2.49597   -43.45948 5.60208   1.000 12.17661  ? 454 ARG A O   1 
ATOM   1000 C CB  . ARG A 1 125 ? 5.13339   -42.18719 4.75101   1.000 11.41022  ? 454 ARG A CB  1 
ATOM   1001 C CG  . ARG A 1 125 ? 5.85304   -41.92153 6.05503   1.000 11.71957  ? 454 ARG A CG  1 
ATOM   1002 C CD  . ARG A 1 125 ? 6.48699   -40.52308 6.18000   1.000 12.44737  ? 454 ARG A CD  1 
ATOM   1003 N NE  . ARG A 1 125 ? 7.40366   -40.27376 5.07758   1.000 12.31256  ? 454 ARG A NE  1 
ATOM   1004 C CZ  . ARG A 1 125 ? 8.65598   -40.69993 5.00530   1.000 12.41013  ? 454 ARG A CZ  1 
ATOM   1005 N NH1 . ARG A 1 125 ? 9.24627   -41.31014 6.03143   1.000 13.33594  ? 454 ARG A NH1 1 
ATOM   1006 N NH2 . ARG A 1 125 ? 9.33058   -40.56677 3.86174   1.000 13.19467  ? 454 ARG A NH2 1 
ATOM   1007 N N   . LEU A 1 126 ? 3.99099   -44.90320 6.54095   1.000 12.07244  ? 455 LEU A N   1 
ATOM   1008 C CA  . LEU A 1 126 ? 3.06975   -45.45496 7.50927   1.000 13.01162  ? 455 LEU A CA  1 
ATOM   1009 C C   . LEU A 1 126 ? 3.19400   -44.79876 8.87387   1.000 12.33214  ? 455 LEU A C   1 
ATOM   1010 O O   . LEU A 1 126 ? 2.24503   -44.86894 9.65089   1.000 14.68913  ? 455 LEU A O   1 
ATOM   1011 C CB  . LEU A 1 126 ? 3.43244   -46.93340 7.67569   1.000 19.52202  ? 455 LEU A CB  1 
ATOM   1012 C CG  . LEU A 1 126 ? 2.79448   -47.83772 8.68220   1.000 20.70600  ? 455 LEU A CG  1 
ATOM   1013 C CD1 . LEU A 1 126 ? 1.26069   -47.62613 8.55247   1.000 23.61736  ? 455 LEU A CD1 1 
ATOM   1014 C CD2 . LEU A 1 126 ? 3.23559   -49.26238 8.50879   1.000 21.32778  ? 455 LEU A CD2 1 
ATOM   1015 N N   . PHE A 1 127 ? 4.35515   -44.19658 9.16713   1.000 13.36155  ? 456 PHE A N   1 
ATOM   1016 C CA  . PHE A 1 127 ? 4.65420   -43.61648 10.47230  1.000 14.80497  ? 456 PHE A CA  1 
ATOM   1017 C C   . PHE A 1 127 ? 5.29207   -42.26239 10.24848  1.000 14.06159  ? 456 PHE A C   1 
ATOM   1018 O O   . PHE A 1 127 ? 6.16874   -42.13287 9.40469   1.000 13.90512  ? 456 PHE A O   1 
ATOM   1019 C CB  . PHE A 1 127 ? 5.66849   -44.47454 11.27338  1.000 15.68455  ? 456 PHE A CB  1 
ATOM   1020 C CG  . PHE A 1 127 ? 5.19308   -45.86503 11.52498  1.000 15.11435  ? 456 PHE A CG  1 
ATOM   1021 C CD1 . PHE A 1 127 ? 4.11982   -46.10633 12.37484  1.000 18.53073  ? 456 PHE A CD1 1 
ATOM   1022 C CD2 . PHE A 1 127 ? 5.83209   -46.95091 10.93383  1.000 16.56666  ? 456 PHE A CD2 1 
ATOM   1023 C CE1 . PHE A 1 127 ? 3.67504   -47.38884 12.63060  1.000 18.77559  ? 456 PHE A CE1 1 
ATOM   1024 C CE2 . PHE A 1 127 ? 5.37203   -48.25057 11.21220  1.000 16.38973  ? 456 PHE A CE2 1 
ATOM   1025 C CZ  . PHE A 1 127 ? 4.29478   -48.44852 12.05079  1.000 17.29835  ? 456 PHE A CZ  1 
ATOM   1026 N N   . ARG A 1 128 ? 4.88394   -41.27396 11.02838  1.000 14.07103  ? 457 ARG A N   1 
ATOM   1027 C CA  . ARG A 1 128 ? 5.53488   -39.98257 10.99560  1.000 14.23366  ? 457 ARG A CA  1 
ATOM   1028 C C   . ARG A 1 128 ? 5.23982   -39.31596 12.33749  1.000 15.32946  ? 457 ARG A C   1 
ATOM   1029 O O   . ARG A 1 128 ? 4.11950   -39.40462 12.87367  1.000 18.15331  ? 457 ARG A O   1 
ATOM   1030 C CB  . ARG A 1 128 ? 5.07263   -39.11101 9.80162   1.000 14.37787  ? 457 ARG A CB  1 
ATOM   1031 C CG  . ARG A 1 128 ? 6.06123   -38.01098 9.45948   1.000 14.96519  ? 457 ARG A CG  1 
ATOM   1032 C CD  . ARG A 1 128 ? 5.58888   -37.23622 8.25097   1.000 15.13675  ? 457 ARG A CD  1 
ATOM   1033 N NE  . ARG A 1 128 ? 6.63098   -36.34242 7.77925   1.000 14.85283  ? 457 ARG A NE  1 
ATOM   1034 C CZ  . ARG A 1 128 ? 6.74566   -35.06677 8.11230   1.000 17.36888  ? 457 ARG A CZ  1 
ATOM   1035 N NH1 . ARG A 1 128 ? 5.85214   -34.47386 8.88612   1.000 17.52869  ? 457 ARG A NH1 1 
ATOM   1036 N NH2 . ARG A 1 128 ? 7.75592   -34.34836 7.60747   1.000 19.08319  ? 457 ARG A NH2 1 
ATOM   1037 N N   . LYS A 1 129 ? 6.22490   -38.57536 12.85227  1.000 17.65506  ? 458 LYS A N   1 
ATOM   1038 C CA  A LYS A 1 129 ? 6.04861   -37.98566 14.17356  0.500 22.01212  ? 458 LYS A CA  1 
ATOM   1039 C CA  B LYS A 1 129 ? 6.04983   -37.98655 14.17368  0.500 22.01147  ? 458 LYS A CA  1 
ATOM   1040 C C   . LYS A 1 129 ? 5.04608   -36.83685 14.16075  1.000 21.91009  ? 458 LYS A C   1 
ATOM   1041 O O   . LYS A 1 129 ? 4.39868   -36.57657 15.18622  1.000 26.19067  ? 458 LYS A O   1 
ATOM   1042 C CB  A LYS A 1 129 ? 7.39660   -37.53363 14.73568  0.500 29.83887  ? 458 LYS A CB  1 
ATOM   1043 C CB  B LYS A 1 129 ? 7.40153   -37.52691 14.72101  0.500 29.83271  ? 458 LYS A CB  1 
ATOM   1044 C CG  A LYS A 1 129 ? 8.33886   -38.69158 15.10670  0.500 36.50107  ? 458 LYS A CG  1 
ATOM   1045 C CG  B LYS A 1 129 ? 8.30529   -38.67616 15.20666  0.500 36.53237  ? 458 LYS A CG  1 
ATOM   1046 C CD  A LYS A 1 129 ? 7.84822   -39.46382 16.32748  0.500 42.01144  ? 458 LYS A CD  1 
ATOM   1047 C CD  B LYS A 1 129 ? 7.72320   -39.42944 16.40100  0.500 41.94594  ? 458 LYS A CD  1 
ATOM   1048 C CE  A LYS A 1 129 ? 8.61331   -40.78483 16.51323  0.500 44.34882  ? 458 LYS A CE  1 
ATOM   1049 C CE  B LYS A 1 129 ? 8.68772   -40.51434 16.90852  0.500 44.45017  ? 458 LYS A CE  1 
ATOM   1050 N NZ  A LYS A 1 129 ? 9.91919   -40.64160 17.22039  0.500 45.12460  ? 458 LYS A NZ  1 
ATOM   1051 N NZ  B LYS A 1 129 ? 8.31015   -41.01865 18.26893  0.500 45.80865  ? 458 LYS A NZ  1 
ATOM   1052 N N   . SER A 1 130 ? 4.90346   -36.12301 13.04678  1.000 19.39013  ? 459 SER A N   1 
ATOM   1053 C CA  . SER A 1 130 ? 3.91950   -35.06117 12.95260  1.000 17.64188  ? 459 SER A CA  1 
ATOM   1054 C C   . SER A 1 130 ? 3.34228   -35.07593 11.54901  1.000 16.37433  ? 459 SER A C   1 
ATOM   1055 O O   . SER A 1 130 ? 3.88029   -35.69027 10.61771  1.000 15.73958  ? 459 SER A O   1 
ATOM   1056 C CB  . SER A 1 130 ? 4.51078   -33.67431 13.16201  1.000 19.67516  ? 459 SER A CB  1 
ATOM   1057 O OG  . SER A 1 130 ? 5.56471   -33.43794 12.27620  1.000 25.86565  ? 459 SER A OG  1 
ATOM   1058 N N   . ASN A 1 131 ? 2.23832   -34.38055 11.40021  1.000 15.60459  ? 460 ASN A N   1 
ATOM   1059 C CA  . ASN A 1 131 ? 1.55979   -34.27359 10.12122  1.000 15.98815  ? 460 ASN A CA  1 
ATOM   1060 C C   . ASN A 1 131 ? 2.31543   -33.40053 9.14143   1.000 15.10174  ? 460 ASN A C   1 
ATOM   1061 O O   . ASN A 1 131 ? 2.94712   -32.41341 9.50652   1.000 16.84626  ? 460 ASN A O   1 
ATOM   1062 C CB  . ASN A 1 131 ? 0.19201   -33.65741 10.33558  1.000 20.88807  ? 460 ASN A CB  1 
ATOM   1063 C CG  . ASN A 1 131 ? -0.73841  -34.62591 11.00046  1.000 28.67867  ? 460 ASN A CG  1 
ATOM   1064 O OD1 . ASN A 1 131 ? -0.33005  -35.75075 11.31941  1.000 30.24453  ? 460 ASN A OD1 1 
ATOM   1065 N ND2 . ASN A 1 131 ? -1.95143  -34.20046 11.27350  1.000 33.77418  ? 460 ASN A ND2 1 
ATOM   1066 N N   . LEU A 1 132 ? 2.16304   -33.73839 7.87224   1.000 14.01581  ? 461 LEU A N   1 
ATOM   1067 C CA  . LEU A 1 132 ? 2.69334   -32.88103 6.82968   1.000 14.15646  ? 461 LEU A CA  1 
ATOM   1068 C C   . LEU A 1 132 ? 1.91594   -31.57605 6.76213   1.000 14.35425  ? 461 LEU A C   1 
ATOM   1069 O O   . LEU A 1 132 ? 0.69586   -31.53508 6.96488   1.000 15.66839  ? 461 LEU A O   1 
ATOM   1070 C CB  . LEU A 1 132 ? 2.49620   -33.51856 5.46501   1.000 15.50450  ? 461 LEU A CB  1 
ATOM   1071 C CG  . LEU A 1 132 ? 3.37534   -34.71593 5.11834   1.000 15.56961  ? 461 LEU A CG  1 
ATOM   1072 C CD1 . LEU A 1 132 ? 2.99029   -35.25392 3.73333   1.000 16.31217  ? 461 LEU A CD1 1 
ATOM   1073 C CD2 . LEU A 1 132 ? 4.84515   -34.36311 5.17653   1.000 15.94609  ? 461 LEU A CD2 1 
ATOM   1074 N N   . LYS A 1 133 ? 2.63017   -30.50018 6.44969   1.000 15.57761  ? 462 LYS A N   1 
ATOM   1075 C CA  . LYS A 1 133 ? 1.98309   -29.25149 6.08689   1.000 15.72702  ? 462 LYS A CA  1 
ATOM   1076 C C   . LYS A 1 133 ? 1.46833   -29.38378 4.65929   1.000 14.45109  ? 462 LYS A C   1 
ATOM   1077 O O   . LYS A 1 133 ? 1.90963   -30.26863 3.92003   1.000 14.72439  ? 462 LYS A O   1 
ATOM   1078 C CB  . LYS A 1 133 ? 3.01599   -28.14636 6.16359   1.000 18.26360  ? 462 LYS A CB  1 
ATOM   1079 C CG  . LYS A 1 133 ? 3.43737   -27.90851 7.59801   1.000 24.49961  ? 462 LYS A CG  1 
ATOM   1080 C CD  . LYS A 1 133 ? 4.19330   -26.61899 7.73256   1.000 32.23615  ? 462 LYS A CD  1 
ATOM   1081 C CE  . LYS A 1 133 ? 4.71247   -26.37309 9.16032   1.000 39.85469  ? 462 LYS A CE  1 
ATOM   1082 N NZ  . LYS A 1 133 ? 4.44932   -27.49371 10.10778  1.000 43.10705  ? 462 LYS A NZ  1 
ATOM   1083 N N   . PRO A 1 134 ? 0.55411   -28.51110 4.22562   1.000 15.28458  ? 463 PRO A N   1 
ATOM   1084 C CA  . PRO A 1 134 ? 0.02251   -28.66929 2.85873   1.000 15.42731  ? 463 PRO A CA  1 
ATOM   1085 C C   . PRO A 1 134 ? 1.13739   -28.60431 1.82107   1.000 14.95722  ? 463 PRO A C   1 
ATOM   1086 O O   . PRO A 1 134 ? 2.03248   -27.75183 1.88311   1.000 16.53275  ? 463 PRO A O   1 
ATOM   1087 C CB  . PRO A 1 134 ? -0.99290  -27.52784 2.72700   1.000 16.88278  ? 463 PRO A CB  1 
ATOM   1088 C CG  . PRO A 1 134 ? -1.43819  -27.28292 4.17789   1.000 17.61130  ? 463 PRO A CG  1 
ATOM   1089 C CD  . PRO A 1 134 ? -0.19057  -27.49302 5.00076   1.000 17.04829  ? 463 PRO A CD  1 
ATOM   1090 N N   . PHE A 1 135 ? 1.10397   -29.54229 0.87865   1.000 14.11194  ? 464 PHE A N   1 
ATOM   1091 C CA  . PHE A 1 135 ? 2.07506   -29.63147 -0.21902  1.000 14.66317  ? 464 PHE A CA  1 
ATOM   1092 C C   . PHE A 1 135 ? 3.49552   -29.93362 0.24514   1.000 13.85037  ? 464 PHE A C   1 
ATOM   1093 O O   . PHE A 1 135 ? 4.42752   -29.87349 -0.57027  1.000 15.68376  ? 464 PHE A O   1 
ATOM   1094 C CB  . PHE A 1 135 ? 2.05758   -28.42100 -1.17195  1.000 14.83823  ? 464 PHE A CB  1 
ATOM   1095 C CG  . PHE A 1 135 ? 0.72868   -28.21284 -1.85596  1.000 14.78630  ? 464 PHE A CG  1 
ATOM   1096 C CD1 . PHE A 1 135 ? 0.21120   -29.18755 -2.69494  1.000 15.15925  ? 464 PHE A CD1 1 
ATOM   1097 C CD2 . PHE A 1 135 ? 0.00951   -27.01968 -1.69203  1.000 16.40366  ? 464 PHE A CD2 1 
ATOM   1098 C CE1 . PHE A 1 135 ? -1.01935  -28.99344 -3.32071  1.000 16.15942  ? 464 PHE A CE1 1 
ATOM   1099 C CE2 . PHE A 1 135 ? -1.22592  -26.81744 -2.33481  1.000 17.60433  ? 464 PHE A CE2 1 
ATOM   1100 C CZ  . PHE A 1 135 ? -1.72478  -27.81394 -3.15721  1.000 18.12214  ? 464 PHE A CZ  1 
ATOM   1101 N N   . GLU A 1 136 ? 3.67029   -30.38848 1.48638   1.000 14.33288  ? 465 GLU A N   1 
ATOM   1102 C CA  . GLU A 1 136 ? 4.98314   -30.80151 1.93407   1.000 14.48114  ? 465 GLU A CA  1 
ATOM   1103 C C   . GLU A 1 136 ? 5.24487   -32.21070 1.40266   1.000 14.03849  ? 465 GLU A C   1 
ATOM   1104 O O   . GLU A 1 136 ? 4.30857   -32.97142 1.09216   1.000 14.48253  ? 465 GLU A O   1 
ATOM   1105 C CB  . GLU A 1 136 ? 5.04882   -30.75712 3.46412   1.000 16.31202  ? 465 GLU A CB  1 
ATOM   1106 C CG  . GLU A 1 136 ? 6.36029   -31.24381 4.07153   1.000 19.04588  ? 465 GLU A CG  1 
ATOM   1107 C CD  . GLU A 1 136 ? 6.46385   -30.94643 5.56938   1.000 19.28554  ? 465 GLU A CD  1 
ATOM   1108 O OE1 . GLU A 1 136 ? 5.43993   -30.76419 6.25663   1.000 18.35401  ? 465 GLU A OE1 1 
ATOM   1109 O OE2 . GLU A 1 136 ? 7.60888   -30.91424 6.05621   1.000 25.62258  ? 465 GLU A OE2 1 
ATOM   1110 N N   . ARG A 1 137 ? 6.52114   -32.53039 1.26478   1.000 14.09843  ? 466 ARG A N   1 
ATOM   1111 C CA  . ARG A 1 137 ? 6.96006   -33.81173 0.71786   1.000 13.52160  ? 466 ARG A CA  1 
ATOM   1112 C C   . ARG A 1 137 ? 8.07780   -34.36045 1.57422   1.000 14.70489  ? 466 ARG A C   1 
ATOM   1113 O O   . ARG A 1 137 ? 9.02339   -33.63258 1.87755   1.000 16.54162  ? 466 ARG A O   1 
ATOM   1114 C CB  . ARG A 1 137 ? 7.41781   -33.59890 -0.72855  1.000 13.38941  ? 466 ARG A CB  1 
ATOM   1115 C CG  . ARG A 1 137 ? 7.70206   -34.85539 -1.52504  1.000 14.29993  ? 466 ARG A CG  1 
ATOM   1116 C CD  . ARG A 1 137 ? 7.83851   -34.49220 -3.00296  1.000 15.58644  ? 466 ARG A CD  1 
ATOM   1117 N NE  . ARG A 1 137 ? 8.11319   -35.61300 -3.89420  1.000 15.22434  ? 466 ARG A NE  1 
ATOM   1118 C CZ  . ARG A 1 137 ? 9.30080   -35.95193 -4.37915  1.000 13.84139  ? 466 ARG A CZ  1 
ATOM   1119 N NH1 . ARG A 1 137 ? 10.42054  -35.42868 -3.89644  1.000 14.05699  ? 466 ARG A NH1 1 
ATOM   1120 N NH2 . ARG A 1 137 ? 9.36561   -36.89132 -5.33376  1.000 15.67086  ? 466 ARG A NH2 1 
ATOM   1121 N N   . ASP A 1 138 ? 7.95254   -35.62032 1.98612   1.000 13.50520  ? 467 ASP A N   1 
ATOM   1122 C CA  . ASP A 1 138 ? 8.92140   -36.26102 2.86993   1.000 13.46244  ? 467 ASP A CA  1 
ATOM   1123 C C   . ASP A 1 138 ? 9.34999   -37.54948 2.18313   1.000 13.20147  ? 467 ASP A C   1 
ATOM   1124 O O   . ASP A 1 138 ? 8.54069   -38.48951 2.05969   1.000 13.04572  ? 467 ASP A O   1 
ATOM   1125 C CB  . ASP A 1 138 ? 8.29627   -36.53320 4.23327   1.000 14.06044  ? 467 ASP A CB  1 
ATOM   1126 C CG  . ASP A 1 138 ? 9.29011   -37.07411 5.22217   1.000 14.53911  ? 467 ASP A CG  1 
ATOM   1127 O OD1 . ASP A 1 138 ? 10.42922  -37.44430 4.83984   1.000 15.09280  ? 467 ASP A OD1 1 
ATOM   1128 O OD2 . ASP A 1 138 ? 8.89901   -37.23419 6.39823   1.000 15.60485  ? 467 ASP A OD2 1 
ATOM   1129 N N   . ILE A 1 139 ? 10.59528  -37.58057 1.72494   1.000 13.76142  ? 468 ILE A N   1 
ATOM   1130 C CA  . ILE A 1 139 ? 11.14722  -38.77495 1.09763   1.000 13.52566  ? 468 ILE A CA  1 
ATOM   1131 C C   . ILE A 1 139 ? 12.22875  -39.42448 1.95363   1.000 13.34520  ? 468 ILE A C   1 
ATOM   1132 O O   . ILE A 1 139 ? 12.94372  -40.31539 1.47985   1.000 14.62927  ? 468 ILE A O   1 
ATOM   1133 C CB  . ILE A 1 139 ? 11.60448  -38.50771 -0.35362  1.000 13.32113  ? 468 ILE A CB  1 
ATOM   1134 C CG1 . ILE A 1 139 ? 12.66679  -37.39709 -0.40692  1.000 14.58157  ? 468 ILE A CG1 1 
ATOM   1135 C CG2 . ILE A 1 139 ? 10.38958  -38.15961 -1.21445  1.000 14.83286  ? 468 ILE A CG2 1 
ATOM   1136 C CD1 . ILE A 1 139 ? 13.31386  -37.26097 -1.73399  1.000 15.85381  ? 468 ILE A CD1 1 
ATOM   1137 N N   . SER A 1 140 ? 12.31352  -39.04387 3.23333   1.000 13.61429  ? 469 SER A N   1 
ATOM   1138 C CA  . SER A 1 140 ? 13.33881  -39.60852 4.10392   1.000 15.04380  ? 469 SER A CA  1 
ATOM   1139 C C   . SER A 1 140 ? 13.02514  -41.06801 4.47544   1.000 13.64102  ? 469 SER A C   1 
ATOM   1140 O O   . SER A 1 140 ? 11.86671  -41.52680 4.40808   1.000 13.32226  ? 469 SER A O   1 
ATOM   1141 C CB  . SER A 1 140 ? 13.46981  -38.76707 5.36966   1.000 15.80732  ? 469 SER A CB  1 
ATOM   1142 O OG  . SER A 1 140 ? 12.29060  -38.81521 6.15753   1.000 15.81934  ? 469 SER A OG  1 
ATOM   1143 N N   . THR A 1 141 ? 14.06572  -41.80431 4.89564   1.000 13.58882  ? 470 THR A N   1 
ATOM   1144 C CA  . THR A 1 141 ? 13.83225  -43.18262 5.33871   1.000 16.37781  ? 470 THR A CA  1 
ATOM   1145 C C   . THR A 1 141 ? 14.67448  -43.44920 6.59507   1.000 14.69464  ? 470 THR A C   1 
ATOM   1146 O O   . THR A 1 141 ? 15.43685  -44.41574 6.68149   1.000 16.40073  ? 470 THR A O   1 
ATOM   1147 C CB  . THR A 1 141 ? 14.15599  -44.24193 4.30812   1.000 23.72953  ? 470 THR A CB  1 
ATOM   1148 O OG1 . THR A 1 141 ? 15.47073  -44.01700 3.85671   1.000 25.61496  ? 470 THR A OG1 1 
ATOM   1149 C CG2 . THR A 1 141 ? 13.23743  -44.04027 3.06172   1.000 24.50600  ? 470 THR A CG2 1 
ATOM   1150 N N   . GLU A 1 142 ? 14.49902  -42.59283 7.58696   1.000 14.20395  ? 471 GLU A N   1 
ATOM   1151 C CA  . GLU A 1 142 ? 15.07023  -42.81990 8.91200   1.000 14.37085  ? 471 GLU A CA  1 
ATOM   1152 C C   . GLU A 1 142 ? 14.22899  -43.83366 9.66843   1.000 12.76483  ? 471 GLU A C   1 
ATOM   1153 O O   . GLU A 1 142 ? 13.00208  -43.85693 9.55954   1.000 14.51389  ? 471 GLU A O   1 
ATOM   1154 C CB  . GLU A 1 142 ? 15.05755  -41.51131 9.67962   1.000 18.87472  ? 471 GLU A CB  1 
ATOM   1155 C CG  . GLU A 1 142 ? 15.82210  -40.42475 8.95539   1.000 28.18332  ? 471 GLU A CG  1 
ATOM   1156 C CD  . GLU A 1 142 ? 16.22074  -39.26403 9.84889   1.000 35.05693  ? 471 GLU A CD  1 
ATOM   1157 O OE1 . GLU A 1 142 ? 16.99338  -38.40536 9.35220   1.000 38.01881  ? 471 GLU A OE1 1 
ATOM   1158 O OE2 . GLU A 1 142 ? 15.76595  -39.20069 11.02025  1.000 35.97102  ? 471 GLU A OE2 1 
ATOM   1159 N N   . ILE A 1 143 ? 14.88283  -44.65717 10.47295  1.000 12.55398  ? 472 ILE A N   1 
ATOM   1160 C CA  . ILE A 1 143 ? 14.12788  -45.58154 11.29196  1.000 13.27028  ? 472 ILE A CA  1 
ATOM   1161 C C   . ILE A 1 143 ? 13.27912  -44.78782 12.27345  1.000 13.95439  ? 472 ILE A C   1 
ATOM   1162 O O   . ILE A 1 143 ? 13.77676  -43.87329 12.95054  1.000 15.05092  ? 472 ILE A O   1 
ATOM   1163 C CB  . ILE A 1 143 ? 15.06528  -46.56294 12.01889  1.000 13.91332  ? 472 ILE A CB  1 
ATOM   1164 C CG1 . ILE A 1 143 ? 15.97886  -47.31317 11.03124  1.000 14.54876  ? 472 ILE A CG1 1 
ATOM   1165 C CG2 . ILE A 1 143 ? 14.28987  -47.54527 12.89420  1.000 15.96489  ? 472 ILE A CG2 1 
ATOM   1166 C CD1 . ILE A 1 143 ? 15.21001  -48.08177 9.95198   1.000 16.06881  ? 472 ILE A CD1 1 
ATOM   1167 N N   . TYR A 1 144 ? 11.99756  -45.13175 12.35606  1.000 13.94250  ? 473 TYR A N   1 
ATOM   1168 C CA  . TYR A 1 144 ? 11.06855  -44.41647 13.20812  1.000 13.77833  ? 473 TYR A CA  1 
ATOM   1169 C C   . TYR A 1 144 ? 11.19012  -44.98856 14.62178  1.000 14.43264  ? 473 TYR A C   1 
ATOM   1170 O O   . TYR A 1 144 ? 10.92719  -46.18138 14.86161  1.000 14.47938  ? 473 TYR A O   1 
ATOM   1171 C CB  . TYR A 1 144 ? 9.66210   -44.67376 12.69595  1.000 14.43414  ? 473 TYR A CB  1 
ATOM   1172 C CG  . TYR A 1 144 ? 8.57323   -43.97656 13.48556  1.000 13.24384  ? 473 TYR A CG  1 
ATOM   1173 C CD1 . TYR A 1 144 ? 8.17652   -42.67089 13.17066  1.000 15.31037  ? 473 TYR A CD1 1 
ATOM   1174 C CD2 . TYR A 1 144 ? 7.95527   -44.60584 14.55920  1.000 16.17784  ? 473 TYR A CD2 1 
ATOM   1175 C CE1 . TYR A 1 144 ? 7.18382   -42.04617 13.86553  1.000 17.22167  ? 473 TYR A CE1 1 
ATOM   1176 C CE2 . TYR A 1 144 ? 6.95456   -43.97243 15.27318  1.000 16.31255  ? 473 TYR A CE2 1 
ATOM   1177 C CZ  . TYR A 1 144 ? 6.58023   -42.69316 14.92252  1.000 18.44669  ? 473 TYR A CZ  1 
ATOM   1178 O OH  . TYR A 1 144 ? 5.59850   -42.05464 15.63732  1.000 25.03481  ? 473 TYR A OH  1 
ATOM   1179 N N   . GLN A 1 145 ? 11.58417  -44.16177 15.57158  1.000 15.14494  ? 474 GLN A N   1 
ATOM   1180 C CA  . GLN A 1 145 ? 11.77462  -44.63439 16.93739  1.000 16.21571  ? 474 GLN A CA  1 
ATOM   1181 C C   . GLN A 1 145 ? 10.46735  -44.54229 17.71684  1.000 15.99602  ? 474 GLN A C   1 
ATOM   1182 O O   . GLN A 1 145 ? 10.02892  -43.45096 18.09941  1.000 17.85063  ? 474 GLN A O   1 
ATOM   1183 C CB  . GLN A 1 145 ? 12.83057  -43.79923 17.61150  1.000 17.23946  ? 474 GLN A CB  1 
ATOM   1184 C CG  . GLN A 1 145 ? 13.08043  -44.32820 19.00681  1.000 19.11633  ? 474 GLN A CG  1 
ATOM   1185 C CD  . GLN A 1 145 ? 14.08041  -43.51570 19.79785  1.000 21.44475  ? 474 GLN A CD  1 
ATOM   1186 O OE1 . GLN A 1 145 ? 14.93936  -42.82693 19.22462  1.000 21.46650  ? 474 GLN A OE1 1 
ATOM   1187 N NE2 . GLN A 1 145 ? 13.92000  -43.50409 21.13982  1.000 21.32587  ? 474 GLN A NE2 1 
ATOM   1188 N N   . ALA A 1 146 ? 9.83169   -45.68938 17.93008  1.000 17.13047  ? 475 ALA A N   1 
ATOM   1189 C CA  . ALA A 1 146 ? 8.50286   -45.72624 18.52072  1.000 17.88233  ? 475 ALA A CA  1 
ATOM   1190 C C   . ALA A 1 146 ? 8.55734   -45.71711 20.04836  1.000 18.91230  ? 475 ALA A C   1 
ATOM   1191 O O   . ALA A 1 146 ? 7.61479   -45.26087 20.69195  1.000 23.09268  ? 475 ALA A O   1 
ATOM   1192 C CB  . ALA A 1 146 ? 7.74931   -46.93909 17.98032  1.000 19.23098  ? 475 ALA A CB  1 
ATOM   1193 N N   . GLY A 1 147 ? 9.65075   -46.17305 20.63333  1.000 19.41069  ? 476 GLY A N   1 
ATOM   1194 C CA  . GLY A 1 147 ? 9.70046   -46.21479 22.06814  1.000 21.63082  ? 476 GLY A CA  1 
ATOM   1195 C C   . GLY A 1 147 ? 10.86310  -45.45307 22.65924  1.000 21.11778  ? 476 GLY A C   1 
ATOM   1196 O O   . GLY A 1 147 ? 11.47911  -44.58430 22.03483  1.000 21.82506  ? 476 GLY A O   1 
ATOM   1197 N N   . SER A 1 148 ? 11.17096  -45.80847 23.88965  1.000 20.68117  ? 477 SER A N   1 
ATOM   1198 C CA  A SER A 1 148 ? 12.23470  -45.20000 24.66825  0.580 20.86308  ? 477 SER A CA  1 
ATOM   1199 C CA  B SER A 1 148 ? 12.25005  -45.13277 24.59145  0.420 20.90518  ? 477 SER A CA  1 
ATOM   1200 C C   . SER A 1 148 ? 13.62037  -45.71359 24.30446  1.000 21.58084  ? 477 SER A C   1 
ATOM   1201 O O   . SER A 1 148 ? 14.61876  -45.07352 24.64320  1.000 23.28635  ? 477 SER A O   1 
ATOM   1202 C CB  A SER A 1 148 ? 11.89803  -45.43265 26.14281  0.580 22.55505  ? 477 SER A CB  1 
ATOM   1203 C CB  B SER A 1 148 ? 12.00098  -45.13609 26.09337  0.420 22.42733  ? 477 SER A CB  1 
ATOM   1204 O OG  A SER A 1 148 ? 12.29554  -46.71901 26.57828  0.580 23.83289  ? 477 SER A OG  1 
ATOM   1205 O OG  B SER A 1 148 ? 10.80237  -44.44543 26.35468  0.420 23.89137  ? 477 SER A OG  1 
ATOM   1206 N N   . THR A 1 149 ? 13.71271  -46.83899 23.61419  1.000 20.52644  ? 478 THR A N   1 
ATOM   1207 C CA  . THR A 1 149 ? 15.00597  -47.39403 23.27095  1.000 20.42345  ? 478 THR A CA  1 
ATOM   1208 C C   . THR A 1 149 ? 15.49070  -46.79091 21.95496  1.000 17.66909  ? 478 THR A C   1 
ATOM   1209 O O   . THR A 1 149 ? 14.80574  -46.91609 20.94346  1.000 18.64746  ? 478 THR A O   1 
ATOM   1210 C CB  . THR A 1 149 ? 14.87070  -48.91592 23.15769  1.000 22.70538  ? 478 THR A CB  1 
ATOM   1211 O OG1 . THR A 1 149 ? 14.32695  -49.44881 24.36919  1.000 26.83554  ? 478 THR A OG1 1 
ATOM   1212 C CG2 . THR A 1 149 ? 16.19485  -49.55351 22.83503  1.000 24.29752  ? 478 THR A CG2 1 
ATOM   1213 N N   . PRO A 1 150 ? 16.66423  -46.18177 21.90998  1.000 17.47707  ? 479 PRO A N   1 
ATOM   1214 C CA  A PRO A 1 150 ? 17.20154  -45.67703 20.63797  0.500 16.42836  ? 479 PRO A CA  1 
ATOM   1215 C CA  B PRO A 1 150 ? 17.16248  -45.67729 20.62866  0.500 16.44424  ? 479 PRO A CA  1 
ATOM   1216 C C   . PRO A 1 150 ? 17.33683  -46.82561 19.65649  1.000 14.85572  ? 479 PRO A C   1 
ATOM   1217 O O   . PRO A 1 150 ? 17.70984  -47.94391 20.03726  1.000 16.71170  ? 479 PRO A O   1 
ATOM   1218 C CB  A PRO A 1 150 ? 18.59103  -45.13967 21.02332  0.500 17.65633  ? 479 PRO A CB  1 
ATOM   1219 C CB  B PRO A 1 150 ? 18.50105  -45.02854 20.99816  0.500 17.72899  ? 479 PRO A CB  1 
ATOM   1220 C CG  A PRO A 1 150 ? 18.94562  -45.85368 22.33101  0.500 18.82162  ? 479 PRO A CG  1 
ATOM   1221 C CG  B PRO A 1 150 ? 18.29927  -44.61598 22.40340  0.500 19.21480  ? 479 PRO A CG  1 
ATOM   1222 C CD  A PRO A 1 150 ? 17.60451  -46.00058 23.02738  0.500 18.59856  ? 479 PRO A CD  1 
ATOM   1223 C CD  B PRO A 1 150 ? 17.47730  -45.71724 23.03785  0.500 18.72099  ? 479 PRO A CD  1 
ATOM   1224 N N   . CYS A 1 151 ? 17.05272  -46.53710 18.37907  1.000 13.89505  ? 480 CYS A N   1 
ATOM   1225 C CA  . CYS A 1 151 ? 17.15150  -47.57626 17.36850  1.000 13.72820  ? 480 CYS A CA  1 
ATOM   1226 C C   . CYS A 1 151 ? 18.54154  -47.74366 16.80330  1.000 14.04541  ? 480 CYS A C   1 
ATOM   1227 O O   . CYS A 1 151 ? 18.86075  -48.80918 16.27522  1.000 14.34869  ? 480 CYS A O   1 
ATOM   1228 C CB  . CYS A 1 151 ? 16.17918  -47.27159 16.22852  1.000 15.66958  ? 480 CYS A CB  1 
ATOM   1229 S SG  . CYS A 1 151 ? 14.47721  -47.20484 16.84370  1.000 17.09791  ? 480 CYS A SG  1 
ATOM   1230 N N   . ASN A 1 152 ? 19.36661  -46.71509 16.86733  1.000 14.37098  ? 481 ASN A N   1 
ATOM   1231 C CA  . ASN A 1 152 ? 20.74148  -46.84595 16.41611  1.000 14.74405  ? 481 ASN A CA  1 
ATOM   1232 C C   . ASN A 1 152 ? 20.82706  -47.37443 14.97552  1.000 15.20984  ? 481 ASN A C   1 
ATOM   1233 O O   . ASN A 1 152 ? 21.73760  -48.12357 14.59817  1.000 16.61017  ? 481 ASN A O   1 
ATOM   1234 C CB  . ASN A 1 152 ? 21.52749  -47.69055 17.41150  1.000 16.09098  ? 481 ASN A CB  1 
ATOM   1235 C CG  . ASN A 1 152 ? 21.51196  -47.04414 18.75867  1.000 15.94178  ? 481 ASN A CG  1 
ATOM   1236 O OD1 . ASN A 1 152 ? 21.68940  -45.84628 18.87875  1.000 17.20869  ? 481 ASN A OD1 1 
ATOM   1237 N ND2 . ASN A 1 152 ? 21.29093  -47.80797 19.78844  1.000 20.58296  ? 481 ASN A ND2 1 
ATOM   1238 N N   . GLY A 1 153 ? 19.88245  -46.94938 14.12980  1.000 15.10927  ? 482 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 153 ? 19.94646  -47.28931 12.72317  1.000 15.54700  ? 482 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 153 ? 19.60002  -48.72098 12.44454  1.000 14.36441  ? 482 GLY A C   1 
ATOM   1241 O O   . GLY A 1 153 ? 19.90933  -49.21640 11.35475  1.000 17.38582  ? 482 GLY A O   1 
ATOM   1242 N N   . VAL A 1 154 ? 18.89279  -49.39348 13.35949  1.000 13.62484  ? 483 VAL A N   1 
ATOM   1243 C CA  . VAL A 1 154 ? 18.49587  -50.78839 13.16975  1.000 13.93778  ? 483 VAL A CA  1 
ATOM   1244 C C   . VAL A 1 154 ? 16.98941  -50.94180 13.35710  1.000 13.14109  ? 483 VAL A C   1 
ATOM   1245 O O   . VAL A 1 154 ? 16.42495  -50.51476 14.37516  1.000 14.66376  ? 483 VAL A O   1 
ATOM   1246 C CB  . VAL A 1 154 ? 19.26759  -51.72257 14.12421  1.000 16.01287  ? 483 VAL A CB  1 
ATOM   1247 C CG1 . VAL A 1 154 ? 18.98078  -53.16770 13.80336  1.000 18.30290  ? 483 VAL A CG1 1 
ATOM   1248 C CG2 . VAL A 1 154 ? 20.78056  -51.45838 14.02692  1.000 17.82888  ? 483 VAL A CG2 1 
ATOM   1249 N N   . GLU A 1 155 ? 16.34654  -51.51265 12.34656  1.000 13.63209  ? 484 GLU A N   1 
ATOM   1250 C CA  . GLU A 1 155 ? 14.93780  -51.79781 12.41227  1.000 14.34690  ? 484 GLU A CA  1 
ATOM   1251 C C   . GLU A 1 155 ? 14.70592  -53.02248 13.27206  1.000 16.06458  ? 484 GLU A C   1 
ATOM   1252 O O   . GLU A 1 155 ? 15.47460  -53.98861 13.26746  1.000 20.48073  ? 484 GLU A O   1 
ATOM   1253 C CB  . GLU A 1 155 ? 14.43036  -52.04634 10.98629  1.000 16.61639  ? 484 GLU A CB  1 
ATOM   1254 C CG  . GLU A 1 155 ? 13.01383  -52.57267 10.84241  1.000 17.88221  ? 484 GLU A CG  1 
ATOM   1255 C CD  . GLU A 1 155 ? 13.03526  -54.10526 10.90738  1.000 19.00680  ? 484 GLU A CD  1 
ATOM   1256 O OE1 . GLU A 1 155 ? 13.99227  -54.71624 10.37590  1.000 24.91953  ? 484 GLU A OE1 1 
ATOM   1257 O OE2 . GLU A 1 155 ? 12.10728  -54.71353 11.47694  1.000 19.18184  ? 484 GLU A OE2 1 
ATOM   1258 N N   . GLY A 1 156 ? 13.58393  -53.00663 13.97126  1.000 15.49865  ? 485 GLY A N   1 
ATOM   1259 C CA  . GLY A 1 156 ? 13.20168  -54.13578 14.78861  1.000 19.63109  ? 485 GLY A CA  1 
ATOM   1260 C C   . GLY A 1 156 ? 12.09908  -53.71127 15.73313  1.000 19.38420  ? 485 GLY A C   1 
ATOM   1261 O O   . GLY A 1 156 ? 11.25347  -52.88310 15.39202  1.000 18.18250  ? 485 GLY A O   1 
ATOM   1262 N N   . PHE A 1 157 ? 12.09459  -54.25924 16.93146  1.000 20.60077  ? 486 PHE A N   1 
ATOM   1263 C CA  . PHE A 1 157 ? 11.05218  -53.94038 17.89818  1.000 21.03713  ? 486 PHE A CA  1 
ATOM   1264 C C   . PHE A 1 157 ? 11.04528  -52.44549 18.20350  1.000 18.65749  ? 486 PHE A C   1 
ATOM   1265 O O   . PHE A 1 157 ? 12.08118  -51.85733 18.52445  1.000 18.55194  ? 486 PHE A O   1 
ATOM   1266 C CB  . PHE A 1 157 ? 11.30886  -54.74324 19.16642  1.000 24.80473  ? 486 PHE A CB  1 
ATOM   1267 C CG  . PHE A 1 157 ? 10.24397  -54.58380 20.19288  1.000 31.60677  ? 486 PHE A CG  1 
ATOM   1268 C CD1 . PHE A 1 157 ? 8.98230   -55.11599 19.97717  1.000 38.08938  ? 486 PHE A CD1 1 
ATOM   1269 C CD2 . PHE A 1 157 ? 10.49879  -53.90435 21.37736  1.000 41.62822  ? 486 PHE A CD2 1 
ATOM   1270 C CE1 . PHE A 1 157 ? 7.97905   -54.96546 20.92505  1.000 35.21950  ? 486 PHE A CE1 1 
ATOM   1271 C CE2 . PHE A 1 157 ? 9.50384   -53.75624 22.33927  1.000 36.84206  ? 486 PHE A CE2 1 
ATOM   1272 C CZ  . PHE A 1 157 ? 8.23870   -54.28477 22.10335  1.000 36.40170  ? 486 PHE A CZ  1 
ATOM   1273 N N   . ASN A 1 158 ? 9.87805   -51.82481 18.08908  1.000 18.05866  ? 487 ASN A N   1 
ATOM   1274 C CA  . ASN A 1 158 ? 9.71861   -50.39514 18.34948  1.000 17.39068  ? 487 ASN A CA  1 
ATOM   1275 C C   . ASN A 1 158 ? 10.62247  -49.50577 17.49330  1.000 15.19323  ? 487 ASN A C   1 
ATOM   1276 O O   . ASN A 1 158 ? 10.81336  -48.32486 17.82454  1.000 15.09367  ? 487 ASN A O   1 
ATOM   1277 C CB  . ASN A 1 158 ? 9.88150   -50.03833 19.82545  1.000 19.20023  ? 487 ASN A CB  1 
ATOM   1278 C CG  . ASN A 1 158 ? 8.75268   -50.54734 20.66189  1.000 22.87670  ? 487 ASN A CG  1 
ATOM   1279 O OD1 . ASN A 1 158 ? 7.70334   -50.89014 20.17140  1.000 26.11969  ? 487 ASN A OD1 1 
ATOM   1280 N ND2 . ASN A 1 158 ? 8.95310   -50.55808 21.94002  1.000 26.81699  ? 487 ASN A ND2 1 
ATOM   1281 N N   . CYS A 1 159 ? 11.13406  -50.02302 16.37336  1.000 14.02004  ? 488 CYS A N   1 
ATOM   1282 C CA  . CYS A 1 159 ? 12.08306  -49.31395 15.51115  1.000 13.46799  ? 488 CYS A CA  1 
ATOM   1283 C C   . CYS A 1 159 ? 11.70914  -49.64076 14.07480  1.000 12.42296  ? 488 CYS A C   1 
ATOM   1284 O O   . CYS A 1 159 ? 12.11191  -50.67784 13.53451  1.000 14.43507  ? 488 CYS A O   1 
ATOM   1285 C CB  . CYS A 1 159 ? 13.48731  -49.77006 15.83749  1.000 13.89235  ? 488 CYS A CB  1 
ATOM   1286 S SG  . CYS A 1 159 ? 14.09164  -49.13438 17.42406  1.000 14.44838  ? 488 CYS A SG  1 
ATOM   1287 N N   . TYR A 1 160 ? 10.87131  -48.79992 13.46334  1.000 13.32231  ? 489 TYR A N   1 
ATOM   1288 C CA  . TYR A 1 160 ? 10.19381  -49.17394 12.23201  1.000 13.29572  ? 489 TYR A CA  1 
ATOM   1289 C C   . TYR A 1 160 ? 10.76857  -48.49133 11.00652  1.000 13.04230  ? 489 TYR A C   1 
ATOM   1290 O O   . TYR A 1 160 ? 10.95206  -47.26127 10.98614  1.000 14.03405  ? 489 TYR A O   1 
ATOM   1291 C CB  . TYR A 1 160 ? 8.69344   -48.89074 12.33016  1.000 15.16050  ? 489 TYR A CB  1 
ATOM   1292 C CG  . TYR A 1 160 ? 8.08026   -49.43637 13.60563  1.000 15.61822  ? 489 TYR A CG  1 
ATOM   1293 C CD1 . TYR A 1 160 ? 8.32120   -50.75640 14.02012  1.000 17.97173  ? 489 TYR A CD1 1 
ATOM   1294 C CD2 . TYR A 1 160 ? 7.21028   -48.66862 14.37644  1.000 17.23856  ? 489 TYR A CD2 1 
ATOM   1295 C CE1 . TYR A 1 160 ? 7.74511   -51.26563 15.18662  1.000 18.23907  ? 489 TYR A CE1 1 
ATOM   1296 C CE2 . TYR A 1 160 ? 6.62217   -49.17702 15.54349  1.000 17.55179  ? 489 TYR A CE2 1 
ATOM   1297 C CZ  . TYR A 1 160 ? 6.90717   -50.48134 15.93113  1.000 18.51265  ? 489 TYR A CZ  1 
ATOM   1298 O OH  . TYR A 1 160 ? 6.32554   -50.97192 17.09185  1.000 21.03397  ? 489 TYR A OH  1 
ATOM   1299 N N   . PHE A 1 161 ? 10.94920  -49.26427 9.94105   1.000 12.93252  ? 490 PHE A N   1 
ATOM   1300 C CA  . PHE A 1 161 ? 11.19024  -48.60533 8.65298   1.000 12.85725  ? 490 PHE A CA  1 
ATOM   1301 C C   . PHE A 1 161 ? 9.90243   -47.87880 8.27445   1.000 12.24754  ? 490 PHE A C   1 
ATOM   1302 O O   . PHE A 1 161 ? 8.81717   -48.45234 8.40265   1.000 13.43390  ? 490 PHE A O   1 
ATOM   1303 C CB  . PHE A 1 161 ? 11.55385  -49.61170 7.57131   1.000 13.57890  ? 490 PHE A CB  1 
ATOM   1304 C CG  . PHE A 1 161 ? 12.07783  -48.95068 6.34070   1.000 12.85014  ? 490 PHE A CG  1 
ATOM   1305 C CD1 . PHE A 1 161 ? 13.31895  -48.30511 6.34897   1.000 14.30714  ? 490 PHE A CD1 1 
ATOM   1306 C CD2 . PHE A 1 161 ? 11.27840  -48.86391 5.19737   1.000 13.91004  ? 490 PHE A CD2 1 
ATOM   1307 C CE1 . PHE A 1 161 ? 13.78997  -47.65512 5.22713   1.000 17.34263  ? 490 PHE A CE1 1 
ATOM   1308 C CE2 . PHE A 1 161 ? 11.75791  -48.19601 4.07671   1.000 16.26757  ? 490 PHE A CE2 1 
ATOM   1309 C CZ  . PHE A 1 161 ? 13.00007  -47.58995 4.10256   1.000 17.47269  ? 490 PHE A CZ  1 
ATOM   1310 N N   . PRO A 1 162 ? 9.95076   -46.62635 7.81628   1.000 12.02516  ? 491 PRO A N   1 
ATOM   1311 C CA  . PRO A 1 162 ? 8.72673   -45.83179 7.78888   1.000 12.28466  ? 491 PRO A CA  1 
ATOM   1312 C C   . PRO A 1 162 ? 7.87964   -45.95868 6.54377   1.000 11.79534  ? 491 PRO A C   1 
ATOM   1313 O O   . PRO A 1 162 ? 6.75718   -45.41117 6.54147   1.000 13.15605  ? 491 PRO A O   1 
ATOM   1314 C CB  . PRO A 1 162 ? 9.24687   -44.38756 7.94860   1.000 13.39567  ? 491 PRO A CB  1 
ATOM   1315 C CG  . PRO A 1 162 ? 10.61202  -44.41936 7.30834   1.000 13.47865  ? 491 PRO A CG  1 
ATOM   1316 C CD  . PRO A 1 162 ? 11.16165  -45.77720 7.70143   1.000 13.23544  ? 491 PRO A CD  1 
ATOM   1317 N N   . LEU A 1 163 ? 8.35615   -46.65982 5.52067   1.000 12.36121  ? 492 LEU A N   1 
ATOM   1318 C CA  . LEU A 1 163 ? 7.59438   -46.84221 4.30760   1.000 12.71692  ? 492 LEU A CA  1 
ATOM   1319 C C   . LEU A 1 163 ? 7.16825   -48.29624 4.22334   1.000 12.89708  ? 492 LEU A C   1 
ATOM   1320 O O   . LEU A 1 163 ? 7.91982   -49.20854 4.58793   1.000 16.66896  ? 492 LEU A O   1 
ATOM   1321 C CB  . LEU A 1 163 ? 8.46744   -46.55522 3.07708   1.000 13.26208  ? 492 LEU A CB  1 
ATOM   1322 C CG  . LEU A 1 163 ? 9.15390   -45.17855 3.03917   1.000 12.86592  ? 492 LEU A CG  1 
ATOM   1323 C CD1 . LEU A 1 163 ? 9.92132   -45.00593 1.73527   1.000 14.34154  ? 492 LEU A CD1 1 
ATOM   1324 C CD2 . LEU A 1 163 ? 8.18360   -44.02239 3.19980   1.000 14.07774  ? 492 LEU A CD2 1 
ATOM   1325 N N   . GLN A 1 164 ? 5.98993   -48.51936 3.66608   1.000 12.13419  ? 493 GLN A N   1 
ATOM   1326 C CA  . GLN A 1 164 ? 5.44251   -49.84573 3.48493   1.000 13.33279  ? 493 GLN A CA  1 
ATOM   1327 C C   . GLN A 1 164 ? 4.90322   -49.99448 2.06871   1.000 11.88262  ? 493 GLN A C   1 
ATOM   1328 O O   . GLN A 1 164 ? 4.29833   -49.07650 1.53148   1.000 12.29379  ? 493 GLN A O   1 
ATOM   1329 C CB  . GLN A 1 164 ? 4.32519   -50.13466 4.44437   1.000 15.66792  ? 493 GLN A CB  1 
ATOM   1330 C CG  . GLN A 1 164 ? 3.96994   -51.62635 4.37927   1.000 18.43880  ? 493 GLN A CG  1 
ATOM   1331 C CD  . GLN A 1 164 ? 3.13386   -52.07951 5.54593   1.000 20.53214  ? 493 GLN A CD  1 
ATOM   1332 O OE1 . GLN A 1 164 ? 3.64342   -52.23571 6.64776   1.000 18.13802  ? 493 GLN A OE1 1 
ATOM   1333 N NE2 . GLN A 1 164 ? 1.85772   -52.35055 5.32074   1.000 25.27942  ? 493 GLN A NE2 1 
ATOM   1334 N N   . SER A 1 165 ? 5.09349   -51.16992 1.48758   1.000 12.80089  ? 494 SER A N   1 
ATOM   1335 C CA  . SER A 1 165 ? 4.54178   -51.47112 0.17245   1.000 12.95305  ? 494 SER A CA  1 
ATOM   1336 C C   . SER A 1 165 ? 3.04393   -51.74109 0.27961   1.000 12.42239  ? 494 SER A C   1 
ATOM   1337 O O   . SER A 1 165 ? 2.57857   -52.49400 1.15610   1.000 13.75901  ? 494 SER A O   1 
ATOM   1338 C CB  . SER A 1 165 ? 5.25673   -52.69752 -0.40615  1.000 15.12465  ? 494 SER A CB  1 
ATOM   1339 O OG  . SER A 1 165 ? 4.62114   -53.10354 -1.62451  1.000 14.79237  ? 494 SER A OG  1 
ATOM   1340 N N   . TYR A 1 166 ? 2.29782   -51.19349 -0.67806  1.000 11.33265  ? 495 TYR A N   1 
ATOM   1341 C CA  . TYR A 1 166 ? 0.89911   -51.55386 -0.82781  1.000 12.41969  ? 495 TYR A CA  1 
ATOM   1342 C C   . TYR A 1 166 ? 0.73269   -53.01294 -1.20590  1.000 12.56210  ? 495 TYR A C   1 
ATOM   1343 O O   . TYR A 1 166 ? -0.30840  -53.60445 -0.92291  1.000 15.52191  ? 495 TYR A O   1 
ATOM   1344 C CB  . TYR A 1 166 ? 0.22707   -50.68983 -1.88426  1.000 12.65044  ? 495 TYR A CB  1 
ATOM   1345 C CG  . TYR A 1 166 ? -0.13607  -49.30341 -1.44755  1.000 11.55835  ? 495 TYR A CG  1 
ATOM   1346 C CD1 . TYR A 1 166 ? -1.20221  -49.10738 -0.55754  1.000 12.18438  ? 495 TYR A CD1 1 
ATOM   1347 C CD2 . TYR A 1 166 ? 0.52893   -48.17811 -1.94709  1.000 12.20229  ? 495 TYR A CD2 1 
ATOM   1348 C CE1 . TYR A 1 166 ? -1.59873  -47.82202 -0.20083  1.000 12.49880  ? 495 TYR A CE1 1 
ATOM   1349 C CE2 . TYR A 1 166 ? 0.14395   -46.91351 -1.60705  1.000 12.26437  ? 495 TYR A CE2 1 
ATOM   1350 C CZ  . TYR A 1 166 ? -0.91802  -46.73315 -0.72240  1.000 11.59970  ? 495 TYR A CZ  1 
ATOM   1351 O OH  . TYR A 1 166 ? -1.32131  -45.46196 -0.39846  1.000 12.46227  ? 495 TYR A OH  1 
ATOM   1352 N N   . GLY A 1 167 ? 1.68959   -53.58967 -1.93420  1.000 12.28855  ? 496 GLY A N   1 
ATOM   1353 C CA  . GLY A 1 167 ? 1.58307   -54.99625 -2.28162  1.000 13.84910  ? 496 GLY A CA  1 
ATOM   1354 C C   . GLY A 1 167 ? 0.42512   -55.30818 -3.19625  1.000 13.30905  ? 496 GLY A C   1 
ATOM   1355 O O   . GLY A 1 167 ? -0.10165  -56.41966 -3.17128  1.000 15.49435  ? 496 GLY A O   1 
ATOM   1356 N N   . PHE A 1 168 ? 0.04686   -54.37342 -4.07355  1.000 13.01101  ? 497 PHE A N   1 
ATOM   1357 C CA  . PHE A 1 168 ? -1.15968  -54.54830 -4.87713  1.000 14.17628  ? 497 PHE A CA  1 
ATOM   1358 C C   . PHE A 1 168 ? -1.10476  -55.86280 -5.65058  1.000 13.17281  ? 497 PHE A C   1 
ATOM   1359 O O   . PHE A 1 168 ? -0.17417  -56.10853 -6.43146  1.000 13.58492  ? 497 PHE A O   1 
ATOM   1360 C CB  . PHE A 1 168 ? -1.22280  -53.42681 -5.89414  1.000 14.54174  ? 497 PHE A CB  1 
ATOM   1361 C CG  . PHE A 1 168 ? -1.48106  -52.05925 -5.29412  1.000 12.99082  ? 497 PHE A CG  1 
ATOM   1362 C CD1 . PHE A 1 168 ? -2.63929  -51.77387 -4.55794  1.000 13.59324  ? 497 PHE A CD1 1 
ATOM   1363 C CD2 . PHE A 1 168 ? -0.55211  -51.05344 -5.49407  1.000 13.83835  ? 497 PHE A CD2 1 
ATOM   1364 C CE1 . PHE A 1 168 ? -2.84402  -50.48075 -4.02889  1.000 13.04016  ? 497 PHE A CE1 1 
ATOM   1365 C CE2 . PHE A 1 168 ? -0.76042  -49.76665 -4.98313  1.000 13.46204  ? 497 PHE A CE2 1 
ATOM   1366 C CZ  . PHE A 1 168 ? -1.92956  -49.48994 -4.25031  1.000 12.68958  ? 497 PHE A CZ  1 
ATOM   1367 N N   . GLN A 1 169 ? -2.15306  -56.67002 -5.50951  1.000 14.67727  ? 498 GLN A N   1 
ATOM   1368 C CA  . GLN A 1 169 ? -2.32620  -57.92605 -6.22788  1.000 15.33605  ? 498 GLN A CA  1 
ATOM   1369 C C   . GLN A 1 169 ? -3.62058  -57.81822 -7.02444  1.000 15.93516  ? 498 GLN A C   1 
ATOM   1370 O O   . GLN A 1 169 ? -4.59414  -57.21824 -6.55204  1.000 15.65914  ? 498 GLN A O   1 
ATOM   1371 C CB  . GLN A 1 169 ? -2.45118  -59.11802 -5.25266  1.000 16.76668  ? 498 GLN A CB  1 
ATOM   1372 C CG  . GLN A 1 169 ? -1.22102  -59.39963 -4.47536  1.000 18.62845  ? 498 GLN A CG  1 
ATOM   1373 C CD  . GLN A 1 169 ? -1.27000  -60.73056 -3.70959  1.000 19.88364  ? 498 GLN A CD  1 
ATOM   1374 O OE1 . GLN A 1 169 ? -1.90857  -61.71159 -4.09368  1.000 20.90310  ? 498 GLN A OE1 1 
ATOM   1375 N NE2 . GLN A 1 169 ? -0.62659  -60.73516 -2.57768  1.000 22.66102  ? 498 GLN A NE2 1 
ATOM   1376 N N   . PRO A 1 170 ? -3.68658  -58.41780 -8.21286  1.000 15.97128  ? 499 PRO A N   1 
ATOM   1377 C CA  . PRO A 1 170 ? -4.85946  -58.17421 -9.08359  1.000 18.08940  ? 499 PRO A CA  1 
ATOM   1378 C C   . PRO A 1 170 ? -6.17105  -58.65382 -8.51718  1.000 17.79182  ? 499 PRO A C   1 
ATOM   1379 O O   . PRO A 1 170 ? -7.22768  -58.13218 -8.89922  1.000 19.16506  ? 499 PRO A O   1 
ATOM   1380 C CB  . PRO A 1 170 ? -4.48419  -58.85535 -10.40972 1.000 20.02871  ? 499 PRO A CB  1 
ATOM   1381 C CG  . PRO A 1 170 ? -3.44082  -59.87323 -10.00112 1.000 20.82221  ? 499 PRO A CG  1 
ATOM   1382 C CD  . PRO A 1 170 ? -2.65630  -59.25018 -8.87157  1.000 18.07598  ? 499 PRO A CD  1 
ATOM   1383 N N   . THR A 1 171 ? -6.12812  -59.58518 -7.57301  1.000 18.48306  ? 500 THR A N   1 
ATOM   1384 C CA  . THR A 1 171 ? -7.26980  -60.17177 -6.90202  1.000 20.94935  ? 500 THR A CA  1 
ATOM   1385 C C   . THR A 1 171 ? -7.76517  -59.35142 -5.71342  1.000 19.92579  ? 500 THR A C   1 
ATOM   1386 O O   . THR A 1 171 ? -8.77618  -59.72331 -5.11264  1.000 21.34571  ? 500 THR A O   1 
ATOM   1387 C CB  . THR A 1 171 ? -6.88138  -61.58874 -6.42718  1.000 22.81238  ? 500 THR A CB  1 
ATOM   1388 O OG1 . THR A 1 171 ? -5.59691  -61.53230 -5.76604  1.000 25.82248  ? 500 THR A OG1 1 
ATOM   1389 C CG2 . THR A 1 171 ? -6.77878  -62.53658 -7.62153  1.000 24.87219  ? 500 THR A CG2 1 
ATOM   1390 N N   . ASN A 1 172 ? -7.10484  -58.26106 -5.35442  1.000 17.94174  ? 501 ASN A N   1 
ATOM   1391 C CA  . ASN A 1 172 ? -7.56946  -57.44318 -4.23886  1.000 18.56444  ? 501 ASN A CA  1 
ATOM   1392 C C   . ASN A 1 172 ? -8.98836  -56.93675 -4.49424  1.000 19.37310  ? 501 ASN A C   1 
ATOM   1393 O O   . ASN A 1 172 ? -9.38738  -56.69628 -5.64022  1.000 19.52428  ? 501 ASN A O   1 
ATOM   1394 C CB  . ASN A 1 172 ? -6.68124  -56.20438 -4.07388  1.000 17.49645  ? 501 ASN A CB  1 
ATOM   1395 C CG  . ASN A 1 172 ? -5.33266  -56.52524 -3.44365  1.000 18.97630  ? 501 ASN A CG  1 
ATOM   1396 O OD1 . ASN A 1 172 ? -5.05877  -57.63951 -3.01598  1.000 20.79996  ? 501 ASN A OD1 1 
ATOM   1397 N ND2 . ASN A 1 172 ? -4.49396  -55.53319 -3.38002  1.000 21.35792  ? 501 ASN A ND2 1 
ATOM   1398 N N   . GLY A 1 173 ? -9.74074  -56.71958 -3.40997  1.000 20.08881  ? 502 GLY A N   1 
ATOM   1399 C CA  . GLY A 1 173 ? -10.99329 -55.99787 -3.52939  1.000 21.38732  ? 502 GLY A CA  1 
ATOM   1400 C C   . GLY A 1 173 ? -10.76291 -54.56916 -3.99662  1.000 21.00293  ? 502 GLY A C   1 
ATOM   1401 O O   . GLY A 1 173 ? -9.67071  -54.00567 -3.86477  1.000 20.98728  ? 502 GLY A O   1 
ATOM   1402 N N   . VAL A 1 174 ? -11.81961 -53.95390 -4.54691  1.000 22.84870  ? 503 VAL A N   1 
ATOM   1403 C CA  A VAL A 1 174 ? -11.66613 -52.65995 -5.21768  0.500 25.22750  ? 503 VAL A CA  1 
ATOM   1404 C CA  B VAL A 1 174 ? -11.67844 -52.65240 -5.21276  0.500 25.23099  ? 503 VAL A CA  1 
ATOM   1405 C C   . VAL A 1 174 ? -11.13356 -51.56499 -4.28118  1.000 24.42532  ? 503 VAL A C   1 
ATOM   1406 O O   . VAL A 1 174 ? -10.36497 -50.69016 -4.71355  1.000 24.51134  ? 503 VAL A O   1 
ATOM   1407 C CB  A VAL A 1 174 ? -12.96867 -52.26395 -5.95042  0.500 28.63650  ? 503 VAL A CB  1 
ATOM   1408 C CB  B VAL A 1 174 ? -12.97945 -52.22556 -5.93258  0.500 28.70971  ? 503 VAL A CB  1 
ATOM   1409 C CG1 A VAL A 1 174 ? -14.10135 -52.04774 -4.96066  0.500 29.96799  ? 503 VAL A CG1 1 
ATOM   1410 C CG1 B VAL A 1 174 ? -12.82604 -50.82206 -6.49013  0.500 30.65196  ? 503 VAL A CG1 1 
ATOM   1411 C CG2 A VAL A 1 174 ? -12.74780 -51.05073 -6.83859  0.500 29.70325  ? 503 VAL A CG2 1 
ATOM   1412 C CG2 B VAL A 1 174 ? -13.32461 -53.18869 -7.05722  0.500 29.04590  ? 503 VAL A CG2 1 
ATOM   1413 N N   . GLY A 1 175 ? -11.51818 -51.57445 -2.99795  1.000 24.05005  ? 504 GLY A N   1 
ATOM   1414 C CA  . GLY A 1 175 ? -11.01472 -50.58845 -2.03629  1.000 22.96558  ? 504 GLY A CA  1 
ATOM   1415 C C   . GLY A 1 175 ? -9.52640  -50.71353 -1.77145  1.000 21.03075  ? 504 GLY A C   1 
ATOM   1416 O O   . GLY A 1 175 ? -8.89303  -49.76022 -1.28959  1.000 23.81720  ? 504 GLY A O   1 
ATOM   1417 N N   . TYR A 1 176 ? -8.95588  -51.87074 -2.08844  1.000 20.33524  ? 505 TYR A N   1 
ATOM   1418 C CA  . TYR A 1 176 ? -7.54058  -52.12343 -1.90159  1.000 19.92452  ? 505 TYR A CA  1 
ATOM   1419 C C   . TYR A 1 176 ? -6.79861  -52.14857 -3.22571  1.000 17.56736  ? 505 TYR A C   1 
ATOM   1420 O O   . TYR A 1 176 ? -5.60215  -52.46009 -3.24575  1.000 18.80808  ? 505 TYR A O   1 
ATOM   1421 C CB  . TYR A 1 176 ? -7.37092  -53.46424 -1.18652  1.000 23.62015  ? 505 TYR A CB  1 
ATOM   1422 C CG  . TYR A 1 176 ? -7.74589  -53.37224 0.27457   1.000 35.09478  ? 505 TYR A CG  1 
ATOM   1423 C CD1 . TYR A 1 176 ? -9.08191  -53.38077 0.64521   1.000 39.63574  ? 505 TYR A CD1 1 
ATOM   1424 C CD2 . TYR A 1 176 ? -6.78733  -53.20940 1.26603   1.000 40.59548  ? 505 TYR A CD2 1 
ATOM   1425 C CE1 . TYR A 1 176 ? -9.46148  -53.27490 1.98021   1.000 43.21644  ? 505 TYR A CE1 1 
ATOM   1426 C CE2 . TYR A 1 176 ? -7.15484  -53.10319 2.60976   1.000 43.70289  ? 505 TYR A CE2 1 
ATOM   1427 C CZ  . TYR A 1 176 ? -8.49386  -53.12946 2.95155   1.000 45.55060  ? 505 TYR A CZ  1 
ATOM   1428 O OH  . TYR A 1 176 ? -8.87244  -53.02616 4.27511   1.000 48.57985  ? 505 TYR A OH  1 
ATOM   1429 N N   . GLN A 1 177 ? -7.48231  -51.85219 -4.34648  1.000 16.25028  ? 506 GLN A N   1 
ATOM   1430 C CA  . GLN A 1 177 ? -6.83187  -51.78158 -5.64107  1.000 14.98584  ? 506 GLN A CA  1 
ATOM   1431 C C   . GLN A 1 177 ? -6.15445  -50.42597 -5.83276  1.000 12.71862  ? 506 GLN A C   1 
ATOM   1432 O O   . GLN A 1 177 ? -6.53975  -49.42460 -5.18680  1.000 13.54630  ? 506 GLN A O   1 
ATOM   1433 C CB  . GLN A 1 177 ? -7.83771  -52.01480 -6.76728  1.000 15.42246  ? 506 GLN A CB  1 
ATOM   1434 C CG  . GLN A 1 177 ? -8.21699  -53.47644 -6.85331  1.000 16.64859  ? 506 GLN A CG  1 
ATOM   1435 C CD  . GLN A 1 177 ? -9.26337  -53.75577 -7.90309  1.000 18.08565  ? 506 GLN A CD  1 
ATOM   1436 O OE1 . GLN A 1 177 ? -9.52086  -52.91459 -8.77402  1.000 19.23622  ? 506 GLN A OE1 1 
ATOM   1437 N NE2 . GLN A 1 177 ? -9.91332  -54.91066 -7.79030  1.000 21.18644  ? 506 GLN A NE2 1 
ATOM   1438 N N   . PRO A 1 178 ? -5.13532  -50.36039 -6.70048  1.000 12.45372  ? 507 PRO A N   1 
ATOM   1439 C CA  . PRO A 1 178 ? -4.44715  -49.09160 -6.94318  1.000 12.48626  ? 507 PRO A CA  1 
ATOM   1440 C C   . PRO A 1 178 ? -5.31106  -48.16167 -7.77086  1.000 12.18581  ? 507 PRO A C   1 
ATOM   1441 O O   . PRO A 1 178 ? -6.02199  -48.59492 -8.68865  1.000 12.81450  ? 507 PRO A O   1 
ATOM   1442 C CB  . PRO A 1 178 ? -3.20427  -49.51581 -7.72719  1.000 13.06431  ? 507 PRO A CB  1 
ATOM   1443 C CG  . PRO A 1 178 ? -3.63810  -50.76370 -8.43240  1.000 13.33321  ? 507 PRO A CG  1 
ATOM   1444 C CD  . PRO A 1 178 ? -4.55567  -51.45595 -7.51438  1.000 12.55639  ? 507 PRO A CD  1 
ATOM   1445 N N   . TYR A 1 179 ? -5.19989  -46.87728 -7.42675  1.000 12.39898  ? 508 TYR A N   1 
ATOM   1446 C CA  . TYR A 1 179 ? -5.79256  -45.79004 -8.18325  1.000 12.69822  ? 508 TYR A CA  1 
ATOM   1447 C C   . TYR A 1 179 ? -4.68367  -44.79939 -8.48570  1.000 11.77676  ? 508 TYR A C   1 
ATOM   1448 O O   . TYR A 1 179 ? -3.92023  -44.41419 -7.58679  1.000 12.18328  ? 508 TYR A O   1 
ATOM   1449 C CB  . TYR A 1 179 ? -6.91732  -45.07141 -7.37394  1.000 13.28918  ? 508 TYR A CB  1 
ATOM   1450 C CG  . TYR A 1 179 ? -8.21297  -45.83641 -7.47074  1.000 13.70614  ? 508 TYR A CG  1 
ATOM   1451 C CD1 . TYR A 1 179 ? -8.30917  -47.09777 -6.90412  1.000 14.35604  ? 508 TYR A CD1 1 
ATOM   1452 C CD2 . TYR A 1 179 ? -9.30609  -45.33645 -8.17667  1.000 14.98224  ? 508 TYR A CD2 1 
ATOM   1453 C CE1 . TYR A 1 179 ? -9.45474  -47.84879 -7.04023  1.000 16.25333  ? 508 TYR A CE1 1 
ATOM   1454 C CE2 . TYR A 1 179 ? -10.48232 -46.08782 -8.33048  1.000 15.56589  ? 508 TYR A CE2 1 
ATOM   1455 C CZ  . TYR A 1 179 ? -10.52571 -47.34899 -7.76256  1.000 16.53407  ? 508 TYR A CZ  1 
ATOM   1456 O OH  . TYR A 1 179 ? -11.65407 -48.13633 -7.92706  1.000 18.69910  ? 508 TYR A OH  1 
ATOM   1457 N N   . ARG A 1 180 ? -4.63145  -44.38295 -9.73941  1.000 12.05766  ? 509 ARG A N   1 
ATOM   1458 C CA  . ARG A 1 180 ? -3.79564  -43.27156 -10.13679 1.000 12.03956  ? 509 ARG A CA  1 
ATOM   1459 C C   . ARG A 1 180 ? -4.54003  -41.97341 -9.87281  1.000 12.71910  ? 509 ARG A C   1 
ATOM   1460 O O   . ARG A 1 180 ? -5.75609  -41.89245 -10.09478 1.000 13.07039  ? 509 ARG A O   1 
ATOM   1461 C CB  . ARG A 1 180 ? -3.41907  -43.39597 -11.61251 1.000 13.00111  ? 509 ARG A CB  1 
ATOM   1462 C CG  . ARG A 1 180 ? -2.24423  -44.34949 -11.76204 1.000 14.40429  ? 509 ARG A CG  1 
ATOM   1463 C CD  . ARG A 1 180 ? -1.99120  -44.74953 -13.20238 1.000 14.95257  ? 509 ARG A CD  1 
ATOM   1464 N NE  . ARG A 1 180 ? -0.95829  -45.79060 -13.23484 1.000 15.17275  ? 509 ARG A NE  1 
ATOM   1465 C CZ  . ARG A 1 180 ? 0.01158   -45.87636 -14.14273 1.000 15.56605  ? 509 ARG A CZ  1 
ATOM   1466 N NH1 . ARG A 1 180 ? 0.01543   -45.12823 -15.22607 1.000 17.97392  ? 509 ARG A NH1 1 
ATOM   1467 N NH2 . ARG A 1 180 ? 0.94300   -46.81192 -14.00542 1.000 17.11722  ? 509 ARG A NH2 1 
ATOM   1468 N N   . VAL A 1 181 ? -3.81866  -40.97508 -9.34629  1.000 11.35587  ? 510 VAL A N   1 
ATOM   1469 C CA  . VAL A 1 181 ? -4.39011  -39.70374 -8.95296  1.000 11.77606  ? 510 VAL A CA  1 
ATOM   1470 C C   . VAL A 1 181 ? -3.59658  -38.58789 -9.59072  1.000 11.63478  ? 510 VAL A C   1 
ATOM   1471 O O   . VAL A 1 181 ? -2.35884  -38.60068 -9.55110  1.000 12.39619  ? 510 VAL A O   1 
ATOM   1472 C CB  . VAL A 1 181 ? -4.40683  -39.54433 -7.41295  1.000 12.24026  ? 510 VAL A CB  1 
ATOM   1473 C CG1 . VAL A 1 181 ? -5.02182  -38.19844 -7.02519  1.000 13.28812  ? 510 VAL A CG1 1 
ATOM   1474 C CG2 . VAL A 1 181 ? -5.11790  -40.72822 -6.75255  1.000 12.76829  ? 510 VAL A CG2 1 
ATOM   1475 N N   . VAL A 1 182 ? -4.30633  -37.60516 -10.12759 1.000 12.43456  ? 511 VAL A N   1 
ATOM   1476 C CA  . VAL A 1 182 ? -3.68909  -36.36146 -10.57443 1.000 12.82724  ? 511 VAL A CA  1 
ATOM   1477 C C   . VAL A 1 182 ? -4.40777  -35.23635 -9.84556  1.000 11.90034  ? 511 VAL A C   1 
ATOM   1478 O O   . VAL A 1 182 ? -5.63972  -35.13819 -9.89955  1.000 13.46510  ? 511 VAL A O   1 
ATOM   1479 C CB  . VAL A 1 182 ? -3.76159  -36.17247 -12.10617 1.000 13.51130  ? 511 VAL A CB  1 
ATOM   1480 C CG1 . VAL A 1 182 ? -3.22243  -34.75911 -12.49735 1.000 15.19908  ? 511 VAL A CG1 1 
ATOM   1481 C CG2 . VAL A 1 182 ? -2.98591  -37.31138 -12.79702 1.000 13.82433  ? 511 VAL A CG2 1 
ATOM   1482 N N   . VAL A 1 183 ? -3.63672  -34.36634 -9.19427  1.000 12.36966  ? 512 VAL A N   1 
ATOM   1483 C CA  . VAL A 1 183 ? -4.16408  -33.19954 -8.48381  1.000 12.25731  ? 512 VAL A CA  1 
ATOM   1484 C C   . VAL A 1 183 ? -3.71626  -31.96489 -9.25875  1.000 12.98228  ? 512 VAL A C   1 
ATOM   1485 O O   . VAL A 1 183 ? -2.51356  -31.72571 -9.40715  1.000 13.93141  ? 512 VAL A O   1 
ATOM   1486 C CB  . VAL A 1 183 ? -3.64263  -33.12394 -7.03827  1.000 13.00238  ? 512 VAL A CB  1 
ATOM   1487 C CG1 . VAL A 1 183 ? -4.18407  -31.90308 -6.35880  1.000 14.06350  ? 512 VAL A CG1 1 
ATOM   1488 C CG2 . VAL A 1 183 ? -3.97317  -34.40813 -6.26768  1.000 14.57488  ? 512 VAL A CG2 1 
ATOM   1489 N N   . LEU A 1 184 ? -4.68282  -31.20116 -9.78038  1.000 13.35514  ? 513 LEU A N   1 
ATOM   1490 C CA  . LEU A 1 184 ? -4.39792  -29.95735 -10.48125 1.000 14.34492  ? 513 LEU A CA  1 
ATOM   1491 C C   . LEU A 1 184 ? -4.60272  -28.80294 -9.51301  1.000 14.85720  ? 513 LEU A C   1 
ATOM   1492 O O   . LEU A 1 184 ? -5.70153  -28.62921 -8.98933  1.000 16.32815  ? 513 LEU A O   1 
ATOM   1493 C CB  . LEU A 1 184 ? -5.31014  -29.81976 -11.70266 1.000 15.96207  ? 513 LEU A CB  1 
ATOM   1494 C CG  . LEU A 1 184 ? -5.25490  -30.92394 -12.73758 1.000 16.47747  ? 513 LEU A CG  1 
ATOM   1495 C CD1 . LEU A 1 184 ? -6.23867  -30.60404 -13.87797 1.000 18.20266  ? 513 LEU A CD1 1 
ATOM   1496 C CD2 . LEU A 1 184 ? -3.84598  -31.13729 -13.29402 1.000 18.22722  ? 513 LEU A CD2 1 
ATOM   1497 N N   . SER A 1 185 ? -3.54065  -28.02546 -9.26832  1.000 15.46902  ? 514 SER A N   1 
ATOM   1498 C CA  . SER A 1 185 ? -3.63382  -26.79582 -8.49942  1.000 17.63268  ? 514 SER A CA  1 
ATOM   1499 C C   . SER A 1 185 ? -3.63928  -25.61107 -9.44142  1.000 18.01727  ? 514 SER A C   1 
ATOM   1500 O O   . SER A 1 185 ? -2.73559  -25.48038 -10.27476 1.000 18.31296  ? 514 SER A O   1 
ATOM   1501 C CB  . SER A 1 185 ? -2.42932  -26.63232 -7.57478  1.000 19.05400  ? 514 SER A CB  1 
ATOM   1502 O OG  . SER A 1 185 ? -2.44179  -27.59444 -6.56407  1.000 19.71017  ? 514 SER A OG  1 
ATOM   1503 N N   . PHE A 1 186 ? -4.59228  -24.71270 -9.23364  1.000 18.50958  ? 515 PHE A N   1 
ATOM   1504 C CA  . PHE A 1 186 ? -4.72585  -23.50021 -10.03466 1.000 19.94914  ? 515 PHE A CA  1 
ATOM   1505 C C   . PHE A 1 186 ? -4.22258  -22.31250 -9.23948  1.000 23.44674  ? 515 PHE A C   1 
ATOM   1506 O O   . PHE A 1 186 ? -4.87315  -21.87882 -8.29064  1.000 26.27641  ? 515 PHE A O   1 
ATOM   1507 C CB  . PHE A 1 186 ? -6.17113  -23.29232 -10.45271 1.000 20.87142  ? 515 PHE A CB  1 
ATOM   1508 C CG  . PHE A 1 186 ? -6.75470  -24.44880 -11.18826 1.000 21.10151  ? 515 PHE A CG  1 
ATOM   1509 C CD1 . PHE A 1 186 ? -6.12972  -24.94781 -12.31765 1.000 26.14520  ? 515 PHE A CD1 1 
ATOM   1510 C CD2 . PHE A 1 186 ? -7.87969  -25.09314 -10.72016 1.000 22.83877  ? 515 PHE A CD2 1 
ATOM   1511 C CE1 . PHE A 1 186 ? -6.67687  -26.03185 -13.02789 1.000 26.42920  ? 515 PHE A CE1 1 
ATOM   1512 C CE2 . PHE A 1 186 ? -8.42875  -26.16013 -11.42201 1.000 23.11466  ? 515 PHE A CE2 1 
ATOM   1513 C CZ  . PHE A 1 186 ? -7.81600  -26.64341 -12.56210 1.000 22.16572  ? 515 PHE A CZ  1 
ATOM   1514 N N   . GLU A 1 187 ? -3.07474  -21.78905 -9.63930  1.000 26.31239  ? 516 GLU A N   1 
ATOM   1515 C CA  . GLU A 1 187 ? -2.38414  -20.75788 -8.88203  1.000 31.57635  ? 516 GLU A CA  1 
ATOM   1516 C C   . GLU A 1 187 ? -2.60555  -19.39120 -9.52093  1.000 35.58624  ? 516 GLU A C   1 
ATOM   1517 O O   . GLU A 1 187 ? -2.34147  -19.20591 -10.71222 1.000 33.25398  ? 516 GLU A O   1 
ATOM   1518 C CB  . GLU A 1 187 ? -0.89018  -21.06238 -8.83325  1.000 32.25835  ? 516 GLU A CB  1 
ATOM   1519 C CG  . GLU A 1 187 ? -0.08508  -20.05286 -8.03726  1.000 35.51875  ? 516 GLU A CG  1 
ATOM   1520 C CD  . GLU A 1 187 ? 1.36537   -20.46340 -7.93693  1.000 37.54304  ? 516 GLU A CD  1 
ATOM   1521 O OE1 . GLU A 1 187 ? 2.05028   -20.39488 -8.98002  1.000 37.04388  ? 516 GLU A OE1 1 
ATOM   1522 O OE2 . GLU A 1 187 ? 1.81352   -20.83949 -6.82861  1.000 40.11518  ? 516 GLU A OE2 1 
ATOM   1523 N N   . LEU A 1 188 ? -3.07404  -18.43649 -8.72308  1.000 41.34757  ? 517 LEU A N   1 
ATOM   1524 C CA  . LEU A 1 188 ? -3.26389  -17.06415 -9.18397  1.000 48.84734  ? 517 LEU A CA  1 
ATOM   1525 C C   . LEU A 1 188 ? -2.37282  -16.15440 -8.34544  1.000 52.39104  ? 517 LEU A C   1 
ATOM   1526 O O   . LEU A 1 188 ? -2.61547  -15.96421 -7.14865  1.000 51.66672  ? 517 LEU A O   1 
ATOM   1527 C CB  . LEU A 1 188 ? -4.73533  -16.65757 -9.11223  1.000 51.56198  ? 517 LEU A CB  1 
ATOM   1528 C CG  . LEU A 1 188 ? -5.13865  -15.38184 -9.85701  1.000 54.24482  ? 517 LEU A CG  1 
ATOM   1529 C CD1 . LEU A 1 188 ? -4.58588  -15.38825 -11.27139 1.000 55.74092  ? 517 LEU A CD1 1 
ATOM   1530 C CD2 . LEU A 1 188 ? -6.65179  -15.26195 -9.88510  1.000 54.24334  ? 517 LEU A CD2 1 
ATOM   1531 N N   . LEU A 1 189 ? -1.32615  -15.62792 -8.96890  1.000 56.13260  ? 518 LEU A N   1 
ATOM   1532 C CA  . LEU A 1 189 ? -0.40400  -14.69325 -8.34789  1.000 59.18998  ? 518 LEU A CA  1 
ATOM   1533 C C   . LEU A 1 189 ? -0.58318  -13.31634 -8.97093  1.000 62.19748  ? 518 LEU A C   1 
ATOM   1534 O O   . LEU A 1 189 ? -1.27533  -13.14638 -9.97964  1.000 60.37412  ? 518 LEU A O   1 
ATOM   1535 C CB  . LEU A 1 189 ? 1.04159   -15.16099 -8.54444  1.000 58.39379  ? 518 LEU A CB  1 
ATOM   1536 C CG  . LEU A 1 189 ? 1.29066   -16.64196 -8.27323  1.000 57.44637  ? 518 LEU A CG  1 
ATOM   1537 C CD1 . LEU A 1 189 ? 2.71724   -17.01201 -8.62870  1.000 57.48317  ? 518 LEU A CD1 1 
ATOM   1538 C CD2 . LEU A 1 189 ? 0.99650   -16.95055 -6.81626  1.000 56.72647  ? 518 LEU A CD2 1 
ATOM   1539 N N   . HIS A 1 190 ? 0.05611   -12.32174 -8.35242  1.000 66.06194  ? 519 HIS A N   1 
ATOM   1540 C CA  . HIS A 1 190 ? 0.10911   -10.97845 -8.92879  1.000 68.24075  ? 519 HIS A CA  1 
ATOM   1541 C C   . HIS A 1 190 ? 1.19081   -10.95534 -10.00772 1.000 64.79515  ? 519 HIS A C   1 
ATOM   1542 O O   . HIS A 1 190 ? 2.25172   -10.33940 -9.88509  1.000 65.71529  ? 519 HIS A O   1 
ATOM   1543 C CB  . HIS A 1 190 ? 0.26526   -9.91541  -7.85086  1.000 73.03477  ? 519 HIS A CB  1 
ATOM   1544 C CG  . HIS A 1 190 ? -0.86970  -9.89944  -6.87321  1.000 78.17132  ? 519 HIS A CG  1 
ATOM   1545 N ND1 . HIS A 1 190 ? -2.14309  -9.50278  -7.22353  1.000 79.91460  ? 519 HIS A ND1 1 
ATOM   1546 C CD2 . HIS A 1 190 ? -0.93281  -10.25344 -5.56768  1.000 81.02824  ? 519 HIS A CD2 1 
ATOM   1547 C CE1 . HIS A 1 190 ? -2.93928  -9.60494  -6.17435  1.000 81.64180  ? 519 HIS A CE1 1 
ATOM   1548 N NE2 . HIS A 1 190 ? -2.22947  -10.05698 -5.15617  1.000 82.26131  ? 519 HIS A NE2 1 
ATOM   1549 N N   . ALA A 1 191 ? 0.88907   -11.67569 -11.08212 1.000 60.28159  ? 520 ALA A N   1 
ATOM   1550 C CA  . ALA A 1 191 ? 1.78357   -11.87951 -12.20959 1.000 57.54831  ? 520 ALA A CA  1 
ATOM   1551 C C   . ALA A 1 191 ? 0.92894   -12.21112 -13.42246 1.000 56.39726  ? 520 ALA A C   1 
ATOM   1552 O O   . ALA A 1 191 ? -0.24485  -12.57548 -13.27534 1.000 56.72023  ? 520 ALA A O   1 
ATOM   1553 C CB  . ALA A 1 191 ? 2.77541   -13.02117 -11.92717 1.000 56.94585  ? 520 ALA A CB  1 
ATOM   1554 N N   . PRO A 1 192 ? 1.47783   -12.09657 -14.62862 1.000 55.14906  ? 521 PRO A N   1 
ATOM   1555 C CA  . PRO A 1 192 ? 0.66280   -12.36076 -15.82374 1.000 53.85960  ? 521 PRO A CA  1 
ATOM   1556 C C   . PRO A 1 192 ? 0.16669   -13.80075 -15.85214 1.000 52.98334  ? 521 PRO A C   1 
ATOM   1557 O O   . PRO A 1 192 ? 0.91631   -14.74425 -15.58535 1.000 53.06900  ? 521 PRO A O   1 
ATOM   1558 C CB  . PRO A 1 192 ? 1.60394   -12.05165 -16.99625 1.000 54.59877  ? 521 PRO A CB  1 
ATOM   1559 C CG  . PRO A 1 192 ? 2.92333   -11.67868 -16.41550 1.000 54.75853  ? 521 PRO A CG  1 
ATOM   1560 C CD  . PRO A 1 192 ? 2.89359   -11.82294 -14.93067 1.000 54.97331  ? 521 PRO A CD  1 
ATOM   1561 N N   . ALA A 1 193 ? -1.11802  -13.96256 -16.15501 1.000 50.97150  ? 522 ALA A N   1 
ATOM   1562 C CA  . ALA A 1 193 ? -1.66601  -15.29882 -16.33009 1.000 50.61592  ? 522 ALA A CA  1 
ATOM   1563 C C   . ALA A 1 193 ? -1.08032  -15.91933 -17.58951 1.000 51.57537  ? 522 ALA A C   1 
ATOM   1564 O O   . ALA A 1 193 ? -0.84510  -15.23411 -18.59099 1.000 52.35878  ? 522 ALA A O   1 
ATOM   1565 C CB  . ALA A 1 193 ? -3.18800  -15.24441 -16.42614 1.000 49.44277  ? 522 ALA A CB  1 
ATOM   1566 N N   . THR A 1 194 ? -0.81785  -17.22061 -17.52832 1.000 50.16969  ? 523 THR A N   1 
ATOM   1567 C CA  . THR A 1 194 ? -0.18790  -17.93348 -18.63285 1.000 47.83594  ? 523 THR A CA  1 
ATOM   1568 C C   . THR A 1 194 ? -0.90071  -19.21528 -19.05356 1.000 44.11086  ? 523 THR A C   1 
ATOM   1569 O O   . THR A 1 194 ? -0.62227  -19.71326 -20.15319 1.000 43.76430  ? 523 THR A O   1 
ATOM   1570 C CB  . THR A 1 194 ? 1.29212   -18.22858 -18.31710 1.000 48.67801  ? 523 THR A CB  1 
ATOM   1571 O OG1 . THR A 1 194 ? 1.40442   -19.37011 -17.44983 1.000 47.85292  ? 523 THR A OG1 1 
ATOM   1572 C CG2 . THR A 1 194 ? 1.93031   -17.01788 -17.63440 1.000 49.41266  ? 523 THR A CG2 1 
ATOM   1573 N N   . VAL A 1 195 ? -1.81312  -19.75519 -18.24383 1.000 37.51174  ? 524 VAL A N   1 
ATOM   1574 C CA  . VAL A 1 195 ? -2.52274  -20.99195 -18.56003 1.000 34.32769  ? 524 VAL A CA  1 
ATOM   1575 C C   . VAL A 1 195 ? -4.00473  -20.67058 -18.60372 1.000 34.24531  ? 524 VAL A C   1 
ATOM   1576 O O   . VAL A 1 195 ? -4.61305  -20.37203 -17.56783 1.000 33.00509  ? 524 VAL A O   1 
ATOM   1577 C CB  . VAL A 1 195 ? -2.23845  -22.09865 -17.54217 1.000 31.09398  ? 524 VAL A CB  1 
ATOM   1578 C CG1 . VAL A 1 195 ? -2.91433  -23.41061 -17.97720 1.000 32.04191  ? 524 VAL A CG1 1 
ATOM   1579 C CG2 . VAL A 1 195 ? -0.74209  -22.27857 -17.38114 1.000 32.18962  ? 524 VAL A CG2 1 
ATOM   1580 N N   . CYS A 1 196 ? -4.59294  -20.75916 -19.78977 1.000 34.49511  ? 525 CYS A N   1 
ATOM   1581 C CA  . CYS A 1 196 ? -5.95793  -20.31999 -19.99639 1.000 37.45181  ? 525 CYS A CA  1 
ATOM   1582 C C   . CYS A 1 196 ? -6.75670  -21.45849 -20.60824 1.000 40.32375  ? 525 CYS A C   1 
ATOM   1583 O O   . CYS A 1 196 ? -6.21336  -22.32072 -21.30180 1.000 37.49912  ? 525 CYS A O   1 
ATOM   1584 C CB  . CYS A 1 196 ? -5.97665  -19.12189 -20.95757 1.000 38.00041  ? 525 CYS A CB  1 
ATOM   1585 S SG  . CYS A 1 196 ? -5.27390  -17.58083 -20.26886 1.000 39.13746  ? 525 CYS A SG  1 
ATOM   1586 N N   . GLY A 1 197 ? -8.05733  -21.46603 -20.33153 1.000 43.59195  ? 526 GLY A N   1 
ATOM   1587 C CA  . GLY A 1 197 ? -8.97055  -22.25281 -21.12024 1.000 46.52222  ? 526 GLY A CA  1 
ATOM   1588 C C   . GLY A 1 197 ? -9.03951  -21.68468 -22.52636 1.000 48.90200  ? 526 GLY A C   1 
ATOM   1589 O O   . GLY A 1 197 ? -8.49416  -20.61269 -22.81550 1.000 49.95785  ? 526 GLY A O   1 
ATOM   1590 N N   . PRO A 1 198 ? -9.69758  -22.40652 -23.43991 1.000 48.25367  ? 527 PRO A N   1 
ATOM   1591 C CA  . PRO A 1 198 ? -9.80910  -21.97679 -24.83721 1.000 49.18177  ? 527 PRO A CA  1 
ATOM   1592 C C   . PRO A 1 198 ? -10.84057 -20.86829 -25.04290 1.000 50.33304  ? 527 PRO A C   1 
ATOM   1593 O O   . PRO A 1 198 ? -10.64332 -20.07324 -25.96139 1.000 51.63860  ? 527 PRO A O   1 
ATOM   1594 C CB  . PRO A 1 198 ? -10.23581 -23.25459 -25.56168 1.000 48.09980  ? 527 PRO A CB  1 
ATOM   1595 C CG  . PRO A 1 198 ? -10.90123 -24.09120 -24.51660 1.000 48.13114  ? 527 PRO A CG  1 
ATOM   1596 C CD  . PRO A 1 198 ? -10.31839 -23.72017 -23.19660 1.000 47.89353  ? 527 PRO A CD  1 
ATOM   1597 N N   . GLN B 2 1   ? 14.88658  -39.77897 -17.93610 1.000 43.19837  ? 1   GLN B N   1 
ATOM   1598 C CA  . GLN B 2 1   ? 16.00434  -40.51344 -18.51268 1.000 34.57484  ? 1   GLN B CA  1 
ATOM   1599 C C   . GLN B 2 1   ? 17.00718  -40.98538 -17.46060 1.000 32.93291  ? 1   GLN B C   1 
ATOM   1600 O O   . GLN B 2 1   ? 18.20284  -41.04084 -17.74450 1.000 32.01818  ? 1   GLN B O   1 
ATOM   1601 C CB  . GLN B 2 1   ? 16.73151  -39.65995 -19.55595 1.000 31.63138  ? 1   GLN B CB  1 
ATOM   1602 C CG  . GLN B 2 1   ? 17.20806  -40.43758 -20.77434 1.000 40.93060  ? 1   GLN B CG  1 
ATOM   1603 C CD  . GLN B 2 1   ? 16.07093  -40.74586 -21.72606 1.000 42.54685  ? 1   GLN B CD  1 
ATOM   1604 O OE1 . GLN B 2 1   ? 15.14607  -39.94012 -21.87496 1.000 54.92531  ? 1   GLN B OE1 1 
ATOM   1605 N NE2 . GLN B 2 1   ? 16.13059  -41.90949 -22.38663 1.000 46.77241  ? 1   GLN B NE2 1 
ATOM   1606 N N   . VAL B 2 2   ? 16.53327  -41.31024 -16.24815 1.000 28.06080  ? 2   VAL B N   1 
ATOM   1607 C CA  . VAL B 2 2   ? 17.36557  -41.93831 -15.22671 1.000 24.12981  ? 2   VAL B CA  1 
ATOM   1608 C C   . VAL B 2 2   ? 16.97866  -43.41207 -15.14642 1.000 19.88581  ? 2   VAL B C   1 
ATOM   1609 O O   . VAL B 2 2   ? 15.79011  -43.75438 -15.21210 1.000 22.94082  ? 2   VAL B O   1 
ATOM   1610 C CB  . VAL B 2 2   ? 17.14620  -41.23778 -13.86622 1.000 24.37096  ? 2   VAL B CB  1 
ATOM   1611 C CG1 . VAL B 2 2   ? 17.79437  -42.00718 -12.74666 1.000 22.92169  ? 2   VAL B CG1 1 
ATOM   1612 C CG2 . VAL B 2 2   ? 17.62945  -39.78928 -13.93587 1.000 27.15762  ? 2   VAL B CG2 1 
ATOM   1613 N N   . GLN B 2 3   ? 17.97566  -44.29189 -15.00580 1.000 18.93148  ? 3   GLN B N   1 
ATOM   1614 C CA  . GLN B 2 3   ? 17.73074  -45.71154 -14.79549 1.000 18.96764  ? 3   GLN B CA  1 
ATOM   1615 C C   . GLN B 2 3   ? 18.60494  -46.28099 -13.70721 1.000 16.48894  ? 3   GLN B C   1 
ATOM   1616 O O   . GLN B 2 3   ? 19.73813  -45.84012 -13.54486 1.000 18.86085  ? 3   GLN B O   1 
ATOM   1617 C CB  . GLN B 2 3   ? 18.04759  -46.45793 -16.07811 1.000 24.72393  ? 3   GLN B CB  1 
ATOM   1618 C CG  . GLN B 2 3   ? 17.29235  -47.73224 -16.08245 1.000 31.63802  ? 3   GLN B CG  1 
ATOM   1619 C CD  . GLN B 2 3   ? 17.70318  -48.62145 -17.19679 1.000 35.86488  ? 3   GLN B CD  1 
ATOM   1620 O OE1 . GLN B 2 3   ? 17.33969  -49.79187 -17.19890 1.000 38.13613  ? 3   GLN B OE1 1 
ATOM   1621 N NE2 . GLN B 2 3   ? 18.45770  -48.08895 -18.16082 1.000 35.76851  ? 3   GLN B NE2 1 
ATOM   1622 N N   . LEU B 2 4   ? 18.06066  -47.22486 -12.95527 1.000 15.12751  ? 4   LEU B N   1 
ATOM   1623 C CA  . LEU B 2 4   ? 18.80540  -48.00338 -11.98499 1.000 13.77187  ? 4   LEU B CA  1 
ATOM   1624 C C   . LEU B 2 4   ? 18.93328  -49.42845 -12.48915 1.000 13.22444  ? 4   LEU B C   1 
ATOM   1625 O O   . LEU B 2 4   ? 17.92819  -50.07757 -12.82977 1.000 14.95422  ? 4   LEU B O   1 
ATOM   1626 C CB  . LEU B 2 4   ? 18.11593  -48.09356 -10.62339 1.000 15.67878  ? 4   LEU B CB  1 
ATOM   1627 C CG  . LEU B 2 4   ? 17.90223  -46.81810 -9.85852  1.000 15.76735  ? 4   LEU B CG  1 
ATOM   1628 C CD1 . LEU B 2 4   ? 17.20159  -47.11267 -8.56071  1.000 16.01482  ? 4   LEU B CD1 1 
ATOM   1629 C CD2 . LEU B 2 4   ? 19.21623  -46.13775 -9.57583  1.000 18.16957  ? 4   LEU B CD2 1 
ATOM   1630 N N   . VAL B 2 5   ? 20.17172  -49.93156 -12.51326 1.000 13.45763  ? 5   VAL B N   1 
ATOM   1631 C CA  . VAL B 2 5   ? 20.45641  -51.27788 -12.99080 1.000 13.66258  ? 5   VAL B CA  1 
ATOM   1632 C C   . VAL B 2 5   ? 21.14671  -52.03304 -11.87232 1.000 13.57965  ? 5   VAL B C   1 
ATOM   1633 O O   . VAL B 2 5   ? 22.20080  -51.60427 -11.36831 1.000 14.63993  ? 5   VAL B O   1 
ATOM   1634 C CB  . VAL B 2 5   ? 21.33061  -51.26373 -14.25865 1.000 15.38408  ? 5   VAL B CB  1 
ATOM   1635 C CG1 . VAL B 2 5   ? 21.77237  -52.70389 -14.61495 1.000 17.59247  ? 5   VAL B CG1 1 
ATOM   1636 C CG2 . VAL B 2 5   ? 20.57274  -50.63444 -15.38891 1.000 17.15560  ? 5   VAL B CG2 1 
ATOM   1637 N N   . GLU B 2 6   ? 20.55106  -53.14852 -11.48260 1.000 11.70429  ? 6   GLU B N   1 
ATOM   1638 C CA  . GLU B 2 6   ? 21.15063  -54.06324 -10.52187 1.000 12.54584  ? 6   GLU B CA  1 
ATOM   1639 C C   . GLU B 2 6   ? 22.02800  -55.10659 -11.15664 1.000 12.05440  ? 6   GLU B C   1 
ATOM   1640 O O   . GLU B 2 6   ? 21.81525  -55.50337 -12.29715 1.000 12.98211  ? 6   GLU B O   1 
ATOM   1641 C CB  . GLU B 2 6   ? 20.12832  -54.73031 -9.60634  1.000 13.16127  ? 6   GLU B CB  1 
ATOM   1642 C CG  . GLU B 2 6   ? 19.11973  -53.76151 -9.09134  1.000 15.23073  ? 6   GLU B CG  1 
ATOM   1643 C CD  . GLU B 2 6   ? 18.11774  -54.40464 -8.18462  1.000 13.45015  ? 6   GLU B CD  1 
ATOM   1644 O OE1 . GLU B 2 6   ? 18.39288  -55.48011 -7.56665  1.000 13.49377  ? 6   GLU B OE1 1 
ATOM   1645 O OE2 . GLU B 2 6   ? 16.94395  -53.98561 -8.29444  1.000 13.33586  ? 6   GLU B OE2 1 
ATOM   1646 N N   . SER B 2 7   ? 22.97620  -55.60918 -10.35864 1.000 12.78518  ? 7   SER B N   1 
ATOM   1647 C CA  A SER B 2 7   ? 23.73824  -56.78418 -10.73617 0.500 13.47894  ? 7   SER B CA  1 
ATOM   1648 C CA  B SER B 2 7   ? 23.76230  -56.78063 -10.73203 0.500 13.60179  ? 7   SER B CA  1 
ATOM   1649 C C   . SER B 2 7   ? 24.18151  -57.49634 -9.46314  1.000 13.29220  ? 7   SER B C   1 
ATOM   1650 O O   . SER B 2 7   ? 24.12183  -56.93325 -8.36483  1.000 14.47332  ? 7   SER B O   1 
ATOM   1651 C CB  A SER B 2 7   ? 24.89815  -56.39793 -11.65699 0.500 15.19598  ? 7   SER B CB  1 
ATOM   1652 C CB  B SER B 2 7   ? 25.03053  -56.46562 -11.54139 0.500 16.34247  ? 7   SER B CB  1 
ATOM   1653 O OG  A SER B 2 7   ? 25.74865  -55.46022 -11.04571 0.500 15.54003  ? 7   SER B OG  1 
ATOM   1654 O OG  B SER B 2 7   ? 24.85215  -55.46538 -12.51596 0.500 18.18166  ? 7   SER B OG  1 
ATOM   1655 N N   . GLY B 2 8   ? 24.57926  -58.75121 -9.60998  1.000 15.26237  ? 8   GLY B N   1 
ATOM   1656 C CA  . GLY B 2 8   ? 25.22018  -59.46708 -8.53253  1.000 15.50399  ? 8   GLY B CA  1 
ATOM   1657 C C   . GLY B 2 8   ? 24.44750  -60.59262 -7.87628  1.000 16.62898  ? 8   GLY B C   1 
ATOM   1658 O O   . GLY B 2 8   ? 25.04004  -61.29734 -7.04747  1.000 19.00694  ? 8   GLY B O   1 
ATOM   1659 N N   . GLY B 2 9   ? 23.20161  -60.82127 -8.19422  1.000 18.02874  ? 9   GLY B N   1 
ATOM   1660 C CA  . GLY B 2 9   ? 22.50727  -61.94126 -7.55620  1.000 20.50062  ? 9   GLY B CA  1 
ATOM   1661 C C   . GLY B 2 9   ? 22.99333  -63.30877 -8.03365  1.000 20.86210  ? 9   GLY B C   1 
ATOM   1662 O O   . GLY B 2 9   ? 23.83808  -63.43104 -8.92532  1.000 23.68049  ? 9   GLY B O   1 
ATOM   1663 N N   . GLY B 2 10  ? 22.47065  -64.35984 -7.40837  1.000 17.85969  ? 10  GLY B N   1 
ATOM   1664 C CA  . GLY B 2 10  ? 22.75848  -65.71666 -7.82838  1.000 18.84561  ? 10  GLY B CA  1 
ATOM   1665 C C   . GLY B 2 10  ? 22.40157  -66.71402 -6.73506  1.000 18.31801  ? 10  GLY B C   1 
ATOM   1666 O O   . GLY B 2 10  ? 21.74600  -66.38979 -5.75833  1.000 18.45125  ? 10  GLY B O   1 
ATOM   1667 N N   . SER B 2 11  ? 22.85759  -67.94390 -6.95084  1.000 21.15583  ? 11  SER B N   1 
ATOM   1668 C CA  . SER B 2 11  ? 22.70021  -69.05147 -6.01911  1.000 21.78808  ? 11  SER B CA  1 
ATOM   1669 C C   . SER B 2 11  ? 23.98591  -69.24852 -5.22023  1.000 24.34563  ? 11  SER B C   1 
ATOM   1670 O O   . SER B 2 11  ? 25.09019  -69.26450 -5.77815  1.000 26.59900  ? 11  SER B O   1 
ATOM   1671 C CB  . SER B 2 11  ? 22.43282  -70.32190 -6.82497  1.000 25.37085  ? 11  SER B CB  1 
ATOM   1672 O OG  . SER B 2 11  ? 21.10239  -70.29992 -7.31934  1.000 25.02821  ? 11  SER B OG  1 
ATOM   1673 N N   . VAL B 2 12  ? 23.85368  -69.44337 -3.91388  1.000 23.03641  ? 12  VAL B N   1 
ATOM   1674 C CA  A VAL B 2 12  ? 25.01029  -69.63917 -3.05113  0.500 27.41799  ? 12  VAL B CA  1 
ATOM   1675 C CA  B VAL B 2 12  ? 25.00523  -69.61578 -3.03817  0.500 27.39632  ? 12  VAL B CA  1 
ATOM   1676 C C   . VAL B 2 12  ? 24.60573  -70.60371 -1.95026  1.000 28.30539  ? 12  VAL B C   1 
ATOM   1677 O O   . VAL B 2 12  ? 23.41709  -70.79656 -1.66693  1.000 26.55876  ? 12  VAL B O   1 
ATOM   1678 C CB  A VAL B 2 12  ? 25.51783  -68.31053 -2.44664  0.500 28.56120  ? 12  VAL B CB  1 
ATOM   1679 C CB  B VAL B 2 12  ? 25.42252  -68.24840 -2.44185  0.500 28.52720  ? 12  VAL B CB  1 
ATOM   1680 C CG1 A VAL B 2 12  ? 26.18320  -67.45175 -3.51682  0.500 28.00093  ? 12  VAL B CG1 1 
ATOM   1681 C CG1 B VAL B 2 12  ? 24.32464  -67.68824 -1.56813  0.500 28.60978  ? 12  VAL B CG1 1 
ATOM   1682 C CG2 A VAL B 2 12  ? 24.38750  -67.56867 -1.78189  0.500 27.51323  ? 12  VAL B CG2 1 
ATOM   1683 C CG2 B VAL B 2 12  ? 26.73784  -68.33712 -1.69166  0.500 27.85037  ? 12  VAL B CG2 1 
ATOM   1684 N N   . GLN B 2 13  ? 25.60472  -71.23590 -1.35039  1.000 32.79149  ? 13  GLN B N   1 
ATOM   1685 C CA  . GLN B 2 13  ? 25.36237  -72.09754 -0.20830  1.000 36.85032  ? 13  GLN B CA  1 
ATOM   1686 C C   . GLN B 2 13  ? 25.30771  -71.24700 1.05182   1.000 32.82694  ? 13  GLN B C   1 
ATOM   1687 O O   . GLN B 2 13  ? 25.95253  -70.19694 1.14401   1.000 30.37344  ? 13  GLN B O   1 
ATOM   1688 C CB  . GLN B 2 13  ? 26.49760  -73.11508 -0.06281  1.000 43.90210  ? 13  GLN B CB  1 
ATOM   1689 C CG  . GLN B 2 13  ? 26.80773  -73.90079 -1.33580  1.000 49.10273  ? 13  GLN B CG  1 
ATOM   1690 C CD  . GLN B 2 13  ? 25.56138  -74.43596 -2.02422  1.000 53.10020  ? 13  GLN B CD  1 
ATOM   1691 O OE1 . GLN B 2 13  ? 24.63342  -74.91626 -1.36789  1.000 54.91996  ? 13  GLN B OE1 1 
ATOM   1692 N NE2 . GLN B 2 13  ? 25.52186  -74.33077 -3.35195  1.000 54.04485  ? 13  GLN B NE2 1 
ATOM   1693 N N   . ALA B 2 14  ? 24.53168  -71.71262 2.02882   1.000 26.54410  ? 14  ALA B N   1 
ATOM   1694 C CA  . ALA B 2 14  ? 24.48836  -71.04813 3.32754   1.000 24.22804  ? 14  ALA B CA  1 
ATOM   1695 C C   . ALA B 2 14  ? 25.90159  -70.83383 3.85549   1.000 24.08565  ? 14  ALA B C   1 
ATOM   1696 O O   . ALA B 2 14  ? 26.76552  -71.71567 3.75494   1.000 25.88753  ? 14  ALA B O   1 
ATOM   1697 C CB  . ALA B 2 14  ? 23.65784  -71.87106 4.31537   1.000 25.61884  ? 14  ALA B CB  1 
ATOM   1698 N N   . GLY B 2 15  ? 26.14119  -69.63419 4.40957   1.000 21.84120  ? 15  GLY B N   1 
ATOM   1699 C CA  . GLY B 2 15  ? 27.44707  -69.21959 4.86725   1.000 22.75743  ? 15  GLY B CA  1 
ATOM   1700 C C   . GLY B 2 15  ? 28.23577  -68.43146 3.84499   1.000 23.66843  ? 15  GLY B C   1 
ATOM   1701 O O   . GLY B 2 15  ? 29.23723  -67.79696 4.20525   1.000 26.09362  ? 15  GLY B O   1 
ATOM   1702 N N   . GLY B 2 16  ? 27.81552  -68.46954 2.58253   1.000 23.81431  ? 16  GLY B N   1 
ATOM   1703 C CA  . GLY B 2 16  ? 28.50256  -67.80110 1.49889   1.000 23.75311  ? 16  GLY B CA  1 
ATOM   1704 C C   . GLY B 2 16  ? 28.19075  -66.31819 1.44431   1.000 21.05346  ? 16  GLY B C   1 
ATOM   1705 O O   . GLY B 2 16  ? 27.50638  -65.75777 2.30173   1.000 21.09552  ? 16  GLY B O   1 
ATOM   1706 N N   . SER B 2 17  ? 28.70442  -65.67137 0.40181   1.000 23.12553  ? 17  SER B N   1 
ATOM   1707 C CA  A SER B 2 17  ? 28.54841  -64.23505 0.26347   0.500 21.15045  ? 17  SER B CA  1 
ATOM   1708 C CA  B SER B 2 17  ? 28.60290  -64.22501 0.25396   0.500 21.11547  ? 17  SER B CA  1 
ATOM   1709 C C   . SER B 2 17  ? 28.23088  -63.86719 -1.17769  1.000 20.78590  ? 17  SER B C   1 
ATOM   1710 O O   . SER B 2 17  ? 28.54117  -64.60297 -2.11671  1.000 22.59029  ? 17  SER B O   1 
ATOM   1711 C CB  A SER B 2 17  ? 29.80242  -63.50768 0.74383   0.500 25.37101  ? 17  SER B CB  1 
ATOM   1712 C CB  B SER B 2 17  ? 29.93688  -63.53810 0.57547   0.500 25.42768  ? 17  SER B CB  1 
ATOM   1713 O OG  A SER B 2 17  ? 30.86410  -63.75394 -0.15566  0.500 26.31949  ? 17  SER B OG  1 
ATOM   1714 O OG  B SER B 2 17  ? 30.30057  -63.70823 1.93101   0.500 26.48398  ? 17  SER B OG  1 
ATOM   1715 N N   . LEU B 2 18  ? 27.56854  -62.72412 -1.33305  1.000 17.87171  ? 18  LEU B N   1 
ATOM   1716 C CA  . LEU B 2 18  ? 27.29155  -62.14031 -2.62868  1.000 18.06283  ? 18  LEU B CA  1 
ATOM   1717 C C   . LEU B 2 18  ? 27.44542  -60.64025 -2.44292  1.000 17.27745  ? 18  LEU B C   1 
ATOM   1718 O O   . LEU B 2 18  ? 27.22658  -60.11444 -1.35020  1.000 18.84081  ? 18  LEU B O   1 
ATOM   1719 C CB  . LEU B 2 18  ? 25.83234  -62.41380 -3.04762  1.000 19.31913  ? 18  LEU B CB  1 
ATOM   1720 C CG  . LEU B 2 18  ? 25.53955  -63.82644 -3.55368  1.000 21.32890  ? 18  LEU B CG  1 
ATOM   1721 C CD1 . LEU B 2 18  ? 24.02262  -64.01070 -3.61321  1.000 21.52639  ? 18  LEU B CD1 1 
ATOM   1722 C CD2 . LEU B 2 18  ? 26.19305  -64.18567 -4.88961  1.000 23.21906  ? 18  LEU B CD2 1 
ATOM   1723 N N   . ARG B 2 19  ? 27.75000  -59.92488 -3.52515  1.000 16.72893  ? 19  ARG B N   1 
ATOM   1724 C CA  A ARG B 2 19  ? 27.76430  -58.47024 -3.50827  0.500 16.09671  ? 19  ARG B CA  1 
ATOM   1725 C CA  B ARG B 2 19  ? 27.74830  -58.46699 -3.50394  0.500 16.05908  ? 19  ARG B CA  1 
ATOM   1726 C C   . ARG B 2 19  ? 26.80671  -57.96738 -4.58264  1.000 15.36081  ? 19  ARG B C   1 
ATOM   1727 O O   . ARG B 2 19  ? 27.00370  -58.24243 -5.76533  1.000 17.95051  ? 19  ARG B O   1 
ATOM   1728 C CB  A ARG B 2 19  ? 29.18863  -57.97916 -3.75400  0.500 18.79735  ? 19  ARG B CB  1 
ATOM   1729 C CB  B ARG B 2 19  ? 29.13926  -57.86064 -3.69466  0.500 18.55908  ? 19  ARG B CB  1 
ATOM   1730 C CG  A ARG B 2 19  ? 29.37537  -56.50959 -3.59634  0.500 20.62692  ? 19  ARG B CG  1 
ATOM   1731 C CG  B ARG B 2 19  ? 29.10246  -56.34130 -3.59152  0.500 19.66411  ? 19  ARG B CG  1 
ATOM   1732 C CD  A ARG B 2 19  ? 30.86526  -56.21525 -3.74284  0.500 25.82317  ? 19  ARG B CD  1 
ATOM   1733 C CD  B ARG B 2 19  ? 30.47998  -55.73173 -3.86410  0.500 24.80488  ? 19  ARG B CD  1 
ATOM   1734 N NE  A ARG B 2 19  ? 31.17446  -54.79574 -3.69071  0.500 28.30153  ? 19  ARG B NE  1 
ATOM   1735 N NE  B ARG B 2 19  ? 30.76264  -55.58726 -5.28601  0.500 28.00470  ? 19  ARG B NE  1 
ATOM   1736 C CZ  A ARG B 2 19  ? 31.59554  -54.18927 -2.58827  0.500 31.01930  ? 19  ARG B CZ  1 
ATOM   1737 C CZ  B ARG B 2 19  ? 31.60937  -54.70476 -5.80191  0.500 30.72138  ? 19  ARG B CZ  1 
ATOM   1738 N NH1 A ARG B 2 19  ? 31.63543  -54.82150 -1.42606  0.500 30.79915  ? 19  ARG B NH1 1 
ATOM   1739 N NH1 B ARG B 2 19  ? 32.30976  -53.88459 -5.03511  0.500 30.33658  ? 19  ARG B NH1 1 
ATOM   1740 N NH2 A ARG B 2 19  ? 31.97687  -52.91607 -2.64863  0.500 31.89973  ? 19  ARG B NH2 1 
ATOM   1741 N NH2 B ARG B 2 19  ? 31.76675  -54.65434 -7.12008  0.500 30.56528  ? 19  ARG B NH2 1 
ATOM   1742 N N   . LEU B 2 20  ? 25.77843  -57.24652 -4.17481  1.000 13.68168  ? 20  LEU B N   1 
ATOM   1743 C CA  . LEU B 2 20  ? 24.86124  -56.64784 -5.13190  1.000 13.77651  ? 20  LEU B CA  1 
ATOM   1744 C C   . LEU B 2 20  ? 25.29444  -55.22673 -5.42112  1.000 13.56476  ? 20  LEU B C   1 
ATOM   1745 O O   . LEU B 2 20  ? 25.86179  -54.54491 -4.55572  1.000 14.47844  ? 20  LEU B O   1 
ATOM   1746 C CB  . LEU B 2 20  ? 23.44240  -56.61863 -4.57407  1.000 13.47723  ? 20  LEU B CB  1 
ATOM   1747 C CG  . LEU B 2 20  ? 22.90510  -57.92756 -3.99671  1.000 13.82944  ? 20  LEU B CG  1 
ATOM   1748 C CD1 . LEU B 2 20  ? 21.44325  -57.77701 -3.61838  1.000 15.12693  ? 20  LEU B CD1 1 
ATOM   1749 C CD2 . LEU B 2 20  ? 23.10507  -59.08239 -4.97769  1.000 15.83421  ? 20  LEU B CD2 1 
ATOM   1750 N N   . SER B 2 21  ? 24.98573  -54.78273 -6.62661  1.000 13.24647  ? 21  SER B N   1 
ATOM   1751 C CA  A SER B 2 21  ? 25.25172  -53.42473 -7.08166  0.500 14.02500  ? 21  SER B CA  1 
ATOM   1752 C CA  B SER B 2 21  ? 25.23117  -53.40511 -7.00263  0.500 14.35009  ? 21  SER B CA  1 
ATOM   1753 C C   . SER B 2 21  ? 23.95794  -52.79374 -7.56462  1.000 13.92226  ? 21  SER B C   1 
ATOM   1754 O O   . SER B 2 21  ? 23.14980  -53.47004 -8.21771  1.000 13.71252  ? 21  SER B O   1 
ATOM   1755 C CB  A SER B 2 21  ? 26.22027  -53.44877 -8.26197  0.500 17.80260  ? 21  SER B CB  1 
ATOM   1756 C CB  B SER B 2 21  ? 26.35313  -53.30729 -8.02602  0.500 17.80996  ? 21  SER B CB  1 
ATOM   1757 O OG  A SER B 2 21  ? 27.48728  -53.93720 -7.89349  0.500 19.61844  ? 21  SER B OG  1 
ATOM   1758 O OG  B SER B 2 21  ? 25.97109  -53.94112 -9.22454  0.500 21.37108  ? 21  SER B OG  1 
ATOM   1759 N N   . CYS B 2 22  ? 23.80136  -51.49740 -7.29916  1.000 13.59786  ? 22  CYS B N   1 
ATOM   1760 C CA  . CYS B 2 22  ? 22.68964  -50.72829 -7.83813  1.000 13.37847  ? 22  CYS B CA  1 
ATOM   1761 C C   . CYS B 2 22  ? 23.31737  -49.50297 -8.49053  1.000 13.67364  ? 22  CYS B C   1 
ATOM   1762 O O   . CYS B 2 22  ? 23.80287  -48.60477 -7.79333  1.000 14.56647  ? 22  CYS B O   1 
ATOM   1763 C CB  . CYS B 2 22  ? 21.73714  -50.34012 -6.70303  1.000 14.58366  ? 22  CYS B CB  1 
ATOM   1764 S SG  . CYS B 2 22  ? 20.32513  -49.33807 -7.28474  1.000 16.60790  ? 22  CYS B SG  1 
ATOM   1765 N N   . ALA B 2 23  ? 23.35042  -49.47211 -9.81644  1.000 13.57546  ? 23  ALA B N   1 
ATOM   1766 C CA  . ALA B 2 23  ? 24.06003  -48.42915 -10.55834 1.000 15.17441  ? 23  ALA B CA  1 
ATOM   1767 C C   . ALA B 2 23  ? 23.06199  -47.48008 -11.21313 1.000 13.91948  ? 23  ALA B C   1 
ATOM   1768 O O   . ALA B 2 23  ? 22.16097  -47.92099 -11.91705 1.000 14.62563  ? 23  ALA B O   1 
ATOM   1769 C CB  . ALA B 2 23  ? 24.93688  -49.07701 -11.63989 1.000 17.31470  ? 23  ALA B CB  1 
ATOM   1770 N N   . ALA B 2 24  ? 23.22950  -46.18134 -10.99923 1.000 14.07134  ? 24  ALA B N   1 
ATOM   1771 C CA  . ALA B 2 24  ? 22.34932  -45.19645 -11.61424 1.000 13.97097  ? 24  ALA B CA  1 
ATOM   1772 C C   . ALA B 2 24  ? 23.01674  -44.67536 -12.88539 1.000 16.14471  ? 24  ALA B C   1 
ATOM   1773 O O   . ALA B 2 24  ? 24.22196  -44.41354 -12.90670 1.000 19.70421  ? 24  ALA B O   1 
ATOM   1774 C CB  . ALA B 2 24  ? 22.08975  -44.02519 -10.66013 1.000 15.10609  ? 24  ALA B CB  1 
ATOM   1775 N N   . SER B 2 25  ? 22.22348  -44.46538 -13.92533 1.000 16.28707  ? 25  SER B N   1 
ATOM   1776 C CA  . SER B 2 25  ? 22.74500  -43.93914 -15.17319 1.000 19.16415  ? 25  SER B CA  1 
ATOM   1777 C C   . SER B 2 25  ? 21.69674  -43.06539 -15.84729 1.000 19.58438  ? 25  SER B C   1 
ATOM   1778 O O   . SER B 2 25  ? 20.52699  -43.03327 -15.45063 1.000 20.00471  ? 25  SER B O   1 
ATOM   1779 C CB  . SER B 2 25  ? 23.21785  -45.06935 -16.09299 1.000 21.20678  ? 25  SER B CB  1 
ATOM   1780 O OG  . SER B 2 25  ? 22.12877  -45.87737 -16.47273 1.000 21.91958  ? 25  SER B OG  1 
ATOM   1781 N N   . GLY B 2 26  ? 22.12725  -42.37373 -16.90746 1.000 19.85254  ? 26  GLY B N   1 
ATOM   1782 C CA  . GLY B 2 26  ? 21.21936  -41.43980 -17.55759 1.000 19.18588  ? 26  GLY B CA  1 
ATOM   1783 C C   . GLY B 2 26  ? 21.45599  -40.00777 -17.10931 1.000 19.21410  ? 26  GLY B C   1 
ATOM   1784 O O   . GLY B 2 26  ? 22.58890  -39.63025 -16.76428 1.000 19.57016  ? 26  GLY B O   1 
ATOM   1785 N N   A ASP B 2 27  ? 20.40148  -39.20261 -17.10523 0.500 18.04676  ? 27  ASP B N   1 
ATOM   1786 N N   B ASP B 2 27  ? 20.41033  -39.18676 -17.13921 0.500 18.19656  ? 27  ASP B N   1 
ATOM   1787 C CA  A ASP B 2 27  ? 20.50324  -37.78581 -16.75530 0.500 18.89959  ? 27  ASP B CA  1 
ATOM   1788 C CA  B ASP B 2 27  ? 20.53475  -37.77646 -16.76493 0.500 18.72502  ? 27  ASP B CA  1 
ATOM   1789 C C   A ASP B 2 27  ? 20.38200  -37.60214 -15.24360 0.500 18.70831  ? 27  ASP B C   1 
ATOM   1790 C C   B ASP B 2 27  ? 20.38194  -37.60346 -15.25271 0.500 18.73682  ? 27  ASP B C   1 
ATOM   1791 O O   A ASP B 2 27  ? 19.53517  -36.85704 -14.73493 0.500 19.23406  ? 27  ASP B O   1 
ATOM   1792 O O   B ASP B 2 27  ? 19.52419  -36.86425 -14.75104 0.500 19.28342  ? 27  ASP B O   1 
ATOM   1793 C CB  A ASP B 2 27  ? 19.44313  -36.99359 -17.49854 0.500 23.66202  ? 27  ASP B CB  1 
ATOM   1794 C CB  B ASP B 2 27  ? 19.57462  -36.90114 -17.56494 0.500 24.20433  ? 27  ASP B CB  1 
ATOM   1795 C CG  A ASP B 2 27  ? 19.64966  -37.02944 -18.98926 0.500 23.39818  ? 27  ASP B CG  1 
ATOM   1796 C CG  B ASP B 2 27  ? 18.10699  -37.24917 -17.34451 0.500 27.72473  ? 27  ASP B CG  1 
ATOM   1797 O OD1 A ASP B 2 27  ? 20.79276  -36.79988 -19.43190 0.500 36.24586  ? 27  ASP B OD1 1 
ATOM   1798 O OD1 B ASP B 2 27  ? 17.79443  -38.37790 -16.91276 0.500 38.58595  ? 27  ASP B OD1 1 
ATOM   1799 O OD2 A ASP B 2 27  ? 18.67375  -37.33445 -19.70501 0.500 34.94579  ? 27  ASP B OD2 1 
ATOM   1800 O OD2 B ASP B 2 27  ? 17.24838  -36.37886 -17.61143 0.500 38.93621  ? 27  ASP B OD2 1 
ATOM   1801 N N   . THR B 2 28  ? 21.25963  -38.29434 -14.53761 1.000 18.51293  ? 28  THR B N   1 
ATOM   1802 C CA  . THR B 2 28  ? 21.25430  -38.24684 -13.07867 1.000 17.79084  ? 28  THR B CA  1 
ATOM   1803 C C   . THR B 2 28  ? 21.72188  -36.90425 -12.53463 1.000 20.93455  ? 28  THR B C   1 
ATOM   1804 O O   . THR B 2 28  ? 22.61709  -36.23641 -13.09875 1.000 21.78015  ? 28  THR B O   1 
ATOM   1805 C CB  . THR B 2 28  ? 22.14579  -39.33140 -12.52625 1.000 20.25434  ? 28  THR B CB  1 
ATOM   1806 O OG1 . THR B 2 28  ? 23.49005  -39.13983 -12.97793 1.000 21.51378  ? 28  THR B OG1 1 
ATOM   1807 C CG2 . THR B 2 28  ? 21.70572  -40.72414 -12.94967 1.000 20.91354  ? 28  THR B CG2 1 
ATOM   1808 N N   . GLY B 2 29  ? 21.10946  -36.49739 -11.44841 1.000 19.47508  ? 29  GLY B N   1 
ATOM   1809 C CA  . GLY B 2 29  ? 21.56570  -35.41289 -10.61924 1.000 17.75961  ? 29  GLY B CA  1 
ATOM   1810 C C   . GLY B 2 29  ? 21.93659  -35.96131 -9.25376  1.000 16.91119  ? 29  GLY B C   1 
ATOM   1811 O O   . GLY B 2 29  ? 22.78151  -36.85811 -9.13085  1.000 20.55739  ? 29  GLY B O   1 
ATOM   1812 N N   . ARG B 2 30  ? 21.36333  -35.39940 -8.21029  1.000 15.22270  ? 30  ARG B N   1 
ATOM   1813 C CA  . ARG B 2 30  ? 21.71978  -35.74679 -6.84147  1.000 14.09760  ? 30  ARG B CA  1 
ATOM   1814 C C   . ARG B 2 30  ? 20.84835  -36.91199 -6.37994  1.000 15.03590  ? 30  ARG B C   1 
ATOM   1815 O O   . ARG B 2 30  ? 19.63580  -36.92198 -6.60914  1.000 15.36018  ? 30  ARG B O   1 
ATOM   1816 C CB  . ARG B 2 30  ? 21.44825  -34.54381 -5.94596  1.000 14.82396  ? 30  ARG B CB  1 
ATOM   1817 C CG  . ARG B 2 30  ? 21.71837  -34.77647 -4.49793  1.000 17.10694  ? 30  ARG B CG  1 
ATOM   1818 C CD  . ARG B 2 30  ? 21.72990  -33.43627 -3.79487  1.000 17.88024  ? 30  ARG B CD  1 
ATOM   1819 N NE  . ARG B 2 30  ? 23.02400  -32.80795 -3.96600  1.000 17.94520  ? 30  ARG B NE  1 
ATOM   1820 C CZ  . ARG B 2 30  ? 24.03776  -33.22152 -3.19791  1.000 21.43229  ? 30  ARG B CZ  1 
ATOM   1821 N NH1 . ARG B 2 30  ? 23.86630  -34.14788 -2.26540  1.000 23.41797  ? 30  ARG B NH1 1 
ATOM   1822 N NH2 . ARG B 2 30  ? 25.23344  -32.72201 -3.36525  1.000 22.97161  ? 30  ARG B NH2 1 
ATOM   1823 N N   . THR B 2 31  ? 21.44645  -37.86423 -5.64974  1.000 14.84654  ? 31  THR B N   1 
ATOM   1824 C CA  . THR B 2 31  ? 20.66021  -38.94323 -5.03750  1.000 15.01876  ? 31  THR B CA  1 
ATOM   1825 C C   . THR B 2 31  ? 20.30886  -38.52049 -3.61163  1.000 15.02469  ? 31  THR B C   1 
ATOM   1826 O O   . THR B 2 31  ? 21.19574  -38.29440 -2.79099  1.000 18.39527  ? 31  THR B O   1 
ATOM   1827 C CB  . THR B 2 31  ? 21.46445  -40.25077 -5.00941  1.000 16.52618  ? 31  THR B CB  1 
ATOM   1828 O OG1 . THR B 2 31  ? 21.63393  -40.71168 -6.35368  1.000 18.32041  ? 31  THR B OG1 1 
ATOM   1829 C CG2 . THR B 2 31  ? 20.67281  -41.37619 -4.23964  1.000 17.66476  ? 31  THR B CG2 1 
ATOM   1830 N N   . CYS B 2 32  ? 19.01798  -38.40878 -3.32903  1.000 14.87660  ? 32  CYS B N   1 
ATOM   1831 C CA  . CYS B 2 32  ? 18.55515  -38.06911 -1.98941  1.000 15.29317  ? 32  CYS B CA  1 
ATOM   1832 C C   . CYS B 2 32  ? 18.66404  -39.27401 -1.06617  1.000 14.92205  ? 32  CYS B C   1 
ATOM   1833 O O   . CYS B 2 32  ? 19.11028  -39.12995 0.07452   1.000 17.78251  ? 32  CYS B O   1 
ATOM   1834 C CB  . CYS B 2 32  ? 17.10707  -37.55995 -2.07426  1.000 16.12007  ? 32  CYS B CB  1 
ATOM   1835 S SG  . CYS B 2 32  ? 16.97967  -35.87520 -2.82033  1.000 17.10572  ? 32  CYS B SG  1 
ATOM   1836 N N   A ASN B 2 33  ? 18.30385  -40.45420 -1.53095  0.500 15.10950  ? 33  ASN B N   1 
ATOM   1837 N N   B ASN B 2 33  ? 18.33118  -40.47350 -1.55103  0.500 15.18432  ? 33  ASN B N   1 
ATOM   1838 C CA  A ASN B 2 33  ? 18.55762  -41.64380 -0.74624  0.500 15.10547  ? 33  ASN B CA  1 
ATOM   1839 C CA  B ASN B 2 33  ? 18.19560  -41.62791 -0.67583  0.500 14.31292  ? 33  ASN B CA  1 
ATOM   1840 C C   A ASN B 2 33  ? 18.41496  -42.85085 -1.64176  0.500 14.22555  ? 33  ASN B C   1 
ATOM   1841 C C   B ASN B 2 33  ? 18.16496  -42.87821 -1.55351  0.500 13.69146  ? 33  ASN B C   1 
ATOM   1842 O O   A ASN B 2 33  ? 17.99954  -42.76073 -2.79851  0.500 14.06815  ? 33  ASN B O   1 
ATOM   1843 O O   B ASN B 2 33  ? 17.66408  -42.81766 -2.67872  0.500 14.62765  ? 33  ASN B O   1 
ATOM   1844 C CB  A ASN B 2 33  ? 17.60222  -41.76687 0.42752   0.500 19.36014  ? 33  ASN B CB  1 
ATOM   1845 C CB  B ASN B 2 33  ? 16.90586  -41.44867 0.13474   0.500 16.88744  ? 33  ASN B CB  1 
ATOM   1846 C CG  A ASN B 2 33  ? 16.20075  -41.50538 0.02976   0.500 21.57905  ? 33  ASN B CG  1 
ATOM   1847 C CG  B ASN B 2 33  ? 16.73060  -42.48316 1.18253   0.500 21.14556  ? 33  ASN B CG  1 
ATOM   1848 O OD1 A ASN B 2 33  ? 15.64267  -42.23245 -0.79424  0.500 22.34815  ? 33  ASN B OD1 1 
ATOM   1849 O OD1 B ASN B 2 33  ? 15.61614  -42.91701 1.46526   0.500 24.14613  ? 33  ASN B OD1 1 
ATOM   1850 N ND2 A ASN B 2 33  ? 15.57640  -40.49445 0.66366   0.500 24.27953  ? 33  ASN B ND2 1 
ATOM   1851 N ND2 B ASN B 2 33  ? 17.83600  -42.96358 1.70791   0.500 20.13050  ? 33  ASN B ND2 1 
ATOM   1852 N N   . LEU B 2 34  ? 18.75092  -43.99091 -1.07343  1.000 13.74930  ? 34  LEU B N   1 
ATOM   1853 C CA  . LEU B 2 34  ? 18.69263  -45.25442 -1.78259  1.000 13.48248  ? 34  LEU B CA  1 
ATOM   1854 C C   . LEU B 2 34  ? 18.40173  -46.35266 -0.77359  1.000 12.30829  ? 34  LEU B C   1 
ATOM   1855 O O   . LEU B 2 34  ? 19.02202  -46.37789 0.29936   1.000 13.33704  ? 34  LEU B O   1 
ATOM   1856 C CB  . LEU B 2 34  ? 19.98489  -45.49641 -2.58609  1.000 15.23465  ? 34  LEU B CB  1 
ATOM   1857 C CG  . LEU B 2 34  ? 19.98200  -46.73626 -3.48512  1.000 15.28585  ? 34  LEU B CG  1 
ATOM   1858 C CD1 . LEU B 2 34  ? 20.84476  -46.42076 -4.70685  1.000 15.96555  ? 34  LEU B CD1 1 
ATOM   1859 C CD2 . LEU B 2 34  ? 20.37997  -48.02140 -2.76784  1.000 15.25169  ? 34  LEU B CD2 1 
ATOM   1860 N N   . VAL B 2 35  ? 17.45858  -47.22508 -1.11991  1.000 11.76436  ? 35  VAL B N   1 
ATOM   1861 C CA  . VAL B 2 35  ? 17.01944  -48.29414 -0.23737  1.000 11.20472  ? 35  VAL B CA  1 
ATOM   1862 C C   . VAL B 2 35  ? 17.16086  -49.61377 -0.97738  1.000 11.16189  ? 35  VAL B C   1 
ATOM   1863 O O   . VAL B 2 35  ? 16.77244  -49.73185 -2.13996  1.000 12.26730  ? 35  VAL B O   1 
ATOM   1864 C CB  . VAL B 2 35  ? 15.55713  -48.11370 0.21585   1.000 12.58499  ? 35  VAL B CB  1 
ATOM   1865 C CG1 . VAL B 2 35  ? 15.17690  -49.19576 1.20862   1.000 12.51359  ? 35  VAL B CG1 1 
ATOM   1866 C CG2 . VAL B 2 35  ? 15.31283  -46.71167 0.77653   1.000 14.15098  ? 35  VAL B CG2 1 
ATOM   1867 N N   . TRP B 2 36  ? 17.68845  -50.62814 -0.28610  1.000 11.46875  ? 36  TRP B N   1 
ATOM   1868 C CA  . TRP B 2 36  ? 17.58485  -52.01964 -0.71485  1.000 11.00366  ? 36  TRP B CA  1 
ATOM   1869 C C   . TRP B 2 36  ? 16.41554  -52.67672 0.00966   1.000 11.20397  ? 36  TRP B C   1 
ATOM   1870 O O   . TRP B 2 36  ? 16.32975  -52.60616 1.24856   1.000 11.65270  ? 36  TRP B O   1 
ATOM   1871 C CB  . TRP B 2 36  ? 18.84814  -52.79984 -0.38441  1.000 12.38768  ? 36  TRP B CB  1 
ATOM   1872 C CG  . TRP B 2 36  ? 19.98310  -52.51760 -1.29947  1.000 12.50465  ? 36  TRP B CG  1 
ATOM   1873 C CD1 . TRP B 2 36  ? 21.02830  -51.68722 -1.06073  1.000 15.59852  ? 36  TRP B CD1 1 
ATOM   1874 C CD2 . TRP B 2 36  ? 20.18855  -53.07754 -2.58801  1.000 13.22330  ? 36  TRP B CD2 1 
ATOM   1875 N NE1 . TRP B 2 36  ? 21.87515  -51.69137 -2.11815  1.000 16.73356  ? 36  TRP B NE1 1 
ATOM   1876 C CE2 . TRP B 2 36  ? 21.40218  -52.54547 -3.07933  1.000 15.53900  ? 36  TRP B CE2 1 
ATOM   1877 C CE3 . TRP B 2 36  ? 19.48661  -54.00491 -3.36012  1.000 14.73426  ? 36  TRP B CE3 1 
ATOM   1878 C CZ2 . TRP B 2 36  ? 21.92964  -52.90005 -4.33233  1.000 19.42680  ? 36  TRP B CZ2 1 
ATOM   1879 C CZ3 . TRP B 2 36  ? 20.00360  -54.34293 -4.60062  1.000 17.03145  ? 36  TRP B CZ3 1 
ATOM   1880 C CH2 . TRP B 2 36  ? 21.21589  -53.78583 -5.07377  1.000 19.60018  ? 36  TRP B CH2 1 
ATOM   1881 N N   . TYR B 2 37  ? 15.53164  -53.31573 -0.76271  1.000 11.43889  ? 37  TYR B N   1 
ATOM   1882 C CA  . TYR B 2 37  ? 14.41811  -54.09580 -0.30443  1.000 11.51155  ? 37  TYR B CA  1 
ATOM   1883 C C   . TYR B 2 37  ? 14.57674  -55.51137 -0.83076  1.000 10.99133  ? 37  TYR B C   1 
ATOM   1884 O O   . TYR B 2 37  ? 15.34332  -55.77829 -1.77226  1.000 11.81441  ? 37  TYR B O   1 
ATOM   1885 C CB  . TYR B 2 37  ? 13.08524  -53.54542 -0.84253  1.000 11.89098  ? 37  TYR B CB  1 
ATOM   1886 C CG  . TYR B 2 37  ? 12.74682  -52.12273 -0.46918  1.000 11.48082  ? 37  TYR B CG  1 
ATOM   1887 C CD1 . TYR B 2 37  ? 12.11703  -51.86468 0.76288   1.000 12.23222  ? 37  TYR B CD1 1 
ATOM   1888 C CD2 . TYR B 2 37  ? 12.95661  -51.03969 -1.33076  1.000 12.41929  ? 37  TYR B CD2 1 
ATOM   1889 C CE1 . TYR B 2 37  ? 11.74889  -50.56767 1.13978   1.000 12.39912  ? 37  TYR B CE1 1 
ATOM   1890 C CE2 . TYR B 2 37  ? 12.56991  -49.77189 -0.97149  1.000 12.56245  ? 37  TYR B CE2 1 
ATOM   1891 C CZ  . TYR B 2 37  ? 11.97779  -49.52938 0.25930   1.000 11.67376  ? 37  TYR B CZ  1 
ATOM   1892 O OH  . TYR B 2 37  ? 11.62296  -48.29182 0.68122   1.000 13.38104  ? 37  TYR B OH  1 
ATOM   1893 N N   . ARG B 2 38  ? 13.78856  -56.43508 -0.28181  1.000 11.57336  ? 38  ARG B N   1 
ATOM   1894 C CA  . ARG B 2 38  ? 13.73861  -57.77729 -0.85002  1.000 11.24359  ? 38  ARG B CA  1 
ATOM   1895 C C   . ARG B 2 38  ? 12.31665  -58.28700 -0.76356  1.000 11.15936  ? 38  ARG B C   1 
ATOM   1896 O O   . ARG B 2 38  ? 11.57460  -57.94310 0.16944   1.000 12.34412  ? 38  ARG B O   1 
ATOM   1897 C CB  . ARG B 2 38  ? 14.75281  -58.67218 -0.17486  1.000 12.42655  ? 38  ARG B CB  1 
ATOM   1898 C CG  . ARG B 2 38  ? 14.46713  -58.92370 1.28699   1.000 13.84511  ? 38  ARG B CG  1 
ATOM   1899 C CD  . ARG B 2 38  ? 15.48831  -59.88220 1.89553   1.000 14.41887  ? 38  ARG B CD  1 
ATOM   1900 N NE  . ARG B 2 38  ? 15.28353  -60.02479 3.32158   1.000 15.30263  ? 38  ARG B NE  1 
ATOM   1901 C CZ  . ARG B 2 38  ? 16.17089  -60.54990 4.15266   1.000 16.17117  ? 38  ARG B CZ  1 
ATOM   1902 N NH1 . ARG B 2 38  ? 17.36928  -60.93817 3.73279   1.000 15.08671  ? 38  ARG B NH1 1 
ATOM   1903 N NH2 . ARG B 2 38  ? 15.80246  -60.79985 5.40392   1.000 19.46121  ? 38  ARG B NH2 1 
ATOM   1904 N N   . GLN B 2 39  ? 11.94027  -59.12964 -1.70879  1.000 12.25854  ? 39  GLN B N   1 
ATOM   1905 C CA  A GLN B 2 39  ? 10.61569  -59.71762 -1.70487  0.500 13.68841  ? 39  GLN B CA  1 
ATOM   1906 C CA  B GLN B 2 39  ? 10.61141  -59.71390 -1.72558  0.500 13.64641  ? 39  GLN B CA  1 
ATOM   1907 C C   . GLN B 2 39  ? 10.69753  -61.12651 -2.26000  1.000 15.87248  ? 39  GLN B C   1 
ATOM   1908 O O   . GLN B 2 39  ? 11.19085  -61.33365 -3.36837  1.000 18.80307  ? 39  GLN B O   1 
ATOM   1909 C CB  A GLN B 2 39  ? 9.63880   -58.89231 -2.55542  0.500 16.32874  ? 39  GLN B CB  1 
ATOM   1910 C CB  B GLN B 2 39  ? 9.63493   -58.91545 -2.60531  0.500 16.24000  ? 39  GLN B CB  1 
ATOM   1911 C CG  A GLN B 2 39  ? 8.18329   -59.34475 -2.44413  0.500 18.06534  ? 39  GLN B CG  1 
ATOM   1912 C CG  B GLN B 2 39  ? 8.20241   -59.44094 -2.50803  0.500 18.97827  ? 39  GLN B CG  1 
ATOM   1913 C CD  A GLN B 2 39  ? 7.18510   -58.31467 -2.97342  0.500 16.34769  ? 39  GLN B CD  1 
ATOM   1914 C CD  B GLN B 2 39  ? 7.30365   -59.01200 -3.65900  0.500 21.88784  ? 39  GLN B CD  1 
ATOM   1915 O OE1 A GLN B 2 39  ? 7.24636   -57.11061 -2.68643  0.500 15.78746  ? 39  GLN B OE1 1 
ATOM   1916 O OE1 B GLN B 2 39  ? 7.75348   -58.63012 -4.75101  0.500 22.84422  ? 39  GLN B OE1 1 
ATOM   1917 N NE2 A GLN B 2 39  ? 6.29641   -58.78314 -3.84090  0.500 17.37788  ? 39  GLN B NE2 1 
ATOM   1918 N NE2 B GLN B 2 39  ? 6.00831   -59.03991 -3.40237  0.500 21.57674  ? 39  GLN B NE2 1 
ATOM   1919 N N   . ALA B 2 40  ? 10.17470  -62.03693 -1.54967  1.000 18.11570  ? 40  ALA B N   1 
ATOM   1920 C CA  . ALA B 2 40  ? 9.91050   -63.31803 -2.18005  1.000 18.64113  ? 40  ALA B CA  1 
ATOM   1921 C C   . ALA B 2 40  ? 8.47186   -63.28526 -2.70835  1.000 19.69603  ? 40  ALA B C   1 
ATOM   1922 O O   . ALA B 2 40  ? 7.62228   -62.54594 -2.17157  1.000 20.60722  ? 40  ALA B O   1 
ATOM   1923 C CB  . ALA B 2 40  ? 9.98901   -64.40731 -1.11921  1.000 20.90335  ? 40  ALA B CB  1 
ATOM   1924 N N   . PRO B 2 41  ? 8.11719   -64.04364 -3.75085  1.000 20.64629  ? 41  PRO B N   1 
ATOM   1925 C CA  . PRO B 2 41  ? 6.76615   -63.91920 -4.33809  1.000 20.09976  ? 41  PRO B CA  1 
ATOM   1926 C C   . PRO B 2 41  ? 5.66351   -64.09906 -3.30784  1.000 18.78227  ? 41  PRO B C   1 
ATOM   1927 O O   . PRO B 2 41  ? 5.69376   -65.02168 -2.49240  1.000 18.16878  ? 41  PRO B O   1 
ATOM   1928 C CB  . PRO B 2 41  ? 6.74172   -65.03204 -5.37873  1.000 22.57738  ? 41  PRO B CB  1 
ATOM   1929 C CG  . PRO B 2 41  ? 8.21183   -65.13515 -5.81124  1.000 23.58958  ? 41  PRO B CG  1 
ATOM   1930 C CD  . PRO B 2 41  ? 9.01149   -64.89525 -4.56196  1.000 22.68279  ? 41  PRO B CD  1 
ATOM   1931 N N   . GLY B 2 42  ? 4.66387   -63.22377 -3.37175  1.000 20.01413  ? 42  GLY B N   1 
ATOM   1932 C CA  . GLY B 2 42  ? 3.50937   -63.29684 -2.48749  1.000 19.98478  ? 42  GLY B CA  1 
ATOM   1933 C C   . GLY B 2 42  ? 3.73786   -62.76062 -1.09208  1.000 23.34200  ? 42  GLY B C   1 
ATOM   1934 O O   . GLY B 2 42  ? 2.77897   -62.67823 -0.29728  1.000 24.04419  ? 42  GLY B O   1 
ATOM   1935 N N   . LYS B 2 43  ? 4.96094   -62.39129 -0.75776  1.000 23.74973  ? 43  LYS B N   1 
ATOM   1936 C CA  . LYS B 2 43  ? 5.23663   -61.92820 0.58316   1.000 28.90446  ? 43  LYS B CA  1 
ATOM   1937 C C   . LYS B 2 43  ? 5.46463   -60.42889 0.51421   1.000 25.00720  ? 43  LYS B C   1 
ATOM   1938 O O   . LYS B 2 43  ? 5.70783   -59.85460 -0.55128  1.000 25.89796  ? 43  LYS B O   1 
ATOM   1939 C CB  . LYS B 2 43  ? 6.37645   -62.75103 1.18504   1.000 35.20794  ? 43  LYS B CB  1 
ATOM   1940 C CG  . LYS B 2 43  ? 6.94562   -62.28151 2.45433   1.000 41.32335  ? 43  LYS B CG  1 
ATOM   1941 C CD  . LYS B 2 43  ? 7.60077   -63.49754 3.09096   1.000 44.88334  ? 43  LYS B CD  1 
ATOM   1942 C CE  . LYS B 2 43  ? 8.72803   -63.12981 4.03468   1.000 46.90332  ? 43  LYS B CE  1 
ATOM   1943 N NZ  . LYS B 2 43  ? 9.65764   -64.28880 4.18285   1.000 48.14371  ? 43  LYS B NZ  1 
ATOM   1944 N N   . GLU B 2 44  ? 5.24396   -59.76583 1.62976   1.000 20.80864  ? 44  GLU B N   1 
ATOM   1945 C CA  . GLU B 2 44  ? 5.35650   -58.31924 1.67868   1.000 21.05483  ? 44  GLU B CA  1 
ATOM   1946 C C   . GLU B 2 44  ? 6.81405   -57.92360 1.42320   1.000 19.28605  ? 44  GLU B C   1 
ATOM   1947 O O   . GLU B 2 44  ? 7.75502   -58.54904 1.92993   1.000 20.13577  ? 44  GLU B O   1 
ATOM   1948 C CB  . GLU B 2 44  ? 4.83020   -57.82222 3.04793   1.000 22.63666  ? 44  GLU B CB  1 
ATOM   1949 C CG  . GLU B 2 44  ? 4.84730   -56.28958 3.31604   1.000 24.96093  ? 44  GLU B CG  1 
ATOM   1950 C CD  . GLU B 2 44  ? 3.95025   -55.39597 2.42940   1.000 27.78017  ? 44  GLU B CD  1 
ATOM   1951 O OE1 . GLU B 2 44  ? 3.10686   -55.86555 1.60190   1.000 30.10138  ? 44  GLU B OE1 1 
ATOM   1952 O OE2 . GLU B 2 44  ? 4.12014   -54.15814 2.54838   1.000 26.38549  ? 44  GLU B OE2 1 
ATOM   1953 N N   . LEU B 2 45  ? 7.01534   -56.89347 0.60243   1.000 18.93960  ? 45  LEU B N   1 
ATOM   1954 C CA  . LEU B 2 45  ? 8.34055   -56.31799 0.42268   1.000 15.78339  ? 45  LEU B CA  1 
ATOM   1955 C C   . LEU B 2 45  ? 8.92660   -56.00393 1.79952   1.000 14.85934  ? 45  LEU B C   1 
ATOM   1956 O O   . LEU B 2 45  ? 8.25053   -55.45055 2.67724   1.000 16.74539  ? 45  LEU B O   1 
ATOM   1957 C CB  . LEU B 2 45  ? 8.17771   -55.01360 -0.38401  1.000 17.35333  ? 45  LEU B CB  1 
ATOM   1958 C CG  . LEU B 2 45  ? 9.48557   -54.30545 -0.79666  1.000 15.78256  ? 45  LEU B CG  1 
ATOM   1959 C CD1 . LEU B 2 45  ? 10.17551  -55.10805 -1.89283  1.000 15.67462  ? 45  LEU B CD1 1 
ATOM   1960 C CD2 . LEU B 2 45  ? 9.19600   -52.92431 -1.27724  1.000 16.59942  ? 45  LEU B CD2 1 
ATOM   1961 N N   . GLU B 2 46  ? 10.20001  -56.31254 1.97166   1.000 13.34265  ? 46  GLU B N   1 
ATOM   1962 C CA  . GLU B 2 46  ? 10.87993  -56.12682 3.23774   1.000 14.16544  ? 46  GLU B CA  1 
ATOM   1963 C C   . GLU B 2 46  ? 12.02930  -55.14902 3.05586   1.000 12.53073  ? 46  GLU B C   1 
ATOM   1964 O O   . GLU B 2 46  ? 12.83653  -55.29713 2.12624   1.000 13.32448  ? 46  GLU B O   1 
ATOM   1965 C CB  . GLU B 2 46  ? 11.49791  -57.42601 3.74612   1.000 19.10786  ? 46  GLU B CB  1 
ATOM   1966 C CG  . GLU B 2 46  ? 10.63652  -58.51492 4.17236   1.000 28.14867  ? 46  GLU B CG  1 
ATOM   1967 C CD  . GLU B 2 46  ? 11.42765  -59.57697 4.94993   1.000 32.28145  ? 46  GLU B CD  1 
ATOM   1968 O OE1 . GLU B 2 46  ? 12.68973  -59.72136 4.76675   1.000 27.87196  ? 46  GLU B OE1 1 
ATOM   1969 O OE2 . GLU B 2 46  ? 10.76703  -60.29507 5.72963   1.000 37.05357  ? 46  GLU B OE2 1 
ATOM   1970 N N   . PHE B 2 47  ? 12.12802  -54.19490 3.96446   1.000 12.15259  ? 47  PHE B N   1 
ATOM   1971 C CA  . PHE B 2 47  ? 13.30977  -53.34690 4.05997   1.000 12.34448  ? 47  PHE B CA  1 
ATOM   1972 C C   . PHE B 2 47  ? 14.54657  -54.16848 4.42486   1.000 11.40844  ? 47  PHE B C   1 
ATOM   1973 O O   . PHE B 2 47  ? 14.50800  -55.00874 5.32790   1.000 12.55091  ? 47  PHE B O   1 
ATOM   1974 C CB  . PHE B 2 47  ? 13.04378  -52.27232 5.14335   1.000 12.86533  ? 47  PHE B CB  1 
ATOM   1975 C CG  . PHE B 2 47  ? 14.28177  -51.61641 5.65188   1.000 11.65852  ? 47  PHE B CG  1 
ATOM   1976 C CD1 . PHE B 2 47  ? 14.99795  -50.76120 4.82950   1.000 12.78611  ? 47  PHE B CD1 1 
ATOM   1977 C CD2 . PHE B 2 47  ? 14.70539  -51.77800 6.97065   1.000 13.22313  ? 47  PHE B CD2 1 
ATOM   1978 C CE1 . PHE B 2 47  ? 16.12582  -50.11764 5.27573   1.000 14.44005  ? 47  PHE B CE1 1 
ATOM   1979 C CE2 . PHE B 2 47  ? 15.82637  -51.09957 7.43758   1.000 14.75562  ? 47  PHE B CE2 1 
ATOM   1980 C CZ  . PHE B 2 47  ? 16.55039  -50.29560 6.61098   1.000 14.91420  ? 47  PHE B CZ  1 
ATOM   1981 N N   . VAL B 2 48  ? 15.64981  -53.90166 3.73637   1.000 11.39097  ? 48  VAL B N   1 
ATOM   1982 C CA  . VAL B 2 48  ? 16.94592  -54.50162 4.03463   1.000 11.77350  ? 48  VAL B CA  1 
ATOM   1983 C C   . VAL B 2 48  ? 17.93157  -53.46198 4.57774   1.000 11.58274  ? 48  VAL B C   1 
ATOM   1984 O O   . VAL B 2 48  ? 18.54248  -53.66438 5.62943   1.000 12.68332  ? 48  VAL B O   1 
ATOM   1985 C CB  . VAL B 2 48  ? 17.51055  -55.26552 2.82111   1.000 12.09248  ? 48  VAL B CB  1 
ATOM   1986 C CG1 . VAL B 2 48  ? 18.87092  -55.86484 3.13593   1.000 13.16952  ? 48  VAL B CG1 1 
ATOM   1987 C CG2 . VAL B 2 48  ? 16.53454  -56.34389 2.39769   1.000 12.95538  ? 48  VAL B CG2 1 
ATOM   1988 N N   . SER B 2 49  ? 18.19004  -52.39964 3.81376   1.000 11.94770  ? 49  SER B N   1 
ATOM   1989 C CA  . SER B 2 49  ? 19.18268  -51.41477 4.23327   1.000 12.57236  ? 49  SER B CA  1 
ATOM   1990 C C   . SER B 2 49  ? 18.96164  -50.13187 3.45304   1.000 11.40181  ? 49  SER B C   1 
ATOM   1991 O O   . SER B 2 49  ? 18.44769  -50.17626 2.33526   1.000 12.87215  ? 49  SER B O   1 
ATOM   1992 C CB  . SER B 2 49  ? 20.58278  -51.97155 3.98598   1.000 12.71240  ? 49  SER B CB  1 
ATOM   1993 O OG  . SER B 2 49  ? 21.59688  -51.06709 4.31513   1.000 13.68262  ? 49  SER B OG  1 
ATOM   1994 N N   . SER B 2 50  ? 19.35024  -48.98124 4.01288   1.000 12.73539  ? 50  SER B N   1 
ATOM   1995 C CA  . SER B 2 50  ? 19.28997  -47.77886 3.20405   1.000 12.94514  ? 50  SER B CA  1 
ATOM   1996 C C   . SER B 2 50  ? 20.48534  -46.89314 3.51091   1.000 12.56190  ? 50  SER B C   1 
ATOM   1997 O O   . SER B 2 50  ? 21.15165  -47.04413 4.54999   1.000 13.73648  ? 50  SER B O   1 
ATOM   1998 C CB  . SER B 2 50  ? 18.02438  -46.92634 3.38472   1.000 14.42293  ? 50  SER B CB  1 
ATOM   1999 O OG  . SER B 2 50  ? 17.89157  -46.27159 4.63151   1.000 15.23634  ? 50  SER B OG  1 
ATOM   2000 N N   . ILE B 2 51  ? 20.72222  -45.94086 2.60553   1.000 12.77792  ? 51  ILE B N   1 
ATOM   2001 C CA  . ILE B 2 51  ? 21.81401  -45.00335 2.77397   1.000 13.90010  ? 51  ILE B CA  1 
ATOM   2002 C C   . ILE B 2 51  ? 21.35317  -43.63870 2.26848   1.000 13.97700  ? 51  ILE B C   1 
ATOM   2003 O O   . ILE B 2 51  ? 20.72350  -43.52139 1.20875   1.000 15.21919  ? 51  ILE B O   1 
ATOM   2004 C CB  . ILE B 2 51  ? 23.08598  -45.49170 2.04603   1.000 14.59460  ? 51  ILE B CB  1 
ATOM   2005 C CG1 . ILE B 2 51  ? 24.24824  -44.52965 2.24717   1.000 17.17069  ? 51  ILE B CG1 1 
ATOM   2006 C CG2 . ILE B 2 51  ? 22.84483  -45.66074 0.50065   1.000 16.39545  ? 51  ILE B CG2 1 
ATOM   2007 C CD1 . ILE B 2 51  ? 25.55039  -45.12858 1.81430   1.000 19.86659  ? 51  ILE B CD1 1 
ATOM   2008 N N   . SER B 2 52  ? 21.70860  -42.60171 3.01234   1.000 14.63722  ? 52  SER B N   1 
ATOM   2009 C CA  . SER B 2 52  ? 21.38984  -41.22173 2.66438   1.000 17.88633  ? 52  SER B CA  1 
ATOM   2010 C C   . SER B 2 52  ? 22.48572  -40.32495 3.17509   1.000 21.11489  ? 52  SER B C   1 
ATOM   2011 O O   . SER B 2 52  ? 22.66904  -40.25027 4.38289   1.000 20.05568  ? 52  SER B O   1 
ATOM   2012 C CB  . SER B 2 52  ? 20.08636  -40.75939 3.30829   1.000 21.18823  ? 52  SER B CB  1 
ATOM   2013 O OG  . SER B 2 52  ? 19.71980  -39.51829 2.71882   1.000 24.45933  ? 52  SER B OG  1 
ATOM   2014 N N   . ASP B 2 53  ? 23.17530  -39.61578 2.28952   1.000 30.48505  ? 53  ASP B N   1 
ATOM   2015 C CA  . ASP B 2 53  ? 24.18335  -38.65238 2.73795   1.000 41.69817  ? 53  ASP B CA  1 
ATOM   2016 C C   . ASP B 2 53  ? 25.11392  -39.28220 3.77751   1.000 42.88117  ? 53  ASP B C   1 
ATOM   2017 O O   . ASP B 2 53  ? 25.38394  -38.71600 4.83619   1.000 40.51530  ? 53  ASP B O   1 
ATOM   2018 C CB  . ASP B 2 53  ? 23.50647  -37.39301 3.28434   1.000 48.31599  ? 53  ASP B CB  1 
ATOM   2019 C CG  . ASP B 2 53  ? 24.49308  -36.28455 3.61668   1.000 52.97264  ? 53  ASP B CG  1 
ATOM   2020 O OD1 . ASP B 2 53  ? 25.55664  -36.19703 2.96698   1.000 53.63614  ? 53  ASP B OD1 1 
ATOM   2021 O OD2 . ASP B 2 53  ? 24.19876  -35.50030 4.54283   1.000 53.68929  ? 53  ASP B OD2 1 
ATOM   2022 N N   . GLY B 2 54  ? 25.56221  -40.50309 3.48883   1.000 39.13830  ? 54  GLY B N   1 
ATOM   2023 C CA  . GLY B 2 54  ? 26.50209  -41.19256 4.34257   1.000 37.32266  ? 54  GLY B CA  1 
ATOM   2024 C C   . GLY B 2 54  ? 25.91574  -41.93181 5.53111   1.000 32.69688  ? 54  GLY B C   1 
ATOM   2025 O O   . GLY B 2 54  ? 26.60713  -42.78866 6.10016   1.000 34.59744  ? 54  GLY B O   1 
ATOM   2026 N N   . SER B 2 55  ? 24.68115  -41.63179 5.94858   1.000 23.49394  ? 55  SER B N   1 
ATOM   2027 C CA  . SER B 2 55  ? 24.07777  -42.34897 7.06221   1.000 21.06402  ? 55  SER B CA  1 
ATOM   2028 C C   . SER B 2 55  ? 23.44410  -43.61845 6.54146   1.000 17.62724  ? 55  SER B C   1 
ATOM   2029 O O   . SER B 2 55  ? 22.82725  -43.61852 5.47842   1.000 19.18109  ? 55  SER B O   1 
ATOM   2030 C CB  . SER B 2 55  ? 23.01918  -41.50916 7.77807   1.000 25.33146  ? 55  SER B CB  1 
ATOM   2031 O OG  . SER B 2 55  ? 23.49759  -40.21176 8.09616   1.000 31.05589  ? 55  SER B OG  1 
ATOM   2032 N N   . THR B 2 56  ? 23.56610  -44.69085 7.30956   1.000 16.13188  ? 56  THR B N   1 
ATOM   2033 C CA  . THR B 2 56  ? 23.07258  -45.99218 6.91054   1.000 15.11274  ? 56  THR B CA  1 
ATOM   2034 C C   . THR B 2 56  ? 22.15541  -46.57617 7.98182   1.000 15.52298  ? 56  THR B C   1 
ATOM   2035 O O   . THR B 2 56  ? 22.28111  -46.28515 9.17416   1.000 16.37701  ? 56  THR B O   1 
ATOM   2036 C CB  . THR B 2 56  ? 24.23336  -46.95147 6.65470   1.000 16.07828  ? 56  THR B CB  1 
ATOM   2037 O OG1 . THR B 2 56  ? 24.97676  -47.12792 7.86089   1.000 17.66236  ? 56  THR B OG1 1 
ATOM   2038 C CG2 . THR B 2 56  ? 25.16196  -46.43401 5.53196   1.000 17.23839  ? 56  THR B CG2 1 
ATOM   2039 N N   . ASN B 2 57  ? 21.27989  -47.46885 7.54695   1.000 13.25012  ? 57  ASN B N   1 
ATOM   2040 C CA  . ASN B 2 57  ? 20.47724  -48.25348 8.47013   1.000 12.92270  ? 57  ASN B CA  1 
ATOM   2041 C C   . ASN B 2 57  ? 20.24600  -49.63936 7.88200   1.000 13.10203  ? 57  ASN B C   1 
ATOM   2042 O O   . ASN B 2 57  ? 20.51003  -49.87861 6.68582   1.000 12.90679  ? 57  ASN B O   1 
ATOM   2043 C CB  . ASN B 2 57  ? 19.22488  -47.48989 8.94086   1.000 15.44381  ? 57  ASN B CB  1 
ATOM   2044 C CG  . ASN B 2 57  ? 18.34894  -47.03770 7.78931   1.000 14.73340  ? 57  ASN B CG  1 
ATOM   2045 O OD1 . ASN B 2 57  ? 18.28032  -47.69424 6.73268   1.000 15.37488  ? 57  ASN B OD1 1 
ATOM   2046 N ND2 . ASN B 2 57  ? 17.63344  -45.93385 7.99881   1.000 15.93318  ? 57  ASN B ND2 1 
ATOM   2047 N N   . TYR B 2 58  ? 19.75457  -50.54882 8.73986   1.000 12.85694  ? 58  TYR B N   1 
ATOM   2048 C CA  . TYR B 2 58  ? 19.67947  -51.96069 8.41481   1.000 12.76593  ? 58  TYR B CA  1 
ATOM   2049 C C   . TYR B 2 58  ? 18.46664  -52.58072 9.08176   1.000 13.00214  ? 58  TYR B C   1 
ATOM   2050 O O   . TYR B 2 58  ? 18.11408  -52.22670 10.20833  1.000 14.02616  ? 58  TYR B O   1 
ATOM   2051 C CB  . TYR B 2 58  ? 20.90416  -52.70404 8.94964   1.000 14.53755  ? 58  TYR B CB  1 
ATOM   2052 C CG  . TYR B 2 58  ? 22.18732  -52.26784 8.28097   1.000 13.71936  ? 58  TYR B CG  1 
ATOM   2053 C CD1 . TYR B 2 58  ? 22.57152  -52.83611 7.08833   1.000 13.28517  ? 58  TYR B CD1 1 
ATOM   2054 C CD2 . TYR B 2 58  ? 22.99522  -51.26084 8.82270   1.000 15.20199  ? 58  TYR B CD2 1 
ATOM   2055 C CE1 . TYR B 2 58  ? 23.71336  -52.44619 6.42396   1.000 14.25967  ? 58  TYR B CE1 1 
ATOM   2056 C CE2 . TYR B 2 58  ? 24.16863  -50.84925 8.16393   1.000 15.15515  ? 58  TYR B CE2 1 
ATOM   2057 C CZ  . TYR B 2 58  ? 24.51160  -51.46160 6.96045   1.000 14.81188  ? 58  TYR B CZ  1 
ATOM   2058 O OH  . TYR B 2 58  ? 25.63371  -51.10634 6.26850   1.000 16.07809  ? 58  TYR B OH  1 
ATOM   2059 N N   . ALA B 2 59  ? 17.92300  -53.61247 8.43169   1.000 13.17794  ? 59  ALA B N   1 
ATOM   2060 C CA  . ALA B 2 59  ? 16.99688  -54.51830 9.09514   1.000 13.37477  ? 59  ALA B CA  1 
ATOM   2061 C C   . ALA B 2 59  ? 17.73862  -55.25814 10.20201  1.000 13.44348  ? 59  ALA B C   1 
ATOM   2062 O O   . ALA B 2 59  ? 18.88308  -55.68109 10.03151  1.000 13.88372  ? 59  ALA B O   1 
ATOM   2063 C CB  . ALA B 2 59  ? 16.48708  -55.53293 8.06349   1.000 14.15465  ? 59  ALA B CB  1 
ATOM   2064 N N   . GLY B 2 60  ? 17.07480  -55.44607 11.34749  1.000 14.63933  ? 60  GLY B N   1 
ATOM   2065 C CA  . GLY B 2 60  ? 17.69388  -56.18328 12.43399  1.000 15.92119  ? 60  GLY B CA  1 
ATOM   2066 C C   . GLY B 2 60  ? 18.15242  -57.56826 12.02556  1.000 15.32975  ? 60  GLY B C   1 
ATOM   2067 O O   . GLY B 2 60  ? 19.15845  -58.06553 12.51992  1.000 16.98378  ? 60  GLY B O   1 
ATOM   2068 N N   . SER B 2 61  ? 17.45352  -58.19605 11.08087  1.000 14.51293  ? 61  SER B N   1 
ATOM   2069 C CA  . SER B 2 61  ? 17.82536  -59.55410 10.72332  1.000 17.00604  ? 61  SER B CA  1 
ATOM   2070 C C   . SER B 2 61  ? 19.07246  -59.61466 9.87035   1.000 16.77768  ? 61  SER B C   1 
ATOM   2071 O O   . SER B 2 61  ? 19.58973  -60.73003 9.65515   1.000 16.68656  ? 61  SER B O   1 
ATOM   2072 C CB  . SER B 2 61  ? 16.71562  -60.22020 9.92436   1.000 22.25102  ? 61  SER B CB  1 
ATOM   2073 O OG  . SER B 2 61  ? 16.46350  -59.48178 8.75853   1.000 23.47626  ? 61  SER B OG  1 
ATOM   2074 N N   . VAL B 2 62  ? 19.54135  -58.48402 9.35917   1.000 14.91269  ? 62  VAL B N   1 
ATOM   2075 C CA  . VAL B 2 62  ? 20.73582  -58.50191 8.52253   1.000 29.15939  ? 62  VAL B CA  1 
ATOM   2076 C C   . VAL B 2 62  ? 21.86916  -57.71195 9.15165   1.000 86.71725  ? 62  VAL B C   1 
ATOM   2077 O O   . VAL B 2 62  ? 23.00481  -57.81443 8.68092   1.000 48.06052  ? 62  VAL B O   1 
ATOM   2078 C CB  . VAL B 2 62  ? 20.47166  -57.99060 7.07304   1.000 15.37573  ? 62  VAL B CB  1 
ATOM   2079 C CG1 . VAL B 2 62  ? 19.35629  -58.80614 6.42667   1.000 15.87701  ? 62  VAL B CG1 1 
ATOM   2080 C CG2 . VAL B 2 62  ? 20.32458  -56.48205 7.00263   1.000 14.29654  ? 62  VAL B CG2 1 
ATOM   2081 N N   . LYS B 2 63  ? 21.59790  -56.91769 10.18575  1.000 176.05294 ? 63  LYS B N   1 
ATOM   2082 C CA  . LYS B 2 63  ? 22.64508  -56.15971 10.85289  1.000 189.22431 ? 63  LYS B CA  1 
ATOM   2083 C C   . LYS B 2 63  ? 23.76763  -57.08607 11.28906  1.000 178.81010 ? 63  LYS B C   1 
ATOM   2084 O O   . LYS B 2 63  ? 23.53051  -58.11858 11.91963  1.000 189.97940 ? 63  LYS B O   1 
ATOM   2085 C CB  . LYS B 2 63  ? 22.06474  -55.43806 12.06828  1.000 198.19943 ? 63  LYS B CB  1 
ATOM   2086 C CG  . LYS B 2 63  ? 23.08923  -54.64300 12.85560  1.000 203.30691 ? 63  LYS B CG  1 
ATOM   2087 C CD  . LYS B 2 63  ? 23.52486  -53.38542 12.12689  1.000 206.71696 ? 63  LYS B CD  1 
ATOM   2088 C CE  . LYS B 2 63  ? 24.39347  -52.51857 13.02472  1.000 208.92724 ? 63  LYS B CE  1 
ATOM   2089 N NZ  . LYS B 2 63  ? 24.77425  -51.23535 12.37776  1.000 209.89628 ? 63  LYS B NZ  1 
ATOM   2090 N N   . GLY B 2 64  ? 24.99452  -56.71002 10.94527  1.000 122.69784 ? 64  GLY B N   1 
ATOM   2091 C CA  . GLY B 2 64  ? 26.15783  -57.50640 11.24359  1.000 72.20277  ? 64  GLY B CA  1 
ATOM   2092 C C   . GLY B 2 64  ? 26.59822  -58.43622 10.13195  1.000 35.41625  ? 64  GLY B C   1 
ATOM   2093 O O   . GLY B 2 64  ? 27.74447  -58.89644 10.14629  1.000 29.11432  ? 64  GLY B O   1 
ATOM   2094 N N   . ARG B 2 65  ? 25.72755  -58.71841 9.16777   1.000 19.32385  ? 65  ARG B N   1 
ATOM   2095 C CA  . ARG B 2 65  ? 26.03480  -59.60312 8.05733   1.000 16.95122  ? 65  ARG B CA  1 
ATOM   2096 C C   . ARG B 2 65  ? 26.08269  -58.85369 6.74029   1.000 16.35667  ? 65  ARG B C   1 
ATOM   2097 O O   . ARG B 2 65  ? 26.89382  -59.19497 5.86887   1.000 15.95231  ? 65  ARG B O   1 
ATOM   2098 C CB  . ARG B 2 65  ? 24.96871  -60.70697 7.95549   1.000 16.60719  ? 65  ARG B CB  1 
ATOM   2099 C CG  . ARG B 2 65  ? 24.99224  -61.62131 9.17377   1.000 19.02681  ? 65  ARG B CG  1 
ATOM   2100 C CD  . ARG B 2 65  ? 24.00722  -62.77990 9.04440   1.000 18.06561  ? 65  ARG B CD  1 
ATOM   2101 N NE  . ARG B 2 65  ? 22.64609  -62.39827 8.72000   1.000 17.13780  ? 65  ARG B NE  1 
ATOM   2102 C CZ  . ARG B 2 65  ? 21.99587  -62.69114 7.60123   1.000 16.16975  ? 65  ARG B CZ  1 
ATOM   2103 N NH1 . ARG B 2 65  ? 22.56642  -63.37831 6.61891   1.000 17.29377  ? 65  ARG B NH1 1 
ATOM   2104 N NH2 . ARG B 2 65  ? 20.73402  -62.28306 7.46595   1.000 16.09976  ? 65  ARG B NH2 1 
ATOM   2105 N N   . PHE B 2 66  ? 25.23395  -57.83704 6.56136   1.000 15.29382  ? 66  PHE B N   1 
ATOM   2106 C CA  . PHE B 2 66  ? 25.18582  -57.08229 5.31554   1.000 14.28208  ? 66  PHE B CA  1 
ATOM   2107 C C   . PHE B 2 66  ? 25.71556  -55.67130 5.54674   1.000 16.00611  ? 66  PHE B C   1 
ATOM   2108 O O   . PHE B 2 66  ? 25.49585  -55.06339 6.60037   1.000 18.28909  ? 66  PHE B O   1 
ATOM   2109 C CB  . PHE B 2 66  ? 23.75435  -56.90807 4.77930   1.000 15.85381  ? 66  PHE B CB  1 
ATOM   2110 C CG  . PHE B 2 66  ? 23.03432  -58.16913 4.37616   1.000 14.62350  ? 66  PHE B CG  1 
ATOM   2111 C CD1 . PHE B 2 66  ? 23.57959  -59.45068 4.54801   1.000 15.12952  ? 66  PHE B CD1 1 
ATOM   2112 C CD2 . PHE B 2 66  ? 21.78751  -58.04340 3.75740   1.000 15.07110  ? 66  PHE B CD2 1 
ATOM   2113 C CE1 . PHE B 2 66  ? 22.85945  -60.58913 4.18059   1.000 16.26250  ? 66  PHE B CE1 1 
ATOM   2114 C CE2 . PHE B 2 66  ? 21.07875  -59.15722 3.34238   1.000 16.21184  ? 66  PHE B CE2 1 
ATOM   2115 C CZ  . PHE B 2 66  ? 21.59837  -60.43635 3.53283   1.000 16.40089  ? 66  PHE B CZ  1 
ATOM   2116 N N   . THR B 2 67  ? 26.37096  -55.12029 4.53068   1.000 14.11941  ? 67  THR B N   1 
ATOM   2117 C CA  . THR B 2 67  ? 26.91379  -53.76117 4.59490   1.000 15.72273  ? 67  THR B CA  1 
ATOM   2118 C C   . THR B 2 67  ? 26.53785  -53.02490 3.32269   1.000 14.02935  ? 67  THR B C   1 
ATOM   2119 O O   . THR B 2 67  ? 26.82971  -53.50768 2.22113   1.000 15.12325  ? 67  THR B O   1 
ATOM   2120 C CB  . THR B 2 67  ? 28.44066  -53.78704 4.73048   1.000 17.53206  ? 67  THR B CB  1 
ATOM   2121 O OG1 . THR B 2 67  ? 28.78226  -54.54913 5.89859   1.000 19.64087  ? 67  THR B OG1 1 
ATOM   2122 C CG2 . THR B 2 67  ? 29.00446  -52.35359 4.89893   1.000 19.52913  ? 67  THR B CG2 1 
ATOM   2123 N N   . ILE B 2 68  ? 25.90853  -51.85042 3.47519   1.000 14.07819  ? 68  ILE B N   1 
ATOM   2124 C CA  . ILE B 2 68  ? 25.57275  -50.98724 2.34141   1.000 13.84970  ? 68  ILE B CA  1 
ATOM   2125 C C   . ILE B 2 68  ? 26.69657  -49.94854 2.22434   1.000 14.78792  ? 68  ILE B C   1 
ATOM   2126 O O   . ILE B 2 68  ? 27.24918  -49.50869 3.24268   1.000 16.12946  ? 68  ILE B O   1 
ATOM   2127 C CB  . ILE B 2 68  ? 24.18656  -50.32903 2.53867   1.000 13.84748  ? 68  ILE B CB  1 
ATOM   2128 C CG1 . ILE B 2 68  ? 23.68505  -49.72573 1.21782   1.000 14.43147  ? 68  ILE B CG1 1 
ATOM   2129 C CG2 . ILE B 2 68  ? 24.20246  -49.28786 3.66148   1.000 14.90305  ? 68  ILE B CG2 1 
ATOM   2130 C CD1 . ILE B 2 68  ? 22.24490  -49.27984 1.32351   1.000 14.27083  ? 68  ILE B CD1 1 
ATOM   2131 N N   . SER B 2 69  ? 27.06866  -49.58253 1.00804   1.000 14.63038  ? 69  SER B N   1 
ATOM   2132 C CA  . SER B 2 69  ? 28.11481  -48.59271 0.83224   1.000 16.58985  ? 69  SER B CA  1 
ATOM   2133 C C   . SER B 2 69  ? 27.92807  -47.86383 -0.48713  1.000 17.28483  ? 69  SER B C   1 
ATOM   2134 O O   . SER B 2 69  ? 27.43268  -48.43457 -1.46906  1.000 15.43213  ? 69  SER B O   1 
ATOM   2135 C CB  . SER B 2 69  ? 29.50902  -49.23119 0.90663   1.000 18.56626  ? 69  SER B CB  1 
ATOM   2136 O OG  . SER B 2 69  ? 29.72792  -50.18031 -0.13784  1.000 18.98390  ? 69  SER B OG  1 
ATOM   2137 N N   . GLN B 2 70  ? 28.34959  -46.61106 -0.49182  1.000 20.38803  ? 70  GLN B N   1 
ATOM   2138 C CA  . GLN B 2 70  ? 28.29461  -45.78815 -1.68767  1.000 28.82274  ? 70  GLN B CA  1 
ATOM   2139 C C   . GLN B 2 70  ? 29.68299  -45.77673 -2.33142  1.000 46.11531  ? 70  GLN B C   1 
ATOM   2140 O O   . GLN B 2 70  ? 30.70217  -45.65394 -1.63619  1.000 33.75955  ? 70  GLN B O   1 
ATOM   2141 C CB  . GLN B 2 70  ? 27.92199  -44.37385 -1.25236  1.000 30.96738  ? 70  GLN B CB  1 
ATOM   2142 C CG  . GLN B 2 70  ? 28.24462  -43.27009 -2.20800  1.000 31.39102  ? 70  GLN B CG  1 
ATOM   2143 C CD  . GLN B 2 70  ? 27.27738  -43.38449 -3.35743  1.000 31.51419  ? 70  GLN B CD  1 
ATOM   2144 O OE1 . GLN B 2 70  ? 26.07439  -43.20146 -3.16270  1.000 29.30943  ? 70  GLN B OE1 1 
ATOM   2145 N NE2 . GLN B 2 70  ? 27.78597  -43.63035 -4.56672  1.000 32.61734  ? 70  GLN B NE2 1 
ATOM   2146 N N   A ASP B 2 71  ? 29.73866  -45.99177 -3.64120  0.500 57.04035  ? 71  ASP B N   1 
ATOM   2147 N N   B ASP B 2 71  ? 29.69580  -45.85220 -3.66251  0.500 57.12918  ? 71  ASP B N   1 
ATOM   2148 C CA  A ASP B 2 71  ? 31.03736  -46.04771 -4.30011  0.500 64.60848  ? 71  ASP B CA  1 
ATOM   2149 C CA  B ASP B 2 71  ? 30.84834  -45.62840 -4.54024  0.500 64.76367  ? 71  ASP B CA  1 
ATOM   2150 C C   A ASP B 2 71  ? 31.68035  -44.66796 -4.27830  0.500 68.59332  ? 71  ASP B C   1 
ATOM   2151 C C   B ASP B 2 71  ? 30.46075  -44.50215 -5.49091  0.500 68.83376  ? 71  ASP B C   1 
ATOM   2152 O O   A ASP B 2 71  ? 31.06104  -43.67638 -4.67540  0.500 68.89113  ? 71  ASP B O   1 
ATOM   2153 O O   B ASP B 2 71  ? 30.08406  -44.76055 -6.63612  0.500 69.08672  ? 71  ASP B O   1 
ATOM   2154 C CB  A ASP B 2 71  ? 30.90037  -46.56021 -5.73318  0.500 65.57325  ? 71  ASP B CB  1 
ATOM   2155 C CB  B ASP B 2 71  ? 31.07565  -46.90924 -5.33156  0.500 65.66422  ? 71  ASP B CB  1 
ATOM   2156 C CG  A ASP B 2 71  ? 32.24208  -46.91934 -6.35741  0.500 65.43552  ? 71  ASP B CG  1 
ATOM   2157 C CG  B ASP B 2 71  ? 32.37376  -46.89995 -6.12341  0.500 65.47154  ? 71  ASP B CG  1 
ATOM   2158 O OD1 A ASP B 2 71  ? 33.16759  -46.08136 -6.31638  0.500 65.50399  ? 71  ASP B OD1 1 
ATOM   2159 O OD1 B ASP B 2 71  ? 32.95872  -45.81525 -6.32814  0.500 65.53231  ? 71  ASP B OD1 1 
ATOM   2160 O OD2 A ASP B 2 71  ? 32.37454  -48.04744 -6.87709  0.500 64.56690  ? 71  ASP B OD2 1 
ATOM   2161 O OD2 B ASP B 2 71  ? 32.77953  -47.98419 -6.58870  0.500 64.66777  ? 71  ASP B OD2 1 
ATOM   2162 N N   A ASN B 2 72  ? 32.92667  -44.60507 -3.80366  0.500 70.51422  ? 72  ASN B N   1 
ATOM   2163 N N   B ASN B 2 72  ? 30.54047  -43.25096 -5.03091  0.500 70.45389  ? 72  ASN B N   1 
ATOM   2164 C CA  A ASN B 2 72  ? 33.59218  -43.31900 -3.63918  0.500 71.80836  ? 72  ASN B CA  1 
ATOM   2165 C CA  B ASN B 2 72  ? 29.97098  -42.18643 -5.85260  0.500 71.93637  ? 72  ASN B CA  1 
ATOM   2166 C C   A ASN B 2 72  ? 33.79863  -42.59547 -4.96152  0.500 70.93855  ? 72  ASN B C   1 
ATOM   2167 C C   B ASN B 2 72  ? 30.65797  -42.08963 -7.20756  0.500 71.15067  ? 72  ASN B C   1 
ATOM   2168 O O   A ASN B 2 72  ? 34.05987  -41.38832 -4.95644  0.500 74.62897  ? 72  ASN B O   1 
ATOM   2169 O O   B ASN B 2 72  ? 29.99213  -41.88040 -8.22509  0.500 74.63329  ? 72  ASN B O   1 
ATOM   2170 C CB  A ASN B 2 72  ? 34.92987  -43.49719 -2.91815  0.500 73.92537  ? 72  ASN B CB  1 
ATOM   2171 C CB  B ASN B 2 72  ? 29.93042  -40.83705 -5.14288  0.500 73.84715  ? 72  ASN B CB  1 
ATOM   2172 C CG  A ASN B 2 72  ? 36.01119  -44.05833 -3.82125  0.500 76.27898  ? 72  ASN B CG  1 
ATOM   2173 C CG  B ASN B 2 72  ? 29.07104  -39.83656 -5.89273  0.500 76.19718  ? 72  ASN B CG  1 
ATOM   2174 O OD1 A ASN B 2 72  ? 35.77476  -44.99144 -4.58825  0.500 77.35431  ? 72  ASN B OD1 1 
ATOM   2175 O OD1 B ASN B 2 72  ? 28.13512  -40.21902 -6.59892  0.500 77.15013  ? 72  ASN B OD1 1 
ATOM   2176 N ND2 A ASN B 2 72  ? 37.20795  -43.48684 -3.73607  0.500 77.00035  ? 72  ASN B ND2 1 
ATOM   2177 N ND2 B ASN B 2 72  ? 29.38219  -38.55926 -5.75280  0.500 76.93188  ? 72  ASN B ND2 1 
ATOM   2178 N N   A ALA B 2 73  ? 33.67889  -43.29520 -6.09038  0.500 64.59436  ? 73  ALA B N   1 
ATOM   2179 N N   B ALA B 2 73  ? 31.97720  -42.28788 -7.24988  0.500 64.87118  ? 73  ALA B N   1 
ATOM   2180 C CA  A ALA B 2 73  ? 33.92862  -42.67905 -7.38566  0.500 59.34285  ? 73  ALA B CA  1 
ATOM   2181 C CA  B ALA B 2 73  ? 32.73404  -42.24473 -8.49814  0.500 59.41074  ? 73  ALA B CA  1 
ATOM   2182 C C   A ALA B 2 73  ? 32.88658  -42.99567 -8.44956  0.500 56.98280  ? 73  ALA B C   1 
ATOM   2183 C C   B ALA B 2 73  ? 32.12019  -43.13266 -9.57508  0.500 57.44650  ? 73  ALA B C   1 
ATOM   2184 O O   A ALA B 2 73  ? 33.02953  -42.51836 -9.57878  0.500 56.33356  ? 73  ALA B O   1 
ATOM   2185 O O   B ALA B 2 73  ? 32.49706  -43.04701 -10.74755 0.500 57.01590  ? 73  ALA B O   1 
ATOM   2186 C CB  A ALA B 2 73  ? 35.32501  -43.05633 -7.90718  0.500 57.13695  ? 73  ALA B CB  1 
ATOM   2187 C CB  B ALA B 2 73  ? 34.18960  -42.65056 -8.25525  0.500 57.56592  ? 73  ALA B CB  1 
ATOM   2188 N N   A LYS B 2 74  ? 31.85611  -43.77931 -8.14161  0.500 54.59728  ? 74  LYS B N   1 
ATOM   2189 N N   B LYS B 2 74  ? 31.17089  -43.98667 -9.18841  0.500 54.43306  ? 74  LYS B N   1 
ATOM   2190 C CA  A LYS B 2 74  ? 30.83299  -44.12068 -9.11569  0.500 51.45409  ? 74  LYS B CA  1 
ATOM   2191 C CA  B LYS B 2 74  ? 30.52723  -44.90673 -10.11301 0.500 51.79741  ? 74  LYS B CA  1 
ATOM   2192 C C   A LYS B 2 74  ? 29.44915  -43.87733 -8.53310  0.500 42.71738  ? 74  LYS B C   1 
ATOM   2193 C C   B LYS B 2 74  ? 29.01202  -44.74530 -10.10621 0.500 42.91305  ? 74  LYS B C   1 
ATOM   2194 O O   A LYS B 2 74  ? 29.24839  -43.85639 -7.31519  0.500 45.10479  ? 74  LYS B O   1 
ATOM   2195 O O   B LYS B 2 74  ? 28.31360  -45.56147 -10.72201 0.500 45.82049  ? 74  LYS B O   1 
ATOM   2196 C CB  A LYS B 2 74  ? 30.92043  -45.58308 -9.57512  0.500 55.49732  ? 74  LYS B CB  1 
ATOM   2197 C CB  B LYS B 2 74  ? 30.90484  -46.34532 -9.74809  0.500 55.59225  ? 74  LYS B CB  1 
ATOM   2198 C CG  A LYS B 2 74  ? 32.31120  -46.05388 -9.94941  0.500 58.24265  ? 74  LYS B CG  1 
ATOM   2199 C CG  B LYS B 2 74  ? 32.35103  -46.67921 -10.07539 0.500 58.24867  ? 74  LYS B CG  1 
ATOM   2200 C CD  A LYS B 2 74  ? 32.34900  -47.56879 -10.05497 0.500 59.72447  ? 74  LYS B CD  1 
ATOM   2201 C CD  B LYS B 2 74  ? 32.57771  -48.15615 -10.32318 0.500 59.70905  ? 74  LYS B CD  1 
ATOM   2202 C CE  A LYS B 2 74  ? 33.27203  -48.02673 -11.16560 0.500 60.51273  ? 74  LYS B CE  1 
ATOM   2203 C CE  B LYS B 2 74  ? 33.99004  -48.38869 -10.83545 0.500 60.51383  ? 74  LYS B CE  1 
ATOM   2204 N NZ  A LYS B 2 74  ? 34.21692  -49.06740 -10.67808 0.500 60.82762  ? 74  LYS B NZ  1 
ATOM   2205 N NZ  B LYS B 2 74  ? 34.60931  -49.60200 -10.23542 0.500 60.83064  ? 74  LYS B NZ  1 
ATOM   2206 N N   . ASN B 2 75  ? 28.49611  -43.70305 -9.44414  1.000 25.07640  ? 75  ASN B N   1 
ATOM   2207 C CA  . ASN B 2 75  ? 27.06828  -43.57863 -9.11960  1.000 18.79211  ? 75  ASN B CA  1 
ATOM   2208 C C   . ASN B 2 75  ? 26.44318  -44.93306 -8.80571  1.000 15.60114  ? 75  ASN B C   1 
ATOM   2209 O O   . ASN B 2 75  ? 25.41075  -45.28154 -9.35967  1.000 14.97447  ? 75  ASN B O   1 
ATOM   2210 C CB  . ASN B 2 75  ? 26.32312  -42.93586 -10.29672 1.000 20.79408  ? 75  ASN B CB  1 
ATOM   2211 C CG  . ASN B 2 75  ? 26.77864  -41.54001 -10.55961 1.000 20.39584  ? 75  ASN B CG  1 
ATOM   2212 O OD1 . ASN B 2 75  ? 27.04563  -40.80201 -9.62298  1.000 21.06338  ? 75  ASN B OD1 1 
ATOM   2213 N ND2 . ASN B 2 75  ? 26.86092  -41.14870 -11.81220 1.000 21.50518  ? 75  ASN B ND2 1 
ATOM   2214 N N   . THR B 2 76  ? 27.05422  -45.68424 -7.89217  1.000 15.34391  ? 76  THR B N   1 
ATOM   2215 C CA  . THR B 2 76  ? 26.66300  -47.04635 -7.57304  1.000 14.37815  ? 76  THR B CA  1 
ATOM   2216 C C   . THR B 2 76  ? 26.67990  -47.22723 -6.06440  1.000 14.45101  ? 76  THR B C   1 
ATOM   2217 O O   . THR B 2 76  ? 27.59374  -46.74909 -5.38321  1.000 15.94215  ? 76  THR B O   1 
ATOM   2218 C CB  . THR B 2 76  ? 27.65307  -48.03545 -8.21453  1.000 15.96092  ? 76  THR B CB  1 
ATOM   2219 O OG1 . THR B 2 76  ? 27.56692  -47.89197 -9.63924  1.000 17.78593  ? 76  THR B OG1 1 
ATOM   2220 C CG2 . THR B 2 76  ? 27.31662  -49.48710 -7.88654  1.000 17.12227  ? 76  THR B CG2 1 
ATOM   2221 N N   . VAL B 2 77  ? 25.67952  -47.92455 -5.55340  1.000 13.03936  ? 77  VAL B N   1 
ATOM   2222 C CA  . VAL B 2 77  ? 25.64127  -48.37674 -4.16948  1.000 13.24046  ? 77  VAL B CA  1 
ATOM   2223 C C   . VAL B 2 77  ? 25.71810  -49.89813 -4.14877  1.000 13.03182  ? 77  VAL B C   1 
ATOM   2224 O O   . VAL B 2 77  ? 25.05927  -50.57889 -4.95459  1.000 15.18803  ? 77  VAL B O   1 
ATOM   2225 C CB  . VAL B 2 77  ? 24.36892  -47.86909 -3.46748  1.000 14.36736  ? 77  VAL B CB  1 
ATOM   2226 C CG1 . VAL B 2 77  ? 24.16356  -48.54586 -2.13689  1.000 15.93821  ? 77  VAL B CG1 1 
ATOM   2227 C CG2 . VAL B 2 77  ? 24.40373  -46.34062 -3.30753  1.000 15.99800  ? 77  VAL B CG2 1 
ATOM   2228 N N   . TYR B 2 78  ? 26.50935  -50.42118 -3.22452  1.000 13.29971  ? 78  TYR B N   1 
ATOM   2229 C CA  . TYR B 2 78  ? 26.66035  -51.85061 -3.07171  1.000 13.58452  ? 78  TYR B CA  1 
ATOM   2230 C C   . TYR B 2 78  ? 25.93965  -52.34916 -1.83008  1.000 14.01296  ? 78  TYR B C   1 
ATOM   2231 O O   . TYR B 2 78  ? 25.79943  -51.62755 -0.82899  1.000 14.97584  ? 78  TYR B O   1 
ATOM   2232 C CB  . TYR B 2 78  ? 28.13894  -52.24819 -2.93373  1.000 16.06219  ? 78  TYR B CB  1 
ATOM   2233 C CG  . TYR B 2 78  ? 28.93324  -51.74594 -4.09669  1.000 16.34921  ? 78  TYR B CG  1 
ATOM   2234 C CD1 . TYR B 2 78  ? 28.90281  -52.39887 -5.31523  1.000 16.91166  ? 78  TYR B CD1 1 
ATOM   2235 C CD2 . TYR B 2 78  ? 29.73380  -50.61761 -3.96021  1.000 18.99537  ? 78  TYR B CD2 1 
ATOM   2236 C CE1 . TYR B 2 78  ? 29.60165  -51.90157 -6.39683  1.000 18.86026  ? 78  TYR B CE1 1 
ATOM   2237 C CE2 . TYR B 2 78  ? 30.46075  -50.13193 -5.01026  1.000 21.42557  ? 78  TYR B CE2 1 
ATOM   2238 C CZ  . TYR B 2 78  ? 30.39465  -50.79361 -6.23075  1.000 20.83332  ? 78  TYR B CZ  1 
ATOM   2239 O OH  . TYR B 2 78  ? 31.09241  -50.31780 -7.30466  1.000 24.21485  ? 78  TYR B OH  1 
ATOM   2240 N N   . LEU B 2 79  ? 25.52191  -53.62048 -1.89162  1.000 13.96620  ? 79  LEU B N   1 
ATOM   2241 C CA  . LEU B 2 79  ? 25.08048  -54.34591 -0.70498  1.000 14.02882  ? 79  LEU B CA  1 
ATOM   2242 C C   . LEU B 2 79  ? 25.95414  -55.58764 -0.60165  1.000 13.54045  ? 79  LEU B C   1 
ATOM   2243 O O   . LEU B 2 79  ? 25.76825  -56.54892 -1.36166  1.000 14.27800  ? 79  LEU B O   1 
ATOM   2244 C CB  . LEU B 2 79  ? 23.60774  -54.71931 -0.80165  1.000 13.59745  ? 79  LEU B CB  1 
ATOM   2245 C CG  . LEU B 2 79  ? 23.05138  -55.32819 0.48546   1.000 13.72651  ? 79  LEU B CG  1 
ATOM   2246 C CD1 . LEU B 2 79  ? 22.98871  -54.29173 1.60671   1.000 15.87526  ? 79  LEU B CD1 1 
ATOM   2247 C CD2 . LEU B 2 79  ? 21.68150  -55.94856 0.21186   1.000 15.80260  ? 79  LEU B CD2 1 
ATOM   2248 N N   . GLN B 2 80  ? 26.90942  -55.57211 0.33656   1.000 13.85640  ? 80  GLN B N   1 
ATOM   2249 C CA  . GLN B 2 80  ? 27.73887  -56.74524 0.56746   1.000 14.76159  ? 80  GLN B CA  1 
ATOM   2250 C C   . GLN B 2 80  ? 27.00960  -57.66211 1.53140   1.000 15.75046  ? 80  GLN B C   1 
ATOM   2251 O O   . GLN B 2 80  ? 26.66111  -57.23829 2.63236   1.000 18.75748  ? 80  GLN B O   1 
ATOM   2252 C CB  . GLN B 2 80  ? 29.08687  -56.31541 1.16110   1.000 18.24565  ? 80  GLN B CB  1 
ATOM   2253 C CG  . GLN B 2 80  ? 30.01127  -57.48774 1.49642   1.000 19.19055  ? 80  GLN B CG  1 
ATOM   2254 C CD  . GLN B 2 80  ? 30.47794  -58.19739 0.23756   1.000 19.48640  ? 80  GLN B CD  1 
ATOM   2255 O OE1 . GLN B 2 80  ? 30.82490  -57.55202 -0.74334  1.000 20.47511  ? 80  GLN B OE1 1 
ATOM   2256 N NE2 . GLN B 2 80  ? 30.50415  -59.52618 0.27038   1.000 21.75800  ? 80  GLN B NE2 1 
ATOM   2257 N N   . MET B 2 81  ? 26.75609  -58.90828 1.11225   1.000 15.40894  ? 81  MET B N   1 
ATOM   2258 C CA  . MET B 2 81  ? 25.89796  -59.81297 1.87391   1.000 14.97719  ? 81  MET B CA  1 
ATOM   2259 C C   . MET B 2 81  ? 26.78908  -60.99554 2.29325   1.000 15.90636  ? 81  MET B C   1 
ATOM   2260 O O   . MET B 2 81  ? 27.12648  -61.86665 1.47129   1.000 19.70083  ? 81  MET B O   1 
ATOM   2261 C CB  . MET B 2 81  ? 24.77744  -60.31172 0.98162   1.000 16.90220  ? 81  MET B CB  1 
ATOM   2262 C CG  . MET B 2 81  ? 23.80541  -59.18162 0.59675   1.000 17.65180  ? 81  MET B CG  1 
ATOM   2263 S SD  . MET B 2 81  ? 22.27802  -59.74980 -0.04038  1.000 25.55560  ? 81  MET B SD  1 
ATOM   2264 C CE  . MET B 2 81  ? 22.93295  -60.15773 -1.35065  1.000 18.78392  ? 81  MET B CE  1 
ATOM   2265 N N   . ASN B 2 82  ? 27.14818  -61.03274 3.57438   1.000 16.50216  ? 82  ASN B N   1 
ATOM   2266 C CA  . ASN B 2 82  ? 27.97727  -62.10432 4.10174   1.000 18.19278  ? 82  ASN B CA  1 
ATOM   2267 C C   . ASN B 2 82  ? 27.14922  -63.03203 4.97036   1.000 18.51087  ? 82  ASN B C   1 
ATOM   2268 O O   . ASN B 2 82  ? 26.03042  -62.70681 5.38837   1.000 19.14606  ? 82  ASN B O   1 
ATOM   2269 C CB  . ASN B 2 82  ? 29.14126  -61.54679 4.93257   1.000 19.17412  ? 82  ASN B CB  1 
ATOM   2270 C CG  . ASN B 2 82  ? 30.10630  -60.74090 4.06457   1.000 20.94373  ? 82  ASN B CG  1 
ATOM   2271 O OD1 . ASN B 2 82  ? 30.24634  -61.01922 2.88674   1.000 22.01234  ? 82  ASN B OD1 1 
ATOM   2272 N ND2 . ASN B 2 82  ? 30.80238  -59.78667 4.65655   1.000 24.11007  ? 82  ASN B ND2 1 
ATOM   2273 N N   . SER B 2 83  ? 27.70570  -64.21167 5.22411   1.000 18.13541  ? 83  SER B N   1 
ATOM   2274 C CA  . SER B 2 83  ? 27.07266  -65.16141 6.13374   1.000 20.16476  ? 83  SER B CA  1 
ATOM   2275 C C   . SER B 2 83  ? 25.62939  -65.41360 5.73380   1.000 18.58038  ? 83  SER B C   1 
ATOM   2276 O O   . SER B 2 83  ? 24.70431  -65.39264 6.55935   1.000 18.63473  ? 83  SER B O   1 
ATOM   2277 C CB  . SER B 2 83  ? 27.18309  -64.66644 7.57705   1.000 21.84486  ? 83  SER B CB  1 
ATOM   2278 O OG  . SER B 2 83  ? 28.52908  -64.60795 7.95884   1.000 24.48164  ? 83  SER B OG  1 
ATOM   2279 N N   . LEU B 2 84  ? 25.43763  -65.68124 4.44128   1.000 17.89754  ? 84  LEU B N   1 
ATOM   2280 C CA  . LEU B 2 84  ? 24.07287  -65.79472 3.93134   1.000 18.17212  ? 84  LEU B CA  1 
ATOM   2281 C C   . LEU B 2 84  ? 23.32912  -66.98597 4.53255   1.000 18.33244  ? 84  LEU B C   1 
ATOM   2282 O O   . LEU B 2 84  ? 23.91512  -68.02658 4.83924   1.000 19.96086  ? 84  LEU B O   1 
ATOM   2283 C CB  . LEU B 2 84  ? 24.04920  -65.85496 2.41213   1.000 17.79220  ? 84  LEU B CB  1 
ATOM   2284 C CG  . LEU B 2 84  ? 24.22561  -64.47177 1.77983   1.000 19.87134  ? 84  LEU B CG  1 
ATOM   2285 C CD1 . LEU B 2 84  ? 24.74787  -64.60426 0.36731   1.000 20.47373  ? 84  LEU B CD1 1 
ATOM   2286 C CD2 . LEU B 2 84  ? 22.87099  -63.72197 1.81622   1.000 19.52496  ? 84  LEU B CD2 1 
ATOM   2287 N N   . LYS B 2 85  ? 22.02028  -66.82318 4.69238   1.000 17.63973  ? 85  LYS B N   1 
ATOM   2288 C CA  . LYS B 2 85  ? 21.16692  -67.83516 5.29348   1.000 19.30207  ? 85  LYS B CA  1 
ATOM   2289 C C   . LYS B 2 85  ? 20.02874  -68.14032 4.33572   1.000 18.53079  ? 85  LYS B C   1 
ATOM   2290 O O   . LYS B 2 85  ? 19.65033  -67.28588 3.51868   1.000 18.77994  ? 85  LYS B O   1 
ATOM   2291 C CB  . LYS B 2 85  ? 20.56871  -67.34721 6.62696   1.000 21.39184  ? 85  LYS B CB  1 
ATOM   2292 C CG  . LYS B 2 85  ? 21.57426  -66.82722 7.66877   1.000 24.34710  ? 85  LYS B CG  1 
ATOM   2293 C CD  . LYS B 2 85  ? 20.81803  -66.11954 8.84383   1.000 26.93801  ? 85  LYS B CD  1 
ATOM   2294 C CE  . LYS B 2 85  ? 21.76561  -65.72659 9.98119   1.000 30.27013  ? 85  LYS B CE  1 
ATOM   2295 N NZ  . LYS B 2 85  ? 21.02235  -65.28418 11.20221  1.000 31.97585  ? 85  LYS B NZ  1 
ATOM   2296 N N   . PRO B 2 86  ? 19.39743  -69.31965 4.46910   1.000 19.86751  ? 86  PRO B N   1 
ATOM   2297 C CA  . PRO B 2 86  ? 18.25438  -69.63742 3.59539   1.000 20.19946  ? 86  PRO B CA  1 
ATOM   2298 C C   . PRO B 2 86  ? 17.17997  -68.57436 3.65419   1.000 19.26582  ? 86  PRO B C   1 
ATOM   2299 O O   . PRO B 2 86  ? 16.55622  -68.26707 2.62004   1.000 19.83273  ? 86  PRO B O   1 
ATOM   2300 C CB  . PRO B 2 86  ? 17.77362  -71.00305 4.10191   1.000 22.22428  ? 86  PRO B CB  1 
ATOM   2301 C CG  . PRO B 2 86  ? 19.00686  -71.62758 4.71032   1.000 24.23540  ? 86  PRO B CG  1 
ATOM   2302 C CD  . PRO B 2 86  ? 19.86264  -70.48703 5.24451   1.000 22.93821  ? 86  PRO B CD  1 
ATOM   2303 N N   . GLU B 2 87  ? 16.98581  -67.95722 4.80946   1.000 18.99637  ? 87  GLU B N   1 
ATOM   2304 C CA  . GLU B 2 87  ? 15.94155  -66.95532 4.98505   1.000 21.26659  ? 87  GLU B CA  1 
ATOM   2305 C C   . GLU B 2 87  ? 16.23801  -65.68653 4.20229   1.000 17.94052  ? 87  GLU B C   1 
ATOM   2306 O O   . GLU B 2 87  ? 15.34960  -64.83714 4.07228   1.000 19.19700  ? 87  GLU B O   1 
ATOM   2307 C CB  . GLU B 2 87  ? 15.84435  -66.55467 6.47400   1.000 24.44731  ? 87  GLU B CB  1 
ATOM   2308 C CG  . GLU B 2 87  ? 17.00362  -65.64388 6.98353   1.000 30.18469  ? 87  GLU B CG  1 
ATOM   2309 C CD  . GLU B 2 87  ? 17.00383  -65.39976 8.50979   1.000 34.80612  ? 87  GLU B CD  1 
ATOM   2310 O OE1 . GLU B 2 87  ? 17.15014  -64.22362 8.95866   1.000 33.16073  ? 87  GLU B OE1 1 
ATOM   2311 O OE2 . GLU B 2 87  ? 16.97608  -66.39906 9.25692   1.000 35.78323  ? 87  GLU B OE2 1 
ATOM   2312 N N   . ASP B 2 88  ? 17.45919  -65.54083 3.67876   1.000 16.32079  ? 88  ASP B N   1 
ATOM   2313 C CA  . ASP B 2 88  ? 17.80196  -64.38627 2.85568   1.000 15.28345  ? 88  ASP B CA  1 
ATOM   2314 C C   . ASP B 2 88  ? 17.34880  -64.56000 1.39400   1.000 14.90599  ? 88  ASP B C   1 
ATOM   2315 O O   . ASP B 2 88  ? 17.51974  -63.63601 0.58941   1.000 15.15451  ? 88  ASP B O   1 
ATOM   2316 C CB  . ASP B 2 88  ? 19.30520  -64.16430 2.91278   1.000 15.64952  ? 88  ASP B CB  1 
ATOM   2317 C CG  . ASP B 2 88  ? 19.78498  -63.70540 4.28578   1.000 15.66639  ? 88  ASP B CG  1 
ATOM   2318 O OD1 . ASP B 2 88  ? 19.10355  -62.93619 4.98255   1.000 15.86316  ? 88  ASP B OD1 1 
ATOM   2319 O OD2 . ASP B 2 88  ? 20.84890  -64.20177 4.67895   1.000 17.64589  ? 88  ASP B OD2 1 
ATOM   2320 N N   . THR B 2 89  ? 16.83273  -65.73333 1.01566   1.000 14.64830  ? 89  THR B N   1 
ATOM   2321 C CA  . THR B 2 89  ? 16.37405  -65.97924 -0.34597  1.000 14.66607  ? 89  THR B CA  1 
ATOM   2322 C C   . THR B 2 89  ? 15.21591  -65.05640 -0.70304  1.000 14.37419  ? 89  THR B C   1 
ATOM   2323 O O   . THR B 2 89  ? 14.22968  -64.96734 0.03942   1.000 15.24238  ? 89  THR B O   1 
ATOM   2324 C CB  . THR B 2 89  ? 15.93695  -67.44372 -0.44687  1.000 15.70567  ? 89  THR B CB  1 
ATOM   2325 O OG1 . THR B 2 89  ? 17.09101  -68.28155 -0.23145  1.000 16.51971  ? 89  THR B OG1 1 
ATOM   2326 C CG2 . THR B 2 89  ? 15.30539  -67.72832 -1.81617  1.000 16.29115  ? 89  THR B CG2 1 
ATOM   2327 N N   . ALA B 2 90  ? 15.34438  -64.37435 -1.83610  1.000 13.84229  ? 90  ALA B N   1 
ATOM   2328 C CA  . ALA B 2 90  ? 14.33879  -63.37777 -2.22649  1.000 13.46303  ? 90  ALA B CA  1 
ATOM   2329 C C   . ALA B 2 90  ? 14.84138  -62.73207 -3.51131  1.000 12.71848  ? 90  ALA B C   1 
ATOM   2330 O O   . ALA B 2 90  ? 16.01040  -62.89604 -3.89400  1.000 13.70520  ? 90  ALA B O   1 
ATOM   2331 C CB  . ALA B 2 90  ? 14.16337  -62.30104 -1.15241  1.000 14.36039  ? 90  ALA B CB  1 
ATOM   2332 N N   . VAL B 2 91  ? 13.95478  -61.92811 -4.14879  1.000 12.20660  ? 91  VAL B N   1 
ATOM   2333 C CA  . VAL B 2 91  ? 14.38648  -60.99409 -5.18034  1.000 12.21278  ? 91  VAL B CA  1 
ATOM   2334 C C   . VAL B 2 91  ? 14.73538  -59.68504 -4.48978  1.000 12.32011  ? 91  VAL B C   1 
ATOM   2335 O O   . VAL B 2 91  ? 13.92341  -59.15485 -3.72595  1.000 12.74690  ? 91  VAL B O   1 
ATOM   2336 C CB  . VAL B 2 91  ? 13.29778  -60.78534 -6.25326  1.000 12.75140  ? 91  VAL B CB  1 
ATOM   2337 C CG1 . VAL B 2 91  ? 13.79778  -59.80282 -7.32665  1.000 13.18087  ? 91  VAL B CG1 1 
ATOM   2338 C CG2 . VAL B 2 91  ? 12.89239  -62.12259 -6.89499  1.000 15.18810  ? 91  VAL B CG2 1 
ATOM   2339 N N   . TYR B 2 92  ? 15.94116  -59.18328 -4.73182  1.000 11.71106  ? 92  TYR B N   1 
ATOM   2340 C CA  . TYR B 2 92  ? 16.39121  -57.94886 -4.09230  1.000 11.38762  ? 92  TYR B CA  1 
ATOM   2341 C C   . TYR B 2 92  ? 16.20010  -56.80809 -5.08524  1.000 11.51357  ? 92  TYR B C   1 
ATOM   2342 O O   . TYR B 2 92  ? 16.60344  -56.90446 -6.26958  1.000 12.27095  ? 92  TYR B O   1 
ATOM   2343 C CB  . TYR B 2 92  ? 17.87852  -58.05625 -3.69226  1.000 11.93393  ? 92  TYR B CB  1 
ATOM   2344 C CG  . TYR B 2 92  ? 18.05122  -58.89465 -2.46140  1.000 12.31983  ? 92  TYR B CG  1 
ATOM   2345 C CD1 . TYR B 2 92  ? 17.78023  -60.26748 -2.47035  1.000 12.56143  ? 92  TYR B CD1 1 
ATOM   2346 C CD2 . TYR B 2 92  ? 18.45874  -58.33203 -1.26338  1.000 12.20896  ? 92  TYR B CD2 1 
ATOM   2347 C CE1 . TYR B 2 92  ? 17.88534  -61.03815 -1.31509  1.000 13.29900  ? 92  TYR B CE1 1 
ATOM   2348 C CE2 . TYR B 2 92  ? 18.58170  -59.08671 -0.10039  1.000 13.27305  ? 92  TYR B CE2 1 
ATOM   2349 C CZ  . TYR B 2 92  ? 18.31414  -60.44755 -0.13329  1.000 13.33388  ? 92  TYR B CZ  1 
ATOM   2350 O OH  . TYR B 2 92  ? 18.41267  -61.20018 1.02791   1.000 13.97755  ? 92  TYR B OH  1 
ATOM   2351 N N   . TYR B 2 93  ? 15.63191  -55.71834 -4.58810  1.000 11.26665  ? 93  TYR B N   1 
ATOM   2352 C CA  . TYR B 2 93  ? 15.34590  -54.52669 -5.38636  1.000 11.83841  ? 93  TYR B CA  1 
ATOM   2353 C C   . TYR B 2 93  ? 16.03378  -53.31987 -4.76672  1.000 11.93038  ? 93  TYR B C   1 
ATOM   2354 O O   . TYR B 2 93  ? 16.03406  -53.16384 -3.54625  1.000 14.19946  ? 93  TYR B O   1 
ATOM   2355 C CB  . TYR B 2 93  ? 13.85896  -54.21035 -5.43375  1.000 13.13099  ? 93  TYR B CB  1 
ATOM   2356 C CG  . TYR B 2 93  ? 13.06016  -55.26715 -6.12469  1.000 13.30293  ? 93  TYR B CG  1 
ATOM   2357 C CD1 . TYR B 2 93  ? 12.95034  -55.25947 -7.51486  1.000 14.66995  ? 93  TYR B CD1 1 
ATOM   2358 C CD2 . TYR B 2 93  ? 12.38064  -56.26030 -5.42937  1.000 14.90839  ? 93  TYR B CD2 1 
ATOM   2359 C CE1 . TYR B 2 93  ? 12.20043  -56.21702 -8.18258  1.000 16.69680  ? 93  TYR B CE1 1 
ATOM   2360 C CE2 . TYR B 2 93  ? 11.61763  -57.21052 -6.09461  1.000 17.94548  ? 93  TYR B CE2 1 
ATOM   2361 C CZ  . TYR B 2 93  ? 11.56154  -57.20219 -7.48020  1.000 17.38053  ? 93  TYR B CZ  1 
ATOM   2362 O OH  . TYR B 2 93  ? 10.82398  -58.13722 -8.16159  1.000 21.87139  ? 93  TYR B OH  1 
ATOM   2363 N N   . CYS B 2 94  ? 16.61241  -52.45436 -5.57772  1.000 12.48774  ? 94  CYS B N   1 
ATOM   2364 C CA  . CYS B 2 94  ? 16.96515  -51.14020 -5.08293  1.000 12.23017  ? 94  CYS B CA  1 
ATOM   2365 C C   . CYS B 2 94  ? 15.95225  -50.12316 -5.57572  1.000 11.27538  ? 94  CYS B C   1 
ATOM   2366 O O   . CYS B 2 94  ? 15.41703  -50.23365 -6.68319  1.000 12.89658  ? 94  CYS B O   1 
ATOM   2367 C CB  . CYS B 2 94  ? 18.37888  -50.73127 -5.45709  1.000 14.79257  ? 94  CYS B CB  1 
ATOM   2368 S SG  . CYS B 2 94  ? 18.73084  -50.65536 -7.21099  1.000 15.24930  ? 94  CYS B SG  1 
ATOM   2369 N N   . ALA B 2 95  ? 15.73727  -49.10891 -4.75497  1.000 12.11216  ? 95  ALA B N   1 
ATOM   2370 C CA  . ALA B 2 95  ? 14.89791  -47.97442 -5.09033  1.000 12.47098  ? 95  ALA B CA  1 
ATOM   2371 C C   . ALA B 2 95  ? 15.64018  -46.73351 -4.65447  1.000 11.69052  ? 95  ALA B C   1 
ATOM   2372 O O   . ALA B 2 95  ? 16.19632  -46.70478 -3.56257  1.000 14.09454  ? 95  ALA B O   1 
ATOM   2373 C CB  . ALA B 2 95  ? 13.51619  -48.03399 -4.39931  1.000 14.77285  ? 95  ALA B CB  1 
ATOM   2374 N N   . ALA B 2 96  ? 15.62034  -45.68904 -5.46186  1.000 11.46391  ? 96  ALA B N   1 
ATOM   2375 C CA  . ALA B 2 96  ? 16.34065  -44.47963 -5.10690  1.000 12.85824  ? 96  ALA B CA  1 
ATOM   2376 C C   . ALA B 2 96  ? 15.49502  -43.27270 -5.45696  1.000 12.29133  ? 96  ALA B C   1 
ATOM   2377 O O   . ALA B 2 96  ? 14.71022  -43.30857 -6.40581  1.000 14.47190  ? 96  ALA B O   1 
ATOM   2378 C CB  . ALA B 2 96  ? 17.67592  -44.38874 -5.82229  1.000 15.14583  ? 96  ALA B CB  1 
ATOM   2379 N N   . THR B 2 97  ? 15.68382  -42.19105 -4.70573  1.000 13.00949  ? 97  THR B N   1 
ATOM   2380 C CA  . THR B 2 97  ? 15.12015  -40.91118 -5.09236  1.000 12.26788  ? 97  THR B CA  1 
ATOM   2381 C C   . THR B 2 97  ? 16.26866  -40.04741 -5.58279  1.000 12.56711  ? 97  THR B C   1 
ATOM   2382 O O   . THR B 2 97  ? 17.25805  -39.85145 -4.85383  1.000 14.05370  ? 97  THR B O   1 
ATOM   2383 C CB  . THR B 2 97  ? 14.31518  -40.28405 -3.94576  1.000 14.00545  ? 97  THR B CB  1 
ATOM   2384 O OG1 . THR B 2 97  ? 15.10219  -40.29807 -2.74809  1.000 15.71940  ? 97  THR B OG1 1 
ATOM   2385 C CG2 . THR B 2 97  ? 12.99383  -41.02541 -3.78716  1.000 16.91642  ? 97  THR B CG2 1 
ATOM   2386 N N   . ILE B 2 98  ? 16.17523  -39.60591 -6.84254  1.000 12.64325  ? 98  ILE B N   1 
ATOM   2387 C CA  . ILE B 2 98  ? 17.27871  -38.96727 -7.55578  1.000 13.06709  ? 98  ILE B CA  1 
ATOM   2388 C C   . ILE B 2 98  ? 16.69292  -37.81732 -8.36950  1.000 12.73510  ? 98  ILE B C   1 
ATOM   2389 O O   . ILE B 2 98  ? 15.65413  -37.99743 -9.01846  1.000 13.36606  ? 98  ILE B O   1 
ATOM   2390 C CB  . ILE B 2 98  ? 17.96525  -39.95348 -8.52832  1.000 14.74239  ? 98  ILE B CB  1 
ATOM   2391 C CG1 . ILE B 2 98  ? 18.46776  -41.22600 -7.80415  1.000 15.49845  ? 98  ILE B CG1 1 
ATOM   2392 C CG2 . ILE B 2 98  ? 19.15293  -39.27324 -9.22957  1.000 17.60357  ? 98  ILE B CG2 1 
ATOM   2393 C CD1 . ILE B 2 98  ? 18.94507  -42.32887 -8.74899  1.000 17.36465  ? 98  ILE B CD1 1 
ATOM   2394 N N   . SER B 2 99  ? 17.32110  -36.63095 -8.33162  1.000 13.58630  ? 99  SER B N   1 
ATOM   2395 C CA  . SER B 2 99  ? 16.86278  -35.54929 -9.18527  1.000 14.21922  ? 99  SER B CA  1 
ATOM   2396 C C   . SER B 2 99  ? 17.54033  -35.71533 -10.55381 1.000 15.96013  ? 99  SER B C   1 
ATOM   2397 O O   . SER B 2 99  ? 18.55463  -36.39256 -10.69962 1.000 20.89140  ? 99  SER B O   1 
ATOM   2398 C CB  . SER B 2 99  ? 17.19775  -34.19039 -8.57704  1.000 15.57957  ? 99  SER B CB  1 
ATOM   2399 O OG  . SER B 2 99  ? 18.56518  -34.11505 -8.30138  1.000 18.13486  ? 99  SER B OG  1 
ATOM   2400 N N   . ARG B 2 100 ? 16.90925  -35.21286 -11.59104 1.000 18.57715  ? 100 ARG B N   1 
ATOM   2401 C CA  . ARG B 2 100 ? 17.50837  -35.28096 -12.91500 1.000 19.03690  ? 100 ARG B CA  1 
ATOM   2402 C C   . ARG B 2 100 ? 17.98224  -33.89558 -13.31968 1.000 17.86328  ? 100 ARG B C   1 
ATOM   2403 O O   . ARG B 2 100 ? 17.55013  -32.87368 -12.75999 1.000 17.28115  ? 100 ARG B O   1 
ATOM   2404 C CB  . ARG B 2 100 ? 16.50555  -35.80095 -13.93259 1.000 22.61156  ? 100 ARG B CB  1 
ATOM   2405 C CG  . ARG B 2 100 ? 15.24188  -35.04545 -14.00591 1.000 26.85344  ? 100 ARG B CG  1 
ATOM   2406 C CD  . ARG B 2 100 ? 14.33288  -35.75575 -15.01228 1.000 30.24300  ? 100 ARG B CD  1 
ATOM   2407 N NE  . ARG B 2 100 ? 15.00578  -36.05077 -16.27846 1.000 33.36855  ? 100 ARG B NE  1 
ATOM   2408 C CZ  . ARG B 2 100 ? 14.43443  -36.68867 -17.29797 1.000 35.89714  ? 100 ARG B CZ  1 
ATOM   2409 N NH1 . ARG B 2 100 ? 13.20544  -37.17583 -17.20842 1.000 37.31517  ? 100 ARG B NH1 1 
ATOM   2410 N NH2 . ARG B 2 100 ? 15.11377  -36.84425 -18.43222 1.000 35.31596  ? 100 ARG B NH2 1 
ATOM   2411 N N   . THR B 2 101 ? 18.86717  -33.87930 -14.30700 1.000 19.01514  ? 101 THR B N   1 
ATOM   2412 C CA  . THR B 2 101 ? 19.39045  -32.63207 -14.81722 1.000 19.51735  ? 101 THR B CA  1 
ATOM   2413 C C   . THR B 2 101 ? 18.22436  -31.67757 -15.08425 1.000 18.50156  ? 101 THR B C   1 
ATOM   2414 O O   . THR B 2 101 ? 17.22380  -32.04308 -15.72420 1.000 20.52953  ? 101 THR B O   1 
ATOM   2415 C CB  . THR B 2 101 ? 20.13535  -32.94520 -16.11473 1.000 20.98645  ? 101 THR B CB  1 
ATOM   2416 O OG1 . THR B 2 101 ? 21.09467  -33.97619 -15.82036 1.000 22.88028  ? 101 THR B OG1 1 
ATOM   2417 C CG2 . THR B 2 101 ? 20.86047  -31.71124 -16.59211 1.000 23.53312  ? 101 THR B CG2 1 
ATOM   2418 N N   . GLY B 2 102 ? 18.38056  -30.44268 -14.61488 1.000 19.64155  ? 102 GLY B N   1 
ATOM   2419 C CA  . GLY B 2 102 ? 17.39163  -29.40580 -14.76888 1.000 19.55846  ? 102 GLY B CA  1 
ATOM   2420 C C   . GLY B 2 102 ? 16.38705  -29.29156 -13.64718 1.000 20.26185  ? 102 GLY B C   1 
ATOM   2421 O O   . GLY B 2 102 ? 15.61703  -28.32821 -13.61687 1.000 23.69530  ? 102 GLY B O   1 
ATOM   2422 N N   . SER B 2 103 ? 16.38371  -30.21662 -12.69498 1.000 17.46013  ? 103 SER B N   1 
ATOM   2423 C CA  . SER B 2 103 ? 15.35380  -30.27489 -11.67150 1.000 16.75567  ? 103 SER B CA  1 
ATOM   2424 C C   . SER B 2 103 ? 15.96867  -30.34713 -10.28653 1.000 14.94608  ? 103 SER B C   1 
ATOM   2425 O O   . SER B 2 103 ? 17.04253  -30.93704 -10.08918 1.000 15.61767  ? 103 SER B O   1 
ATOM   2426 C CB  . SER B 2 103 ? 14.48232  -31.53510 -11.89067 1.000 18.00940  ? 103 SER B CB  1 
ATOM   2427 O OG  . SER B 2 103 ? 13.51405  -31.66719 -10.86082 1.000 19.36210  ? 103 SER B OG  1 
ATOM   2428 N N   . LEU B 2 104 ? 15.23961  -29.79910 -9.32371  1.000 15.33551  ? 104 LEU B N   1 
ATOM   2429 C CA  . LEU B 2 104 ? 15.58581  -29.96473 -7.91890  1.000 17.63720  ? 104 LEU B CA  1 
ATOM   2430 C C   . LEU B 2 104 ? 14.73509  -30.99524 -7.20978  1.000 16.21082  ? 104 LEU B C   1 
ATOM   2431 O O   . LEU B 2 104 ? 14.78712  -31.06439 -5.97809  1.000 19.62175  ? 104 LEU B O   1 
ATOM   2432 C CB  . LEU B 2 104 ? 15.53003  -28.64994 -7.13088  1.000 22.94167  ? 104 LEU B CB  1 
ATOM   2433 C CG  . LEU B 2 104 ? 16.51303  -27.57034 -7.61762  1.000 22.37819  ? 104 LEU B CG  1 
ATOM   2434 C CD1 . LEU B 2 104 ? 15.75437  -26.36998 -8.08317  1.000 23.57115  ? 104 LEU B CD1 1 
ATOM   2435 C CD2 . LEU B 2 104 ? 17.54986  -27.23474 -6.54763  1.000 21.64666  ? 104 LEU B CD2 1 
ATOM   2436 N N   . TRP B 2 105 ? 13.96511  -31.78359 -7.93605  1.000 14.96678  ? 105 TRP B N   1 
ATOM   2437 C CA  . TRP B 2 105 ? 13.05658  -32.73340 -7.29682  1.000 15.41153  ? 105 TRP B CA  1 
ATOM   2438 C C   . TRP B 2 105 ? 13.64368  -34.13690 -7.39396  1.000 14.85992  ? 105 TRP B C   1 
ATOM   2439 O O   . TRP B 2 105 ? 13.86674  -34.65363 -8.50130  1.000 17.27174  ? 105 TRP B O   1 
ATOM   2440 C CB  . TRP B 2 105 ? 11.74628  -32.69770 -8.06362  1.000 17.71042  ? 105 TRP B CB  1 
ATOM   2441 C CG  . TRP B 2 105 ? 10.89146  -31.63692 -7.56414  1.000 19.23527  ? 105 TRP B CG  1 
ATOM   2442 C CD1 . TRP B 2 105 ? 11.13739  -30.29305 -7.68518  1.000 20.31796  ? 105 TRP B CD1 1 
ATOM   2443 C CD2 . TRP B 2 105 ? 9.59768   -31.77630 -6.92980  1.000 18.01192  ? 105 TRP B CD2 1 
ATOM   2444 N NE1 . TRP B 2 105 ? 10.08238  -29.58816 -7.14073  1.000 21.19337  ? 105 TRP B NE1 1 
ATOM   2445 C CE2 . TRP B 2 105 ? 9.13579   -30.47681 -6.67365  1.000 18.09425  ? 105 TRP B CE2 1 
ATOM   2446 C CE3 . TRP B 2 105 ? 8.78697   -32.87103 -6.56789  1.000 18.09742  ? 105 TRP B CE3 1 
ATOM   2447 C CZ2 . TRP B 2 105 ? 7.92833   -30.22829 -6.07770  1.000 19.06940  ? 105 TRP B CZ2 1 
ATOM   2448 C CZ3 . TRP B 2 105 ? 7.54024   -32.62127 -5.94695  1.000 17.49256  ? 105 TRP B CZ3 1 
ATOM   2449 C CH2 . TRP B 2 105 ? 7.13830   -31.30270 -5.69502  1.000 18.50988  ? 105 TRP B CH2 1 
ATOM   2450 N N   . CYS B 2 106 ? 13.87733  -34.76830 -6.25820  1.000 14.06495  ? 106 CYS B N   1 
ATOM   2451 C CA  . CYS B 2 106 ? 14.29391  -36.16108 -6.26829  1.000 13.89122  ? 106 CYS B CA  1 
ATOM   2452 C C   . CYS B 2 106 ? 13.08786  -37.04768 -6.52727  1.000 13.79832  ? 106 CYS B C   1 
ATOM   2453 O O   . CYS B 2 106 ? 12.12506  -37.02446 -5.75837  1.000 15.56052  ? 106 CYS B O   1 
ATOM   2454 C CB  . CYS B 2 106 ? 14.91240  -36.51812 -4.92981  1.000 15.04082  ? 106 CYS B CB  1 
ATOM   2455 S SG  . CYS B 2 106 ? 16.65503  -36.09618 -4.80468  1.000 17.11874  ? 106 CYS B SG  1 
ATOM   2456 N N   . GLU B 2 107 ? 13.13069  -37.81488 -7.61317  1.000 13.91306  ? 107 GLU B N   1 
ATOM   2457 C CA  A GLU B 2 107 ? 12.03525  -38.66606 -8.06152  0.500 13.85646  ? 107 GLU B CA  1 
ATOM   2458 C CA  B GLU B 2 107 ? 12.00925  -38.66322 -7.97932  0.500 13.23245  ? 107 GLU B CA  1 
ATOM   2459 C C   . GLU B 2 107 ? 12.41139  -40.11713 -7.81997  1.000 12.41062  ? 107 GLU B C   1 
ATOM   2460 O O   . GLU B 2 107 ? 13.59243  -40.46108 -7.80251  1.000 12.34570  ? 107 GLU B O   1 
ATOM   2461 C CB  A GLU B 2 107 ? 11.87268  -38.49595 -9.56982  0.500 16.56109  ? 107 GLU B CB  1 
ATOM   2462 C CB  B GLU B 2 107 ? 11.63196  -38.37231 -9.42595  0.500 14.52211  ? 107 GLU B CB  1 
ATOM   2463 C CG  A GLU B 2 107 ? 11.26553  -37.16523 -9.98128  0.500 22.57163  ? 107 GLU B CG  1 
ATOM   2464 C CG  B GLU B 2 107 ? 11.09729  -36.96177 -9.58128  0.500 19.52800  ? 107 GLU B CG  1 
ATOM   2465 C CD  A GLU B 2 107 ? 10.87082  -37.14271 -11.45624 0.500 28.32571  ? 107 GLU B CD  1 
ATOM   2466 C CD  B GLU B 2 107 ? 10.82967  -36.58893 -11.02781 0.500 27.01894  ? 107 GLU B CD  1 
ATOM   2467 O OE1 A GLU B 2 107 ? 9.86746   -37.79484 -11.83919 0.500 30.43261  ? 107 GLU B OE1 1 
ATOM   2468 O OE1 B GLU B 2 107 ? 10.87739  -37.48367 -11.90653 0.500 31.01284  ? 107 GLU B OE1 1 
ATOM   2469 O OE2 A GLU B 2 107 ? 11.59901  -36.50569 -12.24880 0.500 31.86199  ? 107 GLU B OE2 1 
ATOM   2470 O OE2 B GLU B 2 107 ? 10.57213  -35.39125 -11.28442 0.500 28.53476  ? 107 GLU B OE2 1 
ATOM   2471 N N   . GLU B 2 108 ? 11.39919  -40.96551 -7.66402  1.000 13.80995  ? 108 GLU B N   1 
ATOM   2472 C CA  . GLU B 2 108 ? 11.63327  -42.35697 -7.32391  1.000 13.43626  ? 108 GLU B CA  1 
ATOM   2473 C C   . GLU B 2 108 ? 11.90492  -43.18357 -8.58322  1.000 13.09331  ? 108 GLU B C   1 
ATOM   2474 O O   . GLU B 2 108 ? 11.18700  -43.09450 -9.59751  1.000 15.38866  ? 108 GLU B O   1 
ATOM   2475 C CB  . GLU B 2 108 ? 10.36262  -42.85989 -6.61617  1.000 18.62013  ? 108 GLU B CB  1 
ATOM   2476 C CG  . GLU B 2 108 ? 10.18293  -44.30259 -6.56462  1.000 18.25909  ? 108 GLU B CG  1 
ATOM   2477 C CD  . GLU B 2 108 ? 8.77783   -44.66547 -6.16022  1.000 18.32110  ? 108 GLU B CD  1 
ATOM   2478 O OE1 . GLU B 2 108 ? 7.82874   -44.28862 -6.91075  1.000 19.13499  ? 108 GLU B OE1 1 
ATOM   2479 O OE2 . GLU B 2 108 ? 8.66077   -45.36024 -5.14093  1.000 17.93900  ? 108 GLU B OE2 1 
ATOM   2480 N N   . TYR B 2 109 ? 12.91703  -44.03591 -8.49726  1.000 12.11687  ? 109 TYR B N   1 
ATOM   2481 C CA  . TYR B 2 109 ? 13.26683  -44.98728 -9.53790  1.000 12.15725  ? 109 TYR B CA  1 
ATOM   2482 C C   . TYR B 2 109 ? 13.50583  -46.34333 -8.88990  1.000 12.11649  ? 109 TYR B C   1 
ATOM   2483 O O   . TYR B 2 109 ? 13.93684  -46.41656 -7.72914  1.000 12.95654  ? 109 TYR B O   1 
ATOM   2484 C CB  . TYR B 2 109 ? 14.55764  -44.56047 -10.28038 1.000 13.20411  ? 109 TYR B CB  1 
ATOM   2485 C CG  . TYR B 2 109 ? 14.39098  -43.22646 -10.93344 1.000 13.77473  ? 109 TYR B CG  1 
ATOM   2486 C CD1 . TYR B 2 109 ? 13.80766  -43.14052 -12.20872 1.000 17.02264  ? 109 TYR B CD1 1 
ATOM   2487 C CD2 . TYR B 2 109 ? 14.79316  -42.04222 -10.30988 1.000 12.83054  ? 109 TYR B CD2 1 
ATOM   2488 C CE1 . TYR B 2 109 ? 13.60965  -41.93827 -12.83481 1.000 18.68543  ? 109 TYR B CE1 1 
ATOM   2489 C CE2 . TYR B 2 109 ? 14.58901  -40.81195 -10.93184 1.000 15.64346  ? 109 TYR B CE2 1 
ATOM   2490 C CZ  . TYR B 2 109 ? 13.99564  -40.76562 -12.19446 1.000 17.35373  ? 109 TYR B CZ  1 
ATOM   2491 O OH  . TYR B 2 109 ? 13.75851  -39.56006 -12.83937 1.000 19.43268  ? 109 TYR B OH  1 
ATOM   2492 N N   . TRP B 2 110 ? 13.26380  -47.41133 -9.64981  1.000 12.31714  ? 110 TRP B N   1 
ATOM   2493 C CA  . TRP B 2 110 ? 13.42928  -48.77399 -9.16327  1.000 12.51702  ? 110 TRP B CA  1 
ATOM   2494 C C   . TRP B 2 110 ? 14.34799  -49.54457 -10.09312 1.000 11.99065  ? 110 TRP B C   1 
ATOM   2495 O O   . TRP B 2 110 ? 14.24634  -49.43056 -11.31490 1.000 12.38986  ? 110 TRP B O   1 
ATOM   2496 C CB  . TRP B 2 110 ? 12.06653  -49.49945 -9.14105  1.000 12.58569  ? 110 TRP B CB  1 
ATOM   2497 C CG  . TRP B 2 110 ? 11.19484  -49.05074 -8.01046  1.000 12.61145  ? 110 TRP B CG  1 
ATOM   2498 C CD1 . TRP B 2 110 ? 10.37182  -47.94632 -7.94082  1.000 13.99654  ? 110 TRP B CD1 1 
ATOM   2499 C CD2 . TRP B 2 110 ? 11.13007  -49.66887 -6.72966  1.000 11.96868  ? 110 TRP B CD2 1 
ATOM   2500 N NE1 . TRP B 2 110 ? 9.80321   -47.86164 -6.70500  1.000 14.32531  ? 110 TRP B NE1 1 
ATOM   2501 C CE2 . TRP B 2 110 ? 10.24430  -48.90473 -5.93831  1.000 13.21801  ? 110 TRP B CE2 1 
ATOM   2502 C CE3 . TRP B 2 110 ? 11.73533  -50.79636 -6.17969  1.000 12.72617  ? 110 TRP B CE3 1 
ATOM   2503 C CZ2 . TRP B 2 110 ? 9.91681   -49.25210 -4.63091  1.000 13.82025  ? 110 TRP B CZ2 1 
ATOM   2504 C CZ3 . TRP B 2 110 ? 11.41523  -51.14957 -4.88168  1.000 13.65415  ? 110 TRP B CZ3 1 
ATOM   2505 C CH2 . TRP B 2 110 ? 10.50807  -50.37536 -4.11316  1.000 13.99883  ? 110 TRP B CH2 1 
ATOM   2506 N N   . GLY B 2 111 ? 15.20559  -50.39677 -9.49979  1.000 11.64812  ? 111 GLY B N   1 
ATOM   2507 C CA  . GLY B 2 111 ? 15.92528  -51.39096 -10.25333 1.000 12.29152  ? 111 GLY B CA  1 
ATOM   2508 C C   . GLY B 2 111 ? 15.01495  -52.51007 -10.70452 1.000 11.79757  ? 111 GLY B C   1 
ATOM   2509 O O   . GLY B 2 111 ? 13.83828  -52.61002 -10.33291 1.000 13.09599  ? 111 GLY B O   1 
ATOM   2510 N N   . GLN B 2 112 ? 15.59524  -53.39867 -11.50998 1.000 11.85027  ? 112 GLN B N   1 
ATOM   2511 C CA  . GLN B 2 112 ? 14.84697  -54.46701 -12.15536 1.000 12.18541  ? 112 GLN B CA  1 
ATOM   2512 C C   . GLN B 2 112 ? 14.76387  -55.73210 -11.30969 1.000 12.46232  ? 112 GLN B C   1 
ATOM   2513 O O   . GLN B 2 112 ? 14.11738  -56.68768 -11.74551 1.000 13.33532  ? 112 GLN B O   1 
ATOM   2514 C CB  . GLN B 2 112 ? 15.46234  -54.76196 -13.52799 1.000 13.07623  ? 112 GLN B CB  1 
ATOM   2515 C CG  . GLN B 2 112 ? 16.67110  -55.69172 -13.57932 1.000 12.73091  ? 112 GLN B CG  1 
ATOM   2516 C CD  . GLN B 2 112 ? 18.00821  -55.07511 -13.18385 1.000 11.92132  ? 112 GLN B CD  1 
ATOM   2517 O OE1 . GLN B 2 112 ? 18.07343  -53.98606 -12.58969 1.000 12.72128  ? 112 GLN B OE1 1 
ATOM   2518 N NE2 . GLN B 2 112 ? 19.09322  -55.74870 -13.54493 1.000 12.85388  ? 112 GLN B NE2 1 
ATOM   2519 N N   . GLY B 2 113 ? 15.42312  -55.77040 -10.15055 1.000 12.21237  ? 113 GLY B N   1 
ATOM   2520 C CA  . GLY B 2 113 ? 15.43888  -56.94990 -9.30099  1.000 12.62355  ? 113 GLY B CA  1 
ATOM   2521 C C   . GLY B 2 113 ? 16.56777  -57.89540 -9.64567  1.000 12.08315  ? 113 GLY B C   1 
ATOM   2522 O O   . GLY B 2 113 ? 16.98169  -58.00831 -10.79242 1.000 13.21425  ? 113 GLY B O   1 
ATOM   2523 N N   . THR B 2 114 ? 17.03458  -58.64202 -8.62573  1.000 12.26197  ? 114 THR B N   1 
ATOM   2524 C CA  . THR B 2 114 ? 18.00594  -59.71545 -8.83155  1.000 12.24348  ? 114 THR B CA  1 
ATOM   2525 C C   . THR B 2 114 ? 17.68291  -60.84332 -7.86218  1.000 12.57075  ? 114 THR B C   1 
ATOM   2526 O O   . THR B 2 114 ? 17.51024  -60.59271 -6.65946  1.000 12.94003  ? 114 THR B O   1 
ATOM   2527 C CB  . THR B 2 114 ? 19.44830  -59.22128 -8.65269  1.000 13.52573  ? 114 THR B CB  1 
ATOM   2528 O OG1 . THR B 2 114 ? 20.37672  -60.24231 -9.00699  1.000 14.29076  ? 114 THR B OG1 1 
ATOM   2529 C CG2 . THR B 2 114 ? 19.79253  -58.72172 -7.23441  1.000 14.79634  ? 114 THR B CG2 1 
ATOM   2530 N N   . GLN B 2 115 ? 17.54014  -62.05860 -8.36750  1.000 12.84880  ? 115 GLN B N   1 
ATOM   2531 C CA  . GLN B 2 115 ? 17.23920  -63.18801 -7.49988  1.000 13.45630  ? 115 GLN B CA  1 
ATOM   2532 C C   . GLN B 2 115 ? 18.47098  -63.58415 -6.70925  1.000 12.92556  ? 115 GLN B C   1 
ATOM   2533 O O   . GLN B 2 115 ? 19.55739  -63.75261 -7.28105  1.000 14.52536  ? 115 GLN B O   1 
ATOM   2534 C CB  . GLN B 2 115 ? 16.85342  -64.39416 -8.35018  1.000 16.76956  ? 115 GLN B CB  1 
ATOM   2535 C CG  . GLN B 2 115 ? 16.51468  -65.69282 -7.58432  1.000 18.39916  ? 115 GLN B CG  1 
ATOM   2536 C CD  . GLN B 2 115 ? 15.21768  -65.60755 -6.79216  1.000 19.77386  ? 115 GLN B CD  1 
ATOM   2537 O OE1 . GLN B 2 115 ? 14.14035  -65.40928 -7.35465  1.000 21.44062  ? 115 GLN B OE1 1 
ATOM   2538 N NE2 . GLN B 2 115 ? 15.30299  -65.86966 -5.46258  1.000 20.58874  ? 115 GLN B NE2 1 
ATOM   2539 N N   . VAL B 2 116 ? 18.27765  -63.84898 -5.41270  1.000 13.25591  ? 116 VAL B N   1 
ATOM   2540 C CA  . VAL B 2 116 ? 19.28751  -64.43193 -4.53883  1.000 13.70551  ? 116 VAL B CA  1 
ATOM   2541 C C   . VAL B 2 116 ? 18.65350  -65.68594 -3.95884  1.000 14.06067  ? 116 VAL B C   1 
ATOM   2542 O O   . VAL B 2 116 ? 17.58592  -65.60430 -3.34768  1.000 14.71761  ? 116 VAL B O   1 
ATOM   2543 C CB  . VAL B 2 116 ? 19.67348  -63.45259 -3.41127  1.000 14.83537  ? 116 VAL B CB  1 
ATOM   2544 C CG1 . VAL B 2 116 ? 20.53147  -64.15478 -2.35989  1.000 17.45391  ? 116 VAL B CG1 1 
ATOM   2545 C CG2 . VAL B 2 116 ? 20.37799  -62.24821 -4.03250  1.000 15.78687  ? 116 VAL B CG2 1 
ATOM   2546 N N   . THR B 2 117 ? 19.31465  -66.82983 -4.09317  1.000 15.41642  ? 117 THR B N   1 
ATOM   2547 C CA  A THR B 2 117 ? 18.79742  -68.05763 -3.50677  0.500 15.98619  ? 117 THR B CA  1 
ATOM   2548 C CA  B THR B 2 117 ? 18.80318  -68.07719 -3.52786  0.500 15.96191  ? 117 THR B CA  1 
ATOM   2549 C C   . THR B 2 117 ? 19.91441  -68.69122 -2.68999  1.000 17.01011  ? 117 THR B C   1 
ATOM   2550 O O   . THR B 2 117 ? 21.00829  -68.93693 -3.19892  1.000 20.18157  ? 117 THR B O   1 
ATOM   2551 C CB  A THR B 2 117 ? 18.24527  -69.00182 -4.59572  0.500 19.18576  ? 117 THR B CB  1 
ATOM   2552 C CB  B THR B 2 117 ? 18.38549  -69.04910 -4.65074  0.500 17.63027  ? 117 THR B CB  1 
ATOM   2553 O OG1 A THR B 2 117 ? 19.32581  -69.58579 -5.32351  0.500 25.87207  ? 117 THR B OG1 1 
ATOM   2554 O OG1 B THR B 2 117 ? 17.39176  -68.43323 -5.45846  0.500 18.47424  ? 117 THR B OG1 1 
ATOM   2555 C CG2 A THR B 2 117 ? 17.39263  -68.19594 -5.57709  0.500 19.99496  ? 117 THR B CG2 1 
ATOM   2556 C CG2 B THR B 2 117 ? 17.72491  -70.29408 -4.05260  0.500 17.16519  ? 117 THR B CG2 1 
ATOM   2557 N N   . VAL B 2 118 ? 19.64488  -68.93700 -1.42377  1.000 17.30437  ? 118 VAL B N   1 
ATOM   2558 C CA  . VAL B 2 118 ? 20.61894  -69.48744 -0.50136  1.000 18.49462  ? 118 VAL B CA  1 
ATOM   2559 C C   . VAL B 2 118 ? 20.11865  -70.86324 -0.07920  1.000 20.58861  ? 118 VAL B C   1 
ATOM   2560 O O   . VAL B 2 118 ? 19.01502  -70.99832 0.46243   1.000 21.91834  ? 118 VAL B O   1 
ATOM   2561 C CB  . VAL B 2 118 ? 20.79583  -68.57319 0.72472   1.000 18.39039  ? 118 VAL B CB  1 
ATOM   2562 C CG1 . VAL B 2 118 ? 21.88576  -69.13160 1.63461   1.000 19.16196  ? 118 VAL B CG1 1 
ATOM   2563 C CG2 . VAL B 2 118 ? 21.14637  -67.12507 0.31235   1.000 18.25752  ? 118 VAL B CG2 1 
ATOM   2564 N N   . SER B 2 119 ? 20.91008  -71.89007 -0.33641  1.000 24.94281  ? 119 SER B N   1 
ATOM   2565 C CA  . SER B 2 119 ? 20.48503  -73.23930 0.01341   1.000 35.48701  ? 119 SER B CA  1 
ATOM   2566 C C   . SER B 2 119 ? 21.28418  -73.76849 1.19800   1.000 42.21768  ? 119 SER B C   1 
ATOM   2567 O O   . SER B 2 119 ? 22.47137  -73.47018 1.35191   1.000 40.20620  ? 119 SER B O   1 
ATOM   2568 C CB  . SER B 2 119 ? 20.60553  -74.17731 -1.18583  1.000 39.87282  ? 119 SER B CB  1 
ATOM   2569 O OG  . SER B 2 119 ? 21.90673  -74.10652 -1.72845  1.000 42.36033  ? 119 SER B OG  1 
ATOM   2570 N N   . SER B 2 120 ? 20.62175  -74.55895 2.03981   1.000 47.46755  ? 120 SER B N   1 
ATOM   2571 C CA  . SER B 2 120 ? 21.30843  -75.15915 3.18937   1.000 51.10718  ? 120 SER B CA  1 
ATOM   2572 C C   . SER B 2 120 ? 22.20816  -76.31830 2.76039   1.000 52.32528  ? 120 SER B C   1 
ATOM   2573 O O   . SER B 2 120 ? 22.20380  -76.73089 1.59546   1.000 52.51390  ? 120 SER B O   1 
ATOM   2574 C CB  . SER B 2 120 ? 20.31410  -75.61150 4.26424   1.000 52.04352  ? 120 SER B CB  1 
ATOM   2575 O OG  . SER B 2 120 ? 19.15989  -76.19374 3.68941   1.000 52.45422  ? 120 SER B OG  1 
HETATM 2576 C C1  . NAG C 3 .   ? -3.71813  -40.04337 -23.04847 1.000 40.04675  ? 601 NAG A C1  1 
HETATM 2577 C C2  . NAG C 3 .   ? -4.22247  -38.64815 -23.47088 1.000 38.90026  ? 601 NAG A C2  1 
HETATM 2578 C C3  . NAG C 3 .   ? -5.41454  -38.75614 -24.43650 1.000 46.91527  ? 601 NAG A C3  1 
HETATM 2579 C C4  . NAG C 3 .   ? -5.13838  -39.74241 -25.56326 1.000 53.41568  ? 601 NAG A C4  1 
HETATM 2580 C C5  . NAG C 3 .   ? -4.75574  -41.08349 -24.96395 1.000 54.16325  ? 601 NAG A C5  1 
HETATM 2581 C C6  . NAG C 3 .   ? -4.47289  -42.15369 -25.99376 1.000 55.13567  ? 601 NAG A C6  1 
HETATM 2582 C C7  . NAG C 3 .   ? -4.23395  -36.63844 -22.03205 1.000 47.60206  ? 601 NAG A C7  1 
HETATM 2583 C C8  . NAG C 3 .   ? -3.36221  -35.98860 -23.06049 1.000 28.96155  ? 601 NAG A C8  1 
HETATM 2584 N N2  . NAG C 3 .   ? -4.60861  -37.89760 -22.28508 1.000 40.78167  ? 601 NAG A N2  1 
HETATM 2585 O O3  . NAG C 3 .   ? -5.68648  -37.47632 -24.99769 1.000 40.08688  ? 601 NAG A O3  1 
HETATM 2586 O O4  . NAG C 3 .   ? -6.28570  -39.87960 -26.39475 1.000 54.36366  ? 601 NAG A O4  1 
HETATM 2587 O O5  . NAG C 3 .   ? -3.55037  -40.89077 -24.21970 1.000 41.01888  ? 601 NAG A O5  1 
HETATM 2588 O O6  . NAG C 3 .   ? -3.22233  -41.93870 -26.63319 1.000 60.65343  ? 601 NAG A O6  1 
HETATM 2589 O O7  . NAG C 3 .   ? -4.59343  -36.04591 -21.01312 1.000 48.79996  ? 601 NAG A O7  1 
HETATM 2590 C C1  . EDO D 4 .   ? -3.59807  -24.45654 -4.73171  1.000 31.14447  ? 602 EDO A C1  1 
HETATM 2591 O O1  . EDO D 4 .   ? -4.57371  -24.18537 -3.72015  1.000 33.69583  ? 602 EDO A O1  1 
HETATM 2592 C C2  . EDO D 4 .   ? -3.45920  -23.32310 -5.75176  1.000 27.78164  ? 602 EDO A C2  1 
HETATM 2593 O O2  . EDO D 4 .   ? -3.42984  -22.04968 -5.08532  1.000 40.88900  ? 602 EDO A O2  1 
HETATM 2594 H H11 . EDO D 4 .   ? -3.87690  -25.37287 -5.25618  1.000 37.37794  ? 602 EDO A H11 1 
HETATM 2595 H H12 . EDO D 4 .   ? -2.63027  -24.62418 -4.25452  1.000 37.37794  ? 602 EDO A H12 1 
HETATM 2596 H HO1 . EDO D 4 .   ? -5.04906  -23.37259 -3.94044  1.000 40.43957  ? 602 EDO A HO1 1 
HETATM 2597 H H21 . EDO D 4 .   ? -4.29881  -23.35264 -6.44936  1.000 33.34254  ? 602 EDO A H21 1 
HETATM 2598 H H22 . EDO D 4 .   ? -2.54044  -23.45748 -6.32647  1.000 33.34254  ? 602 EDO A H22 1 
HETATM 2599 H HO2 . EDO D 4 .   ? -3.32712  -22.18630 -4.13354  1.000 49.07137  ? 602 EDO A HO2 1 
HETATM 2600 C C   . ACT E 5 .   ? 22.99504  -43.94446 -6.85836  1.000 42.90042  ? 201 ACT B C   1 
HETATM 2601 O O   . ACT E 5 .   ? 21.90484  -43.34314 -7.07074  1.000 31.31738  ? 201 ACT B O   1 
HETATM 2602 O OXT . ACT E 5 .   ? 24.05742  -43.50841 -6.32266  1.000 47.76058  ? 201 ACT B OXT 1 
HETATM 2603 C CH3 . ACT E 5 .   ? 23.04919  -45.43956 -7.30556  1.000 54.13337  ? 201 ACT B CH3 1 
HETATM 2604 C C1  . EDO F 4 .   ? 28.25410  -56.76202 -9.65282  1.000 39.05274  ? 202 EDO B C1  1 
HETATM 2605 O O1  . EDO F 4 .   ? 28.11493  -58.07735 -10.21151 1.000 47.14715  ? 202 EDO B O1  1 
HETATM 2606 C C2  . EDO F 4 .   ? 27.64007  -56.75709 -8.25447  1.000 32.44278  ? 202 EDO B C2  1 
HETATM 2607 O O2  . EDO F 4 .   ? 28.61446  -56.38649 -7.28056  1.000 38.21690  ? 202 EDO B O2  1 
HETATM 2608 H H11 . EDO F 4 .   ? 27.74859  -56.03039 -10.28656 1.000 46.86787  ? 202 EDO B H11 1 
HETATM 2609 H H12 . EDO F 4 .   ? 29.30966  -56.48742 -9.59946  1.000 46.86787  ? 202 EDO B H12 1 
HETATM 2610 H HO1 . EDO F 4 .   ? 27.17628  -58.29278 -10.29882 1.000 56.58116  ? 202 EDO B HO1 1 
HETATM 2611 H H21 . EDO F 4 .   ? 27.25011  -57.75035 -8.02247  1.000 38.93590  ? 202 EDO B H21 1 
HETATM 2612 H H22 . EDO F 4 .   ? 26.80569  -56.05330 -8.22361  1.000 38.93590  ? 202 EDO B H22 1 
HETATM 2613 H HO2 . EDO F 4 .   ? 28.86988  -55.46359 -7.41515  1.000 45.86485  ? 202 EDO B HO2 1 
HETATM 2614 O O   . HOH G 6 .   ? 8.22208   -41.67011 20.39479  1.000 44.51348  ? 701 HOH A O   1 
HETATM 2615 O O   . HOH G 6 .   ? -14.135   -44.084   -0.446    1.000 44.75175  ? 702 HOH A O   1 
HETATM 2616 O O   . HOH G 6 .   ? -4.13022  -35.13473 11.63387  1.000 22.80662  ? 703 HOH A O   1 
HETATM 2617 O O   . HOH G 6 .   ? -7.04727  -36.25688 -23.42959 1.000 46.21536  ? 704 HOH A O   1 
HETATM 2618 O O   . HOH G 6 .   ? -5.02182  -45.84115 4.53479   1.000 22.78549  ? 705 HOH A O   1 
HETATM 2619 O O   . HOH G 6 .   ? 12.24237  -39.59028 16.86390  1.000 39.69171  ? 706 HOH A O   1 
HETATM 2620 O O   . HOH G 6 .   ? -8.25402  -28.68039 8.07536   1.000 38.36385  ? 707 HOH A O   1 
HETATM 2621 O O   . HOH G 6 .   ? -12.21753 -42.74158 -21.63966 1.000 35.56402  ? 708 HOH A O   1 
HETATM 2622 O O   . HOH G 6 .   ? 6.47369   -43.49799 -16.66176 1.000 39.37744  ? 709 HOH A O   1 
HETATM 2623 O O   . HOH G 6 .   ? 5.749     -42.320   18.210    1.000 21.53640  ? 710 HOH A O   1 
HETATM 2624 O O   . HOH G 6 .   ? 15.16945  -48.88453 26.75430  1.000 34.30145  ? 711 HOH A O   1 
HETATM 2625 O O   . HOH G 6 .   ? -12.06080 -42.87008 -8.16485  1.000 25.13310  ? 712 HOH A O   1 
HETATM 2626 O O   . HOH G 6 .   ? 8.11875   -51.76931 5.09611   1.000 19.28599  ? 713 HOH A O   1 
HETATM 2627 O O   . HOH G 6 .   ? 7.40951   -53.20933 17.91725  1.000 22.20680  ? 714 HOH A O   1 
HETATM 2628 O O   . HOH G 6 .   ? 4.53597   -51.18862 -11.12856 1.000 23.33167  ? 715 HOH A O   1 
HETATM 2629 O O   . HOH G 6 .   ? -18.97487 -20.89317 -18.33356 1.000 41.58755  ? 716 HOH A O   1 
HETATM 2630 O O   . HOH G 6 .   ? 13.26318  -39.05210 11.79845  1.000 37.10362  ? 717 HOH A O   1 
HETATM 2631 O O   . HOH G 6 .   ? -8.59123  -22.34646 -16.34772 1.000 29.64907  ? 718 HOH A O   1 
HETATM 2632 O O   . HOH G 6 .   ? -4.19774  -43.09174 10.33616  1.000 19.07135  ? 719 HOH A O   1 
HETATM 2633 O O   . HOH G 6 .   ? -3.88525  -30.24771 -23.39953 1.000 51.37547  ? 720 HOH A O   1 
HETATM 2634 O O   . HOH G 6 .   ? 4.46555   -60.53171 -10.66977 1.000 31.71182  ? 721 HOH A O   1 
HETATM 2635 O O   . HOH G 6 .   ? 11.18524  -57.18733 11.77876  1.000 28.24270  ? 722 HOH A O   1 
HETATM 2636 O O   . HOH G 6 .   ? 18.16119  -50.50968 19.51363  1.000 34.34824  ? 723 HOH A O   1 
HETATM 2637 O O   . HOH G 6 .   ? 16.36924  -43.88042 17.24537  1.000 20.50534  ? 724 HOH A O   1 
HETATM 2638 O O   . HOH G 6 .   ? -20.199   -29.367   -14.205   1.000 20.75380  ? 725 HOH A O   1 
HETATM 2639 O O   . HOH G 6 .   ? 10.15959  -53.31954 12.65536  1.000 18.24027  ? 726 HOH A O   1 
HETATM 2640 O O   . HOH G 6 .   ? -15.04400 -33.86500 -1.42460  1.000 25.03059  ? 727 HOH A O   1 
HETATM 2641 O O   . HOH G 6 .   ? 9.76948   -38.53939 8.56266   1.000 18.98046  ? 728 HOH A O   1 
HETATM 2642 O O   . HOH G 6 .   ? 15.83499  -43.52650 14.64043  1.000 21.01219  ? 729 HOH A O   1 
HETATM 2643 O O   . HOH G 6 .   ? -6.38398  -39.12901 -20.68844 1.000 48.98987  ? 730 HOH A O   1 
HETATM 2644 O O   . HOH G 6 .   ? -1.20990  -29.74877 -7.59514  1.000 17.10135  ? 731 HOH A O   1 
HETATM 2645 O O   . HOH G 6 .   ? -19.12994 -32.51600 -11.45701 1.000 25.71065  ? 732 HOH A O   1 
HETATM 2646 O O   . HOH G 6 .   ? 11.99915  -41.08516 7.56816   1.000 15.49764  ? 733 HOH A O   1 
HETATM 2647 O O   . HOH G 6 .   ? -13.58728 -47.12760 -9.50295  1.000 33.40714  ? 734 HOH A O   1 
HETATM 2648 O O   . HOH G 6 .   ? -1.59164  -43.48655 -16.86054 1.000 28.76125  ? 735 HOH A O   1 
HETATM 2649 O O   . HOH G 6 .   ? -11.11852 -35.06698 -3.89271  1.000 15.40033  ? 736 HOH A O   1 
HETATM 2650 O O   . HOH G 6 .   ? 5.80155   -39.17694 3.11539   1.000 12.26138  ? 737 HOH A O   1 
HETATM 2651 O O   . HOH G 6 .   ? -15.76574 -23.30131 -18.69473 1.000 29.23338  ? 738 HOH A O   1 
HETATM 2652 O O   . HOH G 6 .   ? -7.07325  -18.99580 -24.45732 1.000 47.74060  ? 739 HOH A O   1 
HETATM 2653 O O   . HOH G 6 .   ? -5.77221  -47.94423 -15.75599 1.000 32.21712  ? 740 HOH A O   1 
HETATM 2654 O O   . HOH G 6 .   ? 7.52784   -50.76386 8.98950   1.000 18.13731  ? 741 HOH A O   1 
HETATM 2655 O O   . HOH G 6 .   ? -11.72242 -26.28437 3.13388   1.000 32.30433  ? 742 HOH A O   1 
HETATM 2656 O O   . HOH G 6 .   ? 14.59041  -57.33429 10.78414  1.000 20.75845  ? 743 HOH A O   1 
HETATM 2657 O O   . HOH G 6 .   ? -9.75823  -47.42632 -14.88289 1.000 25.08382  ? 744 HOH A O   1 
HETATM 2658 O O   . HOH G 6 .   ? 10.48697  -42.18156 21.23825  1.000 37.65245  ? 745 HOH A O   1 
HETATM 2659 O O   . HOH G 6 .   ? -10.22942 -29.41915 -27.49813 1.000 46.15580  ? 746 HOH A O   1 
HETATM 2660 O O   . HOH G 6 .   ? 5.57078   -37.04844 1.12749   1.000 13.03988  ? 747 HOH A O   1 
HETATM 2661 O O   . HOH G 6 .   ? -12.13589 -31.23393 8.28477   1.000 32.66051  ? 748 HOH A O   1 
HETATM 2662 O O   . HOH G 6 .   ? 2.63840   -30.64716 11.57065  1.000 30.91674  ? 749 HOH A O   1 
HETATM 2663 O O   . HOH G 6 .   ? 5.15150   -39.05301 -19.32480 1.000 44.99039  ? 750 HOH A O   1 
HETATM 2664 O O   . HOH G 6 .   ? -11.95325 -46.02632 -12.02729 1.000 20.02884  ? 751 HOH A O   1 
HETATM 2665 O O   . HOH G 6 .   ? -6.71033  -29.43258 4.60391   1.000 18.35482  ? 752 HOH A O   1 
HETATM 2666 O O   . HOH G 6 .   ? -6.28447  -32.67334 3.33560   1.000 19.96014  ? 753 HOH A O   1 
HETATM 2667 O O   . HOH G 6 .   ? -13.02288 -31.66754 1.30071   1.000 20.77200  ? 754 HOH A O   1 
HETATM 2668 O O   . HOH G 6 .   ? 2.12229   -25.33262 3.17138   1.000 32.10100  ? 755 HOH A O   1 
HETATM 2669 O O   . HOH G 6 .   ? -3.55302  -22.88161 -1.53029  1.000 32.06650  ? 756 HOH A O   1 
HETATM 2670 O O   . HOH G 6 .   ? 5.62070   -27.95374 -2.12927  1.000 39.03381  ? 757 HOH A O   1 
HETATM 2671 O O   . HOH G 6 .   ? -16.66475 -32.12197 -10.58663 1.000 24.13513  ? 758 HOH A O   1 
HETATM 2672 O O   . HOH G 6 .   ? -11.12736 -53.17142 -10.98984 1.000 29.56369  ? 759 HOH A O   1 
HETATM 2673 O O   . HOH G 6 .   ? 16.70166  -41.02532 4.94787   1.000 25.34976  ? 760 HOH A O   1 
HETATM 2674 O O   . HOH G 6 .   ? -2.74781  -40.91040 10.65586  1.000 18.54810  ? 761 HOH A O   1 
HETATM 2675 O O   . HOH G 6 .   ? -11.96938 -45.86711 -14.71482 1.000 29.51989  ? 762 HOH A O   1 
HETATM 2676 O O   . HOH G 6 .   ? 5.48686   -31.43543 8.92385   1.000 21.55523  ? 763 HOH A O   1 
HETATM 2677 O O   . HOH G 6 .   ? 10.94616  -42.12840 10.16544  1.000 15.68375  ? 764 HOH A O   1 
HETATM 2678 O O   . HOH G 6 .   ? 8.90906   -39.48366 -7.67866  1.000 19.46549  ? 765 HOH A O   1 
HETATM 2679 O O   . HOH G 6 .   ? -10.72041 -25.46509 -0.69706  1.000 24.89869  ? 766 HOH A O   1 
HETATM 2680 O O   . HOH G 6 .   ? 12.22608  -47.56915 20.20853  1.000 18.54583  ? 767 HOH A O   1 
HETATM 2681 O O   . HOH G 6 .   ? -9.19927  -43.79546 3.87565   1.000 15.07661  ? 768 HOH A O   1 
HETATM 2682 O O   . HOH G 6 .   ? -13.21723 -36.59544 0.48963   1.000 22.61321  ? 769 HOH A O   1 
HETATM 2683 O O   . HOH G 6 .   ? 6.38017   -52.39752 7.02444   1.000 20.70194  ? 770 HOH A O   1 
HETATM 2684 O O   . HOH G 6 .   ? -3.97096  -34.03138 7.84601   1.000 16.71814  ? 771 HOH A O   1 
HETATM 2685 O O   . HOH G 6 .   ? 3.04984   -35.13276 -11.76757 1.000 16.42845  ? 772 HOH A O   1 
HETATM 2686 O O   . HOH G 6 .   ? -15.08998 -36.12119 5.07767   1.000 33.01018  ? 773 HOH A O   1 
HETATM 2687 O O   . HOH G 6 .   ? 14.74279  -52.62007 18.45332  1.000 35.09125  ? 774 HOH A O   1 
HETATM 2688 O O   . HOH G 6 .   ? -6.03631  -19.70494 -7.02846  1.000 36.86444  ? 775 HOH A O   1 
HETATM 2689 O O   . HOH G 6 .   ? 8.59467   -31.66076 8.53504   1.000 31.98107  ? 776 HOH A O   1 
HETATM 2690 O O   . HOH G 6 .   ? 4.68825   -38.08730 17.49046  1.000 27.56272  ? 777 HOH A O   1 
HETATM 2691 O O   . HOH G 6 .   ? 8.69634   -41.10995 8.91150   1.000 14.51740  ? 778 HOH A O   1 
HETATM 2692 O O   . HOH G 6 .   ? -4.68295  -54.44531 -6.54237  1.000 18.22630  ? 779 HOH A O   1 
HETATM 2693 O O   . HOH G 6 .   ? -4.355    -47.436   9.347     1.000 35.12970  ? 780 HOH A O   1 
HETATM 2694 O O   . HOH G 6 .   ? 5.25640   -59.79420 -7.52246  1.000 24.16194  ? 781 HOH A O   1 
HETATM 2695 O O   . HOH G 6 .   ? -6.11945  -22.85803 -16.47254 1.000 31.71305  ? 782 HOH A O   1 
HETATM 2696 O O   . HOH G 6 .   ? 1.25926   -48.51870 -17.12909 1.000 38.29351  ? 783 HOH A O   1 
HETATM 2697 O O   . HOH G 6 .   ? -2.62068  -55.10719 -1.31259  1.000 27.26398  ? 784 HOH A O   1 
HETATM 2698 O O   . HOH G 6 .   ? -13.25289 -36.63595 -22.99353 1.000 25.44410  ? 785 HOH A O   1 
HETATM 2699 O O   . HOH G 6 .   ? -1.23524  -62.33432 -6.72870  1.000 19.58238  ? 786 HOH A O   1 
HETATM 2700 O O   . HOH G 6 .   ? 7.39092   -52.70073 -12.60392 1.000 32.42210  ? 787 HOH A O   1 
HETATM 2701 O O   . HOH G 6 .   ? -1.26354  -33.50999 7.20422   1.000 14.81180  ? 788 HOH A O   1 
HETATM 2702 O O   . HOH G 6 .   ? 1.66195   -32.76936 0.22182   1.000 14.79784  ? 789 HOH A O   1 
HETATM 2703 O O   . HOH G 6 .   ? -17.491   -38.822   -22.819   1.000 27.00580  ? 790 HOH A O   1 
HETATM 2704 O O   . HOH G 6 .   ? 2.36267   -38.52798 -14.06058 1.000 19.75232  ? 791 HOH A O   1 
HETATM 2705 O O   . HOH G 6 .   ? -11.84134 -43.28287 -1.29102  1.000 17.59747  ? 792 HOH A O   1 
HETATM 2706 O O   . HOH G 6 .   ? 2.54033   -53.68578 -12.22704 1.000 26.63300  ? 793 HOH A O   1 
HETATM 2707 O O   . HOH G 6 .   ? -11.06063 -42.32539 5.32198   1.000 15.23871  ? 794 HOH A O   1 
HETATM 2708 O O   . HOH G 6 .   ? 2.28413   -45.37059 -3.79694  1.000 13.20790  ? 795 HOH A O   1 
HETATM 2709 O O   . HOH G 6 .   ? 11.64918  -33.93324 0.93964   1.000 31.34784  ? 796 HOH A O   1 
HETATM 2710 O O   . HOH G 6 .   ? 11.85345  -46.85922 -12.15432 1.000 21.34523  ? 797 HOH A O   1 
HETATM 2711 O O   . HOH G 6 .   ? 2.01419   -52.79718 8.86822   1.000 21.92264  ? 798 HOH A O   1 
HETATM 2712 O O   . HOH G 6 .   ? -6.92176  -30.75292 7.80057   1.000 27.85253  ? 799 HOH A O   1 
HETATM 2713 O O   . HOH G 6 .   ? 23.553    -44.675   17.123    1.000 26.86174  ? 800 HOH A O   1 
HETATM 2714 O O   . HOH G 6 .   ? -4.56662  -25.80564 5.36265   1.000 25.91344  ? 801 HOH A O   1 
HETATM 2715 O O   . HOH G 6 .   ? -5.62230  -60.39533 -3.17974  1.000 30.71406  ? 802 HOH A O   1 
HETATM 2716 O O   . HOH G 6 .   ? -15.94724 -28.10381 -3.64983  1.000 31.98771  ? 803 HOH A O   1 
HETATM 2717 O O   . HOH G 6 .   ? 3.08867   -51.69536 -4.40647  1.000 17.25905  ? 804 HOH A O   1 
HETATM 2718 O O   . HOH G 6 .   ? -5.98415  -21.34445 -3.34263  1.000 32.42970  ? 805 HOH A O   1 
HETATM 2719 O O   . HOH G 6 .   ? -1.36428  -50.12838 7.09863   1.000 30.81172  ? 806 HOH A O   1 
HETATM 2720 O O   . HOH G 6 .   ? -8.69445  -16.66507 -12.78355 1.000 47.02934  ? 807 HOH A O   1 
HETATM 2721 O O   . HOH G 6 .   ? 14.24091  -51.43216 20.30726  1.000 40.26138  ? 808 HOH A O   1 
HETATM 2722 O O   . HOH G 6 .   ? -3.68285  -52.38177 -1.16359  1.000 25.58935  ? 809 HOH A O   1 
HETATM 2723 O O   . HOH G 6 .   ? -10.52428 -20.07471 -5.04876  1.000 39.90479  ? 810 HOH A O   1 
HETATM 2724 O O   . HOH G 6 .   ? -5.69170  -43.90516 7.02927   1.000 16.05503  ? 811 HOH A O   1 
HETATM 2725 O O   . HOH G 6 .   ? 9.67270   -51.13604 -11.60667 1.000 33.52517  ? 812 HOH A O   1 
HETATM 2726 O O   . HOH G 6 .   ? -1.37016  -29.74557 7.75820   1.000 23.71975  ? 813 HOH A O   1 
HETATM 2727 O O   . HOH G 6 .   ? 18.08908  -44.75204 13.85711  1.000 19.83013  ? 814 HOH A O   1 
HETATM 2728 O O   . HOH G 6 .   ? 3.26461   -49.66839 -13.07795 1.000 29.95893  ? 815 HOH A O   1 
HETATM 2729 O O   . HOH G 6 .   ? 3.78289   -39.77549 -10.93787 1.000 17.09162  ? 816 HOH A O   1 
HETATM 2730 O O   . HOH G 6 .   ? -4.70312  -34.61818 1.30566   1.000 15.81019  ? 817 HOH A O   1 
HETATM 2731 O O   . HOH G 6 .   ? 23.63578  -50.06149 15.55608  1.000 24.53821  ? 818 HOH A O   1 
HETATM 2732 O O   . HOH G 6 .   ? 14.03186  -56.33270 17.40693  1.000 33.66645  ? 819 HOH A O   1 
HETATM 2733 O O   . HOH G 6 .   ? 4.72061   -26.95115 1.23484   1.000 35.65928  ? 820 HOH A O   1 
HETATM 2734 O O   . HOH G 6 .   ? 8.84142   -38.83154 11.67688  1.000 23.93494  ? 821 HOH A O   1 
HETATM 2735 O O   . HOH G 6 .   ? 4.45726   -40.15395 -13.59918 1.000 23.20486  ? 822 HOH A O   1 
HETATM 2736 O O   . HOH G 6 .   ? -17.44290 -40.67396 -11.89932 1.000 35.82334  ? 823 HOH A O   1 
HETATM 2737 O O   . HOH G 6 .   ? -11.03329 -40.25813 -22.79375 1.000 39.46584  ? 824 HOH A O   1 
HETATM 2738 O O   . HOH G 6 .   ? -16.79933 -41.66816 -14.71196 1.000 37.73874  ? 825 HOH A O   1 
HETATM 2739 O O   . HOH G 6 .   ? -7.85924  -51.27572 -13.95748 1.000 27.18304  ? 826 HOH A O   1 
HETATM 2740 O O   . HOH G 6 .   ? -9.34030  -15.50127 -15.47806 1.000 38.97189  ? 827 HOH A O   1 
HETATM 2741 O O   . HOH G 6 .   ? 16.93829  -51.43862 17.07339  1.000 22.52097  ? 828 HOH A O   1 
HETATM 2742 O O   . HOH G 6 .   ? 0.25435   -52.52511 2.89339   1.000 32.03203  ? 829 HOH A O   1 
HETATM 2743 O O   . HOH G 6 .   ? -10.01331 -58.36211 -8.11719  1.000 35.50050  ? 830 HOH A O   1 
HETATM 2744 O O   . HOH G 6 .   ? -14.88305 -25.65157 -2.63059  1.000 25.13821  ? 831 HOH A O   1 
HETATM 2745 O O   . HOH G 6 .   ? 19.14609  -43.88595 17.48333  1.000 23.04444  ? 832 HOH A O   1 
HETATM 2746 O O   . HOH G 6 .   ? -8.64827  -39.69926 -20.64757 1.000 47.53455  ? 833 HOH A O   1 
HETATM 2747 O O   . HOH G 6 .   ? 2.21619   -26.02547 -4.05332  1.000 33.23677  ? 834 HOH A O   1 
HETATM 2748 O O   . HOH G 6 .   ? 9.73575   -51.90410 10.16301  1.000 16.04239  ? 835 HOH A O   1 
HETATM 2749 O O   . HOH G 6 .   ? 5.92155   -42.19451 -19.10305 1.000 43.13813  ? 836 HOH A O   1 
HETATM 2750 O O   . HOH G 6 .   ? 7.60313   -35.48127 11.82948  1.000 31.23790  ? 837 HOH A O   1 
HETATM 2751 O O   . HOH G 6 .   ? -7.54259  -22.51856 7.16496   1.000 46.09424  ? 838 HOH A O   1 
HETATM 2752 O O   . HOH G 6 .   ? -16.07531 -37.39586 -8.69842  1.000 20.62160  ? 839 HOH A O   1 
HETATM 2753 O O   . HOH G 6 .   ? 11.79450  -41.30413 14.97998  1.000 21.96615  ? 840 HOH A O   1 
HETATM 2754 O O   . HOH G 6 .   ? -16.54007 -30.53363 -8.22216  1.000 21.83806  ? 841 HOH A O   1 
HETATM 2755 O O   . HOH G 6 .   ? 3.55980   -25.88903 -22.49209 1.000 41.43928  ? 842 HOH A O   1 
HETATM 2756 O O   . HOH G 6 .   ? -13.38392 -39.58420 -4.81696  1.000 30.87517  ? 843 HOH A O   1 
HETATM 2757 O O   . HOH G 6 .   ? -7.95039  -50.36142 -17.01320 1.000 44.09379  ? 844 HOH A O   1 
HETATM 2758 O O   . HOH G 6 .   ? 6.37358   -26.27085 -6.97566  1.000 32.43854  ? 845 HOH A O   1 
HETATM 2759 O O   . HOH G 6 .   ? 12.62578  -35.67784 2.65753   1.000 20.86350  ? 846 HOH A O   1 
HETATM 2760 O O   . HOH G 6 .   ? -15.09683 -40.85742 -22.70085 1.000 32.65143  ? 847 HOH A O   1 
HETATM 2761 O O   . HOH G 6 .   ? 9.42584   -47.83317 25.10808  1.000 33.90013  ? 848 HOH A O   1 
HETATM 2762 O O   . HOH G 6 .   ? -14.29635 -55.52798 -4.71426  1.000 36.71658  ? 849 HOH A O   1 
HETATM 2763 O O   . HOH G 6 .   ? -20.20760 -20.89627 -13.88218 1.000 40.39055  ? 850 HOH A O   1 
HETATM 2764 O O   . HOH G 6 .   ? 7.88459   -29.16988 -13.95628 1.000 23.57385  ? 851 HOH A O   1 
HETATM 2765 O O   . HOH G 6 .   ? 11.09466  -33.61003 -1.67587  1.000 16.87826  ? 852 HOH A O   1 
HETATM 2766 O O   . HOH G 6 .   ? 5.10596   -35.32666 -13.68442 1.000 30.89134  ? 853 HOH A O   1 
HETATM 2767 O O   . HOH G 6 .   ? -9.23852  -55.39114 -12.50340 1.000 33.31290  ? 854 HOH A O   1 
HETATM 2768 O O   . HOH G 6 .   ? 3.65016   -26.33903 -19.58489 1.000 38.65317  ? 855 HOH A O   1 
HETATM 2769 O O   . HOH G 6 .   ? -15.76427 -20.91727 -9.74518  1.000 35.30494  ? 856 HOH A O   1 
HETATM 2770 O O   . HOH G 6 .   ? 8.43195   -30.26552 1.13663   1.000 21.96484  ? 857 HOH A O   1 
HETATM 2771 O O   . HOH G 6 .   ? -4.11091  -64.08688 -5.50116  1.000 32.06988  ? 858 HOH A O   1 
HETATM 2772 O O   . HOH G 6 .   ? -8.45831  -57.28181 -0.79336  1.000 32.89815  ? 859 HOH A O   1 
HETATM 2773 O O   . HOH G 6 .   ? -4.05832  -32.63463 9.85767   1.000 40.81161  ? 860 HOH A O   1 
HETATM 2774 O O   . HOH G 6 .   ? -2.57713  -58.28409 -1.48057  1.000 36.73129  ? 861 HOH A O   1 
HETATM 2775 O O   . HOH G 6 .   ? 10.30399  -34.35680 6.03306   1.000 38.75370  ? 862 HOH A O   1 
HETATM 2776 O O   . HOH G 6 .   ? -0.34781  -38.47776 -24.05896 1.000 32.46028  ? 863 HOH A O   1 
HETATM 2777 O O   . HOH G 6 .   ? -1.35783  -58.03843 -12.16868 1.000 37.89442  ? 864 HOH A O   1 
HETATM 2778 O O   . HOH G 6 .   ? -12.98850 -53.49210 -1.20340  1.000 34.95976  ? 865 HOH A O   1 
HETATM 2779 O O   . HOH G 6 .   ? -11.69631 -37.65453 -3.29334  1.000 23.41369  ? 866 HOH A O   1 
HETATM 2780 O O   . HOH G 6 .   ? 9.41103   -33.05080 4.88780   1.000 41.88178  ? 867 HOH A O   1 
HETATM 2781 O O   . HOH G 6 .   ? -5.39573  -23.25587 3.85166   1.000 31.60845  ? 868 HOH A O   1 
HETATM 2782 O O   . HOH G 6 .   ? -9.50623  -45.65969 -16.66179 1.000 30.39289  ? 869 HOH A O   1 
HETATM 2783 O O   . HOH G 6 .   ? 16.34533  -55.52317 15.74421  1.000 33.87669  ? 870 HOH A O   1 
HETATM 2784 O O   . HOH G 6 .   ? -0.07041  -52.49782 7.68310   1.000 39.24041  ? 871 HOH A O   1 
HETATM 2785 O O   . HOH G 6 .   ? -11.87426 -55.86878 -9.94592  1.000 45.41230  ? 872 HOH A O   1 
HETATM 2786 O O   . HOH G 6 .   ? -16.06360 -31.43762 -5.08526  1.000 32.60534  ? 873 HOH A O   1 
HETATM 2787 O O   . HOH G 6 .   ? -20.22763 -16.47831 -13.64508 1.000 42.85413  ? 874 HOH A O   1 
HETATM 2788 O O   . HOH G 6 .   ? 8.13155   -44.64902 24.83443  1.000 36.63457  ? 875 HOH A O   1 
HETATM 2789 O O   . HOH G 6 .   ? -3.91301  -50.97714 6.09049   1.000 38.67935  ? 876 HOH A O   1 
HETATM 2790 O O   . HOH G 6 .   ? 7.01734   -51.21662 24.27522  1.000 42.74698  ? 877 HOH A O   1 
HETATM 2791 O O   . HOH G 6 .   ? 11.62056  -49.07664 22.55414  1.000 25.71528  ? 878 HOH A O   1 
HETATM 2792 O O   . HOH G 6 .   ? -21.76486 -24.42718 -11.49138 1.000 29.66879  ? 879 HOH A O   1 
HETATM 2793 O O   . HOH G 6 .   ? 7.63244   -28.60953 8.18077   1.000 50.20789  ? 880 HOH A O   1 
HETATM 2794 O O   . HOH G 6 .   ? 7.06002   -29.60502 -2.31224  1.000 37.97662  ? 881 HOH A O   1 
HETATM 2795 O O   . HOH G 6 .   ? 12.52273  -38.09513 9.29647   1.000 35.12591  ? 882 HOH A O   1 
HETATM 2796 O O   . HOH G 6 .   ? -17.90960 -35.50898 -8.66421  1.000 34.97432  ? 883 HOH A O   1 
HETATM 2797 O O   . HOH G 6 .   ? -2.69618  -51.95968 1.14828   1.000 35.41569  ? 884 HOH A O   1 
HETATM 2798 O O   . HOH G 6 .   ? -3.04081  -33.17271 -23.35462 1.000 44.30163  ? 885 HOH A O   1 
HETATM 2799 O O   . HOH G 6 .   ? 7.22675   -48.73371 24.07629  1.000 47.69502  ? 886 HOH A O   1 
HETATM 2800 O O   . HOH G 6 .   ? 22.36039  -44.67451 13.96182  1.000 27.97174  ? 887 HOH A O   1 
HETATM 2801 O O   . HOH G 6 .   ? 12.44575  -34.78382 5.37775   1.000 40.83362  ? 888 HOH A O   1 
HETATM 2802 O O   . HOH G 6 .   ? -11.06164 -27.93569 4.72407   1.000 35.62456  ? 889 HOH A O   1 
HETATM 2803 O O   . HOH G 6 .   ? -5.36772  -41.80157 -18.07353 1.000 30.63664  ? 890 HOH A O   1 
HETATM 2804 O O   . HOH G 6 .   ? -19.07219 -20.12062 -16.11439 1.000 46.12978  ? 891 HOH A O   1 
HETATM 2805 O O   . HOH G 6 .   ? -14.15332 -34.10511 1.18434   1.000 23.36593  ? 892 HOH A O   1 
HETATM 2806 O O   . HOH G 6 .   ? -12.44156 -44.53891 -5.45000  1.000 45.79656  ? 893 HOH A O   1 
HETATM 2807 O O   . HOH G 6 .   ? 10.57370  -49.11693 -12.98013 1.000 40.00183  ? 894 HOH A O   1 
HETATM 2808 O O   . HOH G 6 .   ? 15.19154  -36.79197 2.71917   1.000 36.45606  ? 895 HOH A O   1 
HETATM 2809 O O   . HOH G 6 .   ? -8.64460  -37.28857 -21.53106 1.000 43.24008  ? 896 HOH A O   1 
HETATM 2810 O O   . HOH G 6 .   ? 10.76913  -53.64073 8.19548   1.000 26.45067  ? 897 HOH A O   1 
HETATM 2811 O O   . HOH G 6 .   ? -7.94036  -46.01808 4.72474   1.000 25.14530  ? 898 HOH A O   1 
HETATM 2812 O O   . HOH G 6 .   ? -13.34355 -47.25087 -1.58548  1.000 47.64768  ? 899 HOH A O   1 
HETATM 2813 O O   . HOH G 6 .   ? 20.24412  -43.32664 15.00069  1.000 28.82591  ? 900 HOH A O   1 
HETATM 2814 O O   . HOH G 6 .   ? -6.34270  -56.66311 0.38038   1.000 45.54117  ? 901 HOH A O   1 
HETATM 2815 O O   . HOH G 6 .   ? -6.61195  -43.17684 -18.37295 1.000 47.50424  ? 902 HOH A O   1 
HETATM 2816 O O   . HOH G 6 .   ? -13.03845 -46.74775 -4.62482  1.000 49.53589  ? 903 HOH A O   1 
HETATM 2817 O O   . HOH G 6 .   ? 0.47889   -25.52415 -5.21224  1.000 41.67453  ? 904 HOH A O   1 
HETATM 2818 O O   . HOH G 6 .   ? -15.99242 -34.41109 3.22309   1.000 36.50252  ? 905 HOH A O   1 
HETATM 2819 O O   . HOH G 6 .   ? -2.841    -30.627   9.990     1.000 39.20381  ? 906 HOH A O   1 
HETATM 2820 O O   . HOH G 6 .   ? -11.84107 -38.54248 -23.67099 1.000 45.26365  ? 907 HOH A O   1 
HETATM 2821 O O   . HOH G 6 .   ? -0.80593  -48.46322 11.85335  1.000 34.53718  ? 908 HOH A O   1 
HETATM 2822 O O   . HOH G 6 .   ? 0.76458   -28.69687 10.78912  1.000 45.64280  ? 909 HOH A O   1 
HETATM 2823 O O   . HOH G 6 .   ? -10.17001 -28.53233 8.93354   1.000 46.99642  ? 910 HOH A O   1 
HETATM 2824 O O   . HOH G 6 .   ? 6.80211   -39.57685 -15.03186 1.000 41.86501  ? 911 HOH A O   1 
HETATM 2825 O O   . HOH G 6 .   ? -2.31085  -45.14348 -18.47358 1.000 46.29052  ? 912 HOH A O   1 
HETATM 2826 O O   . HOH G 6 .   ? -2.22884  -49.11452 9.41698   1.000 45.34142  ? 913 HOH A O   1 
HETATM 2827 O O   . HOH G 6 .   ? 6.416     -55.093   7.332     1.000 35.62126  ? 914 HOH A O   1 
HETATM 2828 O O   . HOH G 6 .   ? 9.46122   -36.68693 10.66517  1.000 38.38859  ? 915 HOH A O   1 
HETATM 2829 O O   . HOH G 6 .   ? 3.948     -40.453   18.989    1.000 26.69124  ? 916 HOH A O   1 
HETATM 2830 O O   . HOH G 6 .   ? -8.333    -47.475   7.291     1.000 35.98606  ? 917 HOH A O   1 
HETATM 2831 O O   . HOH G 6 .   ? 13.60003  -40.24015 15.33046  1.000 47.87194  ? 918 HOH A O   1 
HETATM 2832 O O   . HOH G 6 .   ? 8.452     -56.838   11.300    1.000 28.16848  ? 919 HOH A O   1 
HETATM 2833 O O   . HOH G 6 .   ? -20.68498 -30.40175 -10.31275 1.000 36.99409  ? 920 HOH A O   1 
HETATM 2834 O O   . HOH G 6 .   ? -14.231   -34.741   -24.748   1.000 29.29934  ? 921 HOH A O   1 
HETATM 2835 O O   . HOH G 6 .   ? 8.130     -55.056   13.334    1.000 24.18638  ? 922 HOH A O   1 
HETATM 2836 O O   . HOH G 6 .   ? -3.74676  -27.90373 7.05049   1.000 48.75947  ? 923 HOH A O   1 
HETATM 2837 O O   . HOH G 6 .   ? -13.19400 -26.55050 -0.45896  1.000 30.35779  ? 924 HOH A O   1 
HETATM 2838 O O   . HOH G 6 .   ? 11.12411  -40.41134 12.41232  1.000 19.96500  ? 925 HOH A O   1 
HETATM 2839 O O   . HOH G 6 .   ? 6.067     -38.927   21.571    1.000 52.40027  ? 926 HOH A O   1 
HETATM 2840 O O   . HOH G 6 .   ? -12.24618 -28.61081 7.24660   1.000 50.80327  ? 927 HOH A O   1 
HETATM 2841 O O   . HOH G 6 .   ? -0.85331  -24.11242 0.43473   1.000 49.36413  ? 928 HOH A O   1 
HETATM 2842 O O   . HOH G 6 .   ? -14.35607 -29.15324 0.79287   1.000 38.28774  ? 929 HOH A O   1 
HETATM 2843 O O   . HOH G 6 .   ? -0.53707  -27.34945 8.77015   1.000 41.14937  ? 930 HOH A O   1 
HETATM 2844 O O   . HOH G 6 .   ? -0.76777  -23.88825 2.72727   1.000 45.73289  ? 931 HOH A O   1 
HETATM 2845 O O   . HOH G 6 .   ? 4.493     -56.834   8.030     1.000 38.56281  ? 932 HOH A O   1 
HETATM 2846 O O   . HOH G 6 .   ? -10.10167 -16.96685 -10.80985 1.000 47.61649  ? 933 HOH A O   1 
HETATM 2847 O O   . HOH G 6 .   ? -16.29977 -29.44121 -1.08253  1.000 33.77236  ? 934 HOH A O   1 
HETATM 2848 O O   . HOH G 6 .   ? -4.05199  -62.29096 -12.31984 1.000 45.72709  ? 935 HOH A O   1 
HETATM 2849 O O   . HOH H 6 .   ? 30.207    -36.765   -6.123    1.000 38.87743  ? 301 HOH B O   1 
HETATM 2850 O O   . HOH H 6 .   ? 31.46830  -43.24946 -12.69911 1.000 47.21804  ? 302 HOH B O   1 
HETATM 2851 O O   . HOH H 6 .   ? 13.42889  -41.89380 -0.79268  1.000 24.72950  ? 303 HOH B O   1 
HETATM 2852 O O   . HOH H 6 .   ? 16.93013  -34.09553 -17.57501 1.000 40.48733  ? 304 HOH B O   1 
HETATM 2853 O O   . HOH H 6 .   ? 26.63400  -46.09081 -12.22094 1.000 34.91772  ? 305 HOH B O   1 
HETATM 2854 O O   . HOH H 6 .   ? 10.38065  -45.59512 -3.49603  1.000 20.17386  ? 306 HOH B O   1 
HETATM 2855 O O   . HOH H 6 .   ? 13.52908  -44.07646 -16.01153 1.000 33.40261  ? 307 HOH B O   1 
HETATM 2856 O O   . HOH H 6 .   ? 27.05834  -34.19455 3.53026   1.000 39.21314  ? 308 HOH B O   1 
HETATM 2857 O O   . HOH H 6 .   ? 22.88593  -49.53926 11.89935  1.000 21.94973  ? 309 HOH B O   1 
HETATM 2858 O O   . HOH H 6 .   ? 0.27003   -63.09115 -0.76032  1.000 23.65282  ? 310 HOH B O   1 
HETATM 2859 O O   . HOH H 6 .   ? 24.55009  -42.66258 -1.11119  1.000 36.96527  ? 311 HOH B O   1 
HETATM 2860 O O   . HOH H 6 .   ? 14.42514  -37.46300 -11.41994 1.000 17.77808  ? 312 HOH B O   1 
HETATM 2861 O O   . HOH H 6 .   ? 29.08506  -43.57893 5.73908   1.000 48.73475  ? 313 HOH B O   1 
HETATM 2862 O O   . HOH H 6 .   ? 21.41008  -59.56237 12.48029  1.000 25.93240  ? 314 HOH B O   1 
HETATM 2863 O O   . HOH H 6 .   ? 22.25432  -47.84447 -14.73615 1.000 22.01810  ? 315 HOH B O   1 
HETATM 2864 O O   . HOH H 6 .   ? 26.95203  -49.12553 7.38183   1.000 23.17426  ? 316 HOH B O   1 
HETATM 2865 O O   . HOH H 6 .   ? 16.49330  -71.72471 0.25284   1.000 43.07472  ? 317 HOH B O   1 
HETATM 2866 O O   . HOH H 6 .   ? 32.21526  -43.65048 -0.81284  1.000 50.27739  ? 318 HOH B O   1 
HETATM 2867 O O   . HOH H 6 .   ? 28.70550  -48.40633 5.15811   1.000 27.12591  ? 319 HOH B O   1 
HETATM 2868 O O   . HOH H 6 .   ? 17.46692  -62.24970 7.21775   1.000 23.05844  ? 320 HOH B O   1 
HETATM 2869 O O   . HOH H 6 .   ? 30.20546  -65.18074 4.13363   1.000 25.89264  ? 321 HOH B O   1 
HETATM 2870 O O   . HOH H 6 .   ? 9.45304   -59.87097 -6.36561  1.000 32.64344  ? 322 HOH B O   1 
HETATM 2871 O O   . HOH H 6 .   ? 21.95559  -35.75567 -21.59142 1.000 42.83893  ? 323 HOH B O   1 
HETATM 2872 O O   . HOH H 6 .   ? 29.10846  -52.62540 0.75371   1.000 20.32995  ? 324 HOH B O   1 
HETATM 2873 O O   . HOH H 6 .   ? 11.34633  -52.87724 -11.27740 1.000 30.77992  ? 325 HOH B O   1 
HETATM 2874 O O   . HOH H 6 .   ? 11.24315  -30.40890 -11.52823 1.000 40.17855  ? 326 HOH B O   1 
HETATM 2875 O O   . HOH H 6 .   ? 26.15859  -42.99335 -14.10726 1.000 28.42875  ? 327 HOH B O   1 
HETATM 2876 O O   . HOH H 6 .   ? 14.41177  -63.07060 2.27909   1.000 20.85646  ? 328 HOH B O   1 
HETATM 2877 O O   . HOH H 6 .   ? 7.60135   -66.79771 -1.82825  1.000 32.99576  ? 329 HOH B O   1 
HETATM 2878 O O   . HOH H 6 .   ? 25.44515  -54.41282 9.21196   1.000 21.24354  ? 330 HOH B O   1 
HETATM 2879 O O   . HOH H 6 .   ? 32.24960  -50.64691 -0.97544  1.000 31.78832  ? 331 HOH B O   1 
HETATM 2880 O O   . HOH H 6 .   ? 16.81541  -51.51026 -14.84078 1.000 17.76265  ? 332 HOH B O   1 
HETATM 2881 O O   . HOH H 6 .   ? 18.28411  -43.60115 4.40003   1.000 25.36956  ? 333 HOH B O   1 
HETATM 2882 O O   . HOH H 6 .   ? 12.05220  -46.36849 -1.18079  1.000 17.24679  ? 334 HOH B O   1 
HETATM 2883 O O   . HOH H 6 .   ? 24.55618  -37.29081 -11.14790 1.000 23.90329  ? 335 HOH B O   1 
HETATM 2884 O O   . HOH H 6 .   ? 26.49608  -52.15562 10.47938  1.000 31.04348  ? 336 HOH B O   1 
HETATM 2885 O O   . HOH H 6 .   ? 19.32436  -68.27800 -7.74682  1.000 23.95088  ? 337 HOH B O   1 
HETATM 2886 O O   . HOH H 6 .   ? 28.73610  -49.73625 -11.27822 1.000 26.33110  ? 338 HOH B O   1 
HETATM 2887 O O   . HOH H 6 .   ? 26.92751  -38.08529 -9.87552  1.000 23.06373  ? 339 HOH B O   1 
HETATM 2888 O O   . HOH H 6 .   ? 13.88623  -34.75491 -11.23800 1.000 18.28347  ? 340 HOH B O   1 
HETATM 2889 O O   . HOH H 6 .   ? 13.15783  -66.70761 1.86891   1.000 32.09686  ? 341 HOH B O   1 
HETATM 2890 O O   . HOH H 6 .   ? 26.06047  -41.65407 1.04844   1.000 34.43588  ? 342 HOH B O   1 
HETATM 2891 O O   . HOH H 6 .   ? 27.64874  -61.22212 -6.18931  1.000 23.72706  ? 343 HOH B O   1 
HETATM 2892 O O   . HOH H 6 .   ? 28.89260  -57.20916 5.21099   1.000 25.44518  ? 344 HOH B O   1 
HETATM 2893 O O   . HOH H 6 .   ? 21.88871  -56.47990 -14.86815 1.000 14.02014  ? 345 HOH B O   1 
HETATM 2894 O O   . HOH H 6 .   ? 21.79193  -36.04768 -1.31777  1.000 29.20440  ? 346 HOH B O   1 
HETATM 2895 O O   . HOH H 6 .   ? 5.04166   -55.90902 -1.55198  1.000 17.69345  ? 347 HOH B O   1 
HETATM 2896 O O   . HOH H 6 .   ? 20.54056  -29.35261 -13.29386 1.000 21.82460  ? 348 HOH B O   1 
HETATM 2897 O O   . HOH H 6 .   ? 29.83684  -58.10006 11.76041  1.000 41.39416  ? 349 HOH B O   1 
HETATM 2898 O O   . HOH H 6 .   ? 21.40788  -44.53325 11.12785  1.000 31.60521  ? 350 HOH B O   1 
HETATM 2899 O O   . HOH H 6 .   ? 15.18076  -47.39513 -12.94915 1.000 23.16570  ? 351 HOH B O   1 
HETATM 2900 O O   . HOH H 6 .   ? 30.73194  -51.27474 -9.88556  1.000 34.52033  ? 352 HOH B O   1 
HETATM 2901 O O   . HOH H 6 .   ? 19.18065  -36.69103 1.39889   1.000 32.09882  ? 353 HOH B O   1 
HETATM 2902 O O   . HOH H 6 .   ? 24.72648  -52.84129 -11.45926 1.000 20.08042  ? 354 HOH B O   1 
HETATM 2903 O O   . HOH H 6 .   ? 7.983     -56.102   5.376     1.000 27.84686  ? 355 HOH B O   1 
HETATM 2904 O O   . HOH H 6 .   ? 14.14781  -26.49353 -12.11055 1.000 34.30340  ? 356 HOH B O   1 
HETATM 2905 O O   . HOH H 6 .   ? 1.98237   -62.74274 2.37919   1.000 38.98426  ? 357 HOH B O   1 
HETATM 2906 O O   . HOH H 6 .   ? 26.421    -49.683   14.017    1.000 24.50366  ? 358 HOH B O   1 
HETATM 2907 O O   . HOH H 6 .   ? 11.98585  -61.45795 2.68926   1.000 42.03572  ? 359 HOH B O   1 
HETATM 2908 O O   . HOH H 6 .   ? 22.57798  -33.32778 -13.53815 1.000 30.99636  ? 360 HOH B O   1 
HETATM 2909 O O   . HOH H 6 .   ? 12.98163  -55.26551 7.66134   1.000 23.18306  ? 361 HOH B O   1 
HETATM 2910 O O   . HOH H 6 .   ? 29.16839  -53.24000 -10.03288 1.000 39.81979  ? 362 HOH B O   1 
HETATM 2911 O O   . HOH H 6 .   ? 24.234    -59.996   -12.111   1.000 19.44895  ? 363 HOH B O   1 
HETATM 2912 O O   . HOH H 6 .   ? 19.94595  -56.86201 14.95241  1.000 37.08910  ? 364 HOH B O   1 
HETATM 2913 O O   . HOH H 6 .   ? 21.87735  -62.07780 11.42423  1.000 28.08515  ? 365 HOH B O   1 
HETATM 2914 O O   . HOH H 6 .   ? 13.91852  -58.78531 7.73520   1.000 41.76568  ? 366 HOH B O   1 
HETATM 2915 O O   . HOH H 6 .   ? 34.44322  -46.75265 -2.73416  1.000 38.55762  ? 367 HOH B O   1 
HETATM 2916 O O   . HOH H 6 .   ? 19.04108  -63.28164 10.85480  1.000 28.60213  ? 368 HOH B O   1 
HETATM 2917 O O   . HOH H 6 .   ? 26.63135  -74.55519 3.78333   1.000 42.71855  ? 369 HOH B O   1 
HETATM 2918 O O   . HOH H 6 .   ? 24.21484  -37.76239 -4.97394  1.000 22.15007  ? 370 HOH B O   1 
HETATM 2919 O O   . HOH H 6 .   ? 7.10170   -52.83952 2.70872   1.000 18.67062  ? 371 HOH B O   1 
HETATM 2920 O O   . HOH H 6 .   ? 13.23272  -33.92783 -3.60040  1.000 17.30201  ? 372 HOH B O   1 
HETATM 2921 O O   . HOH H 6 .   ? 16.38177  -25.98028 -15.06211 1.000 46.59644  ? 373 HOH B O   1 
HETATM 2922 O O   . HOH H 6 .   ? 24.52775  -47.78412 10.61085  1.000 26.44753  ? 374 HOH B O   1 
HETATM 2923 O O   . HOH H 6 .   ? 16.88176  -39.17928 2.99583   1.000 30.80460  ? 375 HOH B O   1 
HETATM 2924 O O   . HOH H 6 .   ? 14.22352  -51.08390 -13.66699 1.000 22.80017  ? 376 HOH B O   1 
HETATM 2925 O O   . HOH H 6 .   ? 24.41504  -68.40698 -9.35089  1.000 33.61981  ? 377 HOH B O   1 
HETATM 2926 O O   . HOH H 6 .   ? 29.38155  -59.16435 -7.63088  1.000 47.82484  ? 378 HOH B O   1 
HETATM 2927 O O   . HOH H 6 .   ? 12.70054  -65.60789 -4.16593  1.000 24.53871  ? 379 HOH B O   1 
HETATM 2928 O O   . HOH H 6 .   ? 3.98982   -61.19573 3.88347   1.000 39.17489  ? 380 HOH B O   1 
HETATM 2929 O O   . HOH H 6 .   ? 29.37537  -45.48629 2.03503   1.000 25.72578  ? 381 HOH B O   1 
HETATM 2930 O O   . HOH H 6 .   ? 22.41685  -39.94491 -0.54571  1.000 27.39907  ? 382 HOH B O   1 
HETATM 2931 O O   . HOH H 6 .   ? 33.01118  -58.28981 3.38556   1.000 36.19467  ? 383 HOH B O   1 
HETATM 2932 O O   . HOH H 6 .   ? 24.88379  -44.08196 9.89981   1.000 31.24853  ? 384 HOH B O   1 
HETATM 2933 O O   . HOH H 6 .   ? 28.90919  -61.75373 8.68440   1.000 34.71213  ? 385 HOH B O   1 
HETATM 2934 O O   . HOH H 6 .   ? 31.09320  -61.51910 -2.10844  1.000 35.92927  ? 386 HOH B O   1 
HETATM 2935 O O   . HOH H 6 .   ? 21.11420  -71.84717 -3.82605  1.000 27.60163  ? 387 HOH B O   1 
HETATM 2936 O O   . HOH H 6 .   ? 12.42288  -33.86214 -13.36328 1.000 39.90034  ? 388 HOH B O   1 
HETATM 2937 O O   . HOH H 6 .   ? 12.91321  -28.00235 -9.90319  1.000 25.46759  ? 389 HOH B O   1 
HETATM 2938 O O   . HOH H 6 .   ? 24.91660  -68.70576 7.58171   1.000 45.54958  ? 390 HOH B O   1 
HETATM 2939 O O   . HOH H 6 .   ? 26.38396  -44.65654 8.82460   1.000 49.56039  ? 391 HOH B O   1 
HETATM 2940 O O   . HOH H 6 .   ? 30.50138  -67.55270 -1.10984  1.000 38.19805  ? 392 HOH B O   1 
HETATM 2941 O O   . HOH H 6 .   ? 32.94130  -58.57881 -2.61958  1.000 39.80094  ? 393 HOH B O   1 
HETATM 2942 O O   . HOH H 6 .   ? 24.33987  -58.21299 14.82489  1.000 36.19253  ? 394 HOH B O   1 
HETATM 2943 O O   . HOH H 6 .   ? 10.60616  -54.77467 6.51203   1.000 37.86933  ? 395 HOH B O   1 
HETATM 2944 O O   . HOH H 6 .   ? 30.75183  -59.95169 7.68398   1.000 44.95034  ? 396 HOH B O   1 
HETATM 2945 O O   . HOH H 6 .   ? 9.75834   -60.78418 1.37726   1.000 29.83813  ? 397 HOH B O   1 
HETATM 2946 O O   . HOH H 6 .   ? 3.48416   -58.10521 -1.76786  1.000 24.80654  ? 398 HOH B O   1 
HETATM 2947 O O   . HOH H 6 .   ? 27.188    -55.631   -14.520   1.000 41.50079  ? 399 HOH B O   1 
HETATM 2948 O O   . HOH H 6 .   ? 22.36764  -42.07385 -0.98000  1.000 42.13436  ? 400 HOH B O   1 
HETATM 2949 O O   . HOH H 6 .   ? 6.76699   -61.37505 -5.79827  1.000 38.94438  ? 401 HOH B O   1 
HETATM 2950 O O   . HOH H 6 .   ? 14.18239  -44.93961 -1.96432  1.000 26.24891  ? 402 HOH B O   1 
HETATM 2951 O O   . HOH H 6 .   ? 14.41920  -70.48858 1.83940   1.000 49.70480  ? 403 HOH B O   1 
HETATM 2952 O O   . HOH H 6 .   ? 9.32907   -61.71418 -5.92337  1.000 36.35183  ? 404 HOH B O   1 
HETATM 2953 O O   . HOH H 6 .   ? 19.87679  -72.97186 -5.99630  1.000 46.26362  ? 405 HOH B O   1 
HETATM 2954 O O   . HOH H 6 .   ? 18.12938  -44.27036 10.75620  1.000 9.12588   ? 406 HOH B O   1 
HETATM 2955 O O   . HOH H 6 .   ? 26.47705  -67.13954 -7.94390  1.000 44.79076  ? 407 HOH B O   1 
HETATM 2956 O O   . HOH H 6 .   ? 23.48289  -63.64351 12.77175  1.000 46.79770  ? 408 HOH B O   1 
HETATM 2957 O O   . HOH H 6 .   ? 31.49408  -55.66561 4.15269   1.000 37.95246  ? 409 HOH B O   1 
HETATM 2958 O O   . HOH H 6 .   ? 20.921    -73.629   -8.422    1.000 43.30905  ? 410 HOH B O   1 
HETATM 2959 O O   . HOH H 6 .   ? 13.30367  -46.39658 -14.49074 1.000 31.71677  ? 411 HOH B O   1 
HETATM 2960 O O   . HOH H 6 .   ? 14.75418  -57.77856 13.60277  1.000 37.45899  ? 412 HOH B O   1 
HETATM 2961 O O   . HOH H 6 .   ? 13.95823  -70.22628 4.55929   1.000 43.53592  ? 413 HOH B O   1 
HETATM 2962 O O   . HOH H 6 .   ? 31.26412  -53.65187 2.18761   1.000 28.24990  ? 414 HOH B O   1 
HETATM 2963 O O   . HOH H 6 .   ? 28.284    -50.261   9.015     1.000 46.68209  ? 415 HOH B O   1 
HETATM 2964 O O   . HOH H 6 .   ? 25.41679  -51.86886 -13.98905 1.000 33.65603  ? 416 HOH B O   1 
HETATM 2965 O O   . HOH H 6 .   ? 25.95815  -56.23299 14.96108  1.000 42.59190  ? 417 HOH B O   1 
HETATM 2966 O O   . HOH H 6 .   ? 22.54661  -70.80780 7.68890   1.000 45.46827  ? 418 HOH B O   1 
HETATM 2967 O O   . HOH H 6 .   ? 29.01377  -45.86671 4.50029   1.000 49.30021  ? 419 HOH B O   1 
HETATM 2968 O O   . HOH H 6 .   ? 24.28983  -49.37119 -15.28954 1.000 31.18886  ? 420 HOH B O   1 
HETATM 2969 O O   . HOH H 6 .   ? 28.77714  -42.65109 1.71513   1.000 42.82492  ? 421 HOH B O   1 
HETATM 2970 O O   . HOH H 6 .   ? 26.16546  -47.59360 -14.96593 1.000 43.56287  ? 422 HOH B O   1 
HETATM 2971 O O   . HOH H 6 .   ? 12.45816  -58.90063 10.21289  1.000 41.84367  ? 423 HOH B O   1 
HETATM 2972 O O   . HOH H 6 .   ? 20.12093  -34.82939 -0.21876  1.000 47.29677  ? 424 HOH B O   1 
HETATM 2973 O O   . HOH H 6 .   ? 29.40004  -63.43105 -6.43152  1.000 44.87670  ? 425 HOH B O   1 
HETATM 2974 O O   . HOH H 6 .   ? 16.17256  -35.70534 0.78980   1.000 45.26148  ? 426 HOH B O   1 
HETATM 2975 O O   . HOH H 6 .   ? 31.16914  -49.61299 5.60345   1.000 42.76416  ? 427 HOH B O   1 
HETATM 2976 O O   . HOH H 6 .   ? 19.52321  -70.32225 9.02857   1.000 42.82109  ? 428 HOH B O   1 
HETATM 2977 O O   . HOH H 6 .   ? 28.43403  -66.18420 -7.22470  1.000 49.33986  ? 429 HOH B 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   . THR A 4   ? 1.02992 1.05937 1.04809 0.09785  0.03969  0.14385  333 THR A N   
2    C CA  . THR A 4   ? 1.00995 1.03858 1.01471 0.08712  0.03994  0.14384  333 THR A CA  
3    C C   . THR A 4   ? 0.92994 0.95972 0.91319 0.06429  0.04266  0.13962  333 THR A C   
4    O O   . THR A 4   ? 0.94410 0.97921 0.93494 0.07647  0.04689  0.13651  333 THR A O   
5    C CB  . THR A 4   ? 1.05439 1.08334 1.05589 0.08360  0.03884  0.15012  333 THR A CB  
6    O OG1 . THR A 4   ? 1.06991 1.10470 1.07481 0.08579  0.04132  0.14485  333 THR A OG1 
7    C CG2 . THR A 4   ? 1.06864 1.09216 1.06055 0.07713  0.04104  0.15411  333 THR A CG2 
8    N N   . ASN A 5   ? 0.82232 0.84404 0.76953 0.02447  0.04499  0.14735  334 ASN A N   
9    C CA  . ASN A 5   ? 0.72150 0.73888 0.63846 -0.00630 0.04323  0.14161  334 ASN A CA  
10   C C   . ASN A 5   ? 0.64499 0.65628 0.52620 -0.02903 0.03894  0.15879  334 ASN A C   
11   O O   . ASN A 5   ? 0.61200 0.59653 0.44101 -0.05022 0.05136  0.21659  334 ASN A O   
12   C CB  . ASN A 5   ? 0.71433 0.73333 0.65047 0.00019  0.04164  0.11975  334 ASN A CB  
13   C CG  . ASN A 5   ? 0.71390 0.74649 0.68480 0.02815  0.03437  0.11518  334 ASN A CG  
14   O OD1 . ASN A 5   ? 0.71989 0.75711 0.70642 0.03339  0.03506  0.10529  334 ASN A OD1 
15   N ND2 . ASN A 5   ? 0.71048 0.75657 0.68334 0.03309  0.03558  0.12195  334 ASN A ND2 
16   N N   . LEU A 6   ? 0.63031 0.65358 0.52128 -0.00669 0.03100  0.14298  335 LEU A N   
17   C CA  . LEU A 6   ? 0.62405 0.66243 0.55744 0.04069  0.02425  0.11722  335 LEU A CA  
18   C C   . LEU A 6   ? 0.56237 0.60120 0.50012 0.04938  0.03062  0.12575  335 LEU A C   
19   O O   . LEU A 6   ? 0.55214 0.59287 0.45591 0.04067  0.06927  0.17418  335 LEU A O   
20   C CB  . LEU A 6   ? 0.67898 0.71916 0.61868 0.06783  0.01967  0.10169  335 LEU A CB  
21   C CG  . LEU A 6   ? 0.72244 0.76787 0.66331 0.07443  0.01613  0.09486  335 LEU A CG  
22   C CD1 . LEU A 6   ? 0.73410 0.76951 0.66876 0.06929  0.02007  0.08863  335 LEU A CD1 
23   C CD2 . LEU A 6   ? 0.74445 0.78999 0.69624 0.08656  0.01660  0.09285  335 LEU A CD2 
24   N N   . CYS A 7   ? 0.48409 0.51022 0.39218 0.03675  0.03389  0.15617  336 CYS A N   
25   C CA  . CYS A 7   ? 0.41973 0.45257 0.33278 0.04941  0.00183  0.13466  336 CYS A CA  
26   C C   . CYS A 7   ? 0.41010 0.42328 0.32488 0.02305  0.00778  0.12710  336 CYS A C   
27   O O   . CYS A 7   ? 0.42822 0.44660 0.27453 0.03975  0.02481  0.14844  336 CYS A O   
28   C CB  . CYS A 7   ? 0.33455 0.44013 0.32576 0.04180  0.04246  0.15481  336 CYS A CB  
29   S SG  . CYS A 7   ? 0.29845 0.42562 0.35170 0.00413  0.03025  0.18849  336 CYS A SG  
30   N N   . PRO A 8   ? 0.37214 0.40821 0.30890 0.01706  0.04004  0.11730  337 PRO A N   
31   C CA  . PRO A 8   ? 0.35030 0.39987 0.32984 0.01613  0.04818  0.09541  337 PRO A CA  
32   C C   . PRO A 8   ? 0.34871 0.39796 0.26781 0.01621  0.05321  0.08321  337 PRO A C   
33   O O   . PRO A 8   ? 0.34021 0.38642 0.30740 0.01044  0.03299  0.09207  337 PRO A O   
34   C CB  . PRO A 8   ? 0.36817 0.41549 0.36422 0.01493  0.04469  0.08892  337 PRO A CB  
35   C CG  . PRO A 8   ? 0.37212 0.41787 0.39814 0.02243  0.01299  0.06145  337 PRO A CG  
36   C CD  . PRO A 8   ? 0.37265 0.40831 0.34845 0.01868  0.03533  0.11225  337 PRO A CD  
37   N N   . PHE A 9   ? 0.36803 0.37728 0.25144 -0.00719 0.05626  0.10302  338 PHE A N   
38   C CA  . PHE A 9   ? 0.34178 0.37176 0.25858 -0.00276 0.05305  0.11334  338 PHE A CA  
39   C C   . PHE A 9   ? 0.31736 0.37575 0.24340 -0.00145 0.04499  0.04577  338 PHE A C   
40   O O   . PHE A 9   ? 0.28664 0.38408 0.25505 0.02351  0.05864  0.09964  338 PHE A O   
41   C CB  . PHE A 9   ? 0.32375 0.35791 0.29377 0.00589  0.05421  0.09360  338 PHE A CB  
42   C CG  . PHE A 9   ? 0.36518 0.38303 0.28435 0.00900  0.03639  0.09508  338 PHE A CG  
43   C CD1 . PHE A 9   ? 0.35785 0.37439 0.32852 -0.00414 0.05095  0.06430  338 PHE A CD1 
44   C CD2 . PHE A 9   ? 0.39278 0.40945 0.35794 0.05583  0.03593  0.07053  338 PHE A CD2 
45   C CE1 . PHE A 9   ? 0.35657 0.39316 0.34159 -0.00362 0.08241  0.08066  338 PHE A CE1 
46   C CE2 . PHE A 9   ? 0.39922 0.38790 0.36613 0.05566  0.01534  0.07093  338 PHE A CE2 
47   C CZ  . PHE A 9   ? 0.38078 0.40597 0.37640 0.02676  0.06697  0.07802  338 PHE A CZ  
48   N N   . GLY A 10  ? 0.37793 0.39663 0.25160 0.03237  0.03715  0.02040  339 GLY A N   
49   C CA  . GLY A 10  ? 0.36675 0.39447 0.26903 0.02013  0.05103  0.05834  339 GLY A CA  
50   C C   . GLY A 10  ? 0.36240 0.38547 0.20241 0.00674  0.05641  0.02175  339 GLY A C   
51   O O   . GLY A 10  ? 0.36184 0.39984 0.21277 0.05534  0.06747  0.04745  339 GLY A O   
52   N N   . GLU A 11  ? 0.34434 0.41939 0.21761 0.00815  0.05450  0.04977  340 GLU A N   
53   C CA  . GLU A 11  ? 0.36228 0.43557 0.26411 0.02264  0.04384  0.05687  340 GLU A CA  
54   C C   . GLU A 11  ? 0.32448 0.40869 0.24823 0.02717  0.08866  0.05839  340 GLU A C   
55   O O   . GLU A 11  ? 0.31922 0.45932 0.27524 0.06542  0.08402  0.04581  340 GLU A O   
56   C CB  . GLU A 11  ? 0.44493 0.48881 0.32901 0.00729  0.07324  0.11115  340 GLU A CB  
57   C CG  . GLU A 11  ? 0.54087 0.57433 0.47911 0.04197  0.04859  0.06756  340 GLU A CG  
58   C CD  . GLU A 11  ? 0.59977 0.64254 0.56680 0.06744  0.02878  0.07682  340 GLU A CD  
59   O OE1 . GLU A 11  ? 0.61972 0.66976 0.61336 0.07161  0.02670  0.06884  340 GLU A OE1 
60   O OE2 . GLU A 11  ? 0.61519 0.67269 0.61370 0.06901  0.02796  0.06807  340 GLU A OE2 
61   N N   . VAL A 12  ? 0.27299 0.36439 0.23628 -0.00308 0.06735  0.00993  341 VAL A N   
62   C CA  . VAL A 12  ? 0.27176 0.32087 0.20000 0.01345  0.05664  0.02364  341 VAL A CA  
63   C C   . VAL A 12  ? 0.22433 0.33944 0.17640 0.00410  0.04141  0.03142  341 VAL A C   
64   O O   . VAL A 12  ? 0.21937 0.35671 0.16168 0.01078  -0.00165 0.01633  341 VAL A O   
65   C CB  . VAL A 12  ? 0.28684 0.32584 0.27384 -0.00846 0.05748  -0.00831 341 VAL A CB  
66   C CG1 . VAL A 12  ? 0.27193 0.34207 0.27958 -0.01901 0.08139  -0.00612 341 VAL A CG1 
67   C CG2 . VAL A 12  ? 0.30516 0.31615 0.29960 -0.04392 0.06447  0.03048  341 VAL A CG2 
68   N N   . PHE A 13  ? 0.19762 0.31716 0.19242 0.00036  0.02308  0.04545  342 PHE A N   
69   C CA  . PHE A 13  ? 0.19459 0.30127 0.18310 0.04905  0.00358  0.01220  342 PHE A CA  
70   C C   . PHE A 13  ? 0.23656 0.34044 0.18917 0.07458  0.01139  0.02420  342 PHE A C   
71   O O   . PHE A 13  ? 0.23924 0.36356 0.19083 0.05034  -0.01148 0.00007  342 PHE A O   
72   C CB  . PHE A 13  ? 0.21889 0.31446 0.19117 0.07767  -0.02442 0.04275  342 PHE A CB  
73   C CG  . PHE A 13  ? 0.18385 0.28168 0.18926 0.04737  -0.01543 0.02316  342 PHE A CG  
74   C CD1 . PHE A 13  ? 0.21580 0.26826 0.22733 0.05688  0.00815  0.02905  342 PHE A CD1 
75   C CD2 . PHE A 13  ? 0.16605 0.29152 0.16689 0.04346  -0.00051 0.04446  342 PHE A CD2 
76   C CE1 . PHE A 13  ? 0.18180 0.29263 0.24403 0.04025  0.00504  0.01305  342 PHE A CE1 
77   C CE2 . PHE A 13  ? 0.18457 0.29768 0.20564 0.05499  -0.02038 0.03341  342 PHE A CE2 
78   C CZ  . PHE A 13  ? 0.18021 0.29854 0.21904 0.04227  -0.02945 0.01018  342 PHE A CZ  
79   N N   . ASN A 14  ? 0.23022 0.38436 0.17393 0.06144  0.00869  0.00142  343 ASN A N   
80   C CA  . ASN A 14  ? 0.27853 0.37493 0.15286 0.04802  0.02059  -0.00563 343 ASN A CA  
81   C C   . ASN A 14  ? 0.28462 0.39591 0.18857 0.08081  0.01306  -0.01364 343 ASN A C   
82   O O   . ASN A 14  ? 0.32655 0.41365 0.22216 0.08992  0.00700  -0.04273 343 ASN A O   
83   C CB  . ASN A 14  ? 0.30359 0.41945 0.20980 0.04949  0.01496  -0.00609 343 ASN A CB  
84   C CG  . ASN A 14  ? 0.36678 0.45931 0.27036 0.04629  -0.00076 0.01391  343 ASN A CG  
85   O OD1 . ASN A 14  ? 0.38382 0.48580 0.23711 0.03916  -0.03950 -0.02314 343 ASN A OD1 
86   N ND2 . ASN A 14  ? 0.39685 0.50783 0.29809 0.03052  -0.03555 0.04109  343 ASN A ND2 
87   N N   . ALA A 15  ? 0.24797 0.41743 0.18456 0.03657  0.00423  -0.00163 344 ALA A N   
88   C CA  . ALA A 15  ? 0.25336 0.41750 0.21187 0.04660  -0.00211 -0.01592 344 ALA A CA  
89   C C   . ALA A 15  ? 0.24542 0.36859 0.20464 0.05027  0.00548  0.01172  344 ALA A C   
90   O O   . ALA A 15  ? 0.26438 0.40371 0.24157 0.03968  -0.01535 0.01918  344 ALA A O   
91   C CB  . ALA A 15  ? 0.26721 0.44441 0.19214 0.02180  0.02169  0.00714  344 ALA A CB  
92   N N   . THR A 16  ? 0.32590 0.40951 0.22989 0.07403  0.01393  -0.03204 345 THR A N   
93   C CA  A THR A 16  ? 0.35356 0.42287 0.26412 0.07076  0.01301  -0.01621 345 THR A CA  
94   C CA  B THR A 16  ? 0.35366 0.42275 0.26401 0.07087  0.01291  -0.01609 345 THR A CA  
95   C C   . THR A 16  ? 0.34293 0.39809 0.25764 0.06616  0.01081  -0.00719 345 THR A C   
96   O O   . THR A 16  ? 0.32714 0.40271 0.22867 0.07579  0.02093  -0.03222 345 THR A O   
97   C CB  A THR A 16  ? 0.40131 0.46283 0.30675 0.09016  0.01912  0.00142  345 THR A CB  
98   C CB  B THR A 16  ? 0.40080 0.46165 0.30071 0.09025  0.02058  0.00561  345 THR A CB  
99   O OG1 A THR A 16  ? 0.41937 0.48353 0.32057 0.08940  0.01649  -0.02481 345 THR A OG1 
100  O OG1 B THR A 16  ? 0.41695 0.48229 0.24590 0.08698  0.03757  0.03047  345 THR A OG1 
101  C CG2 A THR A 16  ? 0.42193 0.47971 0.34649 0.08914  0.02431  0.00889  345 THR A CG2 
102  C CG2 B THR A 16  ? 0.42265 0.47370 0.35166 0.09081  0.01982  -0.00071 345 THR A CG2 
103  N N   . ARG A 17  ? 0.32148 0.42342 0.23819 0.06152  -0.02307 -0.03934 346 ARG A N   
104  C CA  A ARG A 17  ? 0.34973 0.41732 0.26795 0.06627  -0.01807 -0.02110 346 ARG A CA  
105  C CA  B ARG A 17  ? 0.34987 0.41768 0.26780 0.06676  -0.01823 -0.02153 346 ARG A CA  
106  C C   . ARG A 17  ? 0.32046 0.39082 0.25991 0.06582  0.02063  -0.00777 346 ARG A C   
107  O O   . ARG A 17  ? 0.29115 0.41417 0.23334 0.05868  0.08401  -0.03570 346 ARG A O   
108  C CB  A ARG A 17  ? 0.42363 0.47614 0.34726 0.05883  -0.01377 -0.00604 346 ARG A CB  
109  C CB  B ARG A 17  ? 0.42395 0.47805 0.34999 0.05945  -0.01335 -0.00553 346 ARG A CB  
110  C CG  A ARG A 17  ? 0.51094 0.55328 0.46162 0.05753  -0.00725 0.00461  346 ARG A CG  
111  C CG  B ARG A 17  ? 0.51190 0.55909 0.46343 0.05573  -0.00631 0.00613  346 ARG A CG  
112  C CD  A ARG A 17  ? 0.57864 0.61988 0.55623 0.05162  -0.00484 0.01088  346 ARG A CD  
113  C CD  B ARG A 17  ? 0.58182 0.62578 0.56136 0.04800  -0.00564 0.01539  346 ARG A CD  
114  N NE  A ARG A 17  ? 0.63644 0.68276 0.62983 0.06172  0.00367  0.02291  346 ARG A NE  
115  N NE  B ARG A 17  ? 0.64042 0.68563 0.63381 0.05372  -0.00365 0.02451  346 ARG A NE  
116  C CZ  A ARG A 17  ? 0.68216 0.72290 0.67785 0.05967  0.00002  0.02061  346 ARG A CZ  
117  C CZ  B ARG A 17  ? 0.68267 0.72821 0.68268 0.05785  -0.00428 0.01554  346 ARG A CZ  
118  N NH1 A ARG A 17  ? 0.70272 0.73389 0.68921 0.05197  -0.00447 0.02129  346 ARG A NH1 
119  N NH1 B ARG A 17  ? 0.70172 0.73748 0.69009 0.05477  -0.00306 0.01691  346 ARG A NH1 
120  N NH2 A ARG A 17  ? 0.68728 0.72620 0.68898 0.06107  -0.00813 0.00788  346 ARG A NH2 
121  N NH2 B ARG A 17  ? 0.69121 0.73331 0.69404 0.05707  0.00723  0.01447  346 ARG A NH2 
122  N N   . PHE A 18  ? 0.29041 0.32680 0.19894 0.08729  -0.07437 -0.03240 347 PHE A N   
123  C CA  . PHE A 18  ? 0.22134 0.25894 0.13452 0.05326  -0.04115 -0.01360 347 PHE A CA  
124  C C   . PHE A 18  ? 0.19062 0.21419 0.15269 0.03135  -0.00090 0.02834  347 PHE A C   
125  O O   . PHE A 18  ? 0.20333 0.20959 0.16371 0.02239  -0.02444 0.02061  347 PHE A O   
126  C CB  . PHE A 18  ? 0.18351 0.23408 0.19944 0.00050  -0.05710 0.02755  347 PHE A CB  
127  C CG  . PHE A 18  ? 0.19316 0.22467 0.21297 -0.00492 -0.06414 0.00475  347 PHE A CG  
128  C CD1 . PHE A 18  ? 0.19621 0.29844 0.16675 0.01673  -0.05123 0.00345  347 PHE A CD1 
129  C CD2 . PHE A 18  ? 0.19246 0.23121 0.21056 -0.00196 -0.03842 -0.00676 347 PHE A CD2 
130  C CE1 . PHE A 18  ? 0.19522 0.30934 0.18066 0.00654  -0.03043 0.02912  347 PHE A CE1 
131  C CE2 . PHE A 18  ? 0.20155 0.22638 0.23087 -0.00731 -0.01952 0.00237  347 PHE A CE2 
132  C CZ  . PHE A 18  ? 0.22281 0.27128 0.21417 -0.00230 -0.03128 0.05098  347 PHE A CZ  
133  N N   . ALA A 19  ? 0.16040 0.22110 0.13698 0.00689  0.00762  0.00505  348 ALA A N   
134  C CA  . ALA A 19  ? 0.14326 0.23752 0.11534 -0.01853 0.00365  0.04051  348 ALA A CA  
135  C C   . ALA A 19  ? 0.12324 0.18832 0.14411 -0.00437 -0.00763 -0.01254 348 ALA A C   
136  O O   . ALA A 19  ? 0.13640 0.18775 0.14499 -0.00593 -0.00053 0.00937  348 ALA A O   
137  C CB  . ALA A 19  ? 0.20239 0.22787 0.18178 -0.05427 -0.00066 0.02249  348 ALA A CB  
138  N N   . SER A 20  ? 0.13323 0.18780 0.12225 0.00571  -0.02033 0.00440  349 SER A N   
139  C CA  . SER A 20  ? 0.15152 0.17469 0.09762 0.00136  0.00210  0.00600  349 SER A CA  
140  C C   . SER A 20  ? 0.14215 0.17437 0.11569 -0.02444 0.00181  0.00357  349 SER A C   
141  O O   . SER A 20  ? 0.15080 0.17001 0.13327 -0.00643 0.00373  0.00277  349 SER A O   
142  C CB  . SER A 20  ? 0.17482 0.17008 0.11949 0.02177  -0.01767 -0.00320 349 SER A CB  
143  O OG  . SER A 20  ? 0.14876 0.16517 0.14228 0.00755  -0.00919 0.00510  349 SER A OG  
144  N N   . VAL A 21  ? 0.14488 0.17551 0.12115 0.01643  0.00574  0.00203  350 VAL A N   
145  C CA  . VAL A 21  ? 0.11903 0.16725 0.13200 0.01189  0.00558  0.00948  350 VAL A CA  
146  C C   . VAL A 21  ? 0.12457 0.15770 0.13125 -0.00806 -0.00893 0.01122  350 VAL A C   
147  O O   . VAL A 21  ? 0.14027 0.16531 0.14471 0.00416  -0.00318 -0.00115 350 VAL A O   
148  C CB  . VAL A 21  ? 0.13941 0.17338 0.12555 0.00207  -0.00650 0.00125  350 VAL A CB  
149  C CG1 . VAL A 21  ? 0.14184 0.17547 0.11957 -0.00005 0.00067  0.00982  350 VAL A CG1 
150  C CG2 . VAL A 21  ? 0.15920 0.16824 0.15700 0.00640  -0.00583 -0.01521 350 VAL A CG2 
151  N N   . TYR A 22  ? 0.12044 0.18298 0.12405 -0.00474 -0.01173 0.00415  351 TYR A N   
152  C CA  . TYR A 22  ? 0.12792 0.17686 0.14730 -0.00326 -0.01997 0.00778  351 TYR A CA  
153  C C   . TYR A 22  ? 0.12641 0.19033 0.12937 -0.00434 -0.01458 -0.00038 351 TYR A C   
154  O O   . TYR A 22  ? 0.15548 0.18458 0.15360 -0.00689 -0.01231 -0.01271 351 TYR A O   
155  C CB  . TYR A 22  ? 0.14165 0.18035 0.14177 0.01117  -0.00913 0.00385  351 TYR A CB  
156  C CG  . TYR A 22  ? 0.14148 0.20690 0.11889 -0.00142 -0.01761 0.01687  351 TYR A CG  
157  C CD1 . TYR A 22  ? 0.16083 0.21160 0.11489 0.02292  -0.00205 0.02089  351 TYR A CD1 
158  C CD2 . TYR A 22  ? 0.14654 0.21432 0.19561 -0.00794 -0.01944 0.04778  351 TYR A CD2 
159  C CE1 . TYR A 22  ? 0.17752 0.24475 0.15517 0.04466  0.01629  0.05877  351 TYR A CE1 
160  C CE2 . TYR A 22  ? 0.20051 0.26949 0.22656 0.05798  0.03188  0.08087  351 TYR A CE2 
161  C CZ  . TYR A 22  ? 0.17333 0.27524 0.21501 0.07607  0.06072  0.09172  351 TYR A CZ  
162  O OH  . TYR A 22  ? 0.16916 0.33919 0.28454 0.07174  0.04702  0.05744  351 TYR A OH  
163  N N   . ALA A 23  ? 0.13273 0.19709 0.12323 -0.00055 0.00098  0.02926  352 ALA A N   
164  C CA  . ALA A 23  ? 0.13224 0.20513 0.13393 0.00985  0.00611  0.02076  352 ALA A CA  
165  C C   . ALA A 23  ? 0.13892 0.18109 0.13162 -0.01901 -0.01392 0.02993  352 ALA A C   
166  O O   . ALA A 23  ? 0.14682 0.20719 0.12697 0.01683  0.00381  0.01549  352 ALA A O   
167  C CB  . ALA A 23  ? 0.13386 0.20846 0.16048 0.02861  0.01487  0.00930  352 ALA A CB  
168  N N   . TRP A 24  ? 0.12609 0.16796 0.15779 0.01553  -0.00248 0.02348  353 TRP A N   
169  C CA  . TRP A 24  ? 0.12887 0.18093 0.15933 0.01103  -0.01083 0.00822  353 TRP A CA  
170  C C   . TRP A 24  ? 0.12619 0.18302 0.15414 -0.01068 -0.00438 0.02319  353 TRP A C   
171  O O   . TRP A 24  ? 0.14303 0.19154 0.16583 -0.01801 -0.00064 0.01606  353 TRP A O   
172  C CB  . TRP A 24  ? 0.13665 0.17455 0.14867 0.00654  0.00054  0.00323  353 TRP A CB  
173  C CG  . TRP A 24  ? 0.13083 0.17692 0.16617 -0.01094 0.00493  0.00766  353 TRP A CG  
174  C CD1 . TRP A 24  ? 0.14010 0.18063 0.14276 0.00810  -0.00445 -0.00009 353 TRP A CD1 
175  C CD2 . TRP A 24  ? 0.15197 0.16921 0.14317 -0.00224 0.00942  0.00847  353 TRP A CD2 
176  N NE1 . TRP A 24  ? 0.15068 0.16980 0.16597 0.00347  0.01109  0.01572  353 TRP A NE1 
177  C CE2 . TRP A 24  ? 0.14402 0.15985 0.17522 -0.01380 -0.00095 0.00574  353 TRP A CE2 
178  C CE3 . TRP A 24  ? 0.13849 0.16926 0.17183 0.00931  0.01912  -0.00917 353 TRP A CE3 
179  C CZ2 . TRP A 24  ? 0.14449 0.18493 0.20674 -0.00661 0.00675  0.01251  353 TRP A CZ2 
180  C CZ3 . TRP A 24  ? 0.16640 0.17621 0.20809 -0.00157 0.03394  0.00293  353 TRP A CZ3 
181  C CH2 . TRP A 24  ? 0.15665 0.19223 0.21379 -0.00455 0.03527  -0.00002 353 TRP A CH2 
182  N N   . ASN A 25  ? 0.15601 0.20682 0.15435 0.01453  -0.01550 0.03519  354 ASN A N   
183  C CA  A ASN A 25  ? 0.16304 0.21829 0.14037 0.00858  0.01288  0.03964  354 ASN A CA  
184  C CA  B ASN A 25  ? 0.16263 0.21748 0.14133 0.00958  0.01328  0.03894  354 ASN A CA  
185  C C   . ASN A 25  ? 0.15331 0.20222 0.17122 -0.00086 -0.00644 0.02842  354 ASN A C   
186  O O   . ASN A 25  ? 0.13609 0.21289 0.18833 -0.00264 -0.01114 0.04405  354 ASN A O   
187  C CB  A ASN A 25  ? 0.20803 0.23905 0.19002 0.01662  0.00867  0.02725  354 ASN A CB  
188  C CB  B ASN A 25  ? 0.20118 0.23289 0.18956 0.03074  0.00821  0.02881  354 ASN A CB  
189  C CG  A ASN A 25  ? 0.29778 0.26514 0.24402 0.02673  0.03209  0.03924  354 ASN A CG  
190  C CG  B ASN A 25  ? 0.25158 0.23700 0.21055 0.06526  0.02200  0.06019  354 ASN A CG  
191  O OD1 A ASN A 25  ? 0.30927 0.32380 0.28361 0.06789  0.03957  0.04080  354 ASN A OD1 
192  O OD1 B ASN A 25  ? 0.24420 0.22797 0.26213 0.04044  0.04511  0.03789  354 ASN A OD1 
193  N ND2 A ASN A 25  ? 0.34559 0.30493 0.30412 0.03019  0.04170  0.04357  354 ASN A ND2 
194  N ND2 B ASN A 25  ? 0.28439 0.22993 0.20222 0.08380  0.05743  0.06334  354 ASN A ND2 
195  N N   . ARG A 26  ? 0.16203 0.19016 0.19471 0.00121  0.00586  0.03831  355 ARG A N   
196  C CA  . ARG A 26  ? 0.17748 0.19671 0.19081 -0.00823 0.01566  0.04620  355 ARG A CA  
197  C C   . ARG A 26  ? 0.15342 0.22314 0.19306 -0.02463 0.03058  0.04701  355 ARG A C   
198  O O   . ARG A 26  ? 0.16621 0.25283 0.23558 -0.01192 0.02477  0.07072  355 ARG A O   
199  C CB  . ARG A 26  ? 0.17516 0.21260 0.18730 -0.02162 0.02437  -0.00083 355 ARG A CB  
200  C CG  . ARG A 26  ? 0.20942 0.20107 0.21995 -0.00404 0.03384  0.02516  355 ARG A CG  
201  C CD  . ARG A 26  ? 0.21745 0.19624 0.27128 -0.03867 0.08182  -0.00030 355 ARG A CD  
202  N NE  . ARG A 26  ? 0.21128 0.20640 0.20634 -0.02226 0.03097  0.00530  355 ARG A NE  
203  C CZ  . ARG A 26  ? 0.21277 0.20258 0.24962 -0.03336 0.02728  0.02560  355 ARG A CZ  
204  N NH1 . ARG A 26  ? 0.26573 0.20312 0.29479 -0.05876 0.02581  0.00190  355 ARG A NH1 
205  N NH2 . ARG A 26  ? 0.25208 0.19188 0.24743 -0.01852 0.05519  0.02777  355 ARG A NH2 
206  N N   . LYS A 27  ? 0.20262 0.24267 0.17448 -0.00371 0.01186  0.06229  356 LYS A N   
207  C CA  . LYS A 27  ? 0.22185 0.27703 0.20298 -0.00801 0.03930  0.07165  356 LYS A CA  
208  C C   . LYS A 27  ? 0.20227 0.26445 0.24599 -0.00988 0.04526  0.09019  356 LYS A C   
209  O O   . LYS A 27  ? 0.19328 0.28199 0.28899 -0.00670 0.04572  0.10876  356 LYS A O   
210  C CB  . LYS A 27  ? 0.27868 0.31252 0.18323 -0.00458 0.02520  0.07188  356 LYS A CB  
211  C CG  . LYS A 27  ? 0.32789 0.35597 0.26996 0.02775  0.00321  0.07153  356 LYS A CG  
212  C CD  . LYS A 27  ? 0.37610 0.41257 0.33163 0.05898  0.04867  0.08200  356 LYS A CD  
213  C CE  . LYS A 27  ? 0.39798 0.43416 0.34820 0.03209  0.07599  0.11039  356 LYS A CE  
214  N NZ  . LYS A 27  ? 0.41364 0.48169 0.41341 0.03866  0.02100  0.04632  356 LYS A NZ  
215  N N   . ARG A 28  ? 0.22706 0.28055 0.30240 -0.03300 0.02193  0.12573  357 ARG A N   
216  C CA  . ARG A 28  ? 0.26236 0.29884 0.33247 -0.04203 0.01269  0.11664  357 ARG A CA  
217  C C   . ARG A 28  ? 0.29790 0.35187 0.30420 0.04107  0.06047  0.11247  357 ARG A C   
218  O O   . ARG A 28  ? 0.32961 0.37656 0.32736 0.05723  0.05754  0.15985  357 ARG A O   
219  C CB  . ARG A 28  ? 0.30507 0.29385 0.42420 -0.07103 0.00585  0.08216  357 ARG A CB  
220  C CG  . ARG A 28  ? 0.40079 0.38540 0.50453 -0.03537 0.02550  0.06841  357 ARG A CG  
221  C CD  . ARG A 28  ? 0.46973 0.45608 0.53823 -0.01761 0.02802  0.08037  357 ARG A CD  
222  N NE  . ARG A 28  ? 0.53292 0.52259 0.60161 0.00652  0.02909  0.08784  357 ARG A NE  
223  C CZ  . ARG A 28  ? 0.58158 0.57982 0.65541 0.02801  0.04003  0.09046  357 ARG A CZ  
224  N NH1 . ARG A 28  ? 0.58776 0.59389 0.67078 0.02979  0.03107  0.07692  357 ARG A NH1 
225  N NH2 . ARG A 28  ? 0.60700 0.59504 0.67657 0.02021  0.05136  0.09668  357 ARG A NH2 
226  N N   . ILE A 29  ? 0.27973 0.35599 0.31966 0.03100  0.06130  0.15366  358 ILE A N   
227  C CA  . ILE A 29  ? 0.30491 0.34145 0.31550 0.01258  0.02678  0.15177  358 ILE A CA  
228  C C   . ILE A 29  ? 0.31252 0.34882 0.33296 0.01425  0.05042  0.15044  358 ILE A C   
229  O O   . ILE A 29  ? 0.31318 0.36341 0.35936 0.02597  0.03469  0.17064  358 ILE A O   
230  C CB  . ILE A 29  ? 0.33861 0.33015 0.32687 0.01026  0.00539  0.13738  358 ILE A CB  
231  C CG1 . ILE A 29  ? 0.38065 0.36400 0.35359 0.04626  -0.01249 0.09295  358 ILE A CG1 
232  C CG2 . ILE A 29  ? 0.34589 0.34158 0.31748 0.04729  -0.04785 0.14125  358 ILE A CG2 
233  C CD1 . ILE A 29  ? 0.37779 0.37198 0.38935 0.03286  -0.01207 0.05593  358 ILE A CD1 
234  N N   . SER A 30  ? 0.30621 0.36050 0.35858 -0.01700 0.02624  0.16474  359 SER A N   
235  C CA  . SER A 30  ? 0.35629 0.38846 0.39210 -0.01476 0.02349  0.14561  359 SER A CA  
236  C C   . SER A 30  ? 0.33209 0.37282 0.36978 -0.04870 0.03512  0.17065  359 SER A C   
237  O O   . SER A 30  ? 0.31164 0.42361 0.39094 -0.03533 0.06065  0.17429  359 SER A O   
238  C CB  . SER A 30  ? 0.40696 0.43169 0.45917 0.01274  0.01406  0.10743  359 SER A CB  
239  O OG  . SER A 30  ? 0.45730 0.46384 0.51529 0.03284  0.01451  0.11195  359 SER A OG  
240  N N   . ASN A 31  ? 0.32886 0.36560 0.40484 -0.04734 0.02709  0.19011  360 ASN A N   
241  C CA  . ASN A 31  ? 0.36247 0.38468 0.37766 -0.04600 0.04620  0.17705  360 ASN A CA  
242  C C   . ASN A 31  ? 0.35152 0.37758 0.34450 -0.02259 0.08169  0.19180  360 ASN A C   
243  O O   . ASN A 31  ? 0.32395 0.40851 0.38537 -0.04784 0.07724  0.17375  360 ASN A O   
244  C CB  . ASN A 31  ? 0.42978 0.41610 0.41871 -0.02903 0.04745  0.18257  360 ASN A CB  
245  C CG  . ASN A 31  ? 0.48721 0.47930 0.54571 0.02467  0.04213  0.14680  360 ASN A CG  
246  O OD1 . ASN A 31  ? 0.51354 0.52133 0.59827 0.01326  0.06661  0.11827  360 ASN A OD1 
247  N ND2 . ASN A 31  ? 0.50748 0.51093 0.58913 0.03681  0.03565  0.13168  360 ASN A ND2 
248  N N   . CYS A 32  ? 0.31187 0.37895 0.35836 -0.01927 0.03678  0.17805  361 CYS A N   
249  C CA  . CYS A 32  ? 0.31991 0.40180 0.33675 -0.00500 0.05318  0.15929  361 CYS A CA  
250  C C   . CYS A 32  ? 0.33027 0.40170 0.32557 0.00990  0.03322  0.14759  361 CYS A C   
251  O O   . CYS A 32  ? 0.32233 0.40253 0.36958 -0.01352 0.01606  0.18167  361 CYS A O   
252  C CB  . CYS A 32  ? 0.30943 0.41251 0.34465 -0.00220 0.04359  0.17691  361 CYS A CB  
253  S SG  . CYS A 32  ? 0.28051 0.44385 0.35455 -0.01933 0.01746  0.20335  361 CYS A SG  
254  N N   . VAL A 33  ? 0.34497 0.38783 0.36724 -0.02161 0.03254  0.15682  362 VAL A N   
255  C CA  . VAL A 33  ? 0.39099 0.42742 0.35836 0.02133  0.00642  0.16040  362 VAL A CA  
256  C C   . VAL A 33  ? 0.40720 0.45361 0.38103 0.02783  -0.00220 0.13199  362 VAL A C   
257  O O   . VAL A 33  ? 0.39791 0.43840 0.36389 -0.03777 -0.00794 0.16312  362 VAL A O   
258  C CB  . VAL A 33  ? 0.42136 0.42982 0.37830 0.02235  -0.01436 0.18843  362 VAL A CB  
259  C CG1 . VAL A 33  ? 0.42989 0.46317 0.36524 0.02721  -0.03297 0.16389  362 VAL A CG1 
260  C CG2 . VAL A 33  ? 0.45527 0.46881 0.44767 0.03962  -0.01309 0.13100  362 VAL A CG2 
261  N N   . ALA A 34  ? 0.41720 0.45971 0.40912 0.03731  0.01026  0.16586  363 ALA A N   
262  C CA  . ALA A 34  ? 0.46515 0.50283 0.49654 0.07397  0.00671  0.12563  363 ALA A CA  
263  C C   . ALA A 34  ? 0.45725 0.49601 0.48246 0.07427  0.00788  0.11415  363 ALA A C   
264  O O   . ALA A 34  ? 0.47738 0.50883 0.56284 0.10300  0.01668  0.09860  363 ALA A O   
265  C CB  . ALA A 34  ? 0.49236 0.52197 0.51692 0.08077  -0.00212 0.13014  363 ALA A CB  
266  N N   . ASP A 35  ? 0.39007 0.43601 0.34997 0.04492  0.04753  0.14067  364 ASP A N   
267  C CA  . ASP A 35  ? 0.35695 0.38805 0.33663 0.01452  0.04589  0.14187  364 ASP A CA  
268  C C   . ASP A 35  ? 0.27977 0.32028 0.27307 0.01620  0.03680  0.11283  364 ASP A C   
269  O O   . ASP A 35  ? 0.25565 0.30963 0.29325 0.02755  0.07849  0.07855  364 ASP A O   
270  C CB  . ASP A 35  ? 0.40542 0.42826 0.34095 0.04412  0.03038  0.13762  364 ASP A CB  
271  C CG  . ASP A 35  ? 0.42343 0.47084 0.36032 0.07909  -0.01127 0.11357  364 ASP A CG  
272  O OD1 . ASP A 35  ? 0.35721 0.42482 0.24102 0.04570  0.03937  0.10374  364 ASP A OD1 
273  O OD2 . ASP A 35  ? 0.44257 0.53075 0.35450 0.06960  0.05283  0.09637  364 ASP A OD2 
274  N N   . TYR A 36  ? 0.22430 0.29037 0.27063 -0.02189 0.01374  0.06564  365 TYR A N   
275  C CA  . TYR A 36  ? 0.19508 0.25598 0.22941 -0.01311 0.00868  0.05838  365 TYR A CA  
276  C C   . TYR A 36  ? 0.18898 0.25105 0.16698 0.00745  0.00610  0.03810  365 TYR A C   
277  O O   . TYR A 36  ? 0.19113 0.22203 0.19663 0.02049  0.00184  0.03995  365 TYR A O   
278  C CB  . TYR A 36  ? 0.21042 0.24656 0.25814 -0.02234 0.01835  0.01552  365 TYR A CB  
279  C CG  . TYR A 36  ? 0.21380 0.25343 0.29430 -0.01233 -0.01580 0.05593  365 TYR A CG  
280  C CD1 . TYR A 36  ? 0.23445 0.29049 0.29037 -0.03138 -0.06322 0.04431  365 TYR A CD1 
281  C CD2 . TYR A 36  ? 0.25666 0.28699 0.34275 -0.00695 -0.04879 0.03664  365 TYR A CD2 
282  C CE1 . TYR A 36  ? 0.25622 0.31014 0.32580 -0.02945 -0.04714 0.05848  365 TYR A CE1 
283  C CE2 . TYR A 36  ? 0.28352 0.32620 0.37699 -0.01439 -0.04458 0.05515  365 TYR A CE2 
284  C CZ  . TYR A 36  ? 0.26670 0.30237 0.35903 -0.07204 -0.04949 0.03537  365 TYR A CZ  
285  O OH  . TYR A 36  ? 0.28386 0.36823 0.43583 -0.08577 -0.04716 0.04355  365 TYR A OH  
286  N N   . SER A 37  ? 0.18434 0.26913 0.18777 0.02499  0.00644  0.03808  366 SER A N   
287  C CA  . SER A 37  ? 0.20247 0.25387 0.19599 0.02072  -0.00625 0.01808  366 SER A CA  
288  C C   . SER A 37  ? 0.19927 0.27942 0.18178 0.07391  0.00947  0.02822  366 SER A C   
289  O O   . SER A 37  ? 0.19678 0.26140 0.18878 0.05359  -0.02274 0.02933  366 SER A O   
290  C CB  . SER A 37  ? 0.22103 0.30705 0.21411 0.06593  -0.01922 0.04524  366 SER A CB  
291  O OG  . SER A 37  ? 0.27409 0.31296 0.20697 0.08795  0.00109  0.02948  366 SER A OG  
292  N N   . VAL A 38  ? 0.20764 0.30854 0.16336 0.07570  0.02114  0.00921  367 VAL A N   
293  C CA  . VAL A 38  ? 0.22132 0.30720 0.19484 0.06512  0.04595  0.02195  367 VAL A CA  
294  C C   . VAL A 38  ? 0.20483 0.28555 0.19348 0.04821  0.02102  0.02830  367 VAL A C   
295  O O   . VAL A 38  ? 0.24680 0.30547 0.21179 0.05763  -0.03490 -0.00978 367 VAL A O   
296  C CB  . VAL A 38  ? 0.29449 0.36292 0.20621 0.08734  0.07078  0.03278  367 VAL A CB  
297  C CG1 . VAL A 38  ? 0.29632 0.38844 0.30847 0.11219  0.06856  -0.00965 367 VAL A CG1 
298  C CG2 . VAL A 38  ? 0.32326 0.37806 0.23846 0.09765  0.05080  0.04444  367 VAL A CG2 
299  N N   . LEU A 39  ? 0.19171 0.28246 0.17959 0.06425  -0.01202 0.01660  368 LEU A N   
300  C CA  . LEU A 39  ? 0.15733 0.26337 0.18605 0.04263  -0.02545 -0.00640 368 LEU A CA  
301  C C   . LEU A 39  ? 0.16283 0.24177 0.18951 0.08107  -0.00706 0.02279  368 LEU A C   
302  O O   . LEU A 39  ? 0.16503 0.23210 0.20398 0.06499  -0.02338 0.01124  368 LEU A O   
303  C CB  . LEU A 39  ? 0.15482 0.28214 0.19062 0.04294  -0.00290 0.00429  368 LEU A CB  
304  C CG  . LEU A 39  ? 0.16321 0.31577 0.27071 0.04047  0.00109  0.01110  368 LEU A CG  
305  C CD1 . LEU A 39  ? 0.18750 0.32646 0.28127 0.03279  -0.01416 -0.02328 368 LEU A CD1 
306  C CD2 . LEU A 39  ? 0.18225 0.34219 0.27709 0.05880  -0.01991 -0.03406 368 LEU A CD2 
307  N N   . TYR A 40  ? 0.13506 0.25147 0.17645 0.05349  -0.00432 0.02234  369 TYR A N   
308  C CA  . TYR A 40  ? 0.14507 0.21687 0.15812 0.04577  -0.02018 0.00876  369 TYR A CA  
309  C C   . TYR A 40  ? 0.17059 0.20911 0.18591 0.06057  -0.01688 0.02646  369 TYR A C   
310  O O   . TYR A 40  ? 0.18580 0.19110 0.18616 0.03565  -0.02673 0.02215  369 TYR A O   
311  C CB  . TYR A 40  ? 0.16699 0.21581 0.17996 0.06130  -0.00885 0.01347  369 TYR A CB  
312  C CG  . TYR A 40  ? 0.17136 0.19490 0.14959 0.02362  -0.01677 -0.00049 369 TYR A CG  
313  C CD1 . TYR A 40  ? 0.17148 0.22988 0.17866 0.02414  -0.02070 0.00109  369 TYR A CD1 
314  C CD2 . TYR A 40  ? 0.16298 0.21583 0.19851 0.01885  -0.02137 -0.02456 369 TYR A CD2 
315  C CE1 . TYR A 40  ? 0.14691 0.22652 0.21418 0.00115  -0.00244 -0.01779 369 TYR A CE1 
316  C CE2 . TYR A 40  ? 0.19613 0.22134 0.20378 0.03463  0.02301  -0.00644 369 TYR A CE2 
317  C CZ  . TYR A 40  ? 0.17201 0.22795 0.20188 0.02336  0.02171  -0.01816 369 TYR A CZ  
318  O OH  . TYR A 40  ? 0.16713 0.29135 0.23164 0.01700  0.03572  -0.01301 369 TYR A OH  
319  N N   . ASN A 41  ? 0.15306 0.20889 0.15566 0.03815  -0.02048 -0.01739 370 ASN A N   
320  C CA  . ASN A 41  ? 0.18968 0.19952 0.19488 0.05723  -0.03606 -0.00393 370 ASN A CA  
321  C C   . ASN A 41  ? 0.23899 0.20583 0.23016 0.05829  -0.05889 -0.03750 370 ASN A C   
322  O O   . ASN A 41  ? 0.32251 0.23867 0.30074 0.08424  -0.12299 -0.05432 370 ASN A O   
323  C CB  . ASN A 41  ? 0.19405 0.22867 0.17360 0.08156  -0.01436 -0.00396 370 ASN A CB  
324  C CG  . ASN A 41  ? 0.17803 0.26397 0.16064 0.05707  -0.02167 -0.01399 370 ASN A CG  
325  O OD1 . ASN A 41  ? 0.18656 0.24727 0.19330 0.05901  0.01290  0.01712  370 ASN A OD1 
326  N ND2 . ASN A 41  ? 0.19739 0.27879 0.16860 0.06075  0.00703  0.00737  370 ASN A ND2 
327  N N   . SER A 42  ? 0.19462 0.23483 0.20604 0.08938  -0.00969 -0.01071 371 SER A N   
328  C CA  . SER A 42  ? 0.20614 0.22907 0.19817 0.04871  0.00172  0.00872  371 SER A CA  
329  C C   . SER A 42  ? 0.22364 0.23531 0.16552 0.07304  0.00972  0.00871  371 SER A C   
330  O O   . SER A 42  ? 0.28870 0.24406 0.18785 0.07311  0.01097  0.02229  371 SER A O   
331  C CB  . SER A 42  ? 0.24108 0.24026 0.26455 0.11684  -0.01613 0.00624  371 SER A CB  
332  O OG  . SER A 42  ? 0.29860 0.27574 0.30948 0.13852  -0.01419 -0.00584 371 SER A OG  
333  N N   . ALA A 43  ? 0.18340 0.23605 0.22444 0.04111  -0.02738 -0.00288 372 ALA A N   
334  C CA  . ALA A 43  ? 0.23237 0.25284 0.21935 0.02015  -0.07338 -0.02426 372 ALA A CA  
335  C C   . ALA A 43  ? 0.24108 0.21779 0.17874 0.01652  -0.04222 -0.00020 372 ALA A C   
336  O O   . ALA A 43  ? 0.25586 0.31481 0.27340 -0.02746 -0.08042 0.04675  372 ALA A O   
337  C CB  . ALA A 43  ? 0.24390 0.29899 0.28136 0.01497  -0.09934 0.02714  372 ALA A CB  
338  N N   . SER A 44  ? 0.20933 0.21986 0.21875 0.06887  -0.04549 -0.03202 373 SER A N   
339  C CA  A SER A 44  ? 0.23985 0.25879 0.25518 0.07682  -0.09095 -0.03771 373 SER A CA  
340  C CA  B SER A 44  ? 0.24046 0.26139 0.25583 0.07363  -0.09077 -0.03728 373 SER A CA  
341  C C   . SER A 44  ? 0.23801 0.22905 0.24656 0.06955  -0.11927 -0.04193 373 SER A C   
342  O O   . SER A 44  ? 0.33497 0.25793 0.30422 0.07495  -0.17997 -0.02584 373 SER A O   
343  C CB  A SER A 44  ? 0.26109 0.31670 0.29410 0.11578  -0.06363 -0.03147 373 SER A CB  
344  C CB  B SER A 44  ? 0.27128 0.33664 0.30251 0.09810  -0.06256 -0.01821 373 SER A CB  
345  O OG  A SER A 44  ? 0.27019 0.36351 0.30303 0.15584  -0.03285 -0.05432 373 SER A OG  
346  O OG  B SER A 44  ? 0.31611 0.40477 0.36628 0.11866  -0.03640 0.03373  373 SER A OG  
347  N N   . PHE A 45  ? 0.18580 0.22462 0.18387 0.04942  -0.05110 -0.02643 374 PHE A N   
348  C CA  . PHE A 45  ? 0.15824 0.23912 0.19150 0.03949  -0.02198 -0.01204 374 PHE A CA  
349  C C   . PHE A 45  ? 0.18057 0.28637 0.20337 0.06633  -0.03428 0.00802  374 PHE A C   
350  O O   . PHE A 45  ? 0.19476 0.37985 0.27450 0.08392  -0.02790 0.02526  374 PHE A O   
351  C CB  . PHE A 45  ? 0.17448 0.22196 0.20046 0.03339  -0.03451 -0.02291 374 PHE A CB  
352  C CG  . PHE A 45  ? 0.16323 0.22911 0.17993 0.02894  -0.03553 -0.01545 374 PHE A CG  
353  C CD1 . PHE A 45  ? 0.16891 0.26269 0.20624 0.03234  -0.02411 0.00556  374 PHE A CD1 
354  C CD2 . PHE A 45  ? 0.22359 0.27057 0.19967 0.06677  -0.00137 0.03736  374 PHE A CD2 
355  C CE1 . PHE A 45  ? 0.17878 0.27138 0.18804 0.01946  -0.03667 -0.00040 374 PHE A CE1 
356  C CE2 . PHE A 45  ? 0.22235 0.30698 0.22262 0.04792  -0.03471 0.02622  374 PHE A CE2 
357  C CZ  . PHE A 45  ? 0.18180 0.27841 0.20237 0.01012  -0.04552 0.01371  374 PHE A CZ  
358  N N   . SER A 46  ? 0.17765 0.21533 0.22883 0.00144  -0.02155 -0.03017 375 SER A N   
359  C CA  . SER A 46  ? 0.20269 0.22711 0.26230 0.00405  0.01251  -0.03416 375 SER A CA  
360  C C   . SER A 46  ? 0.17398 0.23932 0.23073 0.00624  0.01183  -0.01445 375 SER A C   
361  O O   . SER A 46  ? 0.19393 0.27909 0.28888 -0.02443 0.03748  -0.04656 375 SER A O   
362  C CB  . SER A 46  ? 0.20492 0.23628 0.28715 -0.01528 -0.01229 -0.00983 375 SER A CB  
363  O OG  . SER A 46  ? 0.21664 0.23436 0.26439 -0.00436 -0.00741 -0.00235 375 SER A OG  
364  N N   . THR A 47  ? 0.14840 0.19250 0.21310 0.01174  -0.03430 -0.01857 376 THR A N   
365  C CA  . THR A 47  ? 0.17488 0.18912 0.16801 0.01220  -0.02277 0.00593  376 THR A CA  
366  C C   . THR A 47  ? 0.13133 0.18956 0.19076 0.02164  -0.02751 0.00567  376 THR A C   
367  O O   . THR A 47  ? 0.13526 0.19393 0.18939 0.01684  -0.02327 -0.00530 376 THR A O   
368  C CB  . THR A 47  ? 0.21406 0.20430 0.16129 0.01646  -0.02174 0.04455  376 THR A CB  
369  O OG1 . THR A 47  ? 0.20448 0.26044 0.18450 0.01482  -0.03228 0.02295  376 THR A OG1 
370  C CG2 . THR A 47  ? 0.21019 0.22769 0.20017 0.01580  -0.02676 -0.00152 376 THR A CG2 
371  N N   . PHE A 48  ? 0.14168 0.19572 0.17946 0.01639  -0.02103 0.01042  377 PHE A N   
372  C CA  . PHE A 48  ? 0.18126 0.19636 0.13419 0.02101  -0.01122 0.01059  377 PHE A CA  
373  C C   . PHE A 48  ? 0.14948 0.19040 0.15928 0.03385  -0.03059 0.00410  377 PHE A C   
374  O O   . PHE A 48  ? 0.15280 0.21011 0.21677 0.04284  -0.03637 0.00281  377 PHE A O   
375  C CB  . PHE A 48  ? 0.20950 0.21545 0.17343 0.02622  -0.01391 0.02752  377 PHE A CB  
376  C CG  . PHE A 48  ? 0.18184 0.26319 0.14332 0.02799  -0.04248 0.03387  377 PHE A CG  
377  C CD1 . PHE A 48  ? 0.20721 0.23749 0.22010 -0.01718 -0.05057 0.04677  377 PHE A CD1 
378  C CD2 . PHE A 48  ? 0.21784 0.31856 0.15037 -0.00293 -0.05897 0.01822  377 PHE A CD2 
379  C CE1 . PHE A 48  ? 0.24683 0.31425 0.15990 -0.03438 -0.04032 0.04052  377 PHE A CE1 
380  C CE2 . PHE A 48  ? 0.23605 0.34072 0.19836 -0.02534 -0.01765 0.06471  377 PHE A CE2 
381  C CZ  . PHE A 48  ? 0.24390 0.35451 0.16689 -0.05671 -0.06377 0.04038  377 PHE A CZ  
382  N N   . LYS A 49  ? 0.14845 0.19245 0.15270 0.02350  -0.01582 0.00684  378 LYS A N   
383  C CA  . LYS A 49  ? 0.16395 0.20853 0.17872 0.02640  -0.00331 -0.00770 378 LYS A CA  
384  C C   . LYS A 49  ? 0.14732 0.18042 0.18528 0.00477  -0.00834 0.00513  378 LYS A C   
385  O O   . LYS A 49  ? 0.14710 0.19992 0.24220 0.02919  0.00380  0.01404  378 LYS A O   
386  C CB  . LYS A 49  ? 0.19965 0.21511 0.16072 0.00503  0.00394  0.02065  378 LYS A CB  
387  C CG  . LYS A 49  ? 0.24258 0.24821 0.22053 -0.00635 -0.01287 0.03108  378 LYS A CG  
388  C CD  . LYS A 49  ? 0.27953 0.31565 0.28159 0.00425  0.00125  0.03347  378 LYS A CD  
389  C CE  . LYS A 49  ? 0.31328 0.35496 0.32220 -0.02066 -0.00950 0.09457  378 LYS A CE  
390  N NZ  . LYS A 49  ? 0.39096 0.39669 0.37889 -0.00412 -0.01013 0.08113  378 LYS A NZ  
391  N N   . CYS A 50  ? 0.17777 0.17686 0.18787 0.02708  -0.00344 0.01751  379 CYS A N   
392  C CA  . CYS A 50  ? 0.18741 0.18121 0.21735 0.03083  0.01947  0.01917  379 CYS A CA  
393  C C   . CYS A 50  ? 0.17124 0.19793 0.22111 0.03736  0.02573  0.01146  379 CYS A C   
394  O O   . CYS A 50  ? 0.18802 0.21390 0.22909 0.03771  0.00870  -0.01944 379 CYS A O   
395  C CB  . CYS A 50  ? 0.25646 0.23065 0.19579 0.05061  -0.01548 0.04110  379 CYS A CB  
396  S SG  . CYS A 50  ? 0.24193 0.23932 0.20716 0.03723  -0.01849 0.02726  379 CYS A SG  
397  N N   . TYR A 51  ? 0.21326 0.18333 0.18686 0.04619  -0.00438 0.02134  380 TYR A N   
398  C CA  . TYR A 51  ? 0.23465 0.18074 0.21345 0.03641  -0.00343 0.02195  380 TYR A CA  
399  C C   . TYR A 51  ? 0.24448 0.19788 0.22375 0.05487  0.00364  -0.00535 380 TYR A C   
400  O O   . TYR A 51  ? 0.24940 0.18711 0.24173 0.03909  -0.00340 0.00967  380 TYR A O   
401  C CB  . TYR A 51  ? 0.25077 0.18721 0.20180 0.04862  -0.02313 0.01734  380 TYR A CB  
402  C CG  . TYR A 51  ? 0.21499 0.20805 0.18682 0.05023  -0.00863 0.01924  380 TYR A CG  
403  C CD1 . TYR A 51  ? 0.18320 0.20105 0.18800 0.02618  -0.00063 0.01694  380 TYR A CD1 
404  C CD2 . TYR A 51  ? 0.22807 0.22015 0.19919 0.03671  -0.01979 0.00702  380 TYR A CD2 
405  C CE1 . TYR A 51  ? 0.16742 0.22943 0.18471 0.01609  -0.03521 0.05731  380 TYR A CE1 
406  C CE2 . TYR A 51  ? 0.20658 0.20263 0.21096 0.03599  -0.02791 0.00678  380 TYR A CE2 
407  C CZ  . TYR A 51  ? 0.18759 0.22023 0.15993 0.03800  -0.02006 0.02883  380 TYR A CZ  
408  O OH  . TYR A 51  ? 0.19342 0.19827 0.21918 0.02839  0.00198  0.02267  380 TYR A OH  
409  N N   . GLY A 52  ? 0.25576 0.20322 0.22533 0.04960  -0.02196 -0.01532 381 GLY A N   
410  C CA  . GLY A 52  ? 0.28649 0.18906 0.24910 0.04904  -0.02821 -0.01917 381 GLY A CA  
411  C C   . GLY A 52  ? 0.29339 0.19954 0.29445 0.05587  -0.03841 0.00607  381 GLY A C   
412  O O   . GLY A 52  ? 0.36353 0.20074 0.32132 0.04017  -0.06039 -0.00581 381 GLY A O   
413  N N   . VAL A 53  ? 0.29207 0.19969 0.28110 0.04491  -0.05815 -0.00252 382 VAL A N   
414  C CA  . VAL A 53  ? 0.29110 0.20300 0.24290 0.01256  -0.06951 0.00072  382 VAL A CA  
415  C C   . VAL A 53  ? 0.28084 0.21086 0.25273 0.04416  -0.03517 -0.01081 382 VAL A C   
416  O O   . VAL A 53  ? 0.29265 0.19120 0.31102 0.03288  -0.04891 0.00691  382 VAL A O   
417  C CB  . VAL A 53  ? 0.31649 0.21243 0.26914 -0.01170 -0.06369 0.01401  382 VAL A CB  
418  C CG1 . VAL A 53  ? 0.29322 0.25014 0.27849 0.01495  -0.04526 0.01510  382 VAL A CG1 
419  C CG2 . VAL A 53  ? 0.34716 0.25613 0.31945 0.00084  -0.06631 0.01968  382 VAL A CG2 
420  N N   . SER A 54  ? 0.28726 0.25431 0.27766 0.05224  -0.05843 -0.00830 383 SER A N   
421  C CA  . SER A 54  ? 0.27165 0.29664 0.27789 0.05874  -0.05879 -0.00838 383 SER A CA  
422  C C   . SER A 54  ? 0.23409 0.25478 0.23573 0.03527  -0.04694 0.04204  383 SER A C   
423  O O   . SER A 54  ? 0.24238 0.23406 0.24384 0.05191  -0.03858 0.01509  383 SER A O   
424  C CB  . SER A 54  ? 0.29336 0.35988 0.27809 0.06781  -0.05326 -0.07990 383 SER A CB  
425  O OG  . SER A 54  ? 0.33464 0.40045 0.35177 0.11974  -0.00381 -0.04904 383 SER A OG  
426  N N   . PRO A 55  ? 0.21899 0.25060 0.24117 0.02969  0.00315  0.03430  384 PRO A N   
427  C CA  . PRO A 55  ? 0.23744 0.23107 0.25858 0.01735  0.00279  0.01308  384 PRO A CA  
428  C C   . PRO A 55  ? 0.24462 0.22089 0.22113 0.00424  0.00031  -0.01542 384 PRO A C   
429  O O   . PRO A 55  ? 0.23015 0.22156 0.26031 0.00733  0.00475  -0.00934 384 PRO A O   
430  C CB  . PRO A 55  ? 0.29573 0.22859 0.30188 0.00804  0.01809  0.00635  384 PRO A CB  
431  C CG  . PRO A 55  ? 0.34297 0.28236 0.32970 0.00620  0.00807  0.00413  384 PRO A CG  
432  C CD  . PRO A 55  ? 0.24777 0.24665 0.26225 -0.00858 -0.01866 0.02273  384 PRO A CD  
433  N N   . THR A 56  ? 0.22051 0.18904 0.24890 0.02092  -0.00606 -0.00240 385 THR A N   
434  C CA  . THR A 56  ? 0.22928 0.24346 0.24558 0.03372  -0.02727 0.03510  385 THR A CA  
435  C C   . THR A 56  ? 0.23301 0.28281 0.25608 0.03176  -0.02468 0.05123  385 THR A C   
436  O O   . THR A 56  ? 0.24602 0.34431 0.31203 0.02226  -0.03335 0.09823  385 THR A O   
437  C CB  . THR A 56  ? 0.22693 0.27332 0.24105 0.03480  -0.01817 -0.03627 385 THR A CB  
438  O OG1 . THR A 56  ? 0.25250 0.28382 0.33251 0.09370  -0.04342 -0.06312 385 THR A OG1 
439  C CG2 . THR A 56  ? 0.26065 0.27549 0.26864 0.02374  0.02261  -0.05133 385 THR A CG2 
440  N N   . LYS A 57  ? 0.23349 0.21655 0.34172 0.01410  -0.02153 0.06342  386 LYS A N   
441  C CA  . LYS A 57  ? 0.26722 0.27001 0.35436 0.04584  -0.00164 0.07908  386 LYS A CA  
442  C C   . LYS A 57  ? 0.26402 0.25927 0.34191 0.02924  -0.03189 0.07952  386 LYS A C   
443  O O   . LYS A 57  ? 0.31528 0.22274 0.42327 0.00284  0.02909  0.07500  386 LYS A O   
444  C CB  . LYS A 57  ? 0.35634 0.33232 0.42504 0.06566  -0.01467 0.06736  386 LYS A CB  
445  C CG  . LYS A 57  ? 0.44312 0.41144 0.49700 0.07964  -0.02056 0.05044  386 LYS A CG  
446  C CD  . LYS A 57  ? 0.50107 0.46268 0.53782 0.07231  -0.01958 0.04853  386 LYS A CD  
447  C CE  . LYS A 57  ? 0.52417 0.49086 0.54948 0.04471  -0.01908 0.05937  386 LYS A CE  
448  N NZ  . LYS A 57  ? 0.54229 0.50098 0.54799 0.03893  -0.01619 0.04411  386 LYS A NZ  
449  N N   . LEU A 58  ? 0.23143 0.23830 0.29995 0.01003  -0.05503 0.07142  387 LEU A N   
450  C CA  . LEU A 58  ? 0.22135 0.26484 0.33029 0.01904  -0.01810 0.07636  387 LEU A CA  
451  C C   . LEU A 58  ? 0.26496 0.26215 0.36813 0.01325  -0.01525 0.08252  387 LEU A C   
452  O O   . LEU A 58  ? 0.26562 0.31640 0.44327 -0.02519 0.02935  0.08242  387 LEU A O   
453  C CB  . LEU A 58  ? 0.25602 0.25131 0.25301 0.06194  0.01439  0.06789  387 LEU A CB  
454  C CG  . LEU A 58  ? 0.27723 0.27930 0.26924 0.05607  -0.05428 0.01968  387 LEU A CG  
455  C CD1 . LEU A 58  ? 0.32918 0.27720 0.27453 0.09196  -0.00327 0.06797  387 LEU A CD1 
456  C CD2 . LEU A 58  ? 0.31185 0.30813 0.32346 0.07896  -0.04236 0.01428  387 LEU A CD2 
457  N N   . ASN A 59  ? 0.31104 0.26290 0.29730 0.05443  0.02110  0.10163  388 ASN A N   
458  C CA  . ASN A 59  ? 0.34004 0.29254 0.32699 0.06976  0.01597  0.12049  388 ASN A CA  
459  C C   . ASN A 59  ? 0.37674 0.30040 0.33837 0.07159  -0.00219 0.15969  388 ASN A C   
460  O O   . ASN A 59  ? 0.38687 0.33745 0.37522 0.08198  -0.00333 0.13326  388 ASN A O   
461  C CB  . ASN A 59  ? 0.35067 0.30216 0.30605 0.09602  0.01139  0.09562  388 ASN A CB  
462  C CG  . ASN A 59  ? 0.30291 0.31320 0.29615 0.07824  0.01901  0.11026  388 ASN A CG  
463  O OD1 . ASN A 59  ? 0.32406 0.33848 0.39218 0.12040  0.01502  0.09953  388 ASN A OD1 
464  N ND2 . ASN A 59  ? 0.30721 0.32880 0.27488 0.04925  0.02001  0.07976  388 ASN A ND2 
465  N N   . ASP A 60  ? 0.37366 0.28843 0.41067 0.02587  0.01926  0.14037  389 ASP A N   
466  C CA  . ASP A 60  ? 0.41820 0.33504 0.44938 0.05249  -0.01509 0.16199  389 ASP A CA  
467  C C   . ASP A 60  ? 0.42969 0.36543 0.45982 0.05169  -0.02692 0.12461  389 ASP A C   
468  O O   . ASP A 60  ? 0.45510 0.39262 0.55421 0.04541  -0.03649 0.09588  389 ASP A O   
469  C CB  . ASP A 60  ? 0.48442 0.43502 0.50777 0.07440  -0.00860 0.11979  389 ASP A CB  
470  C CG  . ASP A 60  ? 0.54559 0.50428 0.56206 0.07534  -0.01320 0.10015  389 ASP A CG  
471  O OD1 . ASP A 60  ? 0.56668 0.54375 0.60133 0.08137  -0.03300 0.08008  389 ASP A OD1 
472  O OD2 . ASP A 60  ? 0.58427 0.53801 0.59916 0.06892  -0.02591 0.08609  389 ASP A OD2 
473  N N   . LEU A 61  ? 0.41936 0.35293 0.45417 0.03167  0.01291  0.14585  390 LEU A N   
474  C CA  . LEU A 61  ? 0.42167 0.34056 0.43763 0.02799  0.02212  0.11910  390 LEU A CA  
475  C C   . LEU A 61  ? 0.40268 0.35398 0.44663 0.00853  0.01949  0.10534  390 LEU A C   
476  O O   . LEU A 61  ? 0.38372 0.38806 0.45085 -0.01356 0.06067  0.10662  390 LEU A O   
477  C CB  . LEU A 61  ? 0.42722 0.35795 0.44913 0.01706  0.01203  0.09981  390 LEU A CB  
478  C CG  . LEU A 61  ? 0.43827 0.39577 0.48673 0.01701  0.00559  0.08431  390 LEU A CG  
479  C CD1 . LEU A 61  ? 0.43724 0.41339 0.47003 0.00183  0.00304  0.08916  390 LEU A CD1 
480  C CD2 . LEU A 61  ? 0.44845 0.40596 0.48899 0.02890  -0.01198 0.05579  390 LEU A CD2 
481  N N   . CYS A 62  ? 0.38547 0.31933 0.42084 -0.00837 0.01199  0.10832  391 CYS A N   
482  C CA  . CYS A 62  ? 0.39581 0.32191 0.43523 -0.03511 0.04428  0.12416  391 CYS A CA  
483  C C   . CYS A 62  ? 0.38895 0.30848 0.43698 -0.02662 0.04337  0.10330  391 CYS A C   
484  O O   . CYS A 62  ? 0.40787 0.31401 0.45448 -0.00893 0.04462  0.10523  391 CYS A O   
485  C CB  . CYS A 62  ? 0.43635 0.36423 0.45985 -0.03504 0.01129  0.18520  391 CYS A CB  
486  S SG  . CYS A 62  ? 0.48528 0.39656 0.54309 -0.02747 -0.02533 0.20338  391 CYS A SG  
487  N N   . PHE A 63  ? 0.35164 0.26647 0.42938 -0.01567 -0.00499 0.09224  392 PHE A N   
488  C CA  . PHE A 63  ? 0.36104 0.26905 0.42557 -0.02213 0.01975  0.11976  392 PHE A CA  
489  C C   . PHE A 63  ? 0.37290 0.27851 0.43426 -0.01843 0.03432  0.12562  392 PHE A C   
490  O O   . PHE A 63  ? 0.37547 0.30247 0.47747 -0.03758 0.04093  0.10737  392 PHE A O   
491  C CB  . PHE A 63  ? 0.34478 0.24525 0.42484 -0.03689 0.00932  0.09344  392 PHE A CB  
492  C CG  . PHE A 63  ? 0.36595 0.27071 0.37363 0.01952  0.02335  0.12866  392 PHE A CG  
493  C CD1 . PHE A 63  ? 0.38235 0.27418 0.41524 0.05791  0.02828  0.10398  392 PHE A CD1 
494  C CD2 . PHE A 63  ? 0.35377 0.29230 0.35817 -0.00613 0.00554  0.08966  392 PHE A CD2 
495  C CE1 . PHE A 63  ? 0.37504 0.27074 0.43833 0.05818  0.01293  0.11287  392 PHE A CE1 
496  C CE2 . PHE A 63  ? 0.34584 0.28904 0.36436 0.01534  0.01731  0.10967  392 PHE A CE2 
497  C CZ  . PHE A 63  ? 0.35999 0.28265 0.41408 0.03741  -0.00886 0.10580  392 PHE A CZ  
498  N N   . THR A 64  ? 0.37700 0.28425 0.45412 -0.00740 0.01609  0.11717  393 THR A N   
499  C CA  . THR A 64  ? 0.39075 0.34417 0.46243 -0.01880 0.02122  0.10051  393 THR A CA  
500  C C   . THR A 64  ? 0.37174 0.31216 0.43830 -0.04544 0.02481  0.12585  393 THR A C   
501  O O   . THR A 64  ? 0.36526 0.33414 0.48296 -0.03847 0.03504  0.11841  393 THR A O   
502  C CB  . THR A 64  ? 0.42597 0.39261 0.54641 -0.00798 0.01770  0.06482  393 THR A CB  
503  O OG1 . THR A 64  ? 0.44624 0.41133 0.59866 -0.00317 0.01595  0.06629  393 THR A OG1 
504  C CG2 . THR A 64  ? 0.45301 0.40616 0.54781 -0.01572 0.02237  0.09085  393 THR A CG2 
505  N N   . ASN A 65  ? 0.35073 0.29758 0.47351 -0.05074 -0.01187 0.11134  394 ASN A N   
506  C CA  . ASN A 65  ? 0.33678 0.27836 0.44140 -0.04396 -0.00999 0.10431  394 ASN A CA  
507  C C   . ASN A 65  ? 0.30068 0.25219 0.40747 -0.05481 0.03149  0.09113  394 ASN A C   
508  O O   . ASN A 65  ? 0.28779 0.23515 0.42737 -0.01022 0.04341  0.09329  394 ASN A O   
509  C CB  . ASN A 65  ? 0.34647 0.31131 0.47059 -0.06564 -0.00433 0.08167  394 ASN A CB  
510  C CG  . ASN A 65  ? 0.39456 0.40890 0.49463 -0.01456 0.00161  0.06773  394 ASN A CG  
511  O OD1 . ASN A 65  ? 0.38599 0.44984 0.54292 -0.02872 0.01210  0.09138  394 ASN A OD1 
512  N ND2 . ASN A 65  ? 0.40039 0.40060 0.54923 -0.02932 -0.01104 0.04033  394 ASN A ND2 
513  N N   . VAL A 66  ? 0.27481 0.26157 0.36908 -0.03039 0.01197  0.11972  395 VAL A N   
514  C CA  . VAL A 66  ? 0.23940 0.24922 0.32204 -0.02961 -0.00662 0.12046  395 VAL A CA  
515  C C   . VAL A 66  ? 0.22321 0.27562 0.28178 -0.00111 0.02605  0.11971  395 VAL A C   
516  O O   . VAL A 66  ? 0.25363 0.35095 0.28304 0.04512  0.05968  0.12992  395 VAL A O   
517  C CB  . VAL A 66  ? 0.26224 0.28150 0.31769 0.00538  -0.02241 0.07840  395 VAL A CB  
518  C CG1 . VAL A 66  ? 0.28381 0.27580 0.34705 -0.01785 -0.00583 0.08485  395 VAL A CG1 
519  C CG2 . VAL A 66  ? 0.26628 0.30304 0.34774 0.00318  0.01106  0.08695  395 VAL A CG2 
520  N N   . TYR A 67  ? 0.21570 0.20541 0.26305 -0.01576 -0.00469 0.08511  396 TYR A N   
521  C CA  . TYR A 67  ? 0.21086 0.20612 0.27053 -0.01077 -0.00406 0.06134  396 TYR A CA  
522  C C   . TYR A 67  ? 0.21352 0.20324 0.25225 0.01335  0.04637  0.08473  396 TYR A C   
523  O O   . TYR A 67  ? 0.20197 0.20901 0.30401 0.00530  0.06946  0.05664  396 TYR A O   
524  C CB  . TYR A 67  ? 0.24151 0.24663 0.30644 -0.03485 -0.00213 0.06087  396 TYR A CB  
525  C CG  . TYR A 67  ? 0.30409 0.28456 0.35139 -0.04146 -0.02047 0.03999  396 TYR A CG  
526  C CD1 . TYR A 67  ? 0.33622 0.31577 0.42867 -0.04996 -0.01509 0.03062  396 TYR A CD1 
527  C CD2 . TYR A 67  ? 0.36417 0.31006 0.42341 -0.02138 -0.02098 0.02082  396 TYR A CD2 
528  C CE1 . TYR A 67  ? 0.36523 0.32854 0.46833 -0.05964 0.00486  0.01901  396 TYR A CE1 
529  C CE2 . TYR A 67  ? 0.39820 0.35594 0.47670 -0.00777 0.01229  0.04843  396 TYR A CE2 
530  C CZ  . TYR A 67  ? 0.38771 0.35195 0.50185 -0.05665 0.00132  0.03015  396 TYR A CZ  
531  O OH  . TYR A 67  ? 0.42538 0.39731 0.56037 -0.03302 0.00381  0.01751  396 TYR A OH  
532  N N   . ALA A 68  ? 0.20596 0.21120 0.21930 0.01578  0.03278  0.06993  397 ALA A N   
533  C CA  . ALA A 68  ? 0.20440 0.19598 0.18298 0.00949  0.01755  0.05111  397 ALA A CA  
534  C C   . ALA A 68  ? 0.16976 0.18898 0.17184 0.01497  0.00873  0.05019  397 ALA A C   
535  O O   . ALA A 68  ? 0.17860 0.20835 0.21129 0.02352  0.02182  0.05827  397 ALA A O   
536  C CB  . ALA A 68  ? 0.21286 0.26806 0.16718 0.03277  0.02596  0.04206  397 ALA A CB  
537  N N   . ASP A 69  ? 0.16894 0.18227 0.15234 -0.00910 -0.01071 0.03762  398 ASP A N   
538  C CA  . ASP A 69  ? 0.16549 0.18186 0.16151 0.01264  -0.00007 0.03385  398 ASP A CA  
539  C C   . ASP A 69  ? 0.16111 0.17623 0.17900 0.00860  -0.00500 0.02651  398 ASP A C   
540  O O   . ASP A 69  ? 0.13891 0.20754 0.22248 0.00983  -0.00317 0.01896  398 ASP A O   
541  C CB  . ASP A 69  ? 0.17633 0.18128 0.13664 -0.00659 0.00387  0.02564  398 ASP A CB  
542  C CG  . ASP A 69  ? 0.19341 0.19133 0.16739 -0.00479 -0.00220 0.02396  398 ASP A CG  
543  O OD1 . ASP A 69  ? 0.18777 0.19368 0.20067 -0.02843 0.01588  0.02113  398 ASP A OD1 
544  O OD2 . ASP A 69  ? 0.17806 0.18351 0.18471 -0.01177 0.00414  0.03654  398 ASP A OD2 
545  N N   . SER A 70  ? 0.15789 0.16372 0.18306 -0.00817 -0.00126 0.02512  399 SER A N   
546  C CA  . SER A 70  ? 0.14983 0.19464 0.15091 0.02578  -0.00285 0.03210  399 SER A CA  
547  C C   . SER A 70  ? 0.11644 0.20530 0.14657 0.00270  0.00158  0.01384  399 SER A C   
548  O O   . SER A 70  ? 0.12963 0.18949 0.16250 -0.00127 -0.00562 0.02199  399 SER A O   
549  C CB  . SER A 70  ? 0.16295 0.23490 0.17059 0.02532  0.00553  0.03815  399 SER A CB  
550  O OG  . SER A 70  ? 0.17641 0.21833 0.15950 0.02547  -0.00355 0.02455  399 SER A OG  
551  N N   . PHE A 71  ? 0.12936 0.17372 0.14048 -0.00053 -0.00625 0.01208  400 PHE A N   
552  C CA  . PHE A 71  ? 0.14521 0.16984 0.13858 0.00987  -0.02801 0.00956  400 PHE A CA  
553  C C   . PHE A 71  ? 0.12446 0.16992 0.12992 0.00246  -0.02486 -0.00469 400 PHE A C   
554  O O   . PHE A 71  ? 0.13732 0.16488 0.13947 0.01109  -0.01760 0.01693  400 PHE A O   
555  C CB  . PHE A 71  ? 0.14489 0.17418 0.14275 0.01219  -0.01231 -0.00159 400 PHE A CB  
556  C CG  . PHE A 71  ? 0.14466 0.18124 0.11988 0.02656  -0.00594 0.00415  400 PHE A CG  
557  C CD1 . PHE A 71  ? 0.13074 0.18755 0.11477 0.00149  0.00862  0.01281  400 PHE A CD1 
558  C CD2 . PHE A 71  ? 0.17117 0.17572 0.13789 0.02275  -0.01498 0.00408  400 PHE A CD2 
559  C CE1 . PHE A 71  ? 0.14531 0.18493 0.13395 -0.01737 -0.00842 0.00037  400 PHE A CE1 
560  C CE2 . PHE A 71  ? 0.16222 0.18739 0.15781 0.01397  -0.02718 -0.00817 400 PHE A CE2 
561  C CZ  . PHE A 71  ? 0.14682 0.19165 0.15548 -0.01642 0.00060  0.01773  400 PHE A CZ  
562  N N   . VAL A 72  ? 0.14041 0.14862 0.13220 0.01197  -0.01756 0.01363  401 VAL A N   
563  C CA  . VAL A 72  ? 0.14591 0.15125 0.12233 0.00980  -0.00287 0.01547  401 VAL A CA  
564  C C   . VAL A 72  ? 0.13165 0.16154 0.13671 0.02320  -0.02963 -0.01493 401 VAL A C   
565  O O   . VAL A 72  ? 0.13485 0.17803 0.13887 0.01867  -0.00387 -0.00768 401 VAL A O   
566  C CB  . VAL A 72  ? 0.17946 0.15714 0.13743 0.00704  -0.00179 0.00183  401 VAL A CB  
567  C CG1 . VAL A 72  ? 0.18799 0.15300 0.18501 0.00646  -0.01196 -0.00033 401 VAL A CG1 
568  C CG2 . VAL A 72  ? 0.25107 0.20532 0.12918 0.05105  -0.00156 0.00019  401 VAL A CG2 
569  N N   . ILE A 73  ? 0.12423 0.15208 0.13607 0.01832  -0.00998 0.00958  402 ILE A N   
570  C CA  . ILE A 73  ? 0.15737 0.15383 0.12092 -0.00277 -0.01410 -0.01360 402 ILE A CA  
571  C C   . ILE A 73  ? 0.16926 0.14508 0.13513 0.00337  -0.02312 -0.00004 402 ILE A C   
572  O O   . ILE A 73  ? 0.21067 0.16958 0.14182 -0.02468 -0.02248 -0.00262 402 ILE A O   
573  C CB  . ILE A 73  ? 0.14566 0.16770 0.13803 0.01341  -0.01135 -0.01924 402 ILE A CB  
574  C CG1 . ILE A 73  ? 0.16401 0.16581 0.15388 0.02451  -0.01467 -0.00789 402 ILE A CG1 
575  C CG2 . ILE A 73  ? 0.13814 0.15346 0.16228 -0.01624 -0.01246 -0.01902 402 ILE A CG2 
576  C CD1 . ILE A 73  ? 0.15821 0.18005 0.18475 0.02343  0.00277  0.01698  402 ILE A CD1 
577  N N   . ARG A 74  ? 0.15740 0.16029 0.15514 -0.00976 0.00324  0.01352  403 ARG A N   
578  C CA  . ARG A 74  ? 0.19034 0.18636 0.13782 -0.02877 -0.01072 0.03364  403 ARG A CA  
579  C C   . ARG A 74  ? 0.16207 0.17059 0.16749 -0.01418 0.00519  -0.02546 403 ARG A C   
580  O O   . ARG A 74  ? 0.15382 0.18205 0.20214 -0.01735 0.01073  -0.04702 403 ARG A O   
581  C CB  . ARG A 74  ? 0.27121 0.26866 0.23751 -0.08666 -0.01403 -0.00640 403 ARG A CB  
582  C CG  . ARG A 74  ? 0.32518 0.28110 0.27298 -0.00907 -0.02490 0.01668  403 ARG A CG  
583  C CD  . ARG A 74  ? 0.33381 0.30927 0.19424 0.02859  -0.04270 0.06665  403 ARG A CD  
584  N NE  . ARG A 74  ? 0.40643 0.36935 0.30577 0.03268  -0.00484 0.07643  403 ARG A NE  
585  C CZ  . ARG A 74  ? 0.45184 0.44384 0.43548 0.06120  0.01001  0.03369  403 ARG A CZ  
586  N NH1 . ARG A 74  ? 0.46372 0.45240 0.44799 0.07837  -0.02383 0.07128  403 ARG A NH1 
587  N NH2 . ARG A 74  ? 0.49746 0.46278 0.45227 0.07637  0.00912  0.02339  403 ARG A NH2 
588  N N   . GLY A 75  ? 0.14857 0.18827 0.26470 -0.02099 0.00990  -0.06555 404 GLY A N   
589  C CA  . GLY A 75  ? 0.14742 0.24060 0.26497 -0.02104 0.01261  -0.07999 404 GLY A CA  
590  C C   . GLY A 75  ? 0.15051 0.19354 0.28210 -0.03379 0.00887  -0.04748 404 GLY A C   
591  O O   . GLY A 75  ? 0.15808 0.21868 0.25265 0.00273  -0.00519 -0.04470 404 GLY A O   
592  N N   . ASP A 76  ? 0.15802 0.19468 0.28674 -0.03586 0.05376  -0.03947 405 ASP A N   
593  C CA  . ASP A 76  ? 0.17863 0.19948 0.26558 -0.03363 0.04565  -0.03558 405 ASP A CA  
594  C C   . ASP A 76  ? 0.15443 0.19981 0.21142 -0.01151 0.01274  0.01735  405 ASP A C   
595  O O   . ASP A 76  ? 0.16048 0.20211 0.20706 -0.01433 0.02597  0.00320  405 ASP A O   
596  C CB  . ASP A 76  ? 0.26118 0.24672 0.35095 -0.02068 0.09225  0.03826  405 ASP A CB  
597  C CG  . ASP A 76  ? 0.33314 0.27067 0.37364 -0.03315 0.09688  0.11271  405 ASP A CG  
598  O OD1 . ASP A 76  ? 0.40650 0.34879 0.46509 -0.00639 0.04587  0.13967  405 ASP A OD1 
599  O OD2 . ASP A 76  ? 0.30331 0.26618 0.45751 -0.00128 0.02479  0.11835  405 ASP A OD2 
600  N N   . GLU A 77  ? 0.14637 0.15103 0.20601 -0.01572 -0.00522 0.00320  406 GLU A N   
601  C CA  . GLU A 77  ? 0.12527 0.16342 0.18416 0.00929  0.00374  0.00853  406 GLU A CA  
602  C C   . GLU A 77  ? 0.13630 0.14927 0.15132 -0.00566 0.01083  0.02248  406 GLU A C   
603  O O   . GLU A 77  ? 0.13629 0.15695 0.16443 0.00525  -0.00549 0.00469  406 GLU A O   
604  C CB  . GLU A 77  ? 0.13604 0.18204 0.15374 0.02312  0.01059  0.02244  406 GLU A CB  
605  C CG  . GLU A 77  ? 0.16960 0.18813 0.16882 0.02619  0.01835  0.02479  406 GLU A CG  
606  C CD  . GLU A 77  ? 0.18634 0.17950 0.13447 0.01851  0.00230  0.01030  406 GLU A CD  
607  O OE1 . GLU A 77  ? 0.15495 0.16912 0.16522 0.01852  -0.01060 -0.00358 406 GLU A OE1 
608  O OE2 . GLU A 77  ? 0.23216 0.23034 0.16543 0.02246  -0.02293 0.02945  406 GLU A OE2 
609  N N   . VAL A 78  ? 0.13206 0.19541 0.13951 0.00753  -0.01085 0.00267  407 VAL A N   
610  C CA  . VAL A 78  ? 0.14171 0.20094 0.12641 0.01314  -0.01348 0.00072  407 VAL A CA  
611  C C   . VAL A 78  ? 0.14929 0.18121 0.12324 0.01297  0.00357  -0.00563 407 VAL A C   
612  O O   . VAL A 78  ? 0.15528 0.19288 0.15470 0.01448  -0.01633 -0.00631 407 VAL A O   
613  C CB  . VAL A 78  ? 0.17737 0.23681 0.16230 0.03798  -0.01913 -0.02196 407 VAL A CB  
614  C CG1 . VAL A 78  ? 0.20978 0.25715 0.17265 0.03725  -0.03777 0.02168  407 VAL A CG1 
615  C CG2 . VAL A 78  ? 0.17366 0.25438 0.18316 -0.00484 0.00622  -0.04158 407 VAL A CG2 
616  N N   A ARG A 79  ? 0.14449 0.18910 0.12860 0.01952  -0.00992 -0.00759 408 ARG A N   
617  N N   B ARG A 79  ? 0.14369 0.18974 0.12710 0.02278  -0.00576 -0.00155 408 ARG A N   
618  C CA  A ARG A 79  ? 0.15096 0.20065 0.14727 0.00773  0.00103  -0.00746 408 ARG A CA  
619  C CA  B ARG A 79  ? 0.14928 0.19905 0.14618 0.00655  0.00634  -0.00767 408 ARG A CA  
620  C C   A ARG A 79  ? 0.14164 0.17901 0.15615 0.00992  0.00018  0.00970  408 ARG A C   
621  C C   B ARG A 79  ? 0.14040 0.17821 0.15673 0.00877  0.00316  0.00947  408 ARG A C   
622  O O   A ARG A 79  ? 0.15144 0.19242 0.18685 0.02890  -0.00167 -0.01949 408 ARG A O   
623  O O   B ARG A 79  ? 0.14783 0.18915 0.19413 0.02904  0.00323  -0.01499 408 ARG A O   
624  C CB  A ARG A 79  ? 0.15688 0.22023 0.17339 0.00394  0.01804  -0.00871 408 ARG A CB  
625  C CB  B ARG A 79  ? 0.15895 0.21937 0.17326 0.01391  0.02299  0.00468  408 ARG A CB  
626  C CG  A ARG A 79  ? 0.17582 0.23139 0.20441 -0.02303 0.00292  0.02147  408 ARG A CG  
627  C CG  B ARG A 79  ? 0.15998 0.21024 0.19913 -0.01805 0.01735  0.01230  408 ARG A CG  
628  C CD  A ARG A 79  ? 0.24309 0.29222 0.28949 0.02208  0.01023  0.02871  408 ARG A CD  
629  C CD  B ARG A 79  ? 0.21851 0.25252 0.21995 0.00742  0.02177  0.03304  408 ARG A CD  
630  N NE  A ARG A 79  ? 0.30223 0.31976 0.34062 0.03060  0.05288  0.01158  408 ARG A NE  
631  N NE  B ARG A 79  ? 0.28071 0.30773 0.30972 0.03246  0.01786  0.00997  408 ARG A NE  
632  C CZ  A ARG A 79  ? 0.34200 0.31262 0.32863 0.03781  0.04794  -0.01649 408 ARG A CZ  
633  C CZ  B ARG A 79  ? 0.35708 0.32779 0.35356 0.04675  0.00660  0.01101  408 ARG A CZ  
634  N NH1 A ARG A 79  ? 0.29775 0.16556 0.14532 0.01748  0.10818  0.00319  408 ARG A NH1 
635  N NH1 B ARG A 79  ? 0.32073 0.25921 0.20979 -0.02385 0.07319  -0.04470 408 ARG A NH1 
636  N NH2 A ARG A 79  ? 0.34054 0.30088 0.32715 0.05935  0.02051  0.07357  408 ARG A NH2 
637  N NH2 B ARG A 79  ? 0.41768 0.35412 0.40098 0.03995  -0.02620 0.00800  408 ARG A NH2 
638  N N   . GLN A 80  ? 0.12604 0.17370 0.15070 0.01242  -0.00379 0.01158  409 GLN A N   
639  C CA  . GLN A 80  ? 0.14150 0.17367 0.14788 0.01086  0.00580  0.02536  409 GLN A CA  
640  C C   . GLN A 80  ? 0.14388 0.15227 0.13842 0.01126  0.00173  -0.01472 409 GLN A C   
641  O O   . GLN A 80  ? 0.14404 0.16428 0.15030 0.01203  0.00100  0.00737  409 GLN A O   
642  C CB  . GLN A 80  ? 0.13719 0.16295 0.13683 0.02040  -0.00091 0.01946  409 GLN A CB  
643  C CG  . GLN A 80  ? 0.13588 0.16829 0.13624 -0.00686 -0.02519 0.01630  409 GLN A CG  
644  C CD  . GLN A 80  ? 0.13025 0.17897 0.12621 0.00003  -0.00111 0.00672  409 GLN A CD  
645  O OE1 . GLN A 80  ? 0.13093 0.17391 0.13791 -0.00202 -0.00428 0.00368  409 GLN A OE1 
646  N NE2 . GLN A 80  ? 0.15356 0.17639 0.14178 0.00408  0.01634  0.01250  409 GLN A NE2 
647  N N   . ILE A 81  ? 0.14502 0.16036 0.14085 0.02798  0.00217  0.00687  410 ILE A N   
648  C CA  . ILE A 81  ? 0.13589 0.15653 0.13909 0.01738  0.01159  0.01034  410 ILE A CA  
649  C C   . ILE A 81  ? 0.13905 0.18274 0.13059 0.00787  -0.01125 -0.00456 410 ILE A C   
650  O O   . ILE A 81  ? 0.14050 0.18842 0.14704 0.02026  -0.00424 0.00107  410 ILE A O   
651  C CB  . ILE A 81  ? 0.14908 0.16435 0.13419 0.02642  0.00091  0.02018  410 ILE A CB  
652  C CG1 . ILE A 81  ? 0.13779 0.17880 0.15257 0.00945  -0.02406 0.01084  410 ILE A CG1 
653  C CG2 . ILE A 81  ? 0.15570 0.17296 0.15492 -0.00165 0.01183  0.01666  410 ILE A CG2 
654  C CD1 . ILE A 81  ? 0.17484 0.16358 0.18152 0.02631  0.01324  0.01281  410 ILE A CD1 
655  N N   . ALA A 82  ? 0.16312 0.17534 0.16282 0.02949  0.00643  0.00140  411 ALA A N   
656  C CA  . ALA A 82  ? 0.15802 0.16692 0.16170 0.03562  0.01464  -0.00485 411 ALA A CA  
657  C C   . ALA A 82  ? 0.16964 0.15699 0.16567 0.03535  -0.00694 0.00886  411 ALA A C   
658  O O   . ALA A 82  ? 0.18219 0.16993 0.16726 0.02879  -0.01542 0.00394  411 ALA A O   
659  C CB  . ALA A 82  ? 0.16276 0.19814 0.17403 0.04117  0.00546  0.01654  411 ALA A CB  
660  N N   . PRO A 83  ? 0.21670 0.15431 0.15413 0.03277  -0.01782 -0.00403 412 PRO A N   
661  C CA  . PRO A 83  ? 0.23961 0.15302 0.17920 0.02502  0.00716  0.01382  412 PRO A CA  
662  C C   . PRO A 83  ? 0.21081 0.15207 0.18500 0.02726  0.02460  0.00715  412 PRO A C   
663  O O   . PRO A 83  ? 0.21663 0.18111 0.18930 0.03557  0.01533  0.01508  412 PRO A O   
664  C CB  . PRO A 83  ? 0.27923 0.16671 0.18404 0.02667  -0.02231 0.01673  412 PRO A CB  
665  C CG  . PRO A 83  ? 0.32305 0.18502 0.23192 0.05031  -0.04163 -0.00414 412 PRO A CG  
666  C CD  . PRO A 83  ? 0.25588 0.17112 0.17586 0.05701  -0.03131 0.00106  412 PRO A CD  
667  N N   . GLY A 84  ? 0.23002 0.17084 0.14233 0.04163  -0.00014 0.00167  413 GLY A N   
668  C CA  . GLY A 84  ? 0.25549 0.19028 0.16064 0.03192  0.01646  0.01921  413 GLY A CA  
669  C C   . GLY A 84  ? 0.19912 0.18488 0.15996 0.01302  0.02907  0.01551  413 GLY A C   
670  O O   . GLY A 84  ? 0.23724 0.19817 0.17852 0.02442  0.04937  0.01478  413 GLY A O   
671  N N   . GLN A 85  ? 0.17819 0.16937 0.16555 0.01966  0.00865  -0.01070 414 GLN A N   
672  C CA  . GLN A 85  ? 0.16802 0.16424 0.15380 0.01263  0.00901  0.00757  414 GLN A CA  
673  C C   . GLN A 85  ? 0.17535 0.17741 0.15667 0.01276  0.02686  0.01771  414 GLN A C   
674  O O   . GLN A 85  ? 0.19501 0.16596 0.20254 0.01462  0.02291  0.01762  414 GLN A O   
675  C CB  . GLN A 85  ? 0.20906 0.16479 0.14713 0.01134  0.01123  0.00547  414 GLN A CB  
676  C CG  . GLN A 85  ? 0.21011 0.19934 0.16635 -0.00904 -0.00270 0.04530  414 GLN A CG  
677  C CD  . GLN A 85  ? 0.20147 0.19814 0.19762 -0.01083 -0.01980 0.02832  414 GLN A CD  
678  O OE1 . GLN A 85  ? 0.19256 0.22423 0.23874 0.01974  -0.00978 0.06642  414 GLN A OE1 
679  N NE2 . GLN A 85  ? 0.20921 0.25723 0.24077 0.03237  -0.01738 0.05452  414 GLN A NE2 
680  N N   . THR A 86  ? 0.17025 0.16853 0.12867 0.02413  0.00921  0.00592  415 THR A N   
681  C CA  . THR A 86  ? 0.16216 0.18333 0.14654 0.01508  0.00125  -0.00400 415 THR A CA  
682  C C   . THR A 86  ? 0.16239 0.17253 0.12031 0.01692  0.00491  0.01014  415 THR A C   
683  O O   . THR A 86  ? 0.16111 0.18054 0.13730 0.00620  0.00488  0.00352  415 THR A O   
684  C CB  . THR A 86  ? 0.15072 0.22328 0.12628 0.00849  0.01036  -0.01747 415 THR A CB  
685  O OG1 . THR A 86  ? 0.17774 0.20319 0.14995 0.01197  -0.00182 -0.00278 415 THR A OG1 
686  C CG2 . THR A 86  ? 0.17379 0.24597 0.14905 -0.00724 0.03529  0.00017  415 THR A CG2 
687  N N   . GLY A 87  ? 0.15643 0.16667 0.15857 0.01551  0.01178  -0.00096 416 GLY A N   
688  C CA  . GLY A 87  ? 0.14762 0.15704 0.16206 0.01120  0.02171  -0.00214 416 GLY A CA  
689  C C   . GLY A 87  ? 0.14655 0.17276 0.12593 0.01686  0.01788  0.02486  416 GLY A C   
690  O O   . GLY A 87  ? 0.16008 0.15989 0.13680 -0.01246 0.01683  -0.00219 416 GLY A O   
691  N N   . LYS A 88  ? 0.15470 0.15684 0.13544 0.00262  0.01220  0.00489  417 LYS A N   
692  C CA  . LYS A 88  ? 0.14065 0.17268 0.15018 0.01419  0.02631  0.00582  417 LYS A CA  
693  C C   . LYS A 88  ? 0.12268 0.17664 0.11895 0.01221  0.01967  -0.01237 417 LYS A C   
694  O O   . LYS A 88  ? 0.13195 0.16991 0.13788 0.01101  0.00329  -0.00001 417 LYS A O   
695  C CB  . LYS A 88  ? 0.20344 0.18588 0.20601 0.02092  0.02209  0.03299  417 LYS A CB  
696  C CG  . LYS A 88  ? 0.26657 0.20741 0.21130 0.03035  -0.01497 0.03828  417 LYS A CG  
697  C CD  . LYS A 88  ? 0.30323 0.30775 0.30531 0.01024  -0.01048 0.07132  417 LYS A CD  
698  C CE  . LYS A 88  ? 0.31678 0.28978 0.35184 0.02164  -0.00956 0.03503  417 LYS A CE  
699  N NZ  . LYS A 88  ? 0.32883 0.25294 0.33390 0.01343  0.04608  -0.00544 417 LYS A NZ  
700  N N   . ILE A 89  ? 0.14628 0.15698 0.12282 0.00751  0.00314  -0.00279 418 ILE A N   
701  C CA  . ILE A 89  ? 0.14986 0.16897 0.13460 0.00433  0.00280  -0.00700 418 ILE A CA  
702  C C   . ILE A 89  ? 0.13627 0.16234 0.11763 0.01657  0.00395  -0.00351 418 ILE A C   
703  O O   . ILE A 89  ? 0.13366 0.17898 0.14143 -0.00097 0.00706  0.01844  418 ILE A O   
704  C CB  . ILE A 89  ? 0.13418 0.18228 0.12829 0.00569  -0.01082 -0.01886 418 ILE A CB  
705  C CG1 . ILE A 89  ? 0.15056 0.20524 0.15570 0.00230  -0.01671 -0.03991 418 ILE A CG1 
706  C CG2 . ILE A 89  ? 0.15968 0.25825 0.10780 0.00595  -0.00345 0.01048  418 ILE A CG2 
707  C CD1 . ILE A 89  ? 0.14967 0.23273 0.19402 0.02945  -0.02360 -0.03265 418 ILE A CD1 
708  N N   . ALA A 90  ? 0.15411 0.15845 0.12628 0.01661  0.01133  0.00477  419 ALA A N   
709  C CA  . ALA A 90  ? 0.14675 0.15679 0.13102 0.00880  -0.01069 0.00138  419 ALA A CA  
710  C C   . ALA A 90  ? 0.14764 0.15810 0.13656 -0.01160 0.01317  0.00924  419 ALA A C   
711  O O   . ALA A 90  ? 0.17493 0.16877 0.14440 -0.00909 0.00245  0.00356  419 ALA A O   
712  C CB  . ALA A 90  ? 0.14922 0.18075 0.16727 0.02504  0.01772  -0.01227 419 ALA A CB  
713  N N   . ASP A 91  ? 0.14356 0.17127 0.12197 0.01609  0.00392  -0.00139 420 ASP A N   
714  C CA  . ASP A 91  ? 0.14212 0.18599 0.12246 0.00005  0.01305  0.00036  420 ASP A CA  
715  C C   . ASP A 91  ? 0.15822 0.17663 0.11682 0.00627  0.01171  -0.01225 420 ASP A C   
716  O O   . ASP A 91  ? 0.14837 0.17648 0.16675 0.00241  0.00994  -0.02663 420 ASP A O   
717  C CB  . ASP A 91  ? 0.14504 0.20464 0.12000 -0.00589 0.01349  -0.00940 420 ASP A CB  
718  C CG  . ASP A 91  ? 0.19424 0.15695 0.12036 0.00665  0.00448  0.00860  420 ASP A CG  
719  O OD1 . ASP A 91  ? 0.16684 0.17698 0.15920 0.01372  0.02680  0.02131  420 ASP A OD1 
720  O OD2 . ASP A 91  ? 0.18091 0.17201 0.14008 0.01055  0.01372  0.00306  420 ASP A OD2 
721  N N   . TYR A 92  ? 0.15461 0.15423 0.11816 0.01157  0.01723  -0.00302 421 TYR A N   
722  C CA  . TYR A 92  ? 0.12222 0.16452 0.13781 0.01617  0.01642  0.00369  421 TYR A CA  
723  C C   . TYR A 92  ? 0.13297 0.16782 0.12865 0.01173  0.02452  -0.01829 421 TYR A C   
724  O O   . TYR A 92  ? 0.12941 0.21251 0.13349 0.01339  0.01316  -0.00559 421 TYR A O   
725  C CB  . TYR A 92  ? 0.16049 0.17368 0.12579 0.00551  0.00117  -0.00152 421 TYR A CB  
726  C CG  . TYR A 92  ? 0.14241 0.17700 0.12634 0.00046  -0.00825 -0.00597 421 TYR A CG  
727  C CD1 . TYR A 92  ? 0.15272 0.22282 0.12095 0.00658  0.00752  0.02763  421 TYR A CD1 
728  C CD2 . TYR A 92  ? 0.17346 0.17455 0.17714 -0.00048 -0.00924 0.02263  421 TYR A CD2 
729  C CE1 . TYR A 92  ? 0.18752 0.22585 0.14291 0.03135  0.00287  0.03539  421 TYR A CE1 
730  C CE2 . TYR A 92  ? 0.21344 0.23961 0.14996 0.00575  0.03966  0.04771  421 TYR A CE2 
731  C CZ  . TYR A 92  ? 0.22273 0.23291 0.14778 0.03523  0.03280  0.07069  421 TYR A CZ  
732  O OH  . TYR A 92  ? 0.29567 0.25276 0.19063 0.05721  0.06530  0.06106  421 TYR A OH  
733  N N   . ASN A 93  ? 0.15625 0.15899 0.13141 -0.00175 -0.01333 -0.00317 422 ASN A N   
734  C CA  . ASN A 93  ? 0.15479 0.16650 0.09791 -0.00341 -0.00324 -0.00166 422 ASN A CA  
735  C C   . ASN A 93  ? 0.14437 0.16913 0.11339 -0.00079 0.01375  0.00079  422 ASN A C   
736  O O   . ASN A 93  ? 0.13651 0.18440 0.14132 -0.00589 0.00506  0.00370  422 ASN A O   
737  C CB  . ASN A 93  ? 0.15322 0.16479 0.12447 0.01824  -0.01075 0.00202  422 ASN A CB  
738  C CG  . ASN A 93  ? 0.11394 0.17610 0.11882 0.00027  -0.01491 -0.00220 422 ASN A CG  
739  O OD1 . ASN A 93  ? 0.13019 0.17086 0.14375 0.01322  -0.00578 -0.00263 422 ASN A OD1 
740  N ND2 . ASN A 93  ? 0.13566 0.17910 0.12043 -0.00315 -0.00482 0.01553  422 ASN A ND2 
741  N N   . TYR A 94  ? 0.13102 0.16294 0.14114 0.01506  0.00295  0.00286  423 TYR A N   
742  C CA  . TYR A 94  ? 0.14864 0.15620 0.12578 0.01600  0.00441  0.01136  423 TYR A CA  
743  C C   . TYR A 94  ? 0.13597 0.16282 0.15084 -0.01018 0.00603  0.01895  423 TYR A C   
744  O O   . TYR A 94  ? 0.13540 0.16435 0.14343 0.01219  0.00708  0.00811  423 TYR A O   
745  C CB  . TYR A 94  ? 0.16091 0.16785 0.12648 -0.00049 -0.00151 0.01993  423 TYR A CB  
746  C CG  . TYR A 94  ? 0.14411 0.15024 0.12654 -0.00652 -0.00606 0.00590  423 TYR A CG  
747  C CD1 . TYR A 94  ? 0.18412 0.14745 0.12378 0.00167  0.02097  0.01784  423 TYR A CD1 
748  C CD2 . TYR A 94  ? 0.14887 0.18167 0.12848 0.01580  -0.01515 0.01026  423 TYR A CD2 
749  C CE1 . TYR A 94  ? 0.15826 0.16462 0.16020 -0.00553 0.00913  0.00409  423 TYR A CE1 
750  C CE2 . TYR A 94  ? 0.14607 0.20716 0.13760 0.00156  0.01453  0.02098  423 TYR A CE2 
751  C CZ  . TYR A 94  ? 0.15914 0.15456 0.17383 0.02072  0.00934  0.01046  423 TYR A CZ  
752  O OH  . TYR A 94  ? 0.18062 0.16857 0.17695 0.02282  0.01426  0.04579  423 TYR A OH  
753  N N   . LYS A 95  ? 0.17179 0.15126 0.15587 -0.00186 0.01107  0.00113  424 LYS A N   
754  C CA  . LYS A 95  ? 0.15859 0.16710 0.15501 0.00808  0.00743  -0.01455 424 LYS A CA  
755  C C   . LYS A 95  ? 0.16746 0.16311 0.16791 -0.00816 -0.00124 -0.00489 424 LYS A C   
756  O O   . LYS A 95  ? 0.16618 0.16054 0.19591 -0.00470 -0.00150 0.00345  424 LYS A O   
757  C CB  . LYS A 95  ? 0.19201 0.16173 0.15825 0.00900  -0.00178 0.00256  424 LYS A CB  
758  C CG  . LYS A 95  ? 0.18362 0.16116 0.16557 0.00225  0.02541  -0.00621 424 LYS A CG  
759  C CD  . LYS A 95  ? 0.18114 0.17896 0.16075 0.01285  0.00712  -0.00047 424 LYS A CD  
760  C CE  . LYS A 95  ? 0.17018 0.19783 0.17209 -0.00522 0.03256  -0.01245 424 LYS A CE  
761  N NZ  . LYS A 95  ? 0.20077 0.20056 0.19363 0.01538  0.00967  -0.01086 424 LYS A NZ  
762  N N   . LEU A 96  ? 0.17300 0.16081 0.16067 0.00741  -0.00383 0.00380  425 LEU A N   
763  C CA  . LEU A 96  ? 0.18620 0.17815 0.16611 0.02267  0.00395  0.01265  425 LEU A CA  
764  C C   . LEU A 96  ? 0.21590 0.18186 0.16304 0.02144  0.02022  0.00773  425 LEU A C   
765  O O   . LEU A 96  ? 0.24785 0.19231 0.18656 0.01835  0.01997  -0.02202 425 LEU A O   
766  C CB  . LEU A 96  ? 0.18785 0.17543 0.16993 0.02492  0.01171  0.02859  425 LEU A CB  
767  C CG  . LEU A 96  ? 0.19689 0.17785 0.15476 0.01074  0.01058  0.00621  425 LEU A CG  
768  C CD1 . LEU A 96  ? 0.20552 0.18228 0.24457 0.01512  -0.03666 0.01730  425 LEU A CD1 
769  C CD2 . LEU A 96  ? 0.24534 0.19629 0.18061 0.02441  0.01067  0.02020  425 LEU A CD2 
770  N N   . PRO A 97  ? 0.24077 0.18396 0.20889 0.01028  0.00020  0.00779  426 PRO A N   
771  C CA  . PRO A 97  ? 0.25647 0.17146 0.22564 0.02503  -0.00927 -0.03761 426 PRO A CA  
772  C C   . PRO A 97  ? 0.23838 0.20966 0.21234 0.01770  0.00060  -0.02135 426 PRO A C   
773  O O   . PRO A 97  ? 0.22500 0.21115 0.22745 0.02481  0.01277  -0.01674 426 PRO A O   
774  C CB  . PRO A 97  ? 0.28083 0.16776 0.23349 0.02950  -0.00596 0.00622  426 PRO A CB  
775  C CG  . PRO A 97  ? 0.27312 0.17004 0.22450 0.03510  0.01283  0.00590  426 PRO A CG  
776  C CD  . PRO A 97  ? 0.26643 0.15787 0.21608 0.00630  0.01908  0.01927  426 PRO A CD  
777  N N   . ASP A 98  ? 0.28229 0.22563 0.24290 0.04007  0.03490  -0.03955 427 ASP A N   
778  C CA  . ASP A 98  ? 0.27275 0.24225 0.23351 0.02194  0.01605  -0.05523 427 ASP A CA  
779  C C   . ASP A 98  ? 0.26311 0.26594 0.26113 0.03003  0.00979  -0.06210 427 ASP A C   
780  O O   . ASP A 98  ? 0.27608 0.29725 0.28947 0.05152  0.01150  -0.06738 427 ASP A O   
781  C CB  . ASP A 98  ? 0.32718 0.30211 0.28361 0.06253  0.00712  -0.08884 427 ASP A CB  
782  C CG  . ASP A 98  ? 0.38170 0.32173 0.34242 0.04794  0.04446  -0.07061 427 ASP A CG  
783  O OD1 . ASP A 98  ? 0.38044 0.34048 0.25428 0.02113  0.07754  -0.01992 427 ASP A OD1 
784  O OD2 . ASP A 98  ? 0.42147 0.37191 0.35780 0.09252  0.03919  -0.09863 427 ASP A OD2 
785  N N   . ASP A 99  ? 0.29084 0.21887 0.25017 0.04659  0.00472  -0.02951 428 ASP A N   
786  C CA  . ASP A 99  ? 0.33284 0.21822 0.29923 0.07718  -0.00882 -0.04894 428 ASP A CA  
787  C C   . ASP A 99  ? 0.31258 0.18685 0.27595 0.05493  -0.00077 0.00252  428 ASP A C   
788  O O   . ASP A 99  ? 0.35016 0.18810 0.31091 0.05044  -0.02336 0.01013  428 ASP A O   
789  C CB  . ASP A 99  ? 0.36892 0.21527 0.36450 0.02780  -0.03173 -0.06857 428 ASP A CB  
790  C CG  . ASP A 99  ? 0.38686 0.26243 0.43976 -0.00702 -0.03349 -0.00806 428 ASP A CG  
791  O OD1 . ASP A 99  ? 0.37590 0.26305 0.44237 0.00583  -0.02824 0.02632  428 ASP A OD1 
792  O OD2 . ASP A 99  ? 0.44328 0.30044 0.51044 -0.00274 -0.04127 -0.02803 428 ASP A OD2 
793  N N   . PHE A 100 ? 0.30753 0.16305 0.25737 0.04602  -0.01607 -0.01344 429 PHE A N   
794  C CA  . PHE A 100 ? 0.28360 0.17500 0.24387 0.05200  -0.02940 -0.03304 429 PHE A CA  
795  C C   . PHE A 100 ? 0.23808 0.21756 0.21597 0.01891  -0.01710 -0.01711 429 PHE A C   
796  O O   . PHE A 100 ? 0.23844 0.24456 0.25015 0.04373  -0.01591 -0.02470 429 PHE A O   
797  C CB  . PHE A 100 ? 0.26583 0.15674 0.23436 0.03356  -0.01578 -0.01879 429 PHE A CB  
798  C CG  . PHE A 100 ? 0.22860 0.16936 0.22927 0.03781  0.00023  -0.00404 429 PHE A CG  
799  C CD1 . PHE A 100 ? 0.22080 0.18890 0.23918 0.05378  -0.01118 0.01365  429 PHE A CD1 
800  C CD2 . PHE A 100 ? 0.21594 0.15777 0.20697 0.03103  -0.01356 0.03140  429 PHE A CD2 
801  C CE1 . PHE A 100 ? 0.20848 0.17351 0.24341 0.02603  0.01684  0.02267  429 PHE A CE1 
802  C CE2 . PHE A 100 ? 0.18924 0.19283 0.19961 0.02180  0.01116  0.02107  429 PHE A CE2 
803  C CZ  . PHE A 100 ? 0.20594 0.17542 0.20394 0.03081  0.00038  0.02616  429 PHE A CZ  
804  N N   . THR A 101 ? 0.26490 0.20082 0.20489 0.03253  -0.01008 0.01554  430 THR A N   
805  C CA  . THR A 101 ? 0.27259 0.16071 0.25884 0.00101  -0.01525 0.01509  430 THR A CA  
806  C C   . THR A 101 ? 0.21563 0.18264 0.21668 0.01021  -0.05290 0.01142  430 THR A C   
807  O O   . THR A 101 ? 0.21042 0.19853 0.27798 -0.00725 -0.01256 0.03306  430 THR A O   
808  C CB  . THR A 101 ? 0.31013 0.17739 0.28569 0.02801  -0.04971 0.00708  430 THR A CB  
809  O OG1 . THR A 101 ? 0.34612 0.18245 0.32812 0.05722  -0.05663 -0.02719 430 THR A OG1 
810  C CG2 . THR A 101 ? 0.30130 0.19617 0.28795 0.03174  -0.03870 0.03368  430 THR A CG2 
811  N N   . GLY A 102 ? 0.23566 0.17154 0.20990 0.02556  -0.04445 0.01068  431 GLY A N   
812  C CA  . GLY A 102 ? 0.21021 0.16209 0.21690 -0.00163 -0.00340 -0.00434 431 GLY A CA  
813  C C   . GLY A 102 ? 0.18611 0.16552 0.19757 0.03667  0.00020  0.02634  431 GLY A C   
814  O O   . GLY A 102 ? 0.18489 0.19581 0.22012 0.02901  -0.00007 0.00255  431 GLY A O   
815  N N   . CYS A 103 ? 0.18980 0.15800 0.17587 0.02488  -0.00739 0.02326  432 CYS A N   
816  C CA  . CYS A 103 ? 0.18345 0.15271 0.18961 0.00877  -0.01346 0.01712  432 CYS A CA  
817  C C   . CYS A 103 ? 0.16244 0.16037 0.17249 0.01297  -0.00556 0.03256  432 CYS A C   
818  O O   . CYS A 103 ? 0.16251 0.18697 0.25758 0.00787  0.01952  0.03048  432 CYS A O   
819  C CB  . CYS A 103 ? 0.21700 0.20229 0.20375 0.02848  -0.04868 0.05637  432 CYS A CB  
820  S SG  . CYS A 103 ? 0.21652 0.22643 0.22622 0.02527  -0.03405 0.05418  432 CYS A SG  
821  N N   . VAL A 104 ? 0.15854 0.14774 0.15653 0.00896  -0.00289 0.01002  433 VAL A N   
822  C CA  . VAL A 104 ? 0.16055 0.15853 0.14291 0.00553  -0.01294 0.00673  433 VAL A CA  
823  C C   . VAL A 104 ? 0.12199 0.17341 0.16498 0.01393  0.00865  0.01578  433 VAL A C   
824  O O   . VAL A 104 ? 0.13781 0.18175 0.15929 0.01552  -0.00169 -0.00258 433 VAL A O   
825  C CB  . VAL A 104 ? 0.15697 0.16885 0.16103 0.01216  -0.01563 0.02300  433 VAL A CB  
826  C CG1 . VAL A 104 ? 0.19761 0.15861 0.15655 0.02661  -0.02615 0.00326  433 VAL A CG1 
827  C CG2 . VAL A 104 ? 0.17935 0.17250 0.15385 0.00125  -0.02912 -0.00280 433 VAL A CG2 
828  N N   . ILE A 105 ? 0.13476 0.17647 0.14115 0.01695  -0.00620 0.00730  434 ILE A N   
829  C CA  . ILE A 105 ? 0.16848 0.15782 0.13398 0.00900  -0.02080 0.00326  434 ILE A CA  
830  C C   . ILE A 105 ? 0.12702 0.16186 0.17259 0.00776  -0.02095 0.01021  434 ILE A C   
831  O O   . ILE A 105 ? 0.12512 0.18896 0.22672 0.01946  -0.02009 -0.00292 434 ILE A O   
832  C CB  . ILE A 105 ? 0.17972 0.15919 0.14954 0.01322  -0.01677 -0.00389 434 ILE A CB  
833  C CG1 . ILE A 105 ? 0.17906 0.18973 0.17311 0.01729  -0.00480 0.03648  434 ILE A CG1 
834  C CG2 . ILE A 105 ? 0.15392 0.22070 0.16645 0.01736  0.00180  0.01268  434 ILE A CG2 
835  C CD1 . ILE A 105 ? 0.21267 0.24225 0.17365 0.00365  0.01032  0.05223  434 ILE A CD1 
836  N N   . ALA A 106 ? 0.14914 0.15726 0.14985 0.00836  -0.00404 -0.00125 435 ALA A N   
837  C CA  . ALA A 106 ? 0.16390 0.16480 0.14507 0.01372  -0.01712 0.02303  435 ALA A CA  
838  C C   . ALA A 106 ? 0.14627 0.17674 0.16735 0.00724  -0.03026 0.00212  435 ALA A C   
839  O O   . ALA A 106 ? 0.16402 0.17660 0.21523 0.01651  -0.05299 -0.00097 435 ALA A O   
840  C CB  . ALA A 106 ? 0.18532 0.20481 0.18140 0.01297  -0.03862 0.01101  435 ALA A CB  
841  N N   . TRP A 107 ? 0.17046 0.15282 0.19496 0.02451  -0.02353 -0.01496 436 TRP A N   
842  C CA  . TRP A 107 ? 0.16549 0.16918 0.18550 0.02909  -0.04105 0.00819  436 TRP A CA  
843  C C   . TRP A 107 ? 0.16053 0.16747 0.18066 0.02565  -0.05447 -0.00064 436 TRP A C   
844  O O   . TRP A 107 ? 0.16060 0.18058 0.18569 0.00693  -0.05880 -0.00502 436 TRP A O   
845  C CB  . TRP A 107 ? 0.17619 0.20324 0.19212 0.03293  -0.05369 0.00483  436 TRP A CB  
846  C CG  . TRP A 107 ? 0.19991 0.22599 0.15298 0.03905  -0.04100 0.00100  436 TRP A CG  
847  C CD1 . TRP A 107 ? 0.21752 0.26621 0.16583 0.05518  -0.04293 -0.00843 436 TRP A CD1 
848  C CD2 . TRP A 107 ? 0.17951 0.22027 0.16340 0.03554  -0.03528 0.02963  436 TRP A CD2 
849  N NE1 . TRP A 107 ? 0.22984 0.26946 0.16785 0.05450  -0.01944 -0.03183 436 TRP A NE1 
850  C CE2 . TRP A 107 ? 0.19813 0.22676 0.16553 0.02796  -0.02411 0.00593  436 TRP A CE2 
851  C CE3 . TRP A 107 ? 0.19641 0.19668 0.17172 0.02460  -0.03488 0.01649  436 TRP A CE3 
852  C CZ2 . TRP A 107 ? 0.20852 0.24043 0.17169 0.04649  0.00621  0.04165  436 TRP A CZ2 
853  C CZ3 . TRP A 107 ? 0.19706 0.19958 0.19674 0.02278  -0.01634 0.02624  436 TRP A CZ3 
854  C CH2 . TRP A 107 ? 0.22229 0.24620 0.17627 0.06951  -0.01117 0.01951  436 TRP A CH2 
855  N N   . ASN A 108 ? 0.17457 0.17075 0.20299 -0.00198 -0.06133 -0.01313 437 ASN A N   
856  C CA  . ASN A 108 ? 0.20558 0.17092 0.19223 0.00570  -0.04449 -0.00898 437 ASN A CA  
857  C C   . ASN A 108 ? 0.20573 0.17983 0.19596 0.02525  -0.09008 -0.00474 437 ASN A C   
858  O O   . ASN A 108 ? 0.19998 0.21279 0.22097 0.03502  -0.08593 -0.02246 437 ASN A O   
859  C CB  . ASN A 108 ? 0.20025 0.15814 0.28569 -0.01306 -0.05602 -0.00197 437 ASN A CB  
860  C CG  . ASN A 108 ? 0.18364 0.15827 0.28780 0.00078  -0.07659 0.00461  437 ASN A CG  
861  O OD1 . ASN A 108 ? 0.19647 0.18889 0.29318 0.02958  -0.06612 -0.02161 437 ASN A OD1 
862  N ND2 . ASN A 108 ? 0.20192 0.20249 0.29734 -0.00794 -0.06963 0.02550  437 ASN A ND2 
863  N N   . SER A 109 ? 0.19002 0.17190 0.17682 0.01924  -0.06023 -0.02033 438 SER A N   
864  C CA  . SER A 109 ? 0.20460 0.19673 0.16904 0.03209  -0.04085 -0.00183 438 SER A CA  
865  C C   . SER A 109 ? 0.21611 0.15950 0.15804 0.03195  -0.05508 -0.00981 438 SER A C   
866  O O   . SER A 109 ? 0.21509 0.18715 0.19097 0.04513  -0.05466 -0.02569 438 SER A O   
867  C CB  . SER A 109 ? 0.20382 0.20928 0.15748 0.00594  -0.06368 0.00160  438 SER A CB  
868  O OG  . SER A 109 ? 0.18524 0.18785 0.15988 0.00864  -0.04111 -0.00411 438 SER A OG  
869  N N   . ASN A 110 ? 0.22980 0.15953 0.19096 0.01878  -0.05657 -0.01690 439 ASN A N   
870  C CA  . ASN A 110 ? 0.22098 0.17057 0.18958 0.02546  -0.05458 -0.02842 439 ASN A CA  
871  C C   . ASN A 110 ? 0.23641 0.18452 0.20433 0.02851  -0.07828 -0.03741 439 ASN A C   
872  O O   . ASN A 110 ? 0.27574 0.18073 0.23990 0.03744  -0.04098 -0.01383 439 ASN A O   
873  C CB  . ASN A 110 ? 0.22193 0.18094 0.21388 0.01063  -0.05750 -0.00672 439 ASN A CB  
874  C CG  . ASN A 110 ? 0.24249 0.18182 0.22948 0.02493  -0.05746 -0.02582 439 ASN A CG  
875  O OD1 . ASN A 110 ? 0.27251 0.19302 0.22093 -0.00146 -0.07178 0.00548  439 ASN A OD1 
876  N ND2 . ASN A 110 ? 0.26229 0.19373 0.29500 -0.00238 -0.08805 -0.02016 439 ASN A ND2 
877  N N   . ASN A 111 ? 0.25828 0.23342 0.19483 0.03693  -0.07493 -0.04590 440 ASN A N   
878  C CA  . ASN A 111 ? 0.26830 0.27446 0.18570 0.01226  -0.04999 -0.07486 440 ASN A CA  
879  C C   . ASN A 111 ? 0.28488 0.27610 0.20570 0.02695  -0.03136 -0.06375 440 ASN A C   
880  O O   . ASN A 111 ? 0.32186 0.27951 0.32246 0.02206  0.03191  -0.08462 440 ASN A O   
881  C CB  . ASN A 111 ? 0.33039 0.34995 0.21853 0.04063  -0.09437 -0.09669 440 ASN A CB  
882  C CG  . ASN A 111 ? 0.37391 0.40100 0.23958 0.07853  -0.06599 -0.01971 440 ASN A CG  
883  O OD1 . ASN A 111 ? 0.41231 0.38677 0.26820 0.10111  -0.07573 0.02238  440 ASN A OD1 
884  N ND2 . ASN A 111 ? 0.40464 0.41112 0.27124 0.08772  -0.07052 0.00948  440 ASN A ND2 
885  N N   . LEU A 112 ? 0.25494 0.24339 0.18492 0.01501  -0.05881 -0.02357 441 LEU A N   
886  C CA  . LEU A 112 ? 0.29666 0.23580 0.16391 0.03752  -0.01660 -0.00108 441 LEU A CA  
887  C C   . LEU A 112 ? 0.26015 0.21809 0.16366 0.05599  -0.02250 0.01081  441 LEU A C   
888  O O   . LEU A 112 ? 0.28998 0.26616 0.18781 0.05334  0.00372  -0.01638 441 LEU A O   
889  C CB  . LEU A 112 ? 0.32283 0.26212 0.17835 0.06101  -0.06158 0.02844  441 LEU A CB  
890  C CG  . LEU A 112 ? 0.36638 0.32202 0.25495 0.02527  -0.09613 -0.00234 441 LEU A CG  
891  C CD1 . LEU A 112 ? 0.40532 0.32897 0.26465 0.01213  -0.07943 0.08242  441 LEU A CD1 
892  C CD2 . LEU A 112 ? 0.41017 0.36406 0.27478 0.01682  -0.03008 0.01047  441 LEU A CD2 
893  N N   . ASP A 113 ? 0.22081 0.19521 0.13824 0.00980  -0.01527 0.00936  442 ASP A N   
894  C CA  . ASP A 113 ? 0.22865 0.15410 0.14756 0.00946  -0.03385 -0.00166 442 ASP A CA  
895  C C   . ASP A 113 ? 0.19922 0.18335 0.18356 0.00604  -0.03527 0.00978  442 ASP A C   
896  O O   . ASP A 113 ? 0.19204 0.21566 0.17060 0.00972  -0.05156 0.01778  442 ASP A O   
897  C CB  . ASP A 113 ? 0.18891 0.17666 0.17068 0.01211  -0.00616 -0.00574 442 ASP A CB  
898  C CG  . ASP A 113 ? 0.16600 0.20492 0.14446 -0.00332 -0.03391 0.00208  442 ASP A CG  
899  O OD1 . ASP A 113 ? 0.17071 0.18559 0.14989 0.00816  -0.02502 0.00268  442 ASP A OD1 
900  O OD2 . ASP A 113 ? 0.18595 0.19282 0.15423 0.03273  -0.01968 0.00750  442 ASP A OD2 
901  N N   . SER A 114 ? 0.22440 0.16077 0.18242 0.02152  -0.03442 0.00364  443 SER A N   
902  C CA  . SER A 114 ? 0.23520 0.13826 0.18300 0.01462  -0.04395 0.01561  443 SER A CA  
903  C C   . SER A 114 ? 0.25933 0.15257 0.15896 0.03904  -0.02084 0.01486  443 SER A C   
904  O O   . SER A 114 ? 0.30536 0.24341 0.15903 0.06929  -0.00483 0.02148  443 SER A O   
905  C CB  . SER A 114 ? 0.24287 0.18913 0.21055 -0.01161 -0.04098 -0.03376 443 SER A CB  
906  O OG  . SER A 114 ? 0.27717 0.20326 0.25601 0.01355  -0.06284 -0.01586 443 SER A OG  
907  N N   . LYS A 115 ? 0.23561 0.14841 0.15258 0.02290  -0.01812 -0.00655 444 LYS A N   
908  C CA  . LYS A 115 ? 0.22571 0.14921 0.18554 0.02880  -0.03286 -0.01053 444 LYS A CA  
909  C C   . LYS A 115 ? 0.21369 0.14573 0.17243 0.02738  -0.05765 -0.02791 444 LYS A C   
910  O O   . LYS A 115 ? 0.20358 0.17740 0.15683 0.03146  -0.04530 -0.01962 444 LYS A O   
911  C CB  . LYS A 115 ? 0.22233 0.19210 0.17551 -0.02909 -0.02012 -0.01212 444 LYS A CB  
912  C CG  . LYS A 115 ? 0.21562 0.23034 0.21896 -0.01689 -0.00632 0.01148  444 LYS A CG  
913  C CD  . LYS A 115 ? 0.24651 0.25629 0.23791 -0.02195 0.01508  0.01427  444 LYS A CD  
914  C CE  . LYS A 115 ? 0.27513 0.28614 0.30029 0.03893  0.03715  0.04240  444 LYS A CE  
915  N NZ  . LYS A 115 ? 0.33382 0.30886 0.26219 0.04656  0.02158  -0.03279 444 LYS A NZ  
916  N N   . VAL A 116 ? 0.21219 0.15896 0.18846 -0.00078 -0.03615 -0.01712 445 VAL A N   
917  C CA  . VAL A 116 ? 0.19301 0.16697 0.20501 -0.00971 -0.02733 -0.03434 445 VAL A CA  
918  C C   . VAL A 116 ? 0.18389 0.14973 0.22489 -0.02033 -0.01983 -0.01074 445 VAL A C   
919  O O   . VAL A 116 ? 0.19257 0.17435 0.24343 -0.01904 -0.03619 -0.01056 445 VAL A O   
920  C CB  . VAL A 116 ? 0.23292 0.16138 0.20779 -0.00554 -0.02501 -0.04351 445 VAL A CB  
921  C CG1 . VAL A 116 ? 0.22331 0.15946 0.23819 -0.00013 0.01016  -0.02687 445 VAL A CG1 
922  C CG2 . VAL A 116 ? 0.24453 0.24008 0.25248 0.01323  -0.07492 -0.08882 445 VAL A CG2 
923  N N   . GLY A 117 ? 0.23854 0.14338 0.20641 -0.00347 -0.03096 -0.00813 446 GLY A N   
924  C CA  . GLY A 117 ? 0.24721 0.16148 0.23176 -0.02306 -0.08977 -0.00823 446 GLY A CA  
925  C C   . GLY A 117 ? 0.21752 0.17432 0.19919 -0.03543 -0.07252 0.00120  446 GLY A C   
926  O O   . GLY A 117 ? 0.24730 0.18336 0.24949 -0.02895 -0.10215 0.00267  446 GLY A O   
927  N N   . GLY A 118 ? 0.18988 0.14990 0.21037 0.00665  -0.04321 -0.00827 447 GLY A N   
928  C CA  . GLY A 118 ? 0.19202 0.14576 0.24385 -0.01117 -0.02853 -0.02379 447 GLY A CA  
929  C C   . GLY A 118 ? 0.18653 0.16809 0.19695 0.00844  -0.04934 -0.02548 447 GLY A C   
930  O O   . GLY A 118 ? 0.19023 0.17981 0.26453 0.01866  -0.04370 -0.00658 447 GLY A O   
931  N N   . ASN A 119 ? 0.20770 0.16024 0.16175 -0.01036 -0.01651 -0.00508 448 ASN A N   
932  C CA  . ASN A 119 ? 0.20257 0.17612 0.15993 -0.01257 -0.02449 0.00088  448 ASN A CA  
933  C C   . ASN A 119 ? 0.21024 0.16390 0.14222 -0.00966 -0.04377 -0.02322 448 ASN A C   
934  O O   . ASN A 119 ? 0.25326 0.22843 0.15712 -0.02232 -0.01601 -0.03283 448 ASN A O   
935  C CB  . ASN A 119 ? 0.21417 0.18275 0.19566 -0.00672 -0.05679 0.00667  448 ASN A CB  
936  C CG  . ASN A 119 ? 0.20932 0.20193 0.19731 -0.01392 -0.00478 0.00792  448 ASN A CG  
937  O OD1 . ASN A 119 ? 0.22232 0.22469 0.17412 0.00182  -0.01441 -0.00818 448 ASN A OD1 
938  N ND2 . ASN A 119 ? 0.22052 0.18612 0.20721 0.00716  -0.03844 0.00982  448 ASN A ND2 
939  N N   . TYR A 120 ? 0.18670 0.20606 0.19956 -0.02529 -0.04151 0.02759  449 TYR A N   
940  C CA  . TYR A 120 ? 0.20632 0.23078 0.19504 -0.02830 -0.07689 0.01590  449 TYR A CA  
941  C C   . TYR A 120 ? 0.17984 0.22422 0.19366 -0.00969 -0.02754 -0.01203 449 TYR A C   
942  O O   . TYR A 120 ? 0.22714 0.25571 0.22894 -0.02092 -0.06324 -0.03761 449 TYR A O   
943  C CB  . TYR A 120 ? 0.23968 0.26873 0.26978 0.03426  -0.10390 0.00383  449 TYR A CB  
944  C CG  . TYR A 120 ? 0.18484 0.27173 0.31239 0.02103  -0.09560 -0.02900 449 TYR A CG  
945  C CD1 . TYR A 120 ? 0.21357 0.30137 0.33994 0.05615  -0.08168 -0.06301 449 TYR A CD1 
946  C CD2 . TYR A 120 ? 0.16992 0.31796 0.28468 0.02747  -0.06161 -0.02788 449 TYR A CD2 
947  C CE1 . TYR A 120 ? 0.19143 0.32614 0.34002 0.04987  -0.05638 -0.03849 449 TYR A CE1 
948  C CE2 . TYR A 120 ? 0.19999 0.33293 0.33829 0.01150  -0.00905 -0.03456 449 TYR A CE2 
949  C CZ  . TYR A 120 ? 0.19953 0.32519 0.34635 0.01780  -0.01325 -0.04831 449 TYR A CZ  
950  O OH  . TYR A 120 ? 0.21930 0.36235 0.39383 0.01545  -0.01060 -0.09958 449 TYR A OH  
951  N N   . ASN A 121 ? 0.16868 0.18983 0.18309 -0.00534 0.00248  -0.00926 450 ASN A N   
952  C CA  A ASN A 121 ? 0.21496 0.20255 0.18164 -0.00455 0.04910  -0.01228 450 ASN A CA  
953  C CA  B ASN A 121 ? 0.22284 0.21547 0.19809 0.00698  0.03849  -0.01224 450 ASN A CA  
954  C C   . ASN A 121 ? 0.18545 0.18580 0.18568 -0.03054 -0.00622 -0.00711 450 ASN A C   
955  O O   . ASN A 121 ? 0.18478 0.20853 0.35311 -0.01822 0.04738  -0.04947 450 ASN A O   
956  C CB  A ASN A 121 ? 0.31382 0.27200 0.23306 0.00653  0.08354  0.01138  450 ASN A CB  
957  C CB  B ASN A 121 ? 0.31147 0.29825 0.23386 0.01494  0.05065  -0.01868 450 ASN A CB  
958  C CG  A ASN A 121 ? 0.37301 0.39693 0.37676 0.03814  0.01006  -0.00667 450 ASN A CG  
959  C CG  B ASN A 121 ? 0.38226 0.40033 0.36495 0.02884  -0.01234 -0.02835 450 ASN A CG  
960  O OD1 A ASN A 121 ? 0.37712 0.41487 0.38335 0.02553  -0.00040 -0.03370 450 ASN A OD1 
961  O OD1 B ASN A 121 ? 0.42410 0.43225 0.40647 0.04029  -0.00398 -0.01422 450 ASN A OD1 
962  N ND2 A ASN A 121 ? 0.39526 0.42049 0.42411 0.03694  -0.00696 -0.01474 450 ASN A ND2 
963  N ND2 B ASN A 121 ? 0.40507 0.42398 0.39852 0.02913  0.00386  0.00024  450 ASN A ND2 
964  N N   . TYR A 122 ? 0.15040 0.21193 0.11880 -0.00011 -0.00684 0.00031  451 TYR A N   
965  C CA  . TYR A 122 ? 0.14295 0.18107 0.11601 0.02369  -0.01757 -0.01256 451 TYR A CA  
966  C C   . TYR A 122 ? 0.11841 0.16127 0.12407 0.00435  -0.01016 -0.00626 451 TYR A C   
967  O O   . TYR A 122 ? 0.14830 0.17255 0.13124 -0.00636 -0.00524 0.00125  451 TYR A O   
968  C CB  . TYR A 122 ? 0.13707 0.20966 0.12421 0.01465  -0.01746 0.00320  451 TYR A CB  
969  C CG  . TYR A 122 ? 0.12822 0.19059 0.11421 0.00983  -0.01137 0.00397  451 TYR A CG  
970  C CD1 . TYR A 122 ? 0.19233 0.18801 0.12389 -0.01450 -0.01345 0.01467  451 TYR A CD1 
971  C CD2 . TYR A 122 ? 0.15130 0.17562 0.13496 0.00253  -0.02216 -0.01862 451 TYR A CD2 
972  C CE1 . TYR A 122 ? 0.24426 0.19955 0.13582 -0.00588 -0.04242 0.00712  451 TYR A CE1 
973  C CE2 . TYR A 122 ? 0.18902 0.20993 0.12082 0.02928  -0.02531 0.00971  451 TYR A CE2 
974  C CZ  . TYR A 122 ? 0.20977 0.19926 0.12351 0.00827  -0.01116 0.01669  451 TYR A CZ  
975  O OH  . TYR A 122 ? 0.24096 0.24727 0.14995 -0.00792 -0.02171 0.01434  451 TYR A OH  
976  N N   . LEU A 123 ? 0.14128 0.16099 0.12634 0.00844  -0.02714 -0.00547 452 LEU A N   
977  C CA  . LEU A 123 ? 0.15413 0.17027 0.12623 0.02496  -0.03073 -0.00770 452 LEU A CA  
978  C C   . LEU A 123 ? 0.14984 0.15316 0.12716 0.00753  -0.02085 0.01318  452 LEU A C   
979  O O   . LEU A 123 ? 0.14941 0.16307 0.12495 0.00454  -0.00252 -0.00189 452 LEU A O   
980  C CB  . LEU A 123 ? 0.11210 0.20922 0.16837 0.01311  -0.01209 -0.02595 452 LEU A CB  
981  C CG  . LEU A 123 ? 0.12873 0.18819 0.14711 -0.00802 -0.02568 -0.00427 452 LEU A CG  
982  C CD1 . LEU A 123 ? 0.14352 0.22976 0.19830 0.02288  -0.01391 -0.01800 452 LEU A CD1 
983  C CD2 . LEU A 123 ? 0.16165 0.21534 0.17325 -0.00126 -0.01255 0.02681  452 LEU A CD2 
984  N N   . TYR A 124 ? 0.14415 0.17957 0.11878 0.00213  -0.01882 -0.00565 453 TYR A N   
985  C CA  . TYR A 124 ? 0.13619 0.19374 0.11000 0.02518  -0.03727 -0.02882 453 TYR A CA  
986  C C   . TYR A 124 ? 0.12783 0.16670 0.12886 0.00893  -0.00998 0.00103  453 TYR A C   
987  O O   . TYR A 124 ? 0.16338 0.16907 0.13580 0.02084  -0.02997 -0.00139 453 TYR A O   
988  C CB  . TYR A 124 ? 0.13341 0.16525 0.15169 -0.00778 -0.02280 0.01948  453 TYR A CB  
989  C CG  . TYR A 124 ? 0.15043 0.19940 0.12192 0.02203  -0.02021 -0.02152 453 TYR A CG  
990  C CD1 . TYR A 124 ? 0.14246 0.20218 0.16368 -0.01769 -0.00553 0.01750  453 TYR A CD1 
991  C CD2 . TYR A 124 ? 0.16749 0.26216 0.17611 -0.01031 -0.03388 0.00750  453 TYR A CD2 
992  C CE1 . TYR A 124 ? 0.18432 0.22828 0.22352 -0.03562 -0.01276 0.05735  453 TYR A CE1 
993  C CE2 . TYR A 124 ? 0.22152 0.30872 0.19653 -0.03317 -0.02912 0.07766  453 TYR A CE2 
994  C CZ  . TYR A 124 ? 0.25280 0.29508 0.25036 -0.04292 -0.01648 0.13588  453 TYR A CZ  
995  O OH  . TYR A 124 ? 0.33534 0.33918 0.33522 -0.05858 0.00488  0.17497  453 TYR A OH  
996  N N   . ARG A 125 ? 0.13680 0.16537 0.11203 0.01099  -0.00657 -0.01428 454 ARG A N   
997  C CA  . ARG A 125 ? 0.14814 0.16539 0.10337 -0.00532 0.00292  -0.01507 454 ARG A CA  
998  C C   . ARG A 125 ? 0.13713 0.17219 0.12743 0.01310  -0.03686 -0.02034 454 ARG A C   
999  O O   . ARG A 125 ? 0.13458 0.18924 0.13884 0.01275  -0.01785 0.00453  454 ARG A O   
1000 C CB  . ARG A 125 ? 0.14215 0.17293 0.11846 -0.01136 -0.00849 -0.01032 454 ARG A CB  
1001 C CG  . ARG A 125 ? 0.14298 0.17598 0.12633 0.01219  -0.01470 -0.00625 454 ARG A CG  
1002 C CD  . ARG A 125 ? 0.13580 0.17247 0.16467 -0.01805 -0.00473 -0.01980 454 ARG A CD  
1003 N NE  . ARG A 125 ? 0.12133 0.19093 0.15557 -0.01221 -0.01181 0.00221  454 ARG A NE  
1004 C CZ  . ARG A 125 ? 0.12433 0.19262 0.15458 -0.01561 -0.02271 -0.00912 454 ARG A CZ  
1005 N NH1 . ARG A 125 ? 0.14812 0.21249 0.14610 -0.00306 -0.03249 0.01571  454 ARG A NH1 
1006 N NH2 . ARG A 125 ? 0.15056 0.20583 0.14494 -0.01044 0.01228  0.00917  454 ARG A NH2 
1007 N N   . LEU A 126 ? 0.15080 0.17593 0.13197 0.00743  -0.01434 0.00522  455 LEU A N   
1008 C CA  . LEU A 126 ? 0.19459 0.19758 0.10221 0.00327  -0.01274 0.01465  455 LEU A CA  
1009 C C   . LEU A 126 ? 0.15544 0.18422 0.12891 -0.00180 -0.00405 0.03432  455 LEU A C   
1010 O O   . LEU A 126 ? 0.18229 0.20728 0.16856 -0.00856 0.01376  -0.01075 455 LEU A O   
1011 C CB  . LEU A 126 ? 0.31378 0.24080 0.18717 -0.00977 0.03604  -0.00246 455 LEU A CB  
1012 C CG  . LEU A 126 ? 0.31381 0.24464 0.22828 -0.01066 -0.02966 0.02691  455 LEU A CG  
1013 C CD1 . LEU A 126 ? 0.30471 0.32759 0.26505 -0.03120 -0.01186 0.03865  455 LEU A CD1 
1014 C CD2 . LEU A 126 ? 0.36799 0.17511 0.26726 -0.00766 0.00086  0.01218  455 LEU A CD2 
1015 N N   . PHE A 127 ? 0.18381 0.18150 0.14237 -0.01339 -0.01744 -0.00631 456 PHE A N   
1016 C CA  . PHE A 127 ? 0.22408 0.18719 0.15125 -0.02917 -0.02025 0.01501  456 PHE A CA  
1017 C C   . PHE A 127 ? 0.22187 0.19572 0.11669 -0.01335 -0.02106 0.00986  456 PHE A C   
1018 O O   . PHE A 127 ? 0.19688 0.19609 0.13536 -0.01728 -0.02225 0.00167  456 PHE A O   
1019 C CB  . PHE A 127 ? 0.22612 0.20202 0.16781 0.00929  -0.04308 -0.00149 456 PHE A CB  
1020 C CG  . PHE A 127 ? 0.19994 0.21413 0.16021 -0.01466 -0.04355 0.02941  456 PHE A CG  
1021 C CD1 . PHE A 127 ? 0.25954 0.25541 0.18914 0.01419  0.03669  0.04362  456 PHE A CD1 
1022 C CD2 . PHE A 127 ? 0.18039 0.23726 0.21180 0.02025  -0.00974 0.02272  456 PHE A CD2 
1023 C CE1 . PHE A 127 ? 0.23784 0.25999 0.21555 0.02827  0.02506  0.05996  456 PHE A CE1 
1024 C CE2 . PHE A 127 ? 0.17034 0.25811 0.19428 0.01394  -0.00875 0.04013  456 PHE A CE2 
1025 C CZ  . PHE A 127 ? 0.20045 0.27682 0.17999 0.03366  0.00177  0.03712  456 PHE A CZ  
1026 N N   . ARG A 128 ? 0.21594 0.18401 0.13468 -0.01620 -0.00605 -0.00773 457 ARG A N   
1027 C CA  . ARG A 128 ? 0.19083 0.19993 0.15005 -0.00315 -0.01133 -0.02982 457 ARG A CA  
1028 C C   . ARG A 128 ? 0.20253 0.21285 0.16707 0.01752  -0.03252 -0.04065 457 ARG A C   
1029 O O   . ARG A 128 ? 0.23230 0.28171 0.17574 0.07269  -0.00202 -0.03066 457 ARG A O   
1030 C CB  . ARG A 128 ? 0.18458 0.20291 0.15881 -0.00771 -0.01211 0.01580  457 ARG A CB  
1031 C CG  . ARG A 128 ? 0.17846 0.20924 0.18091 -0.00704 -0.01199 -0.01185 457 ARG A CG  
1032 C CD  . ARG A 128 ? 0.21273 0.18457 0.17782 -0.02856 0.00786  0.01316  457 ARG A CD  
1033 N NE  . ARG A 128 ? 0.20343 0.20088 0.16003 -0.02960 0.00733  -0.02136 457 ARG A NE  
1034 C CZ  . ARG A 128 ? 0.23436 0.23065 0.19493 -0.04485 0.02130  -0.00475 457 ARG A CZ  
1035 N NH1 . ARG A 128 ? 0.25622 0.22369 0.18610 -0.02584 0.02419  -0.00919 457 ARG A NH1 
1036 N NH2 . ARG A 128 ? 0.23700 0.25109 0.23698 -0.08068 0.02058  -0.01406 457 ARG A NH2 
1037 N N   . LYS A 129 ? 0.26974 0.20766 0.19342 0.03523  -0.07675 -0.04308 458 LYS A N   
1038 C CA  A LYS A 129 ? 0.32310 0.27643 0.23683 0.03419  -0.10034 -0.09161 458 LYS A CA  
1039 C CA  B LYS A 129 ? 0.32315 0.27633 0.23685 0.03435  -0.10025 -0.09157 458 LYS A CA  
1040 C C   . LYS A 129 ? 0.35462 0.25750 0.22035 0.08316  -0.05124 -0.08208 458 LYS A C   
1041 O O   . LYS A 129 ? 0.47110 0.30829 0.21574 0.16607  -0.03106 -0.04104 458 LYS A O   
1042 C CB  A LYS A 129 ? 0.38807 0.38854 0.35713 0.02818  -0.07941 -0.05738 458 LYS A CB  
1043 C CB  B LYS A 129 ? 0.38801 0.38829 0.35721 0.02869  -0.07957 -0.05726 458 LYS A CB  
1044 C CG  A LYS A 129 ? 0.46024 0.48481 0.44182 0.03651  -0.06162 -0.03786 458 LYS A CG  
1045 C CG  B LYS A 129 ? 0.45997 0.48420 0.44389 0.03682  -0.06148 -0.03787 458 LYS A CG  
1046 C CD  A LYS A 129 ? 0.52131 0.55699 0.51795 0.04386  -0.04503 -0.02944 458 LYS A CD  
1047 C CD  B LYS A 129 ? 0.52010 0.55671 0.51694 0.04402  -0.04548 -0.02753 458 LYS A CD  
1048 C CE  A LYS A 129 ? 0.56022 0.58211 0.54273 0.04754  -0.03316 -0.02536 458 LYS A CE  
1049 C CE  B LYS A 129 ? 0.56277 0.58359 0.54254 0.04438  -0.03632 -0.02643 458 LYS A CE  
1050 N NZ  A LYS A 129 ? 0.57685 0.59295 0.54472 0.04703  -0.01833 -0.03852 458 LYS A NZ  
1051 N NZ  B LYS A 129 ? 0.57703 0.60451 0.55898 0.03643  -0.04190 -0.02748 458 LYS A NZ  
1052 N N   . SER A 130 ? 0.32811 0.22323 0.18539 0.06036  -0.05571 -0.01805 459 SER A N   
1053 C CA  . SER A 130 ? 0.28845 0.22165 0.16021 0.03564  -0.03518 -0.01748 459 SER A CA  
1054 C C   . SER A 130 ? 0.25113 0.19867 0.17235 0.01546  -0.00893 -0.00385 459 SER A C   
1055 O O   . SER A 130 ? 0.22800 0.21145 0.15857 0.00993  -0.00266 -0.01012 459 SER A O   
1056 C CB  . SER A 130 ? 0.29924 0.25401 0.19432 -0.01257 -0.05623 -0.02203 459 SER A CB  
1057 O OG  . SER A 130 ? 0.35737 0.27580 0.34960 -0.00701 -0.04703 -0.04211 459 SER A OG  
1058 N N   . ASN A 131 ? 0.24495 0.19422 0.15373 0.02358  0.00662  -0.00915 460 ASN A N   
1059 C CA  . ASN A 131 ? 0.20798 0.24499 0.15450 -0.02203 -0.00576 0.00827  460 ASN A CA  
1060 C C   . ASN A 131 ? 0.23128 0.19497 0.14755 -0.01277 0.00003  -0.00582 460 ASN A C   
1061 O O   . ASN A 131 ? 0.26224 0.20673 0.17111 -0.04858 -0.00089 -0.04818 460 ASN A O   
1062 C CB  . ASN A 131 ? 0.24557 0.32446 0.22363 -0.01826 0.02551  0.01609  460 ASN A CB  
1063 C CG  . ASN A 131 ? 0.33425 0.38747 0.36794 0.03202  0.00827  -0.01709 460 ASN A CG  
1064 O OD1 . ASN A 131 ? 0.36512 0.34891 0.43512 -0.00598 0.09774  -0.02206 460 ASN A OD1 
1065 N ND2 . ASN A 131 ? 0.36075 0.45328 0.46924 0.06069  0.02439  -0.07657 460 ASN A ND2 
1066 N N   . LEU A 132 ? 0.21377 0.18408 0.13469 -0.02117 0.00064  -0.01013 461 LEU A N   
1067 C CA  . LEU A 132 ? 0.23355 0.16540 0.13893 -0.00503 0.02440  -0.00949 461 LEU A CA  
1068 C C   . LEU A 132 ? 0.20303 0.18633 0.15604 -0.01372 -0.00878 -0.00769 461 LEU A C   
1069 O O   . LEU A 132 ? 0.21376 0.19229 0.18927 -0.01990 -0.00500 -0.01158 461 LEU A O   
1070 C CB  . LEU A 132 ? 0.21784 0.20906 0.16220 0.00513  -0.01261 -0.03448 461 LEU A CB  
1071 C CG  . LEU A 132 ? 0.22479 0.19040 0.17639 -0.00942 -0.00478 -0.02455 461 LEU A CG  
1072 C CD1 . LEU A 132 ? 0.25938 0.21254 0.14786 -0.03606 0.00693  -0.02999 461 LEU A CD1 
1073 C CD2 . LEU A 132 ? 0.19384 0.20597 0.20607 -0.01257 0.00840  -0.02576 461 LEU A CD2 
1074 N N   . LYS A 133 ? 0.23671 0.16466 0.19051 -0.02618 0.00126  -0.00820 462 LYS A N   
1075 C CA  . LYS A 133 ? 0.23178 0.16594 0.19983 -0.04029 -0.01081 -0.01227 462 LYS A CA  
1076 C C   . LYS A 133 ? 0.20027 0.14946 0.19934 -0.00886 0.00669  -0.01155 462 LYS A C   
1077 O O   . LYS A 133 ? 0.19767 0.16540 0.19639 -0.01420 0.01280  0.00252  462 LYS A O   
1078 C CB  . LYS A 133 ? 0.27739 0.18613 0.23041 -0.02993 -0.03443 -0.03363 462 LYS A CB  
1079 C CG  . LYS A 133 ? 0.33630 0.24035 0.35422 -0.06931 -0.05541 -0.08014 462 LYS A CG  
1080 C CD  . LYS A 133 ? 0.40955 0.37038 0.44490 -0.03929 -0.05479 -0.06159 462 LYS A CD  
1081 C CE  . LYS A 133 ? 0.47976 0.47595 0.55859 0.02454  -0.02569 -0.03930 462 LYS A CE  
1082 N NZ  . LYS A 133 ? 0.52177 0.51967 0.59643 0.06128  -0.03780 -0.02897 462 LYS A NZ  
1083 N N   . PRO A 134 ? 0.20417 0.18408 0.19249 -0.00619 -0.00106 -0.00498 463 PRO A N   
1084 C CA  . PRO A 134 ? 0.21681 0.16628 0.20308 0.01558  0.02570  -0.00597 463 PRO A CA  
1085 C C   . PRO A 134 ? 0.20215 0.16415 0.20201 0.00113  0.01010  0.00520  463 PRO A C   
1086 O O   . PRO A 134 ? 0.21683 0.18311 0.22823 -0.01827 0.00209  0.00689  463 PRO A O   
1087 C CB  . PRO A 134 ? 0.24029 0.18766 0.21352 0.01607  0.02005  -0.01315 463 PRO A CB  
1088 C CG  . PRO A 134 ? 0.24631 0.20071 0.22213 0.02589  0.02163  -0.02658 463 PRO A CG  
1089 C CD  . PRO A 134 ? 0.23245 0.19130 0.22401 0.03401  0.01100  -0.05274 463 PRO A CD  
1090 N N   . PHE A 135 ? 0.20589 0.16836 0.16193 0.00507  0.01128  -0.00214 464 PHE A N   
1091 C CA  . PHE A 135 ? 0.19877 0.16385 0.19451 -0.00131 0.00779  0.01383  464 PHE A CA  
1092 C C   . PHE A 135 ? 0.19133 0.17079 0.16413 -0.01413 0.00678  0.00609  464 PHE A C   
1093 O O   . PHE A 135 ? 0.19995 0.20536 0.19060 -0.01731 0.02988  0.01799  464 PHE A O   
1094 C CB  . PHE A 135 ? 0.19709 0.17567 0.19103 -0.02182 0.00407  0.02356  464 PHE A CB  
1095 C CG  . PHE A 135 ? 0.19589 0.18930 0.17662 -0.02125 0.00906  0.02484  464 PHE A CG  
1096 C CD1 . PHE A 135 ? 0.19744 0.21201 0.16653 -0.03334 0.00018  0.00727  464 PHE A CD1 
1097 C CD2 . PHE A 135 ? 0.21118 0.19320 0.21889 0.00629  0.01525  0.02497  464 PHE A CD2 
1098 C CE1 . PHE A 135 ? 0.20004 0.23743 0.17651 -0.00348 0.01369  0.00655  464 PHE A CE1 
1099 C CE2 . PHE A 135 ? 0.22721 0.21347 0.22820 -0.00232 -0.00206 0.02112  464 PHE A CE2 
1100 C CZ  . PHE A 135 ? 0.22916 0.21552 0.24387 -0.00908 0.01102  0.01862  464 PHE A CZ  
1101 N N   . GLU A 136 ? 0.19435 0.17442 0.17581 -0.01480 0.00377  0.00534  465 GLU A N   
1102 C CA  . GLU A 136 ? 0.19388 0.18215 0.17420 -0.00213 -0.00345 -0.00309 465 GLU A CA  
1103 C C   . GLU A 136 ? 0.15642 0.18492 0.19205 -0.02968 -0.00873 0.01227  465 GLU A C   
1104 O O   . GLU A 136 ? 0.17004 0.18008 0.20015 -0.00971 0.01261  -0.00327 465 GLU A O   
1105 C CB  . GLU A 136 ? 0.21581 0.22078 0.18319 -0.02415 -0.02130 0.01291  465 GLU A CB  
1106 C CG  . GLU A 136 ? 0.22084 0.29730 0.20552 -0.02346 -0.01285 0.00273  465 GLU A CG  
1107 C CD  . GLU A 136 ? 0.20277 0.30680 0.22319 -0.05375 -0.02064 -0.01114 465 GLU A CD  
1108 O OE1 . GLU A 136 ? 0.19939 0.29216 0.20582 -0.03828 -0.00826 -0.02771 465 GLU A OE1 
1109 O OE2 . GLU A 136 ? 0.24776 0.44127 0.28451 -0.02244 -0.01788 -0.02529 465 GLU A OE2 
1110 N N   . ARG A 137 ? 0.17614 0.18991 0.16963 -0.01371 -0.00154 -0.01820 466 ARG A N   
1111 C CA  . ARG A 137 ? 0.16767 0.18011 0.16598 -0.01631 0.00314  -0.00010 466 ARG A CA  
1112 C C   . ARG A 137 ? 0.16422 0.21173 0.18277 -0.02577 -0.00574 0.02083  466 ARG A C   
1113 O O   . ARG A 137 ? 0.17834 0.22736 0.22281 -0.03018 -0.03167 0.01243  466 ARG A O   
1114 C CB  . ARG A 137 ? 0.16964 0.18331 0.15579 -0.00749 0.01823  -0.00913 466 ARG A CB  
1115 C CG  . ARG A 137 ? 0.16563 0.22165 0.15605 -0.02171 0.00609  -0.00518 466 ARG A CG  
1116 C CD  . ARG A 137 ? 0.19730 0.23544 0.15948 -0.00906 0.01168  -0.00895 466 ARG A CD  
1117 N NE  . ARG A 137 ? 0.17725 0.23867 0.16253 0.00293  0.00889  -0.00864 466 ARG A NE  
1118 C CZ  . ARG A 137 ? 0.14353 0.22475 0.15762 -0.00858 0.02100  0.01012  466 ARG A CZ  
1119 N NH1 . ARG A 137 ? 0.15352 0.20406 0.17653 -0.02237 0.00179  -0.00196 466 ARG A NH1 
1120 N NH2 . ARG A 137 ? 0.20048 0.22115 0.17379 -0.01478 0.01334  -0.02557 466 ARG A NH2 
1121 N N   . ASP A 138 ? 0.16662 0.20244 0.14408 -0.01819 0.01523  0.00258  467 ASP A N   
1122 C CA  . ASP A 138 ? 0.15770 0.20485 0.14896 -0.00252 -0.02034 0.00593  467 ASP A CA  
1123 C C   . ASP A 138 ? 0.13668 0.21823 0.14669 -0.01719 -0.01948 0.00429  467 ASP A C   
1124 O O   . ASP A 138 ? 0.14871 0.20733 0.13964 -0.00627 -0.00242 0.00899  467 ASP A O   
1125 C CB  . ASP A 138 ? 0.17485 0.21414 0.14524 0.00310  -0.00959 -0.00375 467 ASP A CB  
1126 C CG  . ASP A 138 ? 0.16689 0.22674 0.15879 -0.01714 0.00372  -0.01900 467 ASP A CG  
1127 O OD1 . ASP A 138 ? 0.19428 0.23034 0.14884 -0.01117 -0.01656 -0.01682 467 ASP A OD1 
1128 O OD2 . ASP A 138 ? 0.19502 0.25387 0.14402 -0.00709 0.00253  -0.00574 467 ASP A OD2 
1129 N N   . ILE A 139 ? 0.15432 0.22417 0.14438 -0.00870 -0.00457 0.01102  468 ILE A N   
1130 C CA  . ILE A 139 ? 0.13708 0.22338 0.15346 -0.01142 0.00540  0.01813  468 ILE A CA  
1131 C C   . ILE A 139 ? 0.12252 0.22037 0.16416 -0.01812 0.00226  0.01962  468 ILE A C   
1132 O O   . ILE A 139 ? 0.17156 0.22418 0.16010 -0.00185 0.00033  0.01527  468 ILE A O   
1133 C CB  . ILE A 139 ? 0.16232 0.20417 0.13965 -0.01342 0.00948  0.02394  468 ILE A CB  
1134 C CG1 . ILE A 139 ? 0.18410 0.19876 0.17117 -0.03518 0.02763  0.02152  468 ILE A CG1 
1135 C CG2 . ILE A 139 ? 0.17694 0.23463 0.15201 -0.01706 -0.02747 0.02941  468 ILE A CG2 
1136 C CD1 . ILE A 139 ? 0.20788 0.20804 0.18646 -0.03088 0.03757  0.02644  468 ILE A CD1 
1137 N N   . SER A 140 ? 0.15715 0.22335 0.13678 -0.02023 -0.02319 0.00789  469 SER A N   
1138 C CA  . SER A 140 ? 0.17427 0.24606 0.15127 -0.00805 -0.02235 -0.01143 469 SER A CA  
1139 C C   . SER A 140 ? 0.14517 0.23092 0.14220 -0.02041 -0.01114 0.00809  469 SER A C   
1140 O O   . SER A 140 ? 0.15276 0.21554 0.13788 0.00549  -0.00732 0.00512  469 SER A O   
1141 C CB  . SER A 140 ? 0.18447 0.25180 0.16434 -0.03049 -0.01497 -0.00850 469 SER A CB  
1142 O OG  . SER A 140 ? 0.21027 0.23618 0.15461 -0.00264 -0.01893 -0.00398 469 SER A OG  
1143 N N   . THR A 141 ? 0.15461 0.21692 0.14478 -0.00541 -0.00393 -0.00577 470 THR A N   
1144 C CA  . THR A 141 ? 0.23866 0.21587 0.16775 0.02148  -0.05961 -0.02948 470 THR A CA  
1145 C C   . THR A 141 ? 0.17714 0.22895 0.15224 0.01497  -0.02008 -0.00734 470 THR A C   
1146 O O   . THR A 141 ? 0.20129 0.24137 0.18049 0.02556  -0.03238 -0.01083 470 THR A O   
1147 C CB  . THR A 141 ? 0.37956 0.32603 0.19602 0.11571  -0.09975 -0.03623 470 THR A CB  
1148 O OG1 . THR A 141 ? 0.36603 0.44859 0.15863 0.18786  -0.03833 -0.02236 470 THR A OG1 
1149 C CG2 . THR A 141 ? 0.38538 0.31328 0.23245 0.09775  -0.14306 -0.07252 470 THR A CG2 
1150 N N   . GLU A 142 ? 0.17053 0.21747 0.15169 -0.00585 -0.01121 0.00805  471 GLU A N   
1151 C CA  . GLU A 142 ? 0.17958 0.24498 0.12147 -0.00809 -0.01685 -0.01169 471 GLU A CA  
1152 C C   . GLU A 142 ? 0.15115 0.20934 0.12451 0.00901  -0.03469 -0.02294 471 GLU A C   
1153 O O   . GLU A 142 ? 0.14149 0.24129 0.16868 0.00093  -0.03797 -0.01692 471 GLU A O   
1154 C CB  . GLU A 142 ? 0.27446 0.27391 0.16878 -0.01206 -0.03823 -0.03225 471 GLU A CB  
1155 C CG  . GLU A 142 ? 0.36501 0.36137 0.34446 -0.00588 -0.03550 -0.04695 471 GLU A CG  
1156 C CD  . GLU A 142 ? 0.43392 0.43706 0.46103 -0.01487 0.00691  -0.01987 471 GLU A CD  
1157 O OE1 . GLU A 142 ? 0.45458 0.46627 0.52369 -0.03488 -0.00850 -0.03012 471 GLU A OE1 
1158 O OE2 . GLU A 142 ? 0.45684 0.43241 0.47748 -0.00065 -0.01107 -0.07107 471 GLU A OE2 
1159 N N   . ILE A 143 ? 0.14731 0.19996 0.12972 -0.00424 -0.00921 -0.02563 472 ILE A N   
1160 C CA  . ILE A 143 ? 0.15366 0.23087 0.11968 -0.02148 0.00931  -0.00034 472 ILE A CA  
1161 C C   . ILE A 143 ? 0.16076 0.24837 0.12107 -0.01878 0.00387  -0.01014 472 ILE A C   
1162 O O   . ILE A 143 ? 0.14977 0.26478 0.15731 -0.00024 -0.01131 -0.03815 472 ILE A O   
1163 C CB  . ILE A 143 ? 0.14915 0.24843 0.13107 0.00056  -0.01460 0.01838  472 ILE A CB  
1164 C CG1 . ILE A 143 ? 0.15432 0.24505 0.15341 -0.00104 -0.00819 -0.00876 472 ILE A CG1 
1165 C CG2 . ILE A 143 ? 0.15780 0.27802 0.17077 0.00540  -0.01444 0.03194  472 ILE A CG2 
1166 C CD1 . ILE A 143 ? 0.17487 0.23890 0.19678 -0.00553 -0.01594 -0.04920 472 ILE A CD1 
1167 N N   . TYR A 144 ? 0.15446 0.24608 0.12922 0.00576  -0.00071 -0.01148 473 TYR A N   
1168 C CA  . TYR A 144 ? 0.14362 0.26895 0.11094 0.02338  -0.01415 -0.00015 473 TYR A CA  
1169 C C   . TYR A 144 ? 0.15070 0.23710 0.16057 0.01413  0.00829  -0.01302 473 TYR A C   
1170 O O   . TYR A 144 ? 0.16023 0.25499 0.13493 0.01588  -0.01158 -0.01025 473 TYR A O   
1171 C CB  . TYR A 144 ? 0.14262 0.26920 0.13660 0.01906  -0.03030 -0.00244 473 TYR A CB  
1172 C CG  . TYR A 144 ? 0.13884 0.21694 0.14743 0.00936  -0.01263 -0.00564 473 TYR A CG  
1173 C CD1 . TYR A 144 ? 0.16225 0.25913 0.16035 0.02739  -0.01149 0.00734  473 TYR A CD1 
1174 C CD2 . TYR A 144 ? 0.18201 0.23265 0.20002 0.00922  0.03751  0.01360  473 TYR A CD2 
1175 C CE1 . TYR A 144 ? 0.22037 0.25484 0.17914 0.03817  0.00719  0.03438  473 TYR A CE1 
1176 C CE2 . TYR A 144 ? 0.20269 0.23962 0.17749 0.02439  0.03245  0.02961  473 TYR A CE2 
1177 C CZ  . TYR A 144 ? 0.22862 0.28200 0.19027 0.07065  0.03928  0.01416  473 TYR A CZ  
1178 O OH  . TYR A 144 ? 0.30402 0.35343 0.29376 0.14939  0.08989  0.02318  473 TYR A OH  
1179 N N   . GLN A 145 ? 0.15018 0.28647 0.13879 0.02419  -0.01614 -0.02938 474 GLN A N   
1180 C CA  . GLN A 145 ? 0.17750 0.30041 0.13821 0.01646  0.00012  -0.01956 474 GLN A CA  
1181 C C   . GLN A 145 ? 0.16593 0.30656 0.13528 0.03572  -0.00225 -0.05105 474 GLN A C   
1182 O O   . GLN A 145 ? 0.20968 0.30936 0.15920 0.04804  0.00904  -0.02780 474 GLN A O   
1183 C CB  . GLN A 145 ? 0.17811 0.32123 0.15568 -0.01586 -0.03535 -0.05363 474 GLN A CB  
1184 C CG  . GLN A 145 ? 0.21455 0.32642 0.18536 -0.00226 -0.03422 -0.03399 474 GLN A CG  
1185 C CD  . GLN A 145 ? 0.21644 0.37615 0.22221 -0.02942 -0.00121 -0.02989 474 GLN A CD  
1186 O OE1 . GLN A 145 ? 0.24403 0.35303 0.21856 -0.03408 -0.01336 -0.03469 474 GLN A OE1 
1187 N NE2 . GLN A 145 ? 0.24300 0.36165 0.20564 -0.03366 -0.02377 -0.04595 474 GLN A NE2 
1188 N N   . ALA A 146 ? 0.16945 0.30811 0.17332 0.01989  -0.00143 -0.04382 475 ALA A N   
1189 C CA  . ALA A 146 ? 0.17930 0.31527 0.18488 0.00465  0.03395  -0.03978 475 ALA A CA  
1190 C C   . ALA A 146 ? 0.18661 0.36995 0.16203 0.00604  0.01691  -0.02021 475 ALA A C   
1191 O O   . ALA A 146 ? 0.26216 0.43538 0.17987 0.07672  0.01498  -0.03989 475 ALA A O   
1192 C CB  . ALA A 146 ? 0.20858 0.30723 0.21488 -0.02723 -0.00489 -0.05498 475 ALA A CB  
1193 N N   . GLY A 147 ? 0.22847 0.34062 0.16843 -0.02891 -0.00988 -0.02046 476 GLY A N   
1194 C CA  . GLY A 147 ? 0.26914 0.36771 0.18502 -0.06771 -0.03662 -0.00352 476 GLY A CA  
1195 C C   . GLY A 147 ? 0.26384 0.37024 0.16829 -0.07358 -0.01446 -0.03178 476 GLY A C   
1196 O O   . GLY A 147 ? 0.26749 0.37142 0.19035 -0.06580 0.03486  -0.01547 476 GLY A O   
1197 N N   . SER A 148 ? 0.23759 0.40087 0.14733 -0.10288 0.01058  -0.04629 477 SER A N   
1198 C CA  A SER A 148 ? 0.24163 0.39383 0.15724 -0.07580 0.02211  -0.07665 477 SER A CA  
1199 C CA  B SER A 148 ? 0.24238 0.38890 0.16302 -0.06564 0.01446  -0.06884 477 SER A CA  
1200 C C   . SER A 148 ? 0.24102 0.36390 0.21505 -0.10120 0.05903  -0.04109 477 SER A C   
1201 O O   . SER A 148 ? 0.24505 0.36026 0.27947 -0.10524 0.01949  -0.07258 477 SER A O   
1202 C CB  A SER A 148 ? 0.26538 0.43359 0.15801 0.00652  0.02277  -0.06092 477 SER A CB  
1203 C CB  B SER A 148 ? 0.26418 0.40239 0.18557 0.01006  -0.00045 -0.06568 477 SER A CB  
1204 O OG  A SER A 148 ? 0.31618 0.43121 0.15815 -0.02842 0.02672  0.02245  477 SER A OG  
1205 O OG  B SER A 148 ? 0.27747 0.38075 0.24955 0.00704  -0.03161 -0.10095 477 SER A OG  
1206 N N   . THR A 149 ? 0.25756 0.33763 0.18473 -0.09790 0.03288  -0.02605 478 THR A N   
1207 C CA  . THR A 149 ? 0.25227 0.33395 0.18978 -0.08035 0.02283  0.01322  478 THR A CA  
1208 C C   . THR A 149 ? 0.24645 0.28797 0.13692 -0.06219 0.01314  0.00625  478 THR A C   
1209 O O   . THR A 149 ? 0.22814 0.31613 0.16425 -0.06699 0.01255  -0.01757 478 THR A O   
1210 C CB  . THR A 149 ? 0.29926 0.35242 0.21102 -0.05164 0.03192  0.06292  478 THR A CB  
1211 O OG1 . THR A 149 ? 0.35029 0.39232 0.27702 -0.04301 0.03207  0.05740  478 THR A OG1 
1212 C CG2 . THR A 149 ? 0.31534 0.37366 0.23419 -0.00338 -0.02442 0.03054  478 THR A CG2 
1213 N N   . PRO A 150 ? 0.21861 0.29015 0.15529 -0.07952 0.01015  -0.02453 479 PRO A N   
1214 C CA  A PRO A 150 ? 0.20207 0.26565 0.15648 -0.07158 0.01883  -0.02020 479 PRO A CA  
1215 C CA  B PRO A 150 ? 0.20152 0.26628 0.15700 -0.07134 0.01934  -0.02145 479 PRO A CA  
1216 C C   . PRO A 150 ? 0.19017 0.21971 0.15457 -0.04581 -0.01691 -0.02245 479 PRO A C   
1217 O O   . PRO A 150 ? 0.23774 0.22436 0.17287 -0.01051 -0.00918 0.00210  479 PRO A O   
1218 C CB  A PRO A 150 ? 0.21439 0.29147 0.16499 -0.07014 0.00292  -0.04882 479 PRO A CB  
1219 C CB  B PRO A 150 ? 0.21516 0.29067 0.16779 -0.07423 -0.00378 -0.04393 479 PRO A CB  
1220 C CG  A PRO A 150 ? 0.20645 0.33726 0.17143 -0.05807 -0.00278 -0.06890 479 PRO A CG  
1221 C CG  B PRO A 150 ? 0.21591 0.32304 0.19112 -0.05673 -0.03367 -0.05487 479 PRO A CG  
1222 C CD  A PRO A 150 ? 0.21671 0.31268 0.17727 -0.09557 -0.00381 -0.00525 479 PRO A CD  
1223 C CD  B PRO A 150 ? 0.21560 0.32038 0.17533 -0.07684 -0.02754 -0.01673 479 PRO A CD  
1224 N N   . CYS A 151 ? 0.17292 0.21637 0.13866 -0.03607 -0.01096 -0.00822 480 CYS A N   
1225 C CA  . CYS A 151 ? 0.15453 0.23486 0.13222 -0.01211 -0.03217 -0.00970 480 CYS A CA  
1226 C C   . CYS A 151 ? 0.15609 0.21543 0.16214 0.00628  -0.01958 -0.00191 480 CYS A C   
1227 O O   . CYS A 151 ? 0.17786 0.21561 0.15171 -0.00488 -0.02640 -0.00039 480 CYS A O   
1228 C CB  . CYS A 151 ? 0.15926 0.25170 0.18441 -0.00790 -0.02950 0.00979  480 CYS A CB  
1229 S SG  . CYS A 151 ? 0.17423 0.27618 0.19924 -0.00583 -0.01839 -0.02006 480 CYS A SG  
1230 N N   . ASN A 152 ? 0.14301 0.22364 0.17938 -0.01681 -0.01791 0.00531  481 ASN A N   
1231 C CA  . ASN A 152 ? 0.16075 0.23458 0.16487 -0.01074 -0.00656 -0.03577 481 ASN A CA  
1232 C C   . ASN A 152 ? 0.18757 0.22082 0.16952 -0.03123 -0.00626 -0.02888 481 ASN A C   
1233 O O   . ASN A 152 ? 0.18664 0.23730 0.20717 -0.02208 0.01257  -0.04066 481 ASN A O   
1234 C CB  . ASN A 152 ? 0.17616 0.23426 0.20097 0.00035  -0.04448 -0.02966 481 ASN A CB  
1235 C CG  . ASN A 152 ? 0.20426 0.22685 0.17460 -0.03930 -0.03193 -0.02325 481 ASN A CG  
1236 O OD1 . ASN A 152 ? 0.23987 0.22410 0.18988 -0.02402 -0.04162 -0.02293 481 ASN A OD1 
1237 N ND2 . ASN A 152 ? 0.33207 0.24963 0.20036 -0.02535 -0.01486 0.02486  481 ASN A ND2 
1238 N N   . GLY A 153 ? 0.20344 0.23978 0.13086 -0.03067 -0.01442 -0.02206 482 GLY A N   
1239 C CA  . GLY A 153 ? 0.22044 0.21041 0.15986 -0.02684 -0.00024 -0.01755 482 GLY A CA  
1240 C C   . GLY A 153 ? 0.17953 0.21810 0.14815 -0.02638 -0.02352 -0.00778 482 GLY A C   
1241 O O   . GLY A 153 ? 0.26811 0.23361 0.15886 0.00494  -0.00154 -0.02408 482 GLY A O   
1242 N N   . VAL A 154 ? 0.14331 0.20539 0.16898 -0.01497 -0.01502 -0.02198 483 VAL A N   
1243 C CA  . VAL A 154 ? 0.14574 0.22522 0.15861 -0.01159 -0.01953 -0.00372 483 VAL A CA  
1244 C C   . VAL A 154 ? 0.13855 0.21557 0.14519 -0.00312 -0.00549 -0.01810 483 VAL A C   
1245 O O   . VAL A 154 ? 0.16130 0.23280 0.16305 -0.00274 -0.01555 -0.02631 483 VAL A O   
1246 C CB  . VAL A 154 ? 0.18792 0.21334 0.20716 0.00556  -0.04651 -0.01314 483 VAL A CB  
1247 C CG1 . VAL A 154 ? 0.21072 0.21787 0.26684 0.00013  -0.06216 -0.02144 483 VAL A CG1 
1248 C CG2 . VAL A 154 ? 0.16873 0.23671 0.27198 0.00310  -0.04201 -0.02469 483 VAL A CG2 
1249 N N   . GLU A 155 ? 0.13848 0.21775 0.16173 -0.01106 -0.03159 -0.02348 484 GLU A N   
1250 C CA  . GLU A 155 ? 0.15751 0.20525 0.18235 -0.03314 -0.03215 -0.01744 484 GLU A CA  
1251 C C   . GLU A 155 ? 0.17172 0.20359 0.23508 -0.01033 0.00285  -0.02625 484 GLU A C   
1252 O O   . GLU A 155 ? 0.19732 0.21920 0.36165 0.01157  0.03261  0.02576  484 GLU A O   
1253 C CB  . GLU A 155 ? 0.16850 0.26955 0.19330 -0.01711 -0.02972 -0.07880 484 GLU A CB  
1254 C CG  . GLU A 155 ? 0.17135 0.27230 0.23580 -0.03501 -0.01367 -0.05497 484 GLU A CG  
1255 C CD  . GLU A 155 ? 0.16274 0.27658 0.28285 -0.04505 0.03087  -0.05657 484 GLU A CD  
1256 O OE1 . GLU A 155 ? 0.20712 0.30445 0.43525 -0.02650 0.06508  -0.09246 484 GLU A OE1 
1257 O OE2 . GLU A 155 ? 0.19034 0.28355 0.25493 -0.01674 -0.00404 -0.05385 484 GLU A OE2 
1258 N N   . GLY A 156 ? 0.15785 0.21477 0.21626 -0.03042 0.00148  -0.00778 485 GLY A N   
1259 C CA  . GLY A 156 ? 0.19116 0.27174 0.28299 -0.01698 0.00603  0.02635  485 GLY A CA  
1260 C C   . GLY A 156 ? 0.20947 0.24004 0.28700 -0.06329 0.00828  0.01101  485 GLY A C   
1261 O O   . GLY A 156 ? 0.17712 0.27868 0.23506 -0.04074 0.00082  -0.00347 485 GLY A O   
1262 N N   . PHE A 157 ? 0.24194 0.27171 0.26908 -0.02956 0.00889  0.04235  486 PHE A N   
1263 C CA  . PHE A 157 ? 0.27319 0.30741 0.21872 -0.00423 0.02028  0.08507  486 PHE A CA  
1264 C C   . PHE A 157 ? 0.21472 0.31227 0.18191 -0.04286 0.00664  0.05573  486 PHE A C   
1265 O O   . PHE A 157 ? 0.20869 0.30727 0.18892 -0.05192 -0.01111 0.05727  486 PHE A O   
1273 N N   . ASN A 158 ? 0.18598 0.32051 0.17966 -0.04388 -0.00854 0.04631  487 ASN A N   
1274 C CA  . ASN A 158 ? 0.19503 0.32274 0.14300 -0.05083 0.03668  0.03585  487 ASN A CA  
1275 C C   . ASN A 158 ? 0.16586 0.28359 0.12783 -0.00770 -0.01405 -0.00836 487 ASN A C   
1276 O O   . ASN A 158 ? 0.17253 0.26909 0.13187 0.00459  -0.01472 -0.00044 487 ASN A O   
1277 C CB  . ASN A 158 ? 0.24423 0.36351 0.12178 -0.06348 0.01712  0.02626  487 ASN A CB  
1278 C CG  . ASN A 158 ? 0.28188 0.42718 0.16016 -0.10141 0.00522  -0.01294 487 ASN A CG  
1279 O OD1 . ASN A 158 ? 0.25960 0.52436 0.20847 -0.12282 0.02079  0.01673  487 ASN A OD1 
1280 N ND2 . ASN A 158 ? 0.34689 0.48112 0.19092 -0.05611 0.02635  0.03626  487 ASN A ND2 
1281 N N   . CYS A 159 ? 0.13174 0.26140 0.13955 -0.01481 -0.00901 0.01371  488 CYS A N   
1282 C CA  . CYS A 159 ? 0.12456 0.26025 0.12691 0.00794  -0.01621 0.01229  488 CYS A CA  
1283 C C   . CYS A 159 ? 0.14563 0.21005 0.11634 -0.00091 -0.02249 -0.00912 488 CYS A C   
1284 O O   . CYS A 159 ? 0.15636 0.22104 0.17107 0.00376  -0.02664 -0.01734 488 CYS A O   
1285 C CB  . CYS A 159 ? 0.14200 0.24333 0.14251 0.00204  -0.02960 0.01316  488 CYS A CB  
1286 S SG  . CYS A 159 ? 0.15291 0.25053 0.14553 -0.01649 -0.02869 0.01815  488 CYS A SG  
1287 N N   . TYR A 160 ? 0.14009 0.25259 0.11351 0.00127  -0.00739 0.00733  489 TYR A N   
1288 C CA  . TYR A 160 ? 0.13686 0.27694 0.09138 -0.00835 -0.00933 0.00079  489 TYR A CA  
1289 C C   . TYR A 160 ? 0.12367 0.24644 0.12544 0.01379  -0.01846 -0.01082 489 TYR A C   
1290 O O   . TYR A 160 ? 0.16379 0.23615 0.13330 -0.00083 -0.01733 -0.01506 489 TYR A O   
1291 C CB  . TYR A 160 ? 0.12433 0.31235 0.13934 -0.01500 -0.01406 -0.00647 489 TYR A CB  
1292 C CG  . TYR A 160 ? 0.13013 0.29753 0.16576 -0.05074 0.01524  -0.04680 489 TYR A CG  
1293 C CD1 . TYR A 160 ? 0.17735 0.30745 0.19804 -0.03638 0.00361  0.02534  489 TYR A CD1 
1294 C CD2 . TYR A 160 ? 0.14545 0.33379 0.17574 -0.01939 0.01251  -0.07231 489 TYR A CD2 
1295 C CE1 . TYR A 160 ? 0.15626 0.36176 0.17499 -0.05239 0.00978  0.01006  489 TYR A CE1 
1296 C CE2 . TYR A 160 ? 0.15076 0.34593 0.17020 -0.01140 0.00965  -0.02615 489 TYR A CE2 
1297 C CZ  . TYR A 160 ? 0.15712 0.36601 0.18026 -0.02351 0.00003  -0.02591 489 TYR A CZ  
1298 O OH  . TYR A 160 ? 0.17593 0.43892 0.18435 -0.04583 0.03370  0.00687  489 TYR A OH  
1299 N N   . PHE A 161 ? 0.14155 0.23707 0.11276 0.02775  -0.00651 -0.01368 490 PHE A N   
1300 C CA  . PHE A 161 ? 0.15355 0.22622 0.10874 0.02840  -0.01629 -0.00328 490 PHE A CA  
1301 C C   . PHE A 161 ? 0.13540 0.20091 0.12904 -0.00617 -0.02839 -0.01630 490 PHE A C   
1302 O O   . PHE A 161 ? 0.14985 0.21081 0.14977 0.01116  -0.02608 -0.01754 490 PHE A O   
1303 C CB  . PHE A 161 ? 0.16418 0.22961 0.12215 0.02991  -0.00919 -0.01342 490 PHE A CB  
1304 C CG  . PHE A 161 ? 0.15972 0.20709 0.12144 0.03667  -0.00390 -0.02452 490 PHE A CG  
1305 C CD1 . PHE A 161 ? 0.15724 0.22677 0.15961 0.02484  0.00242  -0.01871 490 PHE A CD1 
1306 C CD2 . PHE A 161 ? 0.20044 0.19839 0.12969 0.04449  -0.02569 -0.01279 490 PHE A CD2 
1307 C CE1 . PHE A 161 ? 0.20122 0.26493 0.19279 0.05936  0.03748  0.02501  490 PHE A CE1 
1308 C CE2 . PHE A 161 ? 0.24358 0.23499 0.13952 0.09130  -0.00900 0.00878  490 PHE A CE2 
1309 C CZ  . PHE A 161 ? 0.23255 0.26098 0.17035 0.08850  0.01659  -0.01979 490 PHE A CZ  
1310 N N   . PRO A 162 ? 0.14075 0.19798 0.11817 0.01972  -0.02284 -0.01277 491 PRO A N   
1311 C CA  . PRO A 162 ? 0.13533 0.20241 0.12902 0.02525  -0.02648 -0.01269 491 PRO A CA  
1312 C C   . PRO A 162 ? 0.13650 0.19143 0.12024 -0.00210 -0.02329 0.00320  491 PRO A C   
1313 O O   . PRO A 162 ? 0.13159 0.21180 0.15648 0.01790  -0.02469 -0.01857 491 PRO A O   
1314 C CB  . PRO A 162 ? 0.15521 0.19658 0.15718 0.00995  -0.01324 -0.03512 491 PRO A CB  
1315 C CG  . PRO A 162 ? 0.15283 0.20328 0.15602 0.01009  -0.00271 -0.01773 491 PRO A CG  
1316 C CD  . PRO A 162 ? 0.13856 0.20898 0.15535 -0.01005 -0.02735 -0.00692 491 PRO A CD  
1317 N N   . LEU A 163 ? 0.16221 0.18778 0.11968 0.01106  -0.03001 -0.01623 492 LEU A N   
1318 C CA  . LEU A 163 ? 0.16432 0.19684 0.12203 -0.00751 -0.03379 -0.02001 492 LEU A CA  
1319 C C   . LEU A 163 ? 0.16314 0.19201 0.13489 -0.00349 -0.05704 -0.01472 492 LEU A C   
1320 O O   . LEU A 163 ? 0.20146 0.21289 0.21900 0.03923  -0.08991 -0.03302 492 LEU A O   
1321 C CB  . LEU A 163 ? 0.17429 0.20067 0.12894 0.00670  -0.02004 -0.01364 492 LEU A CB  
1322 C CG  . LEU A 163 ? 0.18410 0.18247 0.12227 0.01467  -0.01806 -0.00674 492 LEU A CG  
1323 C CD1 . LEU A 163 ? 0.21406 0.20404 0.12682 0.03328  0.00402  0.00858  492 LEU A CD1 
1324 C CD2 . LEU A 163 ? 0.16894 0.16470 0.20125 0.01929  -0.00008 -0.00860 492 LEU A CD2 
1325 N N   . GLN A 164 ? 0.16581 0.16960 0.12563 0.00473  -0.03374 -0.00511 493 GLN A N   
1326 C CA  . GLN A 164 ? 0.17584 0.19481 0.13593 -0.02431 -0.03803 0.00554  493 GLN A CA  
1327 C C   . GLN A 164 ? 0.15481 0.15008 0.14660 -0.00499 -0.03044 0.01393  493 GLN A C   
1328 O O   . GLN A 164 ? 0.15854 0.17163 0.13694 0.02059  -0.01976 0.00588  493 GLN A O   
1329 C CB  . GLN A 164 ? 0.21284 0.24357 0.13891 -0.04863 -0.01861 -0.00883 493 GLN A CB  
1330 C CG  . GLN A 164 ? 0.26875 0.28954 0.14230 -0.00635 -0.00147 -0.01211 493 GLN A CG  
1331 C CD  . GLN A 164 ? 0.22510 0.32620 0.22884 -0.00446 0.01262  0.01767  493 GLN A CD  
1332 O OE1 . GLN A 164 ? 0.23124 0.27396 0.18396 -0.01408 0.01247  0.02681  493 GLN A OE1 
1333 N NE2 . GLN A 164 ? 0.23680 0.43963 0.28407 -0.03355 0.05285  0.00551  493 GLN A NE2 
1334 N N   . SER A 165 ? 0.15144 0.16502 0.16991 -0.00292 -0.03271 0.01772  494 SER A N   
1335 C CA  . SER A 165 ? 0.13790 0.20518 0.14907 -0.00666 -0.03976 -0.02499 494 SER A CA  
1336 C C   . SER A 165 ? 0.17684 0.15988 0.13527 0.01120  -0.04004 0.00162  494 SER A C   
1337 O O   . SER A 165 ? 0.17679 0.19781 0.14818 -0.00848 -0.02362 0.03254  494 SER A O   
1338 C CB  . SER A 165 ? 0.17445 0.20068 0.19953 0.04927  -0.03970 -0.05218 494 SER A CB  
1339 O OG  . SER A 165 ? 0.17926 0.20688 0.17590 0.00452  -0.01366 -0.02472 494 SER A OG  
1340 N N   . TYR A 166 ? 0.15016 0.16347 0.11695 0.01948  -0.02054 -0.01327 495 TYR A N   
1341 C CA  . TYR A 166 ? 0.14353 0.16353 0.16482 -0.00217 -0.02548 -0.01333 495 TYR A CA  
1342 C C   . TYR A 166 ? 0.18047 0.16676 0.13008 0.00410  -0.01312 0.00171  495 TYR A C   
1343 O O   . TYR A 166 ? 0.18373 0.18502 0.22101 -0.02683 0.02561  -0.01805 495 TYR A O   
1344 C CB  . TYR A 166 ? 0.16048 0.16090 0.15928 0.01342  -0.02061 -0.00599 495 TYR A CB  
1345 C CG  . TYR A 166 ? 0.15451 0.15433 0.13033 0.01080  -0.02410 -0.01366 495 TYR A CG  
1346 C CD1 . TYR A 166 ? 0.13113 0.18031 0.15151 0.02176  -0.00019 -0.01233 495 TYR A CD1 
1347 C CD2 . TYR A 166 ? 0.15103 0.17579 0.13681 0.01274  -0.02946 0.00420  495 TYR A CD2 
1348 C CE1 . TYR A 166 ? 0.13759 0.19090 0.14641 0.01863  -0.00854 0.00395  495 TYR A CE1 
1349 C CE2 . TYR A 166 ? 0.14092 0.18890 0.13617 0.00831  -0.02274 -0.00629 495 TYR A CE2 
1350 C CZ  . TYR A 166 ? 0.14531 0.17023 0.12519 0.00750  -0.00539 0.00223  495 TYR A CZ  
1351 O OH  . TYR A 166 ? 0.15020 0.17073 0.15257 0.02079  -0.01223 -0.00451 495 TYR A OH  
1352 N N   . GLY A 167 ? 0.18014 0.14508 0.14169 0.00494  -0.02462 -0.02394 496 GLY A N   
1353 C CA  . GLY A 167 ? 0.17958 0.17561 0.17101 0.00018  -0.02707 -0.03543 496 GLY A CA  
1354 C C   . GLY A 167 ? 0.18498 0.16872 0.15199 0.01371  -0.03311 -0.02961 496 GLY A C   
1355 O O   . GLY A 167 ? 0.22225 0.18217 0.18429 -0.03435 -0.04527 -0.01250 496 GLY A O   
1356 N N   . PHE A 168 ? 0.17320 0.17741 0.14375 0.02197  -0.04077 -0.02432 497 PHE A N   
1357 C CA  . PHE A 168 ? 0.18774 0.15649 0.19441 0.01437  -0.04958 -0.02353 497 PHE A CA  
1358 C C   . PHE A 168 ? 0.18273 0.15214 0.16564 0.00282  -0.02060 -0.01717 497 PHE A C   
1359 O O   . PHE A 168 ? 0.17777 0.15655 0.18184 0.01102  -0.02143 -0.02146 497 PHE A O   
1360 C CB  . PHE A 168 ? 0.23956 0.13464 0.17833 0.02863  -0.05724 -0.00769 497 PHE A CB  
1361 C CG  . PHE A 168 ? 0.16391 0.16141 0.16827 0.01606  -0.05810 0.00009  497 PHE A CG  
1362 C CD1 . PHE A 168 ? 0.16047 0.18606 0.16995 0.00582  -0.04232 0.00053  497 PHE A CD1 
1363 C CD2 . PHE A 168 ? 0.18739 0.16080 0.17761 0.00535  -0.07336 -0.02329 497 PHE A CD2 
1364 C CE1 . PHE A 168 ? 0.17600 0.16037 0.15909 0.01599  -0.06192 -0.01717 497 PHE A CE1 
1365 C CE2 . PHE A 168 ? 0.18401 0.17598 0.15150 0.01383  -0.05523 -0.00358 497 PHE A CE2 
1366 C CZ  . PHE A 168 ? 0.15346 0.17444 0.15424 -0.00872 -0.04694 -0.00468 497 PHE A CZ  
1367 N N   . GLN A 169 ? 0.18041 0.16999 0.20727 0.00582  -0.02641 -0.02648 498 GLN A N   
1368 C CA  . GLN A 169 ? 0.19115 0.17128 0.22027 0.00273  -0.07253 -0.04191 498 GLN A CA  
1369 C C   . GLN A 169 ? 0.18643 0.16900 0.25003 -0.00208 -0.04320 -0.02609 498 GLN A C   
1370 O O   . GLN A 169 ? 0.17217 0.17575 0.24706 0.00561  -0.02363 -0.02911 498 GLN A O   
1371 C CB  . GLN A 169 ? 0.24540 0.15847 0.23318 0.01806  -0.06800 -0.01380 498 GLN A CB  
1372 C CG  . GLN A 169 ? 0.25812 0.20121 0.24846 0.00972  -0.05993 0.00789  498 GLN A CG  
1373 C CD  . GLN A 169 ? 0.30500 0.22832 0.22216 -0.03999 -0.05923 -0.00715 498 GLN A CD  
1374 O OE1 . GLN A 169 ? 0.33377 0.23822 0.22223 -0.02784 -0.02113 -0.00461 498 GLN A OE1 
1375 N NE2 . GLN A 169 ? 0.34552 0.23793 0.27757 -0.05125 -0.04457 -0.02074 498 GLN A NE2 
1376 N N   . PRO A 170 ? 0.17925 0.20602 0.22157 -0.01029 -0.05523 -0.02059 499 PRO A N   
1377 C CA  . PRO A 170 ? 0.20745 0.23664 0.24323 -0.00168 -0.04846 -0.04390 499 PRO A CA  
1378 C C   . PRO A 170 ? 0.20593 0.21730 0.25279 -0.03161 -0.03926 -0.03755 499 PRO A C   
1379 O O   . PRO A 170 ? 0.20971 0.22122 0.29726 -0.01401 -0.05423 -0.00925 499 PRO A O   
1380 C CB  . PRO A 170 ? 0.21825 0.27159 0.27116 0.00808  -0.04880 -0.07931 499 PRO A CB  
1381 C CG  . PRO A 170 ? 0.24829 0.26284 0.28001 0.02491  -0.04372 -0.08625 499 PRO A CG  
1382 C CD  . PRO A 170 ? 0.21324 0.23843 0.23513 0.02848  -0.02851 -0.07067 499 PRO A CD  
1383 N N   . THR A 171 ? 0.24880 0.20238 0.25109 -0.02663 -0.01247 -0.02493 500 THR A N   
1384 C CA  . THR A 171 ? 0.27526 0.18803 0.33270 -0.03053 0.00005  -0.02522 500 THR A CA  
1385 C C   . THR A 171 ? 0.23330 0.20722 0.31658 -0.03643 -0.00978 -0.01303 500 THR A C   
1386 O O   . THR A 171 ? 0.23986 0.18882 0.38236 -0.02578 0.01822  -0.00726 500 THR A O   
1387 C CB  . THR A 171 ? 0.31033 0.20853 0.34791 -0.01258 -0.01210 -0.02936 500 THR A CB  
1388 O OG1 . THR A 171 ? 0.35700 0.24188 0.38226 -0.00910 -0.00071 0.01797  500 THR A OG1 
1389 C CG2 . THR A 171 ? 0.32322 0.22189 0.39992 0.01075  0.01857  -0.03148 500 THR A CG2 
1390 N N   . ASN A 172 ? 0.22494 0.18095 0.27582 -0.01485 -0.00536 -0.02167 501 ASN A N   
1391 C CA  . ASN A 172 ? 0.22217 0.19956 0.28364 -0.01320 0.00728  0.00201  501 ASN A CA  
1392 C C   . ASN A 172 ? 0.22013 0.20538 0.31058 -0.03628 -0.00548 0.01806  501 ASN A C   
1393 O O   . ASN A 172 ? 0.21975 0.21983 0.30226 -0.02679 -0.02451 0.01589  501 ASN A O   
1394 C CB  . ASN A 172 ? 0.23264 0.19279 0.23936 -0.03939 -0.00980 -0.03338 501 ASN A CB  
1395 C CG  . ASN A 172 ? 0.24376 0.24402 0.23323 -0.03073 0.00880  0.03018  501 ASN A CG  
1396 O OD1 . ASN A 172 ? 0.25113 0.27540 0.26377 -0.01601 -0.02815 0.01273  501 ASN A OD1 
1397 N ND2 . ASN A 172 ? 0.26717 0.25715 0.28718 -0.05942 -0.04391 0.05473  501 ASN A ND2 
1398 N N   . GLY A 173 ? 0.23912 0.18190 0.34227 -0.02306 0.03821  -0.01742 502 GLY A N   
1399 C CA  . GLY A 173 ? 0.24963 0.22157 0.34143 -0.01591 0.03620  -0.01032 502 GLY A CA  
1400 C C   . GLY A 173 ? 0.24478 0.21757 0.33566 -0.03247 0.01868  0.02686  502 GLY A C   
1401 O O   . GLY A 173 ? 0.24872 0.22753 0.32116 -0.02650 0.04329  -0.00297 502 GLY A O   
1402 N N   . VAL A 174 ? 0.25307 0.24991 0.36517 -0.01184 -0.00153 0.04327  503 VAL A N   
1403 C CA  A VAL A 174 ? 0.28981 0.30102 0.36770 0.01749  0.00916  0.02577  503 VAL A CA  
1404 C CA  B VAL A 174 ? 0.28987 0.30110 0.36768 0.01750  0.00899  0.02587  503 VAL A CA  
1405 C C   . VAL A 174 ? 0.28410 0.27433 0.36962 0.00447  0.04831  0.02243  503 VAL A C   
1406 O O   . VAL A 174 ? 0.26142 0.25944 0.41047 0.01939  0.09059  0.03633  503 VAL A O   
1407 C CB  A VAL A 174 ? 0.33370 0.35456 0.39980 0.05155  0.01325  0.02110  503 VAL A CB  
1408 C CB  B VAL A 174 ? 0.33471 0.35632 0.39981 0.05140  0.01061  0.02198  503 VAL A CB  
1409 C CG1 A VAL A 174 ? 0.34231 0.37114 0.42520 0.06491  0.01454  0.00389  503 VAL A CG1 
1410 C CG1 B VAL A 174 ? 0.35545 0.38448 0.42471 0.05551  0.00121  0.01506  503 VAL A CG1 
1411 C CG2 A VAL A 174 ? 0.34857 0.37488 0.40513 0.05175  -0.01392 0.03478  503 VAL A CG2 
1412 C CG2 B VAL A 174 ? 0.33876 0.36771 0.39714 0.05910  -0.02060 0.01638  503 VAL A CG2 
1413 N N   . GLY A 175 ? 0.30776 0.24142 0.36461 0.01060  0.07156  0.00698  504 GLY A N   
1414 C CA  . GLY A 175 ? 0.29203 0.27110 0.30946 -0.01454 0.08231  0.01483  504 GLY A CA  
1415 C C   . GLY A 175 ? 0.31795 0.19589 0.28523 -0.07414 0.10141  -0.04051 504 GLY A C   
1416 O O   . GLY A 175 ? 0.32488 0.19650 0.38357 -0.03776 0.11073  -0.03879 504 GLY A O   
1417 N N   . TYR A 176 ? 0.32590 0.19535 0.25140 -0.02702 0.07069  -0.01290 505 TYR A N   
1418 C CA  . TYR A 176 ? 0.33767 0.19116 0.22821 -0.02252 0.03460  -0.00295 505 TYR A CA  
1419 C C   . TYR A 176 ? 0.26162 0.19994 0.20593 -0.04014 0.02478  0.00245  505 TYR A C   
1420 O O   . TYR A 176 ? 0.24946 0.26332 0.20184 -0.04312 -0.02477 0.00323  505 TYR A O   
1421 C CB  . TYR A 176 ? 0.39024 0.24525 0.26197 -0.04394 0.04946  0.01444  505 TYR A CB  
1422 C CG  . TYR A 176 ? 0.48531 0.39835 0.44979 -0.01175 -0.00140 0.01123  505 TYR A CG  
1423 C CD1 . TYR A 176 ? 0.53066 0.47102 0.50430 0.02388  0.00023  0.03026  505 TYR A CD1 
1424 C CD2 . TYR A 176 ? 0.52963 0.49272 0.52009 0.00705  -0.00019 0.01064  505 TYR A CD2 
1425 C CE1 . TYR A 176 ? 0.56004 0.52956 0.55243 0.02686  0.00061  0.02228  505 TYR A CE1 
1426 C CE2 . TYR A 176 ? 0.56033 0.53738 0.56280 0.01825  -0.00490 -0.00790 505 TYR A CE2 
1427 C CZ  . TYR A 176 ? 0.57940 0.55972 0.59160 0.03343  -0.00234 0.00162  505 TYR A CZ  
1428 O OH  . TYR A 176 ? 0.61866 0.59472 0.63243 0.05911  0.01678  -0.01752 505 TYR A OH  
1429 N N   . GLN A 177 ? 0.23550 0.17877 0.20316 -0.02248 0.01242  0.01349  506 GLN A N   
1430 C CA  . GLN A 177 ? 0.20387 0.15955 0.20597 -0.01833 -0.02849 0.01366  506 GLN A CA  
1431 C C   . GLN A 177 ? 0.17352 0.15181 0.15792 0.00250  -0.02096 0.00530  506 GLN A C   
1432 O O   . GLN A 177 ? 0.15633 0.16518 0.19319 0.00363  0.00376  -0.00785 506 GLN A O   
1433 C CB  . GLN A 177 ? 0.17952 0.16753 0.23893 -0.01902 -0.06001 -0.00010 506 GLN A CB  
1434 C CG  . GLN A 177 ? 0.19005 0.18656 0.25596 -0.02364 -0.04609 -0.03902 506 GLN A CG  
1435 C CD  . GLN A 177 ? 0.23331 0.17275 0.28112 -0.02200 -0.02980 -0.00476 506 GLN A CD  
1436 O OE1 . GLN A 177 ? 0.24795 0.18164 0.30130 -0.02438 -0.07545 -0.01323 506 GLN A OE1 
1437 N NE2 . GLN A 177 ? 0.27455 0.19381 0.33663 -0.05365 -0.04575 0.02163  506 GLN A NE2 
1438 N N   . PRO A 178 ? 0.16632 0.14719 0.15968 -0.00324 -0.03140 0.00236  507 PRO A N   
1439 C CA  . PRO A 178 ? 0.15494 0.16027 0.15922 0.00059  -0.03430 0.00557  507 PRO A CA  
1440 C C   . PRO A 178 ? 0.13686 0.18566 0.14049 -0.01899 -0.02633 0.00369  507 PRO A C   
1441 O O   . PRO A 178 ? 0.15311 0.16773 0.16606 0.00896  -0.04331 -0.01258 507 PRO A O   
1442 C CB  . PRO A 178 ? 0.14966 0.18296 0.16376 0.01300  -0.02097 -0.03627 507 PRO A CB  
1443 C CG  . PRO A 178 ? 0.17480 0.16699 0.16481 0.00239  -0.01090 -0.00815 507 PRO A CG  
1444 C CD  . PRO A 178 ? 0.17798 0.15249 0.14662 0.01442  -0.00570 -0.00990 507 PRO A CD  
1445 N N   . TYR A 179 ? 0.16528 0.14185 0.16397 0.00150  -0.02506 0.00114  508 TYR A N   
1446 C CA  . TYR A 179 ? 0.15742 0.16140 0.16365 0.00889  -0.03079 0.01591  508 TYR A CA  
1447 C C   . TYR A 179 ? 0.13779 0.16578 0.14389 0.01586  -0.03326 -0.01382 508 TYR A C   
1448 O O   . TYR A 179 ? 0.14320 0.17225 0.14746 0.00042  -0.02609 0.00245  508 TYR A O   
1449 C CB  . TYR A 179 ? 0.14340 0.17589 0.18563 -0.00539 -0.02042 -0.00817 508 TYR A CB  
1450 C CG  . TYR A 179 ? 0.15607 0.17997 0.18474 0.00586  -0.00757 -0.00979 508 TYR A CG  
1451 C CD1 . TYR A 179 ? 0.16121 0.16151 0.22274 -0.01113 -0.02819 0.00480  508 TYR A CD1 
1452 C CD2 . TYR A 179 ? 0.16180 0.20551 0.20195 0.03029  -0.03856 -0.01433 508 TYR A CD2 
1453 C CE1 . TYR A 179 ? 0.17632 0.18071 0.26052 0.00149  -0.00709 -0.00673 508 TYR A CE1 
1454 C CE2 . TYR A 179 ? 0.12985 0.19958 0.26200 0.00827  -0.03659 -0.03025 508 TYR A CE2 
1455 C CZ  . TYR A 179 ? 0.15809 0.20734 0.26280 -0.01849 -0.02796 -0.01819 508 TYR A CZ  
1456 O OH  . TYR A 179 ? 0.18831 0.23981 0.28236 -0.03410 -0.02087 -0.00479 508 TYR A OH  
1457 N N   . ARG A 180 ? 0.15581 0.16857 0.13376 0.01771  -0.01562 0.01100  509 ARG A N   
1458 C CA  . ARG A 180 ? 0.16570 0.15208 0.13966 0.03413  -0.01011 -0.01343 509 ARG A CA  
1459 C C   . ARG A 180 ? 0.14297 0.19606 0.14423 0.01215  -0.01213 0.00269  509 ARG A C   
1460 O O   . ARG A 180 ? 0.14114 0.18745 0.16803 0.01303  -0.02912 -0.00697 509 ARG A O   
1461 C CB  . ARG A 180 ? 0.17066 0.18100 0.14232 0.01749  -0.00931 0.00116  509 ARG A CB  
1462 C CG  . ARG A 180 ? 0.19904 0.21925 0.12900 0.05078  -0.01075 -0.00485 509 ARG A CG  
1463 C CD  . ARG A 180 ? 0.20239 0.21975 0.14599 0.03983  0.00130  0.00395  509 ARG A CD  
1464 N NE  . ARG A 180 ? 0.22425 0.19648 0.15577 0.04827  0.01574  0.00067  509 ARG A NE  
1465 C CZ  . ARG A 180 ? 0.25868 0.20751 0.12526 0.05389  0.00818  0.00218  509 ARG A CZ  
1466 N NH1 . ARG A 180 ? 0.27441 0.23728 0.17124 0.07151  0.03673  0.00527  509 ARG A NH1 
1467 N NH2 . ARG A 180 ? 0.24030 0.24222 0.16785 0.07380  0.02348  0.00531  509 ARG A NH2 
1468 N N   . VAL A 181 ? 0.13554 0.13114 0.16479 0.01776  -0.01574 -0.00345 510 VAL A N   
1469 C CA  . VAL A 181 ? 0.14155 0.15685 0.14904 0.00222  -0.01702 0.01780  510 VAL A CA  
1470 C C   . VAL A 181 ? 0.12438 0.17418 0.14351 0.01915  -0.00369 0.00403  510 VAL A C   
1471 O O   . VAL A 181 ? 0.12515 0.17448 0.17137 0.01258  -0.00957 0.01201  510 VAL A O   
1472 C CB  . VAL A 181 ? 0.15447 0.17667 0.13393 0.01746  -0.00565 0.00563  510 VAL A CB  
1473 C CG1 . VAL A 181 ? 0.16170 0.17329 0.16990 0.02967  0.00523  -0.00138 510 VAL A CG1 
1474 C CG2 . VAL A 181 ? 0.15706 0.16648 0.16160 -0.00502 -0.00626 0.01648  510 VAL A CG2 
1475 N N   . VAL A 182 ? 0.15001 0.17086 0.15158 0.01536  -0.01766 0.02444  511 VAL A N   
1476 C CA  . VAL A 182 ? 0.15411 0.16882 0.16445 0.03222  -0.00100 0.02307  511 VAL A CA  
1477 C C   . VAL A 182 ? 0.12997 0.17464 0.14755 0.01328  0.00097  0.04100  511 VAL A C   
1478 O O   . VAL A 182 ? 0.13654 0.17843 0.19664 0.01010  -0.00567 0.03029  511 VAL A O   
1479 C CB  . VAL A 182 ? 0.16201 0.20729 0.14406 0.00771  -0.00408 0.03415  511 VAL A CB  
1480 C CG1 . VAL A 182 ? 0.17993 0.20399 0.19357 -0.00204 0.01075  0.04585  511 VAL A CG1 
1481 C CG2 . VAL A 182 ? 0.16606 0.21024 0.14896 0.03565  0.01295  0.00022  511 VAL A CG2 
1482 N N   . VAL A 183 ? 0.14795 0.16278 0.15926 -0.00541 -0.00058 0.02175  512 VAL A N   
1483 C CA  . VAL A 183 ? 0.15799 0.14842 0.15932 -0.00038 0.00443  0.03480  512 VAL A CA  
1484 C C   . VAL A 183 ? 0.13704 0.18773 0.16850 0.01154  0.00202  0.01925  512 VAL A C   
1485 O O   . VAL A 183 ? 0.15153 0.19243 0.18537 0.00472  -0.00398 0.03021  512 VAL A O   
1486 C CB  . VAL A 183 ? 0.16350 0.18205 0.14849 0.01007  -0.00449 0.03942  512 VAL A CB  
1487 C CG1 . VAL A 183 ? 0.18749 0.16530 0.18156 0.02588  0.02594  0.01321  512 VAL A CG1 
1488 C CG2 . VAL A 183 ? 0.17368 0.20927 0.17083 -0.00255 0.00846  0.05634  512 VAL A CG2 
1489 N N   . LEU A 184 ? 0.17328 0.16968 0.16448 0.01875  -0.00683 0.04059  513 LEU A N   
1490 C CA  . LEU A 184 ? 0.20586 0.18509 0.15408 0.00841  -0.01124 0.03800  513 LEU A CA  
1491 C C   . LEU A 184 ? 0.18371 0.18672 0.19408 0.00273  -0.00057 0.03578  513 LEU A C   
1492 O O   . LEU A 184 ? 0.19020 0.19051 0.23969 -0.00139 0.01086  0.02996  513 LEU A O   
1493 C CB  . LEU A 184 ? 0.22262 0.17863 0.20524 -0.00105 -0.00644 0.03571  513 LEU A CB  
1494 C CG  . LEU A 184 ? 0.23866 0.20644 0.18096 0.00958  -0.03606 0.03155  513 LEU A CG  
1495 C CD1 . LEU A 184 ? 0.24464 0.23375 0.21323 0.01187  -0.04903 0.04029  513 LEU A CD1 
1496 C CD2 . LEU A 184 ? 0.23243 0.25318 0.20695 0.00687  0.02570  0.05272  513 LEU A CD2 
1497 N N   . SER A 185 ? 0.19982 0.17451 0.21343 -0.00576 0.00077  0.04027  514 SER A N   
1498 C CA  . SER A 185 ? 0.23006 0.17588 0.26403 0.01450  0.00291  0.04450  514 SER A CA  
1499 C C   . SER A 185 ? 0.21828 0.17937 0.28693 -0.01084 0.03475  0.03225  514 SER A C   
1500 O O   . SER A 185 ? 0.22031 0.18922 0.28628 -0.00586 0.02610  0.05096  514 SER A O   
1501 C CB  . SER A 185 ? 0.23900 0.20026 0.28470 0.01752  -0.02854 0.05319  514 SER A CB  
1502 O OG  . SER A 185 ? 0.25437 0.24279 0.25173 0.04024  -0.02838 0.00551  514 SER A OG  
1503 N N   . PHE A 186 ? 0.26647 0.16373 0.27307 0.00903  0.01162  0.04015  515 PHE A N   
1504 C CA  . PHE A 186 ? 0.28954 0.17471 0.29373 0.00152  -0.02362 0.05220  515 PHE A CA  
1505 C C   . PHE A 186 ? 0.32027 0.21812 0.35248 -0.01065 0.00099  0.05580  515 PHE A C   
1506 O O   . PHE A 186 ? 0.37156 0.23917 0.38765 0.00524  0.00168  0.04454  515 PHE A O   
1507 C CB  . PHE A 186 ? 0.25330 0.23691 0.30281 0.02900  -0.00839 0.04332  515 PHE A CB  
1508 C CG  . PHE A 186 ? 0.28134 0.24275 0.27767 0.00926  -0.00504 0.04812  515 PHE A CG  
1509 C CD1 . PHE A 186 ? 0.33126 0.28279 0.37934 -0.00564 0.05561  -0.00228 515 PHE A CD1 
1510 C CD2 . PHE A 186 ? 0.29629 0.25544 0.31604 0.00322  -0.02292 0.06877  515 PHE A CD2 
1511 C CE1 . PHE A 186 ? 0.33085 0.28673 0.38661 0.01361  0.04054  -0.02141 515 PHE A CE1 
1512 C CE2 . PHE A 186 ? 0.31480 0.25989 0.30357 0.00803  -0.05787 0.08116  515 PHE A CE2 
1513 C CZ  . PHE A 186 ? 0.29236 0.22826 0.32157 -0.01221 -0.03950 0.06211  515 PHE A CZ  
1514 N N   . GLU A 187 ? 0.34688 0.26953 0.38334 -0.02588 0.00454  0.06097  516 GLU A N   
1515 C CA  . GLU A 187 ? 0.41038 0.32067 0.46871 -0.04245 -0.00468 0.05708  516 GLU A CA  
1516 C C   . GLU A 187 ? 0.46789 0.36882 0.51540 -0.03452 -0.00940 0.06732  516 GLU A C   
1517 O O   . GLU A 187 ? 0.46750 0.29533 0.50067 -0.04244 -0.00108 0.06933  516 GLU A O   
1518 C CB  . GLU A 187 ? 0.41394 0.33260 0.47913 -0.04994 -0.01775 0.02637  516 GLU A CB  
1519 C CG  . GLU A 187 ? 0.44779 0.39177 0.51000 -0.02176 -0.01277 0.02255  516 GLU A CG  
1520 C CD  . GLU A 187 ? 0.47376 0.41447 0.53824 0.00543  -0.00894 0.03462  516 GLU A CD  
1521 O OE1 . GLU A 187 ? 0.45930 0.39019 0.55801 -0.03123 0.01337  0.04588  516 GLU A OE1 
1522 O OE2 . GLU A 187 ? 0.50397 0.44922 0.57101 0.03714  -0.03526 0.01514  516 GLU A OE2 
1523 N N   . LEU A 188 ? 0.53502 0.44200 0.59400 -0.02357 0.00064  0.06495  517 LEU A N   
1524 C CA  . LEU A 188 ? 0.61524 0.54942 0.69131 -0.01152 0.00045  0.05788  517 LEU A CA  
1525 C C   . LEU A 188 ? 0.65952 0.58354 0.74755 -0.00991 0.00829  0.05291  517 LEU A C   
1526 O O   . LEU A 188 ? 0.66151 0.56457 0.73701 -0.02974 0.00318  0.03608  517 LEU A O   
1527 C CB  . LEU A 188 ? 0.64616 0.58489 0.72807 0.01000  0.00308  0.06733  517 LEU A CB  
1528 C CG  . LEU A 188 ? 0.67487 0.62459 0.76160 0.02372  0.00218  0.06181  517 LEU A CG  
1529 C CD1 . LEU A 188 ? 0.68697 0.64781 0.78312 0.03424  0.00924  0.06232  517 LEU A CD1 
1530 C CD2 . LEU A 188 ? 0.68033 0.62437 0.75630 0.01148  0.00426  0.05930  517 LEU A CD2 
1531 N N   . LEU A 189 ? 0.69489 0.62912 0.80877 -0.00221 0.00095  0.05630  518 LEU A N   
1532 C CA  . LEU A 189 ? 0.73163 0.66757 0.84974 -0.00110 0.00423  0.06551  518 LEU A CA  
1533 C C   . LEU A 189 ? 0.77332 0.69556 0.89434 -0.01052 0.00804  0.06861  518 LEU A C   
1534 O O   . LEU A 189 ? 0.77369 0.65875 0.86150 -0.03509 0.00751  0.06882  518 LEU A O   
1535 C CB  . LEU A 189 ? 0.72435 0.65992 0.83442 -0.01090 0.00681  0.06047  518 LEU A CB  
1536 C CG  . LEU A 189 ? 0.71442 0.65109 0.81719 -0.02839 0.01199  0.06041  518 LEU A CG  
1537 C CD1 . LEU A 189 ? 0.71271 0.65668 0.81471 -0.03312 0.01618  0.06019  518 LEU A CD1 
1538 C CD2 . LEU A 189 ? 0.71471 0.64415 0.79649 -0.03617 0.00312  0.05911  518 LEU A CD2 
1539 N N   . HIS A 190 ? 0.81025 0.74298 0.95683 -0.00038 0.01040  0.07159  519 HIS A N   
1540 C CA  . HIS A 190 ? 0.83838 0.76364 0.99081 -0.01199 0.01489  0.07287  519 HIS A CA  
1541 C C   . HIS A 190 ? 0.79636 0.72464 0.94093 -0.02075 0.02110  0.08028  519 HIS A C   
1542 O O   . HIS A 190 ? 0.80551 0.73363 0.95774 -0.00968 0.01788  0.07461  519 HIS A O   
1543 C CB  . HIS A 190 ? 0.90377 0.81201 1.05921 -0.00908 0.01157  0.06254  519 HIS A CB  
1544 C CG  . HIS A 190 ? 0.96639 0.87518 1.12858 0.00395  0.00861  0.05473  519 HIS A CG  
1545 N ND1 . HIS A 190 ? 0.99315 0.89066 1.15257 0.01094  0.00910  0.04894  519 HIS A ND1 
1546 C CD2 . HIS A 190 ? 0.99112 0.91406 1.17353 0.01962  0.00732  0.05266  519 HIS A CD2 
1547 C CE1 . HIS A 190 ? 1.00475 0.91813 1.17914 0.01488  0.00963  0.05069  519 HIS A CE1 
1548 N NE2 . HIS A 190 ? 1.00469 0.92897 1.19190 0.02226  0.00906  0.05149  519 HIS A NE2 
1549 N N   . ALA A 191 ? 0.74974 0.67288 0.86780 -0.04310 0.01901  0.08417  520 ALA A N   
1550 C CA  . ALA A 191 ? 0.71315 0.64498 0.82844 -0.04488 0.01796  0.08784  520 ALA A CA  
1551 C C   . ALA A 191 ? 0.69196 0.64029 0.81059 -0.02765 0.02507  0.09931  520 ALA A C   
1552 O O   . ALA A 191 ? 0.68920 0.64326 0.82265 -0.02625 0.01867  0.08309  520 ALA A O   
1553 C CB  . ALA A 191 ? 0.70596 0.64042 0.81730 -0.05587 0.02424  0.08883  520 ALA A CB  
1554 N N   . PRO A 192 ? 0.67495 0.62619 0.79426 -0.02631 0.02987  0.11022  521 PRO A N   
1555 C CA  . PRO A 192 ? 0.66383 0.60904 0.77355 -0.01474 0.03014  0.11876  521 PRO A CA  
1556 C C   . PRO A 192 ? 0.65173 0.60371 0.75768 -0.01004 0.03218  0.10976  521 PRO A C   
1557 O O   . PRO A 192 ? 0.64765 0.60358 0.76515 -0.00126 0.03325  0.12677  521 PRO A O   
1558 C CB  . PRO A 192 ? 0.66900 0.62322 0.78228 -0.00799 0.02843  0.11462  521 PRO A CB  
1559 C CG  . PRO A 192 ? 0.66582 0.62509 0.78966 -0.02275 0.03248  0.11644  521 PRO A CG  
1560 C CD  . PRO A 192 ? 0.66965 0.62743 0.79166 -0.01965 0.03327  0.11642  521 PRO A CD  
1561 N N   . ALA A 193 ? 0.63866 0.57324 0.72479 -0.01224 0.03552  0.11553  522 ALA A N   
1562 C CA  . ALA A 193 ? 0.63535 0.58132 0.70650 -0.00527 0.02759  0.11383  522 ALA A CA  
1563 C C   . ALA A 193 ? 0.64524 0.60100 0.71339 0.02064  0.02217  0.11709  522 ALA A C   
1564 O O   . ALA A 193 ? 0.65697 0.60429 0.72814 0.02734  0.01861  0.13767  522 ALA A O   
1565 C CB  . ALA A 193 ? 0.62800 0.55955 0.69106 -0.03128 0.02503  0.10911  522 ALA A CB  
1566 N N   . THR A 194 ? 0.62392 0.58125 0.70105 0.01551  0.03763  0.13021  523 THR A N   
1567 C CA  . THR A 194 ? 0.59505 0.56556 0.65694 0.01440  0.03237  0.11670  523 THR A CA  
1568 C C   . THR A 194 ? 0.55408 0.52066 0.60127 0.01088  0.04037  0.13015  523 THR A C   
1569 O O   . THR A 194 ? 0.56313 0.50446 0.59526 -0.00687 0.06314  0.14970  523 THR A O   
1570 C CB  . THR A 194 ? 0.60229 0.57730 0.66995 0.00197  0.03174  0.11769  523 THR A CB  
1571 O OG1 . THR A 194 ? 0.59821 0.56938 0.65061 0.00713  0.03215  0.12251  523 THR A OG1 
1572 C CG2 . THR A 194 ? 0.60812 0.59176 0.67758 0.00154  0.02786  0.11116  523 THR A CG2 
1573 N N   . VAL A 195 ? 0.47085 0.45752 0.49691 -0.01084 0.05470  0.16462  524 VAL A N   
1574 C CA  . VAL A 195 ? 0.42930 0.42978 0.44522 -0.00640 0.02940  0.12476  524 VAL A CA  
1575 C C   . VAL A 195 ? 0.43082 0.41901 0.45133 -0.01704 0.00973  0.13619  524 VAL A C   
1576 O O   . VAL A 195 ? 0.42423 0.39654 0.43327 -0.01078 -0.01231 0.14392  524 VAL A O   
1577 C CB  . VAL A 195 ? 0.40371 0.35496 0.42277 -0.03630 -0.00159 0.12247  524 VAL A CB  
1578 C CG1 . VAL A 195 ? 0.40398 0.37862 0.43485 -0.04073 0.00999  0.09549  524 VAL A CG1 
1579 C CG2 . VAL A 195 ? 0.40254 0.37434 0.44618 -0.01701 0.02354  0.10387  524 VAL A CG2 
1580 N N   . CYS A 196 ? 0.44263 0.42063 0.44740 -0.01976 0.02138  0.16922  525 CYS A N   
1581 C CA  . CYS A 196 ? 0.47327 0.46218 0.48755 -0.00035 0.00987  0.13893  525 CYS A CA  
1582 C C   . CYS A 196 ? 0.50534 0.51733 0.50946 0.03679  -0.00098 0.12073  525 CYS A C   
1583 O O   . CYS A 196 ? 0.45584 0.49354 0.47542 0.01636  -0.00463 0.14376  525 CYS A O   
1584 C CB  . CYS A 196 ? 0.49183 0.44899 0.50302 -0.00771 0.00581  0.13714  525 CYS A CB  
1585 S SG  . CYS A 196 ? 0.51843 0.44469 0.52392 -0.04087 0.03988  0.18737  525 CYS A SG  
1586 N N   . GLY A 197 ? 0.54956 0.55630 0.55043 0.04002  0.00189  0.12121  526 GLY A N   
1587 C CA  . GLY A 197 ? 0.59294 0.58972 0.58497 0.05136  0.00836  0.11730  526 GLY A CA  
1588 C C   . GLY A 197 ? 0.62357 0.62332 0.61116 0.06773  -0.01190 0.12297  526 GLY A C   
1589 O O   . GLY A 197 ? 0.63201 0.63207 0.63409 0.09528  -0.03848 0.14124  526 GLY A O   
1590 N N   . PRO A 198 ? 0.62594 0.62042 0.58706 0.05168  -0.00807 0.12112  527 PRO A N   
1591 C CA  . PRO A 198 ? 0.63534 0.63665 0.59669 0.05433  -0.00809 0.11322  527 PRO A CA  
1592 C C   . PRO A 198 ? 0.64449 0.64614 0.62179 0.06446  -0.01720 0.11323  527 PRO A C   
1593 O O   . PRO A 198 ? 0.65432 0.66354 0.64417 0.07055  -0.01990 0.10472  527 PRO A O   
1594 C CB  . PRO A 198 ? 0.62680 0.62756 0.57321 0.04653  0.00013  0.11612  527 PRO A CB  
1595 C CG  . PRO A 198 ? 0.61952 0.63005 0.57920 0.03630  0.00602  0.10174  527 PRO A CG  
1596 C CD  . PRO A 198 ? 0.61910 0.62013 0.58051 0.03952  0.00297  0.11063  527 PRO A CD  
1606 N N   . VAL B 2   ? 0.36044 0.37114 0.33461 0.00145  0.00829  0.00890  2   VAL B N   
1607 C CA  . VAL B 2   ? 0.31847 0.31029 0.28806 -0.01503 -0.01634 0.02628  2   VAL B CA  
1608 C C   . VAL B 2   ? 0.27035 0.27154 0.21368 -0.05397 -0.02504 0.03204  2   VAL B C   
1609 O O   . VAL B 2   ? 0.29624 0.29434 0.28106 -0.00670 -0.01582 -0.00791 2   VAL B O   
1610 C CB  . VAL B 2   ? 0.27963 0.32373 0.32262 -0.02145 0.00610  0.04395  2   VAL B CB  
1611 C CG1 . VAL B 2   ? 0.24918 0.33975 0.28200 -0.04085 0.01003  -0.00556 2   VAL B CG1 
1612 C CG2 . VAL B 2   ? 0.31617 0.33844 0.37725 0.01672  -0.02012 0.02410  2   VAL B CG2 
1613 N N   . GLN B 3   ? 0.28212 0.23861 0.19858 -0.01477 -0.00726 0.06544  3   GLN B N   
1614 C CA  . GLN B 3   ? 0.27631 0.27229 0.17208 -0.00011 -0.05389 0.03310  3   GLN B CA  
1615 C C   . GLN B 3   ? 0.22949 0.21058 0.18644 -0.04092 0.00124  0.01482  3   GLN B C   
1616 O O   . GLN B 3   ? 0.20402 0.28285 0.22976 -0.04702 -0.01407 0.06932  3   GLN B O   
1617 C CB  . GLN B 3   ? 0.36172 0.32695 0.25073 -0.01229 -0.10544 0.04851  3   GLN B CB  
1618 C CG  . GLN B 3   ? 0.41386 0.43364 0.35460 0.00518  -0.04256 0.03611  3   GLN B CG  
1619 C CD  . GLN B 3   ? 0.47019 0.49170 0.40081 0.01957  0.00077  0.06188  3   GLN B CD  
1620 O OE1 . GLN B 3   ? 0.50716 0.52463 0.41720 0.02546  0.01417  0.03585  3   GLN B OE1 
1621 N NE2 . GLN B 3   ? 0.47681 0.47627 0.40596 0.02630  -0.01165 0.03427  3   GLN B NE2 
1622 N N   . LEU B 4   ? 0.18743 0.20243 0.18491 -0.01260 -0.00719 0.02177  4   LEU B N   
1623 C CA  . LEU B 4   ? 0.18946 0.17262 0.16119 -0.02600 0.00932  -0.02584 4   LEU B CA  
1624 C C   . LEU B 4   ? 0.19193 0.17143 0.13911 -0.01866 -0.01952 -0.01115 4   LEU B C   
1625 O O   . LEU B 4   ? 0.19758 0.20521 0.16541 -0.04616 -0.00789 -0.02527 4   LEU B O   
1626 C CB  . LEU B 4   ? 0.18611 0.22558 0.18403 -0.03972 0.03620  -0.02923 4   LEU B CB  
1627 C CG  . LEU B 4   ? 0.19225 0.19802 0.20882 -0.05315 0.04639  -0.04861 4   LEU B CG  
1628 C CD1 . LEU B 4   ? 0.19691 0.19936 0.21222 -0.01400 0.04491  -0.02247 4   LEU B CD1 
1629 C CD2 . LEU B 4   ? 0.22646 0.20717 0.25673 -0.07756 0.04382  -0.05970 4   LEU B CD2 
1630 N N   . VAL B 5   ? 0.17168 0.17853 0.16112 -0.01256 -0.01453 0.00038  5   VAL B N   
1631 C CA  . VAL B 5   ? 0.19940 0.16546 0.15425 -0.01081 -0.01802 0.01282  5   VAL B CA  
1632 C C   . VAL B 5   ? 0.16862 0.18801 0.15934 -0.00810 -0.00044 -0.00233 5   VAL B C   
1633 O O   . VAL B 5   ? 0.17173 0.20368 0.18085 -0.03689 -0.02341 -0.00538 5   VAL B O   
1634 C CB  . VAL B 5   ? 0.24750 0.21882 0.11821 0.00937  0.02490  0.01640  5   VAL B CB  
1635 C CG1 . VAL B 5   ? 0.29903 0.19586 0.17355 0.01829  0.02523  -0.02019 5   VAL B CG1 
1636 C CG2 . VAL B 5   ? 0.27887 0.22209 0.15087 0.01743  0.01773  0.00826  5   VAL B CG2 
1637 N N   . GLU B 6   ? 0.15291 0.16990 0.12190 -0.00250 0.00253  0.00554  6   GLU B N   
1638 C CA  . GLU B 6   ? 0.14911 0.17096 0.15662 -0.03168 -0.00157 -0.00470 6   GLU B CA  
1639 C C   . GLU B 6   ? 0.14976 0.16592 0.14234 -0.00758 0.00164  -0.01350 6   GLU B C   
1640 O O   . GLU B 6   ? 0.18271 0.17989 0.13067 -0.01256 -0.01005 -0.01109 6   GLU B O   
1641 C CB  . GLU B 6   ? 0.16166 0.18035 0.15805 -0.03788 0.03700  -0.00955 6   GLU B CB  
1642 C CG  . GLU B 6   ? 0.16972 0.19759 0.21139 -0.02053 0.04929  -0.01495 6   GLU B CG  
1643 C CD  . GLU B 6   ? 0.16542 0.18192 0.16370 0.01509  -0.02724 -0.01593 6   GLU B CD  
1644 O OE1 . GLU B 6   ? 0.16581 0.18718 0.15972 0.00937  -0.00123 0.00833  6   GLU B OE1 
1645 O OE2 . GLU B 6   ? 0.19280 0.18672 0.12719 -0.01557 -0.01033 -0.00685 6   GLU B OE2 
1646 N N   . SER B 7   ? 0.14222 0.20310 0.14046 -0.00179 -0.01068 -0.00598 7   SER B N   
1647 C CA  A SER B 7   ? 0.15268 0.19479 0.16468 0.02638  0.00397  -0.00520 7   SER B CA  
1648 C CA  B SER B 7   ? 0.15506 0.19761 0.16414 0.01656  0.00399  -0.00632 7   SER B CA  
1649 C C   . SER B 7   ? 0.17742 0.18585 0.14178 0.00738  -0.01159 -0.00765 7   SER B C   
1650 O O   . SER B 7   ? 0.20856 0.19453 0.14683 0.00596  -0.01773 -0.00478 7   SER B O   
1651 C CB  A SER B 7   ? 0.16865 0.21265 0.19607 0.02225  0.01379  -0.00755 7   SER B CB  
1652 C CB  B SER B 7   ? 0.19365 0.23674 0.19055 -0.00537 0.01727  0.01524  7   SER B CB  
1653 O OG  A SER B 7   ? 0.16928 0.22494 0.19623 0.01927  0.03236  -0.00917 7   SER B OG  
1654 O OG  B SER B 7   ? 0.22349 0.26486 0.20247 0.02924  -0.00701 -0.01904 7   SER B OG  
1655 N N   . GLY B 8   ? 0.22405 0.17546 0.18039 0.02153  -0.01558 0.00555  8   GLY B N   
1656 C CA  . GLY B 8   ? 0.19705 0.20290 0.18913 0.01669  -0.00756 0.01426  8   GLY B CA  
1657 C C   . GLY B 8   ? 0.24937 0.20666 0.17580 0.02847  0.00019  -0.01134 8   GLY B C   
1658 O O   . GLY B 8   ? 0.25584 0.25443 0.21190 0.04326  0.01664  0.03796  8   GLY B O   
1659 N N   . GLY B 9   ? 0.22306 0.26647 0.19547 0.00419  0.00780  -0.02530 9   GLY B N   
1660 C CA  . GLY B 9   ? 0.24210 0.29349 0.24333 0.04533  0.02335  -0.01719 9   GLY B CA  
1661 C C   . GLY B 9   ? 0.24555 0.28111 0.26601 0.07110  0.01046  -0.03774 9   GLY B C   
1662 O O   . GLY B 9   ? 0.30176 0.29318 0.30482 0.09274  0.04241  -0.00764 9   GLY B O   
1663 N N   . GLY B 10  ? 0.25646 0.21970 0.20243 0.06156  0.01624  -0.00031 10  GLY B N   
1664 C CA  . GLY B 10  ? 0.28472 0.22712 0.20421 0.05456  0.00922  -0.00975 10  GLY B CA  
1665 C C   . GLY B 10  ? 0.28130 0.23494 0.17976 0.02323  0.01991  0.00219  10  GLY B C   
1666 O O   . GLY B 10  ? 0.26762 0.19088 0.24257 0.00305  0.02897  0.01184  10  GLY B O   
1667 N N   . SER B 11  ? 0.32916 0.24323 0.23144 0.05046  0.04698  0.01716  11  SER B N   
1668 C CA  . SER B 11  ? 0.31861 0.24881 0.26043 0.02584  0.00930  -0.02844 11  SER B CA  
1669 C C   . SER B 11  ? 0.31768 0.31240 0.29495 0.08346  0.00768  -0.00658 11  SER B C   
1670 O O   . SER B 11  ? 0.33077 0.39169 0.28818 0.11793  -0.01865 0.04360  11  SER B O   
1671 C CB  . SER B 11  ? 0.33020 0.28795 0.34582 0.04112  -0.01495 -0.03091 11  SER B CB  
1672 O OG  . SER B 11  ? 0.31907 0.30710 0.32479 0.02541  -0.02689 -0.06599 11  SER B OG  
1673 N N   . VAL B 12  ? 0.30965 0.29849 0.26713 0.06066  0.01839  0.02224  12  VAL B N   
1674 C CA  A VAL B 12  ? 0.33113 0.34974 0.36089 0.06102  0.00262  0.01596  12  VAL B CA  
1675 C CA  B VAL B 12  ? 0.33078 0.34904 0.36112 0.06031  0.00218  0.01596  12  VAL B CA  
1676 C C   . VAL B 12  ? 0.33920 0.35545 0.38083 0.06843  -0.00418 0.00337  12  VAL B C   
1677 O O   . VAL B 12  ? 0.35665 0.29839 0.35407 0.07166  -0.00855 0.07676  12  VAL B O   
1678 C CB  A VAL B 12  ? 0.34631 0.36946 0.36943 0.02834  -0.01055 0.02471  12  VAL B CB  
1679 C CB  B VAL B 12  ? 0.34266 0.36977 0.37148 0.02880  -0.01533 0.02164  12  VAL B CB  
1680 C CG1 A VAL B 12  ? 0.34934 0.35584 0.35873 0.02717  -0.00020 0.04039  12  VAL B CG1 
1681 C CG1 B VAL B 12  ? 0.34491 0.36319 0.37894 0.03529  -0.00381 0.02002  12  VAL B CG1 
1682 C CG2 A VAL B 12  ? 0.33897 0.34784 0.35857 0.01398  0.00485  0.02001  12  VAL B CG2 
1683 C CG2 B VAL B 12  ? 0.33257 0.36147 0.36414 0.02390  -0.02437 0.01127  12  VAL B CG2 
1684 N N   . GLN B 13  ? 0.39636 0.40627 0.44330 0.12797  0.00253  -0.02522 13  GLN B N   
1685 C CA  . GLN B 13  ? 0.43797 0.45348 0.50870 0.12809  -0.02373 -0.00831 13  GLN B CA  
1686 C C   . GLN B 13  ? 0.39864 0.40738 0.44125 0.12685  -0.04614 0.00638  13  GLN B C   
1687 O O   . GLN B 13  ? 0.38394 0.38763 0.38248 0.13521  -0.03930 0.04711  13  GLN B O   
1688 C CB  . GLN B 13  ? 0.51292 0.54603 0.60913 0.11517  -0.03195 -0.00993 13  GLN B CB  
1689 C CG  . GLN B 13  ? 0.57816 0.61343 0.67409 0.08877  -0.03264 -0.01248 13  GLN B CG  
1690 C CD  . GLN B 13  ? 0.63650 0.65927 0.72180 0.07245  -0.01632 -0.01805 13  GLN B CD  
1691 O OE1 . GLN B 13  ? 0.65968 0.68213 0.74490 0.07111  -0.02095 -0.02450 13  GLN B OE1 
1692 N NE2 . GLN B 13  ? 0.65250 0.66335 0.73760 0.06741  -0.01270 -0.02010 13  GLN B NE2 
1693 N N   . ALA B 14  ? 0.33999 0.31722 0.35135 0.09021  -0.04659 0.02409  14  ALA B N   
1694 C CA  . ALA B 14  ? 0.32310 0.28096 0.31649 0.07452  -0.05481 0.04428  14  ALA B CA  
1695 C C   . ALA B 14  ? 0.30709 0.28731 0.32074 0.08516  -0.03538 0.05977  14  ALA B C   
1696 O O   . ALA B 14  ? 0.35781 0.30309 0.32271 0.11005  -0.04595 0.07138  14  ALA B O   
1697 C CB  . ALA B 14  ? 0.31485 0.32781 0.33074 0.06099  -0.04634 0.01194  14  ALA B CB  
1698 N N   . GLY B 15  ? 0.27543 0.28886 0.26557 0.05016  -0.02274 0.04368  15  GLY B N   
1699 C CA  . GLY B 15  ? 0.27572 0.28912 0.29984 0.03710  -0.00181 0.04819  15  GLY B CA  
1700 C C   . GLY B 15  ? 0.27836 0.28381 0.33712 0.05975  -0.03002 0.04929  15  GLY B C   
1701 O O   . GLY B 15  ? 0.29498 0.29562 0.40084 0.08763  -0.01578 0.06562  15  GLY B O   
1702 N N   . GLY B 16  ? 0.29165 0.28308 0.33010 0.06937  -0.01116 0.02445  16  GLY B N   
1703 C CA  . GLY B 16  ? 0.26766 0.29695 0.33790 0.08313  0.01627  0.03880  16  GLY B CA  
1704 C C   . GLY B 16  ? 0.24258 0.28664 0.27071 0.09142  -0.00743 0.03334  16  GLY B C   
1705 O O   . GLY B 16  ? 0.24950 0.27323 0.27881 0.06270  0.00586  0.00535  16  GLY B O   
1706 N N   . SER B 17  ? 0.27797 0.26494 0.33575 0.09706  0.03405  0.01939  17  SER B N   
1707 C CA  A SER B 17  ? 0.26716 0.25086 0.28560 0.06291  -0.00129 0.01544  17  SER B CA  
1708 C CA  B SER B 17  ? 0.26647 0.25092 0.28490 0.06228  0.00144  0.01567  17  SER B CA  
1709 C C   . SER B 17  ? 0.26559 0.25827 0.26591 0.07942  0.02384  -0.01669 17  SER B C   
1710 O O   . SER B 17  ? 0.28372 0.28470 0.28991 0.09988  0.03133  -0.02239 17  SER B O   
1711 C CB  A SER B 17  ? 0.30169 0.32114 0.34116 0.05866  -0.02437 -0.02018 17  SER B CB  
1712 C CB  B SER B 17  ? 0.30738 0.31774 0.34102 0.05545  -0.03455 -0.01301 17  SER B CB  
1713 O OG  A SER B 17  ? 0.28808 0.35821 0.35373 0.05324  -0.02144 -0.03448 17  SER B OG  
1714 O OG  B SER B 17  ? 0.31480 0.33655 0.35492 0.07925  -0.05007 0.00403  17  SER B OG  
1715 N N   . LEU B 18  ? 0.21367 0.22122 0.24416 0.04553  0.01621  -0.00046 18  LEU B N   
1716 C CA  . LEU B 18  ? 0.21931 0.22755 0.23945 0.03458  -0.02790 -0.00910 18  LEU B CA  
1717 C C   . LEU B 18  ? 0.19530 0.24123 0.21993 0.03373  -0.01365 0.00557  18  LEU B C   
1718 O O   . LEU B 18  ? 0.27341 0.24550 0.19695 0.03885  0.01073  -0.01093 18  LEU B O   
1719 C CB  . LEU B 18  ? 0.23204 0.24767 0.25432 -0.00969 -0.04164 -0.01294 18  LEU B CB  
1720 C CG  . LEU B 18  ? 0.24388 0.28739 0.27914 0.00821  0.00183  -0.01205 18  LEU B CG  
1721 C CD1 . LEU B 18  ? 0.24154 0.28943 0.28694 -0.00999 -0.03077 0.00724  18  LEU B CD1 
1722 C CD2 . LEU B 18  ? 0.28782 0.29968 0.29472 0.02742  -0.00075 -0.03565 18  LEU B CD2 
1723 N N   . ARG B 19  ? 0.18451 0.24074 0.21037 0.04238  0.00890  0.00466  19  ARG B N   
1724 C CA  A ARG B 19  ? 0.16449 0.25105 0.19606 0.00988  -0.00063 0.01144  19  ARG B CA  
1725 C CA  B ARG B 19  ? 0.16455 0.24985 0.19577 0.01096  -0.00245 0.01257  19  ARG B CA  
1726 C C   . ARG B 19  ? 0.17685 0.23285 0.17394 0.03658  -0.01302 -0.02848 19  ARG B C   
1727 O O   . ARG B 19  ? 0.18491 0.31641 0.18071 0.04245  0.00640  -0.03992 19  ARG B O   
1728 C CB  A ARG B 19  ? 0.18019 0.30338 0.23065 -0.02237 0.00445  -0.00277 19  ARG B CB  
1729 C CB  B ARG B 19  ? 0.17804 0.30420 0.22292 -0.01452 -0.00788 -0.00613 19  ARG B CB  
1730 C CG  A ARG B 19  ? 0.20821 0.31519 0.26032 -0.05297 -0.01852 0.03012  19  ARG B CG  
1731 C CG  B ARG B 19  ? 0.18625 0.30119 0.25970 -0.07624 -0.03417 0.03306  19  ARG B CG  
1732 C CD  A ARG B 19  ? 0.26429 0.37730 0.33957 -0.01294 -0.00458 0.01923  19  ARG B CD  
1733 C CD  B ARG B 19  ? 0.25850 0.36676 0.31721 -0.01074 -0.03423 0.04067  19  ARG B CD  
1734 N NE  A ARG B 19  ? 0.30100 0.39683 0.37750 0.01985  0.00014  0.00452  19  ARG B NE  
1735 N NE  B ARG B 19  ? 0.29103 0.40144 0.37158 0.01485  -0.00330 0.02219  19  ARG B NE  
1736 C CZ  A ARG B 19  ? 0.33944 0.42237 0.41678 0.03470  0.00274  0.00669  19  ARG B CZ  
1737 C CZ  B ARG B 19  ? 0.33511 0.41201 0.42015 0.04131  0.00265  0.00545  19  ARG B CZ  
1738 N NH1 A ARG B 19  ? 0.34687 0.41750 0.40586 0.00942  0.03804  0.00668  19  ARG B NH1 
1739 N NH1 B ARG B 19  ? 0.32455 0.41875 0.40935 0.01522  0.00908  0.01688  19  ARG B NH1 
1740 N NH2 A ARG B 19  ? 0.35182 0.40766 0.45257 -0.00731 -0.00954 0.02078  19  ARG B NH2 
1741 N NH2 B ARG B 19  ? 0.33481 0.40518 0.42135 0.02242  0.01825  0.01557  19  ARG B NH2 
1742 N N   . LEU B 20  ? 0.16950 0.18273 0.16762 0.00932  -0.00116 -0.01029 20  LEU B N   
1743 C CA  . LEU B 20  ? 0.15319 0.19437 0.17588 0.01172  -0.03166 0.01499  20  LEU B CA  
1744 C C   . LEU B 20  ? 0.15340 0.19534 0.16666 -0.00342 -0.01350 0.01717  20  LEU B C   
1745 O O   . LEU B 20  ? 0.16975 0.21037 0.16999 -0.01814 -0.01583 -0.00212 20  LEU B O   
1746 C CB  . LEU B 20  ? 0.14013 0.20721 0.16473 -0.00530 -0.00159 -0.00372 20  LEU B CB  
1747 C CG  . LEU B 20  ? 0.15484 0.19095 0.17966 -0.03636 0.00309  -0.00491 20  LEU B CG  
1748 C CD1 . LEU B 20  ? 0.15833 0.22701 0.18941 -0.00880 0.01310  0.01602  20  LEU B CD1 
1749 C CD2 . LEU B 20  ? 0.18388 0.22970 0.18805 -0.00907 -0.02408 -0.00247 20  LEU B CD2 
1750 N N   . SER B 21  ? 0.15044 0.17960 0.17327 -0.00388 -0.01059 0.00583  21  SER B N   
1751 C CA  A SER B 21  ? 0.18056 0.19189 0.16044 -0.00505 -0.01923 0.01502  21  SER B CA  
1752 C CA  B SER B 21  ? 0.18468 0.19420 0.16636 -0.00518 -0.00476 0.03003  21  SER B CA  
1753 C C   . SER B 21  ? 0.18584 0.16996 0.17318 -0.01923 -0.01782 -0.00450 21  SER B C   
1754 O O   . SER B 21  ? 0.17635 0.17863 0.16603 -0.02190 -0.01050 -0.00929 21  SER B O   
1755 C CB  A SER B 21  ? 0.20663 0.25176 0.21803 0.00961  0.02027  0.01835  21  SER B CB  
1756 C CB  B SER B 21  ? 0.22469 0.23518 0.21683 0.00354  0.01744  0.03207  21  SER B CB  
1757 O OG  A SER B 21  ? 0.21912 0.25468 0.27161 -0.00008 0.04434  -0.00854 21  SER B OG  
1758 O OG  B SER B 21  ? 0.24340 0.25747 0.31113 0.00635  0.02266  -0.01383 21  SER B OG  
1759 N N   . CYS B 22  ? 0.16017 0.17950 0.17699 -0.01409 -0.00309 0.00451  22  CYS B N   
1760 C CA  . CYS B 22  ? 0.15995 0.18226 0.16611 -0.02575 0.00186  0.01493  22  CYS B CA  
1761 C C   . CYS B 22  ? 0.17595 0.18171 0.16188 -0.02519 -0.01764 -0.01537 22  CYS B C   
1762 O O   . CYS B 22  ? 0.19989 0.17711 0.17646 -0.03503 -0.02712 -0.00167 22  CYS B O   
1763 C CB  . CYS B 22  ? 0.16418 0.21349 0.17645 -0.02745 -0.01955 0.01362  22  CYS B CB  
1764 S SG  . CYS B 22  ? 0.18010 0.21332 0.23760 -0.00381 -0.03013 -0.00373 22  CYS B SG  
1765 N N   . ALA B 23  ? 0.16972 0.19558 0.15050 -0.02730 0.00238  0.00864  23  ALA B N   
1766 C CA  . ALA B 23  ? 0.19590 0.21245 0.16821 -0.02510 -0.00294 0.00711  23  ALA B CA  
1767 C C   . ALA B 23  ? 0.18359 0.18490 0.16039 -0.06279 -0.02514 0.00583  23  ALA B C   
1768 O O   . ALA B 23  ? 0.19777 0.18208 0.17586 -0.05262 -0.01189 0.00671  23  ALA B O   
1769 C CB  . ALA B 23  ? 0.21667 0.24617 0.19505 -0.01765 0.02158  0.01633  23  ALA B CB  
1770 N N   . ALA B 24  ? 0.17264 0.18632 0.17568 -0.03974 0.00705  -0.00857 24  ALA B N   
1771 C CA  . ALA B 24  ? 0.17870 0.18327 0.16885 -0.01836 0.01954  0.03328  24  ALA B CA  
1772 C C   . ALA B 24  ? 0.19490 0.22841 0.19012 -0.04523 -0.00663 -0.01505 24  ALA B C   
1773 O O   . ALA B 24  ? 0.23575 0.27073 0.24219 -0.08224 0.01902  0.00744  24  ALA B O   
1774 C CB  . ALA B 24  ? 0.19120 0.17194 0.21082 -0.02864 -0.00138 -0.01961 24  ALA B CB  
1775 N N   . SER B 25  ? 0.21056 0.22361 0.18467 -0.06446 0.02748  -0.01360 25  SER B N   
1776 C CA  . SER B 25  ? 0.24017 0.26267 0.22531 -0.03279 0.05258  0.01418  25  SER B CA  
1777 C C   . SER B 25  ? 0.28161 0.27349 0.18902 -0.05682 0.04784  -0.01462 25  SER B C   
1778 O O   . SER B 25  ? 0.29884 0.28132 0.17993 -0.03681 0.00014  0.01167  25  SER B O   
1779 C CB  . SER B 25  ? 0.27228 0.30959 0.22389 -0.06138 0.04708  -0.03366 25  SER B CB  
1780 O OG  . SER B 25  ? 0.33981 0.27132 0.22171 -0.03698 0.03682  -0.01075 25  SER B OG  
1781 N N   . GLY B 26  ? 0.33080 0.23404 0.18947 -0.00565 0.02888  -0.00465 26  GLY B N   
1782 C CA  . GLY B 26  ? 0.31081 0.22823 0.18994 -0.03436 0.02649  -0.00069 26  GLY B CA  
1783 C C   . GLY B 26  ? 0.26716 0.23514 0.22775 -0.03428 0.04220  0.01849  26  GLY B C   
1784 O O   . GLY B 26  ? 0.29140 0.25382 0.19835 -0.01658 0.05419  -0.00086 26  GLY B O   
1808 N N   . GLY B 29  ? 0.29606 0.23939 0.20452 -0.00050 0.02526  -0.01974 29  GLY B N   
1809 C CA  . GLY B 29  ? 0.22424 0.26273 0.18781 -0.04306 0.00889  -0.02177 29  GLY B CA  
1810 C C   . GLY B 29  ? 0.18392 0.29375 0.16487 -0.04566 0.01069  0.01249  29  GLY B C   
1811 O O   . GLY B 29  ? 0.28114 0.33475 0.16520 0.02754  0.02746  -0.01729 29  GLY B O   
1812 N N   . ARG B 30  ? 0.18684 0.21336 0.17820 -0.04650 0.00632  -0.00798 30  ARG B N   
1813 C CA  . ARG B 30  ? 0.17764 0.18544 0.17257 -0.03821 0.01034  -0.01234 30  ARG B CA  
1814 C C   . ARG B 30  ? 0.18544 0.20993 0.17592 -0.03592 -0.01003 -0.01872 30  ARG B C   
1815 O O   . ARG B 30  ? 0.18914 0.19678 0.19769 -0.05211 -0.01142 0.01280  30  ARG B O   
1816 C CB  . ARG B 30  ? 0.19566 0.20096 0.16663 -0.03853 0.01799  -0.01548 30  ARG B CB  
1817 C CG  . ARG B 30  ? 0.27239 0.20824 0.16935 -0.02557 0.01801  -0.04106 30  ARG B CG  
1818 C CD  . ARG B 30  ? 0.22844 0.26045 0.19048 -0.06487 -0.00177 -0.00803 30  ARG B CD  
1819 N NE  . ARG B 30  ? 0.20437 0.29146 0.18601 -0.05703 -0.03780 -0.04262 30  ARG B NE  
1820 C CZ  . ARG B 30  ? 0.26947 0.30426 0.24060 -0.03533 -0.00803 -0.03790 30  ARG B CZ  
1821 N NH1 . ARG B 30  ? 0.31091 0.33700 0.24186 -0.01475 -0.05886 -0.00946 30  ARG B NH1 
1822 N NH2 . ARG B 30  ? 0.27349 0.33386 0.26547 -0.03305 0.00982  -0.09533 30  ARG B NH2 
1823 N N   . THR B 31  ? 0.18212 0.22061 0.16137 -0.02308 0.00296  -0.00380 31  THR B N   
1824 C CA  . THR B 31  ? 0.20981 0.19017 0.17066 -0.03539 0.00971  0.03213  31  THR B CA  
1825 C C   . THR B 31  ? 0.21944 0.19486 0.15656 -0.07033 -0.00440 -0.00265 31  THR B C   
1826 O O   . THR B 31  ? 0.21160 0.30573 0.18161 -0.07145 -0.00638 -0.03930 31  THR B O   
1827 C CB  . THR B 31  ? 0.21653 0.21859 0.19280 -0.02134 0.00582  0.00091  31  THR B CB  
1828 O OG1 . THR B 31  ? 0.25626 0.23622 0.20361 -0.00145 0.00457  0.01014  31  THR B OG1 
1829 C CG2 . THR B 31  ? 0.23133 0.22855 0.21130 -0.06388 -0.00836 0.05251  31  THR B CG2 
1830 N N   . CYS B 32  ? 0.18783 0.18736 0.19005 -0.04787 0.01518  -0.01421 32  CYS B N   
1831 C CA  . CYS B 32  ? 0.22127 0.18758 0.17222 -0.03810 0.03329  -0.02229 32  CYS B CA  
1832 C C   . CYS B 32  ? 0.22503 0.19841 0.14353 -0.05824 0.01583  -0.03963 32  CYS B C   
1833 O O   . CYS B 32  ? 0.29539 0.20386 0.17641 -0.05915 -0.00995 -0.04009 32  CYS B O   
1834 C CB  . CYS B 32  ? 0.21813 0.18047 0.21390 -0.02941 0.02134  -0.01500 32  CYS B CB  
1835 S SG  . CYS B 32  ? 0.24466 0.18694 0.21834 -0.03544 0.02820  -0.01254 32  CYS B SG  
1836 N N   A ASN B 33  ? 0.23526 0.18244 0.15639 -0.04358 -0.00647 -0.00911 33  ASN B N   
1837 N N   B ASN B 33  ? 0.24006 0.18034 0.15654 -0.04551 -0.00902 -0.01284 33  ASN B N   
1838 C CA  A ASN B 33  ? 0.24990 0.17444 0.14959 -0.04702 0.00840  0.00230  33  ASN B CA  
1839 C CA  B ASN B 33  ? 0.24157 0.16332 0.13893 -0.04883 -0.00103 -0.01270 33  ASN B CA  
1840 C C   A ASN B 33  ? 0.21244 0.17869 0.14938 -0.05601 -0.03037 0.00724  33  ASN B C   
1841 C C   B ASN B 33  ? 0.21588 0.16858 0.13575 -0.05176 -0.01204 0.01075  33  ASN B C   
1842 O O   A ASN B 33  ? 0.23164 0.17120 0.13169 -0.05414 -0.01536 0.02973  33  ASN B O   
1843 O O   B ASN B 33  ? 0.23445 0.17314 0.14819 -0.02958 -0.04208 -0.00349 33  ASN B O   
1844 C CB  A ASN B 33  ? 0.29541 0.20668 0.23350 -0.01081 0.04004  -0.00697 33  ASN B CB  
1845 C CB  B ASN B 33  ? 0.26001 0.18237 0.19927 -0.03739 0.02424  -0.02149 33  ASN B CB  
1846 C CG  A ASN B 33  ? 0.29657 0.25483 0.26850 0.00286  0.02772  -0.03548 33  ASN B CG  
1847 C CG  B ASN B 33  ? 0.28961 0.23871 0.27511 -0.00916 0.05599  -0.03600 33  ASN B CG  
1848 O OD1 A ASN B 33  ? 0.28397 0.27190 0.29326 -0.03246 0.03976  0.00453  33  ASN B OD1 
1849 O OD1 B ASN B 33  ? 0.25538 0.33569 0.32638 -0.00430 0.02195  0.03179  33  ASN B OD1 
1850 N ND2 A ASN B 33  ? 0.29328 0.34163 0.28761 0.05220  0.06864  -0.09009 33  ASN B ND2 
1851 N ND2 B ASN B 33  ? 0.25274 0.26998 0.24214 -0.02018 0.01195  -0.08392 33  ASN B ND2 
1852 N N   . LEU B 34  ? 0.20962 0.17641 0.13637 -0.05036 -0.02514 -0.00877 34  LEU B N   
1853 C CA  . LEU B 34  ? 0.18627 0.18813 0.13787 -0.02969 -0.00737 0.00507  34  LEU B CA  
1854 C C   . LEU B 34  ? 0.15798 0.19401 0.11567 -0.02176 -0.01278 -0.00231 34  LEU B C   
1855 O O   . LEU B 34  ? 0.17047 0.19707 0.13921 -0.03864 -0.01923 0.00214  34  LEU B O   
1856 C CB  . LEU B 34  ? 0.19645 0.21472 0.16768 -0.05008 -0.01182 0.00002  34  LEU B CB  
1857 C CG  . LEU B 34  ? 0.17419 0.21853 0.18808 -0.02652 -0.00851 -0.00336 34  LEU B CG  
1858 C CD1 . LEU B 34  ? 0.17234 0.23874 0.19554 -0.01859 0.01598  -0.00468 34  LEU B CD1 
1859 C CD2 . LEU B 34  ? 0.17782 0.19769 0.20398 0.00172  0.00610  0.01953  34  LEU B CD2 
1860 N N   . VAL B 35  ? 0.15697 0.15851 0.13151 -0.01153 -0.00205 -0.00038 35  VAL B N   
1861 C CA  . VAL B 35  ? 0.15743 0.14702 0.12128 -0.02275 0.00561  -0.00697 35  VAL B CA  
1862 C C   . VAL B 35  ? 0.14471 0.17669 0.10270 -0.01982 -0.02454 0.01792  35  VAL B C   
1863 O O   . VAL B 35  ? 0.17495 0.17174 0.11941 -0.00602 -0.01618 0.00541  35  VAL B O   
1864 C CB  . VAL B 35  ? 0.14678 0.18244 0.14895 -0.00574 -0.00292 -0.00873 35  VAL B CB  
1865 C CG1 . VAL B 35  ? 0.16179 0.17852 0.13514 -0.01607 0.00167  0.02078  35  VAL B CG1 
1866 C CG2 . VAL B 35  ? 0.19231 0.18043 0.16493 0.02287  -0.00871 -0.03460 35  VAL B CG2 
1867 N N   . TRP B 36  ? 0.13959 0.16674 0.12943 -0.01489 -0.01450 0.00965  36  TRP B N   
1868 C CA  . TRP B 36  ? 0.13094 0.16474 0.12241 -0.00399 -0.00044 -0.01307 36  TRP B CA  
1869 C C   . TRP B 36  ? 0.15144 0.17382 0.10043 0.01612  0.01338  0.00620  36  TRP B C   
1870 O O   . TRP B 36  ? 0.15237 0.16768 0.12270 -0.01033 -0.00473 0.00007  36  TRP B O   
1871 C CB  . TRP B 36  ? 0.13754 0.20156 0.13157 0.00155  -0.01391 0.01684  36  TRP B CB  
1872 C CG  . TRP B 36  ? 0.13794 0.18764 0.14954 -0.00013 -0.01371 -0.01161 36  TRP B CG  
1873 C CD1 . TRP B 36  ? 0.15610 0.22420 0.21238 -0.00799 0.00616  0.00893  36  TRP B CD1 
1874 C CD2 . TRP B 36  ? 0.17302 0.18484 0.14456 0.00644  0.00579  0.01993  36  TRP B CD2 
1875 N NE1 . TRP B 36  ? 0.17242 0.19982 0.26356 0.00499  0.03099  0.02803  36  TRP B NE1 
1876 C CE2 . TRP B 36  ? 0.19701 0.19986 0.19353 0.02393  0.04575  0.05836  36  TRP B CE2 
1877 C CE3 . TRP B 36  ? 0.21919 0.20577 0.13488 0.04466  0.00276  -0.00925 36  TRP B CE3 
1878 C CZ2 . TRP B 36  ? 0.23910 0.26020 0.23884 0.07533  0.07196  0.08835  36  TRP B CZ2 
1879 C CZ3 . TRP B 36  ? 0.25510 0.24177 0.15024 0.07801  -0.00920 -0.01833 36  TRP B CZ3 
1880 C CH2 . TRP B 36  ? 0.27717 0.28885 0.17870 0.10375  0.06198  0.05027  36  TRP B CH2 
1881 N N   . TYR B 37  ? 0.14671 0.15914 0.12878 -0.02140 -0.00523 -0.00426 37  TYR B N   
1882 C CA  . TYR B 37  ? 0.13841 0.15523 0.14374 -0.00999 -0.00204 -0.00816 37  TYR B CA  
1883 C C   . TYR B 37  ? 0.13196 0.15951 0.12615 -0.00538 -0.01376 -0.01302 37  TYR B C   
1884 O O   . TYR B 37  ? 0.15171 0.16673 0.13045 -0.00718 -0.00021 -0.01465 37  TYR B O   
1885 C CB  . TYR B 37  ? 0.13302 0.16242 0.15637 0.00239  -0.02733 0.00128  37  TYR B CB  
1886 C CG  . TYR B 37  ? 0.13068 0.15177 0.15377 -0.00802 -0.02285 -0.00224 37  TYR B CG  
1887 C CD1 . TYR B 37  ? 0.15002 0.18790 0.12684 0.00391  0.00036  -0.01009 37  TYR B CD1 
1888 C CD2 . TYR B 37  ? 0.15389 0.16822 0.14976 -0.01296 -0.01932 0.00764  37  TYR B CD2 
1889 C CE1 . TYR B 37  ? 0.14792 0.19928 0.12391 0.01696  -0.01603 -0.02589 37  TYR B CE1 
1890 C CE2 . TYR B 37  ? 0.16471 0.17685 0.13575 -0.00145 -0.01213 0.00117  37  TYR B CE2 
1891 C CZ  . TYR B 37  ? 0.15162 0.18207 0.10986 -0.00967 -0.02324 0.00693  37  TYR B CZ  
1892 O OH  . TYR B 37  ? 0.17574 0.17858 0.15410 0.01541  -0.02016 -0.02049 37  TYR B OH  
1893 N N   . ARG B 38  ? 0.15397 0.14660 0.13917 -0.01607 -0.01050 -0.00686 38  ARG B N   
1894 C CA  . ARG B 38  ? 0.14028 0.14726 0.13967 -0.02442 -0.00002 0.00709  38  ARG B CA  
1895 C C   . ARG B 38  ? 0.13641 0.15768 0.12991 -0.00705 -0.00280 -0.00006 38  ARG B C   
1896 O O   . ARG B 38  ? 0.13778 0.18467 0.14657 -0.00584 0.00375  -0.01304 38  ARG B O   
1897 C CB  . ARG B 38  ? 0.15281 0.19431 0.12504 0.01046  -0.02078 0.01781  38  ARG B CB  
1898 C CG  . ARG B 38  ? 0.14393 0.21894 0.16318 -0.00538 -0.01571 0.01553  38  ARG B CG  
1899 C CD  . ARG B 38  ? 0.20372 0.22323 0.12090 0.01608  -0.02275 0.01920  38  ARG B CD  
1900 N NE  . ARG B 38  ? 0.20828 0.20375 0.16940 0.01198  -0.02073 0.03229  38  ARG B NE  
1901 C CZ  . ARG B 38  ? 0.21435 0.22732 0.17276 -0.00201 -0.01785 0.04568  38  ARG B CZ  
1902 N NH1 . ARG B 38  ? 0.19431 0.19853 0.18038 -0.00934 -0.02989 0.00849  38  ARG B NH1 
1903 N NH2 . ARG B 38  ? 0.24658 0.32106 0.17180 0.04611  -0.00162 0.06180  38  ARG B NH2 
1904 N N   . GLN B 39  ? 0.14058 0.17552 0.14967 -0.01482 -0.01059 -0.01535 39  GLN B N   
1905 C CA  A GLN B 39  ? 0.15222 0.20824 0.15964 -0.02524 -0.01024 -0.02285 39  GLN B CA  
1906 C CA  B GLN B 39  ? 0.15177 0.20854 0.15819 -0.02510 -0.00979 -0.02283 39  GLN B CA  
1907 C C   . GLN B 39  ? 0.16423 0.25357 0.18529 -0.03178 0.01675  -0.04180 39  GLN B C   
1908 O O   . GLN B 39  ? 0.18218 0.30136 0.23089 -0.02334 0.03737  -0.09844 39  GLN B O   
1909 C CB  A GLN B 39  ? 0.16645 0.25021 0.20376 -0.02606 -0.04823 0.03748  39  GLN B CB  
1910 C CB  B GLN B 39  ? 0.16439 0.25284 0.19982 -0.02939 -0.04927 0.03696  39  GLN B CB  
1911 C CG  A GLN B 39  ? 0.18568 0.26001 0.24071 -0.01935 -0.04526 0.03834  39  GLN B CG  
1912 C CG  B GLN B 39  ? 0.19509 0.27843 0.24756 -0.03581 -0.03744 0.04444  39  GLN B CG  
1913 C CD  A GLN B 39  ? 0.17730 0.23124 0.21260 0.02435  -0.03577 0.03385  39  GLN B CD  
1914 C CD  B GLN B 39  ? 0.24563 0.28814 0.29787 -0.00247 -0.03109 0.03319  39  GLN B CD  
1915 O OE1 A GLN B 39  ? 0.18111 0.21127 0.20747 0.03041  -0.05124 0.00145  39  GLN B OE1 
1916 O OE1 B GLN B 39  ? 0.23271 0.34481 0.29046 -0.02233 0.00298  0.00870  39  GLN B OE1 
1917 N NE2 A GLN B 39  ? 0.18651 0.20361 0.27016 0.03879  -0.04472 -0.01914 39  GLN B NE2 
1918 N NE2 B GLN B 39  ? 0.24349 0.27559 0.30074 0.01943  -0.05343 -0.06430 39  GLN B NE2 
1919 N N   . ALA B 40  ? 0.22720 0.22295 0.23817 -0.03391 0.01090  -0.00507 40  ALA B N   
1920 C CA  . ALA B 40  ? 0.26971 0.21955 0.21902 -0.06801 0.01089  -0.00585 40  ALA B CA  
1921 C C   . ALA B 40  ? 0.26430 0.25454 0.22952 -0.05954 -0.01073 -0.05299 40  ALA B C   
1922 O O   . ALA B 40  ? 0.27899 0.27532 0.22867 -0.04773 -0.03729 -0.02661 40  ALA B O   
1923 C CB  . ALA B 40  ? 0.28250 0.25912 0.25261 -0.03970 -0.01461 0.03426  40  ALA B CB  
1924 N N   . PRO B 41  ? 0.28330 0.28877 0.21239 -0.05623 0.00700  -0.03075 41  PRO B N   
1925 C CA  . PRO B 41  ? 0.27479 0.30985 0.17906 -0.06998 -0.00363 -0.05713 41  PRO B CA  
1926 C C   . PRO B 41  ? 0.26917 0.23161 0.21286 -0.05516 -0.00101 0.01762  41  PRO B C   
1927 O O   . PRO B 41  ? 0.28896 0.20152 0.19984 -0.05809 -0.00180 -0.01641 41  PRO B O   
1928 C CB  . PRO B 41  ? 0.28271 0.32390 0.25123 -0.09642 0.02342  -0.04691 41  PRO B CB  
1929 C CG  . PRO B 41  ? 0.29037 0.33209 0.27384 -0.07966 0.03448  -0.09639 41  PRO B CG  
1930 C CD  . PRO B 41  ? 0.29184 0.33198 0.23802 -0.05281 0.05610  -0.06474 41  PRO B CD  
1931 N N   . GLY B 42  ? 0.25703 0.29239 0.21103 0.01083  -0.00914 0.00746  42  GLY B N   
1932 C CA  . GLY B 42  ? 0.28750 0.24630 0.22554 0.00530  -0.03061 0.00285  42  GLY B CA  
1933 C C   . GLY B 42  ? 0.28969 0.30140 0.29580 0.00600  -0.00581 -0.02251 42  GLY B C   
1934 O O   . GLY B 42  ? 0.29938 0.30268 0.31151 -0.00021 -0.02423 -0.01709 42  GLY B O   
1935 N N   . LYS B 43  ? 0.32461 0.28866 0.28911 -0.03119 -0.04397 -0.04114 43  LYS B N   
1936 C CA  . LYS B 43  ? 0.34924 0.38501 0.36398 0.01322  -0.02013 -0.02149 43  LYS B CA  
1937 C C   . LYS B 43  ? 0.26673 0.34417 0.33927 -0.08339 -0.07277 -0.00240 43  LYS B C   
1938 O O   . LYS B 43  ? 0.29291 0.37103 0.32006 -0.03353 -0.05873 0.02246  43  LYS B O   
1939 C CB  . LYS B 43  ? 0.43936 0.45964 0.43874 0.02909  0.00419  0.02398  43  LYS B CB  
1940 C CG  . LYS B 43  ? 0.51010 0.50692 0.55307 0.03217  -0.00472 0.01489  43  LYS B CG  
1941 C CD  . LYS B 43  ? 0.55071 0.55275 0.60190 0.03705  -0.01421 0.00312  43  LYS B CD  
1942 C CE  . LYS B 43  ? 0.58060 0.58453 0.61698 0.04394  -0.02621 0.00623  43  LYS B CE  
1943 N NZ  . LYS B 43  ? 0.60440 0.59040 0.63444 0.04168  -0.01533 0.00297  43  LYS B NZ  
1944 N N   . GLU B 44  ? 0.22013 0.29253 0.27798 -0.09335 -0.03201 0.04304  44  GLU B N   
1945 C CA  . GLU B 44  ? 0.21898 0.27963 0.30138 -0.08827 0.00963  0.05355  44  GLU B CA  
1946 C C   . GLU B 44  ? 0.15154 0.27172 0.30953 -0.06645 -0.04655 0.04808  44  GLU B C   
1947 O O   . GLU B 44  ? 0.18087 0.26145 0.32276 -0.06565 -0.06616 0.06751  44  GLU B O   
1948 C CB  . GLU B 44  ? 0.28301 0.28531 0.29177 -0.00827 0.02513  0.02625  44  GLU B CB  
1949 C CG  . GLU B 44  ? 0.31585 0.31239 0.32017 0.00610  -0.01642 0.03446  44  GLU B CG  
1950 C CD  . GLU B 44  ? 0.34830 0.35605 0.35117 0.02087  -0.05726 0.01555  44  GLU B CD  
1951 O OE1 . GLU B 44  ? 0.36107 0.37899 0.40366 0.01151  -0.03314 0.02013  44  GLU B OE1 
1952 O OE2 . GLU B 44  ? 0.32938 0.36791 0.30523 0.03967  -0.07874 0.01788  44  GLU B OE2 
1953 N N   . LEU B 45  ? 0.15989 0.21477 0.34496 -0.04968 -0.04006 0.05936  45  LEU B N   
1954 C CA  . LEU B 45  ? 0.15831 0.18943 0.25196 -0.01426 -0.02843 0.05485  45  LEU B CA  
1955 C C   . LEU B 45  ? 0.15914 0.19904 0.20641 0.00928  0.00006  0.01867  45  LEU B C   
1956 O O   . LEU B 45  ? 0.18146 0.23297 0.22182 0.03079  0.04066  0.03901  45  LEU B O   
1957 C CB  . LEU B 45  ? 0.15356 0.23407 0.27172 -0.02252 -0.02456 0.06437  45  LEU B CB  
1958 C CG  . LEU B 45  ? 0.16431 0.20724 0.22811 0.00173  -0.02736 0.04397  45  LEU B CG  
1959 C CD1 . LEU B 45  ? 0.17488 0.21499 0.20569 0.00473  -0.04182 0.01437  45  LEU B CD1 
1960 C CD2 . LEU B 45  ? 0.19639 0.20355 0.23076 0.01653  -0.05455 0.05528  45  LEU B CD2 
1961 N N   . GLU B 46  ? 0.13988 0.18990 0.17717 -0.01037 -0.00298 -0.02466 46  GLU B N   
1962 C CA  . GLU B 46  ? 0.15900 0.22468 0.15454 -0.02763 -0.01232 -0.01926 46  GLU B CA  
1963 C C   . GLU B 46  ? 0.13532 0.19839 0.14240 -0.01120 -0.02044 -0.02213 46  GLU B C   
1964 O O   . GLU B 46  ? 0.17480 0.20351 0.12796 -0.01998 0.01138  -0.02103 46  GLU B O   
1965 C CB  . GLU B 46  ? 0.28559 0.25020 0.19022 -0.02467 -0.04780 0.04038  46  GLU B CB  
1966 C CG  . GLU B 46  ? 0.35938 0.35824 0.35190 0.01819  -0.03998 0.00997  46  GLU B CG  
1967 C CD  . GLU B 46  ? 0.39298 0.38759 0.44598 0.04280  0.00515  0.08674  46  GLU B CD  
1968 O OE1 . GLU B 46  ? 0.33764 0.33870 0.38267 0.01652  0.05746  0.15278  46  GLU B OE1 
1969 O OE2 . GLU B 46  ? 0.44725 0.45630 0.50432 0.01553  0.02599  0.04999  46  GLU B OE2 
1970 N N   . PHE B 47  ? 0.13923 0.17431 0.14821 -0.01317 0.00107  -0.02165 47  PHE B N   
1971 C CA  . PHE B 47  ? 0.14385 0.18152 0.14367 0.01236  -0.00384 -0.00031 47  PHE B CA  
1972 C C   . PHE B 47  ? 0.14912 0.17193 0.11242 0.00087  0.00444  0.00765  47  PHE B C   
1973 O O   . PHE B 47  ? 0.15409 0.18844 0.13435 0.00025  -0.00076 0.01074  47  PHE B O   
1974 C CB  . PHE B 47  ? 0.16600 0.17039 0.15243 0.00873  0.01286  -0.02522 47  PHE B CB  
1975 C CG  . PHE B 47  ? 0.14313 0.16898 0.13087 0.00828  0.00262  -0.01862 47  PHE B CG  
1976 C CD1 . PHE B 47  ? 0.14465 0.18403 0.15714 0.00951  0.00218  -0.01951 47  PHE B CD1 
1977 C CD2 . PHE B 47  ? 0.17146 0.18322 0.14775 0.03201  -0.00899 0.00302  47  PHE B CD2 
1978 C CE1 . PHE B 47  ? 0.16649 0.20942 0.17274 0.01265  0.00046  -0.01400 47  PHE B CE1 
1979 C CE2 . PHE B 47  ? 0.16450 0.21526 0.18089 0.01188  -0.01670 -0.02719 47  PHE B CE2 
1980 C CZ  . PHE B 47  ? 0.14688 0.22300 0.19679 -0.00005 -0.01122 -0.04818 47  PHE B CZ  
1981 N N   . VAL B 48  ? 0.12815 0.17973 0.12493 -0.00369 -0.00716 -0.00918 48  VAL B N   
1982 C CA  . VAL B 48  ? 0.13999 0.18225 0.12509 0.00531  -0.02214 -0.01622 48  VAL B CA  
1983 C C   . VAL B 48  ? 0.14356 0.16948 0.12705 0.00114  -0.00900 -0.00367 48  VAL B C   
1984 O O   . VAL B 48  ? 0.15123 0.19970 0.13098 0.00655  -0.02269 0.00111  48  VAL B O   
1985 C CB  . VAL B 48  ? 0.14207 0.17726 0.14013 0.00430  0.00641  -0.01583 48  VAL B CB  
1986 C CG1 . VAL B 48  ? 0.15078 0.20757 0.14203 0.02374  -0.01878 0.01259  48  VAL B CG1 
1987 C CG2 . VAL B 48  ? 0.17388 0.15590 0.16247 0.00493  -0.01641 -0.02166 48  VAL B CG2 
1988 N N   . SER B 49  ? 0.15108 0.16869 0.13419 -0.01330 -0.00250 -0.00539 49  SER B N   
1989 C CA  . SER B 49  ? 0.13465 0.18943 0.15362 -0.02998 -0.01561 -0.01395 49  SER B CA  
1990 C C   . SER B 49  ? 0.15961 0.16376 0.10985 0.00930  -0.01650 0.00067  49  SER B C   
1991 O O   . SER B 49  ? 0.16823 0.19786 0.12299 -0.01261 -0.02490 -0.00155 49  SER B O   
1992 C CB  . SER B 49  ? 0.13659 0.20611 0.14031 -0.02129 -0.00567 -0.01474 49  SER B CB  
1993 O OG  . SER B 49  ? 0.14296 0.22792 0.14899 -0.01653 -0.02580 -0.00436 49  SER B OG  
1994 N N   . SER B 50  ? 0.19354 0.14814 0.14220 -0.01057 -0.01431 -0.01547 50  SER B N   
1995 C CA  . SER B 50  ? 0.15579 0.17530 0.16076 -0.01944 -0.02443 -0.01876 50  SER B CA  
1996 C C   . SER B 50  ? 0.15828 0.18530 0.13372 -0.00604 -0.01201 0.00429  50  SER B C   
1997 O O   . SER B 50  ? 0.18516 0.19237 0.14439 -0.01227 -0.03214 0.00026  50  SER B O   
1998 C CB  . SER B 50  ? 0.18684 0.19301 0.16816 0.00369  0.00486  -0.01884 50  SER B CB  
1999 O OG  . SER B 50  ? 0.17204 0.22935 0.17752 -0.00822 0.00129  -0.01612 50  SER B OG  
2000 N N   . ILE B 51  ? 0.16252 0.18017 0.14281 -0.04505 -0.01605 -0.00166 51  ILE B N   
2001 C CA  . ILE B 51  ? 0.16505 0.18967 0.17341 -0.01254 -0.02005 -0.00373 51  ILE B CA  
2002 C C   . ILE B 51  ? 0.19515 0.18690 0.14901 -0.03484 -0.03792 -0.00708 51  ILE B C   
2003 O O   . ILE B 51  ? 0.22551 0.19257 0.16017 -0.03605 -0.03397 -0.00428 51  ILE B O   
2004 C CB  . ILE B 51  ? 0.15555 0.23336 0.16562 -0.04703 -0.01621 -0.02235 51  ILE B CB  
2005 C CG1 . ILE B 51  ? 0.16860 0.27437 0.20944 -0.03751 -0.01084 -0.01969 51  ILE B CG1 
2006 C CG2 . ILE B 51  ? 0.18168 0.27999 0.16128 -0.02817 0.00478  -0.00897 51  ILE B CG2 
2007 C CD1 . ILE B 51  ? 0.18371 0.29772 0.27341 -0.03548 0.01251  -0.00034 51  ILE B CD1 
2008 N N   . SER B 52  ? 0.21749 0.18473 0.15392 -0.04151 -0.02758 -0.01629 52  SER B N   
2009 C CA  . SER B 52  ? 0.25482 0.18812 0.23666 -0.04034 -0.05601 -0.00763 52  SER B CA  
2010 C C   . SER B 52  ? 0.29607 0.25375 0.25245 -0.04054 -0.06473 -0.06674 52  SER B C   
2011 O O   . SER B 52  ? 0.27495 0.25456 0.23252 -0.07312 -0.06223 -0.04145 52  SER B O   
2012 C CB  . SER B 52  ? 0.24395 0.20949 0.35162 -0.04369 -0.07525 0.01264  52  SER B CB  
2013 O OG  . SER B 52  ? 0.33577 0.24511 0.34846 0.00885  -0.06761 -0.01711 52  SER B OG  
2014 N N   . ASP B 53  ? 0.36061 0.38787 0.40981 -0.06879 -0.02644 0.00131  53  ASP B N   
2015 C CA  . ASP B 53  ? 0.46481 0.54634 0.57319 -0.00554 -0.02217 0.00755  53  ASP B CA  
2016 C C   . ASP B 53  ? 0.46854 0.55691 0.60384 -0.01715 0.01047  0.02854  53  ASP B C   
2017 O O   . ASP B 53  ? 0.45829 0.50941 0.57170 -0.06616 -0.01301 0.01377  53  ASP B O   
2018 C CB  . ASP B 53  ? 0.55570 0.61164 0.66845 0.00417  -0.02610 -0.01231 53  ASP B CB  
2019 C CG  . ASP B 53  ? 0.62243 0.66457 0.72572 0.01460  -0.01089 -0.00021 53  ASP B CG  
2020 O OD1 . ASP B 53  ? 0.63830 0.66604 0.73359 0.00568  -0.01154 -0.00355 53  ASP B OD1 
2021 O OD2 . ASP B 53  ? 0.63509 0.66552 0.73935 -0.00511 0.00520  0.00180  53  ASP B OD2 
2022 N N   . GLY B 54  ? 0.41954 0.52121 0.54633 -0.05066 0.02835  0.03463  54  GLY B N   
2023 C CA  . GLY B 54  ? 0.40700 0.50015 0.51094 -0.02420 0.01342  0.01824  54  GLY B CA  
2024 C C   . GLY B 54  ? 0.35679 0.42884 0.45670 -0.06600 -0.02891 0.00022  54  GLY B C   
2025 O O   . GLY B 54  ? 0.34840 0.46324 0.50291 -0.01882 -0.01824 0.01272  54  GLY B O   
2026 N N   . SER B 55  ? 0.30990 0.30337 0.27939 -0.12195 -0.03491 -0.01079 55  SER B N   
2027 C CA  . SER B 55  ? 0.28804 0.26187 0.25042 -0.10281 -0.04509 0.00414  55  SER B CA  
2028 C C   . SER B 55  ? 0.24846 0.22136 0.19993 -0.05354 -0.03885 -0.01722 55  SER B C   
2029 O O   . SER B 55  ? 0.28412 0.24245 0.20222 -0.01878 -0.06380 -0.02221 55  SER B O   
2030 C CB  . SER B 55  ? 0.34350 0.28039 0.33859 -0.05395 -0.04329 -0.08519 55  SER B CB  
2031 O OG  . SER B 55  ? 0.40498 0.36556 0.40945 -0.01243 -0.06969 -0.07148 55  SER B OG  
2032 N N   . THR B 56  ? 0.21529 0.23142 0.16623 -0.04040 -0.03764 -0.02937 56  THR B N   
2033 C CA  . THR B 56  ? 0.19778 0.21309 0.16334 -0.03850 -0.02804 -0.02448 56  THR B CA  
2034 C C   . THR B 56  ? 0.17984 0.24550 0.16446 -0.01792 -0.04874 -0.01868 56  THR B C   
2035 O O   . THR B 56  ? 0.18569 0.27558 0.16098 -0.03352 -0.03270 -0.03188 56  THR B O   
2036 C CB  . THR B 56  ? 0.19134 0.26175 0.15782 -0.00359 -0.00523 -0.01029 56  THR B CB  
2037 O OG1 . THR B 56  ? 0.19549 0.28510 0.19050 -0.02172 -0.03554 -0.01929 56  THR B OG1 
2038 C CG2 . THR B 56  ? 0.19142 0.26856 0.19500 -0.03192 0.01254  -0.02967 56  THR B CG2 
2039 N N   . ASN B 57  ? 0.14055 0.21418 0.14872 -0.01376 -0.02124 -0.01698 57  ASN B N   
2040 C CA  . ASN B 57  ? 0.14509 0.20297 0.14294 -0.02165 -0.01466 0.00711  57  ASN B CA  
2041 C C   . ASN B 57  ? 0.16113 0.20675 0.12995 -0.00246 -0.05529 -0.01010 57  ASN B C   
2042 O O   . ASN B 57  ? 0.15283 0.20747 0.13009 -0.00757 -0.02659 0.00494  57  ASN B O   
2043 C CB  . ASN B 57  ? 0.16518 0.23347 0.18815 0.02309  -0.03041 -0.02299 57  ASN B CB  
2044 C CG  . ASN B 57  ? 0.16068 0.22851 0.17061 -0.02218 -0.02397 -0.01105 57  ASN B CG  
2045 O OD1 . ASN B 57  ? 0.18517 0.23147 0.16753 0.00436  -0.04008 -0.01178 57  ASN B OD1 
2046 N ND2 . ASN B 57  ? 0.18484 0.23715 0.18340 0.01138  -0.01046 -0.02944 57  ASN B ND2 
2047 N N   . TYR B 58  ? 0.17097 0.18055 0.13699 -0.00444 -0.02431 0.01402  58  TYR B N   
2048 C CA  . TYR B 58  ? 0.14837 0.19551 0.14117 -0.01038 -0.01240 -0.00193 58  TYR B CA  
2049 C C   . TYR B 58  ? 0.16528 0.20116 0.12758 0.00044  -0.01203 0.00700  58  TYR B C   
2050 O O   . TYR B 58  ? 0.17324 0.22756 0.13213 0.00509  -0.00141 -0.00037 58  TYR B O   
2051 C CB  . TYR B 58  ? 0.14800 0.25010 0.15427 0.00839  -0.04346 0.01351  58  TYR B CB  
2052 C CG  . TYR B 58  ? 0.15301 0.22210 0.14616 0.01264  -0.02358 0.00631  58  TYR B CG  
2053 C CD1 . TYR B 58  ? 0.13745 0.22069 0.14664 0.00380  -0.01906 0.00287  58  TYR B CD1 
2054 C CD2 . TYR B 58  ? 0.16418 0.24631 0.16712 0.00056  -0.05641 -0.02651 58  TYR B CD2 
2055 C CE1 . TYR B 58  ? 0.16519 0.22654 0.15007 -0.01193 -0.02870 0.00281  58  TYR B CE1 
2056 C CE2 . TYR B 58  ? 0.16762 0.25592 0.15229 -0.00317 -0.02302 0.00590  58  TYR B CE2 
2057 C CZ  . TYR B 58  ? 0.17361 0.23290 0.15627 -0.00528 -0.02807 0.00453  58  TYR B CZ  
2058 O OH  . TYR B 58  ? 0.17379 0.27051 0.16659 -0.01154 -0.01182 -0.01099 58  TYR B OH  
2059 N N   . ALA B 59  ? 0.16547 0.20573 0.12950 0.01477  -0.02781 0.00179  59  ALA B N   
2060 C CA  . ALA B 59  ? 0.16779 0.20014 0.14024 -0.02076 -0.03123 0.02141  59  ALA B CA  
2061 C C   . ALA B 59  ? 0.17000 0.20474 0.13605 0.00192  -0.03006 -0.02152 59  ALA B C   
2062 O O   . ALA B 59  ? 0.18679 0.19331 0.14742 0.01016  -0.02739 -0.00055 59  ALA B O   
2063 C CB  . ALA B 59  ? 0.17052 0.21776 0.14953 -0.01326 -0.01662 0.00656  59  ALA B CB  
2064 N N   . GLY B 60  ? 0.19907 0.23262 0.12454 0.01590  -0.00574 0.01354  60  GLY B N   
2065 C CA  . GLY B 60  ? 0.24691 0.22236 0.13567 0.04338  -0.00912 0.02471  60  GLY B CA  
2066 C C   . GLY B 60  ? 0.20721 0.23176 0.14349 0.00766  -0.01385 0.01146  60  GLY B C   
2067 O O   . GLY B 60  ? 0.22253 0.24872 0.17406 0.00993  -0.01694 0.02425  60  GLY B O   
2068 N N   . SER B 61  ? 0.20731 0.20345 0.14066 -0.00105 0.00525  0.01063  61  SER B N   
2069 C CA  . SER B 61  ? 0.22112 0.23993 0.18510 -0.01479 0.01058  -0.01102 61  SER B CA  
2070 C C   . SER B 61  ? 0.23810 0.24231 0.15707 0.03053  -0.01467 0.02057  61  SER B C   
2071 O O   . SER B 61  ? 0.22442 0.22316 0.18643 0.01204  0.00876  0.02040  61  SER B O   
2072 C CB  . SER B 61  ? 0.27601 0.31425 0.25518 -0.03160 0.00750  -0.03046 61  SER B CB  
2073 O OG  . SER B 61  ? 0.25021 0.42252 0.21926 -0.03953 -0.00533 -0.06444 61  SER B OG  
2074 N N   . VAL B 62  ? 0.21160 0.24699 0.10802 -0.04086 -0.01417 0.03134  62  VAL B N   
2075 C CA  . VAL B 62  ? 0.48646 0.43180 0.18967 0.00543  -0.03332 0.13683  62  VAL B CA  
2076 C C   . VAL B 62  ? 1.21639 1.15929 0.91919 0.31422  -0.08993 0.05980  62  VAL B C   
2077 O O   . VAL B 62  ? 0.81560 0.72918 0.28131 -0.08029 -0.17590 -0.02287 62  VAL B O   
2078 C CB  . VAL B 62  ? 0.20367 0.25839 0.12214 -0.03695 -0.02765 0.02384  62  VAL B CB  
2079 C CG1 . VAL B 62  ? 0.18560 0.22496 0.19269 -0.02289 -0.03461 0.02484  62  VAL B CG1 
2080 C CG2 . VAL B 62  ? 0.21454 0.18057 0.14809 0.01786  -0.02026 0.02609  62  VAL B CG2 
2081 N N   . LYS B 63  ? 2.20648 2.26391 2.21882 1.03438  -0.04607 0.03018  63  LYS B N   
2082 C CA  . LYS B 63  ? 2.35478 2.41549 2.41940 0.75592  -0.03386 0.01231  63  LYS B CA  
2083 C C   . LYS B 63  ? 2.22961 2.29666 2.26769 0.69650  -0.03138 0.00264  63  LYS B C   
2084 O O   . LYS B 63  ? 2.35886 2.40433 2.45516 0.69512  -0.02994 0.00314  63  LYS B O   
2085 C CB  . LYS B 63  ? 2.48869 2.49053 2.55145 0.44719  -0.03318 0.00725  63  LYS B CB  
2086 C CG  . LYS B 63  ? 2.55988 2.55910 2.60576 0.22201  -0.03258 0.00445  63  LYS B CG  
2087 C CD  . LYS B 63  ? 2.59815 2.62453 2.63163 0.09761  -0.03277 0.00144  63  LYS B CD  
2088 C CE  . LYS B 63  ? 2.61778 2.67351 2.64699 0.04376  -0.03314 -0.00169 63  LYS B CE  
2089 N NZ  . LYS B 63  ? 2.62560 2.69476 2.65475 0.02712  -0.03339 -0.00448 63  LYS B NZ  
2090 N N   . GLY B 64  ? 1.65427 1.59602 1.41166 0.28580  -0.03358 -0.00760 64  GLY B N   
2091 C CA  . GLY B 64  ? 1.04789 0.98137 0.71412 -0.02372 -0.02719 -0.01473 64  GLY B CA  
2092 C C   . GLY B 64  ? 0.49745 0.53373 0.31448 -0.11417 -0.00877 -0.00920 64  GLY B C   
2093 O O   . GLY B 64  ? 0.32480 0.50047 0.28094 -0.05747 -0.05479 -0.10490 64  GLY B O   
2094 N N   . ARG B 65  ? 0.26571 0.30738 0.16113 -0.05361 -0.04087 0.04493  65  ARG B N   
2095 C CA  . ARG B 65  ? 0.21768 0.26353 0.16286 0.00448  -0.00480 0.01668  65  ARG B CA  
2096 C C   . ARG B 65  ? 0.17675 0.25556 0.18917 0.01852  -0.03085 0.00668  65  ARG B C   
2097 O O   . ARG B 65  ? 0.17351 0.23907 0.19354 0.02945  -0.01683 0.01911  65  ARG B O   
2098 C CB  . ARG B 65  ? 0.22592 0.24754 0.15754 0.01185  -0.04047 0.04424  65  ARG B CB  
2099 C CG  . ARG B 65  ? 0.24643 0.26319 0.21331 0.00365  -0.04686 0.01453  65  ARG B CG  
2100 C CD  . ARG B 65  ? 0.24769 0.24143 0.19729 0.00854  -0.06276 0.01752  65  ARG B CD  
2101 N NE  . ARG B 65  ? 0.25039 0.22749 0.17328 0.03499  -0.04506 0.02173  65  ARG B NE  
2102 C CZ  . ARG B 65  ? 0.25381 0.20478 0.15578 0.02899  -0.05132 0.01731  65  ARG B CZ  
2103 N NH1 . ARG B 65  ? 0.25769 0.22589 0.17350 0.03103  -0.01670 -0.00478 65  ARG B NH1 
2104 N NH2 . ARG B 65  ? 0.22906 0.20376 0.17890 0.02087  -0.03731 0.02399  65  ARG B NH2 
2105 N N   . PHE B 66  ? 0.17592 0.22018 0.18499 0.01204  -0.01716 0.01920  66  PHE B N   
2106 C CA  . PHE B 66  ? 0.17654 0.20470 0.16142 -0.00644 -0.01750 0.03617  66  PHE B CA  
2107 C C   . PHE B 66  ? 0.20338 0.23710 0.16767 0.03352  -0.01140 0.01867  66  PHE B C   
2108 O O   . PHE B 66  ? 0.27457 0.22902 0.19132 0.01668  0.01205  0.01144  66  PHE B O   
2109 C CB  . PHE B 66  ? 0.18888 0.21633 0.19716 0.01803  -0.01329 -0.00443 66  PHE B CB  
2110 C CG  . PHE B 66  ? 0.16943 0.22884 0.15736 0.01857  -0.00252 0.00865  66  PHE B CG  
2111 C CD1 . PHE B 66  ? 0.17987 0.20651 0.18847 -0.00174 -0.00519 0.01903  66  PHE B CD1 
2112 C CD2 . PHE B 66  ? 0.15758 0.27501 0.14004 0.02572  -0.00221 0.01759  66  PHE B CD2 
2113 C CE1 . PHE B 66  ? 0.20099 0.23009 0.18681 0.02603  -0.01017 0.02766  66  PHE B CE1 
2114 C CE2 . PHE B 66  ? 0.18772 0.25999 0.16827 0.00407  -0.03168 0.00306  66  PHE B CE2 
2115 C CZ  . PHE B 66  ? 0.17896 0.24387 0.20033 0.00334  -0.02495 0.03704  66  PHE B CZ  
2116 N N   . THR B 67  ? 0.14889 0.22611 0.16148 -0.00296 -0.02950 0.00650  67  THR B N   
2117 C CA  . THR B 67  ? 0.16917 0.24072 0.18751 -0.01847 -0.03438 0.00297  67  THR B CA  
2118 C C   . THR B 67  ? 0.17416 0.21353 0.14537 -0.01815 -0.02581 0.00472  67  THR B C   
2119 O O   . THR B 67  ? 0.18088 0.21924 0.17450 -0.01198 -0.01909 -0.00743 67  THR B O   
2120 C CB  . THR B 67  ? 0.19566 0.23986 0.23062 -0.01954 -0.07928 0.01727  67  THR B CB  
2121 O OG1 . THR B 67  ? 0.21332 0.30397 0.22897 -0.00610 -0.08170 0.02570  67  THR B OG1 
2122 C CG2 . THR B 67  ? 0.20160 0.27373 0.26669 -0.02195 -0.07275 0.01000  67  THR B CG2 
2123 N N   . ILE B 68  ? 0.15496 0.22057 0.15938 -0.03257 -0.00412 0.00239  68  ILE B N   
2124 C CA  . ILE B 68  ? 0.16245 0.19425 0.16952 -0.03350 -0.02243 0.01686  68  ILE B CA  
2125 C C   . ILE B 68  ? 0.17091 0.24239 0.14857 -0.02599 -0.02990 -0.00370 68  ILE B C   
2126 O O   . ILE B 68  ? 0.19171 0.26556 0.15558 -0.04407 -0.03964 -0.00303 68  ILE B O   
2127 C CB  . ILE B 68  ? 0.17952 0.20297 0.14365 -0.01368 -0.01420 -0.01687 68  ILE B CB  
2128 C CG1 . ILE B 68  ? 0.15895 0.23535 0.15403 -0.01304 -0.01395 0.00336  68  ILE B CG1 
2129 C CG2 . ILE B 68  ? 0.19371 0.23104 0.14149 -0.01123 -0.01139 -0.00707 68  ILE B CG2 
2130 C CD1 . ILE B 68  ? 0.15900 0.22154 0.16169 -0.00705 0.00238  -0.00376 68  ILE B CD1 
2131 N N   . SER B 69  ? 0.16304 0.24359 0.14926 -0.04657 -0.01634 0.02327  69  SER B N   
2132 C CA  . SER B 69  ? 0.16652 0.27236 0.19146 -0.06997 -0.02124 0.01775  69  SER B CA  
2133 C C   . SER B 69  ? 0.20884 0.27487 0.17304 -0.07560 -0.02287 0.01837  69  SER B C   
2134 O O   . SER B 69  ? 0.20173 0.23060 0.15402 -0.04324 -0.01083 -0.00446 69  SER B O   
2135 C CB  . SER B 69  ? 0.16873 0.30083 0.23588 -0.06995 -0.01177 0.00437  69  SER B CB  
2136 O OG  . SER B 69  ? 0.19400 0.31018 0.21712 -0.02211 0.01262  0.01859  69  SER B OG  
2137 N N   . GLN B 70  ? 0.26730 0.27699 0.23037 -0.10411 -0.05331 0.05757  70  GLN B N   
2138 C CA  . GLN B 70  ? 0.33423 0.41306 0.34784 -0.12353 -0.00201 0.06723  70  GLN B CA  
2139 C C   . GLN B 70  ? 0.53151 0.62051 0.60015 -0.00420 0.00558  0.03997  70  GLN B C   
2140 O O   . GLN B 70  ? 0.40301 0.49166 0.38805 -0.19080 -0.00659 0.06948  70  GLN B O   
2141 C CB  . GLN B 70  ? 0.36868 0.42641 0.38152 -0.05497 0.00195  0.08881  70  GLN B CB  
2142 C CG  . GLN B 70  ? 0.37471 0.42229 0.39571 -0.05355 -0.01929 0.02264  70  GLN B CG  
2143 C CD  . GLN B 70  ? 0.36852 0.43005 0.39883 -0.05385 0.00037  0.00214  70  GLN B CD  
2144 O OE1 . GLN B 70  ? 0.33895 0.39157 0.38311 -0.08478 0.00144  -0.02262 70  GLN B OE1 
2145 N NE2 . GLN B 70  ? 0.39324 0.44148 0.40459 -0.02662 -0.00163 -0.03034 70  GLN B NE2 
2146 N N   A ASP B 71  ? 0.64820 0.76816 0.75091 0.05382  0.00410  0.01776  71  ASP B N   
2147 N N   B ASP B 71  ? 0.64898 0.76996 0.75171 0.05269  0.00522  0.01608  71  ASP B N   
2148 C CA  A ASP B 71  ? 0.74575 0.85017 0.85891 0.05982  0.01069  0.01577  71  ASP B CA  
2149 C CA  B ASP B 71  ? 0.74626 0.85416 0.86031 0.05977  0.01147  0.01477  71  ASP B CA  
2150 C C   A ASP B 71  ? 0.80543 0.89653 0.90427 0.02478  0.02539  0.01484  71  ASP B C   
2151 C C   B ASP B 71  ? 0.80465 0.89922 0.91149 0.02507  0.02729  0.01644  71  ASP B C   
2152 O O   A ASP B 71  ? 0.81113 0.89648 0.90994 0.00463  0.03263  0.00945  71  ASP B O   
2153 O O   B ASP B 71  ? 0.81428 0.89760 0.91311 0.00601  0.03434  0.01398  71  ASP B O   
2154 C CB  A ASP B 71  ? 0.76333 0.85377 0.87439 0.03226  0.00944  0.01679  71  ASP B CB  
2155 C CB  B ASP B 71  ? 0.76370 0.85576 0.87548 0.03248  0.00856  0.01708  71  ASP B CB  
2156 C CG  A ASP B 71  ? 0.76122 0.85993 0.86511 -0.00322 0.01240  0.02022  71  ASP B CG  
2157 C CG  B ASP B 71  ? 0.76163 0.86043 0.86555 -0.00320 0.01148  0.01908  71  ASP B CG  
2158 O OD1 A ASP B 71  ? 0.75493 0.86186 0.87206 -0.00784 0.01303  0.01832  71  ASP B OD1 
2159 O OD1 B ASP B 71  ? 0.75420 0.86274 0.87299 -0.00800 0.01146  0.01816  71  ASP B OD1 
2160 O OD2 A ASP B 71  ? 0.75459 0.85114 0.84752 -0.03236 0.02178  0.03088  71  ASP B OD2 
2161 O OD2 B ASP B 71  ? 0.75736 0.85296 0.84676 -0.03245 0.02143  0.02827  71  ASP B OD2 
2162 N N   A ASN B 72  ? 0.83430 0.92054 0.92438 0.01377  0.02189  0.01665  72  ASN B N   
2163 N N   B ASN B 72  ? 0.83121 0.91986 0.92586 0.00611  0.02671  0.01273  72  ASN B N   
2164 C CA  A ASN B 72  ? 0.85044 0.93914 0.93881 0.01330  0.01961  0.01611  72  ASN B CA  
2165 C CA  B ASN B 72  ? 0.85097 0.94211 0.94017 0.01359  0.02271  0.01514  72  ASN B CA  
2166 C C   A ASN B 72  ? 0.82424 0.93685 0.93425 0.02867  0.02509  0.02406  72  ASN B C   
2167 C C   B ASN B 72  ? 0.82937 0.93687 0.93716 0.03051  0.02376  0.02187  72  ASN B C   
2168 O O   A ASN B 72  ? 0.85161 0.99050 0.99345 0.08075  0.02557  0.02452  72  ASN B O   
2169 O O   B ASN B 72  ? 0.85254 0.98808 0.99511 0.08235  0.02880  0.02379  72  ASN B O   
2170 C CB  A ASN B 72  ? 0.88431 0.96775 0.95677 0.00436  0.01753  0.01358  72  ASN B CB  
2171 C CB  B ASN B 72  ? 0.88189 0.96716 0.95680 0.00463  0.01739  0.01333  72  ASN B CB  
2172 C CG  A ASN B 72  ? 0.90796 1.00141 0.98889 0.01130  0.01316  0.01207  72  ASN B CG  
2173 C CG  B ASN B 72  ? 0.90640 1.00098 0.98777 0.01145  0.01718  0.00978  72  ASN B CG  
2174 O OD1 A ASN B 72  ? 0.91576 1.01447 1.00889 0.01636  0.01311  0.01290  72  ASN B OD1 
2175 O OD1 B ASN B 72  ? 0.91399 1.01171 1.00566 0.02046  0.01954  0.01224  72  ASN B OD1 
2176 N ND2 A ASN B 72  ? 0.91628 1.01197 0.99742 0.01829  0.00978  0.00874  72  ASN B ND2 
2177 N ND2 B ASN B 72  ? 0.91489 1.01218 0.99599 0.01401  0.01381  0.00682  72  ASN B ND2 
2178 N N   A ALA B 73  ? 0.75884 0.85094 0.84451 -0.01871 0.02946  0.02916  73  ALA B N   
2179 N N   B ALA B 73  ? 0.76366 0.85310 0.84805 -0.02116 0.02559  0.02667  73  ALA B N   
2180 C CA  A ALA B 73  ? 0.69952 0.78518 0.77006 -0.04630 0.03094  0.02658  73  ALA B CA  
2181 C CA  B ALA B 73  ? 0.70004 0.78519 0.77211 -0.05105 0.02559  0.02624  73  ALA B CA  
2182 C C   A ALA B 73  ? 0.65884 0.75966 0.74659 -0.02687 0.03457  0.03230  73  ALA B C   
2183 C C   B ALA B 73  ? 0.66687 0.76425 0.75159 -0.01321 0.04010  0.03129  73  ALA B C   
2184 O O   A ALA B 73  ? 0.65064 0.75002 0.73976 -0.03164 0.04603  0.04600  73  ALA B O   
2185 O O   B ALA B 73  ? 0.66124 0.75214 0.75297 -0.02324 0.05735  0.03937  73  ALA B O   
2186 C CB  A ALA B 73  ? 0.68167 0.75879 0.73048 -0.08178 0.03014  0.02684  73  ALA B CB  
2187 C CB  B ALA B 73  ? 0.68655 0.76193 0.73877 -0.08306 0.02756  0.02618  73  ALA B CB  
2188 N N   A LYS B 74  ? 0.62398 0.73301 0.71745 0.00355  0.04440  0.04117  74  LYS B N   
2189 N N   B LYS B 74  ? 0.62028 0.72970 0.71822 0.00183  0.04610  0.03943  74  LYS B N   
2190 C CA  A LYS B 74  ? 0.58060 0.69419 0.68024 0.01565  0.03765  0.03978  74  LYS B CA  
2191 C CA  B LYS B 74  ? 0.58178 0.70053 0.68576 0.02289  0.04356  0.03747  74  LYS B CA  
2192 C C   A LYS B 74  ? 0.47544 0.57156 0.57607 -0.01211 0.04207  0.04957  74  LYS B C   
2193 C C   B LYS B 74  ? 0.47430 0.58609 0.57010 -0.00266 0.04328  0.06450  74  LYS B C   
2194 O O   A LYS B 74  ? 0.49138 0.61561 0.60680 0.02266  0.04807  0.03451  74  LYS B O   
2195 O O   B LYS B 74  ? 0.50043 0.62466 0.61588 0.05458  0.04028  0.04598  74  LYS B O   
2196 C CB  A LYS B 74  ? 0.63077 0.75256 0.72532 0.03077  0.03529  0.03074  74  LYS B CB  
2197 C CB  B LYS B 74  ? 0.63357 0.75026 0.72842 0.03005  0.03551  0.03236  74  LYS B CB  
2198 C CG  A LYS B 74  ? 0.67180 0.78415 0.75700 0.03099  0.03344  0.02893  74  LYS B CG  
2199 C CG  B LYS B 74  ? 0.67038 0.78548 0.75732 0.03046  0.03452  0.02917  74  LYS B CG  
2200 C CD  A LYS B 74  ? 0.69381 0.80414 0.77130 0.02131  0.03363  0.02467  74  LYS B CD  
2201 C CD  B LYS B 74  ? 0.69371 0.80440 0.77057 0.02024  0.03188  0.02314  74  LYS B CD  
2202 C CE  A LYS B 74  ? 0.70848 0.81500 0.77573 0.01318  0.03099  0.02244  74  LYS B CE  
2203 C CE  B LYS B 74  ? 0.70929 0.81490 0.77507 0.01500  0.03259  0.02311  74  LYS B CE  
2204 N NZ  A LYS B 74  ? 0.71553 0.81895 0.77669 0.01037  0.03273  0.02319  74  LYS B NZ  
2205 N NZ  B LYS B 74  ? 0.71552 0.81829 0.77748 0.01137  0.03141  0.02210  74  LYS B NZ  
2206 N N   . ASN B 75  ? 0.30744 0.32168 0.32367 -0.14053 0.04559  0.10491  75  ASN B N   
2207 C CA  . ASN B 75  ? 0.22642 0.25888 0.22872 -0.11259 -0.00513 0.05964  75  ASN B CA  
2208 C C   . ASN B 75  ? 0.18863 0.24326 0.16089 -0.06529 -0.03143 0.02175  75  ASN B C   
2209 O O   . ASN B 75  ? 0.17067 0.21489 0.18340 -0.05517 -0.01516 0.01611  75  ASN B O   
2210 C CB  . ASN B 75  ? 0.24821 0.26360 0.27827 -0.08619 -0.04569 0.07951  75  ASN B CB  
2211 C CG  . ASN B 75  ? 0.21939 0.28731 0.26826 -0.09201 -0.01680 0.05736  75  ASN B CG  
2212 O OD1 . ASN B 75  ? 0.26947 0.26654 0.26430 -0.03015 0.00390  0.03627  75  ASN B OD1 
2213 N ND2 . ASN B 75  ? 0.25629 0.28754 0.27327 -0.06532 0.01405  0.05884  75  ASN B ND2 
2214 N N   . THR B 76  ? 0.16859 0.23251 0.18190 -0.06770 0.00473  0.00134  76  THR B N   
2215 C CA  . THR B 76  ? 0.17781 0.20892 0.15957 -0.05179 0.00522  0.01778  76  THR B CA  
2216 C C   . THR B 76  ? 0.15965 0.20217 0.18725 -0.05695 -0.01165 0.00159  76  THR B C   
2217 O O   . THR B 76  ? 0.16821 0.24811 0.18941 -0.05730 -0.02118 0.01411  76  THR B O   
2218 C CB  . THR B 76  ? 0.20048 0.24057 0.16540 -0.01887 0.00433  0.00714  76  THR B CB  
2219 O OG1 . THR B 76  ? 0.21493 0.27833 0.18253 -0.05096 0.01450  0.00009  76  THR B OG1 
2220 C CG2 . THR B 76  ? 0.23381 0.19464 0.22212 -0.01838 0.02101  0.01325  76  THR B CG2 
2221 N N   . VAL B 77  ? 0.15135 0.18459 0.15950 -0.04515 -0.00005 0.00259  77  VAL B N   
2222 C CA  . VAL B 77  ? 0.15606 0.19587 0.15115 -0.01905 0.00145  0.00416  77  VAL B CA  
2223 C C   . VAL B 77  ? 0.15487 0.18902 0.15126 -0.04518 -0.01902 -0.00439 77  VAL B C   
2224 O O   . VAL B 77  ? 0.18506 0.20136 0.19066 -0.03437 -0.03430 0.00831  77  VAL B O   
2225 C CB  . VAL B 77  ? 0.16789 0.20436 0.17365 -0.02493 -0.00206 0.02076  77  VAL B CB  
2226 C CG1 . VAL B 77  ? 0.17793 0.25578 0.17187 -0.00504 -0.00902 0.02309  77  VAL B CG1 
2227 C CG2 . VAL B 77  ? 0.21400 0.17874 0.21511 -0.01635 0.01174  -0.01554 77  VAL B CG2 
2228 N N   . TYR B 78  ? 0.15915 0.19458 0.15160 -0.02599 0.01005  0.01348  78  TYR B N   
2229 C CA  . TYR B 78  ? 0.15872 0.19569 0.16174 -0.01882 0.00452  0.01276  78  TYR B CA  
2230 C C   . TYR B 78  ? 0.17381 0.20000 0.15862 -0.02235 -0.00810 0.00574  78  TYR B C   
2231 O O   . TYR B 78  ? 0.19374 0.21847 0.15681 -0.01372 0.00588  -0.00824 78  TYR B O   
2232 C CB  . TYR B 78  ? 0.14879 0.23634 0.22516 -0.01181 0.00050  0.02432  78  TYR B CB  
2233 C CG  . TYR B 78  ? 0.14421 0.25528 0.22171 -0.01035 0.01696  -0.00071 78  TYR B CG  
2234 C CD1 . TYR B 78  ? 0.17231 0.26271 0.20754 -0.01657 0.01250  0.01005  78  TYR B CD1 
2235 C CD2 . TYR B 78  ? 0.17564 0.25928 0.28681 -0.04020 0.02852  0.00366  78  TYR B CD2 
2236 C CE1 . TYR B 78  ? 0.17445 0.29379 0.24837 -0.03117 0.01673  0.02220  78  TYR B CE1 
2237 C CE2 . TYR B 78  ? 0.20424 0.31663 0.29320 -0.04137 0.05884  0.01442  78  TYR B CE2 
2238 C CZ  . TYR B 78  ? 0.20009 0.32560 0.26589 -0.05560 0.04266  0.02768  78  TYR B CZ  
2239 O OH  . TYR B 78  ? 0.24812 0.38773 0.28420 -0.07156 0.05609  0.04037  78  TYR B OH  
2240 N N   . LEU B 79  ? 0.15698 0.21253 0.16114 -0.01950 -0.01227 0.01523  79  LEU B N   
2241 C CA  . LEU B 79  ? 0.15260 0.22328 0.15715 -0.00011 0.00088  0.02197  79  LEU B CA  
2242 C C   . LEU B 79  ? 0.14922 0.19791 0.16734 -0.00911 -0.00938 -0.00702 79  LEU B C   
2243 O O   . LEU B 79  ? 0.17230 0.21273 0.15747 -0.00674 -0.01283 0.01328  79  LEU B O   
2244 C CB  . LEU B 79  ? 0.13755 0.20884 0.17025 -0.00878 0.00589  0.03764  79  LEU B CB  
2245 C CG  . LEU B 79  ? 0.16226 0.21518 0.14411 0.00277  -0.00575 -0.00427 79  LEU B CG  
2246 C CD1 . LEU B 79  ? 0.18979 0.24734 0.16606 0.02914  -0.01323 0.02461  79  LEU B CD1 
2247 C CD2 . LEU B 79  ? 0.14414 0.26405 0.19224 -0.00235 -0.00918 0.03303  79  LEU B CD2 
2248 N N   . GLN B 80  ? 0.14226 0.21081 0.17340 -0.00882 -0.02611 0.01791  80  GLN B N   
2249 C CA  . GLN B 80  ? 0.15029 0.23446 0.17612 -0.01401 -0.03647 0.02636  80  GLN B CA  
2250 C C   . GLN B 80  ? 0.18594 0.23476 0.17775 0.00214  -0.00268 0.00441  80  GLN B C   
2251 O O   . GLN B 80  ? 0.30475 0.22959 0.17836 -0.01565 0.00668  -0.00443 80  GLN B O   
2252 C CB  . GLN B 80  ? 0.19592 0.28806 0.20928 0.00583  -0.05514 0.00990  80  GLN B CB  
2253 C CG  . GLN B 80  ? 0.20310 0.29496 0.23109 0.03550  -0.05167 -0.00339 80  GLN B CG  
2254 C CD  . GLN B 80  ? 0.17308 0.31068 0.25664 0.01596  -0.04564 0.02358  80  GLN B CD  
2255 O OE1 . GLN B 80  ? 0.17361 0.33560 0.26874 0.04055  0.00104  0.03262  80  GLN B OE1 
2256 N NE2 . GLN B 80  ? 0.24565 0.29310 0.28796 0.05510  -0.01546 0.01144  80  GLN B NE2 
2257 N N   . MET B 81  ? 0.18206 0.21266 0.19075 0.01513  -0.01857 -0.00033 81  MET B N   
2258 C CA  . MET B 81  ? 0.15864 0.21169 0.19873 0.02328  -0.01035 0.03566  81  MET B CA  
2259 C C   . MET B 81  ? 0.18413 0.21685 0.20338 0.02116  -0.02333 0.02936  81  MET B C   
2260 O O   . MET B 81  ? 0.25759 0.26893 0.22202 0.08656  -0.02390 -0.00988 81  MET B O   
2261 C CB  . MET B 81  ? 0.17049 0.21673 0.25499 0.01210  -0.05713 0.02372  81  MET B CB  
2262 C CG  . MET B 81  ? 0.17506 0.22990 0.26573 -0.01258 -0.09249 0.02441  81  MET B CG  
2263 S SD  . MET B 81  ? 0.25361 0.29897 0.41841 0.03416  -0.12125 -0.01536 81  MET B SD  
2264 C CE  . MET B 81  ? 0.15285 0.41524 0.14561 -0.04575 -0.02058 0.09654  81  MET B CE  
2265 N N   . ASN B 82  ? 0.18148 0.25650 0.18903 0.03992  -0.04963 0.02340  82  ASN B N   
2266 C CA  . ASN B 82  ? 0.20758 0.26712 0.21655 0.05276  -0.03235 0.03168  82  ASN B CA  
2267 C C   . ASN B 82  ? 0.22605 0.25514 0.22213 0.04100  -0.03695 0.03000  82  ASN B C   
2268 O O   . ASN B 82  ? 0.22944 0.27256 0.22547 0.05235  -0.03460 0.00754  82  ASN B O   
2269 C CB  . ASN B 82  ? 0.20875 0.29910 0.22068 0.02909  -0.07783 0.00227  82  ASN B CB  
2270 C CG  . ASN B 82  ? 0.22681 0.30753 0.26143 0.04005  -0.06798 -0.01107 82  ASN B CG  
2271 O OD1 . ASN B 82  ? 0.22081 0.34663 0.26892 0.03143  -0.03038 -0.00340 82  ASN B OD1 
2272 N ND2 . ASN B 82  ? 0.26449 0.32707 0.32450 0.01992  -0.06399 0.00829  82  ASN B ND2 
2273 N N   . SER B 83  ? 0.20836 0.23666 0.24405 0.04501  -0.03015 0.02974  83  SER B N   
2274 C CA  . SER B 83  ? 0.24950 0.28105 0.23562 0.04896  -0.05468 0.01488  83  SER B CA  
2275 C C   . SER B 83  ? 0.24368 0.22355 0.23874 0.03877  -0.02021 0.00351  83  SER B C   
2276 O O   . SER B 83  ? 0.24749 0.23733 0.22322 0.04500  -0.03440 0.03889  83  SER B O   
2277 C CB  . SER B 83  ? 0.25891 0.30933 0.26177 0.01586  -0.08609 0.02550  83  SER B CB  
2278 O OG  . SER B 83  ? 0.28533 0.35501 0.28985 0.03161  -0.09463 0.03918  83  SER B OG  
2279 N N   . LEU B 84  ? 0.21140 0.24856 0.22006 0.03624  -0.04525 0.00944  84  LEU B N   
2280 C CA  . LEU B 84  ? 0.23385 0.23061 0.22600 0.02067  -0.02764 0.00595  84  LEU B CA  
2281 C C   . LEU B 84  ? 0.23780 0.23128 0.22747 0.02253  -0.04000 0.02623  84  LEU B C   
2282 O O   . LEU B 84  ? 0.25393 0.23302 0.27147 0.05266  -0.03461 0.03845  84  LEU B O   
2283 C CB  . LEU B 84  ? 0.26573 0.21267 0.19762 0.04845  0.00996  0.03384  84  LEU B CB  
2284 C CG  . LEU B 84  ? 0.25796 0.23658 0.26048 0.02809  -0.01132 0.02724  84  LEU B CG  
2285 C CD1 . LEU B 84  ? 0.29554 0.27092 0.21145 0.00160  -0.00897 0.04493  84  LEU B CD1 
2286 C CD2 . LEU B 84  ? 0.24850 0.21680 0.27655 0.04096  -0.00496 0.00790  84  LEU B CD2 
2287 N N   . LYS B 85  ? 0.24162 0.24123 0.18738 -0.00422 -0.01996 0.03123  85  LYS B N   
2288 C CA  . LYS B 85  ? 0.25936 0.26633 0.20769 -0.00697 -0.01507 0.05010  85  LYS B CA  
2289 C C   . LYS B 85  ? 0.25563 0.25737 0.19109 0.00913  -0.00975 0.02325  85  LYS B C   
2290 O O   . LYS B 85  ? 0.25673 0.23896 0.21786 0.01069  -0.02167 0.04618  85  LYS B O   
2291 C CB  . LYS B 85  ? 0.28914 0.31742 0.20624 -0.02656 -0.02456 0.00701  85  LYS B CB  
2292 C CG  . LYS B 85  ? 0.31536 0.34877 0.26095 -0.00109 -0.01723 -0.00838 85  LYS B CG  
2293 C CD  . LYS B 85  ? 0.34209 0.36463 0.31680 0.00912  -0.03724 0.01161  85  LYS B CD  
2294 C CE  . LYS B 85  ? 0.37702 0.38565 0.38745 0.02450  -0.01925 0.00346  85  LYS B CE  
2295 N NZ  . LYS B 85  ? 0.42566 0.39089 0.39838 0.02890  -0.02280 -0.00608 85  LYS B NZ  
2296 N N   . PRO B 86  ? 0.28340 0.26510 0.20638 0.02274  -0.03487 0.06562  86  PRO B N   
2297 C CA  . PRO B 86  ? 0.29060 0.26030 0.21659 -0.00352 -0.01863 0.05845  86  PRO B CA  
2298 C C   . PRO B 86  ? 0.27980 0.25206 0.20016 -0.01906 -0.04053 0.06889  86  PRO B C   
2299 O O   . PRO B 86  ? 0.30669 0.23149 0.21537 -0.04248 -0.06783 0.04648  86  PRO B O   
2300 C CB  . PRO B 86  ? 0.29114 0.25709 0.29620 -0.01561 -0.01946 0.07184  86  PRO B CB  
2301 C CG  . PRO B 86  ? 0.33000 0.27593 0.31491 0.01817  -0.05261 0.05975  86  PRO B CG  
2302 C CD  . PRO B 86  ? 0.32386 0.26511 0.28258 0.00863  -0.07016 0.06616  86  PRO B CD  
2303 N N   . GLU B 87  ? 0.28586 0.23960 0.19631 -0.01613 -0.02015 0.03047  87  GLU B N   
2304 C CA  . GLU B 87  ? 0.30122 0.28866 0.21816 0.01720  0.02640  0.07788  87  GLU B CA  
2305 C C   . GLU B 87  ? 0.24418 0.24140 0.19608 -0.02481 -0.02851 0.04150  87  GLU B C   
2306 O O   . GLU B 87  ? 0.24951 0.26922 0.21067 0.01215  -0.00752 0.03439  87  GLU B O   
2307 C CB  . GLU B 87  ? 0.32559 0.32130 0.28200 0.01066  0.04515  0.08581  87  GLU B CB  
2308 C CG  . GLU B 87  ? 0.37942 0.41076 0.35670 0.02158  -0.00952 0.02840  87  GLU B CG  
2309 C CD  . GLU B 87  ? 0.44097 0.43047 0.45104 0.02554  -0.00539 0.04664  87  GLU B CD  
2310 O OE1 . GLU B 87  ? 0.44611 0.40825 0.40559 0.05639  -0.00198 0.06991  87  GLU B OE1 
2311 O OE2 . GLU B 87  ? 0.47251 0.44149 0.44560 -0.00719 -0.02486 0.10056  87  GLU B OE2 
2312 N N   . ASP B 88  ? 0.24203 0.22430 0.15378 -0.01532 0.00098  0.02362  88  ASP B N   
2313 C CA  . ASP B 88  ? 0.23139 0.19461 0.15470 -0.03017 -0.01966 -0.00240 88  ASP B CA  
2314 C C   . ASP B 88  ? 0.21851 0.18584 0.16201 -0.00357 -0.00405 0.01199  88  ASP B C   
2315 O O   . ASP B 88  ? 0.21622 0.19619 0.16339 -0.01495 -0.02931 0.01266  88  ASP B O   
2316 C CB  . ASP B 88  ? 0.19472 0.24290 0.15699 -0.00888 -0.01957 0.00700  88  ASP B CB  
2317 C CG  . ASP B 88  ? 0.19691 0.22057 0.17778 -0.00413 -0.02615 0.04209  88  ASP B CG  
2318 O OD1 . ASP B 88  ? 0.20870 0.21959 0.17443 0.00898  -0.02481 0.01840  88  ASP B OD1 
2319 O OD2 . ASP B 88  ? 0.22909 0.21409 0.22728 0.01935  -0.06298 0.00714  88  ASP B OD2 
2320 N N   . THR B 89  ? 0.21262 0.18362 0.16033 -0.00940 -0.02290 0.00017  89  THR B N   
2321 C CA  . THR B 89  ? 0.21304 0.18904 0.15516 -0.02309 -0.02662 0.00142  89  THR B CA  
2322 C C   . THR B 89  ? 0.20463 0.19113 0.15040 -0.01383 -0.02645 0.01128  89  THR B C   
2323 O O   . THR B 89  ? 0.21464 0.18747 0.17703 -0.01701 -0.00823 0.01957  89  THR B O   
2324 C CB  . THR B 89  ? 0.21299 0.18216 0.20159 -0.01355 -0.01302 0.01284  89  THR B CB  
2325 O OG1 . THR B 89  ? 0.23955 0.19000 0.19812 0.00503  -0.02021 0.01292  89  THR B OG1 
2326 C CG2 . THR B 89  ? 0.24235 0.19302 0.18363 -0.03980 -0.04006 0.01137  89  THR B CG2 
2327 N N   . ALA B 90  ? 0.19205 0.17797 0.15593 0.00657  -0.01865 0.01098  90  ALA B N   
2328 C CA  . ALA B 90  ? 0.19520 0.16818 0.14816 -0.01297 -0.00882 0.02035  90  ALA B CA  
2329 C C   . ALA B 90  ? 0.18877 0.15731 0.13717 -0.00269 -0.00461 -0.00252 90  ALA B C   
2330 O O   . ALA B 90  ? 0.17753 0.18628 0.15692 -0.00057 -0.00659 0.00963  90  ALA B O   
2331 C CB  . ALA B 90  ? 0.21743 0.17705 0.15115 -0.00655 -0.01190 -0.01363 90  ALA B CB  
2332 N N   . VAL B 91  ? 0.18257 0.15193 0.12929 -0.00722 -0.01921 0.01318  91  VAL B N   
2333 C CA  . VAL B 91  ? 0.17862 0.15514 0.13026 -0.00007 -0.01675 0.00230  91  VAL B CA  
2334 C C   . VAL B 91  ? 0.17629 0.17911 0.11271 0.00068  -0.01243 -0.01997 91  VAL B C   
2335 O O   . VAL B 91  ? 0.17133 0.17457 0.13843 -0.01174 0.01397  -0.00962 91  VAL B O   
2336 C CB  . VAL B 91  ? 0.18373 0.18618 0.11458 -0.01331 -0.02658 -0.01878 91  VAL B CB  
2337 C CG1 . VAL B 91  ? 0.16700 0.19480 0.13901 -0.00738 -0.00788 0.01491  91  VAL B CG1 
2338 C CG2 . VAL B 91  ? 0.20607 0.20739 0.16362 -0.00960 -0.03505 -0.03069 91  VAL B CG2 
2339 N N   . TYR B 92  ? 0.13755 0.17245 0.13497 -0.00856 -0.00292 0.00206  92  TYR B N   
2340 C CA  . TYR B 92  ? 0.14266 0.15697 0.13305 -0.01294 -0.00915 0.00384  92  TYR B CA  
2341 C C   . TYR B 92  ? 0.14822 0.16009 0.12915 -0.00012 -0.00880 -0.02357 92  TYR B C   
2342 O O   . TYR B 92  ? 0.16497 0.17128 0.12999 0.00456  0.00974  -0.01032 92  TYR B O   
2343 C CB  . TYR B 92  ? 0.14905 0.16492 0.13947 0.01234  -0.02651 0.00948  92  TYR B CB  
2344 C CG  . TYR B 92  ? 0.14553 0.16421 0.15835 -0.02209 -0.00914 0.00273  92  TYR B CG  
2345 C CD1 . TYR B 92  ? 0.15021 0.18188 0.14519 -0.00125 -0.02580 0.01325  92  TYR B CD1 
2346 C CD2 . TYR B 92  ? 0.13616 0.19223 0.13549 -0.00162 -0.01939 0.01008  92  TYR B CD2 
2347 C CE1 . TYR B 92  ? 0.16596 0.18758 0.15176 0.01321  -0.01204 0.01193  92  TYR B CE1 
2348 C CE2 . TYR B 92  ? 0.16797 0.18189 0.15445 -0.01080 -0.02040 0.00022  92  TYR B CE2 
2349 C CZ  . TYR B 92  ? 0.16073 0.20803 0.13787 -0.00382 -0.00986 -0.00207 92  TYR B CZ  
2350 O OH  . TYR B 92  ? 0.18477 0.20307 0.14324 0.01209  -0.01714 0.02160  92  TYR B OH  
2351 N N   . TYR B 93  ? 0.14447 0.14909 0.13452 -0.00338 -0.00014 0.00307  93  TYR B N   
2352 C CA  . TYR B 93  ? 0.15337 0.15849 0.13795 -0.00080 0.00334  0.00166  93  TYR B CA  
2353 C C   . TYR B 93  ? 0.17099 0.17414 0.10817 -0.01292 0.01218  -0.00527 93  TYR B C   
2354 O O   . TYR B 93  ? 0.23363 0.18558 0.12031 -0.03334 0.00873  -0.00846 93  TYR B O   
2355 C CB  . TYR B 93  ? 0.15038 0.18529 0.16324 0.01358  -0.00709 -0.02407 93  TYR B CB  
2356 C CG  . TYR B 93  ? 0.15145 0.19701 0.15698 0.01668  0.00912  -0.00338 93  TYR B CG  
2357 C CD1 . TYR B 93  ? 0.14241 0.23560 0.17938 0.02114  -0.02911 -0.02031 93  TYR B CD1 
2358 C CD2 . TYR B 93  ? 0.16051 0.21165 0.19428 0.01536  0.01392  -0.01785 93  TYR B CD2 
2359 C CE1 . TYR B 93  ? 0.15234 0.25945 0.22261 0.03704  -0.02338 -0.06950 93  TYR B CE1 
2360 C CE2 . TYR B 93  ? 0.20244 0.21270 0.26671 0.00263  -0.00138 -0.06510 93  TYR B CE2 
2361 C CZ  . TYR B 93  ? 0.15549 0.23185 0.27304 -0.00914 -0.01821 -0.08506 93  TYR B CZ  
2362 O OH  . TYR B 93  ? 0.17838 0.27902 0.37361 0.02539  -0.07184 -0.14628 93  TYR B OH  
2363 N N   . CYS B 94  ? 0.17898 0.15977 0.13573 -0.00974 0.00992  0.00261  94  CYS B N   
2364 C CA  . CYS B 94  ? 0.15643 0.16704 0.14122 -0.01806 -0.00433 0.01468  94  CYS B CA  
2365 C C   . CYS B 94  ? 0.14630 0.17097 0.11114 -0.03078 -0.02373 0.00900  94  CYS B C   
2366 O O   . CYS B 94  ? 0.16409 0.18677 0.13915 -0.00911 -0.01249 -0.01272 94  CYS B O   
2367 C CB  . CYS B 94  ? 0.16945 0.22082 0.17178 0.00133  0.00233  0.00188  94  CYS B CB  
2368 S SG  . CYS B 94  ? 0.19132 0.20677 0.18131 -0.00526 0.00615  -0.01624 94  CYS B SG  
2369 N N   . ALA B 95  ? 0.19001 0.13727 0.13292 -0.02408 -0.01521 0.00121  95  ALA B N   
2370 C CA  . ALA B 95  ? 0.19380 0.16236 0.11768 -0.02741 -0.03221 0.00438  95  ALA B CA  
2371 C C   . ALA B 95  ? 0.17025 0.15961 0.11433 -0.03214 -0.01956 -0.00035 95  ALA B C   
2372 O O   . ALA B 95  ? 0.21053 0.17989 0.14511 -0.04712 -0.05232 0.00954  95  ALA B O   
2373 C CB  . ALA B 95  ? 0.16971 0.21410 0.17749 -0.04886 0.01874  0.00412  95  ALA B CB  
2374 N N   . ALA B 96  ? 0.16251 0.14539 0.12768 -0.02716 -0.00951 -0.00359 96  ALA B N   
2375 C CA  . ALA B 96  ? 0.18760 0.14894 0.15201 -0.01841 -0.02058 0.00128  96  ALA B CA  
2376 C C   . ALA B 96  ? 0.17074 0.15353 0.14274 -0.03051 -0.00987 0.00302  96  ALA B C   
2377 O O   . ALA B 96  ? 0.20616 0.16751 0.17620 -0.01352 -0.04935 -0.01176 96  ALA B O   
2378 C CB  . ALA B 96  ? 0.17155 0.17156 0.23236 -0.02933 0.00746  -0.00267 96  ALA B CB  
2379 N N   . THR B 97  ? 0.19673 0.14731 0.15026 -0.03305 0.00056  -0.01546 97  THR B N   
2380 C CA  . THR B 97  ? 0.17170 0.13926 0.15517 -0.02354 0.01515  0.00123  97  THR B CA  
2381 C C   . THR B 97  ? 0.17746 0.15233 0.14770 -0.02002 0.00176  -0.00150 97  THR B C   
2382 O O   . THR B 97  ? 0.18889 0.17218 0.17291 -0.03350 -0.01118 -0.00872 97  THR B O   
2383 C CB  . THR B 97  ? 0.18577 0.18114 0.16524 -0.02626 0.02727  -0.02374 97  THR B CB  
2384 O OG1 . THR B 97  ? 0.23056 0.20511 0.16160 -0.00452 -0.00536 -0.02637 97  THR B OG1 
2385 C CG2 . THR B 97  ? 0.21634 0.22168 0.20473 -0.02104 0.05198  -0.00341 97  THR B CG2 
2386 N N   . ILE B 98  ? 0.16773 0.16093 0.15172 -0.01920 0.00990  0.00999  98  ILE B N   
2387 C CA  . ILE B 98  ? 0.17347 0.17623 0.14679 -0.03088 0.01715  0.01109  98  ILE B CA  
2388 C C   . ILE B 98  ? 0.15423 0.17588 0.15376 -0.04321 0.03369  -0.00861 98  ILE B C   
2389 O O   . ILE B 98  ? 0.14706 0.19511 0.16568 -0.03141 0.00761  -0.00173 98  ILE B O   
2390 C CB  . ILE B 98  ? 0.17917 0.18148 0.19950 -0.00446 0.02547  -0.01652 98  ILE B CB  
2391 C CG1 . ILE B 98  ? 0.18874 0.18564 0.21449 -0.02856 0.02494  0.00507  98  ILE B CG1 
2392 C CG2 . ILE B 98  ? 0.18965 0.22040 0.25881 -0.04070 0.08065  -0.00403 98  ILE B CG2 
2393 C CD1 . ILE B 98  ? 0.21827 0.20253 0.23898 0.02848  0.04710  -0.03015 98  ILE B CD1 
2394 N N   . SER B 99  ? 0.16910 0.16951 0.17761 -0.03041 0.02495  0.00226  99  SER B N   
2395 C CA  . SER B 99  ? 0.20322 0.18358 0.15346 -0.02426 0.01784  0.03727  99  SER B CA  
2396 C C   . SER B 99  ? 0.21029 0.23569 0.16043 -0.00572 0.00364  -0.00540 99  SER B C   
2397 O O   . SER B 99  ? 0.24117 0.38493 0.16768 0.08385  0.03668  0.03424  99  SER B O   
2398 C CB  . SER B 99  ? 0.20338 0.18526 0.20331 -0.06955 0.01132  -0.01297 99  SER B CB  
2399 O OG  . SER B 99  ? 0.27154 0.18289 0.23461 -0.04609 -0.01906 0.02526  99  SER B OG  
2400 N N   . ARG B 100 ? 0.27171 0.28190 0.15223 0.05122  0.04490  0.05256  100 ARG B N   
2401 C CA  . ARG B 100 ? 0.27049 0.29687 0.15596 -0.01570 0.02176  0.03984  100 ARG B CA  
2402 C C   . ARG B 100 ? 0.23216 0.30906 0.13750 -0.03116 0.01680  0.00655  100 ARG B C   
2403 O O   . ARG B 100 ? 0.22858 0.26806 0.15997 -0.03152 0.01101  0.01962  100 ARG B O   
2404 C CB  . ARG B 100 ? 0.34500 0.34243 0.17171 0.00543  0.02195  0.04785  100 ARG B CB  
2405 C CG  . ARG B 100 ? 0.36754 0.39119 0.26158 -0.01608 -0.01701 0.02231  100 ARG B CG  
2406 C CD  . ARG B 100 ? 0.37630 0.42821 0.34458 -0.05102 -0.01839 -0.00665 100 ARG B CD  
2407 N NE  . ARG B 100 ? 0.39374 0.47906 0.39506 -0.03156 -0.01943 -0.01130 100 ARG B NE  
2408 C CZ  . ARG B 100 ? 0.42809 0.50366 0.43217 -0.01260 0.01512  0.03342  100 ARG B CZ  
2409 N NH1 . ARG B 100 ? 0.44116 0.51598 0.46067 -0.00039 -0.03862 0.02926  100 ARG B NH1 
2410 N NH2 . ARG B 100 ? 0.43077 0.49478 0.41630 0.00444  0.02010  0.03257  100 ARG B NH2 
2411 N N   . THR B 101 ? 0.23027 0.32966 0.16255 -0.03087 0.01677  0.01616  101 THR B N   
2412 C CA  . THR B 101 ? 0.22539 0.32769 0.18848 -0.05597 0.02666  0.00687  101 THR B CA  
2413 C C   . THR B 101 ? 0.23557 0.29685 0.17055 -0.06273 0.00603  0.01325  101 THR B C   
2414 O O   . THR B 101 ? 0.25218 0.31699 0.21086 -0.06548 -0.02701 0.05126  101 THR B O   
2415 C CB  . THR B 101 ? 0.23815 0.34387 0.21536 -0.05106 0.01769  -0.00058 101 THR B CB  
2416 O OG1 . THR B 101 ? 0.24495 0.38610 0.23829 -0.06598 0.03111  -0.03231 101 THR B OG1 
2417 C CG2 . THR B 101 ? 0.27672 0.39362 0.22381 -0.03345 0.07335  0.01733  101 THR B CG2 
2418 N N   . GLY B 102 ? 0.27390 0.30286 0.16952 -0.06984 0.02846  0.02756  102 GLY B N   
2419 C CA  . GLY B 102 ? 0.27103 0.28237 0.18973 -0.06905 0.00748  0.02515  102 GLY B CA  
2420 C C   . GLY B 102 ? 0.28409 0.27575 0.21001 -0.06338 -0.03665 0.03794  102 GLY B C   
2421 O O   . GLY B 102 ? 0.35976 0.28487 0.25568 -0.03219 -0.03459 0.06490  102 GLY B O   
2422 N N   . SER B 103 ? 0.23873 0.24707 0.17761 -0.06628 -0.02900 0.05619  103 SER B N   
2423 C CA  . SER B 103 ? 0.19083 0.24910 0.19670 -0.05100 0.00387  0.05440  103 SER B CA  
2424 C C   . SER B 103 ? 0.17470 0.20970 0.18348 -0.02821 0.00288  0.03272  103 SER B C   
2425 O O   . SER B 103 ? 0.16411 0.24630 0.18299 -0.01564 -0.00108 0.02267  103 SER B O   
2426 C CB  . SER B 103 ? 0.21049 0.26022 0.21356 -0.08268 0.01871  0.03898  103 SER B CB  
2427 O OG  . SER B 103 ? 0.20117 0.28642 0.24808 -0.06107 -0.00682 0.04174  103 SER B OG  
2428 N N   . LEU B 104 ? 0.18965 0.19580 0.19723 -0.03631 0.02901  0.00753  104 LEU B N   
2429 C CA  . LEU B 104 ? 0.23044 0.20538 0.23431 -0.06782 0.06564  -0.02634 104 LEU B CA  
2430 C C   . LEU B 104 ? 0.18829 0.22953 0.19812 -0.05597 0.00974  0.00836  104 LEU B C   
2431 O O   . LEU B 104 ? 0.25290 0.29536 0.19728 -0.10930 0.01080  -0.00018 104 LEU B O   
2432 C CB  . LEU B 104 ? 0.29810 0.21257 0.36102 -0.09626 0.12699  -0.03886 104 LEU B CB  
2433 C CG  . LEU B 104 ? 0.28941 0.24588 0.31498 -0.07227 0.07679  -0.04511 104 LEU B CG  
2434 C CD1 . LEU B 104 ? 0.29437 0.32251 0.27871 -0.11615 -0.05295 0.03887  104 LEU B CD1 
2435 C CD2 . LEU B 104 ? 0.22008 0.22948 0.37292 -0.01331 0.03374  0.06231  104 LEU B CD2 
2436 N N   . TRP B 105 ? 0.15045 0.19033 0.22789 -0.03106 0.00585  0.00540  105 TRP B N   
2437 C CA  . TRP B 105 ? 0.16386 0.17287 0.24883 -0.04506 0.02535  0.01071  105 TRP B CA  
2438 C C   . TRP B 105 ? 0.19783 0.16615 0.20063 -0.03585 0.05327  -0.00162 105 TRP B C   
2439 O O   . TRP B 105 ? 0.27083 0.18994 0.19548 -0.00562 0.05492  0.00731  105 TRP B O   
2440 C CB  . TRP B 105 ? 0.16880 0.20431 0.29980 -0.04280 0.03105  -0.02732 105 TRP B CB  
2441 C CG  . TRP B 105 ? 0.20580 0.21738 0.30768 -0.03559 -0.02166 -0.00047 105 TRP B CG  
2442 C CD1 . TRP B 105 ? 0.18808 0.25856 0.32534 -0.03303 -0.01068 0.01896  105 TRP B CD1 
2443 C CD2 . TRP B 105 ? 0.16439 0.30562 0.21436 -0.04958 -0.00772 0.06445  105 TRP B CD2 
2444 N NE1 . TRP B 105 ? 0.19505 0.27506 0.33514 -0.01828 0.00078  -0.01986 105 TRP B NE1 
2445 C CE2 . TRP B 105 ? 0.17488 0.27197 0.24065 -0.05679 -0.00481 -0.00554 105 TRP B CE2 
2446 C CE3 . TRP B 105 ? 0.21506 0.29359 0.17897 0.08278  -0.01465 0.01117  105 TRP B CE3 
2447 C CZ2 . TRP B 105 ? 0.17422 0.30098 0.24935 -0.05136 0.01138  -0.01356 105 TRP B CZ2 
2448 C CZ3 . TRP B 105 ? 0.19762 0.27192 0.19509 0.00424  -0.04057 0.00978  105 TRP B CZ3 
2449 C CH2 . TRP B 105 ? 0.18281 0.27658 0.24390 -0.04092 0.02418  0.00284  105 TRP B CH2 
2450 N N   . CYS B 106 ? 0.18049 0.16602 0.18789 -0.02187 0.03195  0.01098  106 CYS B N   
2451 C CA  . CYS B 106 ? 0.18075 0.16718 0.17988 -0.02288 0.02594  0.00436  106 CYS B CA  
2452 C C   . CYS B 106 ? 0.16926 0.16217 0.19285 -0.02501 0.02667  -0.00224 106 CYS B C   
2453 O O   . CYS B 106 ? 0.17592 0.22181 0.19350 -0.02948 0.03772  -0.01851 106 CYS B O   
2454 C CB  . CYS B 106 ? 0.18990 0.18612 0.19546 -0.03883 -0.00517 -0.00013 106 CYS B CB  
2455 S SG  . CYS B 106 ? 0.19228 0.21181 0.24634 -0.03719 0.04794  -0.00697 106 CYS B SG  
2456 N N   . GLU B 107 ? 0.17517 0.15286 0.20060 -0.01285 0.01467  -0.01868 107 GLU B N   
2457 C CA  A GLU B 107 ? 0.15935 0.15901 0.20812 -0.02582 -0.00001 -0.01097 107 GLU B CA  
2458 C CA  B GLU B 107 ? 0.15418 0.15354 0.19505 -0.02553 -0.00250 -0.00993 107 GLU B CA  
2459 C C   . GLU B 107 ? 0.13936 0.15423 0.17796 -0.02472 0.01697  0.00888  107 GLU B C   
2460 O O   . GLU B 107 ? 0.13987 0.17066 0.15855 -0.01542 0.00380  0.00249  107 GLU B O   
2461 C CB  A GLU B 107 ? 0.22410 0.17979 0.22536 0.00324  -0.05826 0.02212  107 GLU B CB  
2462 C CB  B GLU B 107 ? 0.19811 0.17416 0.17950 -0.00259 0.00163  0.02478  107 GLU B CB  
2463 C CG  A GLU B 107 ? 0.28589 0.26385 0.30788 0.02297  -0.02421 0.04495  107 GLU B CG  
2464 C CG  B GLU B 107 ? 0.26895 0.24121 0.23182 0.02846  0.00656  0.04202  107 GLU B CG  
2465 C CD  A GLU B 107 ? 0.35769 0.34759 0.37097 0.05531  0.00402  0.06071  107 GLU B CD  
2466 C CD  B GLU B 107 ? 0.34542 0.32804 0.35313 0.07962  0.01008  0.06431  107 GLU B CD  
2467 O OE1 A GLU B 107 ? 0.37913 0.37732 0.39985 0.05764  0.03482  0.09045  107 GLU B OE1 
2468 O OE1 B GLU B 107 ? 0.38006 0.38761 0.41068 0.08071  -0.00120 0.08552  107 GLU B OE1 
2469 O OE2 A GLU B 107 ? 0.40873 0.40683 0.39506 0.07110  0.01190  0.03356  107 GLU B OE2 
2470 O OE2 B GLU B 107 ? 0.36754 0.34402 0.37263 0.12198  0.01167  0.09777  107 GLU B OE2 
2471 N N   . GLU B 108 ? 0.16382 0.16457 0.19632 -0.02463 0.00325  -0.01098 108 GLU B N   
2472 C CA  . GLU B 108 ? 0.15688 0.15626 0.19738 -0.03460 0.03294  0.01773  108 GLU B CA  
2473 C C   . GLU B 108 ? 0.16740 0.16038 0.16970 -0.01949 -0.00084 -0.00900 108 GLU B C   
2474 O O   . GLU B 108 ? 0.18879 0.18376 0.21215 0.00943  -0.03228 -0.02554 108 GLU B O   
2475 C CB  . GLU B 108 ? 0.18554 0.18775 0.33420 -0.03052 0.04408  0.00213  108 GLU B CB  
2476 C CG  . GLU B 108 ? 0.16698 0.22925 0.29753 -0.01361 -0.00162 0.03296  108 GLU B CG  
2477 C CD  . GLU B 108 ? 0.18192 0.25131 0.26289 0.03488  0.00940  0.01280  108 GLU B CD  
2478 O OE1 . GLU B 108 ? 0.16009 0.27260 0.29435 0.00298  0.02315  -0.00348 108 GLU B OE1 
2479 O OE2 . GLU B 108 ? 0.16200 0.23075 0.28885 0.01778  0.03151  0.04068  108 GLU B OE2 
2480 N N   . TYR B 109 ? 0.16341 0.15649 0.14049 -0.01512 0.00519  -0.01500 109 TYR B N   
2481 C CA  . TYR B 109 ? 0.16030 0.15470 0.14692 -0.00370 0.00700  -0.00916 109 TYR B CA  
2482 C C   . TYR B 109 ? 0.16765 0.16534 0.12738 -0.01974 0.00275  0.01753  109 TYR B C   
2483 O O   . TYR B 109 ? 0.17450 0.17320 0.14459 -0.01727 -0.01459 -0.00668 109 TYR B O   
2484 C CB  . TYR B 109 ? 0.17922 0.17152 0.15095 -0.01686 0.03097  0.00609  109 TYR B CB  
2485 C CG  . TYR B 109 ? 0.19246 0.19371 0.13721 -0.03710 -0.00278 0.00551  109 TYR B CG  
2486 C CD1 . TYR B 109 ? 0.27755 0.18687 0.18236 -0.03967 -0.01562 0.02281  109 TYR B CD1 
2487 C CD2 . TYR B 109 ? 0.16930 0.18243 0.13576 -0.01282 0.02144  0.01057  109 TYR B CD2 
2488 C CE1 . TYR B 109 ? 0.31409 0.18352 0.21235 -0.03153 -0.03912 0.03457  109 TYR B CE1 
2489 C CE2 . TYR B 109 ? 0.20377 0.21541 0.17520 -0.00678 0.01252  0.02846  109 TYR B CE2 
2490 C CZ  . TYR B 109 ? 0.26562 0.18837 0.20537 -0.04850 -0.01925 0.04072  109 TYR B CZ  
2491 O OH  . TYR B 109 ? 0.35430 0.18934 0.19472 -0.02503 -0.03577 0.04283  109 TYR B OH  
2492 N N   . TRP B 110 ? 0.15964 0.15968 0.14867 -0.00482 -0.00639 -0.01752 110 TRP B N   
2493 C CA  . TRP B 110 ? 0.17335 0.14954 0.15270 0.00037  -0.01141 -0.00129 110 TRP B CA  
2494 C C   . TRP B 110 ? 0.17193 0.17209 0.11157 -0.01199 -0.03309 -0.01194 110 TRP B C   
2495 O O   . TRP B 110 ? 0.17445 0.16964 0.12667 -0.00468 -0.01677 -0.00340 110 TRP B O   
2496 C CB  . TRP B 110 ? 0.15745 0.16161 0.15914 -0.01747 -0.00824 -0.00316 110 TRP B CB  
2497 C CG  . TRP B 110 ? 0.15307 0.16827 0.15784 0.00056  -0.00467 0.01384  110 TRP B CG  
2498 C CD1 . TRP B 110 ? 0.14961 0.19319 0.18901 0.00237  -0.00225 0.02247  110 TRP B CD1 
2499 C CD2 . TRP B 110 ? 0.13727 0.16509 0.15240 -0.01556 -0.00329 0.01547  110 TRP B CD2 
2500 N NE1 . TRP B 110 ? 0.16571 0.20728 0.17131 0.02344  0.01022  0.01401  110 TRP B NE1 
2501 C CE2 . TRP B 110 ? 0.13987 0.20298 0.15937 0.00727  -0.00464 0.00040  110 TRP B CE2 
2502 C CE3 . TRP B 110 ? 0.15562 0.16761 0.16031 -0.01495 -0.01522 0.00810  110 TRP B CE3 
2503 C CZ2 . TRP B 110 ? 0.14381 0.19756 0.18373 0.01557  -0.01541 -0.02016 110 TRP B CZ2 
2504 C CZ3 . TRP B 110 ? 0.16486 0.18212 0.17181 -0.02213 0.00332  0.00869  110 TRP B CZ3 
2505 C CH2 . TRP B 110 ? 0.13802 0.20880 0.18508 0.00343  0.01692  -0.02849 110 TRP B CH2 
2506 N N   . GLY B 111 ? 0.14746 0.16308 0.13204 -0.01906 -0.01937 -0.00030 111 GLY B N   
2507 C CA  . GLY B 111 ? 0.15383 0.14759 0.16560 0.00877  -0.00911 -0.05162 111 GLY B CA  
2508 C C   . GLY B 111 ? 0.15074 0.17748 0.12003 0.00347  0.00638  -0.01731 111 GLY B C   
2509 O O   . GLY B 111 ? 0.16766 0.16401 0.16593 -0.00824 0.01348  -0.00732 111 GLY B O   
2510 N N   . GLN B 112 ? 0.16105 0.15232 0.13689 -0.01260 0.00327  -0.01019 112 GLN B N   
2511 C CA  . GLN B 112 ? 0.17558 0.14349 0.14391 -0.02579 -0.00052 -0.01090 112 GLN B CA  
2512 C C   . GLN B 112 ? 0.15652 0.15532 0.16167 -0.02686 -0.01011 -0.01666 112 GLN B C   
2513 O O   . GLN B 112 ? 0.18176 0.18101 0.14391 -0.02982 -0.02210 0.01005  112 GLN B O   
2514 C CB  . GLN B 112 ? 0.16494 0.19831 0.13359 0.00231  -0.00792 -0.02059 112 GLN B CB  
2515 C CG  . GLN B 112 ? 0.16635 0.16520 0.15217 -0.02788 -0.00670 -0.00667 112 GLN B CG  
2516 C CD  . GLN B 112 ? 0.18744 0.14740 0.11812 -0.00023 0.01206  -0.01431 112 GLN B CD  
2517 O OE1 . GLN B 112 ? 0.13769 0.19332 0.15235 -0.00913 -0.00089 -0.01750 112 GLN B OE1 
2518 N NE2 . GLN B 112 ? 0.17441 0.17892 0.13506 0.00224  0.01425  -0.00965 112 GLN B NE2 
2519 N N   . GLY B 113 ? 0.16224 0.16763 0.13415 -0.00923 -0.01080 -0.00164 113 GLY B N   
2520 C CA  . GLY B 113 ? 0.18714 0.16819 0.12431 0.00122  -0.00603 -0.01545 113 GLY B CA  
2521 C C   . GLY B 113 ? 0.19088 0.15845 0.10978 -0.01823 0.01147  -0.01464 113 GLY B C   
2522 O O   . GLY B 113 ? 0.19289 0.16971 0.13948 0.00611  -0.00950 -0.01743 113 GLY B O   
2523 N N   . THR B 114 ? 0.16612 0.17903 0.12075 0.00316  0.00648  -0.00506 114 THR B N   
2524 C CA  . THR B 114 ? 0.15711 0.16383 0.14426 -0.00850 -0.00147 -0.00004 114 THR B CA  
2525 C C   . THR B 114 ? 0.15880 0.19249 0.12635 -0.01870 -0.00683 0.00046  114 THR B C   
2526 O O   . THR B 114 ? 0.17233 0.18885 0.13048 0.00850  0.00499  -0.00070 114 THR B O   
2527 C CB  . THR B 114 ? 0.16980 0.19998 0.14413 0.01061  -0.00818 -0.03910 114 THR B CB  
2528 O OG1 . THR B 114 ? 0.16740 0.21369 0.16190 0.01596  -0.00868 -0.01157 114 THR B OG1 
2529 C CG2 . THR B 114 ? 0.17147 0.22197 0.16875 -0.00296 -0.00287 -0.00352 114 THR B CG2 
2530 N N   . GLN B 115 ? 0.17885 0.16406 0.14529 -0.00780 -0.00851 0.00684  115 GLN B N   
2531 C CA  . GLN B 115 ? 0.20563 0.15530 0.15035 -0.02817 -0.06107 0.01187  115 GLN B CA  
2532 C C   . GLN B 115 ? 0.17558 0.16959 0.14594 -0.00944 -0.00670 0.00203  115 GLN B C   
2533 O O   . GLN B 115 ? 0.19573 0.19364 0.16253 0.01565  -0.00019 0.00509  115 GLN B O   
2534 C CB  . GLN B 115 ? 0.26283 0.19568 0.17866 -0.03742 -0.05234 0.01121  115 GLN B CB  
2535 C CG  . GLN B 115 ? 0.28176 0.21062 0.20671 -0.03951 -0.05102 0.05500  115 GLN B CG  
2536 C CD  . GLN B 115 ? 0.29813 0.25411 0.19908 -0.00099 -0.03173 0.04010  115 GLN B CD  
2537 O OE1 . GLN B 115 ? 0.34545 0.31476 0.15443 0.08795  -0.00452 0.01497  115 GLN B OE1 
2538 N NE2 . GLN B 115 ? 0.31213 0.24613 0.22402 -0.03717 -0.02906 0.04191  115 GLN B NE2 
2539 N N   . VAL B 116 ? 0.18701 0.17500 0.14166 -0.00011 -0.01874 0.00876  116 VAL B N   
2540 C CA  . VAL B 116 ? 0.20624 0.15602 0.15849 -0.01681 -0.05192 0.00682  116 VAL B CA  
2541 C C   . VAL B 116 ? 0.22456 0.15210 0.15759 0.02046  -0.01969 -0.01784 116 VAL B C   
2542 O O   . VAL B 116 ? 0.21441 0.18844 0.15636 0.01189  0.00068  0.00956  116 VAL B O   
2543 C CB  . VAL B 116 ? 0.22624 0.17670 0.16073 -0.03338 -0.03964 0.00635  116 VAL B CB  
2544 C CG1 . VAL B 116 ? 0.24603 0.22154 0.19560 -0.00415 -0.07870 0.01883  116 VAL B CG1 
2545 C CG2 . VAL B 116 ? 0.22833 0.19502 0.17647 -0.03144 -0.03584 0.00830  116 VAL B CG2 
2546 N N   . THR B 117 ? 0.24888 0.16959 0.16728 0.00403  -0.01615 0.01382  117 THR B N   
2547 C CA  A THR B 117 ? 0.28665 0.16496 0.15580 -0.00522 -0.04715 0.02087  117 THR B CA  
2548 C CA  B THR B 117 ? 0.28406 0.16318 0.15924 -0.00104 -0.04405 0.02250  117 THR B CA  
2549 C C   . THR B 117 ? 0.28317 0.18685 0.17629 0.00140  -0.01146 0.02511  117 THR B C   
2550 O O   . THR B 117 ? 0.29323 0.30477 0.16881 0.02893  -0.00398 0.03661  117 THR B O   
2551 C CB  A THR B 117 ? 0.31075 0.20933 0.20890 -0.03228 -0.04715 0.03856  117 THR B CB  
2552 C CB  B THR B 117 ? 0.28611 0.18966 0.19409 -0.01896 -0.05364 0.05052  117 THR B CB  
2553 O OG1 A THR B 117 ? 0.39061 0.26508 0.32733 0.04700  -0.00566 0.03740  117 THR B OG1 
2554 O OG1 B THR B 117 ? 0.32137 0.18825 0.19232 -0.01145 -0.08929 0.05061  117 THR B OG1 
2555 C CG2 A THR B 117 ? 0.30226 0.22120 0.23625 -0.03587 -0.06876 0.02193  117 THR B CG2 
2556 C CG2 B THR B 117 ? 0.24673 0.17946 0.22601 -0.01301 -0.09689 0.01262  117 THR B CG2 
2557 N N   . VAL B 118 ? 0.27754 0.20825 0.17169 0.02779  -0.00803 0.03373  118 VAL B N   
2558 C CA  . VAL B 118 ? 0.30595 0.19954 0.19722 0.02541  -0.04804 0.04272  118 VAL B CA  
2559 C C   . VAL B 118 ? 0.33316 0.23664 0.21247 -0.00421 -0.04095 0.05252  118 VAL B C   
2560 O O   . VAL B 118 ? 0.37569 0.22619 0.23092 0.01745  -0.04147 0.05284  118 VAL B O   
2561 C CB  . VAL B 118 ? 0.30667 0.20526 0.18682 0.01388  -0.05785 -0.00623 118 VAL B CB  
2562 C CG1 . VAL B 118 ? 0.29056 0.23987 0.19763 0.03826  -0.05549 0.02369  118 VAL B CG1 
2563 C CG2 . VAL B 118 ? 0.27659 0.18467 0.23244 -0.00377 -0.04159 0.03278  118 VAL B CG2 
2564 N N   . SER B 119 ? 0.36298 0.27825 0.30649 0.02972  -0.03604 0.06473  119 SER B N   
2565 C CA  . SER B 119 ? 0.44653 0.42301 0.47880 0.04640  -0.03675 0.01453  119 SER B CA  
2566 C C   . SER B 119 ? 0.52203 0.50432 0.57773 0.05857  -0.03461 0.02980  119 SER B C   
2567 O O   . SER B 119 ? 0.52596 0.46226 0.53943 0.03294  -0.06386 0.06342  119 SER B O   
2568 C CB  . SER B 119 ? 0.48299 0.46677 0.56523 0.05545  -0.01894 -0.00824 119 SER B CB  
2569 O OG  . SER B 119 ? 0.50734 0.48619 0.61597 0.06812  -0.00820 -0.04340 119 SER B OG  
2570 N N   . SER B 120 ? 0.57541 0.57449 0.65365 0.07019  -0.03280 0.01083  120 SER B N   
2571 C CA  . SER B 120 ? 0.62016 0.62324 0.69843 0.06029  -0.03440 0.00762  120 SER B CA  
2572 C C   . SER B 120 ? 0.63962 0.62833 0.72018 0.06734  -0.03710 0.01730  120 SER B C   
2573 O O   . SER B 120 ? 0.64090 0.62080 0.73359 0.07243  -0.02673 0.02320  120 SER B O   
2574 C CB  . SER B 120 ? 0.63467 0.63025 0.71250 0.05001  -0.03249 0.02178  120 SER B CB  
2575 O OG  . SER B 120 ? 0.64204 0.63335 0.71762 0.04009  -0.01820 0.03902  120 SER B OG  
# 
