data_8Y2K
# 
_entry.id   8Y2K 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y2K         pdb_00008y2k 10.2210/pdb8y2k/pdb 
WWPDB D_1300044719 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        8Y2K 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              wfeng@ibp.ac.cn 
_pdbx_contact_author.name_first         Wei 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9738-9398 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, W.'   1 0000-0001-6016-8399 
'Feng, W.' 2 0000-0001-9738-9398 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            268 
_citation.language                  ? 
_citation.page_first                131721 
_citation.page_last                 131721 
_citation.title                     
;Structural basis for the recognition of IFNAR1 by the humanized therapeutic monoclonal antibody QX006N for the treatment of systemic lupus erythematosus.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.131721 
_citation.pdbx_database_id_PubMed   38649079 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, X.' 1 ? 
primary 'Ke, H.'   2 ? 
primary 'Li, W.'   3 ? 
primary 'Yin, L.'  4 ? 
primary 'Chen, W.' 5 ? 
primary 'Chen, T.' 6 ? 
primary 'Wu, Y.'   7 ? 
primary 'Qiu, J.'  8 ? 
primary 'Feng, W.' 9 ? 
# 
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 QX006N-Fab-LC 23200.725 2 ? ? ? ? 
2 polymer man QX006N-Fab-HC 24517.518 2 ? ? ? ? 
# 
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 
;AIQMTQSPSSLSASVGDRVTITCQASQSISNQLSWYQQKPGKAPKLLIYDASSLASGVPSRFSGSRSGTKFTLTISSLQP
EDFATYYCLGIYGDGADDGIAFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS
GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
;AIQMTQSPSSLSASVGDRVTITCQASQSISNQLSWYQQKPGKAPKLLIYDASSLASGVPSRFSGSRSGTKFTLTISSLQP
EDFATYYCLGIYGDGADDGIAFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS
GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
A,C ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVQPGGSLRLSCAASGFSLSSYYMTWVRQAPGKGLEWVSVINVYGGTYYASWAKGRFTISRDNSKNTLYL
QMNSLRAEDTAVYYCAREDVAVYMAIDLWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGGHHHHHH
;
;EVQLVESGGGLVQPGGSLRLSCAASGFSLSSYYMTWVRQAPGKGLEWVSVINVYGGTYYASWAKGRFTISRDNSKNTLYL
QMNSLRAEDTAVYYCAREDVAVYMAIDLWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGGHHHHHH
;
B,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ILE n 
1 3   GLN n 
1 4   MET n 
1 5   THR n 
1 6   GLN n 
1 7   SER n 
1 8   PRO n 
1 9   SER n 
1 10  SER n 
1 11  LEU n 
1 12  SER n 
1 13  ALA n 
1 14  SER n 
1 15  VAL n 
1 16  GLY n 
1 17  ASP n 
1 18  ARG n 
1 19  VAL n 
1 20  THR n 
1 21  ILE n 
1 22  THR n 
1 23  CYS n 
1 24  GLN n 
1 25  ALA n 
1 26  SER n 
1 27  GLN n 
1 28  SER n 
1 29  ILE n 
1 30  SER n 
1 31  ASN n 
1 32  GLN n 
1 33  LEU n 
1 34  SER n 
1 35  TRP n 
1 36  TYR n 
1 37  GLN n 
1 38  GLN n 
1 39  LYS n 
1 40  PRO n 
1 41  GLY n 
1 42  LYS n 
1 43  ALA n 
1 44  PRO n 
1 45  LYS n 
1 46  LEU n 
1 47  LEU n 
1 48  ILE n 
1 49  TYR n 
1 50  ASP n 
1 51  ALA n 
1 52  SER n 
1 53  SER n 
1 54  LEU n 
1 55  ALA n 
1 56  SER n 
1 57  GLY n 
1 58  VAL n 
1 59  PRO n 
1 60  SER n 
1 61  ARG n 
1 62  PHE n 
1 63  SER n 
1 64  GLY n 
1 65  SER n 
1 66  ARG n 
1 67  SER n 
1 68  GLY n 
1 69  THR n 
1 70  LYS n 
1 71  PHE n 
1 72  THR n 
1 73  LEU n 
1 74  THR n 
1 75  ILE n 
1 76  SER n 
1 77  SER n 
1 78  LEU n 
1 79  GLN n 
1 80  PRO n 
1 81  GLU n 
1 82  ASP n 
1 83  PHE n 
1 84  ALA n 
1 85  THR n 
1 86  TYR n 
1 87  TYR n 
1 88  CYS n 
1 89  LEU n 
1 90  GLY n 
1 91  ILE n 
1 92  TYR n 
1 93  GLY n 
1 94  ASP n 
1 95  GLY n 
1 96  ALA n 
1 97  ASP n 
1 98  ASP n 
1 99  GLY n 
1 100 ILE n 
1 101 ALA n 
1 102 PHE n 
1 103 GLY n 
1 104 GLY n 
1 105 GLY n 
1 106 THR n 
1 107 LYS n 
1 108 VAL n 
1 109 GLU n 
1 110 ILE n 
1 111 LYS n 
1 112 ARG n 
1 113 THR n 
1 114 VAL n 
1 115 ALA n 
1 116 ALA n 
1 117 PRO n 
1 118 SER n 
1 119 VAL n 
1 120 PHE n 
1 121 ILE n 
1 122 PHE n 
1 123 PRO n 
1 124 PRO n 
1 125 SER n 
1 126 ASP n 
1 127 GLU n 
1 128 GLN n 
1 129 LEU n 
1 130 LYS n 
1 131 SER n 
1 132 GLY n 
1 133 THR n 
1 134 ALA n 
1 135 SER n 
1 136 VAL n 
1 137 VAL n 
1 138 CYS n 
1 139 LEU n 
1 140 LEU n 
1 141 ASN n 
1 142 ASN n 
1 143 PHE n 
1 144 TYR n 
1 145 PRO n 
1 146 ARG n 
1 147 GLU n 
1 148 ALA n 
1 149 LYS n 
1 150 VAL n 
1 151 GLN n 
1 152 TRP n 
1 153 LYS n 
1 154 VAL n 
1 155 ASP n 
1 156 ASN n 
1 157 ALA n 
1 158 LEU n 
1 159 GLN n 
1 160 SER n 
1 161 GLY n 
1 162 ASN n 
1 163 SER n 
1 164 GLN n 
1 165 GLU n 
1 166 SER n 
1 167 VAL n 
1 168 THR n 
1 169 GLU n 
1 170 GLN n 
1 171 ASP n 
1 172 SER n 
1 173 LYS n 
1 174 ASP n 
1 175 SER n 
1 176 THR n 
1 177 TYR n 
1 178 SER n 
1 179 LEU n 
1 180 SER n 
1 181 SER n 
1 182 THR n 
1 183 LEU n 
1 184 THR n 
1 185 LEU n 
1 186 SER n 
1 187 LYS n 
1 188 ALA n 
1 189 ASP n 
1 190 TYR n 
1 191 GLU n 
1 192 LYS n 
1 193 HIS n 
1 194 LYS n 
1 195 VAL n 
1 196 TYR n 
1 197 ALA n 
1 198 CYS n 
1 199 GLU n 
1 200 VAL n 
1 201 THR n 
1 202 GLN n 
1 203 GLY n 
1 204 THR n 
1 205 THR n 
1 206 SER n 
1 207 VAL n 
1 208 THR n 
1 209 LYS n 
1 210 SER n 
1 211 PHE n 
1 212 ASN n 
1 213 ARG n 
1 214 GLY n 
1 215 GLU n 
1 216 CYS n 
2 1   GLU 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  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO 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  PHE n 
2 28  SER n 
2 29  LEU n 
2 30  SER n 
2 31  SER n 
2 32  TYR n 
2 33  TYR n 
2 34  MET n 
2 35  THR n 
2 36  TRP n 
2 37  VAL 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  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  VAL n 
2 49  SER n 
2 50  VAL n 
2 51  ILE n 
2 52  ASN n 
2 53  VAL n 
2 54  TYR n 
2 55  GLY n 
2 56  GLY n 
2 57  THR n 
2 58  TYR n 
2 59  TYR n 
2 60  ALA n 
2 61  SER n 
2 62  TRP n 
2 63  ALA n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ARG n 
2 72  ASP n 
2 73  ASN n 
2 74  SER n 
2 75  LYS n 
2 76  ASN n 
2 77  THR n 
2 78  LEU n 
2 79  TYR n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  ARG n 
2 87  ALA n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ALA n 
2 97  ARG n 
2 98  GLU n 
2 99  ASP n 
2 100 VAL n 
2 101 ALA n 
2 102 VAL n 
2 103 TYR n 
2 104 MET n 
2 105 ALA n 
2 106 ILE n 
2 107 ASP n 
2 108 LEU n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 THR n 
2 114 LEU n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 SER n 
2 120 ALA n 
2 121 SER n 
2 122 THR n 
2 123 LYS n 
2 124 GLY n 
2 125 PRO n 
2 126 SER n 
2 127 VAL n 
2 128 PHE n 
2 129 PRO n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 SER n 
2 134 SER n 
2 135 LYS n 
2 136 SER n 
2 137 THR n 
2 138 SER n 
2 139 GLY n 
2 140 GLY n 
2 141 THR n 
2 142 ALA n 
2 143 ALA n 
2 144 LEU n 
2 145 GLY n 
2 146 CYS n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 ASP n 
2 151 TYR n 
2 152 PHE n 
2 153 PRO n 
2 154 GLU n 
2 155 PRO n 
2 156 VAL n 
2 157 THR n 
2 158 VAL n 
2 159 SER n 
2 160 TRP n 
2 161 ASN n 
2 162 SER n 
2 163 GLY n 
2 164 ALA n 
2 165 LEU n 
2 166 THR n 
2 167 SER n 
2 168 GLY n 
2 169 VAL n 
2 170 HIS n 
2 171 THR n 
2 172 PHE n 
2 173 PRO n 
2 174 ALA n 
2 175 VAL n 
2 176 LEU n 
2 177 GLN n 
2 178 SER n 
2 179 SER n 
2 180 GLY n 
2 181 LEU n 
2 182 TYR n 
2 183 SER n 
2 184 LEU n 
2 185 SER n 
2 186 SER n 
2 187 VAL n 
2 188 VAL n 
2 189 THR n 
2 190 VAL n 
2 191 PRO n 
2 192 SER n 
2 193 SER n 
2 194 SER n 
2 195 LEU n 
2 196 GLY n 
2 197 THR n 
2 198 GLN n 
2 199 THR n 
2 200 TYR n 
2 201 ILE n 
2 202 CYS n 
2 203 ASN n 
2 204 VAL n 
2 205 ASN n 
2 206 HIS n 
2 207 LYS n 
2 208 PRO n 
2 209 SER n 
2 210 ASN n 
2 211 THR n 
2 212 LYS n 
2 213 VAL n 
2 214 ASP n 
2 215 LYS n 
2 216 LYS n 
2 217 VAL n 
2 218 GLU n 
2 219 PRO n 
2 220 LYS n 
2 221 SER n 
2 222 CYS n 
2 223 GLY n 
2 224 GLY n 
2 225 HIS n 
2 226 HIS n 
2 227 HIS n 
2 228 HIS n 
2 229 HIS n 
2 230 HIS 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' 1 216 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 230 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
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_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   ALA 1   1   1   ALA ALA A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  CYS 23  23  23  CYS CYS A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 CYS 138 138 138 CYS CYS A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 TRP 152 152 152 TRP TRP A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 GLN 202 202 202 GLN GLN A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 CYS 216 216 216 CYS CYS A . n 
B 2 1   GLU 1   1   1   GLU GLU 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  LEU 11  11  11  LEU LEU 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  PRO 14  14  14  PRO PRO 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  PHE 27  27  27  PHE PHE B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  LEU 29  29  29  LEU LEU B . n 
B 2 30  SER 30  30  30  SER SER B . n 
B 2 31  SER 31  31  31  SER SER B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  TYR 33  33  33  TYR TYR B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  THR 35  35  35  THR THR B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  VAL 37  37  37  VAL VAL 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  GLY 44  44  44  GLY GLY 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  TRP 47  47  47  TRP TRP 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  VAL 50  50  50  VAL VAL B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  VAL 53  53  53  VAL VAL B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  TYR 58  58  58  TYR TYR B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  ALA 60  60  60  ALA ALA B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  TRP 62  62  62  TRP TRP B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  LYS 64  64  64  LYS LYS B . n 
B 2 65  GLY 65  65  65  GLY GLY B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  PHE 67  67  67  PHE PHE B . n 
B 2 68  THR 68  68  68  THR THR B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  SER 70  70  70  SER SER B . n 
B 2 71  ARG 71  71  71  ARG ARG B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  ASN 73  73  73  ASN ASN B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LYS 75  75  75  LYS LYS B . n 
B 2 76  ASN 76  76  76  ASN ASN B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  TYR 79  79  79  TYR TYR B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  GLN 81  81  81  GLN GLN B . n 
B 2 82  MET 82  82  82  MET MET B . n 
B 2 83  ASN 83  83  83  ASN ASN B . n 
B 2 84  SER 84  84  84  SER SER B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  GLU 88  88  88  GLU GLU B . n 
B 2 89  ASP 89  89  89  ASP ASP B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  VAL 92  92  92  VAL VAL B . n 
B 2 93  TYR 93  93  93  TYR TYR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  CYS 95  95  95  CYS CYS B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  ARG 97  97  97  ARG ARG B . n 
B 2 98  GLU 98  98  98  GLU GLU B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 ALA 101 101 101 ALA ALA B . n 
B 2 102 VAL 102 102 102 VAL VAL B . n 
B 2 103 TYR 103 103 103 TYR TYR B . n 
B 2 104 MET 104 104 104 MET MET B . n 
B 2 105 ALA 105 105 105 ALA ALA B . n 
B 2 106 ILE 106 106 106 ILE ILE B . n 
B 2 107 ASP 107 107 107 ASP ASP B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 TRP 109 109 109 TRP TRP B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 GLY 112 112 112 GLY GLY B . n 
B 2 113 THR 113 113 113 THR THR B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 VAL 117 117 117 VAL VAL B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 ALA 120 120 120 ALA ALA B . n 
B 2 121 SER 121 121 121 SER SER B . n 
B 2 122 THR 122 122 122 THR THR B . n 
B 2 123 LYS 123 123 123 LYS LYS B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 PRO 129 129 129 PRO PRO B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 ALA 131 131 131 ALA ALA B . n 
B 2 132 PRO 132 132 132 PRO PRO B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 SER 134 134 134 SER SER B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 SER 136 136 136 SER SER B . n 
B 2 137 THR 137 137 137 THR THR B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 GLY 139 139 139 GLY GLY B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 THR 141 141 141 THR THR B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 ALA 143 143 143 ALA ALA B . n 
B 2 144 LEU 144 144 144 LEU LEU B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 CYS 146 146 146 CYS CYS B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 ASP 150 150 150 ASP ASP B . n 
B 2 151 TYR 151 151 151 TYR TYR B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 PRO 153 153 153 PRO PRO B . n 
B 2 154 GLU 154 154 154 GLU GLU B . n 
B 2 155 PRO 155 155 155 PRO PRO B . n 
B 2 156 VAL 156 156 156 VAL VAL B . n 
B 2 157 THR 157 157 157 THR THR B . n 
B 2 158 VAL 158 158 158 VAL VAL B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 TRP 160 160 160 TRP TRP B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 SER 162 162 162 SER SER B . n 
B 2 163 GLY 163 163 163 GLY GLY B . n 
B 2 164 ALA 164 164 164 ALA ALA B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 HIS 170 170 170 HIS HIS B . n 
B 2 171 THR 171 171 171 THR THR B . n 
B 2 172 PHE 172 172 172 PHE PHE B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 GLN 177 177 177 GLN GLN B . n 
B 2 178 SER 178 178 178 SER SER B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 GLY 180 180 180 GLY GLY B . n 
B 2 181 LEU 181 181 181 LEU LEU B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 SER 183 183 183 SER SER B . n 
B 2 184 LEU 184 184 184 LEU LEU B . n 
B 2 185 SER 185 185 185 SER SER B . n 
B 2 186 SER 186 186 186 SER SER B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 THR 189 189 189 THR THR B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 PRO 191 191 191 PRO PRO B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 SER 194 194 194 SER SER B . n 
B 2 195 LEU 195 195 195 LEU LEU B . n 
B 2 196 GLY 196 196 196 GLY GLY B . n 
B 2 197 THR 197 197 197 THR THR B . n 
B 2 198 GLN 198 198 198 GLN GLN B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 ILE 201 201 201 ILE ILE B . n 
B 2 202 CYS 202 202 202 CYS CYS B . n 
B 2 203 ASN 203 203 203 ASN ASN B . n 
B 2 204 VAL 204 204 204 VAL VAL B . n 
B 2 205 ASN 205 205 205 ASN ASN B . n 
B 2 206 HIS 206 206 206 HIS HIS B . n 
B 2 207 LYS 207 207 207 LYS LYS B . n 
B 2 208 PRO 208 208 208 PRO PRO B . n 
B 2 209 SER 209 209 209 SER SER B . n 
B 2 210 ASN 210 210 210 ASN ASN B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 VAL 213 213 213 VAL VAL B . n 
B 2 214 ASP 214 214 214 ASP ASP B . n 
B 2 215 LYS 215 215 215 LYS LYS B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 GLU 218 218 218 GLU GLU B . n 
B 2 219 PRO 219 219 219 PRO PRO B . n 
B 2 220 LYS 220 220 220 LYS LYS B . n 
B 2 221 SER 221 221 221 SER SER B . n 
B 2 222 CYS 222 222 222 CYS CYS B . n 
B 2 223 GLY 223 223 223 GLY GLY B . n 
B 2 224 GLY 224 224 ?   ?   ?   B . n 
B 2 225 HIS 225 225 ?   ?   ?   B . n 
B 2 226 HIS 226 226 ?   ?   ?   B . n 
B 2 227 HIS 227 227 ?   ?   ?   B . n 
B 2 228 HIS 228 228 ?   ?   ?   B . n 
B 2 229 HIS 229 229 ?   ?   ?   B . n 
B 2 230 HIS 230 230 ?   ?   ?   B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   ILE 2   2   2   ILE ILE C . n 
C 1 3   GLN 3   3   3   GLN GLN C . n 
C 1 4   MET 4   4   4   MET MET C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   GLN 6   6   6   GLN GLN C . n 
C 1 7   SER 7   7   7   SER SER C . n 
C 1 8   PRO 8   8   8   PRO PRO C . n 
C 1 9   SER 9   9   9   SER SER C . n 
C 1 10  SER 10  10  10  SER SER C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  SER 12  12  12  SER SER C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  VAL 15  15  15  VAL VAL C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ASP 17  17  17  ASP ASP C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  THR 20  20  20  THR THR C . n 
C 1 21  ILE 21  21  21  ILE ILE C . n 
C 1 22  THR 22  22  22  THR THR C . n 
C 1 23  CYS 23  23  23  CYS CYS C . n 
C 1 24  GLN 24  24  24  GLN GLN C . n 
C 1 25  ALA 25  25  25  ALA ALA C . n 
C 1 26  SER 26  26  26  SER SER C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  ILE 29  29  29  ILE ILE C . n 
C 1 30  SER 30  30  30  SER SER C . n 
C 1 31  ASN 31  31  31  ASN ASN C . n 
C 1 32  GLN 32  32  32  GLN GLN C . n 
C 1 33  LEU 33  33  33  LEU LEU C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  TRP 35  35  35  TRP TRP C . n 
C 1 36  TYR 36  36  36  TYR TYR C . n 
C 1 37  GLN 37  37  37  GLN GLN C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  LYS 45  45  45  LYS LYS C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ILE 48  48  48  ILE ILE C . n 
C 1 49  TYR 49  49  49  TYR TYR C . n 
C 1 50  ASP 50  50  50  ASP ASP C . n 
C 1 51  ALA 51  51  51  ALA ALA C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  SER 53  53  53  SER SER C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  VAL 58  58  58  VAL VAL C . n 
C 1 59  PRO 59  59  59  PRO PRO C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  ARG 61  61  61  ARG ARG C . n 
C 1 62  PHE 62  62  62  PHE PHE C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  SER 65  65  65  SER SER C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  THR 69  69  69  THR THR C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  PHE 71  71  71  PHE PHE C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  LEU 73  73  73  LEU LEU C . n 
C 1 74  THR 74  74  74  THR THR C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  SER 77  77  77  SER SER C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  PRO 80  80  80  PRO PRO C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  PHE 83  83  83  PHE PHE C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  THR 85  85  85  THR THR C . n 
C 1 86  TYR 86  86  86  TYR TYR C . n 
C 1 87  TYR 87  87  87  TYR TYR C . n 
C 1 88  CYS 88  88  88  CYS CYS C . n 
C 1 89  LEU 89  89  89  LEU LEU C . n 
C 1 90  GLY 90  90  90  GLY GLY C . n 
C 1 91  ILE 91  91  91  ILE ILE C . n 
C 1 92  TYR 92  92  92  TYR TYR C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  ASP 94  94  94  ASP ASP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ALA 96  96  96  ALA ALA C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  ASP 98  98  98  ASP ASP C . n 
C 1 99  GLY 99  99  99  GLY GLY C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 ALA 101 101 101 ALA ALA C . n 
C 1 102 PHE 102 102 102 PHE PHE C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 GLY 105 105 105 GLY GLY C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 LYS 107 107 107 LYS LYS C . n 
C 1 108 VAL 108 108 108 VAL VAL C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 ILE 110 110 110 ILE ILE C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 ARG 112 112 112 ARG ARG C . n 
C 1 113 THR 113 113 113 THR THR C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 ALA 116 116 116 ALA ALA C . n 
C 1 117 PRO 117 117 117 PRO PRO C . n 
C 1 118 SER 118 118 118 SER SER C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 PHE 120 120 120 PHE PHE C . n 
C 1 121 ILE 121 121 121 ILE ILE C . n 
C 1 122 PHE 122 122 122 PHE PHE C . n 
C 1 123 PRO 123 123 123 PRO PRO C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 SER 125 125 125 SER SER C . n 
C 1 126 ASP 126 126 126 ASP ASP C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 GLN 128 128 128 GLN GLN C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 LYS 130 130 130 LYS LYS C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 GLY 132 132 132 GLY GLY C . n 
C 1 133 THR 133 133 133 THR THR C . n 
C 1 134 ALA 134 134 134 ALA ALA C . n 
C 1 135 SER 135 135 135 SER SER C . n 
C 1 136 VAL 136 136 136 VAL VAL C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 CYS 138 138 138 CYS CYS C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 LEU 140 140 140 LEU LEU C . n 
C 1 141 ASN 141 141 141 ASN ASN C . n 
C 1 142 ASN 142 142 142 ASN ASN C . n 
C 1 143 PHE 143 143 143 PHE PHE C . n 
C 1 144 TYR 144 144 144 TYR TYR C . n 
C 1 145 PRO 145 145 145 PRO PRO C . n 
C 1 146 ARG 146 146 146 ARG ARG C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 ALA 148 148 148 ALA ALA C . n 
C 1 149 LYS 149 149 149 LYS LYS C . n 
C 1 150 VAL 150 150 150 VAL VAL C . n 
C 1 151 GLN 151 151 151 GLN GLN C . n 
C 1 152 TRP 152 152 152 TRP TRP C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 VAL 154 154 154 VAL VAL C . n 
C 1 155 ASP 155 155 155 ASP ASP C . n 
C 1 156 ASN 156 156 156 ASN ASN C . n 
C 1 157 ALA 157 157 157 ALA ALA C . n 
C 1 158 LEU 158 158 158 LEU LEU C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 GLY 161 161 161 GLY GLY C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 GLN 164 164 164 GLN GLN C . n 
C 1 165 GLU 165 165 165 GLU GLU C . n 
C 1 166 SER 166 166 166 SER SER C . n 
C 1 167 VAL 167 167 167 VAL VAL C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 GLU 169 169 169 GLU GLU C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 ASP 171 171 171 ASP ASP C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 ASP 174 174 174 ASP ASP C . n 
C 1 175 SER 175 175 175 SER SER C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 TYR 177 177 177 TYR TYR C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 LEU 179 179 179 LEU LEU C . n 
C 1 180 SER 180 180 180 SER SER C . n 
C 1 181 SER 181 181 181 SER SER C . n 
C 1 182 THR 182 182 182 THR THR C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 THR 184 184 184 THR THR C . n 
C 1 185 LEU 185 185 185 LEU LEU C . n 
C 1 186 SER 186 186 186 SER SER C . n 
C 1 187 LYS 187 187 187 LYS LYS C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 ASP 189 189 189 ASP ASP C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 GLU 191 191 191 GLU GLU C . n 
C 1 192 LYS 192 192 192 LYS LYS C . n 
C 1 193 HIS 193 193 193 HIS HIS C . n 
C 1 194 LYS 194 194 194 LYS LYS C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 TYR 196 196 196 TYR TYR C . n 
C 1 197 ALA 197 197 197 ALA ALA C . n 
C 1 198 CYS 198 198 198 CYS CYS C . n 
C 1 199 GLU 199 199 199 GLU GLU C . n 
C 1 200 VAL 200 200 200 VAL VAL C . n 
C 1 201 THR 201 201 201 THR THR C . n 
C 1 202 GLN 202 202 202 GLN GLN C . n 
C 1 203 GLY 203 203 203 GLY GLY C . n 
C 1 204 THR 204 204 204 THR THR C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 SER 206 206 206 SER SER C . n 
C 1 207 VAL 207 207 207 VAL VAL C . n 
C 1 208 THR 208 208 208 THR THR C . n 
C 1 209 LYS 209 209 209 LYS LYS C . n 
C 1 210 SER 210 210 210 SER SER C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ASN 212 212 212 ASN ASN C . n 
C 1 213 ARG 213 213 213 ARG ARG C . n 
C 1 214 GLY 214 214 214 GLY GLY C . n 
C 1 215 GLU 215 215 215 GLU GLU C . n 
C 1 216 CYS 216 216 216 CYS CYS C . n 
D 2 1   GLU 1   1   1   GLU GLU D . n 
D 2 2   VAL 2   2   2   VAL VAL D . n 
D 2 3   GLN 3   3   3   GLN GLN D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   VAL 5   5   5   VAL VAL D . n 
D 2 6   GLU 6   6   6   GLU GLU D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   GLY 9   9   9   GLY GLY D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  LEU 11  11  11  LEU LEU D . n 
D 2 12  VAL 12  12  12  VAL VAL D . n 
D 2 13  GLN 13  13  13  GLN GLN D . n 
D 2 14  PRO 14  14  14  PRO PRO D . n 
D 2 15  GLY 15  15  15  GLY GLY D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  SER 17  17  17  SER SER D . n 
D 2 18  LEU 18  18  18  LEU LEU D . n 
D 2 19  ARG 19  19  19  ARG ARG D . n 
D 2 20  LEU 20  20  20  LEU LEU D . n 
D 2 21  SER 21  21  21  SER SER D . n 
D 2 22  CYS 22  22  22  CYS CYS D . n 
D 2 23  ALA 23  23  23  ALA ALA D . n 
D 2 24  ALA 24  24  24  ALA ALA D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  GLY 26  26  26  GLY GLY D . n 
D 2 27  PHE 27  27  27  PHE PHE D . n 
D 2 28  SER 28  28  28  SER SER D . n 
D 2 29  LEU 29  29  29  LEU LEU D . n 
D 2 30  SER 30  30  30  SER SER D . n 
D 2 31  SER 31  31  31  SER SER D . n 
D 2 32  TYR 32  32  32  TYR TYR D . n 
D 2 33  TYR 33  33  33  TYR TYR D . n 
D 2 34  MET 34  34  34  MET MET D . n 
D 2 35  THR 35  35  35  THR THR D . n 
D 2 36  TRP 36  36  36  TRP TRP D . n 
D 2 37  VAL 37  37  37  VAL VAL D . n 
D 2 38  ARG 38  38  38  ARG ARG D . n 
D 2 39  GLN 39  39  39  GLN GLN D . n 
D 2 40  ALA 40  40  40  ALA ALA D . n 
D 2 41  PRO 41  41  41  PRO PRO D . n 
D 2 42  GLY 42  42  42  GLY GLY D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  GLY 44  44  44  GLY GLY D . n 
D 2 45  LEU 45  45  45  LEU LEU D . n 
D 2 46  GLU 46  46  46  GLU GLU D . n 
D 2 47  TRP 47  47  47  TRP TRP D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  SER 49  49  49  SER SER D . n 
D 2 50  VAL 50  50  50  VAL VAL D . n 
D 2 51  ILE 51  51  51  ILE ILE D . n 
D 2 52  ASN 52  52  52  ASN ASN D . n 
D 2 53  VAL 53  53  53  VAL VAL D . n 
D 2 54  TYR 54  54  54  TYR TYR D . n 
D 2 55  GLY 55  55  55  GLY GLY D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  THR 57  57  57  THR THR D . n 
D 2 58  TYR 58  58  58  TYR TYR D . n 
D 2 59  TYR 59  59  59  TYR TYR D . n 
D 2 60  ALA 60  60  60  ALA ALA D . n 
D 2 61  SER 61  61  61  SER SER D . n 
D 2 62  TRP 62  62  62  TRP TRP D . n 
D 2 63  ALA 63  63  63  ALA ALA D . n 
D 2 64  LYS 64  64  64  LYS LYS D . n 
D 2 65  GLY 65  65  65  GLY GLY D . n 
D 2 66  ARG 66  66  66  ARG ARG D . n 
D 2 67  PHE 67  67  67  PHE PHE D . n 
D 2 68  THR 68  68  68  THR THR D . n 
D 2 69  ILE 69  69  69  ILE ILE D . n 
D 2 70  SER 70  70  70  SER SER D . n 
D 2 71  ARG 71  71  71  ARG ARG D . n 
D 2 72  ASP 72  72  72  ASP ASP D . n 
D 2 73  ASN 73  73  73  ASN ASN D . n 
D 2 74  SER 74  74  74  SER SER D . n 
D 2 75  LYS 75  75  75  LYS LYS D . n 
D 2 76  ASN 76  76  76  ASN ASN D . n 
D 2 77  THR 77  77  77  THR THR D . n 
D 2 78  LEU 78  78  78  LEU LEU D . n 
D 2 79  TYR 79  79  79  TYR TYR D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  GLN 81  81  81  GLN GLN D . n 
D 2 82  MET 82  82  82  MET MET D . n 
D 2 83  ASN 83  83  83  ASN ASN D . n 
D 2 84  SER 84  84  84  SER SER D . n 
D 2 85  LEU 85  85  85  LEU LEU D . n 
D 2 86  ARG 86  86  86  ARG ARG D . n 
D 2 87  ALA 87  87  87  ALA ALA D . n 
D 2 88  GLU 88  88  88  GLU GLU D . n 
D 2 89  ASP 89  89  89  ASP ASP D . n 
D 2 90  THR 90  90  90  THR THR D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  VAL 92  92  92  VAL VAL D . n 
D 2 93  TYR 93  93  93  TYR TYR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  CYS 95  95  95  CYS CYS D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  ARG 97  97  97  ARG ARG D . n 
D 2 98  GLU 98  98  98  GLU GLU D . n 
D 2 99  ASP 99  99  99  ASP ASP D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 ALA 101 101 101 ALA ALA D . n 
D 2 102 VAL 102 102 102 VAL VAL D . n 
D 2 103 TYR 103 103 103 TYR TYR D . n 
D 2 104 MET 104 104 104 MET MET D . n 
D 2 105 ALA 105 105 105 ALA ALA D . n 
D 2 106 ILE 106 106 106 ILE ILE D . n 
D 2 107 ASP 107 107 107 ASP ASP D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 TRP 109 109 109 TRP TRP D . n 
D 2 110 GLY 110 110 110 GLY GLY D . n 
D 2 111 GLN 111 111 111 GLN GLN D . n 
D 2 112 GLY 112 112 112 GLY GLY D . n 
D 2 113 THR 113 113 113 THR THR D . n 
D 2 114 LEU 114 114 114 LEU LEU D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 THR 116 116 116 THR THR D . n 
D 2 117 VAL 117 117 117 VAL VAL D . n 
D 2 118 SER 118 118 118 SER SER D . n 
D 2 119 SER 119 119 119 SER SER D . n 
D 2 120 ALA 120 120 120 ALA ALA D . n 
D 2 121 SER 121 121 121 SER SER D . n 
D 2 122 THR 122 122 122 THR THR D . n 
D 2 123 LYS 123 123 123 LYS LYS D . n 
D 2 124 GLY 124 124 124 GLY GLY D . n 
D 2 125 PRO 125 125 125 PRO PRO D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 VAL 127 127 127 VAL VAL D . n 
D 2 128 PHE 128 128 128 PHE PHE D . n 
D 2 129 PRO 129 129 129 PRO PRO D . n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 ALA 131 131 131 ALA ALA D . n 
D 2 132 PRO 132 132 132 PRO PRO D . n 
D 2 133 SER 133 133 133 SER SER D . n 
D 2 134 SER 134 134 134 SER SER D . n 
D 2 135 LYS 135 135 135 LYS LYS D . n 
D 2 136 SER 136 136 ?   ?   ?   D . n 
D 2 137 THR 137 137 ?   ?   ?   D . n 
D 2 138 SER 138 138 ?   ?   ?   D . n 
D 2 139 GLY 139 139 139 GLY GLY D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 THR 141 141 141 THR THR D . n 
D 2 142 ALA 142 142 142 ALA ALA D . n 
D 2 143 ALA 143 143 143 ALA ALA D . n 
D 2 144 LEU 144 144 144 LEU LEU D . n 
D 2 145 GLY 145 145 145 GLY GLY D . n 
D 2 146 CYS 146 146 146 CYS CYS D . n 
D 2 147 LEU 147 147 147 LEU LEU D . n 
D 2 148 VAL 148 148 148 VAL VAL D . n 
D 2 149 LYS 149 149 149 LYS LYS D . n 
D 2 150 ASP 150 150 150 ASP ASP D . n 
D 2 151 TYR 151 151 151 TYR TYR D . n 
D 2 152 PHE 152 152 152 PHE PHE D . n 
D 2 153 PRO 153 153 153 PRO PRO D . n 
D 2 154 GLU 154 154 154 GLU GLU D . n 
D 2 155 PRO 155 155 155 PRO PRO D . n 
D 2 156 VAL 156 156 156 VAL VAL D . n 
D 2 157 THR 157 157 157 THR THR D . n 
D 2 158 VAL 158 158 158 VAL VAL D . n 
D 2 159 SER 159 159 159 SER SER D . n 
D 2 160 TRP 160 160 160 TRP TRP D . n 
D 2 161 ASN 161 161 161 ASN ASN D . n 
D 2 162 SER 162 162 162 SER SER D . n 
D 2 163 GLY 163 163 163 GLY GLY D . n 
D 2 164 ALA 164 164 164 ALA ALA D . n 
D 2 165 LEU 165 165 165 LEU LEU D . n 
D 2 166 THR 166 166 166 THR THR D . n 
D 2 167 SER 167 167 167 SER SER D . n 
D 2 168 GLY 168 168 168 GLY GLY D . n 
D 2 169 VAL 169 169 169 VAL VAL D . n 
D 2 170 HIS 170 170 170 HIS HIS D . n 
D 2 171 THR 171 171 171 THR THR D . n 
D 2 172 PHE 172 172 172 PHE PHE D . n 
D 2 173 PRO 173 173 173 PRO PRO D . n 
D 2 174 ALA 174 174 174 ALA ALA D . n 
D 2 175 VAL 175 175 175 VAL VAL D . n 
D 2 176 LEU 176 176 176 LEU LEU D . n 
D 2 177 GLN 177 177 177 GLN GLN D . n 
D 2 178 SER 178 178 178 SER SER D . n 
D 2 179 SER 179 179 179 SER SER D . n 
D 2 180 GLY 180 180 180 GLY GLY D . n 
D 2 181 LEU 181 181 181 LEU LEU D . n 
D 2 182 TYR 182 182 182 TYR TYR D . n 
D 2 183 SER 183 183 183 SER SER D . n 
D 2 184 LEU 184 184 184 LEU LEU D . n 
D 2 185 SER 185 185 185 SER SER D . n 
D 2 186 SER 186 186 186 SER SER D . n 
D 2 187 VAL 187 187 187 VAL VAL D . n 
D 2 188 VAL 188 188 188 VAL VAL D . n 
D 2 189 THR 189 189 189 THR THR D . n 
D 2 190 VAL 190 190 190 VAL VAL D . n 
D 2 191 PRO 191 191 191 PRO PRO D . n 
D 2 192 SER 192 192 192 SER SER D . n 
D 2 193 SER 193 193 193 SER SER D . n 
D 2 194 SER 194 194 194 SER SER D . n 
D 2 195 LEU 195 195 195 LEU LEU D . n 
D 2 196 GLY 196 196 196 GLY GLY D . n 
D 2 197 THR 197 197 197 THR THR D . n 
D 2 198 GLN 198 198 198 GLN GLN D . n 
D 2 199 THR 199 199 199 THR THR D . n 
D 2 200 TYR 200 200 200 TYR TYR D . n 
D 2 201 ILE 201 201 201 ILE ILE D . n 
D 2 202 CYS 202 202 202 CYS CYS D . n 
D 2 203 ASN 203 203 203 ASN ASN D . n 
D 2 204 VAL 204 204 204 VAL VAL D . n 
D 2 205 ASN 205 205 205 ASN ASN D . n 
D 2 206 HIS 206 206 206 HIS HIS D . n 
D 2 207 LYS 207 207 207 LYS LYS D . n 
D 2 208 PRO 208 208 208 PRO PRO D . n 
D 2 209 SER 209 209 209 SER SER D . n 
D 2 210 ASN 210 210 210 ASN ASN D . n 
D 2 211 THR 211 211 211 THR THR D . n 
D 2 212 LYS 212 212 212 LYS LYS D . n 
D 2 213 VAL 213 213 213 VAL VAL D . n 
D 2 214 ASP 214 214 214 ASP ASP D . n 
D 2 215 LYS 215 215 215 LYS LYS D . n 
D 2 216 LYS 216 216 216 LYS LYS D . n 
D 2 217 VAL 217 217 217 VAL VAL D . n 
D 2 218 GLU 218 218 218 GLU GLU D . n 
D 2 219 PRO 219 219 219 PRO PRO D . n 
D 2 220 LYS 220 220 220 LYS LYS D . n 
D 2 221 SER 221 221 221 SER SER D . n 
D 2 222 CYS 222 222 222 CYS CYS D . n 
D 2 223 GLY 223 223 223 GLY GLY D . n 
D 2 224 GLY 224 224 ?   ?   ?   D . n 
D 2 225 HIS 225 225 ?   ?   ?   D . n 
D 2 226 HIS 226 226 ?   ?   ?   D . n 
D 2 227 HIS 227 227 ?   ?   ?   D . n 
D 2 228 HIS 228 228 ?   ?   ?   D . n 
D 2 229 HIS 229 229 ?   ?   ?   D . n 
D 2 230 HIS 230 230 ?   ?   ?   D . n 
# 
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   ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.96 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y2K 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.748 
_cell.length_a_esd                 ? 
_cell.length_b                     137.496 
_cell.length_b_esd                 ? 
_cell.length_c                     73.723 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8Y2K 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8Y2K 
_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             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'EVAPORATION, RECRYSTALLIZATION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.2 M potassium sodium tartrate tetrahydrate pH 4.5, 20%(w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR CCD 130 mm' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-03 
_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   0.979 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          60.7 
_reflns.entry_id                                       8Y2K 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.85 
_reflns.d_resolution_low                               50 
_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                                     21423 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.9 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.85 
_reflns_shell.d_res_low                                     2.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2170 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  1 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               ? 
_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                                 8Y2K 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.87 
_refine.ls_d_res_low                             47.63 
_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                     21335 
_refine.ls_number_reflns_R_free                  1005 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.14 
_refine.ls_percent_reflns_R_free                 4.71 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2174 
_refine.ls_R_factor_R_free                       0.2684 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2150 
_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                          1.38 
_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       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 31.68 
_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                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.87 
_refine_hist.d_res_low                        47.63 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6558 
_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        6558 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 6695 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.707  ? 9099 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.217 ? 2382 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 1038 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1159 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.87 3.02  . . 133 2861 96.00  . . . . 0.3224 . . . . . . . . . . . 0.4204 
'X-RAY DIFFRACTION' 3.02 3.21  . . 167 2855 98.00  . . . . 0.2735 . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 3.21 3.46  . . 143 2917 100.00 . . . . 0.2571 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 3.46 3.81  . . 134 2930 99.00  . . . . 0.2363 . . . . . . . . . . . 0.3034 
'X-RAY DIFFRACTION' 3.81 4.36  . . 152 2903 98.00  . . . . 0.2037 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 4.36 5.49  . . 137 2914 99.00  . . . . 0.1771 . . . . . . . . . . . 0.2201 
'X-RAY DIFFRACTION' 5.49 47.63 . . 139 2950 98.00  . . . . 0.1872 . . . . . . . . . . . 0.2209 
# 
_struct.entry_id                     8Y2K 
_struct.title                        'The crystal structure of QX006N-Fab' 
_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        8Y2K 
_struct_keywords.text            'therapeutic monoclonal antibody, QX006N, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 1 ? 
D N N 2 ? 
# 
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 PDB 8Y2K 8Y2K ? 1 ? 1 
2 PDB 8Y2K 8Y2K ? 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 8Y2K A 1 ? 216 ? 8Y2K 1 ? 216 ? 1 216 
2 2 8Y2K B 1 ? 230 ? 8Y2K 1 ? 230 ? 1 230 
3 1 8Y2K C 1 ? 216 ? 8Y2K 1 ? 216 ? 1 216 
4 2 8Y2K D 1 ? 230 ? 8Y2K 1 ? 230 ? 1 230 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3610  ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  19750 ? 
2 'ABSA (A^2)' 3750  ? 
2 MORE         -27   ? 
2 'SSA (A^2)'  19980 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B 
2 1 C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 GLN A 79  ? PHE A 83  ? GLN A 79  PHE A 83  5 ? 5 
HELX_P HELX_P2  AA2 SER A 125 ? LYS A 130 ? SER A 125 LYS A 130 1 ? 6 
HELX_P HELX_P3  AA3 LYS A 187 ? LYS A 192 ? LYS A 187 LYS A 192 1 ? 6 
HELX_P HELX_P4  AA4 SER B 28  ? TYR B 32  ? SER B 28  TYR B 32  5 ? 5 
HELX_P HELX_P5  AA5 ARG B 86  ? THR B 90  ? ARG B 86  THR B 90  5 ? 5 
HELX_P HELX_P6  AA6 SER B 162 ? ALA B 164 ? SER B 162 ALA B 164 5 ? 3 
HELX_P HELX_P7  AA7 SER B 193 ? LEU B 195 ? SER B 193 LEU B 195 5 ? 3 
HELX_P HELX_P8  AA8 LYS B 207 ? ASN B 210 ? LYS B 207 ASN B 210 5 ? 4 
HELX_P HELX_P9  AA9 SER C 125 ? LYS C 130 ? SER C 125 LYS C 130 1 ? 6 
HELX_P HELX_P10 AB1 LYS C 187 ? LYS C 192 ? LYS C 187 LYS C 192 1 ? 6 
HELX_P HELX_P11 AB2 SER D 28  ? TYR D 32  ? SER D 28  TYR D 32  5 ? 5 
HELX_P HELX_P12 AB3 ARG D 86  ? THR D 90  ? ARG D 86  THR D 90  5 ? 5 
HELX_P HELX_P13 AB4 SER D 162 ? ALA D 164 ? SER D 162 ALA D 164 5 ? 3 
HELX_P HELX_P14 AB5 SER D 193 ? LEU D 195 ? SER D 193 LEU D 195 5 ? 3 
HELX_P HELX_P15 AB6 LYS D 207 ? ASN D 210 ? LYS D 207 ASN D 210 5 ? 4 
# 
_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 23  SG ? ? ? 1_555 A CYS 88  SG ? ? A CYS 23  A CYS 88  1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf2 disulf ? ? A CYS 138 SG ? ? ? 1_555 A CYS 198 SG ? ? A CYS 138 A CYS 198 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3 disulf ? ? A CYS 216 SG ? ? ? 1_555 B CYS 222 SG ? ? A CYS 216 B CYS 222 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf4 disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 95  SG ? ? B CYS 22  B CYS 95  1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf5 disulf ? ? B CYS 146 SG ? ? ? 1_555 B CYS 202 SG ? ? B CYS 146 B CYS 202 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf6 disulf ? ? C CYS 23  SG ? ? ? 1_555 C CYS 88  SG ? ? C CYS 23  C CYS 88  1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf7 disulf ? ? C CYS 138 SG ? ? ? 1_555 C CYS 198 SG ? ? C CYS 138 C CYS 198 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf8 disulf ? ? D CYS 22  SG ? ? ? 1_555 D CYS 95  SG ? ? D CYS 22  D CYS 95  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf9 disulf ? ? D CYS 146 SG ? ? ? 1_555 D CYS 202 SG ? ? D CYS 146 D CYS 202 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 CYS A 23  ? CYS A 88  ? CYS A 23  ? 1_555 CYS A 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 138 ? CYS A 198 ? CYS A 138 ? 1_555 CYS A 198 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 216 ? CYS B 222 ? CYS A 216 ? 1_555 CYS B 222 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 22  ? CYS B 95  ? CYS B 22  ? 1_555 CYS B 95  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS B 146 ? CYS B 202 ? CYS B 146 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS C 23  ? CYS C 88  ? CYS C 23  ? 1_555 CYS C 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS C 138 ? CYS C 198 ? CYS C 138 ? 1_555 CYS C 198 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8 CYS D 22  ? CYS D 95  ? CYS D 22  ? 1_555 CYS D 95  ? 1_555 SG SG . . . None 'Disulfide bridge' 
9 CYS D 146 ? CYS D 202 ? CYS D 146 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 7   A . ? SER 7   A PRO 8   A ? PRO 8   A 1 -4.90 
2 TYR 144 A . ? TYR 144 A PRO 145 A ? PRO 145 A 1 1.97  
3 PHE 152 B . ? PHE 152 B PRO 153 B ? PRO 153 B 1 -2.36 
4 GLU 154 B . ? GLU 154 B PRO 155 B ? PRO 155 B 1 3.31  
5 SER 7   C . ? SER 7   C PRO 8   C ? PRO 8   C 1 -5.49 
6 TYR 144 C . ? TYR 144 C PRO 145 C ? PRO 145 C 1 2.35  
7 PHE 152 D . ? PHE 152 D PRO 153 D ? PRO 153 D 1 -3.71 
8 GLU 154 D . ? GLU 154 D PRO 155 D ? PRO 155 D 1 3.02  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? 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 MET A 4   ? SER A 7   ? MET A 4   SER A 7   
AA1 2 VAL A 19  ? ALA A 25  ? VAL A 19  ALA A 25  
AA1 3 LYS A 70  ? ILE A 75  ? LYS A 70  ILE A 75  
AA1 4 PHE A 62  ? SER A 67  ? PHE A 62  SER A 67  
AA2 1 SER A 10  ? SER A 14  ? SER A 10  SER A 14  
AA2 2 THR A 106 ? LYS A 111 ? THR A 106 LYS A 111 
AA2 3 ALA A 84  ? ILE A 91  ? ALA A 84  ILE A 91  
AA2 4 LEU A 33  ? GLN A 38  ? LEU A 33  GLN A 38  
AA2 5 LYS A 45  ? TYR A 49  ? LYS A 45  TYR A 49  
AA2 6 SER A 53  ? LEU A 54  ? SER A 53  LEU A 54  
AA3 1 SER A 10  ? SER A 14  ? SER A 10  SER A 14  
AA3 2 THR A 106 ? LYS A 111 ? THR A 106 LYS A 111 
AA3 3 ALA A 84  ? ILE A 91  ? ALA A 84  ILE A 91  
AA3 4 ILE A 100 ? PHE A 102 ? ILE A 100 PHE A 102 
AA4 1 SER A 118 ? PHE A 122 ? SER A 118 PHE A 122 
AA4 2 THR A 133 ? PHE A 143 ? THR A 133 PHE A 143 
AA4 3 TYR A 177 ? SER A 186 ? TYR A 177 SER A 186 
AA4 4 SER A 163 ? VAL A 167 ? SER A 163 VAL A 167 
AA5 1 ALA A 157 ? GLN A 159 ? ALA A 157 GLN A 159 
AA5 2 LYS A 149 ? VAL A 154 ? LYS A 149 VAL A 154 
AA5 3 VAL A 195 ? GLN A 202 ? VAL A 195 GLN A 202 
AA5 4 THR A 205 ? ASN A 212 ? THR A 205 ASN A 212 
AA6 1 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA6 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA6 3 THR B 77  ? MET B 82  ? THR B 77  MET B 82  
AA6 4 PHE B 67  ? ASP B 72  ? PHE B 67  ASP B 72  
AA7 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA7 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA7 3 ALA B 91  ? ASP B 99  ? ALA B 91  ASP B 99  
AA7 4 TYR B 33  ? GLN B 39  ? TYR B 33  GLN B 39  
AA7 5 LEU B 45  ? ILE B 51  ? LEU B 45  ILE B 51  
AA7 6 THR B 57  ? TYR B 59  ? THR B 57  TYR B 59  
AA8 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA8 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA8 3 ALA B 91  ? ASP B 99  ? ALA B 91  ASP B 99  
AA8 4 ALA B 105 ? TRP B 109 ? ALA B 105 TRP B 109 
AA9 1 SER B 126 ? LEU B 130 ? SER B 126 LEU B 130 
AA9 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AA9 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AA9 4 VAL B 169 ? THR B 171 ? VAL B 169 THR B 171 
AB1 1 SER B 126 ? LEU B 130 ? SER B 126 LEU B 130 
AB1 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AB1 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AB1 4 VAL B 175 ? LEU B 176 ? VAL B 175 LEU B 176 
AB2 1 THR B 157 ? TRP B 160 ? THR B 157 TRP B 160 
AB2 2 TYR B 200 ? HIS B 206 ? TYR B 200 HIS B 206 
AB2 3 THR B 211 ? VAL B 217 ? THR B 211 VAL B 217 
AB3 1 MET C 4   ? SER C 7   ? MET C 4   SER C 7   
AB3 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AB3 3 LYS C 70  ? ILE C 75  ? LYS C 70  ILE C 75  
AB3 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AB4 1 SER C 10  ? ALA C 13  ? SER C 10  ALA C 13  
AB4 2 THR C 106 ? ILE C 110 ? THR C 106 ILE C 110 
AB4 3 THR C 85  ? ILE C 91  ? THR C 85  ILE C 91  
AB4 4 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AB4 5 LYS C 45  ? TYR C 49  ? LYS C 45  TYR C 49  
AB4 6 SER C 53  ? LEU C 54  ? SER C 53  LEU C 54  
AB5 1 SER C 10  ? ALA C 13  ? SER C 10  ALA C 13  
AB5 2 THR C 106 ? ILE C 110 ? THR C 106 ILE C 110 
AB5 3 THR C 85  ? ILE C 91  ? THR C 85  ILE C 91  
AB5 4 ILE C 100 ? PHE C 102 ? ILE C 100 PHE C 102 
AB6 1 SER C 118 ? PHE C 122 ? SER C 118 PHE C 122 
AB6 2 THR C 133 ? PHE C 143 ? THR C 133 PHE C 143 
AB6 3 TYR C 177 ? SER C 186 ? TYR C 177 SER C 186 
AB6 4 SER C 163 ? VAL C 167 ? SER C 163 VAL C 167 
AB7 1 ALA C 157 ? LEU C 158 ? ALA C 157 LEU C 158 
AB7 2 LYS C 149 ? VAL C 154 ? LYS C 149 VAL C 154 
AB7 3 VAL C 195 ? GLN C 202 ? VAL C 195 GLN C 202 
AB7 4 THR C 205 ? ASN C 212 ? THR C 205 ASN C 212 
AB8 1 GLN D 3   ? SER D 7   ? GLN D 3   SER D 7   
AB8 2 LEU D 18  ? SER D 25  ? LEU D 18  SER D 25  
AB8 3 THR D 77  ? MET D 82  ? THR D 77  MET D 82  
AB8 4 PHE D 67  ? ASP D 72  ? PHE D 67  ASP D 72  
AB9 1 LEU D 11  ? VAL D 12  ? LEU D 11  VAL D 12  
AB9 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AB9 3 ALA D 91  ? ASP D 99  ? ALA D 91  ASP D 99  
AB9 4 TYR D 33  ? GLN D 39  ? TYR D 33  GLN D 39  
AB9 5 LEU D 45  ? ILE D 51  ? LEU D 45  ILE D 51  
AB9 6 THR D 57  ? TYR D 59  ? THR D 57  TYR D 59  
AC1 1 LEU D 11  ? VAL D 12  ? LEU D 11  VAL D 12  
AC1 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AC1 3 ALA D 91  ? ASP D 99  ? ALA D 91  ASP D 99  
AC1 4 ALA D 105 ? TRP D 109 ? ALA D 105 TRP D 109 
AC2 1 SER D 126 ? LEU D 130 ? SER D 126 LEU D 130 
AC2 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC2 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC2 4 VAL D 169 ? THR D 171 ? VAL D 169 THR D 171 
AC3 1 SER D 126 ? LEU D 130 ? SER D 126 LEU D 130 
AC3 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC3 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC3 4 VAL D 175 ? LEU D 176 ? VAL D 175 LEU D 176 
AC4 1 THR D 157 ? TRP D 160 ? THR D 157 TRP D 160 
AC4 2 TYR D 200 ? HIS D 206 ? TYR D 200 HIS D 206 
AC4 3 THR D 211 ? VAL D 217 ? THR D 211 VAL D 217 
# 
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 SER A 7   ? N SER A 7   O THR A 22  ? O THR A 22  
AA1 2 3 N CYS A 23  ? N CYS A 23  O PHE A 71  ? O PHE A 71  
AA1 3 4 O THR A 74  ? O THR A 74  N SER A 63  ? N SER A 63  
AA2 1 2 N ALA A 13  ? N ALA A 13  O LYS A 111 ? O LYS A 111 
AA2 2 3 O VAL A 108 ? O VAL A 108 N ALA A 84  ? N ALA A 84  
AA2 3 4 O TYR A 87  ? O TYR A 87  N TYR A 36  ? N TYR A 36  
AA2 4 5 N TRP A 35  ? N TRP A 35  O LEU A 47  ? O LEU A 47  
AA2 5 6 N TYR A 49  ? N TYR A 49  O SER A 53  ? O SER A 53  
AA3 1 2 N ALA A 13  ? N ALA A 13  O LYS A 111 ? O LYS A 111 
AA3 2 3 O VAL A 108 ? O VAL A 108 N ALA A 84  ? N ALA A 84  
AA3 3 4 N GLY A 90  ? N GLY A 90  O ALA A 101 ? O ALA A 101 
AA4 1 2 N PHE A 122 ? N PHE A 122 O VAL A 137 ? O VAL A 137 
AA4 2 3 N VAL A 136 ? N VAL A 136 O LEU A 183 ? O LEU A 183 
AA4 3 4 O THR A 182 ? O THR A 182 N GLN A 164 ? N GLN A 164 
AA5 1 2 O GLN A 159 ? O GLN A 159 N TRP A 152 ? N TRP A 152 
AA5 2 3 N LYS A 153 ? N LYS A 153 O ALA A 197 ? O ALA A 197 
AA5 3 4 N TYR A 196 ? N TYR A 196 O PHE A 211 ? O PHE A 211 
AA6 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA6 2 3 N LEU B 18  ? N LEU B 18  O MET B 82  ? O MET B 82  
AA6 3 4 O GLN B 81  ? O GLN B 81  N THR B 68  ? N THR B 68  
AA7 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA7 2 3 O VAL B 115 ? O VAL B 115 N ALA B 91  ? N ALA B 91  
AA7 3 4 O TYR B 94  ? O TYR B 94  N VAL B 37  ? N VAL B 37  
AA7 4 5 N ARG B 38  ? N ARG B 38  O GLU B 46  ? O GLU B 46  
AA7 5 6 N VAL B 50  ? N VAL B 50  O TYR B 58  ? O TYR B 58  
AA8 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA8 2 3 O VAL B 115 ? O VAL B 115 N ALA B 91  ? N ALA B 91  
AA8 3 4 N ARG B 97  ? N ARG B 97  O LEU B 108 ? O LEU B 108 
AA9 1 2 N SER B 126 ? N SER B 126 O LYS B 149 ? O LYS B 149 
AA9 2 3 N ALA B 142 ? N ALA B 142 O VAL B 190 ? O VAL B 190 
AA9 3 4 O VAL B 187 ? O VAL B 187 N HIS B 170 ? N HIS B 170 
AB1 1 2 N SER B 126 ? N SER B 126 O LYS B 149 ? O LYS B 149 
AB1 2 3 N ALA B 142 ? N ALA B 142 O VAL B 190 ? O VAL B 190 
AB1 3 4 O SER B 183 ? O SER B 183 N VAL B 175 ? N VAL B 175 
AB2 1 2 N SER B 159 ? N SER B 159 O ASN B 203 ? O ASN B 203 
AB2 2 3 N VAL B 204 ? N VAL B 204 O VAL B 213 ? O VAL B 213 
AB3 1 2 N SER C 7   ? N SER C 7   O THR C 22  ? O THR C 22  
AB3 2 3 N CYS C 23  ? N CYS C 23  O PHE C 71  ? O PHE C 71  
AB3 3 4 O THR C 74  ? O THR C 74  N SER C 63  ? N SER C 63  
AB4 1 2 N LEU C 11  ? N LEU C 11  O GLU C 109 ? O GLU C 109 
AB4 2 3 O THR C 106 ? O THR C 106 N TYR C 86  ? N TYR C 86  
AB4 3 4 O THR C 85  ? O THR C 85  N GLN C 38  ? N GLN C 38  
AB4 4 5 N GLN C 37  ? N GLN C 37  O LYS C 45  ? O LYS C 45  
AB4 5 6 N TYR C 49  ? N TYR C 49  O SER C 53  ? O SER C 53  
AB5 1 2 N LEU C 11  ? N LEU C 11  O GLU C 109 ? O GLU C 109 
AB5 2 3 O THR C 106 ? O THR C 106 N TYR C 86  ? N TYR C 86  
AB5 3 4 N GLY C 90  ? N GLY C 90  O ALA C 101 ? O ALA C 101 
AB6 1 2 N PHE C 122 ? N PHE C 122 O VAL C 137 ? O VAL C 137 
AB6 2 3 N VAL C 136 ? N VAL C 136 O LEU C 183 ? O LEU C 183 
AB6 3 4 O THR C 182 ? O THR C 182 N GLN C 164 ? N GLN C 164 
AB7 1 2 O ALA C 157 ? O ALA C 157 N VAL C 154 ? N VAL C 154 
AB7 2 3 N LYS C 153 ? N LYS C 153 O ALA C 197 ? O ALA C 197 
AB7 3 4 N VAL C 200 ? N VAL C 200 O VAL C 207 ? O VAL C 207 
AB8 1 2 N VAL D 5   ? N VAL D 5   O ALA D 23  ? O ALA D 23  
AB8 2 3 N LEU D 18  ? N LEU D 18  O MET D 82  ? O MET D 82  
AB8 3 4 O GLN D 81  ? O GLN D 81  N THR D 68  ? N THR D 68  
AB9 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AB9 2 3 O VAL D 115 ? O VAL D 115 N ALA D 91  ? N ALA D 91  
AB9 3 4 O ALA D 96  ? O ALA D 96  N THR D 35  ? N THR D 35  
AB9 4 5 N ARG D 38  ? N ARG D 38  O GLU D 46  ? O GLU D 46  
AB9 5 6 N VAL D 50  ? N VAL D 50  O TYR D 58  ? O TYR D 58  
AC1 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AC1 2 3 O VAL D 115 ? O VAL D 115 N ALA D 91  ? N ALA D 91  
AC1 3 4 N ASP D 99  ? N ASP D 99  O ALA D 105 ? O ALA D 105 
AC2 1 2 N SER D 126 ? N SER D 126 O LYS D 149 ? O LYS D 149 
AC2 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC2 3 4 O VAL D 187 ? O VAL D 187 N HIS D 170 ? N HIS D 170 
AC3 1 2 N SER D 126 ? N SER D 126 O LYS D 149 ? O LYS D 149 
AC3 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC3 3 4 O SER D 183 ? O SER D 183 N VAL D 175 ? N VAL D 175 
AC4 1 2 N SER D 159 ? N SER D 159 O ASN D 203 ? O ASN D 203 
AC4 2 3 N TYR D 200 ? N TYR D 200 O VAL D 217 ? O VAL D 217 
# 
_pdbx_entry_details.entry_id                   8Y2K 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 GLN A 27  ? ? -113.17 -153.40 
2  1 SER A 30  ? ? 60.65   -116.56 
3  1 ALA A 51  ? ? 69.90   -53.35  
4  1 ASN A 162 ? ? -141.32 -9.89   
5  1 LYS A 173 ? ? -106.92 -61.94  
6  1 LYS A 194 ? ? -135.05 -52.34  
7  1 SER B 84  ? ? -109.54 65.68   
8  1 VAL B 102 ? ? -131.81 -62.38  
9  1 SER B 134 ? ? -69.73  -175.80 
10 1 SER B 138 ? ? 37.92   45.07   
11 1 ASP B 150 ? ? 60.43   69.37   
12 1 GLN C 27  ? ? -114.65 -154.57 
13 1 ASN C 31  ? ? 72.34   -8.64   
14 1 ALA C 51  ? ? 69.06   -52.68  
15 1 ALA C 84  ? ? -167.12 -167.26 
16 1 ASP C 94  ? ? 69.17   -42.26  
17 1 ASN C 142 ? ? 57.36   70.21   
18 1 LYS C 173 ? ? -107.01 -63.71  
19 1 LYS C 194 ? ? -133.94 -56.72  
20 1 ALA D 101 ? ? 72.27   -16.26  
21 1 VAL D 102 ? ? -131.47 -66.29  
22 1 SER D 133 ? ? -102.20 -169.03 
23 1 SER D 134 ? ? -126.57 -78.66  
24 1 ASP D 150 ? ? 59.50   70.29   
25 1 CYS D 222 ? ? 76.25   31.67   
# 
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 B GLY 224 ? B GLY 224 
2  1 Y 1 B HIS 225 ? B HIS 225 
3  1 Y 1 B HIS 226 ? B HIS 226 
4  1 Y 1 B HIS 227 ? B HIS 227 
5  1 Y 1 B HIS 228 ? B HIS 228 
6  1 Y 1 B HIS 229 ? B HIS 229 
7  1 Y 1 B HIS 230 ? B HIS 230 
8  1 Y 1 D SER 136 ? D SER 136 
9  1 Y 1 D THR 137 ? D THR 137 
10 1 Y 1 D SER 138 ? D SER 138 
11 1 Y 1 D GLY 224 ? D GLY 224 
12 1 Y 1 D HIS 225 ? D HIS 225 
13 1 Y 1 D HIS 226 ? D HIS 226 
14 1 Y 1 D HIS 227 ? D HIS 227 
15 1 Y 1 D HIS 228 ? D HIS 228 
16 1 Y 1 D HIS 229 ? D HIS 229 
17 1 Y 1 D HIS 230 ? D HIS 230 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32071191 1 
'National Natural Science Foundation of China (NSFC)' China 31971160 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HMW 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y2K 
_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]   0.020943 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001448 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007273 
_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]   0.013597 
_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 
C 
N 
O 
S 
# 
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   . ALA A 1 1   ? 29.998  29.699  39.797  1.00 106.98 ?  1   ALA A N   1 
ATOM 2    C CA  . ALA A 1 1   ? 28.834  29.590  38.927  1.00 103.01 ?  1   ALA A CA  1 
ATOM 3    C C   . ALA A 1 1   ? 29.267  29.410  37.475  1.00 99.16  ?  1   ALA A C   1 
ATOM 4    O O   . ALA A 1 1   ? 29.327  30.375  36.710  1.00 103.06 ?  1   ALA A O   1 
ATOM 5    C CB  . ALA A 1 1   ? 27.945  30.817  39.075  1.00 104.54 ?  1   ALA A CB  1 
ATOM 6    N N   . ILE A 1 2   ? 29.586  28.170  37.104  1.00 96.86  ?  2   ILE A N   1 
ATOM 7    C CA  . ILE A 1 2   ? 30.074  27.844  35.768  1.00 93.93  ?  2   ILE A CA  1 
ATOM 8    C C   . ILE A 1 2   ? 29.188  26.758  35.165  1.00 86.23  ?  2   ILE A C   1 
ATOM 9    O O   . ILE A 1 2   ? 28.706  25.867  35.876  1.00 86.58  ?  2   ILE A O   1 
ATOM 10   C CB  . ILE A 1 2   ? 31.559  27.420  35.799  1.00 89.35  ?  2   ILE A CB  1 
ATOM 11   C CG1 . ILE A 1 2   ? 32.106  27.298  34.380  1.00 86.11  ?  2   ILE A CG1 1 
ATOM 12   C CG2 . ILE A 1 2   ? 31.746  26.119  36.565  1.00 86.02  ?  2   ILE A CG2 1 
ATOM 13   C CD1 . ILE A 1 2   ? 33.600  27.152  34.342  1.00 89.01  ?  2   ILE A CD1 1 
ATOM 14   N N   . GLN A 1 3   ? 28.975  26.836  33.849  1.00 79.85  ?  3   GLN A N   1 
ATOM 15   C CA  . GLN A 1 3   ? 28.096  25.927  33.124  1.00 76.71  ?  3   GLN A CA  1 
ATOM 16   C C   . GLN A 1 3   ? 28.820  25.372  31.906  1.00 76.33  ?  3   GLN A C   1 
ATOM 17   O O   . GLN A 1 3   ? 29.553  26.096  31.226  1.00 75.71  ?  3   GLN A O   1 
ATOM 18   C CB  . GLN A 1 3   ? 26.805  26.636  32.659  1.00 73.05  ?  3   GLN A CB  1 
ATOM 19   C CG  . GLN A 1 3   ? 25.884  27.117  33.777  1.00 79.02  ?  3   GLN A CG  1 
ATOM 20   C CD  . GLN A 1 3   ? 26.354  28.417  34.424  1.00 83.30  ?  3   GLN A CD  1 
ATOM 21   O OE1 . GLN A 1 3   ? 26.688  29.382  33.735  1.00 74.33  ?  3   GLN A OE1 1 
ATOM 22   N NE2 . GLN A 1 3   ? 26.386  28.441  35.753  1.00 87.85  ?  3   GLN A NE2 1 
ATOM 23   N N   . MET A 1 4   ? 28.593  24.091  31.621  1.00 75.59  ?  4   MET A N   1 
ATOM 24   C CA  . MET A 1 4   ? 29.166  23.423  30.457  1.00 66.27  ?  4   MET A CA  1 
ATOM 25   C C   . MET A 1 4   ? 28.057  23.158  29.448  1.00 64.26  ?  4   MET A C   1 
ATOM 26   O O   . MET A 1 4   ? 27.125  22.396  29.728  1.00 66.11  ?  4   MET A O   1 
ATOM 27   C CB  . MET A 1 4   ? 29.854  22.117  30.851  1.00 66.91  ?  4   MET A CB  1 
ATOM 28   C CG  . MET A 1 4   ? 31.115  22.307  31.673  1.00 65.74  ?  4   MET A CG  1 
ATOM 29   S SD  . MET A 1 4   ? 32.404  23.139  30.732  1.00 66.42  ?  4   MET A SD  1 
ATOM 30   C CE  . MET A 1 4   ? 33.206  24.090  32.018  1.00 65.06  ?  4   MET A CE  1 
ATOM 31   N N   . THR A 1 5   ? 28.164  23.780  28.279  1.00 65.97  ?  5   THR A N   1 
ATOM 32   C CA  . THR A 1 5   ? 27.194  23.607  27.206  1.00 66.86  ?  5   THR A CA  1 
ATOM 33   C C   . THR A 1 5   ? 27.755  22.581  26.229  1.00 65.91  ?  5   THR A C   1 
ATOM 34   O O   . THR A 1 5   ? 28.738  22.849  25.533  1.00 60.79  ?  5   THR A O   1 
ATOM 35   C CB  . THR A 1 5   ? 26.908  24.934  26.507  1.00 63.43  ?  5   THR A CB  1 
ATOM 36   O OG1 . THR A 1 5   ? 26.449  25.894  27.469  1.00 56.11  ?  5   THR A OG1 1 
ATOM 37   C CG2 . THR A 1 5   ? 25.836  24.746  25.436  1.00 56.14  ?  5   THR A CG2 1 
ATOM 38   N N   . GLN A 1 6   ? 27.156  21.398  26.204  1.00 61.39  ?  6   GLN A N   1 
ATOM 39   C CA  . GLN A 1 6   ? 27.613  20.327  25.333  1.00 61.05  ?  6   GLN A CA  1 
ATOM 40   C C   . GLN A 1 6   ? 26.741  20.243  24.086  1.00 57.27  ?  6   GLN A C   1 
ATOM 41   O O   . GLN A 1 6   ? 25.537  20.501  24.132  1.00 60.96  ?  6   GLN A O   1 
ATOM 42   C CB  . GLN A 1 6   ? 27.595  18.993  26.073  1.00 54.80  ?  6   GLN A CB  1 
ATOM 43   C CG  . GLN A 1 6   ? 28.462  17.932  25.456  1.00 54.69  ?  6   GLN A CG  1 
ATOM 44   C CD  . GLN A 1 6   ? 28.525  16.692  26.316  1.00 59.41  ?  6   GLN A CD  1 
ATOM 45   O OE1 . GLN A 1 6   ? 28.271  16.747  27.523  1.00 50.59  ?  6   GLN A OE1 1 
ATOM 46   N NE2 . GLN A 1 6   ? 28.831  15.553  25.695  1.00 58.58  ?  6   GLN A NE2 1 
ATOM 47   N N   . SER A 1 7   ? 27.361  19.865  22.965  1.00 60.06  ?  7   SER A N   1 
ATOM 48   C CA  . SER A 1 7   ? 26.639  19.779  21.701  1.00 58.37  ?  7   SER A CA  1 
ATOM 49   C C   . SER A 1 7   ? 27.289  18.757  20.780  1.00 48.10  ?  7   SER A C   1 
ATOM 50   O O   . SER A 1 7   ? 28.524  18.699  20.704  1.00 48.93  ?  7   SER A O   1 
ATOM 51   C CB  . SER A 1 7   ? 26.590  21.146  21.007  1.00 58.04  ?  7   SER A CB  1 
ATOM 52   O OG  . SER A 1 7   ? 25.674  21.141  19.927  1.00 64.88  ?  7   SER A OG  1 
ATOM 53   N N   . PRO A 1 8   ? 26.500  17.947  20.062  1.00 49.69  ?  8   PRO A N   1 
ATOM 54   C CA  . PRO A 1 8   ? 25.038  17.883  20.155  1.00 58.80  ?  8   PRO A CA  1 
ATOM 55   C C   . PRO A 1 8   ? 24.548  16.903  21.222  1.00 58.36  ?  8   PRO A C   1 
ATOM 56   O O   . PRO A 1 8   ? 25.359  16.205  21.827  1.00 51.71  ?  8   PRO A O   1 
ATOM 57   C CB  . PRO A 1 8   ? 24.634  17.400  18.765  1.00 54.95  ?  8   PRO A CB  1 
ATOM 58   C CG  . PRO A 1 8   ? 25.763  16.500  18.372  1.00 52.86  ?  8   PRO A CG  1 
ATOM 59   C CD  . PRO A 1 8   ? 27.013  17.123  18.952  1.00 46.63  ?  8   PRO A CD  1 
ATOM 60   N N   . SER A 1 9   ? 23.227  16.834  21.417  1.00 59.45  ?  9   SER A N   1 
ATOM 61   C CA  . SER A 1 9   ? 22.668  15.910  22.399  1.00 55.35  ?  9   SER A CA  1 
ATOM 62   C C   . SER A 1 9   ? 22.820  14.461  21.963  1.00 59.99  ?  9   SER A C   1 
ATOM 63   O O   . SER A 1 9   ? 22.956  13.571  22.813  1.00 56.18  ?  9   SER A O   1 
ATOM 64   C CB  . SER A 1 9   ? 21.190  16.221  22.641  1.00 57.35  ?  9   SER A CB  1 
ATOM 65   O OG  . SER A 1 9   ? 20.995  17.577  23.006  1.00 69.40  ?  9   SER A OG  1 
ATOM 66   N N   . SER A 1 10  ? 22.790  14.205  20.658  1.00 58.12  ?  10  SER A N   1 
ATOM 67   C CA  . SER A 1 10  ? 22.915  12.852  20.136  1.00 52.16  ?  10  SER A CA  1 
ATOM 68   C C   . SER A 1 10  ? 23.308  12.938  18.671  1.00 60.49  ?  10  SER A C   1 
ATOM 69   O O   . SER A 1 10  ? 23.159  13.983  18.031  1.00 61.36  ?  10  SER A O   1 
ATOM 70   C CB  . SER A 1 10  ? 21.620  12.051  20.308  1.00 53.01  ?  10  SER A CB  1 
ATOM 71   O OG  . SER A 1 10  ? 20.519  12.734  19.742  1.00 67.50  ?  10  SER A OG  1 
ATOM 72   N N   . LEU A 1 11  ? 23.837  11.832  18.151  1.00 61.41  ?  11  LEU A N   1 
ATOM 73   C CA  . LEU A 1 11  ? 24.223  11.789  16.749  1.00 56.82  ?  11  LEU A CA  1 
ATOM 74   C C   . LEU A 1 11  ? 24.381  10.341  16.307  1.00 58.79  ?  11  LEU A C   1 
ATOM 75   O O   . LEU A 1 11  ? 24.755  9.473   17.098  1.00 61.76  ?  11  LEU A O   1 
ATOM 76   C CB  . LEU A 1 11  ? 25.513  12.581  16.493  1.00 54.61  ?  11  LEU A CB  1 
ATOM 77   C CG  . LEU A 1 11  ? 26.832  12.156  17.136  1.00 50.36  ?  11  LEU A CG  1 
ATOM 78   C CD1 . LEU A 1 11  ? 27.589  11.210  16.225  1.00 58.46  ?  11  LEU A CD1 1 
ATOM 79   C CD2 . LEU A 1 11  ? 27.678  13.382  17.429  1.00 39.06  ?  11  LEU A CD2 1 
ATOM 80   N N   . SER A 1 12  ? 24.078  10.098  15.036  1.00 65.62  ?  12  SER A N   1 
ATOM 81   C CA  . SER A 1 12  ? 24.211  8.789   14.413  1.00 63.16  ?  12  SER A CA  1 
ATOM 82   C C   . SER A 1 12  ? 25.318  8.835   13.374  1.00 61.27  ?  12  SER A C   1 
ATOM 83   O O   . SER A 1 12  ? 25.478  9.837   12.671  1.00 66.24  ?  12  SER A O   1 
ATOM 84   C CB  . SER A 1 12  ? 22.903  8.342   13.755  1.00 60.73  ?  12  SER A CB  1 
ATOM 85   O OG  . SER A 1 12  ? 21.891  8.119   14.721  1.00 76.51  ?  12  SER A OG  1 
ATOM 86   N N   . ALA A 1 13  ? 26.083  7.751   13.284  1.00 60.68  ?  13  ALA A N   1 
ATOM 87   C CA  . ALA A 1 13  ? 27.154  7.651   12.306  1.00 55.21  ?  13  ALA A CA  1 
ATOM 88   C C   . ALA A 1 13  ? 27.398  6.184   11.988  1.00 59.68  ?  13  ALA A C   1 
ATOM 89   O O   . ALA A 1 13  ? 26.963  5.287   12.716  1.00 59.43  ?  13  ALA A O   1 
ATOM 90   C CB  . ALA A 1 13  ? 28.435  8.325   12.809  1.00 51.04  ?  13  ALA A CB  1 
ATOM 91   N N   . SER A 1 14  ? 28.115  5.948   10.896  1.00 64.12  ?  14  SER A N   1 
ATOM 92   C CA  . SER A 1 14  ? 28.458  4.603   10.463  1.00 62.65  ?  14  SER A CA  1 
ATOM 93   C C   . SER A 1 14  ? 29.864  4.259   10.933  1.00 58.40  ?  14  SER A C   1 
ATOM 94   O O   . SER A 1 14  ? 30.648  5.128   11.324  1.00 51.73  ?  14  SER A O   1 
ATOM 95   C CB  . SER A 1 14  ? 28.369  4.475   8.936   1.00 57.55  ?  14  SER A CB  1 
ATOM 96   O OG  . SER A 1 14  ? 27.037  4.607   8.468   1.00 57.01  ?  14  SER A OG  1 
ATOM 97   N N   . VAL A 1 15  ? 30.182  2.967   10.870  1.00 60.82  ?  15  VAL A N   1 
ATOM 98   C CA  . VAL A 1 15  ? 31.494  2.498   11.299  1.00 58.60  ?  15  VAL A CA  1 
ATOM 99   C C   . VAL A 1 15  ? 32.545  3.077   10.362  1.00 57.42  ?  15  VAL A C   1 
ATOM 100  O O   . VAL A 1 15  ? 32.528  2.825   9.150   1.00 49.42  ?  15  VAL A O   1 
ATOM 101  C CB  . VAL A 1 15  ? 31.548  0.965   11.334  1.00 49.17  ?  15  VAL A CB  1 
ATOM 102  C CG1 . VAL A 1 15  ? 32.923  0.491   11.780  1.00 41.41  ?  15  VAL A CG1 1 
ATOM 103  C CG2 . VAL A 1 15  ? 30.467  0.420   12.255  1.00 47.79  ?  15  VAL A CG2 1 
ATOM 104  N N   . GLY A 1 16  ? 33.447  3.886   10.915  1.00 53.19  ?  16  GLY A N   1 
ATOM 105  C CA  . GLY A 1 16  ? 34.487  4.532   10.143  1.00 55.55  ?  16  GLY A CA  1 
ATOM 106  C C   . GLY A 1 16  ? 34.331  6.031   10.014  1.00 58.90  ?  16  GLY A C   1 
ATOM 107  O O   . GLY A 1 16  ? 35.284  6.697   9.589   1.00 59.12  ?  16  GLY A O   1 
ATOM 108  N N   . ASP A 1 17  ? 33.167  6.585   10.352  1.00 53.92  ?  17  ASP A N   1 
ATOM 109  C CA  . ASP A 1 17  ? 32.985  8.023   10.262  1.00 55.40  ?  17  ASP A CA  1 
ATOM 110  C C   . ASP A 1 17  ? 33.771  8.749   11.354  1.00 56.76  ?  17  ASP A C   1 
ATOM 111  O O   . ASP A 1 17  ? 34.156  8.177   12.376  1.00 59.18  ?  17  ASP A O   1 
ATOM 112  C CB  . ASP A 1 17  ? 31.508  8.399   10.371  1.00 60.60  ?  17  ASP A CB  1 
ATOM 113  C CG  . ASP A 1 17  ? 30.705  7.984   9.159   1.00 63.98  ?  17  ASP A CG  1 
ATOM 114  O OD1 . ASP A 1 17  ? 29.623  7.392   9.343   1.00 67.41  ?  17  ASP A OD1 1 
ATOM 115  O OD2 . ASP A 1 17  ? 31.150  8.257   8.023   1.00 67.44  ?  17  ASP A OD2 1 
ATOM 116  N N   . ARG A 1 18  ? 33.990  10.037  11.122  1.00 56.94  ?  18  ARG A N   1 
ATOM 117  C CA  . ARG A 1 18  ? 34.645  10.925  12.070  1.00 62.98  ?  18  ARG A CA  1 
ATOM 118  C C   . ARG A 1 18  ? 33.575  11.764  12.757  1.00 67.67  ?  18  ARG A C   1 
ATOM 119  O O   . ARG A 1 18  ? 32.838  12.499  12.088  1.00 66.16  ?  18  ARG A O   1 
ATOM 120  C CB  . ARG A 1 18  ? 35.653  11.817  11.345  1.00 64.46  ?  18  ARG A CB  1 
ATOM 121  C CG  . ARG A 1 18  ? 36.275  12.916  12.190  1.00 68.70  ?  18  ARG A CG  1 
ATOM 122  C CD  . ARG A 1 18  ? 37.054  13.885  11.306  1.00 77.34  ?  18  ARG A CD  1 
ATOM 123  N NE  . ARG A 1 18  ? 37.556  15.041  12.046  1.00 91.01  ?  18  ARG A NE  1 
ATOM 124  C CZ  . ARG A 1 18  ? 38.022  16.147  11.472  1.00 98.53  ?  18  ARG A CZ  1 
ATOM 125  N NH1 . ARG A 1 18  ? 38.045  16.249  10.149  1.00 96.23  ?  18  ARG A NH1 1 
ATOM 126  N NH2 . ARG A 1 18  ? 38.460  17.155  12.219  1.00 91.20  ?  18  ARG A NH2 1 
ATOM 127  N N   . VAL A 1 19  ? 33.488  11.658  14.086  1.00 58.21  ?  19  VAL A N   1 
ATOM 128  C CA  . VAL A 1 19  ? 32.457  12.365  14.835  1.00 56.25  ?  19  VAL A CA  1 
ATOM 129  C C   . VAL A 1 19  ? 33.110  13.321  15.823  1.00 58.40  ?  19  VAL A C   1 
ATOM 130  O O   . VAL A 1 19  ? 34.222  13.090  16.316  1.00 56.61  ?  19  VAL A O   1 
ATOM 131  C CB  . VAL A 1 19  ? 31.479  11.408  15.550  1.00 56.94  ?  19  VAL A CB  1 
ATOM 132  C CG1 . VAL A 1 19  ? 30.792  10.501  14.532  1.00 60.71  ?  19  VAL A CG1 1 
ATOM 133  C CG2 . VAL A 1 19  ? 32.189  10.599  16.604  1.00 59.82  ?  19  VAL A CG2 1 
ATOM 134  N N   . THR A 1 20  ? 32.392  14.408  16.110  1.00 56.71  ?  20  THR A N   1 
ATOM 135  C CA  . THR A 1 20  ? 32.894  15.525  16.898  1.00 54.87  ?  20  THR A CA  1 
ATOM 136  C C   . THR A 1 20  ? 31.869  15.919  17.956  1.00 53.83  ?  20  THR A C   1 
ATOM 137  O O   . THR A 1 20  ? 30.676  16.044  17.656  1.00 51.72  ?  20  THR A O   1 
ATOM 138  C CB  . THR A 1 20  ? 33.210  16.724  15.989  1.00 58.28  ?  20  THR A CB  1 
ATOM 139  O OG1 . THR A 1 20  ? 34.290  16.391  15.104  1.00 54.07  ?  20  THR A OG1 1 
ATOM 140  C CG2 . THR A 1 20  ? 33.592  17.947  16.818  1.00 54.38  ?  20  THR A CG2 1 
ATOM 141  N N   . ILE A 1 21  ? 32.332  16.085  19.195  1.00 50.32  ?  21  ILE A N   1 
ATOM 142  C CA  . ILE A 1 21  ? 31.527  16.588  20.300  1.00 49.56  ?  21  ILE A CA  1 
ATOM 143  C C   . ILE A 1 21  ? 32.182  17.870  20.795  1.00 52.90  ?  21  ILE A C   1 
ATOM 144  O O   . ILE A 1 21  ? 33.409  17.927  20.934  1.00 56.90  ?  21  ILE A O   1 
ATOM 145  C CB  . ILE A 1 21  ? 31.436  15.562  21.449  1.00 54.94  ?  21  ILE A CB  1 
ATOM 146  C CG1 . ILE A 1 21  ? 31.201  14.144  20.909  1.00 49.72  ?  21  ILE A CG1 1 
ATOM 147  C CG2 . ILE A 1 21  ? 30.359  15.973  22.450  1.00 52.01  ?  21  ILE A CG2 1 
ATOM 148  C CD1 . ILE A 1 21  ? 29.900  13.956  20.212  1.00 44.92  ?  21  ILE A CD1 1 
ATOM 149  N N   . THR A 1 22  ? 31.377  18.894  21.074  1.00 51.66  ?  22  THR A N   1 
ATOM 150  C CA  . THR A 1 22  ? 31.903  20.180  21.509  1.00 58.09  ?  22  THR A CA  1 
ATOM 151  C C   . THR A 1 22  ? 31.364  20.525  22.889  1.00 53.31  ?  22  THR A C   1 
ATOM 152  O O   . THR A 1 22  ? 30.223  20.201  23.231  1.00 53.89  ?  22  THR A O   1 
ATOM 153  C CB  . THR A 1 22  ? 31.557  21.316  20.529  1.00 57.17  ?  22  THR A CB  1 
ATOM 154  O OG1 . THR A 1 22  ? 30.158  21.280  20.220  1.00 63.85  ?  22  THR A OG1 1 
ATOM 155  C CG2 . THR A 1 22  ? 32.367  21.178  19.252  1.00 51.71  ?  22  THR A CG2 1 
ATOM 156  N N   . CYS A 1 23  ? 32.199  21.214  23.661  1.00 54.53  ?  23  CYS A N   1 
ATOM 157  C CA  . CYS A 1 23  ? 31.893  21.616  25.028  1.00 56.07  ?  23  CYS A CA  1 
ATOM 158  C C   . CYS A 1 23  ? 32.317  23.070  25.176  1.00 57.50  ?  23  CYS A C   1 
ATOM 159  O O   . CYS A 1 23  ? 33.467  23.416  24.887  1.00 54.34  ?  23  CYS A O   1 
ATOM 160  C CB  . CYS A 1 23  ? 32.626  20.711  26.031  1.00 52.10  ?  23  CYS A CB  1 
ATOM 161  S SG  . CYS A 1 23  ? 32.122  20.778  27.778  1.00 89.98  ?  23  CYS A SG  1 
ATOM 162  N N   . GLN A 1 24  ? 31.379  23.928  25.561  1.00 60.06  ?  24  GLN A N   1 
ATOM 163  C CA  . GLN A 1 24  ? 31.626  25.352  25.744  1.00 61.85  ?  24  GLN A CA  1 
ATOM 164  C C   . GLN A 1 24  ? 31.567  25.688  27.230  1.00 64.71  ?  24  GLN A C   1 
ATOM 165  O O   . GLN A 1 24  ? 30.612  25.311  27.921  1.00 64.18  ?  24  GLN A O   1 
ATOM 166  C CB  . GLN A 1 24  ? 30.597  26.178  24.968  1.00 64.35  ?  24  GLN A CB  1 
ATOM 167  C CG  . GLN A 1 24  ? 30.770  27.681  25.079  1.00 64.28  ?  24  GLN A CG  1 
ATOM 168  C CD  . GLN A 1 24  ? 31.948  28.197  24.276  1.00 69.52  ?  24  GLN A CD  1 
ATOM 169  O OE1 . GLN A 1 24  ? 32.959  28.622  24.840  1.00 67.30  ?  24  GLN A OE1 1 
ATOM 170  N NE2 . GLN A 1 24  ? 31.824  28.167  22.951  1.00 67.83  ?  24  GLN A NE2 1 
ATOM 171  N N   . ALA A 1 25  ? 32.580  26.401  27.713  1.00 67.34  ?  25  ALA A N   1 
ATOM 172  C CA  . ALA A 1 25  ? 32.678  26.804  29.109  1.00 68.82  ?  25  ALA A CA  1 
ATOM 173  C C   . ALA A 1 25  ? 32.151  28.224  29.298  1.00 71.90  ?  25  ALA A C   1 
ATOM 174  O O   . ALA A 1 25  ? 32.277  29.076  28.414  1.00 74.97  ?  25  ALA A O   1 
ATOM 175  C CB  . ALA A 1 25  ? 34.124  26.714  29.601  1.00 59.11  ?  25  ALA A CB  1 
ATOM 176  N N   . SER A 1 26  ? 31.550  28.469  30.464  1.00 70.92  ?  26  SER A N   1 
ATOM 177  C CA  . SER A 1 26  ? 31.018  29.798  30.756  1.00 74.09  ?  26  SER A CA  1 
ATOM 178  C C   . SER A 1 26  ? 32.141  30.814  30.938  1.00 74.15  ?  26  SER A C   1 
ATOM 179  O O   . SER A 1 26  ? 32.100  31.911  30.369  1.00 81.00  ?  26  SER A O   1 
ATOM 180  C CB  . SER A 1 26  ? 30.132  29.741  32.000  1.00 78.42  ?  26  SER A CB  1 
ATOM 181  O OG  . SER A 1 26  ? 29.010  28.907  31.775  1.00 82.23  ?  26  SER A OG  1 
ATOM 182  N N   . GLN A 1 27  ? 33.153  30.462  31.727  1.00 70.59  ?  27  GLN A N   1 
ATOM 183  C CA  . GLN A 1 27  ? 34.348  31.251  31.947  1.00 69.61  ?  27  GLN A CA  1 
ATOM 184  C C   . GLN A 1 27  ? 35.532  30.494  31.339  1.00 69.65  ?  27  GLN A C   1 
ATOM 185  O O   . GLN A 1 27  ? 35.342  29.699  30.404  1.00 75.72  ?  27  GLN A O   1 
ATOM 186  C CB  . GLN A 1 27  ? 34.494  31.526  33.441  1.00 80.68  ?  27  GLN A CB  1 
ATOM 187  C CG  . GLN A 1 27  ? 33.314  32.239  34.076  1.00 84.16  ?  27  GLN A CG  1 
ATOM 188  C CD  . GLN A 1 27  ? 33.478  32.401  35.577  1.00 89.88  ?  27  GLN A CD  1 
ATOM 189  O OE1 . GLN A 1 27  ? 34.524  32.843  36.055  1.00 90.28  ?  27  GLN A OE1 1 
ATOM 190  N NE2 . GLN A 1 27  ? 32.448  32.029  36.329  1.00 89.34  ?  27  GLN A NE2 1 
ATOM 191  N N   . SER A 1 28  ? 36.730  30.722  31.865  1.00 68.05  ?  28  SER A N   1 
ATOM 192  C CA  . SER A 1 28  ? 37.934  30.044  31.402  1.00 66.14  ?  28  SER A CA  1 
ATOM 193  C C   . SER A 1 28  ? 38.409  29.075  32.475  1.00 74.01  ?  28  SER A C   1 
ATOM 194  O O   . SER A 1 28  ? 38.712  29.485  33.601  1.00 79.46  ?  28  SER A O   1 
ATOM 195  C CB  . SER A 1 28  ? 39.036  31.042  31.053  1.00 71.22  ?  28  SER A CB  1 
ATOM 196  O OG  . SER A 1 28  ? 40.244  30.365  30.746  1.00 74.58  ?  28  SER A OG  1 
ATOM 197  N N   . ILE A 1 29  ? 38.468  27.793  32.119  1.00 76.04  ?  29  ILE A N   1 
ATOM 198  C CA  . ILE A 1 29  ? 38.921  26.734  33.014  1.00 73.78  ?  29  ILE A CA  1 
ATOM 199  C C   . ILE A 1 29  ? 40.374  26.362  32.747  1.00 72.45  ?  29  ILE A C   1 
ATOM 200  O O   . ILE A 1 29  ? 40.870  25.376  33.304  1.00 72.47  ?  29  ILE A O   1 
ATOM 201  C CB  . ILE A 1 29  ? 38.017  25.496  32.925  1.00 70.10  ?  29  ILE A CB  1 
ATOM 202  C CG1 . ILE A 1 29  ? 37.666  25.197  31.472  1.00 65.34  ?  29  ILE A CG1 1 
ATOM 203  C CG2 . ILE A 1 29  ? 36.762  25.700  33.743  1.00 72.56  ?  29  ILE A CG2 1 
ATOM 204  C CD1 . ILE A 1 29  ? 36.724  24.037  31.312  1.00 60.55  ?  29  ILE A CD1 1 
ATOM 205  N N   . SER A 1 30  ? 41.059  27.120  31.886  1.00 72.45  ?  30  SER A N   1 
ATOM 206  C CA  . SER A 1 30  ? 42.429  26.841  31.477  1.00 72.58  ?  30  SER A CA  1 
ATOM 207  C C   . SER A 1 30  ? 42.377  25.469  30.815  1.00 71.26  ?  30  SER A C   1 
ATOM 208  O O   . SER A 1 30  ? 41.711  25.305  29.786  1.00 67.68  ?  30  SER A O   1 
ATOM 209  C CB  . SER A 1 30  ? 43.368  26.876  32.691  1.00 67.04  ?  30  SER A CB  1 
ATOM 210  O OG  . SER A 1 30  ? 44.676  26.459  32.353  1.00 71.38  ?  30  SER A OG  1 
ATOM 211  N N   . ASN A 1 31  ? 43.057  24.479  31.383  1.00 69.65  ?  31  ASN A N   1 
ATOM 212  C CA  . ASN A 1 31  ? 43.125  23.150  30.794  1.00 63.06  ?  31  ASN A CA  1 
ATOM 213  C C   . ASN A 1 31  ? 42.341  22.110  31.573  1.00 64.86  ?  31  ASN A C   1 
ATOM 214  O O   . ASN A 1 31  ? 42.244  20.964  31.122  1.00 64.30  ?  31  ASN A O   1 
ATOM 215  C CB  . ASN A 1 31  ? 44.584  22.706  30.666  1.00 66.62  ?  31  ASN A CB  1 
ATOM 216  C CG  . ASN A 1 31  ? 45.256  23.288  29.449  1.00 74.17  ?  31  ASN A CG  1 
ATOM 217  O OD1 . ASN A 1 31  ? 44.778  24.265  28.872  1.00 74.72  ?  31  ASN A OD1 1 
ATOM 218  N ND2 . ASN A 1 31  ? 46.376  22.697  29.050  1.00 81.69  ?  31  ASN A ND2 1 
ATOM 219  N N   . GLN A 1 32  ? 41.758  22.477  32.714  1.00 71.37  ?  32  GLN A N   1 
ATOM 220  C CA  . GLN A 1 32  ? 41.109  21.511  33.601  1.00 75.39  ?  32  GLN A CA  1 
ATOM 221  C C   . GLN A 1 32  ? 39.759  21.088  33.014  1.00 66.12  ?  32  GLN A C   1 
ATOM 222  O O   . GLN A 1 32  ? 38.681  21.435  33.502  1.00 66.48  ?  32  GLN A O   1 
ATOM 223  C CB  . GLN A 1 32  ? 40.956  22.092  35.002  1.00 76.03  ?  32  GLN A CB  1 
ATOM 224  C CG  . GLN A 1 32  ? 42.257  22.597  35.621  1.00 75.08  ?  32  GLN A CG  1 
ATOM 225  C CD  . GLN A 1 32  ? 42.123  22.912  37.102  1.00 88.68  ?  32  GLN A CD  1 
ATOM 226  O OE1 . GLN A 1 32  ? 41.573  22.119  37.869  1.00 92.73  ?  32  GLN A OE1 1 
ATOM 227  N NE2 . GLN A 1 32  ? 42.625  24.074  37.512  1.00 92.02  ?  32  GLN A NE2 1 
ATOM 228  N N   . LEU A 1 33  ? 39.839  20.317  31.928  1.00 62.11  ?  33  LEU A N   1 
ATOM 229  C CA  . LEU A 1 33  ? 38.659  19.715  31.322  1.00 62.21  ?  33  LEU A CA  1 
ATOM 230  C C   . LEU A 1 33  ? 38.969  18.267  30.956  1.00 56.11  ?  33  LEU A C   1 
ATOM 231  O O   . LEU A 1 33  ? 40.040  17.967  30.417  1.00 57.19  ?  33  LEU A O   1 
ATOM 232  C CB  . LEU A 1 33  ? 38.199  20.496  30.080  1.00 52.65  ?  33  LEU A CB  1 
ATOM 233  C CG  . LEU A 1 33  ? 36.882  19.989  29.490  1.00 50.37  ?  33  LEU A CG  1 
ATOM 234  C CD1 . LEU A 1 33  ? 35.918  21.134  29.279  1.00 49.85  ?  33  LEU A CD1 1 
ATOM 235  C CD2 . LEU A 1 33  ? 37.112  19.236  28.190  1.00 51.05  ?  33  LEU A CD2 1 
ATOM 236  N N   . SER A 1 34  ? 38.026  17.371  31.249  1.00 43.04  ?  34  SER A N   1 
ATOM 237  C CA  . SER A 1 34  ? 38.201  15.952  30.973  1.00 46.71  ?  34  SER A CA  1 
ATOM 238  C C   . SER A 1 34  ? 36.977  15.399  30.256  1.00 47.45  ?  34  SER A C   1 
ATOM 239  O O   . SER A 1 34  ? 35.856  15.880  30.431  1.00 43.25  ?  34  SER A O   1 
ATOM 240  C CB  . SER A 1 34  ? 38.469  15.136  32.255  1.00 49.47  ?  34  SER A CB  1 
ATOM 241  O OG  . SER A 1 34  ? 37.620  15.513  33.319  1.00 50.91  ?  34  SER A OG  1 
ATOM 242  N N   . TRP A 1 35  ? 37.217  14.376  29.442  1.00 49.98  ?  35  TRP A N   1 
ATOM 243  C CA  . TRP A 1 35  ? 36.198  13.694  28.655  1.00 50.61  ?  35  TRP A CA  1 
ATOM 244  C C   . TRP A 1 35  ? 36.033  12.270  29.162  1.00 49.17  ?  35  TRP A C   1 
ATOM 245  O O   . TRP A 1 35  ? 37.030  11.564  29.373  1.00 48.74  ?  35  TRP A O   1 
ATOM 246  C CB  . TRP A 1 35  ? 36.565  13.660  27.170  1.00 43.53  ?  35  TRP A CB  1 
ATOM 247  C CG  . TRP A 1 35  ? 36.550  14.978  26.483  1.00 43.60  ?  35  TRP A CG  1 
ATOM 248  C CD1 . TRP A 1 35  ? 37.620  15.785  26.232  1.00 47.64  ?  35  TRP A CD1 1 
ATOM 249  C CD2 . TRP A 1 35  ? 35.406  15.646  25.944  1.00 45.21  ?  35  TRP A CD2 1 
ATOM 250  N NE1 . TRP A 1 35  ? 37.212  16.915  25.561  1.00 50.96  ?  35  TRP A NE1 1 
ATOM 251  C CE2 . TRP A 1 35  ? 35.856  16.854  25.375  1.00 46.42  ?  35  TRP A CE2 1 
ATOM 252  C CE3 . TRP A 1 35  ? 34.043  15.339  25.886  1.00 47.06  ?  35  TRP A CE3 1 
ATOM 253  C CZ2 . TRP A 1 35  ? 34.992  17.755  24.759  1.00 45.26  ?  35  TRP A CZ2 1 
ATOM 254  C CZ3 . TRP A 1 35  ? 33.187  16.236  25.271  1.00 51.78  ?  35  TRP A CZ3 1 
ATOM 255  C CH2 . TRP A 1 35  ? 33.665  17.431  24.720  1.00 45.89  ?  35  TRP A CH2 1 
ATOM 256  N N   . TYR A 1 36  ? 34.777  11.855  29.330  1.00 45.33  ?  36  TYR A N   1 
ATOM 257  C CA  . TYR A 1 36  ? 34.415  10.553  29.865  1.00 48.43  ?  36  TYR A CA  1 
ATOM 258  C C   . TYR A 1 36  ? 33.414  9.875   28.938  1.00 48.03  ?  36  TYR A C   1 
ATOM 259  O O   . TYR A 1 36  ? 32.647  10.539  28.229  1.00 44.57  ?  36  TYR A O   1 
ATOM 260  C CB  . TYR A 1 36  ? 33.798  10.672  31.277  1.00 51.82  ?  36  TYR A CB  1 
ATOM 261  C CG  . TYR A 1 36  ? 34.649  11.427  32.281  1.00 53.20  ?  36  TYR A CG  1 
ATOM 262  C CD1 . TYR A 1 36  ? 35.375  10.749  33.254  1.00 54.91  ?  36  TYR A CD1 1 
ATOM 263  C CD2 . TYR A 1 36  ? 34.718  12.816  32.265  1.00 46.93  ?  36  TYR A CD2 1 
ATOM 264  C CE1 . TYR A 1 36  ? 36.149  11.430  34.173  1.00 54.25  ?  36  TYR A CE1 1 
ATOM 265  C CE2 . TYR A 1 36  ? 35.493  13.504  33.177  1.00 43.99  ?  36  TYR A CE2 1 
ATOM 266  C CZ  . TYR A 1 36  ? 36.207  12.807  34.127  1.00 53.80  ?  36  TYR A CZ  1 
ATOM 267  O OH  . TYR A 1 36  ? 36.981  13.483  35.040  1.00 58.69  ?  36  TYR A OH  1 
ATOM 268  N N   . GLN A 1 37  ? 33.412  8.543   28.980  1.00 50.41  ?  37  GLN A N   1 
ATOM 269  C CA  . GLN A 1 37  ? 32.506  7.698   28.216  1.00 43.73  ?  37  GLN A CA  1 
ATOM 270  C C   . GLN A 1 37  ? 31.726  6.803   29.169  1.00 42.97  ?  37  GLN A C   1 
ATOM 271  O O   . GLN A 1 37  ? 32.313  6.190   30.064  1.00 53.79  ?  37  GLN A O   1 
ATOM 272  C CB  . GLN A 1 37  ? 33.288  6.837   27.219  1.00 46.55  ?  37  GLN A CB  1 
ATOM 273  C CG  . GLN A 1 37  ? 32.462  5.790   26.498  1.00 47.19  ?  37  GLN A CG  1 
ATOM 274  C CD  . GLN A 1 37  ? 33.317  4.738   25.814  1.00 46.69  ?  37  GLN A CD  1 
ATOM 275  O OE1 . GLN A 1 37  ? 34.249  4.184   26.405  1.00 40.99  ?  37  GLN A OE1 1 
ATOM 276  N NE2 . GLN A 1 37  ? 32.999  4.454   24.559  1.00 47.87  ?  37  GLN A NE2 1 
ATOM 277  N N   . GLN A 1 38  ? 30.412  6.689   28.962  1.00 43.47  ?  38  GLN A N   1 
ATOM 278  C CA  . GLN A 1 38  ? 29.567  5.883   29.837  1.00 51.29  ?  38  GLN A CA  1 
ATOM 279  C C   . GLN A 1 38  ? 28.689  4.963   29.004  1.00 53.19  ?  38  GLN A C   1 
ATOM 280  O O   . GLN A 1 38  ? 27.949  5.424   28.130  1.00 54.37  ?  38  GLN A O   1 
ATOM 281  C CB  . GLN A 1 38  ? 28.686  6.771   30.728  1.00 53.99  ?  38  GLN A CB  1 
ATOM 282  C CG  . GLN A 1 38  ? 27.839  6.011   31.749  1.00 56.16  ?  38  GLN A CG  1 
ATOM 283  C CD  . GLN A 1 38  ? 26.854  6.911   32.482  1.00 57.31  ?  38  GLN A CD  1 
ATOM 284  O OE1 . GLN A 1 38  ? 26.474  7.968   31.978  1.00 62.70  ?  38  GLN A OE1 1 
ATOM 285  N NE2 . GLN A 1 38  ? 26.440  6.497   33.675  1.00 50.44  ?  38  GLN A NE2 1 
ATOM 286  N N   . LYS A 1 39  ? 28.748  3.682   29.301  1.00 57.60  ?  39  LYS A N   1 
ATOM 287  C CA  . LYS A 1 39  ? 27.936  2.654   28.673  1.00 61.94  ?  39  LYS A CA  1 
ATOM 288  C C   . LYS A 1 39  ? 26.778  2.266   29.584  1.00 59.27  ?  39  LYS A C   1 
ATOM 289  O O   . LYS A 1 39  ? 26.828  2.491   30.796  1.00 55.89  ?  39  LYS A O   1 
ATOM 290  C CB  . LYS A 1 39  ? 28.808  1.437   28.340  1.00 53.73  ?  39  LYS A CB  1 
ATOM 291  C CG  . LYS A 1 39  ? 29.828  1.731   27.245  1.00 43.34  ?  39  LYS A CG  1 
ATOM 292  C CD  . LYS A 1 39  ? 30.860  0.631   27.120  1.00 51.66  ?  39  LYS A CD  1 
ATOM 293  C CE  . LYS A 1 39  ? 31.585  0.690   25.777  1.00 56.45  ?  39  LYS A CE  1 
ATOM 294  N NZ  . LYS A 1 39  ? 30.681  0.270   24.644  1.00 53.86  ?  39  LYS A NZ  1 
ATOM 295  N N   . PRO A 1 40  ? 25.693  1.723   29.028  1.00 62.55  ?  40  PRO A N   1 
ATOM 296  C CA  . PRO A 1 40  ? 24.496  1.474   29.844  1.00 60.98  ?  40  PRO A CA  1 
ATOM 297  C C   . PRO A 1 40  ? 24.787  0.595   31.050  1.00 63.12  ?  40  PRO A C   1 
ATOM 298  O O   . PRO A 1 40  ? 25.515  -0.396  30.963  1.00 64.89  ?  40  PRO A O   1 
ATOM 299  C CB  . PRO A 1 40  ? 23.536  0.784   28.867  1.00 65.48  ?  40  PRO A CB  1 
ATOM 300  C CG  . PRO A 1 40  ? 24.388  0.338   27.720  1.00 60.38  ?  40  PRO A CG  1 
ATOM 301  C CD  . PRO A 1 40  ? 25.475  1.354   27.619  1.00 55.03  ?  40  PRO A CD  1 
ATOM 302  N N   . GLY A 1 41  ? 24.228  0.993   32.192  1.00 64.10  ?  41  GLY A N   1 
ATOM 303  C CA  . GLY A 1 41  ? 24.407  0.261   33.427  1.00 55.69  ?  41  GLY A CA  1 
ATOM 304  C C   . GLY A 1 41  ? 25.774  0.388   34.060  1.00 60.47  ?  41  GLY A C   1 
ATOM 305  O O   . GLY A 1 41  ? 25.972  -0.122  35.169  1.00 64.58  ?  41  GLY A O   1 
ATOM 306  N N   . LYS A 1 42  ? 26.715  1.062   33.407  1.00 56.19  ?  42  LYS A N   1 
ATOM 307  C CA  . LYS A 1 42  ? 28.083  1.174   33.882  1.00 55.07  ?  42  LYS A CA  1 
ATOM 308  C C   . LYS A 1 42  ? 28.376  2.599   34.329  1.00 52.21  ?  42  LYS A C   1 
ATOM 309  O O   . LYS A 1 42  ? 27.661  3.542   33.987  1.00 53.61  ?  42  LYS A O   1 
ATOM 310  C CB  . LYS A 1 42  ? 29.073  0.757   32.785  1.00 55.38  ?  42  LYS A CB  1 
ATOM 311  C CG  . LYS A 1 42  ? 28.857  -0.658  32.262  1.00 57.50  ?  42  LYS A CG  1 
ATOM 312  C CD  . LYS A 1 42  ? 28.975  -1.673  33.387  1.00 63.57  ?  42  LYS A CD  1 
ATOM 313  C CE  . LYS A 1 42  ? 28.648  -3.080  32.908  1.00 79.25  ?  42  LYS A CE  1 
ATOM 314  N NZ  . LYS A 1 42  ? 28.744  -4.086  34.010  1.00 88.99  ?  42  LYS A NZ  1 
ATOM 315  N N   . ALA A 1 43  ? 29.435  2.738   35.117  1.00 54.45  ?  43  ALA A N   1 
ATOM 316  C CA  . ALA A 1 43  ? 29.924  4.043   35.524  1.00 48.10  ?  43  ALA A CA  1 
ATOM 317  C C   . ALA A 1 43  ? 30.853  4.603   34.448  1.00 58.21  ?  43  ALA A C   1 
ATOM 318  O O   . ALA A 1 43  ? 31.466  3.843   33.693  1.00 62.23  ?  43  ALA A O   1 
ATOM 319  C CB  . ALA A 1 43  ? 30.660  3.948   36.853  1.00 52.88  ?  43  ALA A CB  1 
ATOM 320  N N   . PRO A 1 44  ? 30.963  5.928   34.342  1.00 60.48  ?  44  PRO A N   1 
ATOM 321  C CA  . PRO A 1 44  ? 31.792  6.507   33.280  1.00 55.04  ?  44  PRO A CA  1 
ATOM 322  C C   . PRO A 1 44  ? 33.257  6.122   33.425  1.00 55.31  ?  44  PRO A C   1 
ATOM 323  O O   . PRO A 1 44  ? 33.742  5.820   34.517  1.00 58.38  ?  44  PRO A O   1 
ATOM 324  C CB  . PRO A 1 44  ? 31.591  8.016   33.459  1.00 55.75  ?  44  PRO A CB  1 
ATOM 325  C CG  . PRO A 1 44  ? 30.275  8.141   34.148  1.00 53.52  ?  44  PRO A CG  1 
ATOM 326  C CD  . PRO A 1 44  ? 30.212  6.962   35.075  1.00 59.43  ?  44  PRO A CD  1 
ATOM 327  N N   . LYS A 1 45  ? 33.959  6.133   32.295  1.00 49.87  ?  45  LYS A N   1 
ATOM 328  C CA  . LYS A 1 45  ? 35.381  5.829   32.246  1.00 54.99  ?  45  LYS A CA  1 
ATOM 329  C C   . LYS A 1 45  ? 36.120  7.044   31.705  1.00 54.19  ?  45  LYS A C   1 
ATOM 330  O O   . LYS A 1 45  ? 35.699  7.644   30.710  1.00 48.65  ?  45  LYS A O   1 
ATOM 331  C CB  . LYS A 1 45  ? 35.667  4.600   31.379  1.00 59.80  ?  45  LYS A CB  1 
ATOM 332  C CG  . LYS A 1 45  ? 37.154  4.301   31.207  1.00 70.25  ?  45  LYS A CG  1 
ATOM 333  C CD  . LYS A 1 45  ? 37.386  3.153   30.233  1.00 82.11  ?  45  LYS A CD  1 
ATOM 334  C CE  . LYS A 1 45  ? 38.872  2.902   29.996  1.00 86.04  ?  45  LYS A CE  1 
ATOM 335  N NZ  . LYS A 1 45  ? 39.103  1.772   29.048  1.00 79.12  ?  45  LYS A NZ  1 
ATOM 336  N N   . LEU A 1 46  ? 37.218  7.399   32.362  1.00 56.02  ?  46  LEU A N   1 
ATOM 337  C CA  . LEU A 1 46  ? 37.993  8.564   31.967  1.00 54.42  ?  46  LEU A CA  1 
ATOM 338  C C   . LEU A 1 46  ? 38.670  8.303   30.624  1.00 54.46  ?  46  LEU A C   1 
ATOM 339  O O   . LEU A 1 46  ? 39.477  7.376   30.494  1.00 59.13  ?  46  LEU A O   1 
ATOM 340  C CB  . LEU A 1 46  ? 39.018  8.890   33.052  1.00 50.35  ?  46  LEU A CB  1 
ATOM 341  C CG  . LEU A 1 46  ? 39.863  10.165  32.958  1.00 56.87  ?  46  LEU A CG  1 
ATOM 342  C CD1 . LEU A 1 46  ? 41.161  9.911   32.209  1.00 58.93  ?  46  LEU A CD1 1 
ATOM 343  C CD2 . LEU A 1 46  ? 39.084  11.303  32.314  1.00 54.66  ?  46  LEU A CD2 1 
ATOM 344  N N   . LEU A 1 47  ? 38.326  9.111   29.621  1.00 55.03  ?  47  LEU A N   1 
ATOM 345  C CA  . LEU A 1 47  ? 38.930  9.029   28.295  1.00 55.84  ?  47  LEU A CA  1 
ATOM 346  C C   . LEU A 1 47  ? 40.094  10.002  28.139  1.00 53.42  ?  47  LEU A C   1 
ATOM 347  O O   . LEU A 1 47  ? 41.186  9.615   27.708  1.00 50.70  ?  47  LEU A O   1 
ATOM 348  C CB  . LEU A 1 47  ? 37.884  9.317   27.215  1.00 48.26  ?  47  LEU A CB  1 
ATOM 349  C CG  . LEU A 1 47  ? 36.829  8.260   26.918  1.00 48.76  ?  47  LEU A CG  1 
ATOM 350  C CD1 . LEU A 1 47  ? 35.988  8.719   25.743  1.00 51.15  ?  47  LEU A CD1 1 
ATOM 351  C CD2 . LEU A 1 47  ? 37.495  6.931   26.617  1.00 50.32  ?  47  LEU A CD2 1 
ATOM 352  N N   . ILE A 1 48  ? 39.879  11.267  28.481  1.00 48.86  ?  48  ILE A N   1 
ATOM 353  C CA  . ILE A 1 48  ? 40.877  12.301  28.229  1.00 55.68  ?  48  ILE A CA  1 
ATOM 354  C C   . ILE A 1 48  ? 40.917  13.244  29.418  1.00 51.83  ?  48  ILE A C   1 
ATOM 355  O O   . ILE A 1 48  ? 39.874  13.605  29.964  1.00 52.93  ?  48  ILE A O   1 
ATOM 356  C CB  . ILE A 1 48  ? 40.570  13.058  26.918  1.00 56.16  ?  48  ILE A CB  1 
ATOM 357  C CG1 . ILE A 1 48  ? 40.891  12.168  25.716  1.00 55.52  ?  48  ILE A CG1 1 
ATOM 358  C CG2 . ILE A 1 48  ? 41.341  14.369  26.843  1.00 56.67  ?  48  ILE A CG2 1 
ATOM 359  C CD1 . ILE A 1 48  ? 40.556  12.783  24.385  1.00 52.78  ?  48  ILE A CD1 1 
ATOM 360  N N   . TYR A 1 49  ? 42.119  13.637  29.828  1.00 53.58  ?  49  TYR A N   1 
ATOM 361  C CA  . TYR A 1 49  ? 42.294  14.624  30.882  1.00 62.36  ?  49  TYR A CA  1 
ATOM 362  C C   . TYR A 1 49  ? 43.153  15.771  30.373  1.00 63.09  ?  49  TYR A C   1 
ATOM 363  O O   . TYR A 1 49  ? 43.850  15.642  29.364  1.00 68.03  ?  49  TYR A O   1 
ATOM 364  C CB  . TYR A 1 49  ? 42.929  14.004  32.135  1.00 64.59  ?  49  TYR A CB  1 
ATOM 365  C CG  . TYR A 1 49  ? 44.361  13.542  31.954  1.00 66.39  ?  49  TYR A CG  1 
ATOM 366  C CD1 . TYR A 1 49  ? 44.645  12.264  31.468  1.00 64.39  ?  49  TYR A CD1 1 
ATOM 367  C CD2 . TYR A 1 49  ? 45.428  14.381  32.263  1.00 63.81  ?  49  TYR A CD2 1 
ATOM 368  C CE1 . TYR A 1 49  ? 45.954  11.832  31.307  1.00 64.28  ?  49  TYR A CE1 1 
ATOM 369  C CE2 . TYR A 1 49  ? 46.739  13.962  32.101  1.00 66.33  ?  49  TYR A CE2 1 
ATOM 370  C CZ  . TYR A 1 49  ? 46.996  12.688  31.622  1.00 69.04  ?  49  TYR A CZ  1 
ATOM 371  O OH  . TYR A 1 49  ? 48.300  12.271  31.460  1.00 63.73  ?  49  TYR A OH  1 
ATOM 372  N N   . ASP A 1 50  ? 43.103  16.893  31.093  1.00 59.67  ?  50  ASP A N   1 
ATOM 373  C CA  . ASP A 1 50  ? 43.863  18.094  30.741  1.00 61.96  ?  50  ASP A CA  1 
ATOM 374  C C   . ASP A 1 50  ? 43.703  18.439  29.259  1.00 67.74  ?  50  ASP A C   1 
ATOM 375  O O   . ASP A 1 50  ? 44.675  18.713  28.549  1.00 68.49  ?  50  ASP A O   1 
ATOM 376  C CB  . ASP A 1 50  ? 45.337  17.943  31.118  1.00 58.32  ?  50  ASP A CB  1 
ATOM 377  C CG  . ASP A 1 50  ? 45.634  18.447  32.520  1.00 79.89  ?  50  ASP A CG  1 
ATOM 378  O OD1 . ASP A 1 50  ? 44.977  19.420  32.955  1.00 83.08  ?  50  ASP A OD1 1 
ATOM 379  O OD2 . ASP A 1 50  ? 46.520  17.871  33.191  1.00 84.70  ?  50  ASP A OD2 1 
ATOM 380  N N   . ALA A 1 51  ? 42.452  18.396  28.795  1.00 60.18  ?  51  ALA A N   1 
ATOM 381  C CA  . ALA A 1 51  ? 42.055  18.784  27.443  1.00 62.89  ?  51  ALA A CA  1 
ATOM 382  C C   . ALA A 1 51  ? 42.533  17.830  26.345  1.00 67.98  ?  51  ALA A C   1 
ATOM 383  O O   . ALA A 1 51  ? 41.717  17.369  25.539  1.00 66.66  ?  51  ALA A O   1 
ATOM 384  C CB  . ALA A 1 51  ? 42.526  20.210  27.135  1.00 61.57  ?  51  ALA A CB  1 
ATOM 385  N N   . SER A 1 52  ? 43.837  17.524  26.275  1.00 64.27  ?  52  SER A N   1 
ATOM 386  C CA  . SER A 1 52  ? 44.359  16.801  25.117  1.00 54.96  ?  52  SER A CA  1 
ATOM 387  C C   . SER A 1 52  ? 45.280  15.643  25.492  1.00 62.42  ?  52  SER A C   1 
ATOM 388  O O   . SER A 1 52  ? 46.064  15.194  24.647  1.00 53.86  ?  52  SER A O   1 
ATOM 389  C CB  . SER A 1 52  ? 45.090  17.751  24.164  1.00 54.78  ?  52  SER A CB  1 
ATOM 390  O OG  . SER A 1 52  ? 46.174  18.408  24.796  1.00 56.48  ?  52  SER A OG  1 
ATOM 391  N N   . SER A 1 53  ? 45.207  15.142  26.726  1.00 68.27  ?  53  SER A N   1 
ATOM 392  C CA  . SER A 1 53  ? 46.058  14.042  27.170  1.00 63.15  ?  53  SER A CA  1 
ATOM 393  C C   . SER A 1 53  ? 45.263  12.743  27.194  1.00 56.61  ?  53  SER A C   1 
ATOM 394  O O   . SER A 1 53  ? 44.143  12.701  27.715  1.00 56.43  ?  53  SER A O   1 
ATOM 395  C CB  . SER A 1 53  ? 46.645  14.320  28.554  1.00 58.70  ?  53  SER A CB  1 
ATOM 396  O OG  . SER A 1 53  ? 47.477  15.466  28.533  1.00 65.72  ?  53  SER A OG  1 
ATOM 397  N N   . LEU A 1 54  ? 45.845  11.689  26.630  1.00 58.24  ?  54  LEU A N   1 
ATOM 398  C CA  . LEU A 1 54  ? 45.199  10.385  26.605  1.00 62.85  ?  54  LEU A CA  1 
ATOM 399  C C   . LEU A 1 54  ? 45.358  9.664   27.937  1.00 61.04  ?  54  LEU A C   1 
ATOM 400  O O   . LEU A 1 54  ? 46.366  9.810   28.635  1.00 61.06  ?  54  LEU A O   1 
ATOM 401  C CB  . LEU A 1 54  ? 45.784  9.518   25.491  1.00 59.05  ?  54  LEU A CB  1 
ATOM 402  C CG  . LEU A 1 54  ? 45.027  9.476   24.172  1.00 58.75  ?  54  LEU A CG  1 
ATOM 403  C CD1 . LEU A 1 54  ? 45.689  8.486   23.232  1.00 61.26  ?  54  LEU A CD1 1 
ATOM 404  C CD2 . LEU A 1 54  ? 43.585  9.083   24.431  1.00 57.36  ?  54  LEU A CD2 1 
ATOM 405  N N   . ALA A 1 55  ? 44.359  8.854   28.271  1.00 60.88  ?  55  ALA A N   1 
ATOM 406  C CA  . ALA A 1 55  ? 44.405  8.053   29.480  1.00 64.29  ?  55  ALA A CA  1 
ATOM 407  C C   . ALA A 1 55  ? 45.150  6.748   29.204  1.00 69.54  ?  55  ALA A C   1 
ATOM 408  O O   . ALA A 1 55  ? 45.668  6.516   28.109  1.00 78.14  ?  55  ALA A O   1 
ATOM 409  C CB  . ALA A 1 55  ? 42.993  7.790   29.999  1.00 58.51  ?  55  ALA A CB  1 
ATOM 410  N N   . SER A 1 56  ? 45.203  5.880   30.208  1.00 67.32  ?  56  SER A N   1 
ATOM 411  C CA  . SER A 1 56  ? 45.864  4.589   30.085  1.00 70.84  ?  56  SER A CA  1 
ATOM 412  C C   . SER A 1 56  ? 44.854  3.565   29.579  1.00 73.23  ?  56  SER A C   1 
ATOM 413  O O   . SER A 1 56  ? 43.839  3.306   30.235  1.00 70.57  ?  56  SER A O   1 
ATOM 414  C CB  . SER A 1 56  ? 46.464  4.152   31.421  1.00 77.77  ?  56  SER A CB  1 
ATOM 415  O OG  . SER A 1 56  ? 47.560  4.973   31.784  1.00 87.19  ?  56  SER A OG  1 
ATOM 416  N N   . GLY A 1 57  ? 45.114  3.011   28.400  1.00 78.92  ?  57  GLY A N   1 
ATOM 417  C CA  . GLY A 1 57  ? 44.259  1.979   27.853  1.00 79.34  ?  57  GLY A CA  1 
ATOM 418  C C   . GLY A 1 57  ? 43.125  2.479   26.993  1.00 77.07  ?  57  GLY A C   1 
ATOM 419  O O   . GLY A 1 57  ? 42.136  1.759   26.816  1.00 69.30  ?  57  GLY A O   1 
ATOM 420  N N   . VAL A 1 58  ? 43.224  3.692   26.470  1.00 78.37  ?  58  VAL A N   1 
ATOM 421  C CA  . VAL A 1 58  ? 42.206  4.276   25.600  1.00 75.13  ?  58  VAL A CA  1 
ATOM 422  C C   . VAL A 1 58  ? 42.775  4.322   24.188  1.00 70.41  ?  58  VAL A C   1 
ATOM 423  O O   . VAL A 1 58  ? 43.879  4.843   23.995  1.00 71.83  ?  58  VAL A O   1 
ATOM 424  C CB  . VAL A 1 58  ? 41.791  5.684   26.069  1.00 70.72  ?  58  VAL A CB  1 
ATOM 425  C CG1 . VAL A 1 58  ? 40.771  6.284   25.112  1.00 62.89  ?  58  VAL A CG1 1 
ATOM 426  C CG2 . VAL A 1 58  ? 41.230  5.627   27.484  1.00 66.62  ?  58  VAL A CG2 1 
ATOM 427  N N   . PRO A 1 59  ? 42.066  3.806   23.185  1.00 67.13  ?  59  PRO A N   1 
ATOM 428  C CA  . PRO A 1 59  ? 42.630  3.764   21.832  1.00 67.98  ?  59  PRO A CA  1 
ATOM 429  C C   . PRO A 1 59  ? 42.907  5.158   21.292  1.00 61.61  ?  59  PRO A C   1 
ATOM 430  O O   . PRO A 1 59  ? 42.318  6.150   21.726  1.00 64.66  ?  59  PRO A O   1 
ATOM 431  C CB  . PRO A 1 59  ? 41.544  3.051   21.015  1.00 69.21  ?  59  PRO A CB  1 
ATOM 432  C CG  . PRO A 1 59  ? 40.292  3.188   21.821  1.00 65.06  ?  59  PRO A CG  1 
ATOM 433  C CD  . PRO A 1 59  ? 40.733  3.185   23.251  1.00 70.55  ?  59  PRO A CD  1 
ATOM 434  N N   . SER A 1 60  ? 43.828  5.221   20.325  1.00 57.61  ?  60  SER A N   1 
ATOM 435  C CA  . SER A 1 60  ? 44.281  6.505   19.798  1.00 53.97  ?  60  SER A CA  1 
ATOM 436  C C   . SER A 1 60  ? 43.231  7.216   18.957  1.00 51.22  ?  60  SER A C   1 
ATOM 437  O O   . SER A 1 60  ? 43.409  8.403   18.664  1.00 52.13  ?  60  SER A O   1 
ATOM 438  C CB  . SER A 1 60  ? 45.556  6.326   18.974  1.00 50.86  ?  60  SER A CB  1 
ATOM 439  O OG  . SER A 1 60  ? 46.636  5.916   19.793  1.00 60.26  ?  60  SER A OG  1 
ATOM 440  N N   . ARG A 1 61  ? 42.150  6.535   18.569  1.00 52.35  ?  61  ARG A N   1 
ATOM 441  C CA  . ARG A 1 61  ? 41.119  7.172   17.757  1.00 53.95  ?  61  ARG A CA  1 
ATOM 442  C C   . ARG A 1 61  ? 40.252  8.135   18.558  1.00 54.93  ?  61  ARG A C   1 
ATOM 443  O O   . ARG A 1 61  ? 39.365  8.773   17.978  1.00 59.27  ?  61  ARG A O   1 
ATOM 444  C CB  . ARG A 1 61  ? 40.241  6.117   17.080  1.00 55.70  ?  61  ARG A CB  1 
ATOM 445  C CG  . ARG A 1 61  ? 39.756  5.031   18.004  1.00 57.64  ?  61  ARG A CG  1 
ATOM 446  C CD  . ARG A 1 61  ? 39.106  3.886   17.244  1.00 55.31  ?  61  ARG A CD  1 
ATOM 447  N NE  . ARG A 1 61  ? 38.607  2.869   18.166  1.00 64.80  ?  61  ARG A NE  1 
ATOM 448  C CZ  . ARG A 1 61  ? 37.462  2.969   18.834  1.00 64.23  ?  61  ARG A CZ  1 
ATOM 449  N NH1 . ARG A 1 61  ? 36.698  4.043   18.668  1.00 61.17  ?  61  ARG A NH1 1 
ATOM 450  N NH2 . ARG A 1 61  ? 37.081  2.001   19.662  1.00 57.29  ?  61  ARG A NH2 1 
ATOM 451  N N   . PHE A 1 62  ? 40.467  8.240   19.865  1.00 53.85  ?  62  PHE A N   1 
ATOM 452  C CA  . PHE A 1 62  ? 39.868  9.284   20.683  1.00 48.83  ?  62  PHE A CA  1 
ATOM 453  C C   . PHE A 1 62  ? 40.888  10.402  20.840  1.00 50.06  ?  62  PHE A C   1 
ATOM 454  O O   . PHE A 1 62  ? 42.043  10.142  21.194  1.00 50.17  ?  62  PHE A O   1 
ATOM 455  C CB  . PHE A 1 62  ? 39.447  8.750   22.053  1.00 46.47  ?  62  PHE A CB  1 
ATOM 456  C CG  . PHE A 1 62  ? 38.278  7.804   22.006  1.00 46.90  ?  62  PHE A CG  1 
ATOM 457  C CD1 . PHE A 1 62  ? 36.977  8.283   22.021  1.00 47.57  ?  62  PHE A CD1 1 
ATOM 458  C CD2 . PHE A 1 62  ? 38.480  6.435   21.958  1.00 51.54  ?  62  PHE A CD2 1 
ATOM 459  C CE1 . PHE A 1 62  ? 35.898  7.412   21.979  1.00 47.62  ?  62  PHE A CE1 1 
ATOM 460  C CE2 . PHE A 1 62  ? 37.409  5.561   21.915  1.00 49.72  ?  62  PHE A CE2 1 
ATOM 461  C CZ  . PHE A 1 62  ? 36.116  6.049   21.925  1.00 46.03  ?  62  PHE A CZ  1 
ATOM 462  N N   . SER A 1 63  ? 40.481  11.634  20.526  1.00 51.11  ?  63  SER A N   1 
ATOM 463  C CA  . SER A 1 63  ? 41.379  12.776  20.625  1.00 50.43  ?  63  SER A CA  1 
ATOM 464  C C   . SER A 1 63  ? 40.650  13.963  21.239  1.00 55.37  ?  63  SER A C   1 
ATOM 465  O O   . SER A 1 63  ? 39.433  14.100  21.104  1.00 54.44  ?  63  SER A O   1 
ATOM 466  C CB  . SER A 1 63  ? 41.945  13.154  19.255  1.00 47.14  ?  63  SER A CB  1 
ATOM 467  O OG  . SER A 1 63  ? 40.900  13.344  18.318  1.00 58.64  ?  63  SER A OG  1 
ATOM 468  N N   . GLY A 1 64  ? 41.405  14.810  21.925  1.00 56.03  ?  64  GLY A N   1 
ATOM 469  C CA  . GLY A 1 64  ? 40.850  16.013  22.531  1.00 50.09  ?  64  GLY A CA  1 
ATOM 470  C C   . GLY A 1 64  ? 41.650  17.235  22.140  1.00 52.72  ?  64  GLY A C   1 
ATOM 471  O O   . GLY A 1 64  ? 42.870  17.171  21.997  1.00 53.17  ?  64  GLY A O   1 
ATOM 472  N N   . SER A 1 65  ? 40.945  18.356  21.965  1.00 54.35  ?  65  SER A N   1 
ATOM 473  C CA  . SER A 1 65  ? 41.557  19.604  21.518  1.00 60.97  ?  65  SER A CA  1 
ATOM 474  C C   . SER A 1 65  ? 40.928  20.800  22.227  1.00 57.82  ?  65  SER A C   1 
ATOM 475  O O   . SER A 1 65  ? 39.742  20.789  22.564  1.00 53.60  ?  65  SER A O   1 
ATOM 476  C CB  . SER A 1 65  ? 41.430  19.779  19.998  1.00 56.87  ?  65  SER A CB  1 
ATOM 477  O OG  . SER A 1 65  ? 41.746  21.110  19.621  1.00 63.04  ?  65  SER A OG  1 
ATOM 478  N N   . ARG A 1 66  ? 41.723  21.858  22.401  1.00 52.90  ?  66  ARG A N   1 
ATOM 479  C CA  . ARG A 1 66  ? 41.282  23.072  23.074  1.00 55.73  ?  66  ARG A CA  1 
ATOM 480  C C   . ARG A 1 66  ? 41.473  24.289  22.177  1.00 64.41  ?  66  ARG A C   1 
ATOM 481  O O   . ARG A 1 66  ? 42.475  24.401  21.462  1.00 61.87  ?  66  ARG A O   1 
ATOM 482  C CB  . ARG A 1 66  ? 42.054  23.293  24.381  1.00 53.20  ?  66  ARG A CB  1 
ATOM 483  C CG  . ARG A 1 66  ? 41.622  24.526  25.156  1.00 53.12  ?  66  ARG A CG  1 
ATOM 484  C CD  . ARG A 1 66  ? 42.767  25.112  25.967  1.00 60.97  ?  66  ARG A CD  1 
ATOM 485  N NE  . ARG A 1 66  ? 42.345  26.272  26.754  1.00 69.26  ?  66  ARG A NE  1 
ATOM 486  C CZ  . ARG A 1 66  ? 43.180  27.115  27.355  1.00 70.78  ?  66  ARG A CZ  1 
ATOM 487  N NH1 . ARG A 1 66  ? 42.709  28.142  28.056  1.00 62.05  ?  66  ARG A NH1 1 
ATOM 488  N NH2 . ARG A 1 66  ? 44.490  26.933  27.250  1.00 74.21  ?  66  ARG A NH2 1 
ATOM 489  N N   . SER A 1 67  ? 40.502  25.202  22.223  1.00 58.02  ?  67  SER A N   1 
ATOM 490  C CA  . SER A 1 67  ? 40.594  26.493  21.547  1.00 52.78  ?  67  SER A CA  1 
ATOM 491  C C   . SER A 1 67  ? 39.909  27.490  22.479  1.00 57.59  ?  67  SER A C   1 
ATOM 492  O O   . SER A 1 67  ? 38.683  27.637  22.457  1.00 59.53  ?  67  SER A O   1 
ATOM 493  C CB  . SER A 1 67  ? 39.946  26.445  20.170  1.00 56.12  ?  67  SER A CB  1 
ATOM 494  O OG  . SER A 1 67  ? 40.138  27.662  19.473  1.00 56.43  ?  67  SER A OG  1 
ATOM 495  N N   . GLY A 1 68  ? 40.706  28.149  23.318  1.00 57.41  ?  68  GLY A N   1 
ATOM 496  C CA  . GLY A 1 68  ? 40.168  29.064  24.304  1.00 54.32  ?  68  GLY A CA  1 
ATOM 497  C C   . GLY A 1 68  ? 39.245  28.382  25.291  1.00 59.12  ?  68  GLY A C   1 
ATOM 498  O O   . GLY A 1 68  ? 39.698  27.642  26.170  1.00 59.62  ?  68  GLY A O   1 
ATOM 499  N N   . THR A 1 69  ? 37.941  28.620  25.153  1.00 60.79  ?  69  THR A N   1 
ATOM 500  C CA  . THR A 1 69  ? 36.944  27.999  26.012  1.00 57.93  ?  69  THR A CA  1 
ATOM 501  C C   . THR A 1 69  ? 36.166  26.894  25.314  1.00 57.04  ?  69  THR A C   1 
ATOM 502  O O   . THR A 1 69  ? 35.263  26.312  25.925  1.00 61.30  ?  69  THR A O   1 
ATOM 503  C CB  . THR A 1 69  ? 35.963  29.053  26.541  1.00 63.14  ?  69  THR A CB  1 
ATOM 504  O OG1 . THR A 1 69  ? 35.286  29.676  25.443  1.00 62.95  ?  69  THR A OG1 1 
ATOM 505  C CG2 . THR A 1 69  ? 36.703  30.118  27.338  1.00 61.24  ?  69  THR A CG2 1 
ATOM 506  N N   . LYS A 1 70  ? 36.475  26.597  24.053  1.00 60.30  ?  70  LYS A N   1 
ATOM 507  C CA  . LYS A 1 70  ? 35.787  25.548  23.308  1.00 61.31  ?  70  LYS A CA  1 
ATOM 508  C C   . LYS A 1 70  ? 36.660  24.300  23.287  1.00 57.14  ?  70  LYS A C   1 
ATOM 509  O O   . LYS A 1 70  ? 37.805  24.344  22.824  1.00 59.48  ?  70  LYS A O   1 
ATOM 510  C CB  . LYS A 1 70  ? 35.447  25.995  21.886  1.00 62.65  ?  70  LYS A CB  1 
ATOM 511  C CG  . LYS A 1 70  ? 34.567  24.993  21.137  1.00 65.86  ?  70  LYS A CG  1 
ATOM 512  C CD  . LYS A 1 70  ? 34.148  25.507  19.760  1.00 86.65  ?  70  LYS A CD  1 
ATOM 513  C CE  . LYS A 1 70  ? 33.298  26.770  19.873  1.00 98.98  ?  70  LYS A CE  1 
ATOM 514  N NZ  . LYS A 1 70  ? 32.817  27.254  18.546  1.00 100.84 ?  70  LYS A NZ  1 
ATOM 515  N N   . PHE A 1 71  ? 36.128  23.200  23.802  1.00 51.36  ?  71  PHE A N   1 
ATOM 516  C CA  . PHE A 1 71  ? 36.830  21.928  23.840  1.00 55.92  ?  71  PHE A CA  1 
ATOM 517  C C   . PHE A 1 71  ? 36.148  20.940  22.899  1.00 55.57  ?  71  PHE A C   1 
ATOM 518  O O   . PHE A 1 71  ? 34.918  20.929  22.776  1.00 54.05  ?  71  PHE A O   1 
ATOM 519  C CB  . PHE A 1 71  ? 36.877  21.390  25.277  1.00 51.00  ?  71  PHE A CB  1 
ATOM 520  C CG  . PHE A 1 71  ? 37.596  22.303  26.241  1.00 50.60  ?  71  PHE A CG  1 
ATOM 521  C CD1 . PHE A 1 71  ? 36.956  23.410  26.786  1.00 48.74  ?  71  PHE A CD1 1 
ATOM 522  C CD2 . PHE A 1 71  ? 38.917  22.056  26.596  1.00 50.57  ?  71  PHE A CD2 1 
ATOM 523  C CE1 . PHE A 1 71  ? 37.620  24.251  27.667  1.00 50.53  ?  71  PHE A CE1 1 
ATOM 524  C CE2 . PHE A 1 71  ? 39.587  22.890  27.478  1.00 49.29  ?  71  PHE A CE2 1 
ATOM 525  C CZ  . PHE A 1 71  ? 38.939  23.989  28.014  1.00 49.64  ?  71  PHE A CZ  1 
ATOM 526  N N   . THR A 1 72  ? 36.946  20.121  22.219  1.00 51.32  ?  72  THR A N   1 
ATOM 527  C CA  . THR A 1 72  ? 36.437  19.233  21.183  1.00 53.08  ?  72  THR A CA  1 
ATOM 528  C C   . THR A 1 72  ? 36.966  17.825  21.397  1.00 52.05  ?  72  THR A C   1 
ATOM 529  O O   . THR A 1 72  ? 38.181  17.622  21.492  1.00 55.75  ?  72  THR A O   1 
ATOM 530  C CB  . THR A 1 72  ? 36.830  19.732  19.782  1.00 53.76  ?  72  THR A CB  1 
ATOM 531  O OG1 . THR A 1 72  ? 36.086  20.914  19.464  1.00 51.27  ?  72  THR A OG1 1 
ATOM 532  C CG2 . THR A 1 72  ? 36.557  18.667  18.737  1.00 48.73  ?  72  THR A CG2 1 
ATOM 533  N N   . LEU A 1 73  ? 36.051  16.862  21.470  1.00 51.47  ?  73  LEU A N   1 
ATOM 534  C CA  . LEU A 1 73  ? 36.375  15.442  21.512  1.00 48.28  ?  73  LEU A CA  1 
ATOM 535  C C   . LEU A 1 73  ? 36.049  14.836  20.158  1.00 48.39  ?  73  LEU A C   1 
ATOM 536  O O   . LEU A 1 73  ? 34.913  14.944  19.690  1.00 48.50  ?  73  LEU A O   1 
ATOM 537  C CB  . LEU A 1 73  ? 35.582  14.720  22.607  1.00 46.15  ?  73  LEU A CB  1 
ATOM 538  C CG  . LEU A 1 73  ? 35.685  13.190  22.631  1.00 43.63  ?  73  LEU A CG  1 
ATOM 539  C CD1 . LEU A 1 73  ? 37.060  12.724  23.110  1.00 42.09  ?  73  LEU A CD1 1 
ATOM 540  C CD2 . LEU A 1 73  ? 34.569  12.564  23.454  1.00 42.51  ?  73  LEU A CD2 1 
ATOM 541  N N   . THR A 1 74  ? 37.029  14.180  19.545  1.00 52.64  ?  74  THR A N   1 
ATOM 542  C CA  . THR A 1 74  ? 36.881  13.624  18.206  1.00 57.74  ?  74  THR A CA  1 
ATOM 543  C C   . THR A 1 74  ? 37.133  12.125  18.223  1.00 57.66  ?  74  THR A C   1 
ATOM 544  O O   . THR A 1 74  ? 38.180  11.669  18.700  1.00 59.17  ?  74  THR A O   1 
ATOM 545  C CB  . THR A 1 74  ? 37.836  14.279  17.211  1.00 51.11  ?  74  THR A CB  1 
ATOM 546  O OG1 . THR A 1 74  ? 37.509  15.665  17.077  1.00 58.91  ?  74  THR A OG1 1 
ATOM 547  C CG2 . THR A 1 74  ? 37.725  13.602  15.865  1.00 58.61  ?  74  THR A CG2 1 
ATOM 548  N N   . ILE A 1 75  ? 36.184  11.373  17.680  1.00 50.86  ?  75  ILE A N   1 
ATOM 549  C CA  . ILE A 1 75  ? 36.368  9.959   17.393  1.00 52.64  ?  75  ILE A CA  1 
ATOM 550  C C   . ILE A 1 75  ? 36.646  9.857   15.899  1.00 62.42  ?  75  ILE A C   1 
ATOM 551  O O   . ILE A 1 75  ? 35.765  10.119  15.071  1.00 60.26  ?  75  ILE A O   1 
ATOM 552  C CB  . ILE A 1 75  ? 35.140  9.135   17.793  1.00 50.50  ?  75  ILE A CB  1 
ATOM 553  C CG1 . ILE A 1 75  ? 34.738  9.444   19.232  1.00 49.95  ?  75  ILE A CG1 1 
ATOM 554  C CG2 . ILE A 1 75  ? 35.409  7.647   17.615  1.00 56.73  ?  75  ILE A CG2 1 
ATOM 555  C CD1 . ILE A 1 75  ? 33.476  8.736   19.670  1.00 40.50  ?  75  ILE A CD1 1 
ATOM 556  N N   . SER A 1 76  ? 37.882  9.493   15.552  1.00 59.60  ?  76  SER A N   1 
ATOM 557  C CA  . SER A 1 76  ? 38.311  9.556   14.159  1.00 64.71  ?  76  SER A CA  1 
ATOM 558  C C   . SER A 1 76  ? 37.670  8.445   13.333  1.00 70.40  ?  76  SER A C   1 
ATOM 559  O O   . SER A 1 76  ? 37.157  8.693   12.233  1.00 67.05  ?  76  SER A O   1 
ATOM 560  C CB  . SER A 1 76  ? 39.837  9.497   14.080  1.00 60.83  ?  76  SER A CB  1 
ATOM 561  O OG  . SER A 1 76  ? 40.332  8.305   14.657  1.00 61.34  ?  76  SER A OG  1 
ATOM 562  N N   . SER A 1 77  ? 37.712  7.210   13.832  1.00 60.11  ?  77  SER A N   1 
ATOM 563  C CA  . SER A 1 77  ? 37.093  6.065   13.164  1.00 60.95  ?  77  SER A CA  1 
ATOM 564  C C   . SER A 1 77  ? 36.106  5.421   14.132  1.00 53.29  ?  77  SER A C   1 
ATOM 565  O O   . SER A 1 77  ? 36.506  4.644   15.004  1.00 59.47  ?  77  SER A O   1 
ATOM 566  C CB  . SER A 1 77  ? 38.147  5.061   12.697  1.00 66.57  ?  77  SER A CB  1 
ATOM 567  O OG  . SER A 1 77  ? 37.564  4.031   11.912  1.00 59.47  ?  77  SER A OG  1 
ATOM 568  N N   . LEU A 1 78  ? 34.817  5.699   13.954  1.00 48.89  ?  78  LEU A N   1 
ATOM 569  C CA  . LEU A 1 78  ? 33.815  5.166   14.867  1.00 52.22  ?  78  LEU A CA  1 
ATOM 570  C C   . LEU A 1 78  ? 33.762  3.645   14.767  1.00 52.81  ?  78  LEU A C   1 
ATOM 571  O O   . LEU A 1 78  ? 33.692  3.085   13.670  1.00 52.13  ?  78  LEU A O   1 
ATOM 572  C CB  . LEU A 1 78  ? 32.444  5.765   14.554  1.00 50.29  ?  78  LEU A CB  1 
ATOM 573  C CG  . LEU A 1 78  ? 31.431  5.720   15.697  1.00 51.93  ?  78  LEU A CG  1 
ATOM 574  C CD1 . LEU A 1 78  ? 31.959  6.520   16.873  1.00 59.18  ?  78  LEU A CD1 1 
ATOM 575  C CD2 . LEU A 1 78  ? 30.071  6.237   15.264  1.00 45.95  ?  78  LEU A CD2 1 
ATOM 576  N N   . GLN A 1 79  ? 33.804  2.977   15.918  1.00 56.90  ?  79  GLN A N   1 
ATOM 577  C CA  . GLN A 1 79  ? 33.747  1.525   15.995  1.00 57.86  ?  79  GLN A CA  1 
ATOM 578  C C   . GLN A 1 79  ? 32.454  1.076   16.660  1.00 55.24  ?  79  GLN A C   1 
ATOM 579  O O   . GLN A 1 79  ? 31.876  1.805   17.470  1.00 51.28  ?  79  GLN A O   1 
ATOM 580  C CB  . GLN A 1 79  ? 34.938  0.966   16.784  1.00 58.65  ?  79  GLN A CB  1 
ATOM 581  C CG  . GLN A 1 79  ? 36.277  1.340   16.187  1.00 65.07  ?  79  GLN A CG  1 
ATOM 582  C CD  . GLN A 1 79  ? 36.404  0.922   14.742  1.00 56.74  ?  79  GLN A CD  1 
ATOM 583  O OE1 . GLN A 1 79  ? 36.737  1.738   13.879  1.00 51.42  ?  79  GLN A OE1 1 
ATOM 584  N NE2 . GLN A 1 79  ? 36.141  -0.349  14.466  1.00 51.89  ?  79  GLN A NE2 1 
ATOM 585  N N   . PRO A 1 80  ? 31.993  -0.146  16.377  1.00 54.58  ?  80  PRO A N   1 
ATOM 586  C CA  . PRO A 1 80  ? 30.721  -0.589  16.967  1.00 56.70  ?  80  PRO A CA  1 
ATOM 587  C C   . PRO A 1 80  ? 30.711  -0.604  18.492  1.00 53.16  ?  80  PRO A C   1 
ATOM 588  O O   . PRO A 1 80  ? 29.619  -0.625  19.071  1.00 52.54  ?  80  PRO A O   1 
ATOM 589  C CB  . PRO A 1 80  ? 30.530  -1.993  16.369  1.00 50.17  ?  80  PRO A CB  1 
ATOM 590  C CG  . PRO A 1 80  ? 31.906  -2.419  15.966  1.00 53.40  ?  80  PRO A CG  1 
ATOM 591  C CD  . PRO A 1 80  ? 32.544  -1.158  15.464  1.00 47.65  ?  80  PRO A CD  1 
ATOM 592  N N   . GLU A 1 81  ? 31.861  -0.477  19.155  1.00 55.64  ?  81  GLU A N   1 
ATOM 593  C CA  . GLU A 1 81  ? 31.929  -0.519  20.612  1.00 58.91  ?  81  GLU A CA  1 
ATOM 594  C C   . GLU A 1 81  ? 31.958  0.873   21.228  1.00 53.89  ?  81  GLU A C   1 
ATOM 595  O O   . GLU A 1 81  ? 32.154  0.998   22.441  1.00 48.72  ?  81  GLU A O   1 
ATOM 596  C CB  . GLU A 1 81  ? 33.140  -1.332  21.101  1.00 48.59  ?  81  GLU A CB  1 
ATOM 597  C CG  . GLU A 1 81  ? 34.505  -0.877  20.595  1.00 50.61  ?  81  GLU A CG  1 
ATOM 598  C CD  . GLU A 1 81  ? 34.980  -1.637  19.370  1.00 62.77  ?  81  GLU A CD  1 
ATOM 599  O OE1 . GLU A 1 81  ? 34.131  -2.178  18.630  1.00 61.35  ?  81  GLU A OE1 1 
ATOM 600  O OE2 . GLU A 1 81  ? 36.210  -1.685  19.147  1.00 68.26  ?  81  GLU A OE2 1 
ATOM 601  N N   . ASP A 1 82  ? 31.788  1.917   20.420  1.00 52.16  ?  82  ASP A N   1 
ATOM 602  C CA  . ASP A 1 82  ? 31.790  3.283   20.924  1.00 49.60  ?  82  ASP A CA  1 
ATOM 603  C C   . ASP A 1 82  ? 30.395  3.776   21.273  1.00 45.96  ?  82  ASP A C   1 
ATOM 604  O O   . ASP A 1 82  ? 30.257  4.903   21.759  1.00 46.49  ?  82  ASP A O   1 
ATOM 605  C CB  . ASP A 1 82  ? 32.426  4.240   19.918  1.00 45.73  ?  82  ASP A CB  1 
ATOM 606  C CG  . ASP A 1 82  ? 33.817  3.817   19.518  1.00 56.43  ?  82  ASP A CG  1 
ATOM 607  O OD1 . ASP A 1 82  ? 34.168  3.963   18.324  1.00 64.31  ?  82  ASP A OD1 1 
ATOM 608  O OD2 . ASP A 1 82  ? 34.563  3.333   20.394  1.00 55.56  ?  82  ASP A OD2 1 
ATOM 609  N N   . PHE A 1 83  ? 29.368  2.960   21.040  1.00 45.23  ?  83  PHE A N   1 
ATOM 610  C CA  . PHE A 1 83  ? 28.007  3.291   21.431  1.00 44.87  ?  83  PHE A CA  1 
ATOM 611  C C   . PHE A 1 83  ? 27.945  3.539   22.932  1.00 49.32  ?  83  PHE A C   1 
ATOM 612  O O   . PHE A 1 83  ? 28.140  2.622   23.735  1.00 50.17  ?  83  PHE A O   1 
ATOM 613  C CB  . PHE A 1 83  ? 27.056  2.163   21.033  1.00 51.41  ?  83  PHE A CB  1 
ATOM 614  C CG  . PHE A 1 83  ? 25.772  2.154   21.809  1.00 61.52  ?  83  PHE A CG  1 
ATOM 615  C CD1 . PHE A 1 83  ? 25.590  1.274   22.864  1.00 57.05  ?  83  PHE A CD1 1 
ATOM 616  C CD2 . PHE A 1 83  ? 24.748  3.030   21.487  1.00 63.81  ?  83  PHE A CD2 1 
ATOM 617  C CE1 . PHE A 1 83  ? 24.411  1.269   23.584  1.00 61.02  ?  83  PHE A CE1 1 
ATOM 618  C CE2 . PHE A 1 83  ? 23.560  3.025   22.202  1.00 67.04  ?  83  PHE A CE2 1 
ATOM 619  C CZ  . PHE A 1 83  ? 23.393  2.145   23.254  1.00 59.31  ?  83  PHE A CZ  1 
ATOM 620  N N   . ALA A 1 84  ? 27.715  4.784   23.314  1.00 58.54  ?  84  ALA A N   1 
ATOM 621  C CA  . ALA A 1 84  ? 27.745  5.210   24.709  1.00 52.91  ?  84  ALA A CA  1 
ATOM 622  C C   . ALA A 1 84  ? 27.192  6.629   24.782  1.00 45.77  ?  84  ALA A C   1 
ATOM 623  O O   . ALA A 1 84  ? 26.621  7.147   23.814  1.00 52.07  ?  84  ALA A O   1 
ATOM 624  C CB  . ALA A 1 84  ? 29.166  5.138   25.272  1.00 49.42  ?  84  ALA A CB  1 
ATOM 625  N N   . THR A 1 85  ? 27.330  7.243   25.951  1.00 46.82  ?  85  THR A N   1 
ATOM 626  C CA  . THR A 1 85  ? 27.060  8.659   26.142  1.00 47.54  ?  85  THR A CA  1 
ATOM 627  C C   . THR A 1 85  ? 28.340  9.310   26.640  1.00 50.42  ?  85  THR A C   1 
ATOM 628  O O   . THR A 1 85  ? 28.965  8.824   27.592  1.00 48.41  ?  85  THR A O   1 
ATOM 629  C CB  . THR A 1 85  ? 25.903  8.903   27.111  1.00 48.59  ?  85  THR A CB  1 
ATOM 630  O OG1 . THR A 1 85  ? 24.718  8.272   26.608  1.00 46.35  ?  85  THR A OG1 1 
ATOM 631  C CG2 . THR A 1 85  ? 25.643  10.393  27.252  1.00 47.96  ?  85  THR A CG2 1 
ATOM 632  N N   . TYR A 1 86  ? 28.724  10.407  26.007  1.00 48.10  ?  86  TYR A N   1 
ATOM 633  C CA  . TYR A 1 86  ? 29.988  11.061  26.291  1.00 46.45  ?  86  TYR A CA  1 
ATOM 634  C C   . TYR A 1 86  ? 29.728  12.365  27.025  1.00 49.93  ?  86  TYR A C   1 
ATOM 635  O O   . TYR A 1 86  ? 28.768  13.080  26.719  1.00 52.41  ?  86  TYR A O   1 
ATOM 636  C CB  . TYR A 1 86  ? 30.771  11.299  24.997  1.00 44.94  ?  86  TYR A CB  1 
ATOM 637  C CG  . TYR A 1 86  ? 31.168  10.004  24.340  1.00 43.02  ?  86  TYR A CG  1 
ATOM 638  C CD1 . TYR A 1 86  ? 30.254  9.273   23.587  1.00 44.46  ?  86  TYR A CD1 1 
ATOM 639  C CD2 . TYR A 1 86  ? 32.453  9.495   24.491  1.00 44.75  ?  86  TYR A CD2 1 
ATOM 640  C CE1 . TYR A 1 86  ? 30.606  8.068   23.000  1.00 44.82  ?  86  TYR A CE1 1 
ATOM 641  C CE2 . TYR A 1 86  ? 32.817  8.291   23.903  1.00 47.75  ?  86  TYR A CE2 1 
ATOM 642  C CZ  . TYR A 1 86  ? 31.890  7.585   23.157  1.00 43.37  ?  86  TYR A CZ  1 
ATOM 643  O OH  . TYR A 1 86  ? 32.247  6.393   22.573  1.00 38.61  ?  86  TYR A OH  1 
ATOM 644  N N   . TYR A 1 87  ? 30.566  12.639  28.026  1.00 53.89  ?  87  TYR A N   1 
ATOM 645  C CA  . TYR A 1 87  ? 30.413  13.804  28.885  1.00 49.36  ?  87  TYR A CA  1 
ATOM 646  C C   . TYR A 1 87  ? 31.733  14.553  28.998  1.00 52.35  ?  87  TYR A C   1 
ATOM 647  O O   . TYR A 1 87  ? 32.812  13.952  28.967  1.00 53.09  ?  87  TYR A O   1 
ATOM 648  C CB  . TYR A 1 87  ? 29.947  13.417  30.296  1.00 45.53  ?  87  TYR A CB  1 
ATOM 649  C CG  . TYR A 1 87  ? 28.569  12.798  30.383  1.00 44.77  ?  87  TYR A CG  1 
ATOM 650  C CD1 . TYR A 1 87  ? 27.432  13.585  30.512  1.00 45.96  ?  87  TYR A CD1 1 
ATOM 651  C CD2 . TYR A 1 87  ? 28.410  11.426  30.361  1.00 48.52  ?  87  TYR A CD2 1 
ATOM 652  C CE1 . TYR A 1 87  ? 26.172  13.015  30.602  1.00 44.28  ?  87  TYR A CE1 1 
ATOM 653  C CE2 . TYR A 1 87  ? 27.161  10.848  30.451  1.00 53.61  ?  87  TYR A CE2 1 
ATOM 654  C CZ  . TYR A 1 87  ? 26.044  11.644  30.571  1.00 52.59  ?  87  TYR A CZ  1 
ATOM 655  O OH  . TYR A 1 87  ? 24.803  11.055  30.660  1.00 58.35  ?  87  TYR A OH  1 
ATOM 656  N N   . CYS A 1 88  ? 31.638  15.870  29.148  1.00 56.14  ?  88  CYS A N   1 
ATOM 657  C CA  . CYS A 1 88  ? 32.774  16.696  29.525  1.00 53.18  ?  88  CYS A CA  1 
ATOM 658  C C   . CYS A 1 88  ? 32.605  17.136  30.970  1.00 51.23  ?  88  CYS A C   1 
ATOM 659  O O   . CYS A 1 88  ? 31.484  17.260  31.472  1.00 50.64  ?  88  CYS A O   1 
ATOM 660  C CB  . CYS A 1 88  ? 32.938  17.935  28.625  1.00 50.88  ?  88  CYS A CB  1 
ATOM 661  S SG  . CYS A 1 88  ? 31.442  18.908  28.260  1.00 68.33  ?  88  CYS A SG  1 
ATOM 662  N N   . LEU A 1 89  ? 33.734  17.324  31.644  1.00 53.74  ?  89  LEU A N   1 
ATOM 663  C CA  . LEU A 1 89  ? 33.768  17.794  33.022  1.00 57.93  ?  89  LEU A CA  1 
ATOM 664  C C   . LEU A 1 89  ? 34.779  18.924  33.105  1.00 56.88  ?  89  LEU A C   1 
ATOM 665  O O   . LEU A 1 89  ? 35.955  18.732  32.773  1.00 53.80  ?  89  LEU A O   1 
ATOM 666  C CB  . LEU A 1 89  ? 34.141  16.668  33.991  1.00 51.15  ?  89  LEU A CB  1 
ATOM 667  C CG  . LEU A 1 89  ? 34.273  17.107  35.448  1.00 56.30  ?  89  LEU A CG  1 
ATOM 668  C CD1 . LEU A 1 89  ? 32.931  17.610  35.951  1.00 60.21  ?  89  LEU A CD1 1 
ATOM 669  C CD2 . LEU A 1 89  ? 34.807  15.987  36.335  1.00 53.31  ?  89  LEU A CD2 1 
ATOM 670  N N   . GLY A 1 90  ? 34.323  20.096  33.520  1.00 61.52  ?  90  GLY A N   1 
ATOM 671  C CA  . GLY A 1 90  ? 35.190  21.254  33.682  1.00 65.50  ?  90  GLY A CA  1 
ATOM 672  C C   . GLY A 1 90  ? 35.197  21.692  35.133  1.00 69.56  ?  90  GLY A C   1 
ATOM 673  O O   . GLY A 1 90  ? 34.151  21.709  35.785  1.00 73.56  ?  90  GLY A O   1 
ATOM 674  N N   . ILE A 1 91  ? 36.378  22.046  35.635  1.00 75.23  ?  91  ILE A N   1 
ATOM 675  C CA  . ILE A 1 91  ? 36.539  22.439  37.032  1.00 79.86  ?  91  ILE A CA  1 
ATOM 676  C C   . ILE A 1 91  ? 37.239  23.790  37.075  1.00 84.91  ?  91  ILE A C   1 
ATOM 677  O O   . ILE A 1 91  ? 38.405  23.903  36.675  1.00 82.73  ?  91  ILE A O   1 
ATOM 678  C CB  . ILE A 1 91  ? 37.330  21.397  37.835  1.00 77.20  ?  91  ILE A CB  1 
ATOM 679  C CG1 . ILE A 1 91  ? 36.732  19.998  37.650  1.00 69.01  ?  91  ILE A CG1 1 
ATOM 680  C CG2 . ILE A 1 91  ? 37.377  21.784  39.305  1.00 87.74  ?  91  ILE A CG2 1 
ATOM 681  C CD1 . ILE A 1 91  ? 37.486  18.909  38.385  1.00 69.12  ?  91  ILE A CD1 1 
ATOM 682  N N   . TYR A 1 92  ? 36.532  24.815  37.553  1.00 92.60  ?  92  TYR A N   1 
ATOM 683  C CA  . TYR A 1 92  ? 37.128  26.132  37.772  1.00 92.42  ?  92  TYR A CA  1 
ATOM 684  C C   . TYR A 1 92  ? 37.898  26.067  39.084  1.00 90.49  ?  92  TYR A C   1 
ATOM 685  O O   . TYR A 1 92  ? 37.319  26.208  40.164  1.00 92.20  ?  92  TYR A O   1 
ATOM 686  C CB  . TYR A 1 92  ? 36.069  27.230  37.803  1.00 94.41  ?  92  TYR A CB  1 
ATOM 687  C CG  . TYR A 1 92  ? 36.636  28.634  37.648  1.00 99.59  ?  92  TYR A CG  1 
ATOM 688  C CD1 . TYR A 1 92  ? 36.243  29.449  36.589  1.00 102.76 ?  92  TYR A CD1 1 
ATOM 689  C CD2 . TYR A 1 92  ? 37.585  29.132  38.538  1.00 93.56  ?  92  TYR A CD2 1 
ATOM 690  C CE1 . TYR A 1 92  ? 36.763  30.724  36.432  1.00 103.62 ?  92  TYR A CE1 1 
ATOM 691  C CE2 . TYR A 1 92  ? 38.111  30.405  38.390  1.00 97.68  ?  92  TYR A CE2 1 
ATOM 692  C CZ  . TYR A 1 92  ? 37.696  31.197  37.335  1.00 106.86 ?  92  TYR A CZ  1 
ATOM 693  O OH  . TYR A 1 92  ? 38.215  32.465  37.180  1.00 107.04 ?  92  TYR A OH  1 
ATOM 694  N N   . GLY A 1 93  ? 39.203  25.841  39.000  1.00 90.35  ?  93  GLY A N   1 
ATOM 695  C CA  . GLY A 1 93  ? 40.024  25.900  40.189  1.00 93.67  ?  93  GLY A CA  1 
ATOM 696  C C   . GLY A 1 93  ? 39.764  24.774  41.168  1.00 100.23 ?  93  GLY A C   1 
ATOM 697  O O   . GLY A 1 93  ? 40.253  23.656  40.973  1.00 96.96  ?  93  GLY A O   1 
ATOM 698  N N   . ASP A 1 94  ? 38.995  25.050  42.225  1.00 101.30 ?  94  ASP A N   1 
ATOM 699  C CA  . ASP A 1 94  ? 38.734  24.064  43.267  1.00 105.99 ?  94  ASP A CA  1 
ATOM 700  C C   . ASP A 1 94  ? 37.294  23.568  43.306  1.00 107.42 ?  94  ASP A C   1 
ATOM 701  O O   . ASP A 1 94  ? 36.987  22.667  44.097  1.00 108.33 ?  94  ASP A O   1 
ATOM 702  C CB  . ASP A 1 94  ? 39.102  24.647  44.640  1.00 109.26 ?  94  ASP A CB  1 
ATOM 703  C CG  . ASP A 1 94  ? 38.426  25.994  44.914  1.00 107.64 ?  94  ASP A CG  1 
ATOM 704  O OD1 . ASP A 1 94  ? 37.615  26.454  44.075  1.00 109.37 ?  94  ASP A OD1 1 
ATOM 705  O OD2 . ASP A 1 94  ? 38.702  26.589  45.980  1.00 101.17 ?  94  ASP A OD2 1 
ATOM 706  N N   . GLY A 1 95  ? 36.413  24.095  42.458  1.00 102.71 ?  95  GLY A N   1 
ATOM 707  C CA  . GLY A 1 95  ? 35.031  23.658  42.435  1.00 103.14 ?  95  GLY A CA  1 
ATOM 708  C C   . GLY A 1 95  ? 34.072  24.514  43.238  1.00 109.83 ?  95  GLY A C   1 
ATOM 709  O O   . GLY A 1 95  ? 32.852  24.341  43.104  1.00 105.43 ?  95  GLY A O   1 
ATOM 710  N N   . ALA A 1 96  ? 34.586  25.418  44.072  1.00 107.56 ?  96  ALA A N   1 
ATOM 711  C CA  . ALA A 1 96  ? 33.746  26.307  44.862  1.00 104.84 ?  96  ALA A CA  1 
ATOM 712  C C   . ALA A 1 96  ? 32.852  27.158  43.968  1.00 108.80 ?  96  ALA A C   1 
ATOM 713  O O   . ALA A 1 96  ? 33.177  27.439  42.811  1.00 111.91 ?  96  ALA A O   1 
ATOM 714  C CB  . ALA A 1 96  ? 34.609  27.204  45.745  1.00 106.91 ?  96  ALA A CB  1 
ATOM 715  N N   . ASP A 1 97  ? 31.710  27.568  44.526  1.00 113.66 ?  97  ASP A N   1 
ATOM 716  C CA  . ASP A 1 97  ? 30.673  28.301  43.796  1.00 112.51 ?  97  ASP A CA  1 
ATOM 717  C C   . ASP A 1 97  ? 30.219  27.523  42.562  1.00 108.26 ?  97  ASP A C   1 
ATOM 718  O O   . ASP A 1 97  ? 30.105  28.068  41.461  1.00 105.17 ?  97  ASP A O   1 
ATOM 719  C CB  . ASP A 1 97  ? 31.158  29.703  43.412  1.00 114.55 ?  97  ASP A CB  1 
ATOM 720  C CG  . ASP A 1 97  ? 31.612  30.511  44.610  1.00 115.08 ?  97  ASP A CG  1 
ATOM 721  O OD1 . ASP A 1 97  ? 31.117  30.248  45.729  1.00 116.54 ?  97  ASP A OD1 1 
ATOM 722  O OD2 . ASP A 1 97  ? 32.464  31.409  44.428  1.00 111.42 ?  97  ASP A OD2 1 
ATOM 723  N N   . ASP A 1 98  ? 29.965  26.231  42.759  1.00 107.84 ?  98  ASP A N   1 
ATOM 724  C CA  . ASP A 1 98  ? 29.607  25.306  41.684  1.00 113.16 ?  98  ASP A CA  1 
ATOM 725  C C   . ASP A 1 98  ? 30.622  25.384  40.543  1.00 109.28 ?  98  ASP A C   1 
ATOM 726  O O   . ASP A 1 98  ? 30.287  25.631  39.381  1.00 100.86 ?  98  ASP A O   1 
ATOM 727  C CB  . ASP A 1 98  ? 28.181  25.562  41.184  1.00 112.79 ?  98  ASP A CB  1 
ATOM 728  C CG  . ASP A 1 98  ? 27.148  25.475  42.293  1.00 109.30 ?  98  ASP A CG  1 
ATOM 729  O OD1 . ASP A 1 98  ? 26.792  26.530  42.859  1.00 106.22 ?  98  ASP A OD1 1 
ATOM 730  O OD2 . ASP A 1 98  ? 26.702  24.349  42.604  1.00 101.59 ?  98  ASP A OD2 1 
ATOM 731  N N   . GLY A 1 99  ? 31.889  25.177  40.907  1.00 108.15 ?  99  GLY A N   1 
ATOM 732  C CA  . GLY A 1 99  ? 32.979  25.206  39.952  1.00 100.16 ?  99  GLY A CA  1 
ATOM 733  C C   . GLY A 1 99  ? 33.184  23.917  39.193  1.00 93.18  ?  99  GLY A C   1 
ATOM 734  O O   . GLY A 1 99  ? 33.919  23.902  38.202  1.00 87.56  ?  99  GLY A O   1 
ATOM 735  N N   . ILE A 1 100 ? 32.551  22.837  39.640  1.00 92.33  ?  100 ILE A N   1 
ATOM 736  C CA  . ILE A 1 100 ? 32.592  21.547  38.964  1.00 80.92  ?  100 ILE A CA  1 
ATOM 737  C C   . ILE A 1 100 ? 31.320  21.421  38.142  1.00 79.99  ?  100 ILE A C   1 
ATOM 738  O O   . ILE A 1 100 ? 30.214  21.391  38.697  1.00 83.95  ?  100 ILE A O   1 
ATOM 739  C CB  . ILE A 1 100 ? 32.711  20.394  39.972  1.00 81.43  ?  100 ILE A CB  1 
ATOM 740  C CG1 . ILE A 1 100 ? 34.030  20.488  40.742  1.00 82.51  ?  100 ILE A CG1 1 
ATOM 741  C CG2 . ILE A 1 100 ? 32.570  19.053  39.276  1.00 74.66  ?  100 ILE A CG2 1 
ATOM 742  C CD1 . ILE A 1 100 ? 34.113  19.536  41.915  1.00 85.28  ?  100 ILE A CD1 1 
ATOM 743  N N   . ALA A 1 101 ? 31.467  21.333  36.822  1.00 76.28  ?  101 ALA A N   1 
ATOM 744  C CA  . ALA A 1 101 ? 30.325  21.345  35.921  1.00 69.24  ?  101 ALA A CA  1 
ATOM 745  C C   . ALA A 1 101 ? 30.450  20.220  34.905  1.00 65.41  ?  101 ALA A C   1 
ATOM 746  O O   . ALA A 1 101 ? 31.484  20.079  34.240  1.00 62.67  ?  101 ALA A O   1 
ATOM 747  C CB  . ALA A 1 101 ? 30.205  22.695  35.207  1.00 71.57  ?  101 ALA A CB  1 
ATOM 748  N N   . PHE A 1 102 ? 29.396  19.421  34.797  1.00 58.25  ?  102 PHE A N   1 
ATOM 749  C CA  . PHE A 1 102 ? 29.315  18.383  33.788  1.00 52.03  ?  102 PHE A CA  1 
ATOM 750  C C   . PHE A 1 102 ? 28.587  18.918  32.565  1.00 53.64  ?  102 PHE A C   1 
ATOM 751  O O   . PHE A 1 102 ? 27.740  19.811  32.661  1.00 53.84  ?  102 PHE A O   1 
ATOM 752  C CB  . PHE A 1 102 ? 28.578  17.152  34.325  1.00 54.98  ?  102 PHE A CB  1 
ATOM 753  C CG  . PHE A 1 102 ? 29.453  16.201  35.091  1.00 52.94  ?  102 PHE A CG  1 
ATOM 754  C CD1 . PHE A 1 102 ? 30.324  15.355  34.428  1.00 48.09  ?  102 PHE A CD1 1 
ATOM 755  C CD2 . PHE A 1 102 ? 29.388  16.139  36.475  1.00 55.77  ?  102 PHE A CD2 1 
ATOM 756  C CE1 . PHE A 1 102 ? 31.126  14.482  35.128  1.00 50.29  ?  102 PHE A CE1 1 
ATOM 757  C CE2 . PHE A 1 102 ? 30.188  15.264  37.184  1.00 49.34  ?  102 PHE A CE2 1 
ATOM 758  C CZ  . PHE A 1 102 ? 31.059  14.435  36.511  1.00 47.51  ?  102 PHE A CZ  1 
ATOM 759  N N   . GLY A 1 103 ? 28.910  18.344  31.408  1.00 56.87  ?  103 GLY A N   1 
ATOM 760  C CA  . GLY A 1 103 ? 28.185  18.661  30.199  1.00 50.31  ?  103 GLY A CA  1 
ATOM 761  C C   . GLY A 1 103 ? 26.851  17.940  30.152  1.00 50.22  ?  103 GLY A C   1 
ATOM 762  O O   . GLY A 1 103 ? 26.551  17.065  30.966  1.00 58.81  ?  103 GLY A O   1 
ATOM 763  N N   . GLY A 1 104 ? 26.027  18.333  29.181  1.00 46.18  ?  104 GLY A N   1 
ATOM 764  C CA  . GLY A 1 104 ? 24.709  17.742  29.043  1.00 43.61  ?  104 GLY A CA  1 
ATOM 765  C C   . GLY A 1 104 ? 24.717  16.301  28.585  1.00 45.21  ?  104 GLY A C   1 
ATOM 766  O O   . GLY A 1 104 ? 23.733  15.590  28.814  1.00 46.49  ?  104 GLY A O   1 
ATOM 767  N N   . GLY A 1 105 ? 25.787  15.865  27.932  1.00 47.32  ?  105 GLY A N   1 
ATOM 768  C CA  . GLY A 1 105 ? 25.941  14.511  27.433  1.00 51.30  ?  105 GLY A CA  1 
ATOM 769  C C   . GLY A 1 105 ? 25.574  14.382  25.966  1.00 48.27  ?  105 GLY A C   1 
ATOM 770  O O   . GLY A 1 105 ? 24.705  15.091  25.449  1.00 52.76  ?  105 GLY A O   1 
ATOM 771  N N   . THR A 1 106 ? 26.234  13.445  25.281  1.00 52.76  ?  106 THR A N   1 
ATOM 772  C CA  . THR A 1 106 ? 25.961  13.160  23.872  1.00 50.97  ?  106 THR A CA  1 
ATOM 773  C C   . THR A 1 106 ? 25.829  11.656  23.682  1.00 46.93  ?  106 THR A C   1 
ATOM 774  O O   . THR A 1 106 ? 26.795  10.920  23.905  1.00 47.86  ?  106 THR A O   1 
ATOM 775  C CB  . THR A 1 106 ? 27.070  13.688  22.956  1.00 55.22  ?  106 THR A CB  1 
ATOM 776  O OG1 . THR A 1 106 ? 27.182  15.110  23.083  1.00 59.89  ?  106 THR A OG1 1 
ATOM 777  C CG2 . THR A 1 106 ? 26.743  13.347  21.512  1.00 51.30  ?  106 THR A CG2 1 
ATOM 778  N N   . LYS A 1 107 ? 24.653  11.209  23.239  1.00 47.35  ?  107 LYS A N   1 
ATOM 779  C CA  . LYS A 1 107 ? 24.392  9.794   22.991  1.00 47.67  ?  107 LYS A CA  1 
ATOM 780  C C   . LYS A 1 107 ? 24.765  9.469   21.550  1.00 52.90  ?  107 LYS A C   1 
ATOM 781  O O   . LYS A 1 107 ? 24.224  10.070  20.616  1.00 56.16  ?  107 LYS A O   1 
ATOM 782  C CB  . LYS A 1 107 ? 22.918  9.464   23.246  1.00 45.89  ?  107 LYS A CB  1 
ATOM 783  C CG  . LYS A 1 107 ? 22.546  7.980   23.069  1.00 60.27  ?  107 LYS A CG  1 
ATOM 784  C CD  . LYS A 1 107 ? 23.441  7.084   23.920  1.00 65.05  ?  107 LYS A CD  1 
ATOM 785  C CE  . LYS A 1 107 ? 22.806  5.754   24.273  1.00 59.31  ?  107 LYS A CE  1 
ATOM 786  N NZ  . LYS A 1 107 ? 23.655  5.066   25.281  1.00 49.77  ?  107 LYS A NZ  1 
ATOM 787  N N   . VAL A 1 108 ? 25.679  8.520   21.366  1.00 53.41  ?  108 VAL A N   1 
ATOM 788  C CA  . VAL A 1 108 ? 26.224  8.204   20.049  1.00 55.12  ?  108 VAL A CA  1 
ATOM 789  C C   . VAL A 1 108 ? 25.634  6.880   19.578  1.00 56.28  ?  108 VAL A C   1 
ATOM 790  O O   . VAL A 1 108 ? 26.062  5.811   20.025  1.00 58.33  ?  108 VAL A O   1 
ATOM 791  C CB  . VAL A 1 108 ? 27.755  8.156   20.065  1.00 53.60  ?  108 VAL A CB  1 
ATOM 792  C CG1 . VAL A 1 108 ? 28.277  7.794   18.694  1.00 52.73  ?  108 VAL A CG1 1 
ATOM 793  C CG2 . VAL A 1 108 ? 28.311  9.511   20.492  1.00 49.30  ?  108 VAL A CG2 1 
ATOM 794  N N   . GLU A 1 109 ? 24.640  6.937   18.689  1.00 59.55  ?  109 GLU A N   1 
ATOM 795  C CA  . GLU A 1 109 ? 24.148  5.711   18.079  1.00 61.66  ?  109 GLU A CA  1 
ATOM 796  C C   . GLU A 1 109 ? 25.039  5.337   16.893  1.00 62.37  ?  109 GLU A C   1 
ATOM 797  O O   . GLU A 1 109 ? 25.887  6.120   16.452  1.00 59.82  ?  109 GLU A O   1 
ATOM 798  C CB  . GLU A 1 109 ? 22.691  5.866   17.637  1.00 63.36  ?  109 GLU A CB  1 
ATOM 799  C CG  . GLU A 1 109 ? 21.749  6.393   18.722  1.00 70.01  ?  109 GLU A CG  1 
ATOM 800  C CD  . GLU A 1 109 ? 21.273  5.306   19.687  1.00 82.11  ?  109 GLU A CD  1 
ATOM 801  O OE1 . GLU A 1 109 ? 21.735  4.146   19.569  1.00 71.01  ?  109 GLU A OE1 1 
ATOM 802  O OE2 . GLU A 1 109 ? 20.430  5.616   20.563  1.00 84.66  ?  109 GLU A OE2 1 
ATOM 803  N N   . ILE A 1 110 ? 24.831  4.134   16.354  1.00 63.01  ?  110 ILE A N   1 
ATOM 804  C CA  . ILE A 1 110 ? 25.660  3.622   15.267  1.00 60.29  ?  110 ILE A CA  1 
ATOM 805  C C   . ILE A 1 110 ? 24.800  3.197   14.085  1.00 62.62  ?  110 ILE A C   1 
ATOM 806  O O   . ILE A 1 110 ? 23.869  2.398   14.241  1.00 56.82  ?  110 ILE A O   1 
ATOM 807  C CB  . ILE A 1 110 ? 26.549  2.463   15.744  1.00 52.81  ?  110 ILE A CB  1 
ATOM 808  C CG1 . ILE A 1 110 ? 27.547  3.000   16.771  1.00 48.97  ?  110 ILE A CG1 1 
ATOM 809  C CG2 . ILE A 1 110 ? 27.241  1.790   14.570  1.00 51.56  ?  110 ILE A CG2 1 
ATOM 810  C CD1 . ILE A 1 110 ? 28.476  1.973   17.305  1.00 53.13  ?  110 ILE A CD1 1 
ATOM 811  N N   . LYS A 1 111 ? 25.133  3.715   12.900  1.00 62.88  ?  111 LYS A N   1 
ATOM 812  C CA  . LYS A 1 111 ? 24.432  3.390   11.666  1.00 60.16  ?  111 LYS A CA  1 
ATOM 813  C C   . LYS A 1 111 ? 25.075  2.172   11.009  1.00 57.03  ?  111 LYS A C   1 
ATOM 814  O O   . LYS A 1 111 ? 26.293  2.139   10.800  1.00 53.15  ?  111 LYS A O   1 
ATOM 815  C CB  . LYS A 1 111 ? 24.437  4.588   10.713  1.00 66.27  ?  111 LYS A CB  1 
ATOM 816  C CG  . LYS A 1 111 ? 23.686  4.361   9.406   1.00 76.15  ?  111 LYS A CG  1 
ATOM 817  C CD  . LYS A 1 111 ? 22.205  4.727   9.519   1.00 80.74  ?  111 LYS A CD  1 
ATOM 818  C CE  . LYS A 1 111 ? 21.510  4.643   8.155   1.00 79.57  ?  111 LYS A CE  1 
ATOM 819  N NZ  . LYS A 1 111 ? 20.075  5.056   8.204   1.00 76.01  ?  111 LYS A NZ  1 
ATOM 820  N N   . ARG A 1 112 ? 24.249  1.189   10.660  1.00 55.32  ?  112 ARG A N   1 
ATOM 821  C CA  . ARG A 1 112 ? 24.695  -0.027  9.997   1.00 60.51  ?  112 ARG A CA  1 
ATOM 822  C C   . ARG A 1 112 ? 23.631  -0.473  9.003   1.00 62.49  ?  112 ARG A C   1 
ATOM 823  O O   . ARG A 1 112 ? 22.595  0.178   8.836   1.00 64.00  ?  112 ARG A O   1 
ATOM 824  C CB  . ARG A 1 112 ? 24.979  -1.145  11.003  1.00 58.85  ?  112 ARG A CB  1 
ATOM 825  C CG  . ARG A 1 112 ? 23.737  -1.585  11.753  1.00 56.19  ?  112 ARG A CG  1 
ATOM 826  C CD  . ARG A 1 112 ? 23.883  -2.968  12.336  1.00 57.35  ?  112 ARG A CD  1 
ATOM 827  N NE  . ARG A 1 112 ? 24.079  -3.964  11.288  1.00 59.85  ?  112 ARG A NE  1 
ATOM 828  C CZ  . ARG A 1 112 ? 24.162  -5.270  11.510  1.00 58.51  ?  112 ARG A CZ  1 
ATOM 829  N NH1 . ARG A 1 112 ? 24.337  -6.106  10.499  1.00 48.49  ?  112 ARG A NH1 1 
ATOM 830  N NH2 . ARG A 1 112 ? 24.075  -5.735  12.749  1.00 65.86  ?  112 ARG A NH2 1 
ATOM 831  N N   . THR A 1 113 ? 23.894  -1.593  8.335   1.00 58.21  ?  113 THR A N   1 
ATOM 832  C CA  . THR A 1 113 ? 22.952  -2.098  7.350   1.00 63.03  ?  113 THR A CA  1 
ATOM 833  C C   . THR A 1 113 ? 21.744  -2.721  8.042   1.00 58.76  ?  113 THR A C   1 
ATOM 834  O O   . THR A 1 113 ? 21.810  -3.168  9.189   1.00 67.32  ?  113 THR A O   1 
ATOM 835  C CB  . THR A 1 113 ? 23.608  -3.139  6.439   1.00 66.33  ?  113 THR A CB  1 
ATOM 836  O OG1 . THR A 1 113 ? 23.999  -4.278  7.217   1.00 62.16  ?  113 THR A OG1 1 
ATOM 837  C CG2 . THR A 1 113 ? 24.833  -2.550  5.750   1.00 57.34  ?  113 THR A CG2 1 
ATOM 838  N N   . VAL A 1 114 ? 20.630  -2.753  7.315   1.00 57.13  ?  114 VAL A N   1 
ATOM 839  C CA  . VAL A 1 114 ? 19.399  -3.330  7.836   1.00 57.02  ?  114 VAL A CA  1 
ATOM 840  C C   . VAL A 1 114 ? 19.589  -4.825  8.064   1.00 55.40  ?  114 VAL A C   1 
ATOM 841  O O   . VAL A 1 114 ? 20.184  -5.527  7.237   1.00 61.58  ?  114 VAL A O   1 
ATOM 842  C CB  . VAL A 1 114 ? 18.240  -3.051  6.862   1.00 57.68  ?  114 VAL A CB  1 
ATOM 843  C CG1 . VAL A 1 114 ? 16.928  -3.620  7.382   1.00 56.25  ?  114 VAL A CG1 1 
ATOM 844  C CG2 . VAL A 1 114 ? 18.118  -1.553  6.589   1.00 47.25  ?  114 VAL A CG2 1 
ATOM 845  N N   . ALA A 1 115 ? 19.109  -5.311  9.210   1.00 58.70  ?  115 ALA A N   1 
ATOM 846  C CA  . ALA A 1 115 ? 19.154  -6.726  9.565   1.00 57.93  ?  115 ALA A CA  1 
ATOM 847  C C   . ALA A 1 115 ? 17.789  -7.120  10.108  1.00 56.57  ?  115 ALA A C   1 
ATOM 848  O O   . ALA A 1 115 ? 17.219  -6.405  10.937  1.00 59.00  ?  115 ALA A O   1 
ATOM 849  C CB  . ALA A 1 115 ? 20.249  -7.015  10.594  1.00 57.58  ?  115 ALA A CB  1 
ATOM 850  N N   . ALA A 1 116 ? 17.272  -8.248  9.649   1.00 56.40  ?  116 ALA A N   1 
ATOM 851  C CA  . ALA A 1 116 ? 15.929  -8.647  10.051  1.00 56.95  ?  116 ALA A CA  1 
ATOM 852  C C   . ALA A 1 116 ? 15.941  -9.337  11.414  1.00 61.21  ?  116 ALA A C   1 
ATOM 853  O O   . ALA A 1 116 ? 16.897  -10.045 11.749  1.00 60.48  ?  116 ALA A O   1 
ATOM 854  C CB  . ALA A 1 116 ? 15.310  -9.574  9.010   1.00 59.56  ?  116 ALA A CB  1 
ATOM 855  N N   . PRO A 1 117 ? 14.900  -9.140  12.216  1.00 60.92  ?  117 PRO A N   1 
ATOM 856  C CA  . PRO A 1 117 ? 14.843  -9.792  13.523  1.00 53.67  ?  117 PRO A CA  1 
ATOM 857  C C   . PRO A 1 117 ? 14.405  -11.239 13.405  1.00 57.69  ?  117 PRO A C   1 
ATOM 858  O O   . PRO A 1 117 ? 13.720  -11.637 12.460  1.00 56.45  ?  117 PRO A O   1 
ATOM 859  C CB  . PRO A 1 117 ? 13.786  -8.977  14.274  1.00 51.24  ?  117 PRO A CB  1 
ATOM 860  C CG  . PRO A 1 117 ? 12.863  -8.523  13.210  1.00 46.84  ?  117 PRO A CG  1 
ATOM 861  C CD  . PRO A 1 117 ? 13.736  -8.263  11.994  1.00 59.91  ?  117 PRO A CD  1 
ATOM 862  N N   . SER A 1 118 ? 14.818  -12.027 14.390  1.00 62.96  ?  118 SER A N   1 
ATOM 863  C CA  . SER A 1 118 ? 14.212  -13.327 14.640  1.00 50.91  ?  118 SER A CA  1 
ATOM 864  C C   . SER A 1 118 ? 13.061  -13.102 15.614  1.00 54.41  ?  118 SER A C   1 
ATOM 865  O O   . SER A 1 118 ? 13.253  -12.491 16.670  1.00 56.31  ?  118 SER A O   1 
ATOM 866  C CB  . SER A 1 118 ? 15.239  -14.305 15.202  1.00 52.55  ?  118 SER A CB  1 
ATOM 867  O OG  . SER A 1 118 ? 16.408  -14.295 14.401  1.00 52.89  ?  118 SER A OG  1 
ATOM 868  N N   . VAL A 1 119 ? 11.859  -13.515 15.229  1.00 49.87  ?  119 VAL A N   1 
ATOM 869  C CA  . VAL A 1 119 ? 10.645  -13.204 15.978  1.00 51.80  ?  119 VAL A CA  1 
ATOM 870  C C   . VAL A 1 119 ? 10.147  -14.463 16.674  1.00 53.03  ?  119 VAL A C   1 
ATOM 871  O O   . VAL A 1 119 ? 9.872   -15.475 16.022  1.00 60.37  ?  119 VAL A O   1 
ATOM 872  C CB  . VAL A 1 119 ? 9.564   -12.609 15.064  1.00 50.77  ?  119 VAL A CB  1 
ATOM 873  C CG1 . VAL A 1 119 ? 8.279   -12.378 15.836  1.00 51.61  ?  119 VAL A CG1 1 
ATOM 874  C CG2 . VAL A 1 119 ? 10.061  -11.304 14.462  1.00 52.11  ?  119 VAL A CG2 1 
ATOM 875  N N   . PHE A 1 120 ? 10.019  -14.394 17.996  1.00 50.86  ?  120 PHE A N   1 
ATOM 876  C CA  . PHE A 1 120 ? 9.427   -15.463 18.788  1.00 54.09  ?  120 PHE A CA  1 
ATOM 877  C C   . PHE A 1 120 ? 8.185   -14.939 19.497  1.00 55.05  ?  120 PHE A C   1 
ATOM 878  O O   . PHE A 1 120 ? 8.038   -13.735 19.716  1.00 56.96  ?  120 PHE A O   1 
ATOM 879  C CB  . PHE A 1 120 ? 10.412  -16.022 19.825  1.00 52.29  ?  120 PHE A CB  1 
ATOM 880  C CG  . PHE A 1 120 ? 11.692  -16.551 19.239  1.00 52.63  ?  120 PHE A CG  1 
ATOM 881  C CD1 . PHE A 1 120 ? 11.786  -17.865 18.814  1.00 52.19  ?  120 PHE A CD1 1 
ATOM 882  C CD2 . PHE A 1 120 ? 12.813  -15.743 19.146  1.00 53.76  ?  120 PHE A CD2 1 
ATOM 883  C CE1 . PHE A 1 120 ? 12.969  -18.356 18.290  1.00 54.52  ?  120 PHE A CE1 1 
ATOM 884  C CE2 . PHE A 1 120 ? 13.998  -16.231 18.621  1.00 51.89  ?  120 PHE A CE2 1 
ATOM 885  C CZ  . PHE A 1 120 ? 14.074  -17.536 18.193  1.00 48.32  ?  120 PHE A CZ  1 
ATOM 886  N N   . ILE A 1 121 ? 7.280   -15.847 19.857  1.00 51.97  ?  121 ILE A N   1 
ATOM 887  C CA  . ILE A 1 121 ? 6.086   -15.479 20.609  1.00 51.57  ?  121 ILE A CA  1 
ATOM 888  C C   . ILE A 1 121 ? 5.876   -16.470 21.748  1.00 59.80  ?  121 ILE A C   1 
ATOM 889  O O   . ILE A 1 121 ? 5.926   -17.689 21.541  1.00 57.70  ?  121 ILE A O   1 
ATOM 890  C CB  . ILE A 1 121 ? 4.840   -15.394 19.707  1.00 55.16  ?  121 ILE A CB  1 
ATOM 891  C CG1 . ILE A 1 121 ? 3.626   -14.961 20.531  1.00 62.34  ?  121 ILE A CG1 1 
ATOM 892  C CG2 . ILE A 1 121 ? 4.584   -16.715 18.984  1.00 59.57  ?  121 ILE A CG2 1 
ATOM 893  C CD1 . ILE A 1 121 ? 2.460   -14.479 19.694  1.00 66.21  ?  121 ILE A CD1 1 
ATOM 894  N N   . PHE A 1 122 ? 5.644   -15.943 22.951  1.00 62.53  ?  122 PHE A N   1 
ATOM 895  C CA  . PHE A 1 122 ? 5.432   -16.729 24.157  1.00 60.03  ?  122 PHE A CA  1 
ATOM 896  C C   . PHE A 1 122 ? 4.030   -16.454 24.672  1.00 63.80  ?  122 PHE A C   1 
ATOM 897  O O   . PHE A 1 122 ? 3.708   -15.292 24.992  1.00 63.20  ?  122 PHE A O   1 
ATOM 898  C CB  . PHE A 1 122 ? 6.449   -16.388 25.248  1.00 60.84  ?  122 PHE A CB  1 
ATOM 899  C CG  . PHE A 1 122 ? 7.873   -16.597 24.850  1.00 56.40  ?  122 PHE A CG  1 
ATOM 900  C CD1 . PHE A 1 122 ? 8.514   -17.790 25.138  1.00 53.99  ?  122 PHE A CD1 1 
ATOM 901  C CD2 . PHE A 1 122 ? 8.580   -15.590 24.213  1.00 47.05  ?  122 PHE A CD2 1 
ATOM 902  C CE1 . PHE A 1 122 ? 9.828   -17.980 24.781  1.00 54.21  ?  122 PHE A CE1 1 
ATOM 903  C CE2 . PHE A 1 122 ? 9.895   -15.772 23.854  1.00 46.52  ?  122 PHE A CE2 1 
ATOM 904  C CZ  . PHE A 1 122 ? 10.522  -16.969 24.135  1.00 50.38  ?  122 PHE A CZ  1 
ATOM 905  N N   . PRO A 1 123 ? 3.174   -17.466 24.755  1.00 71.71  ?  123 PRO A N   1 
ATOM 906  C CA  . PRO A 1 123 ? 1.874   -17.299 25.404  1.00 69.58  ?  123 PRO A CA  1 
ATOM 907  C C   . PRO A 1 123 ? 2.050   -17.104 26.898  1.00 67.21  ?  123 PRO A C   1 
ATOM 908  O O   . PRO A 1 123 ? 3.125   -17.392 27.446  1.00 68.21  ?  123 PRO A O   1 
ATOM 909  C CB  . PRO A 1 123 ? 1.155   -18.627 25.104  1.00 68.54  ?  123 PRO A CB  1 
ATOM 910  C CG  . PRO A 1 123 ? 1.921   -19.251 23.981  1.00 65.55  ?  123 PRO A CG  1 
ATOM 911  C CD  . PRO A 1 123 ? 3.335   -18.808 24.173  1.00 67.46  ?  123 PRO A CD  1 
ATOM 912  N N   . PRO A 1 124 ? 1.028   -16.609 27.590  1.00 71.01  ?  124 PRO A N   1 
ATOM 913  C CA  . PRO A 1 124 ? 1.102   -16.544 29.054  1.00 74.93  ?  124 PRO A CA  1 
ATOM 914  C C   . PRO A 1 124 ? 1.046   -17.941 29.653  1.00 68.20  ?  124 PRO A C   1 
ATOM 915  O O   . PRO A 1 124 ? 0.349   -18.823 29.147  1.00 72.21  ?  124 PRO A O   1 
ATOM 916  C CB  . PRO A 1 124 ? -0.129  -15.715 29.435  1.00 77.54  ?  124 PRO A CB  1 
ATOM 917  C CG  . PRO A 1 124 ? -1.080  -15.918 28.292  1.00 70.72  ?  124 PRO A CG  1 
ATOM 918  C CD  . PRO A 1 124 ? -0.223  -16.029 27.070  1.00 68.57  ?  124 PRO A CD  1 
ATOM 919  N N   . SER A 1 125 ? 1.797   -18.141 30.735  1.00 74.07  ?  125 SER A N   1 
ATOM 920  C CA  . SER A 1 125 ? 1.829   -19.437 31.399  1.00 80.63  ?  125 SER A CA  1 
ATOM 921  C C   . SER A 1 125 ? 0.565   -19.658 32.228  1.00 79.88  ?  125 SER A C   1 
ATOM 922  O O   . SER A 1 125 ? -0.164  -18.721 32.561  1.00 82.68  ?  125 SER A O   1 
ATOM 923  C CB  . SER A 1 125 ? 3.068   -19.555 32.289  1.00 76.21  ?  125 SER A CB  1 
ATOM 924  O OG  . SER A 1 125 ? 3.118   -18.502 33.233  1.00 73.94  ?  125 SER A OG  1 
ATOM 925  N N   . ASP A 1 126 ? 0.315   -20.926 32.570  1.00 82.81  ?  126 ASP A N   1 
ATOM 926  C CA  . ASP A 1 126 ? -0.819  -21.241 33.434  1.00 87.77  ?  126 ASP A CA  1 
ATOM 927  C C   . ASP A 1 126 ? -0.624  -20.678 34.836  1.00 89.30  ?  126 ASP A C   1 
ATOM 928  O O   . ASP A 1 126 ? -1.595  -20.258 35.484  1.00 90.27  ?  126 ASP A O   1 
ATOM 929  C CB  . ASP A 1 126 ? -1.021  -22.755 33.504  1.00 90.60  ?  126 ASP A CB  1 
ATOM 930  C CG  . ASP A 1 126 ? -1.030  -23.406 32.138  1.00 94.72  ?  126 ASP A CG  1 
ATOM 931  O OD1 . ASP A 1 126 ? 0.067   -23.611 31.574  1.00 96.93  ?  126 ASP A OD1 1 
ATOM 932  O OD2 . ASP A 1 126 ? -2.130  -23.700 31.623  1.00 96.28  ?  126 ASP A OD2 1 
ATOM 933  N N   . GLU A 1 127 ? 0.623   -20.664 35.311  1.00 84.47  ?  127 GLU A N   1 
ATOM 934  C CA  . GLU A 1 127 ? 0.934   -20.074 36.605  1.00 82.70  ?  127 GLU A CA  1 
ATOM 935  C C   . GLU A 1 127 ? 0.505   -18.611 36.661  1.00 83.08  ?  127 GLU A C   1 
ATOM 936  O O   . GLU A 1 127 ? 0.072   -18.124 37.711  1.00 85.47  ?  127 GLU A O   1 
ATOM 937  C CB  . GLU A 1 127 ? 2.430   -20.226 36.881  1.00 82.76  ?  127 GLU A CB  1 
ATOM 938  C CG  . GLU A 1 127 ? 2.896   -19.740 38.237  1.00 84.64  ?  127 GLU A CG  1 
ATOM 939  C CD  . GLU A 1 127 ? 4.368   -20.040 38.470  1.00 87.09  ?  127 GLU A CD  1 
ATOM 940  O OE1 . GLU A 1 127 ? 4.933   -20.848 37.693  1.00 74.32  ?  127 GLU A OE1 1 
ATOM 941  O OE2 . GLU A 1 127 ? 4.958   -19.456 39.409  1.00 79.88  ?  127 GLU A OE2 1 
ATOM 942  N N   . GLN A 1 128 ? 0.621   -17.890 35.540  1.00 81.54  ?  128 GLN A N   1 
ATOM 943  C CA  . GLN A 1 128 ? 0.153   -16.507 35.501  1.00 81.28  ?  128 GLN A CA  1 
ATOM 944  C C   . GLN A 1 128 ? -1.357  -16.414 35.295  1.00 82.63  ?  128 GLN A C   1 
ATOM 945  O O   . GLN A 1 128 ? -1.988  -15.471 35.787  1.00 85.91  ?  128 GLN A O   1 
ATOM 946  C CB  . GLN A 1 128 ? 0.877   -15.724 34.402  1.00 72.61  ?  128 GLN A CB  1 
ATOM 947  C CG  . GLN A 1 128 ? 0.581   -14.227 34.448  1.00 74.66  ?  128 GLN A CG  1 
ATOM 948  C CD  . GLN A 1 128 ? 0.964   -13.495 33.178  1.00 74.67  ?  128 GLN A CD  1 
ATOM 949  O OE1 . GLN A 1 128 ? 1.491   -14.089 32.235  1.00 77.06  ?  128 GLN A OE1 1 
ATOM 950  N NE2 . GLN A 1 128 ? 0.697   -12.193 33.145  1.00 64.72  ?  128 GLN A NE2 1 
ATOM 951  N N   . LEU A 1 129 ? -1.949  -17.363 34.566  1.00 86.40  ?  129 LEU A N   1 
ATOM 952  C CA  . LEU A 1 129 ? -3.397  -17.354 34.372  1.00 89.18  ?  129 LEU A CA  1 
ATOM 953  C C   . LEU A 1 129 ? -4.148  -17.606 35.672  1.00 88.21  ?  129 LEU A C   1 
ATOM 954  O O   . LEU A 1 129 ? -5.286  -17.146 35.827  1.00 88.20  ?  129 LEU A O   1 
ATOM 955  C CB  . LEU A 1 129 ? -3.793  -18.393 33.320  1.00 85.39  ?  129 LEU A CB  1 
ATOM 956  C CG  . LEU A 1 129 ? -3.493  -18.030 31.866  1.00 76.26  ?  129 LEU A CG  1 
ATOM 957  C CD1 . LEU A 1 129 ? -3.774  -19.206 30.948  1.00 80.95  ?  129 LEU A CD1 1 
ATOM 958  C CD2 . LEU A 1 129 ? -4.324  -16.830 31.455  1.00 72.20  ?  129 LEU A CD2 1 
ATOM 959  N N   . LYS A 1 130 ? -3.530  -18.319 36.619  1.00 86.74  ?  130 LYS A N   1 
ATOM 960  C CA  . LYS A 1 130 ? -4.181  -18.564 37.903  1.00 91.24  ?  130 LYS A CA  1 
ATOM 961  C C   . LYS A 1 130 ? -4.500  -17.275 38.653  1.00 89.17  ?  130 LYS A C   1 
ATOM 962  O O   . LYS A 1 130 ? -5.323  -17.297 39.575  1.00 96.65  ?  130 LYS A O   1 
ATOM 963  C CB  . LYS A 1 130 ? -3.315  -19.482 38.774  1.00 92.61  ?  130 LYS A CB  1 
ATOM 964  C CG  . LYS A 1 130 ? -3.351  -20.949 38.355  1.00 91.46  ?  130 LYS A CG  1 
ATOM 965  C CD  . LYS A 1 130 ? -2.548  -21.836 39.298  1.00 84.75  ?  130 LYS A CD  1 
ATOM 966  C CE  . LYS A 1 130 ? -2.676  -23.300 38.896  1.00 89.87  ?  130 LYS A CE  1 
ATOM 967  N NZ  . LYS A 1 130 ? -2.198  -23.541 37.501  1.00 85.51  ?  130 LYS A NZ  1 
ATOM 968  N N   . SER A 1 131 ? -3.878  -16.158 38.282  1.00 83.31  ?  131 SER A N   1 
ATOM 969  C CA  . SER A 1 131 ? -4.054  -14.892 38.979  1.00 82.01  ?  131 SER A CA  1 
ATOM 970  C C   . SER A 1 131 ? -4.950  -13.917 38.219  1.00 88.24  ?  131 SER A C   1 
ATOM 971  O O   . SER A 1 131 ? -5.053  -12.750 38.613  1.00 83.12  ?  131 SER A O   1 
ATOM 972  C CB  . SER A 1 131 ? -2.691  -14.251 39.245  1.00 84.96  ?  131 SER A CB  1 
ATOM 973  O OG  . SER A 1 131 ? -2.016  -13.964 38.030  1.00 83.58  ?  131 SER A OG  1 
ATOM 974  N N   . GLY A 1 132 ? -5.595  -14.363 37.143  1.00 86.80  ?  132 GLY A N   1 
ATOM 975  C CA  . GLY A 1 132 ? -6.531  -13.519 36.429  1.00 81.71  ?  132 GLY A CA  1 
ATOM 976  C C   . GLY A 1 132 ? -5.911  -12.472 35.534  1.00 85.89  ?  132 GLY A C   1 
ATOM 977  O O   . GLY A 1 132 ? -6.554  -11.457 35.246  1.00 83.86  ?  132 GLY A O   1 
ATOM 978  N N   . THR A 1 133 ? -4.678  -12.681 35.082  1.00 85.11  ?  133 THR A N   1 
ATOM 979  C CA  . THR A 1 133 ? -4.040  -11.765 34.149  1.00 81.60  ?  133 THR A CA  1 
ATOM 980  C C   . THR A 1 133 ? -3.139  -12.578 33.232  1.00 81.63  ?  133 THR A C   1 
ATOM 981  O O   . THR A 1 133 ? -2.489  -13.530 33.675  1.00 83.69  ?  133 THR A O   1 
ATOM 982  C CB  . THR A 1 133 ? -3.245  -10.674 34.881  1.00 78.72  ?  133 THR A CB  1 
ATOM 983  O OG1 . THR A 1 133 ? -4.125  -9.951  35.750  1.00 84.70  ?  133 THR A OG1 1 
ATOM 984  C CG2 . THR A 1 133 ? -2.615  -9.697  33.899  1.00 70.76  ?  133 THR A CG2 1 
ATOM 985  N N   . ALA A 1 134 ? -3.113  -12.206 31.954  1.00 77.16  ?  134 ALA A N   1 
ATOM 986  C CA  . ALA A 1 134 ? -2.348  -12.919 30.942  1.00 74.97  ?  134 ALA A CA  1 
ATOM 987  C C   . ALA A 1 134 ? -1.485  -11.925 30.183  1.00 72.68  ?  134 ALA A C   1 
ATOM 988  O O   . ALA A 1 134 ? -2.002  -10.960 29.610  1.00 71.92  ?  134 ALA A O   1 
ATOM 989  C CB  . ALA A 1 134 ? -3.273  -13.666 29.978  1.00 72.69  ?  134 ALA A CB  1 
ATOM 990  N N   . SER A 1 135 ? -0.178  -12.157 30.182  1.00 70.70  ?  135 SER A N   1 
ATOM 991  C CA  . SER A 1 135 ? 0.765   -11.362 29.411  1.00 62.21  ?  135 SER A CA  1 
ATOM 992  C C   . SER A 1 135 ? 1.371   -12.265 28.347  1.00 68.08  ?  135 SER A C   1 
ATOM 993  O O   . SER A 1 135 ? 2.023   -13.263 28.673  1.00 72.93  ?  135 SER A O   1 
ATOM 994  C CB  . SER A 1 135 ? 1.855   -10.765 30.303  1.00 66.21  ?  135 SER A CB  1 
ATOM 995  O OG  . SER A 1 135 ? 1.310   -9.862  31.255  1.00 68.64  ?  135 SER A OG  1 
ATOM 996  N N   . VAL A 1 136 ? 1.121   -11.942 27.083  1.00 61.74  ?  136 VAL A N   1 
ATOM 997  C CA  . VAL A 1 136 ? 1.738   -12.644 25.965  1.00 59.64  ?  136 VAL A CA  1 
ATOM 998  C C   . VAL A 1 136 ? 2.847   -11.760 25.423  1.00 56.34  ?  136 VAL A C   1 
ATOM 999  O O   . VAL A 1 136 ? 2.643   -10.560 25.207  1.00 62.06  ?  136 VAL A O   1 
ATOM 1000 C CB  . VAL A 1 136 ? 0.707   -12.997 24.877  1.00 59.41  ?  136 VAL A CB  1 
ATOM 1001 C CG1 . VAL A 1 136 ? -0.182  -11.813 24.571  1.00 58.99  ?  136 VAL A CG1 1 
ATOM 1002 C CG2 . VAL A 1 136 ? 1.407   -13.477 23.613  1.00 60.32  ?  136 VAL A CG2 1 
ATOM 1003 N N   . VAL A 1 137 ? 4.031   -12.330 25.230  1.00 58.97  ?  137 VAL A N   1 
ATOM 1004 C CA  . VAL A 1 137 ? 5.208   -11.527 24.917  1.00 61.66  ?  137 VAL A CA  1 
ATOM 1005 C C   . VAL A 1 137 ? 5.750   -11.923 23.546  1.00 60.82  ?  137 VAL A C   1 
ATOM 1006 O O   . VAL A 1 137 ? 5.906   -13.110 23.241  1.00 57.18  ?  137 VAL A O   1 
ATOM 1007 C CB  . VAL A 1 137 ? 6.276   -11.638 26.021  1.00 53.77  ?  137 VAL A CB  1 
ATOM 1008 C CG1 . VAL A 1 137 ? 6.453   -13.068 26.427  1.00 60.57  ?  137 VAL A CG1 1 
ATOM 1009 C CG2 . VAL A 1 137 ? 7.594   -11.013 25.577  1.00 49.08  ?  137 VAL A CG2 1 
ATOM 1010 N N   . CYS A 1 138 ? 6.040   -10.916 22.729  1.00 60.68  ?  138 CYS A N   1 
ATOM 1011 C CA  . CYS A 1 138 ? 6.596   -11.061 21.393  1.00 56.56  ?  138 CYS A CA  1 
ATOM 1012 C C   . CYS A 1 138 ? 8.024   -10.535 21.433  1.00 55.60  ?  138 CYS A C   1 
ATOM 1013 O O   . CYS A 1 138 ? 8.253   -9.378  21.805  1.00 57.66  ?  138 CYS A O   1 
ATOM 1014 C CB  . CYS A 1 138 ? 5.746   -10.285 20.381  1.00 58.66  ?  138 CYS A CB  1 
ATOM 1015 S SG  . CYS A 1 138 ? 6.145   -10.427 18.613  1.00 63.65  ?  138 CYS A SG  1 
ATOM 1016 N N   . LEU A 1 139 ? 8.978   -11.390 21.087  1.00 54.10  ?  139 LEU A N   1 
ATOM 1017 C CA  . LEU A 1 139 ? 10.396  -11.066 21.141  1.00 52.40  ?  139 LEU A CA  1 
ATOM 1018 C C   . LEU A 1 139 ? 10.938  -10.868 19.729  1.00 51.18  ?  139 LEU A C   1 
ATOM 1019 O O   . LEU A 1 139 ? 10.622  -11.646 18.822  1.00 54.73  ?  139 LEU A O   1 
ATOM 1020 C CB  . LEU A 1 139 ? 11.165  -12.174 21.862  1.00 48.53  ?  139 LEU A CB  1 
ATOM 1021 C CG  . LEU A 1 139 ? 12.684  -12.191 21.708  1.00 51.62  ?  139 LEU A CG  1 
ATOM 1022 C CD1 . LEU A 1 139 ? 13.304  -10.950 22.318  1.00 50.66  ?  139 LEU A CD1 1 
ATOM 1023 C CD2 . LEU A 1 139 ? 13.244  -13.450 22.342  1.00 51.12  ?  139 LEU A CD2 1 
ATOM 1024 N N   . LEU A 1 140 ? 11.727  -9.812  19.547  1.00 42.76  ?  140 LEU A N   1 
ATOM 1025 C CA  . LEU A 1 140 ? 12.413  -9.493  18.301  1.00 44.90  ?  140 LEU A CA  1 
ATOM 1026 C C   . LEU A 1 140 ? 13.900  -9.438  18.612  1.00 51.19  ?  140 LEU A C   1 
ATOM 1027 O O   . LEU A 1 140 ? 14.366  -8.490  19.251  1.00 54.04  ?  140 LEU A O   1 
ATOM 1028 C CB  . LEU A 1 140 ? 11.939  -8.157  17.727  1.00 43.49  ?  140 LEU A CB  1 
ATOM 1029 C CG  . LEU A 1 140 ? 10.575  -7.999  17.057  1.00 45.39  ?  140 LEU A CG  1 
ATOM 1030 C CD1 . LEU A 1 140 ? 9.418   -8.314  17.982  1.00 50.78  ?  140 LEU A CD1 1 
ATOM 1031 C CD2 . LEU A 1 140 ? 10.468  -6.575  16.561  1.00 49.32  ?  140 LEU A CD2 1 
ATOM 1032 N N   . ASN A 1 141 ? 14.646  -10.432 18.152  1.00 54.32  ?  141 ASN A N   1 
ATOM 1033 C CA  . ASN A 1 141 ? 16.048  -10.574 18.512  1.00 59.17  ?  141 ASN A CA  1 
ATOM 1034 C C   . ASN A 1 141 ? 16.915  -10.140 17.337  1.00 56.39  ?  141 ASN A C   1 
ATOM 1035 O O   . ASN A 1 141 ? 16.658  -10.549 16.197  1.00 60.84  ?  141 ASN A O   1 
ATOM 1036 C CB  . ASN A 1 141 ? 16.342  -12.026 18.911  1.00 59.49  ?  141 ASN A CB  1 
ATOM 1037 C CG  . ASN A 1 141 ? 17.416  -12.141 19.979  1.00 58.97  ?  141 ASN A CG  1 
ATOM 1038 O OD1 . ASN A 1 141 ? 17.742  -11.165 20.661  1.00 62.74  ?  141 ASN A OD1 1 
ATOM 1039 N ND2 . ASN A 1 141 ? 17.946  -13.348 20.155  1.00 51.36  ?  141 ASN A ND2 1 
ATOM 1040 N N   . ASN A 1 142 ? 17.922  -9.298  17.620  1.00 54.28  ?  142 ASN A N   1 
ATOM 1041 C CA  . ASN A 1 142 ? 19.024  -8.985  16.705  1.00 56.84  ?  142 ASN A CA  1 
ATOM 1042 C C   . ASN A 1 142 ? 18.509  -8.398  15.384  1.00 57.33  ?  142 ASN A C   1 
ATOM 1043 O O   . ASN A 1 142 ? 18.594  -9.012  14.317  1.00 62.10  ?  142 ASN A O   1 
ATOM 1044 C CB  . ASN A 1 142 ? 19.898  -10.222 16.460  1.00 60.14  ?  142 ASN A CB  1 
ATOM 1045 C CG  . ASN A 1 142 ? 20.590  -10.712 17.718  1.00 62.43  ?  142 ASN A CG  1 
ATOM 1046 O OD1 . ASN A 1 142 ? 21.681  -10.255 18.059  1.00 67.89  ?  142 ASN A OD1 1 
ATOM 1047 N ND2 . ASN A 1 142 ? 19.966  -11.658 18.405  1.00 62.75  ?  142 ASN A ND2 1 
ATOM 1048 N N   . PHE A 1 143 ? 17.985  -7.177  15.475  1.00 55.77  ?  143 PHE A N   1 
ATOM 1049 C CA  . PHE A 1 143 ? 17.527  -6.455  14.293  1.00 58.03  ?  143 PHE A CA  1 
ATOM 1050 C C   . PHE A 1 143 ? 18.125  -5.055  14.262  1.00 54.38  ?  143 PHE A C   1 
ATOM 1051 O O   . PHE A 1 143 ? 18.685  -4.567  15.246  1.00 55.78  ?  143 PHE A O   1 
ATOM 1052 C CB  . PHE A 1 143 ? 15.997  -6.363  14.228  1.00 55.03  ?  143 PHE A CB  1 
ATOM 1053 C CG  . PHE A 1 143 ? 15.391  -5.529  15.311  1.00 56.68  ?  143 PHE A CG  1 
ATOM 1054 C CD1 . PHE A 1 143 ? 14.963  -4.238  15.050  1.00 57.92  ?  143 PHE A CD1 1 
ATOM 1055 C CD2 . PHE A 1 143 ? 15.231  -6.039  16.587  1.00 57.77  ?  143 PHE A CD2 1 
ATOM 1056 C CE1 . PHE A 1 143 ? 14.398  -3.462  16.042  1.00 56.29  ?  143 PHE A CE1 1 
ATOM 1057 C CE2 . PHE A 1 143 ? 14.671  -5.269  17.585  1.00 57.95  ?  143 PHE A CE2 1 
ATOM 1058 C CZ  . PHE A 1 143 ? 14.253  -3.976  17.312  1.00 56.60  ?  143 PHE A CZ  1 
ATOM 1059 N N   . TYR A 1 144 ? 17.988  -4.411  13.100  1.00 56.39  ?  144 TYR A N   1 
ATOM 1060 C CA  . TYR A 1 144 ? 18.418  -3.039  12.865  1.00 56.93  ?  144 TYR A CA  1 
ATOM 1061 C C   . TYR A 1 144 ? 17.643  -2.508  11.672  1.00 64.13  ?  144 TYR A C   1 
ATOM 1062 O O   . TYR A 1 144 ? 17.426  -3.263  10.714  1.00 67.10  ?  144 TYR A O   1 
ATOM 1063 C CB  . TYR A 1 144 ? 19.926  -2.943  12.601  1.00 56.05  ?  144 TYR A CB  1 
ATOM 1064 C CG  . TYR A 1 144 ? 20.382  -1.508  12.503  1.00 60.85  ?  144 TYR A CG  1 
ATOM 1065 C CD1 . TYR A 1 144 ? 20.382  -0.843  11.282  1.00 59.01  ?  144 TYR A CD1 1 
ATOM 1066 C CD2 . TYR A 1 144 ? 20.761  -0.800  13.638  1.00 60.13  ?  144 TYR A CD2 1 
ATOM 1067 C CE1 . TYR A 1 144 ? 20.763  0.478   11.196  1.00 64.03  ?  144 TYR A CE1 1 
ATOM 1068 C CE2 . TYR A 1 144 ? 21.150  0.521   13.558  1.00 59.63  ?  144 TYR A CE2 1 
ATOM 1069 C CZ  . TYR A 1 144 ? 21.149  1.153   12.334  1.00 64.75  ?  144 TYR A CZ  1 
ATOM 1070 O OH  . TYR A 1 144 ? 21.535  2.467   12.245  1.00 67.14  ?  144 TYR A OH  1 
ATOM 1071 N N   . PRO A 1 145 ? 17.200  -1.237  11.684  1.00 64.61  ?  145 PRO A N   1 
ATOM 1072 C CA  . PRO A 1 145 ? 17.417  -0.244  12.741  1.00 64.28  ?  145 PRO A CA  1 
ATOM 1073 C C   . PRO A 1 145 ? 16.463  -0.416  13.900  1.00 61.59  ?  145 PRO A C   1 
ATOM 1074 O O   . PRO A 1 145 ? 15.637  -1.330  13.875  1.00 54.84  ?  145 PRO A O   1 
ATOM 1075 C CB  . PRO A 1 145 ? 17.156  1.083   12.026  1.00 62.00  ?  145 PRO A CB  1 
ATOM 1076 C CG  . PRO A 1 145 ? 16.116  0.733   11.014  1.00 57.67  ?  145 PRO A CG  1 
ATOM 1077 C CD  . PRO A 1 145 ? 16.429  -0.675  10.559  1.00 56.32  ?  145 PRO A CD  1 
ATOM 1078 N N   . ARG A 1 146 ? 16.573  0.476   14.891  1.00 66.20  ?  146 ARG A N   1 
ATOM 1079 C CA  . ARG A 1 146 ? 15.714  0.411   16.065  1.00 64.78  ?  146 ARG A CA  1 
ATOM 1080 C C   . ARG A 1 146 ? 14.249  0.539   15.691  1.00 67.23  ?  146 ARG A C   1 
ATOM 1081 O O   . ARG A 1 146 ? 13.379  0.069   16.432  1.00 70.65  ?  146 ARG A O   1 
ATOM 1082 C CB  . ARG A 1 146 ? 16.078  1.524   17.047  1.00 65.95  ?  146 ARG A CB  1 
ATOM 1083 C CG  . ARG A 1 146 ? 15.278  1.478   18.337  1.00 73.84  ?  146 ARG A CG  1 
ATOM 1084 C CD  . ARG A 1 146 ? 15.518  2.682   19.238  1.00 73.94  ?  146 ARG A CD  1 
ATOM 1085 N NE  . ARG A 1 146 ? 14.577  2.655   20.354  1.00 81.94  ?  146 ARG A NE  1 
ATOM 1086 C CZ  . ARG A 1 146 ? 13.336  3.134   20.289  1.00 87.17  ?  146 ARG A CZ  1 
ATOM 1087 N NH1 . ARG A 1 146 ? 12.894  3.683   19.163  1.00 84.74  ?  146 ARG A NH1 1 
ATOM 1088 N NH2 . ARG A 1 146 ? 12.535  3.060   21.346  1.00 87.82  ?  146 ARG A NH2 1 
ATOM 1089 N N   . GLU A 1 147 ? 13.961  1.153   14.553  1.00 70.97  ?  147 GLU A N   1 
ATOM 1090 C CA  . GLU A 1 147 ? 12.583  1.371   14.154  1.00 74.69  ?  147 GLU A CA  1 
ATOM 1091 C C   . GLU A 1 147 ? 11.968  0.051   13.711  1.00 76.50  ?  147 GLU A C   1 
ATOM 1092 O O   . GLU A 1 147 ? 12.579  -0.706  12.948  1.00 85.28  ?  147 GLU A O   1 
ATOM 1093 C CB  . GLU A 1 147 ? 12.537  2.403   13.031  1.00 76.74  ?  147 GLU A CB  1 
ATOM 1094 C CG  . GLU A 1 147 ? 13.470  3.588   13.300  1.00 81.77  ?  147 GLU A CG  1 
ATOM 1095 C CD  . GLU A 1 147 ? 13.136  4.361   14.569  1.00 87.42  ?  147 GLU A CD  1 
ATOM 1096 O OE1 . GLU A 1 147 ? 11.993  4.257   15.065  1.00 89.60  ?  147 GLU A OE1 1 
ATOM 1097 O OE2 . GLU A 1 147 ? 14.037  5.063   15.084  1.00 88.66  ?  147 GLU A OE2 1 
ATOM 1098 N N   . ALA A 1 148 ? 10.763  -0.229  14.199  1.00 70.35  ?  148 ALA A N   1 
ATOM 1099 C CA  . ALA A 1 148 ? 10.067  -1.458  13.842  1.00 67.98  ?  148 ALA A CA  1 
ATOM 1100 C C   . ALA A 1 148 ? 8.606   -1.347  14.237  1.00 68.09  ?  148 ALA A C   1 
ATOM 1101 O O   . ALA A 1 148 ? 8.294   -0.969  15.369  1.00 72.61  ?  148 ALA A O   1 
ATOM 1102 C CB  . ALA A 1 148 ? 10.716  -2.665  14.517  1.00 66.60  ?  148 ALA A CB  1 
ATOM 1103 N N   . LYS A 1 149 ? 7.702   -1.702  13.335  1.00 66.48  ?  149 LYS A N   1 
ATOM 1104 C CA  . LYS A 1 149 ? 6.272   -1.556  13.583  1.00 65.82  ?  149 LYS A CA  1 
ATOM 1105 C C   . LYS A 1 149 ? 5.744   -2.896  14.075  1.00 67.20  ?  149 LYS A C   1 
ATOM 1106 O O   . LYS A 1 149 ? 5.545   -3.822  13.288  1.00 77.30  ?  149 LYS A O   1 
ATOM 1107 C CB  . LYS A 1 149 ? 5.563   -1.099  12.315  1.00 70.84  ?  149 LYS A CB  1 
ATOM 1108 C CG  . LYS A 1 149 ? 4.090   -0.786  12.476  1.00 77.44  ?  149 LYS A CG  1 
ATOM 1109 C CD  . LYS A 1 149 ? 3.522   -0.261  11.163  1.00 86.33  ?  149 LYS A CD  1 
ATOM 1110 C CE  . LYS A 1 149 ? 2.011   -0.143  11.217  1.00 95.38  ?  149 LYS A CE  1 
ATOM 1111 N NZ  . LYS A 1 149 ? 1.430   0.037   9.860   1.00 97.69  ?  149 LYS A NZ  1 
ATOM 1112 N N   . VAL A 1 150 ? 5.508   -3.002  15.376  1.00 55.32  ?  150 VAL A N   1 
ATOM 1113 C CA  . VAL A 1 150 ? 5.051   -4.246  15.984  1.00 61.09  ?  150 VAL A CA  1 
ATOM 1114 C C   . VAL A 1 150 ? 3.583   -4.079  16.336  1.00 59.64  ?  150 VAL A C   1 
ATOM 1115 O O   . VAL A 1 150 ? 3.231   -3.240  17.175  1.00 70.40  ?  150 VAL A O   1 
ATOM 1116 C CB  . VAL A 1 150 ? 5.873   -4.621  17.226  1.00 62.12  ?  150 VAL A CB  1 
ATOM 1117 C CG1 . VAL A 1 150 ? 5.400   -5.955  17.781  1.00 53.78  ?  150 VAL A CG1 1 
ATOM 1118 C CG2 . VAL A 1 150 ? 7.354   -4.671  16.896  1.00 62.91  ?  150 VAL A CG2 1 
ATOM 1119 N N   . GLN A 1 151 ? 2.732   -4.879  15.706  1.00 58.21  ?  151 GLN A N   1 
ATOM 1120 C CA  . GLN A 1 151 ? 1.302   -4.835  15.946  1.00 63.16  ?  151 GLN A CA  1 
ATOM 1121 C C   . GLN A 1 151 ? 0.822   -6.191  16.439  1.00 59.38  ?  151 GLN A C   1 
ATOM 1122 O O   . GLN A 1 151 ? 1.451   -7.223  16.198  1.00 63.40  ?  151 GLN A O   1 
ATOM 1123 C CB  . GLN A 1 151 ? 0.542   -4.424  14.678  1.00 69.88  ?  151 GLN A CB  1 
ATOM 1124 C CG  . GLN A 1 151 ? 0.841   -2.997  14.215  1.00 75.61  ?  151 GLN A CG  1 
ATOM 1125 C CD  . GLN A 1 151 ? 0.028   -2.581  12.993  1.00 82.13  ?  151 GLN A CD  1 
ATOM 1126 O OE1 . GLN A 1 151 ? 0.397   -2.878  11.855  1.00 79.70  ?  151 GLN A OE1 1 
ATOM 1127 N NE2 . GLN A 1 151 ? -1.082  -1.887  13.226  1.00 81.42  ?  151 GLN A NE2 1 
ATOM 1128 N N   . TRP A 1 152 ? -0.301  -6.175  17.147  1.00 58.08  ?  152 TRP A N   1 
ATOM 1129 C CA  . TRP A 1 152 ? -0.892  -7.372  17.724  1.00 65.67  ?  152 TRP A CA  1 
ATOM 1130 C C   . TRP A 1 152 ? -2.238  -7.651  17.071  1.00 68.54  ?  152 TRP A C   1 
ATOM 1131 O O   . TRP A 1 152 ? -2.984  -6.723  16.743  1.00 73.72  ?  152 TRP A O   1 
ATOM 1132 C CB  . TRP A 1 152 ? -1.061  -7.234  19.242  1.00 66.76  ?  152 TRP A CB  1 
ATOM 1133 C CG  . TRP A 1 152 ? 0.223   -7.412  20.017  1.00 61.08  ?  152 TRP A CG  1 
ATOM 1134 C CD1 . TRP A 1 152 ? 1.093   -6.432  20.395  1.00 60.75  ?  152 TRP A CD1 1 
ATOM 1135 C CD2 . TRP A 1 152 ? 0.770   -8.643  20.511  1.00 59.46  ?  152 TRP A CD2 1 
ATOM 1136 N NE1 . TRP A 1 152 ? 2.151   -6.974  21.082  1.00 58.22  ?  152 TRP A NE1 1 
ATOM 1137 C CE2 . TRP A 1 152 ? 1.977   -8.329  21.169  1.00 59.68  ?  152 TRP A CE2 1 
ATOM 1138 C CE3 . TRP A 1 152 ? 0.360   -9.979  20.456  1.00 63.29  ?  152 TRP A CE3 1 
ATOM 1139 C CZ2 . TRP A 1 152 ? 2.777   -9.300  21.775  1.00 60.56  ?  152 TRP A CZ2 1 
ATOM 1140 C CZ3 . TRP A 1 152 ? 1.156   -10.946 21.060  1.00 66.49  ?  152 TRP A CZ3 1 
ATOM 1141 C CH2 . TRP A 1 152 ? 2.351   -10.599 21.710  1.00 61.17  ?  152 TRP A CH2 1 
ATOM 1142 N N   . LYS A 1 153 ? -2.528  -8.932  16.859  1.00 58.51  ?  153 LYS A N   1 
ATOM 1143 C CA  . LYS A 1 153 ? -3.807  -9.383  16.339  1.00 62.81  ?  153 LYS A CA  1 
ATOM 1144 C C   . LYS A 1 153 ? -4.329  -10.508 17.217  1.00 67.34  ?  153 LYS A C   1 
ATOM 1145 O O   . LYS A 1 153 ? -3.569  -11.385 17.637  1.00 70.94  ?  153 LYS A O   1 
ATOM 1146 C CB  . LYS A 1 153 ? -3.690  -9.863  14.885  1.00 71.82  ?  153 LYS A CB  1 
ATOM 1147 C CG  . LYS A 1 153 ? -3.283  -8.782  13.889  1.00 70.74  ?  153 LYS A CG  1 
ATOM 1148 C CD  . LYS A 1 153 ? -3.352  -9.302  12.460  1.00 77.73  ?  153 LYS A CD  1 
ATOM 1149 C CE  . LYS A 1 153 ? -2.766  -8.309  11.465  1.00 82.03  ?  153 LYS A CE  1 
ATOM 1150 N NZ  . LYS A 1 153 ? -2.599  -8.915  10.110  1.00 82.92  ?  153 LYS A NZ  1 
ATOM 1151 N N   . VAL A 1 154 ? -5.620  -10.456 17.528  1.00 72.36  ?  154 VAL A N   1 
ATOM 1152 C CA  . VAL A 1 154 ? -6.306  -11.536 18.231  1.00 75.46  ?  154 VAL A CA  1 
ATOM 1153 C C   . VAL A 1 154 ? -7.530  -11.913 17.405  1.00 76.76  ?  154 VAL A C   1 
ATOM 1154 O O   . VAL A 1 154 ? -8.396  -11.065 17.154  1.00 79.96  ?  154 VAL A O   1 
ATOM 1155 C CB  . VAL A 1 154 ? -6.690  -11.147 19.669  1.00 76.77  ?  154 VAL A CB  1 
ATOM 1156 C CG1 . VAL A 1 154 ? -7.243  -9.728  19.717  1.00 86.01  ?  154 VAL A CG1 1 
ATOM 1157 C CG2 . VAL A 1 154 ? -7.683  -12.131 20.237  1.00 71.76  ?  154 VAL A CG2 1 
ATOM 1158 N N   . ASP A 1 155 ? -7.588  -13.173 16.963  1.00 76.00  ?  155 ASP A N   1 
ATOM 1159 C CA  . ASP A 1 155 ? -8.574  -13.615 15.974  1.00 75.22  ?  155 ASP A CA  1 
ATOM 1160 C C   . ASP A 1 155 ? -8.583  -12.682 14.763  1.00 79.67  ?  155 ASP A C   1 
ATOM 1161 O O   . ASP A 1 155 ? -9.637  -12.293 14.255  1.00 75.79  ?  155 ASP A O   1 
ATOM 1162 C CB  . ASP A 1 155 ? -9.971  -13.736 16.588  1.00 74.05  ?  155 ASP A CB  1 
ATOM 1163 C CG  . ASP A 1 155 ? -10.123 -14.971 17.460  1.00 81.55  ?  155 ASP A CG  1 
ATOM 1164 O OD1 . ASP A 1 155 ? -9.373  -15.947 17.245  1.00 81.97  ?  155 ASP A OD1 1 
ATOM 1165 O OD2 . ASP A 1 155 ? -11.006 -14.978 18.344  1.00 79.40  ?  155 ASP A OD2 1 
ATOM 1166 N N   . ASN A 1 156 ? -7.381  -12.312 14.310  1.00 78.56  ?  156 ASN A N   1 
ATOM 1167 C CA  . ASN A 1 156 ? -7.172  -11.414 13.169  1.00 80.63  ?  156 ASN A CA  1 
ATOM 1168 C C   . ASN A 1 156 ? -7.815  -10.044 13.387  1.00 78.44  ?  156 ASN A C   1 
ATOM 1169 O O   . ASN A 1 156 ? -8.151  -9.344  12.428  1.00 79.68  ?  156 ASN A O   1 
ATOM 1170 C CB  . ASN A 1 156 ? -7.674  -12.037 11.859  1.00 84.36  ?  156 ASN A CB  1 
ATOM 1171 C CG  . ASN A 1 156 ? -7.002  -11.438 10.627  1.00 80.97  ?  156 ASN A CG  1 
ATOM 1172 O OD1 . ASN A 1 156 ? -5.775  -11.438 10.511  1.00 80.10  ?  156 ASN A OD1 1 
ATOM 1173 N ND2 . ASN A 1 156 ? -7.806  -10.916 9.708   1.00 82.83  ?  156 ASN A ND2 1 
ATOM 1174 N N   . ALA A 1 157 ? -7.973  -9.638  14.645  1.00 81.52  ?  157 ALA A N   1 
ATOM 1175 C CA  . ALA A 1 157 ? -8.466  -8.308  14.992  1.00 79.57  ?  157 ALA A CA  1 
ATOM 1176 C C   . ALA A 1 157 ? -7.315  -7.498  15.580  1.00 79.59  ?  157 ALA A C   1 
ATOM 1177 O O   . ALA A 1 157 ? -6.688  -7.926  16.557  1.00 83.77  ?  157 ALA A O   1 
ATOM 1178 C CB  . ALA A 1 157 ? -9.631  -8.399  15.977  1.00 77.86  ?  157 ALA A CB  1 
ATOM 1179 N N   . LEU A 1 158 ? -7.036  -6.343  14.979  1.00 68.66  ?  158 LEU A N   1 
ATOM 1180 C CA  . LEU A 1 158 ? -5.881  -5.545  15.373  1.00 76.16  ?  158 LEU A CA  1 
ATOM 1181 C C   . LEU A 1 158 ? -6.098  -4.891  16.732  1.00 78.83  ?  158 LEU A C   1 
ATOM 1182 O O   . LEU A 1 158 ? -7.202  -4.447  17.057  1.00 83.21  ?  158 LEU A O   1 
ATOM 1183 C CB  . LEU A 1 158 ? -5.604  -4.468  14.320  1.00 77.38  ?  158 LEU A CB  1 
ATOM 1184 C CG  . LEU A 1 158 ? -4.334  -3.622  14.459  1.00 73.82  ?  158 LEU A CG  1 
ATOM 1185 C CD1 . LEU A 1 158 ? -3.079  -4.475  14.366  1.00 74.21  ?  158 LEU A CD1 1 
ATOM 1186 C CD2 . LEU A 1 158 ? -4.317  -2.512  13.418  1.00 61.98  ?  158 LEU A CD2 1 
ATOM 1187 N N   . GLN A 1 159 ? -5.029  -4.823  17.524  1.00 82.82  ?  159 GLN A N   1 
ATOM 1188 C CA  . GLN A 1 159 ? -5.072  -4.271  18.871  1.00 78.76  ?  159 GLN A CA  1 
ATOM 1189 C C   . GLN A 1 159 ? -4.304  -2.954  18.947  1.00 86.81  ?  159 GLN A C   1 
ATOM 1190 O O   . GLN A 1 159 ? -3.310  -2.751  18.243  1.00 87.01  ?  159 GLN A O   1 
ATOM 1191 C CB  . GLN A 1 159 ? -4.501  -5.260  19.888  1.00 65.78  ?  159 GLN A CB  1 
ATOM 1192 C CG  . GLN A 1 159 ? -5.309  -6.536  20.025  1.00 73.54  ?  159 GLN A CG  1 
ATOM 1193 C CD  . GLN A 1 159 ? -6.724  -6.282  20.506  1.00 79.33  ?  159 GLN A CD  1 
ATOM 1194 O OE1 . GLN A 1 159 ? -7.692  -6.619  19.825  1.00 85.19  ?  159 GLN A OE1 1 
ATOM 1195 N NE2 . GLN A 1 159 ? -6.852  -5.669  21.676  1.00 82.81  ?  159 GLN A NE2 1 
ATOM 1196 N N   . SER A 1 160 ? -4.776  -2.058  19.814  1.00 85.45  ?  160 SER A N   1 
ATOM 1197 C CA  . SER A 1 160 ? -4.117  -0.778  20.033  1.00 83.72  ?  160 SER A CA  1 
ATOM 1198 C C   . SER A 1 160 ? -4.384  -0.318  21.457  1.00 81.24  ?  160 SER A C   1 
ATOM 1199 O O   . SER A 1 160 ? -5.437  -0.611  22.031  1.00 82.10  ?  160 SER A O   1 
ATOM 1200 C CB  . SER A 1 160 ? -4.590  0.279   19.030  1.00 87.46  ?  160 SER A CB  1 
ATOM 1201 O OG  . SER A 1 160 ? -5.973  0.542   19.188  1.00 87.33  ?  160 SER A OG  1 
ATOM 1202 N N   . GLY A 1 161 ? -3.416  0.402   22.025  1.00 79.05  ?  161 GLY A N   1 
ATOM 1203 C CA  . GLY A 1 161 ? -3.547  0.843   23.402  1.00 74.57  ?  161 GLY A CA  1 
ATOM 1204 C C   . GLY A 1 161 ? -3.616  -0.298  24.388  1.00 78.77  ?  161 GLY A C   1 
ATOM 1205 O O   . GLY A 1 161 ? -4.346  -0.215  25.379  1.00 88.89  ?  161 GLY A O   1 
ATOM 1206 N N   . ASN A 1 162 ? -2.886  -1.377  24.129  1.00 73.81  ?  162 ASN A N   1 
ATOM 1207 C CA  . ASN A 1 162 ? -3.066  -2.614  24.872  1.00 71.42  ?  162 ASN A CA  1 
ATOM 1208 C C   . ASN A 1 162 ? -1.753  -3.324  25.164  1.00 66.99  ?  162 ASN A C   1 
ATOM 1209 O O   . ASN A 1 162 ? -1.752  -4.291  25.932  1.00 62.71  ?  162 ASN A O   1 
ATOM 1210 C CB  . ASN A 1 162 ? -4.007  -3.550  24.095  1.00 76.33  ?  162 ASN A CB  1 
ATOM 1211 C CG  . ASN A 1 162 ? -4.489  -4.709  24.925  1.00 79.50  ?  162 ASN A CG  1 
ATOM 1212 O OD1 . ASN A 1 162 ? -4.861  -5.751  24.393  1.00 80.77  ?  162 ASN A OD1 1 
ATOM 1213 N ND2 . ASN A 1 162 ? -4.476  -4.541  26.243  1.00 82.27  ?  162 ASN A ND2 1 
ATOM 1214 N N   . SER A 1 163 ? -0.645  -2.891  24.572  1.00 65.80  ?  163 SER A N   1 
ATOM 1215 C CA  . SER A 1 163 ? 0.654   -3.519  24.738  1.00 64.19  ?  163 SER A CA  1 
ATOM 1216 C C   . SER A 1 163 ? 1.669   -2.459  25.137  1.00 58.45  ?  163 SER A C   1 
ATOM 1217 O O   . SER A 1 163 ? 1.425   -1.257  25.021  1.00 56.68  ?  163 SER A O   1 
ATOM 1218 C CB  . SER A 1 163 ? 1.096   -4.234  23.448  1.00 67.23  ?  163 SER A CB  1 
ATOM 1219 O OG  . SER A 1 163 ? 1.087   -3.344  22.341  1.00 48.65  ?  163 SER A OG  1 
ATOM 1220 N N   . GLN A 1 164 ? 2.829   -2.929  25.588  1.00 61.89  ?  164 GLN A N   1 
ATOM 1221 C CA  . GLN A 1 164 ? 3.940   -2.064  25.963  1.00 67.12  ?  164 GLN A CA  1 
ATOM 1222 C C   . GLN A 1 164 ? 5.229   -2.628  25.388  1.00 64.29  ?  164 GLN A C   1 
ATOM 1223 O O   . GLN A 1 164 ? 5.428   -3.845  25.366  1.00 63.38  ?  164 GLN A O   1 
ATOM 1224 C CB  . GLN A 1 164 ? 4.065   -1.932  27.489  1.00 65.63  ?  164 GLN A CB  1 
ATOM 1225 C CG  . GLN A 1 164 ? 3.021   -1.030  28.130  1.00 66.99  ?  164 GLN A CG  1 
ATOM 1226 C CD  . GLN A 1 164 ? 3.172   -0.939  29.637  1.00 78.22  ?  164 GLN A CD  1 
ATOM 1227 O OE1 . GLN A 1 164 ? 3.350   -1.953  30.318  1.00 79.19  ?  164 GLN A OE1 1 
ATOM 1228 N NE2 . GLN A 1 164 ? 3.118   0.281   30.165  1.00 73.27  ?  164 GLN A NE2 1 
ATOM 1229 N N   . GLU A 1 165 ? 6.106   -1.742  24.927  1.00 60.36  ?  165 GLU A N   1 
ATOM 1230 C CA  . GLU A 1 165 ? 7.322   -2.150  24.245  1.00 57.78  ?  165 GLU A CA  1 
ATOM 1231 C C   . GLU A 1 165 ? 8.551   -1.719  25.029  1.00 58.40  ?  165 GLU A C   1 
ATOM 1232 O O   . GLU A 1 165 ? 8.547   -0.694  25.716  1.00 63.84  ?  165 GLU A O   1 
ATOM 1233 C CB  . GLU A 1 165 ? 7.375   -1.572  22.834  1.00 64.27  ?  165 GLU A CB  1 
ATOM 1234 C CG  . GLU A 1 165 ? 6.307   -2.142  21.926  1.00 63.94  ?  165 GLU A CG  1 
ATOM 1235 C CD  . GLU A 1 165 ? 6.444   -1.668  20.505  1.00 62.82  ?  165 GLU A CD  1 
ATOM 1236 O OE1 . GLU A 1 165 ? 5.671   -2.151  19.650  1.00 67.06  ?  165 GLU A OE1 1 
ATOM 1237 O OE2 . GLU A 1 165 ? 7.314   -0.804  20.251  1.00 65.04  ?  165 GLU A OE2 1 
ATOM 1238 N N   . SER A 1 166 ? 9.616   -2.504  24.891  1.00 61.68  ?  166 SER A N   1 
ATOM 1239 C CA  . SER A 1 166 ? 10.883  -2.218  25.549  1.00 63.72  ?  166 SER A CA  1 
ATOM 1240 C C   . SER A 1 166 ? 12.030  -2.595  24.627  1.00 60.68  ?  166 SER A C   1 
ATOM 1241 O O   . SER A 1 166 ? 12.041  -3.689  24.055  1.00 55.06  ?  166 SER A O   1 
ATOM 1242 C CB  . SER A 1 166 ? 11.007  -2.976  26.874  1.00 56.29  ?  166 SER A CB  1 
ATOM 1243 O OG  . SER A 1 166 ? 12.241  -2.676  27.503  1.00 58.50  ?  166 SER A OG  1 
ATOM 1244 N N   . VAL A 1 167 ? 13.009  -1.701  24.520  1.00 61.74  ?  167 VAL A N   1 
ATOM 1245 C CA  . VAL A 1 167 ? 14.136  -1.851  23.610  1.00 59.20  ?  167 VAL A CA  1 
ATOM 1246 C C   . VAL A 1 167 ? 15.411  -1.994  24.423  1.00 58.23  ?  167 VAL A C   1 
ATOM 1247 O O   . VAL A 1 167 ? 15.607  -1.284  25.417  1.00 63.83  ?  167 VAL A O   1 
ATOM 1248 C CB  . VAL A 1 167 ? 14.261  -0.644  22.657  1.00 62.45  ?  167 VAL A CB  1 
ATOM 1249 C CG1 . VAL A 1 167 ? 15.267  -0.942  21.545  1.00 70.34  ?  167 VAL A CG1 1 
ATOM 1250 C CG2 . VAL A 1 167 ? 12.898  -0.225  22.115  1.00 72.59  ?  167 VAL A CG2 1 
ATOM 1251 N N   . THR A 1 168 ? 16.285  -2.895  23.990  1.00 51.15  ?  168 THR A N   1 
ATOM 1252 C CA  . THR A 1 168 ? 17.603  -2.965  24.590  1.00 55.29  ?  168 THR A CA  1 
ATOM 1253 C C   . THR A 1 168 ? 18.472  -1.837  24.048  1.00 62.96  ?  168 THR A C   1 
ATOM 1254 O O   . THR A 1 168 ? 18.135  -1.167  23.068  1.00 71.71  ?  168 THR A O   1 
ATOM 1255 C CB  . THR A 1 168 ? 18.273  -4.303  24.298  1.00 57.79  ?  168 THR A CB  1 
ATOM 1256 O OG1 . THR A 1 168 ? 18.404  -4.457  22.880  1.00 57.56  ?  168 THR A OG1 1 
ATOM 1257 C CG2 . THR A 1 168 ? 17.448  -5.451  24.858  1.00 59.45  ?  168 THR A CG2 1 
ATOM 1258 N N   . GLU A 1 169 ? 19.594  -1.604  24.712  1.00 66.93  ?  169 GLU A N   1 
ATOM 1259 C CA  . GLU A 1 169 ? 20.569  -0.695  24.143  1.00 63.05  ?  169 GLU A CA  1 
ATOM 1260 C C   . GLU A 1 169 ? 21.244  -1.360  22.944  1.00 65.69  ?  169 GLU A C   1 
ATOM 1261 O O   . GLU A 1 169 ? 21.168  -2.578  22.754  1.00 59.64  ?  169 GLU A O   1 
ATOM 1262 C CB  . GLU A 1 169 ? 21.595  -0.287  25.201  1.00 67.27  ?  169 GLU A CB  1 
ATOM 1263 C CG  . GLU A 1 169 ? 21.000  0.443   26.425  1.00 75.49  ?  169 GLU A CG  1 
ATOM 1264 C CD  . GLU A 1 169 ? 20.266  1.744   26.081  1.00 80.44  ?  169 GLU A CD  1 
ATOM 1265 O OE1 . GLU A 1 169 ? 20.771  2.523   25.236  1.00 74.43  ?  169 GLU A OE1 1 
ATOM 1266 O OE2 . GLU A 1 169 ? 19.188  1.991   26.673  1.00 72.52  ?  169 GLU A OE2 1 
ATOM 1267 N N   . GLN A 1 170 ? 21.884  -0.538  22.112  1.00 70.17  ?  170 GLN A N   1 
ATOM 1268 C CA  . GLN A 1 170 ? 22.525  -1.041  20.901  1.00 63.36  ?  170 GLN A CA  1 
ATOM 1269 C C   . GLN A 1 170 ? 23.645  -2.011  21.254  1.00 62.19  ?  170 GLN A C   1 
ATOM 1270 O O   . GLN A 1 170 ? 24.504  -1.712  22.088  1.00 66.12  ?  170 GLN A O   1 
ATOM 1271 C CB  . GLN A 1 170 ? 23.070  0.118   20.058  1.00 63.71  ?  170 GLN A CB  1 
ATOM 1272 C CG  . GLN A 1 170 ? 23.473  -0.281  18.635  1.00 61.67  ?  170 GLN A CG  1 
ATOM 1273 C CD  . GLN A 1 170 ? 23.693  0.910   17.711  1.00 63.18  ?  170 GLN A CD  1 
ATOM 1274 O OE1 . GLN A 1 170 ? 24.044  2.004   18.154  1.00 67.99  ?  170 GLN A OE1 1 
ATOM 1275 N NE2 . GLN A 1 170 ? 23.484  0.698   16.418  1.00 60.44  ?  170 GLN A NE2 1 
ATOM 1276 N N   . ASP A 1 171 ? 23.620  -3.185  20.627  1.00 62.01  ?  171 ASP A N   1 
ATOM 1277 C CA  . ASP A 1 171 ? 24.605  -4.215  20.921  1.00 60.84  ?  171 ASP A CA  1 
ATOM 1278 C C   . ASP A 1 171 ? 26.012  -3.674  20.683  1.00 62.48  ?  171 ASP A C   1 
ATOM 1279 O O   . ASP A 1 171 ? 26.261  -2.935  19.727  1.00 64.32  ?  171 ASP A O   1 
ATOM 1280 C CB  . ASP A 1 171 ? 24.344  -5.442  20.041  1.00 60.92  ?  171 ASP A CB  1 
ATOM 1281 C CG  . ASP A 1 171 ? 25.136  -6.664  20.475  1.00 66.79  ?  171 ASP A CG  1 
ATOM 1282 O OD1 . ASP A 1 171 ? 24.530  -7.594  21.051  1.00 72.45  ?  171 ASP A OD1 1 
ATOM 1283 O OD2 . ASP A 1 171 ? 26.363  -6.695  20.242  1.00 61.29  ?  171 ASP A OD2 1 
ATOM 1284 N N   . SER A 1 172 ? 26.933  -4.029  21.575  1.00 63.57  ?  172 SER A N   1 
ATOM 1285 C CA  . SER A 1 172 ? 28.303  -3.539  21.491  1.00 59.75  ?  172 SER A CA  1 
ATOM 1286 C C   . SER A 1 172 ? 29.141  -4.264  20.443  1.00 61.78  ?  172 SER A C   1 
ATOM 1287 O O   . SER A 1 172 ? 30.275  -3.842  20.187  1.00 60.83  ?  172 SER A O   1 
ATOM 1288 C CB  . SER A 1 172 ? 28.984  -3.663  22.856  1.00 66.05  ?  172 SER A CB  1 
ATOM 1289 O OG  . SER A 1 172 ? 28.989  -5.014  23.302  1.00 69.33  ?  172 SER A OG  1 
ATOM 1290 N N   . LYS A 1 173 ? 28.620  -5.330  19.834  1.00 61.81  ?  173 LYS A N   1 
ATOM 1291 C CA  . LYS A 1 173 ? 29.359  -6.117  18.852  1.00 65.50  ?  173 LYS A CA  1 
ATOM 1292 C C   . LYS A 1 173 ? 28.858  -5.882  17.433  1.00 56.56  ?  173 LYS A C   1 
ATOM 1293 O O   . LYS A 1 173 ? 29.626  -5.434  16.577  1.00 53.53  ?  173 LYS A O   1 
ATOM 1294 C CB  . LYS A 1 173 ? 29.286  -7.615  19.196  1.00 71.18  ?  173 LYS A CB  1 
ATOM 1295 C CG  . LYS A 1 173 ? 29.898  -7.990  20.545  1.00 84.48  ?  173 LYS A CG  1 
ATOM 1296 C CD  . LYS A 1 173 ? 31.416  -7.831  20.545  1.00 87.69  ?  173 LYS A CD  1 
ATOM 1297 C CE  . LYS A 1 173 ? 32.027  -8.288  21.864  1.00 80.01  ?  173 LYS A CE  1 
ATOM 1298 N NZ  . LYS A 1 173 ? 33.510  -8.160  21.849  1.00 80.63  ?  173 LYS A NZ  1 
ATOM 1299 N N   . ASP A 1 174 ? 27.595  -6.205  17.151  1.00 52.82  ?  174 ASP A N   1 
ATOM 1300 C CA  . ASP A 1 174 ? 27.029  -6.082  15.813  1.00 57.88  ?  174 ASP A CA  1 
ATOM 1301 C C   . ASP A 1 174 ? 26.053  -4.915  15.681  1.00 64.68  ?  174 ASP A C   1 
ATOM 1302 O O   . ASP A 1 174 ? 25.305  -4.856  14.695  1.00 65.28  ?  174 ASP A O   1 
ATOM 1303 C CB  . ASP A 1 174 ? 26.345  -7.391  15.412  1.00 58.12  ?  174 ASP A CB  1 
ATOM 1304 C CG  . ASP A 1 174 ? 25.252  -7.797  16.378  1.00 62.28  ?  174 ASP A CG  1 
ATOM 1305 O OD1 . ASP A 1 174 ? 24.363  -8.585  15.986  1.00 61.59  ?  174 ASP A OD1 1 
ATOM 1306 O OD2 . ASP A 1 174 ? 25.273  -7.312  17.528  1.00 67.80  ?  174 ASP A OD2 1 
ATOM 1307 N N   . SER A 1 175 ? 26.045  -3.987  16.644  1.00 59.48  ?  175 SER A N   1 
ATOM 1308 C CA  . SER A 1 175 ? 25.249  -2.757  16.570  1.00 52.93  ?  175 SER A CA  1 
ATOM 1309 C C   . SER A 1 175 ? 23.766  -3.049  16.356  1.00 55.58  ?  175 SER A C   1 
ATOM 1310 O O   . SER A 1 175 ? 23.072  -2.320  15.647  1.00 56.98  ?  175 SER A O   1 
ATOM 1311 C CB  . SER A 1 175 ? 25.772  -1.829  15.474  1.00 47.65  ?  175 SER A CB  1 
ATOM 1312 O OG  . SER A 1 175 ? 27.164  -1.615  15.607  1.00 55.29  ?  175 SER A OG  1 
ATOM 1313 N N   . THR A 1 176 ? 23.267  -4.104  16.990  1.00 58.28  ?  176 THR A N   1 
ATOM 1314 C CA  . THR A 1 176 ? 21.910  -4.571  16.751  1.00 58.54  ?  176 THR A CA  1 
ATOM 1315 C C   . THR A 1 176 ? 21.045  -4.316  17.983  1.00 59.44  ?  176 THR A C   1 
ATOM 1316 O O   . THR A 1 176 ? 21.531  -3.914  19.045  1.00 60.23  ?  176 THR A O   1 
ATOM 1317 C CB  . THR A 1 176 ? 21.921  -6.062  16.373  1.00 61.25  ?  176 THR A CB  1 
ATOM 1318 O OG1 . THR A 1 176 ? 20.738  -6.389  15.634  1.00 64.40  ?  176 THR A OG1 1 
ATOM 1319 C CG2 . THR A 1 176 ? 21.996  -6.941  17.615  1.00 58.84  ?  176 THR A CG2 1 
ATOM 1320 N N   . TYR A 1 177 ? 19.744  -4.562  17.833  1.00 60.13  ?  177 TYR A N   1 
ATOM 1321 C CA  . TYR A 1 177 ? 18.765  -4.279  18.873  1.00 55.18  ?  177 TYR A CA  1 
ATOM 1322 C C   . TYR A 1 177 ? 17.924  -5.510  19.178  1.00 54.29  ?  177 TYR A C   1 
ATOM 1323 O O   . TYR A 1 177 ? 17.849  -6.461  18.393  1.00 61.36  ?  177 TYR A O   1 
ATOM 1324 C CB  . TYR A 1 177 ? 17.829  -3.127  18.472  1.00 59.19  ?  177 TYR A CB  1 
ATOM 1325 C CG  . TYR A 1 177 ? 18.513  -1.788  18.365  1.00 61.94  ?  177 TYR A CG  1 
ATOM 1326 C CD1 . TYR A 1 177 ? 18.921  -1.103  19.508  1.00 60.16  ?  177 TYR A CD1 1 
ATOM 1327 C CD2 . TYR A 1 177 ? 18.758  -1.207  17.123  1.00 55.82  ?  177 TYR A CD2 1 
ATOM 1328 C CE1 . TYR A 1 177 ? 19.550  0.124   19.420  1.00 60.77  ?  177 TYR A CE1 1 
ATOM 1329 C CE2 . TYR A 1 177 ? 19.390  0.020   17.024  1.00 60.46  ?  177 TYR A CE2 1 
ATOM 1330 C CZ  . TYR A 1 177 ? 19.784  0.680   18.178  1.00 61.43  ?  177 TYR A CZ  1 
ATOM 1331 O OH  . TYR A 1 177 ? 20.414  1.898   18.093  1.00 62.52  ?  177 TYR A OH  1 
ATOM 1332 N N   . SER A 1 178 ? 17.273  -5.471  20.335  1.00 52.75  ?  178 SER A N   1 
ATOM 1333 C CA  . SER A 1 178 ? 16.301  -6.487  20.708  1.00 53.09  ?  178 SER A CA  1 
ATOM 1334 C C   . SER A 1 178 ? 15.108  -5.785  21.338  1.00 53.71  ?  178 SER A C   1 
ATOM 1335 O O   . SER A 1 178 ? 15.280  -4.878  22.158  1.00 61.78  ?  178 SER A O   1 
ATOM 1336 C CB  . SER A 1 178 ? 16.908  -7.521  21.660  1.00 58.63  ?  178 SER A CB  1 
ATOM 1337 O OG  . SER A 1 178 ? 17.855  -8.339  20.986  1.00 57.70  ?  178 SER A OG  1 
ATOM 1338 N N   . LEU A 1 179 ? 13.910  -6.201  20.939  1.00 43.36  ?  179 LEU A N   1 
ATOM 1339 C CA  . LEU A 1 179 ? 12.663  -5.538  21.291  1.00 47.02  ?  179 LEU A CA  1 
ATOM 1340 C C   . LEU A 1 179 ? 11.704  -6.547  21.899  1.00 52.12  ?  179 LEU A C   1 
ATOM 1341 O O   . LEU A 1 179 ? 11.635  -7.694  21.454  1.00 50.51  ?  179 LEU A O   1 
ATOM 1342 C CB  . LEU A 1 179 ? 12.033  -4.876  20.046  1.00 53.85  ?  179 LEU A CB  1 
ATOM 1343 C CG  . LEU A 1 179 ? 10.799  -3.961  20.071  1.00 50.42  ?  179 LEU A CG  1 
ATOM 1344 C CD1 . LEU A 1 179 ? 9.486   -4.746  20.194  1.00 54.19  ?  179 LEU A CD1 1 
ATOM 1345 C CD2 . LEU A 1 179 ? 10.910  -2.911  21.155  1.00 60.99  ?  179 LEU A CD2 1 
ATOM 1346 N N   . SER A 1 180 ? 10.950  -6.119  22.907  1.00 55.24  ?  180 SER A N   1 
ATOM 1347 C CA  . SER A 1 180 ? 9.944   -6.974  23.521  1.00 55.44  ?  180 SER A CA  1 
ATOM 1348 C C   . SER A 1 180 ? 8.632   -6.215  23.545  1.00 54.53  ?  180 SER A C   1 
ATOM 1349 O O   . SER A 1 180 ? 8.601   -5.043  23.929  1.00 61.25  ?  180 SER A O   1 
ATOM 1350 C CB  . SER A 1 180 ? 10.335  -7.406  24.938  1.00 55.75  ?  180 SER A CB  1 
ATOM 1351 O OG  . SER A 1 180 ? 10.194  -6.335  25.857  1.00 68.85  ?  180 SER A OG  1 
ATOM 1352 N N   . SER A 1 181 ? 7.567   -6.869  23.097  1.00 52.09  ?  181 SER A N   1 
ATOM 1353 C CA  . SER A 1 181 ? 6.226   -6.300  23.109  1.00 57.61  ?  181 SER A CA  1 
ATOM 1354 C C   . SER A 1 181 ? 5.346   -7.189  23.972  1.00 62.79  ?  181 SER A C   1 
ATOM 1355 O O   . SER A 1 181 ? 5.165   -8.371  23.668  1.00 58.40  ?  181 SER A O   1 
ATOM 1356 C CB  . SER A 1 181 ? 5.656   -6.185  21.695  1.00 59.18  ?  181 SER A CB  1 
ATOM 1357 O OG  . SER A 1 181 ? 4.360   -5.611  21.720  1.00 60.46  ?  181 SER A OG  1 
ATOM 1358 N N   . THR A 1 182 ? 4.818   -6.630  25.052  1.00 64.03  ?  182 THR A N   1 
ATOM 1359 C CA  . THR A 1 182 ? 4.003   -7.374  25.999  1.00 59.79  ?  182 THR A CA  1 
ATOM 1360 C C   . THR A 1 182 ? 2.556   -6.925  25.855  1.00 62.48  ?  182 THR A C   1 
ATOM 1361 O O   . THR A 1 182 ? 2.251   -5.739  26.023  1.00 64.26  ?  182 THR A O   1 
ATOM 1362 C CB  . THR A 1 182 ? 4.505   -7.162  27.424  1.00 55.44  ?  182 THR A CB  1 
ATOM 1363 O OG1 . THR A 1 182 ? 5.929   -7.318  27.445  1.00 56.08  ?  182 THR A OG1 1 
ATOM 1364 C CG2 . THR A 1 182 ? 3.879   -8.187  28.356  1.00 58.13  ?  182 THR A CG2 1 
ATOM 1365 N N   . LEU A 1 183 ? 1.681   -7.867  25.522  1.00 56.62  ?  183 LEU A N   1 
ATOM 1366 C CA  . LEU A 1 183 ? 0.253   -7.619  25.401  1.00 60.39  ?  183 LEU A CA  1 
ATOM 1367 C C   . LEU A 1 183 ? -0.439  -8.197  26.628  1.00 59.78  ?  183 LEU A C   1 
ATOM 1368 O O   . LEU A 1 183 ? -0.339  -9.401  26.890  1.00 58.87  ?  183 LEU A O   1 
ATOM 1369 C CB  . LEU A 1 183 ? -0.297  -8.252  24.127  1.00 65.17  ?  183 LEU A CB  1 
ATOM 1370 C CG  . LEU A 1 183 ? -1.774  -7.990  23.848  1.00 69.96  ?  183 LEU A CG  1 
ATOM 1371 C CD1 . LEU A 1 183 ? -1.951  -6.619  23.189  1.00 64.18  ?  183 LEU A CD1 1 
ATOM 1372 C CD2 . LEU A 1 183 ? -2.365  -9.106  23.005  1.00 62.14  ?  183 LEU A CD2 1 
ATOM 1373 N N   . THR A 1 184 ? -1.137  -7.344  27.373  1.00 66.74  ?  184 THR A N   1 
ATOM 1374 C CA  . THR A 1 184 ? -1.762  -7.724  28.631  1.00 66.42  ?  184 THR A CA  1 
ATOM 1375 C C   . THR A 1 184 ? -3.277  -7.782  28.481  1.00 63.47  ?  184 THR A C   1 
ATOM 1376 O O   . THR A 1 184 ? -3.886  -6.896  27.874  1.00 64.69  ?  184 THR A O   1 
ATOM 1377 C CB  . THR A 1 184 ? -1.389  -6.738  29.742  1.00 60.52  ?  184 THR A CB  1 
ATOM 1378 O OG1 . THR A 1 184 ? 0.016   -6.461  29.686  1.00 56.20  ?  184 THR A OG1 1 
ATOM 1379 C CG2 . THR A 1 184 ? -1.731  -7.320  31.102  1.00 60.23  ?  184 THR A CG2 1 
ATOM 1380 N N   . LEU A 1 185 ? -3.878  -8.830  29.041  1.00 66.47  ?  185 LEU A N   1 
ATOM 1381 C CA  . LEU A 1 185 ? -5.321  -9.012  29.023  1.00 69.55  ?  185 LEU A CA  1 
ATOM 1382 C C   . LEU A 1 185 ? -5.761  -9.633  30.340  1.00 73.83  ?  185 LEU A C   1 
ATOM 1383 O O   . LEU A 1 185 ? -4.950  -10.143 31.117  1.00 74.72  ?  185 LEU A O   1 
ATOM 1384 C CB  . LEU A 1 185 ? -5.769  -9.904  27.858  1.00 76.00  ?  185 LEU A CB  1 
ATOM 1385 C CG  . LEU A 1 185 ? -5.509  -9.438  26.425  1.00 78.66  ?  185 LEU A CG  1 
ATOM 1386 C CD1 . LEU A 1 185 ? -5.861  -10.542 25.441  1.00 67.89  ?  185 LEU A CD1 1 
ATOM 1387 C CD2 . LEU A 1 185 ? -6.296  -8.171  26.120  1.00 85.56  ?  185 LEU A CD2 1 
ATOM 1388 N N   . SER A 1 186 ? -7.065  -9.582  30.590  1.00 75.99  ?  186 SER A N   1 
ATOM 1389 C CA  . SER A 1 186 ? -7.646  -10.333 31.689  1.00 84.58  ?  186 SER A CA  1 
ATOM 1390 C C   . SER A 1 186 ? -7.800  -11.796 31.285  1.00 85.83  ?  186 SER A C   1 
ATOM 1391 O O   . SER A 1 186 ? -7.723  -12.145 30.104  1.00 90.76  ?  186 SER A O   1 
ATOM 1392 C CB  . SER A 1 186 ? -8.995  -9.738  32.097  1.00 88.07  ?  186 SER A CB  1 
ATOM 1393 O OG  . SER A 1 186 ? -9.902  -9.725  31.009  1.00 87.95  ?  186 SER A OG  1 
ATOM 1394 N N   . LYS A 1 187 ? -8.002  -12.662 32.282  1.00 81.85  ?  187 LYS A N   1 
ATOM 1395 C CA  . LYS A 1 187 ? -8.189  -14.079 31.980  1.00 86.19  ?  187 LYS A CA  1 
ATOM 1396 C C   . LYS A 1 187 ? -9.405  -14.292 31.089  1.00 90.19  ?  187 LYS A C   1 
ATOM 1397 O O   . LYS A 1 187 ? -9.375  -15.120 30.169  1.00 92.68  ?  187 LYS A O   1 
ATOM 1398 C CB  . LYS A 1 187 ? -8.324  -14.898 33.263  1.00 85.05  ?  187 LYS A CB  1 
ATOM 1399 C CG  . LYS A 1 187 ? -8.591  -16.376 32.995  1.00 77.70  ?  187 LYS A CG  1 
ATOM 1400 C CD  . LYS A 1 187 ? -8.668  -17.181 34.275  1.00 85.52  ?  187 LYS A CD  1 
ATOM 1401 C CE  . LYS A 1 187 ? -8.975  -18.643 33.994  1.00 79.51  ?  187 LYS A CE  1 
ATOM 1402 N NZ  . LYS A 1 187 ? -9.090  -19.418 35.260  1.00 81.85  ?  187 LYS A NZ  1 
ATOM 1403 N N   . ALA A 1 188 ? -10.484 -13.548 31.342  1.00 93.42  ?  188 ALA A N   1 
ATOM 1404 C CA  . ALA A 1 188 ? -11.694 -13.691 30.538  1.00 98.23  ?  188 ALA A CA  1 
ATOM 1405 C C   . ALA A 1 188 ? -11.438 -13.314 29.082  1.00 92.09  ?  188 ALA A C   1 
ATOM 1406 O O   . ALA A 1 188 ? -11.826 -14.047 28.163  1.00 87.88  ?  188 ALA A O   1 
ATOM 1407 C CB  . ALA A 1 188 ? -12.817 -12.837 31.130  1.00 100.74 ?  188 ALA A CB  1 
ATOM 1408 N N   . ASP A 1 189 ? -10.775 -12.174 28.852  1.00 87.09  ?  189 ASP A N   1 
ATOM 1409 C CA  . ASP A 1 189 ? -10.464 -11.761 27.485  1.00 93.58  ?  189 ASP A CA  1 
ATOM 1410 C C   . ASP A 1 189 ? -9.545  -12.755 26.788  1.00 90.90  ?  189 ASP A C   1 
ATOM 1411 O O   . ASP A 1 189 ? -9.584  -12.876 25.558  1.00 89.18  ?  189 ASP A O   1 
ATOM 1412 C CB  . ASP A 1 189 ? -9.831  -10.368 27.473  1.00 91.64  ?  189 ASP A CB  1 
ATOM 1413 C CG  . ASP A 1 189 ? -10.841 -9.264  27.720  1.00 96.02  ?  189 ASP A CG  1 
ATOM 1414 O OD1 . ASP A 1 189 ? -11.080 -8.922  28.899  1.00 102.87 ?  189 ASP A OD1 1 
ATOM 1415 O OD2 . ASP A 1 189 ? -11.397 -8.739  26.732  1.00 89.44  ?  189 ASP A OD2 1 
ATOM 1416 N N   . TYR A 1 190 ? -8.702  -13.459 27.546  1.00 85.59  ?  190 TYR A N   1 
ATOM 1417 C CA  . TYR A 1 190 ? -7.853  -14.479 26.940  1.00 86.34  ?  190 TYR A CA  1 
ATOM 1418 C C   . TYR A 1 190 ? -8.661  -15.719 26.565  1.00 86.91  ?  190 TYR A C   1 
ATOM 1419 O O   . TYR A 1 190 ? -8.450  -16.301 25.495  1.00 85.78  ?  190 TYR A O   1 
ATOM 1420 C CB  . TYR A 1 190 ? -6.707  -14.833 27.889  1.00 88.38  ?  190 TYR A CB  1 
ATOM 1421 C CG  . TYR A 1 190 ? -5.727  -15.855 27.347  1.00 87.98  ?  190 TYR A CG  1 
ATOM 1422 C CD1 . TYR A 1 190 ? -4.834  -15.522 26.332  1.00 80.88  ?  190 TYR A CD1 1 
ATOM 1423 C CD2 . TYR A 1 190 ? -5.684  -17.147 27.863  1.00 81.19  ?  190 TYR A CD2 1 
ATOM 1424 C CE1 . TYR A 1 190 ? -3.934  -16.451 25.840  1.00 81.28  ?  190 TYR A CE1 1 
ATOM 1425 C CE2 . TYR A 1 190 ? -4.786  -18.082 27.380  1.00 80.33  ?  190 TYR A CE2 1 
ATOM 1426 C CZ  . TYR A 1 190 ? -3.914  -17.730 26.368  1.00 85.29  ?  190 TYR A CZ  1 
ATOM 1427 O OH  . TYR A 1 190 ? -3.020  -18.661 25.882  1.00 80.63  ?  190 TYR A OH  1 
ATOM 1428 N N   . GLU A 1 191 ? -9.601  -16.131 27.424  1.00 88.47  ?  191 GLU A N   1 
ATOM 1429 C CA  . GLU A 1 191 ? -10.440 -17.284 27.100  1.00 87.45  ?  191 GLU A CA  1 
ATOM 1430 C C   . GLU A 1 191 ? -11.448 -16.992 25.995  1.00 84.97  ?  191 GLU A C   1 
ATOM 1431 O O   . GLU A 1 191 ? -11.934 -17.933 25.361  1.00 87.03  ?  191 GLU A O   1 
ATOM 1432 C CB  . GLU A 1 191 ? -11.194 -17.782 28.339  1.00 88.91  ?  191 GLU A CB  1 
ATOM 1433 C CG  . GLU A 1 191 ? -10.352 -17.980 29.590  1.00 85.95  ?  191 GLU A CG  1 
ATOM 1434 C CD  . GLU A 1 191 ? -9.563  -19.277 29.583  1.00 89.19  ?  191 GLU A CD  1 
ATOM 1435 O OE1 . GLU A 1 191 ? -9.122  -19.713 28.499  1.00 88.44  ?  191 GLU A OE1 1 
ATOM 1436 O OE2 . GLU A 1 191 ? -9.390  -19.866 30.670  1.00 89.99  ?  191 GLU A OE2 1 
ATOM 1437 N N   . LYS A 1 192 ? -11.781 -15.720 25.755  1.00 85.76  ?  192 LYS A N   1 
ATOM 1438 C CA  . LYS A 1 192 ? -12.788 -15.381 24.749  1.00 86.72  ?  192 LYS A CA  1 
ATOM 1439 C C   . LYS A 1 192 ? -12.306 -15.569 23.313  1.00 89.35  ?  192 LYS A C   1 
ATOM 1440 O O   . LYS A 1 192 ? -13.090 -15.318 22.389  1.00 86.24  ?  192 LYS A O   1 
ATOM 1441 C CB  . LYS A 1 192 ? -13.260 -13.932 24.919  1.00 84.04  ?  192 LYS A CB  1 
ATOM 1442 C CG  . LYS A 1 192 ? -14.276 -13.704 26.029  1.00 87.79  ?  192 LYS A CG  1 
ATOM 1443 C CD  . LYS A 1 192 ? -14.622 -12.222 26.163  1.00 87.27  ?  192 LYS A CD  1 
ATOM 1444 C CE  . LYS A 1 192 ? -15.608 -11.968 27.302  1.00 86.39  ?  192 LYS A CE  1 
ATOM 1445 N NZ  . LYS A 1 192 ? -16.955 -12.552 27.047  1.00 81.36  ?  192 LYS A NZ  1 
ATOM 1446 N N   . HIS A 1 193 ? -11.057 -15.971 23.084  1.00 85.56  ?  193 HIS A N   1 
ATOM 1447 C CA  . HIS A 1 193 ? -10.522 -16.033 21.732  1.00 84.76  ?  193 HIS A CA  1 
ATOM 1448 C C   . HIS A 1 193 ? -9.637  -17.266 21.589  1.00 88.10  ?  193 HIS A C   1 
ATOM 1449 O O   . HIS A 1 193 ? -9.511  -18.079 22.513  1.00 86.40  ?  193 HIS A O   1 
ATOM 1450 C CB  . HIS A 1 193 ? -9.773  -14.743 21.384  1.00 85.90  ?  193 HIS A CB  1 
ATOM 1451 C CG  . HIS A 1 193 ? -10.623 -13.513 21.472  1.00 82.57  ?  193 HIS A CG  1 
ATOM 1452 N ND1 . HIS A 1 193 ? -11.768 -13.345 20.723  1.00 82.42  ?  193 HIS A ND1 1 
ATOM 1453 C CD2 . HIS A 1 193 ? -10.488 -12.385 22.209  1.00 84.21  ?  193 HIS A CD2 1 
ATOM 1454 C CE1 . HIS A 1 193 ? -12.306 -12.171 21.002  1.00 83.91  ?  193 HIS A CE1 1 
ATOM 1455 N NE2 . HIS A 1 193 ? -11.548 -11.568 21.899  1.00 85.67  ?  193 HIS A NE2 1 
ATOM 1456 N N   . LYS A 1 194 ? -9.019  -17.404 20.411  1.00 89.04  ?  194 LYS A N   1 
ATOM 1457 C CA  . LYS A 1 194 ? -8.252  -18.603 20.078  1.00 89.56  ?  194 LYS A CA  1 
ATOM 1458 C C   . LYS A 1 194 ? -6.910  -18.270 19.433  1.00 84.60  ?  194 LYS A C   1 
ATOM 1459 O O   . LYS A 1 194 ? -5.870  -18.775 19.867  1.00 85.24  ?  194 LYS A O   1 
ATOM 1460 C CB  . LYS A 1 194 ? -9.063  -19.527 19.164  1.00 81.69  ?  194 LYS A CB  1 
ATOM 1461 C CG  . LYS A 1 194 ? -8.300  -20.770 18.725  1.00 84.44  ?  194 LYS A CG  1 
ATOM 1462 C CD  . LYS A 1 194 ? -9.057  -21.564 17.671  1.00 81.41  ?  194 LYS A CD  1 
ATOM 1463 C CE  . LYS A 1 194 ? -8.209  -22.715 17.139  1.00 91.53  ?  194 LYS A CE  1 
ATOM 1464 N NZ  . LYS A 1 194 ? -8.858  -23.422 15.996  1.00 90.31  ?  194 LYS A NZ  1 
ATOM 1465 N N   . VAL A 1 195 ? -6.920  -17.454 18.382  1.00 76.84  ?  195 VAL A N   1 
ATOM 1466 C CA  . VAL A 1 195 ? -5.731  -17.187 17.576  1.00 78.53  ?  195 VAL A CA  1 
ATOM 1467 C C   . VAL A 1 195 ? -5.116  -15.863 18.014  1.00 75.02  ?  195 VAL A C   1 
ATOM 1468 O O   . VAL A 1 195 ? -5.784  -14.822 17.997  1.00 78.11  ?  195 VAL A O   1 
ATOM 1469 C CB  . VAL A 1 195 ? -6.072  -17.161 16.078  1.00 79.50  ?  195 VAL A CB  1 
ATOM 1470 C CG1 . VAL A 1 195 ? -4.824  -16.907 15.253  1.00 75.06  ?  195 VAL A CG1 1 
ATOM 1471 C CG2 . VAL A 1 195 ? -6.745  -18.461 15.660  1.00 77.31  ?  195 VAL A CG2 1 
ATOM 1472 N N   . TYR A 1 196 ? -3.839  -15.895 18.394  1.00 71.71  ?  196 TYR A N   1 
ATOM 1473 C CA  . TYR A 1 196 ? -3.088  -14.707 18.776  1.00 73.28  ?  196 TYR A CA  1 
ATOM 1474 C C   . TYR A 1 196 ? -1.847  -14.599 17.901  1.00 67.46  ?  196 TYR A C   1 
ATOM 1475 O O   . TYR A 1 196 ? -1.232  -15.614 17.560  1.00 68.73  ?  196 TYR A O   1 
ATOM 1476 C CB  . TYR A 1 196 ? -2.687  -14.758 20.259  1.00 75.79  ?  196 TYR A CB  1 
ATOM 1477 C CG  . TYR A 1 196 ? -3.864  -14.711 21.208  1.00 73.24  ?  196 TYR A CG  1 
ATOM 1478 C CD1 . TYR A 1 196 ? -4.251  -13.518 21.813  1.00 67.76  ?  196 TYR A CD1 1 
ATOM 1479 C CD2 . TYR A 1 196 ? -4.591  -15.860 21.496  1.00 75.44  ?  196 TYR A CD2 1 
ATOM 1480 C CE1 . TYR A 1 196 ? -5.331  -13.473 22.677  1.00 69.45  ?  196 TYR A CE1 1 
ATOM 1481 C CE2 . TYR A 1 196 ? -5.673  -15.825 22.356  1.00 80.46  ?  196 TYR A CE2 1 
ATOM 1482 C CZ  . TYR A 1 196 ? -6.037  -14.631 22.943  1.00 79.06  ?  196 TYR A CZ  1 
ATOM 1483 O OH  . TYR A 1 196 ? -7.112  -14.602 23.799  1.00 81.27  ?  196 TYR A OH  1 
ATOM 1484 N N   . ALA A 1 197 ? -1.467  -13.374 17.546  1.00 57.09  ?  197 ALA A N   1 
ATOM 1485 C CA  . ALA A 1 197 ? -0.349  -13.200 16.631  1.00 59.14  ?  197 ALA A CA  1 
ATOM 1486 C C   . ALA A 1 197 ? 0.261   -11.824 16.818  1.00 61.54  ?  197 ALA A C   1 
ATOM 1487 O O   . ALA A 1 197 ? -0.432  -10.866 17.166  1.00 64.51  ?  197 ALA A O   1 
ATOM 1488 C CB  . ALA A 1 197 ? -0.794  -13.370 15.176  1.00 66.26  ?  197 ALA A CB  1 
ATOM 1489 N N   . CYS A 1 198 ? 1.563   -11.730 16.568  1.00 61.23  ?  198 CYS A N   1 
ATOM 1490 C CA  . CYS A 1 198 ? 2.229   -10.439 16.468  1.00 63.03  ?  198 CYS A CA  1 
ATOM 1491 C C   . CYS A 1 198 ? 2.875   -10.339 15.100  1.00 64.32  ?  198 CYS A C   1 
ATOM 1492 O O   . CYS A 1 198 ? 3.504   -11.295 14.629  1.00 66.72  ?  198 CYS A O   1 
ATOM 1493 C CB  . CYS A 1 198 ? 3.266   -10.203 17.580  1.00 62.46  ?  198 CYS A CB  1 
ATOM 1494 S SG  . CYS A 1 198 ? 4.577   -11.438 17.788  1.00 79.49  ?  198 CYS A SG  1 
ATOM 1495 N N   . GLU A 1 199 ? 2.668   -9.197  14.458  1.00 63.66  ?  199 GLU A N   1 
ATOM 1496 C CA  . GLU A 1 199 ? 3.190   -8.895  13.135  1.00 60.49  ?  199 GLU A CA  1 
ATOM 1497 C C   . GLU A 1 199 ? 4.245   -7.806  13.267  1.00 63.23  ?  199 GLU A C   1 
ATOM 1498 O O   . GLU A 1 199 ? 3.970   -6.732  13.815  1.00 64.94  ?  199 GLU A O   1 
ATOM 1499 C CB  . GLU A 1 199 ? 2.064   -8.446  12.206  1.00 66.30  ?  199 GLU A CB  1 
ATOM 1500 C CG  . GLU A 1 199 ? 2.515   -8.110  10.802  1.00 68.43  ?  199 GLU A CG  1 
ATOM 1501 C CD  . GLU A 1 199 ? 1.371   -7.664  9.918   1.00 72.90  ?  199 GLU A CD  1 
ATOM 1502 O OE1 . GLU A 1 199 ? 0.240   -7.516  10.429  1.00 68.65  ?  199 GLU A OE1 1 
ATOM 1503 O OE2 . GLU A 1 199 ? 1.609   -7.454  8.710   1.00 84.37  ?  199 GLU A OE2 1 
ATOM 1504 N N   . VAL A 1 200 ? 5.450   -8.085  12.781  1.00 64.68  ?  200 VAL A N   1 
ATOM 1505 C CA  . VAL A 1 200 ? 6.543   -7.121  12.780  1.00 65.82  ?  200 VAL A CA  1 
ATOM 1506 C C   . VAL A 1 200 ? 6.752   -6.648  11.348  1.00 63.97  ?  200 VAL A C   1 
ATOM 1507 O O   . VAL A 1 200 ? 6.999   -7.460  10.447  1.00 67.39  ?  200 VAL A O   1 
ATOM 1508 C CB  . VAL A 1 200 ? 7.832   -7.724  13.355  1.00 66.59  ?  200 VAL A CB  1 
ATOM 1509 C CG1 . VAL A 1 200 ? 8.977   -6.723  13.252  1.00 57.60  ?  200 VAL A CG1 1 
ATOM 1510 C CG2 . VAL A 1 200 ? 7.613   -8.153  14.795  1.00 69.16  ?  200 VAL A CG2 1 
ATOM 1511 N N   . THR A 1 201 ? 6.648   -5.340  11.141  1.00 62.85  ?  201 THR A N   1 
ATOM 1512 C CA  . THR A 1 201 ? 6.871   -4.709  9.849   1.00 65.51  ?  201 THR A CA  1 
ATOM 1513 C C   . THR A 1 201 ? 8.163   -3.908  9.907   1.00 64.86  ?  201 THR A C   1 
ATOM 1514 O O   . THR A 1 201 ? 8.373   -3.122  10.841  1.00 68.11  ?  201 THR A O   1 
ATOM 1515 C CB  . THR A 1 201 ? 5.700   -3.800  9.474   1.00 68.49  ?  201 THR A CB  1 
ATOM 1516 O OG1 . THR A 1 201 ? 4.474   -4.540  9.553   1.00 73.46  ?  201 THR A OG1 1 
ATOM 1517 C CG2 . THR A 1 201 ? 5.875   -3.251  8.067   1.00 62.85  ?  201 THR A CG2 1 
ATOM 1518 N N   . GLN A 1 202 ? 9.033   -4.126  8.908   1.00 63.50  ?  202 GLN A N   1 
ATOM 1519 C CA  . GLN A 1 202 ? 10.352  -3.498  8.804   1.00 61.36  ?  202 GLN A CA  1 
ATOM 1520 C C   . GLN A 1 202 ? 10.578  -3.173  7.324   1.00 66.16  ?  202 GLN A C   1 
ATOM 1521 O O   . GLN A 1 202 ? 11.196  -3.938  6.578   1.00 70.97  ?  202 GLN A O   1 
ATOM 1522 C CB  . GLN A 1 202 ? 11.434  -4.421  9.368   1.00 64.55  ?  202 GLN A CB  1 
ATOM 1523 C CG  . GLN A 1 202 ? 12.846  -3.855  9.416   1.00 70.40  ?  202 GLN A CG  1 
ATOM 1524 C CD  . GLN A 1 202 ? 13.875  -4.917  9.810   1.00 70.49  ?  202 GLN A CD  1 
ATOM 1525 O OE1 . GLN A 1 202 ? 13.689  -6.104  9.532   1.00 72.81  ?  202 GLN A OE1 1 
ATOM 1526 N NE2 . GLN A 1 202 ? 14.954  -4.495  10.469  1.00 61.40  ?  202 GLN A NE2 1 
ATOM 1527 N N   . GLY A 1 203 ? 10.044  -2.035  6.887   1.00 65.22  ?  203 GLY A N   1 
ATOM 1528 C CA  . GLY A 1 203 ? 10.178  -1.627  5.499   1.00 76.36  ?  203 GLY A CA  1 
ATOM 1529 C C   . GLY A 1 203 ? 9.190   -2.302  4.564   1.00 73.66  ?  203 GLY A C   1 
ATOM 1530 O O   . GLY A 1 203 ? 7.975   -2.119  4.692   1.00 69.73  ?  203 GLY A O   1 
ATOM 1531 N N   . THR A 1 204 ? 9.695   -3.096  3.623   1.00 68.38  ?  204 THR A N   1 
ATOM 1532 C CA  . THR A 1 204 ? 8.834   -3.804  2.684   1.00 71.60  ?  204 THR A CA  1 
ATOM 1533 C C   . THR A 1 204 ? 8.468   -5.210  3.148   1.00 73.56  ?  204 THR A C   1 
ATOM 1534 O O   . THR A 1 204 ? 7.804   -5.933  2.400   1.00 70.82  ?  204 THR A O   1 
ATOM 1535 C CB  . THR A 1 204 ? 9.498   -3.894  1.302   1.00 69.35  ?  204 THR A CB  1 
ATOM 1536 O OG1 . THR A 1 204 ? 10.825  -4.420  1.437   1.00 77.95  ?  204 THR A OG1 1 
ATOM 1537 C CG2 . THR A 1 204 ? 9.552   -2.532  0.630   1.00 70.41  ?  204 THR A CG2 1 
ATOM 1538 N N   . THR A 1 205 ? 8.867   -5.615  4.352   1.00 73.14  ?  205 THR A N   1 
ATOM 1539 C CA  . THR A 1 205 ? 8.594   -6.953  4.858   1.00 68.24  ?  205 THR A CA  1 
ATOM 1540 C C   . THR A 1 205 ? 7.769   -6.865  6.135   1.00 64.28  ?  205 THR A C   1 
ATOM 1541 O O   . THR A 1 205 ? 7.946   -5.943  6.936   1.00 64.12  ?  205 THR A O   1 
ATOM 1542 C CB  . THR A 1 205 ? 9.896   -7.720  5.120   1.00 70.96  ?  205 THR A CB  1 
ATOM 1543 O OG1 . THR A 1 205 ? 10.745  -7.627  3.967   1.00 75.12  ?  205 THR A OG1 1 
ATOM 1544 C CG2 . THR A 1 205 ? 9.606   -9.186  5.405   1.00 56.76  ?  205 THR A CG2 1 
ATOM 1545 N N   . SER A 1 206 ? 6.854   -7.820  6.314   1.00 60.43  ?  206 SER A N   1 
ATOM 1546 C CA  . SER A 1 206 ? 5.989   -7.836  7.494   1.00 63.06  ?  206 SER A CA  1 
ATOM 1547 C C   . SER A 1 206 ? 5.706   -9.297  7.840   1.00 61.32  ?  206 SER A C   1 
ATOM 1548 O O   . SER A 1 206 ? 4.822   -9.923  7.247   1.00 59.74  ?  206 SER A O   1 
ATOM 1549 C CB  . SER A 1 206 ? 4.706   -7.049  7.256   1.00 62.72  ?  206 SER A CB  1 
ATOM 1550 O OG  . SER A 1 206 ? 3.766   -7.814  6.523   1.00 74.25  ?  206 SER A OG  1 
ATOM 1551 N N   . VAL A 1 207 ? 6.447   -9.821  8.812   1.00 61.14  ?  207 VAL A N   1 
ATOM 1552 C CA  . VAL A 1 207 ? 6.374   -11.229 9.193   1.00 60.00  ?  207 VAL A CA  1 
ATOM 1553 C C   . VAL A 1 207 ? 5.540   -11.364 10.463  1.00 60.14  ?  207 VAL A C   1 
ATOM 1554 O O   . VAL A 1 207 ? 5.746   -10.630 11.438  1.00 58.23  ?  207 VAL A O   1 
ATOM 1555 C CB  . VAL A 1 207 ? 7.782   -11.825 9.379   1.00 56.13  ?  207 VAL A CB  1 
ATOM 1556 C CG1 . VAL A 1 207 ? 8.671   -10.870 10.154  1.00 65.57  ?  207 VAL A CG1 1 
ATOM 1557 C CG2 . VAL A 1 207 ? 7.707   -13.169 10.080  1.00 53.68  ?  207 VAL A CG2 1 
ATOM 1558 N N   . THR A 1 208 ? 4.603   -12.309 10.455  1.00 58.56  ?  208 THR A N   1 
ATOM 1559 C CA  . THR A 1 208 ? 3.677   -12.525 11.558  1.00 54.96  ?  208 THR A CA  1 
ATOM 1560 C C   . THR A 1 208 ? 3.920   -13.896 12.165  1.00 60.36  ?  208 THR A C   1 
ATOM 1561 O O   . THR A 1 208 ? 3.875   -14.907 11.457  1.00 64.89  ?  208 THR A O   1 
ATOM 1562 C CB  . THR A 1 208 ? 2.222   -12.444 11.082  1.00 56.94  ?  208 THR A CB  1 
ATOM 1563 O OG1 . THR A 1 208 ? 1.983   -11.186 10.442  1.00 67.63  ?  208 THR A OG1 1 
ATOM 1564 C CG2 . THR A 1 208 ? 1.266   -12.615 12.247  1.00 58.27  ?  208 THR A CG2 1 
ATOM 1565 N N   . LYS A 1 209 ? 4.138   -13.933 13.475  1.00 64.29  ?  209 LYS A N   1 
ATOM 1566 C CA  . LYS A 1 209 ? 4.241   -15.182 14.215  1.00 56.19  ?  209 LYS A CA  1 
ATOM 1567 C C   . LYS A 1 209 ? 3.014   -15.318 15.100  1.00 59.43  ?  209 LYS A C   1 
ATOM 1568 O O   . LYS A 1 209 ? 2.610   -14.360 15.769  1.00 71.80  ?  209 LYS A O   1 
ATOM 1569 C CB  . LYS A 1 209 ? 5.517   -15.231 15.061  1.00 58.02  ?  209 LYS A CB  1 
ATOM 1570 C CG  . LYS A 1 209 ? 6.802   -15.276 14.245  1.00 61.11  ?  209 LYS A CG  1 
ATOM 1571 C CD  . LYS A 1 209 ? 7.141   -16.691 13.796  1.00 57.69  ?  209 LYS A CD  1 
ATOM 1572 C CE  . LYS A 1 209 ? 8.332   -16.708 12.833  1.00 57.50  ?  209 LYS A CE  1 
ATOM 1573 N NZ  . LYS A 1 209 ? 9.579   -16.089 13.374  1.00 56.98  ?  209 LYS A NZ  1 
ATOM 1574 N N   . SER A 1 210 ? 2.431   -16.511 15.114  1.00 58.01  ?  210 SER A N   1 
ATOM 1575 C CA  . SER A 1 210 ? 1.139   -16.716 15.746  1.00 63.39  ?  210 SER A CA  1 
ATOM 1576 C C   . SER A 1 210 ? 1.139   -18.009 16.551  1.00 70.12  ?  210 SER A C   1 
ATOM 1577 O O   . SER A 1 210 ? 2.081   -18.807 16.509  1.00 68.38  ?  210 SER A O   1 
ATOM 1578 C CB  . SER A 1 210 ? 0.015   -16.738 14.700  1.00 64.58  ?  210 SER A CB  1 
ATOM 1579 O OG  . SER A 1 210 ? 0.158   -17.831 13.805  1.00 72.80  ?  210 SER A OG  1 
ATOM 1580 N N   . PHE A 1 211 ? 0.058   -18.192 17.304  1.00 73.55  ?  211 PHE A N   1 
ATOM 1581 C CA  . PHE A 1 211 ? -0.240  -19.436 17.999  1.00 76.07  ?  211 PHE A CA  1 
ATOM 1582 C C   . PHE A 1 211 ? -1.729  -19.441 18.309  1.00 76.87  ?  211 PHE A C   1 
ATOM 1583 O O   . PHE A 1 211 ? -2.338  -18.383 18.496  1.00 78.23  ?  211 PHE A O   1 
ATOM 1584 C CB  . PHE A 1 211 ? 0.580   -19.593 19.285  1.00 70.69  ?  211 PHE A CB  1 
ATOM 1585 C CG  . PHE A 1 211 ? 0.054   -18.791 20.447  1.00 75.96  ?  211 PHE A CG  1 
ATOM 1586 C CD1 . PHE A 1 211 ? 0.428   -17.465 20.618  1.00 73.90  ?  211 PHE A CD1 1 
ATOM 1587 C CD2 . PHE A 1 211 ? -0.804  -19.365 21.375  1.00 74.02  ?  211 PHE A CD2 1 
ATOM 1588 C CE1 . PHE A 1 211 ? -0.051  -16.725 21.686  1.00 71.26  ?  211 PHE A CE1 1 
ATOM 1589 C CE2 . PHE A 1 211 ? -1.288  -18.629 22.441  1.00 76.14  ?  211 PHE A CE2 1 
ATOM 1590 C CZ  . PHE A 1 211 ? -0.911  -17.307 22.596  1.00 74.19  ?  211 PHE A CZ  1 
ATOM 1591 N N   . ASN A 1 212 ? -2.310  -20.633 18.365  1.00 76.01  ?  212 ASN A N   1 
ATOM 1592 C CA  . ASN A 1 212 ? -3.711  -20.778 18.724  1.00 86.30  ?  212 ASN A CA  1 
ATOM 1593 C C   . ASN A 1 212 ? -3.840  -21.460 20.078  1.00 93.28  ?  212 ASN A C   1 
ATOM 1594 O O   . ASN A 1 212 ? -3.099  -22.401 20.381  1.00 95.80  ?  212 ASN A O   1 
ATOM 1595 C CB  . ASN A 1 212 ? -4.460  -21.583 17.660  1.00 90.48  ?  212 ASN A CB  1 
ATOM 1596 C CG  . ASN A 1 212 ? -4.218  -21.060 16.254  1.00 97.38  ?  212 ASN A CG  1 
ATOM 1597 O OD1 . ASN A 1 212 ? -3.785  -19.922 16.066  1.00 96.31  ?  212 ASN A OD1 1 
ATOM 1598 N ND2 . ASN A 1 212 ? -4.497  -21.894 15.257  1.00 101.60 ?  212 ASN A ND2 1 
ATOM 1599 N N   . ARG A 1 213 ? -4.790  -20.990 20.884  1.00 91.32  ?  213 ARG A N   1 
ATOM 1600 C CA  . ARG A 1 213 ? -4.983  -21.553 22.212  1.00 94.12  ?  213 ARG A CA  1 
ATOM 1601 C C   . ARG A 1 213 ? -5.361  -23.026 22.115  1.00 104.04 ?  213 ARG A C   1 
ATOM 1602 O O   . ARG A 1 213 ? -5.924  -23.483 21.116  1.00 101.87 ?  213 ARG A O   1 
ATOM 1603 C CB  . ARG A 1 213 ? -6.063  -20.788 22.977  1.00 93.21  ?  213 ARG A CB  1 
ATOM 1604 C CG  . ARG A 1 213 ? -5.662  -19.393 23.424  1.00 90.69  ?  213 ARG A CG  1 
ATOM 1605 C CD  . ARG A 1 213 ? -6.712  -18.794 24.355  1.00 86.97  ?  213 ARG A CD  1 
ATOM 1606 N NE  . ARG A 1 213 ? -7.337  -19.814 25.198  1.00 89.34  ?  213 ARG A NE  1 
ATOM 1607 C CZ  . ARG A 1 213 ? -8.619  -20.159 25.132  1.00 89.27  ?  213 ARG A CZ  1 
ATOM 1608 N NH1 . ARG A 1 213 ? -9.423  -19.560 24.262  1.00 81.44  ?  213 ARG A NH1 1 
ATOM 1609 N NH2 . ARG A 1 213 ? -9.096  -21.104 25.937  1.00 79.65  ?  213 ARG A NH2 1 
ATOM 1610 N N   . GLY A 1 214 ? -5.045  -23.772 23.171  1.00 105.06 ?  214 GLY A N   1 
ATOM 1611 C CA  . GLY A 1 214 ? -5.360  -25.187 23.210  1.00 111.83 ?  214 GLY A CA  1 
ATOM 1612 C C   . GLY A 1 214 ? -4.484  -26.044 22.319  1.00 119.12 ?  214 GLY A C   1 
ATOM 1613 O O   . GLY A 1 214 ? -3.653  -26.814 22.816  1.00 118.61 ?  214 GLY A O   1 
ATOM 1614 N N   . GLU A 1 215 ? -4.657  -25.930 21.001  1.00 119.34 ?  215 GLU A N   1 
ATOM 1615 C CA  . GLU A 1 215 ? -3.878  -26.743 20.071  1.00 118.44 ?  215 GLU A CA  1 
ATOM 1616 C C   . GLU A 1 215 ? -2.409  -26.338 20.163  1.00 122.18 ?  215 GLU A C   1 
ATOM 1617 O O   . GLU A 1 215 ? -2.028  -25.225 19.784  1.00 120.04 ?  215 GLU A O   1 
ATOM 1618 C CB  . GLU A 1 215 ? -4.448  -26.609 18.657  1.00 113.01 ?  215 GLU A CB  1 
ATOM 1619 C CG  . GLU A 1 215 ? -4.354  -25.232 17.990  1.00 110.56 ?  215 GLU A CG  1 
ATOM 1620 C CD  . GLU A 1 215 ? -4.866  -25.243 16.558  1.00 113.78 ?  215 GLU A CD  1 
ATOM 1621 O OE1 . GLU A 1 215 ? -5.103  -26.346 16.017  1.00 113.12 ?  215 GLU A OE1 1 
ATOM 1622 O OE2 . GLU A 1 215 ? -5.054  -24.152 15.978  1.00 109.67 ?  215 GLU A OE2 1 
ATOM 1623 N N   . CYS A 1 216 ? -1.592  -27.260 20.670  1.00 124.26 ?  216 CYS A N   1 
ATOM 1624 C CA  . CYS A 1 216 ? -0.163  -27.073 20.925  1.00 127.19 ?  216 CYS A CA  1 
ATOM 1625 C C   . CYS A 1 216 ? 0.185   -25.840 21.773  1.00 126.07 ?  216 CYS A C   1 
ATOM 1626 O O   . CYS A 1 216 ? 0.930   -25.962 22.746  1.00 125.26 ?  216 CYS A O   1 
ATOM 1627 C CB  . CYS A 1 216 ? 0.608   -27.034 19.605  1.00 129.71 ?  216 CYS A CB  1 
ATOM 1628 S SG  . CYS A 1 216 ? 1.023   -28.700 19.034  1.00 142.94 ?  216 CYS A SG  1 
ATOM 1629 O OXT . CYS A 1 216 ? -0.239  -24.709 21.544  1.00 122.62 ?  216 CYS A OXT 1 
ATOM 1630 N N   . GLU B 2 1   ? 42.080  -4.382  40.559  1.00 90.39  ?  1   GLU B N   1 
ATOM 1631 C CA  . GLU B 2 1   ? 42.654  -4.509  41.896  1.00 100.03 ?  1   GLU B CA  1 
ATOM 1632 C C   . GLU B 2 1   ? 42.400  -3.258  42.730  1.00 95.88  ?  1   GLU B C   1 
ATOM 1633 O O   . GLU B 2 1   ? 42.583  -3.261  43.947  1.00 93.00  ?  1   GLU B O   1 
ATOM 1634 C CB  . GLU B 2 1   ? 44.155  -4.790  41.817  1.00 102.61 ?  1   GLU B CB  1 
ATOM 1635 C CG  . GLU B 2 1   ? 44.506  -6.148  41.228  1.00 107.84 ?  1   GLU B CG  1 
ATOM 1636 C CD  . GLU B 2 1   ? 46.000  -6.402  41.202  1.00 99.85  ?  1   GLU B CD  1 
ATOM 1637 O OE1 . GLU B 2 1   ? 46.498  -6.922  40.179  1.00 93.13  ?  1   GLU B OE1 1 
ATOM 1638 O OE2 . GLU B 2 1   ? 46.674  -6.076  42.204  1.00 93.17  ?  1   GLU B OE2 1 
ATOM 1639 N N   . VAL B 2 2   ? 41.986  -2.185  42.065  1.00 89.95  ?  2   VAL B N   1 
ATOM 1640 C CA  . VAL B 2 2   ? 41.600  -0.942  42.722  1.00 87.44  ?  2   VAL B CA  1 
ATOM 1641 C C   . VAL B 2 2   ? 40.108  -0.739  42.485  1.00 84.53  ?  2   VAL B C   1 
ATOM 1642 O O   . VAL B 2 2   ? 39.673  -0.573  41.337  1.00 82.13  ?  2   VAL B O   1 
ATOM 1643 C CB  . VAL B 2 2   ? 42.418  0.249   42.197  1.00 83.78  ?  2   VAL B CB  1 
ATOM 1644 C CG1 . VAL B 2 2   ? 42.193  1.468   43.058  1.00 76.25  ?  2   VAL B CG1 1 
ATOM 1645 C CG2 . VAL B 2 2   ? 43.899  -0.104  42.151  1.00 87.07  ?  2   VAL B CG2 1 
ATOM 1646 N N   . GLN B 2 3   ? 39.319  -0.763  43.564  1.00 72.55  ?  3   GLN B N   1 
ATOM 1647 C CA  . GLN B 2 3   ? 37.867  -0.748  43.439  1.00 71.61  ?  3   GLN B CA  1 
ATOM 1648 C C   . GLN B 2 3   ? 37.235  0.169   44.477  1.00 67.43  ?  3   GLN B C   1 
ATOM 1649 O O   . GLN B 2 3   ? 37.799  0.415   45.546  1.00 66.58  ?  3   GLN B O   1 
ATOM 1650 C CB  . GLN B 2 3   ? 37.255  -2.151  43.593  1.00 71.25  ?  3   GLN B CB  1 
ATOM 1651 C CG  . GLN B 2 3   ? 37.262  -3.007  42.336  1.00 75.66  ?  3   GLN B CG  1 
ATOM 1652 C CD  . GLN B 2 3   ? 36.561  -4.339  42.543  1.00 78.24  ?  3   GLN B CD  1 
ATOM 1653 O OE1 . GLN B 2 3   ? 36.314  -4.752  43.677  1.00 72.41  ?  3   GLN B OE1 1 
ATOM 1654 N NE2 . GLN B 2 3   ? 36.242  -5.020  41.447  1.00 85.31  ?  3   GLN B NE2 1 
ATOM 1655 N N   . LEU B 2 4   ? 36.047  0.672   44.131  1.00 66.77  ?  4   LEU B N   1 
ATOM 1656 C CA  . LEU B 2 4   ? 35.161  1.393   45.042  1.00 54.75  ?  4   LEU B CA  1 
ATOM 1657 C C   . LEU B 2 4   ? 33.797  0.718   44.975  1.00 53.32  ?  4   LEU B C   1 
ATOM 1658 O O   . LEU B 2 4   ? 33.112  0.796   43.949  1.00 49.71  ?  4   LEU B O   1 
ATOM 1659 C CB  . LEU B 2 4   ? 35.055  2.872   44.669  1.00 56.12  ?  4   LEU B CB  1 
ATOM 1660 C CG  . LEU B 2 4   ? 36.312  3.732   44.783  1.00 58.51  ?  4   LEU B CG  1 
ATOM 1661 C CD1 . LEU B 2 4   ? 36.056  5.104   44.189  1.00 51.90  ?  4   LEU B CD1 1 
ATOM 1662 C CD2 . LEU B 2 4   ? 36.740  3.847   46.232  1.00 60.84  ?  4   LEU B CD2 1 
ATOM 1663 N N   . VAL B 2 5   ? 33.401  0.060   46.059  1.00 58.44  ?  5   VAL B N   1 
ATOM 1664 C CA  . VAL B 2 5   ? 32.157  -0.700  46.123  1.00 56.19  ?  5   VAL B CA  1 
ATOM 1665 C C   . VAL B 2 5   ? 31.163  0.076   46.972  1.00 56.89  ?  5   VAL B C   1 
ATOM 1666 O O   . VAL B 2 5   ? 31.433  0.370   48.141  1.00 59.44  ?  5   VAL B O   1 
ATOM 1667 C CB  . VAL B 2 5   ? 32.381  -2.104  46.697  1.00 52.12  ?  5   VAL B CB  1 
ATOM 1668 C CG1 . VAL B 2 5   ? 31.135  -2.951  46.504  1.00 51.75  ?  5   VAL B CG1 1 
ATOM 1669 C CG2 . VAL B 2 5   ? 33.597  -2.748  46.052  1.00 53.98  ?  5   VAL B CG2 1 
ATOM 1670 N N   . GLU B 2 6   ? 30.013  0.394   46.395  1.00 61.04  ?  6   GLU B N   1 
ATOM 1671 C CA  . GLU B 2 6   ? 29.000  1.197   47.062  1.00 53.51  ?  6   GLU B CA  1 
ATOM 1672 C C   . GLU B 2 6   ? 27.877  0.314   47.588  1.00 53.11  ?  6   GLU B C   1 
ATOM 1673 O O   . GLU B 2 6   ? 27.441  -0.630  46.920  1.00 56.66  ?  6   GLU B O   1 
ATOM 1674 C CB  . GLU B 2 6   ? 28.431  2.232   46.099  1.00 50.80  ?  6   GLU B CB  1 
ATOM 1675 C CG  . GLU B 2 6   ? 29.475  3.153   45.533  1.00 54.91  ?  6   GLU B CG  1 
ATOM 1676 C CD  . GLU B 2 6   ? 28.875  4.118   44.558  1.00 60.22  ?  6   GLU B CD  1 
ATOM 1677 O OE1 . GLU B 2 6   ? 27.700  4.489   44.761  1.00 60.03  ?  6   GLU B OE1 1 
ATOM 1678 O OE2 . GLU B 2 6   ? 29.555  4.461   43.566  1.00 59.82  ?  6   GLU B OE2 1 
ATOM 1679 N N   . SER B 2 7   ? 27.421  0.627   48.793  1.00 54.61  ?  7   SER B N   1 
ATOM 1680 C CA  . SER B 2 7   ? 26.299  -0.045  49.423  1.00 55.13  ?  7   SER B CA  1 
ATOM 1681 C C   . SER B 2 7   ? 25.369  1.003   50.025  1.00 61.11  ?  7   SER B C   1 
ATOM 1682 O O   . SER B 2 7   ? 25.724  2.180   50.184  1.00 53.04  ?  7   SER B O   1 
ATOM 1683 C CB  . SER B 2 7   ? 26.766  -1.051  50.487  1.00 53.14  ?  7   SER B CB  1 
ATOM 1684 O OG  . SER B 2 7   ? 27.642  -0.442  51.417  1.00 58.94  ?  7   SER B OG  1 
ATOM 1685 N N   . GLY B 2 8   ? 24.168  0.552   50.371  1.00 59.74  ?  8   GLY B N   1 
ATOM 1686 C CA  . GLY B 2 8   ? 23.098  1.431   50.778  1.00 43.02  ?  8   GLY B CA  1 
ATOM 1687 C C   . GLY B 2 8   ? 22.265  1.867   49.591  1.00 56.28  ?  8   GLY B C   1 
ATOM 1688 O O   . GLY B 2 8   ? 22.633  1.702   48.424  1.00 59.38  ?  8   GLY B O   1 
ATOM 1689 N N   . GLY B 2 9   ? 21.112  2.440   49.898  1.00 55.40  ?  9   GLY B N   1 
ATOM 1690 C CA  . GLY B 2 9   ? 20.245  2.910   48.840  1.00 52.04  ?  9   GLY B CA  1 
ATOM 1691 C C   . GLY B 2 9   ? 19.105  1.965   48.532  1.00 49.65  ?  9   GLY B C   1 
ATOM 1692 O O   . GLY B 2 9   ? 19.250  0.740   48.579  1.00 43.20  ?  9   GLY B O   1 
ATOM 1693 N N   . GLY B 2 10  ? 17.955  2.548   48.222  1.00 48.41  ?  10  GLY B N   1 
ATOM 1694 C CA  . GLY B 2 10  ? 16.745  1.807   47.957  1.00 44.56  ?  10  GLY B CA  1 
ATOM 1695 C C   . GLY B 2 10  ? 15.571  2.756   48.032  1.00 53.46  ?  10  GLY B C   1 
ATOM 1696 O O   . GLY B 2 10  ? 15.693  3.927   47.658  1.00 57.59  ?  10  GLY B O   1 
ATOM 1697 N N   . LEU B 2 11  ? 14.455  2.294   48.581  1.00 55.61  ?  11  LEU B N   1 
ATOM 1698 C CA  . LEU B 2 11  ? 13.257  3.111   48.694  1.00 60.49  ?  11  LEU B CA  1 
ATOM 1699 C C   . LEU B 2 11  ? 13.318  3.930   49.980  1.00 64.44  ?  11  LEU B C   1 
ATOM 1700 O O   . LEU B 2 11  ? 13.637  3.398   51.048  1.00 65.37  ?  11  LEU B O   1 
ATOM 1701 C CB  . LEU B 2 11  ? 12.009  2.226   48.675  1.00 60.39  ?  11  LEU B CB  1 
ATOM 1702 C CG  . LEU B 2 11  ? 10.647  2.920   48.650  1.00 64.15  ?  11  LEU B CG  1 
ATOM 1703 C CD1 . LEU B 2 11  ? 10.550  3.882   47.480  1.00 61.57  ?  11  LEU B CD1 1 
ATOM 1704 C CD2 . LEU B 2 11  ? 9.534   1.891   48.596  1.00 63.00  ?  11  LEU B CD2 1 
ATOM 1705 N N   . VAL B 2 12  ? 13.022  5.224   49.870  1.00 66.97  ?  12  VAL B N   1 
ATOM 1706 C CA  . VAL B 2 12  ? 13.002  6.139   51.008  1.00 67.54  ?  12  VAL B CA  1 
ATOM 1707 C C   . VAL B 2 12  ? 11.804  7.066   50.859  1.00 72.75  ?  12  VAL B C   1 
ATOM 1708 O O   . VAL B 2 12  ? 11.554  7.605   49.775  1.00 68.37  ?  12  VAL B O   1 
ATOM 1709 C CB  . VAL B 2 12  ? 14.306  6.957   51.111  1.00 67.37  ?  12  VAL B CB  1 
ATOM 1710 C CG1 . VAL B 2 12  ? 14.191  8.011   52.201  1.00 65.17  ?  12  VAL B CG1 1 
ATOM 1711 C CG2 . VAL B 2 12  ? 15.488  6.046   51.385  1.00 73.64  ?  12  VAL B CG2 1 
ATOM 1712 N N   . GLN B 2 13  ? 11.073  7.269   51.956  1.00 72.20  ?  13  GLN B N   1 
ATOM 1713 C CA  . GLN B 2 13  ? 9.915   8.144   51.887  1.00 72.08  ?  13  GLN B CA  1 
ATOM 1714 C C   . GLN B 2 13  ? 10.343  9.610   51.861  1.00 69.66  ?  13  GLN B C   1 
ATOM 1715 O O   . GLN B 2 13  ? 11.390  9.965   52.410  1.00 70.00  ?  13  GLN B O   1 
ATOM 1716 C CB  . GLN B 2 13  ? 8.999   7.894   53.077  1.00 72.21  ?  13  GLN B CB  1 
ATOM 1717 C CG  . GLN B 2 13  ? 8.319   6.542   53.030  1.00 81.30  ?  13  GLN B CG  1 
ATOM 1718 C CD  . GLN B 2 13  ? 7.485   6.266   54.261  1.00 90.42  ?  13  GLN B CD  1 
ATOM 1719 O OE1 . GLN B 2 13  ? 7.142   7.179   55.014  1.00 91.88  ?  13  GLN B OE1 1 
ATOM 1720 N NE2 . GLN B 2 13  ? 7.148   4.998   54.473  1.00 95.32  ?  13  GLN B NE2 1 
ATOM 1721 N N   . PRO B 2 14  ? 9.553   10.474  51.216  1.00 71.97  ?  14  PRO B N   1 
ATOM 1722 C CA  . PRO B 2 14  ? 9.903   11.899  51.168  1.00 71.72  ?  14  PRO B CA  1 
ATOM 1723 C C   . PRO B 2 14  ? 10.046  12.480  52.566  1.00 74.12  ?  14  PRO B C   1 
ATOM 1724 O O   . PRO B 2 14  ? 9.255   12.192  53.467  1.00 72.21  ?  14  PRO B O   1 
ATOM 1725 C CB  . PRO B 2 14  ? 8.731   12.527  50.408  1.00 68.61  ?  14  PRO B CB  1 
ATOM 1726 C CG  . PRO B 2 14  ? 8.193   11.420  49.572  1.00 61.26  ?  14  PRO B CG  1 
ATOM 1727 C CD  . PRO B 2 14  ? 8.365   10.174  50.397  1.00 71.49  ?  14  PRO B CD  1 
ATOM 1728 N N   . GLY B 2 15  ? 11.078  13.302  52.738  1.00 72.62  ?  15  GLY B N   1 
ATOM 1729 C CA  . GLY B 2 15  ? 11.457  13.791  54.043  1.00 72.53  ?  15  GLY B CA  1 
ATOM 1730 C C   . GLY B 2 15  ? 12.269  12.822  54.871  1.00 71.32  ?  15  GLY B C   1 
ATOM 1731 O O   . GLY B 2 15  ? 12.842  13.236  55.887  1.00 73.09  ?  15  GLY B O   1 
ATOM 1732 N N   . GLY B 2 16  ? 12.352  11.546  54.464  1.00 69.48  ?  16  GLY B N   1 
ATOM 1733 C CA  . GLY B 2 16  ? 13.131  10.566  55.190  1.00 70.07  ?  16  GLY B CA  1 
ATOM 1734 C C   . GLY B 2 16  ? 14.620  10.675  54.916  1.00 69.51  ?  16  GLY B C   1 
ATOM 1735 O O   . GLY B 2 16  ? 15.077  11.442  54.070  1.00 68.98  ?  16  GLY B O   1 
ATOM 1736 N N   . SER B 2 17  ? 15.388  9.871   55.645  1.00 69.34  ?  17  SER B N   1 
ATOM 1737 C CA  . SER B 2 17  ? 16.839  9.898   55.565  1.00 67.58  ?  17  SER B CA  1 
ATOM 1738 C C   . SER B 2 17  ? 17.377  8.569   55.050  1.00 68.16  ?  17  SER B C   1 
ATOM 1739 O O   . SER B 2 17  ? 16.680  7.551   55.030  1.00 71.89  ?  17  SER B O   1 
ATOM 1740 C CB  . SER B 2 17  ? 17.465  10.221  56.927  1.00 71.87  ?  17  SER B CB  1 
ATOM 1741 O OG  . SER B 2 17  ? 17.061  11.504  57.378  1.00 76.39  ?  17  SER B OG  1 
ATOM 1742 N N   . LEU B 2 18  ? 18.635  8.603   54.619  1.00 61.23  ?  18  LEU B N   1 
ATOM 1743 C CA  . LEU B 2 18  ? 19.325  7.428   54.109  1.00 58.56  ?  18  LEU B CA  1 
ATOM 1744 C C   . LEU B 2 18  ? 20.821  7.677   54.223  1.00 59.47  ?  18  LEU B C   1 
ATOM 1745 O O   . LEU B 2 18  ? 21.271  8.823   54.302  1.00 59.49  ?  18  LEU B O   1 
ATOM 1746 C CB  . LEU B 2 18  ? 18.923  7.134   52.662  1.00 64.72  ?  18  LEU B CB  1 
ATOM 1747 C CG  . LEU B 2 18  ? 19.418  5.846   52.003  1.00 69.76  ?  18  LEU B CG  1 
ATOM 1748 C CD1 . LEU B 2 18  ? 18.962  4.608   52.772  1.00 64.63  ?  18  LEU B CD1 1 
ATOM 1749 C CD2 . LEU B 2 18  ? 18.971  5.795   50.550  1.00 66.83  ?  18  LEU B CD2 1 
ATOM 1750 N N   . ARG B 2 19  ? 21.592  6.593   54.243  1.00 61.28  ?  19  ARG B N   1 
ATOM 1751 C CA  . ARG B 2 19  ? 23.045  6.699   54.313  1.00 60.88  ?  19  ARG B CA  1 
ATOM 1752 C C   . ARG B 2 19  ? 23.662  5.739   53.308  1.00 64.72  ?  19  ARG B C   1 
ATOM 1753 O O   . ARG B 2 19  ? 23.378  4.537   53.336  1.00 63.48  ?  19  ARG B O   1 
ATOM 1754 C CB  . ARG B 2 19  ? 23.562  6.413   55.727  1.00 56.20  ?  19  ARG B CB  1 
ATOM 1755 C CG  . ARG B 2 19  ? 24.971  6.931   55.962  1.00 60.93  ?  19  ARG B CG  1 
ATOM 1756 C CD  . ARG B 2 19  ? 25.482  6.616   57.361  1.00 64.50  ?  19  ARG B CD  1 
ATOM 1757 N NE  . ARG B 2 19  ? 25.849  5.215   57.539  1.00 70.83  ?  19  ARG B NE  1 
ATOM 1758 C CZ  . ARG B 2 19  ? 26.270  4.703   58.691  1.00 76.17  ?  19  ARG B CZ  1 
ATOM 1759 N NH1 . ARG B 2 19  ? 26.586  3.417   58.781  1.00 74.81  ?  19  ARG B NH1 1 
ATOM 1760 N NH2 . ARG B 2 19  ? 26.381  5.484   59.757  1.00 82.19  ?  19  ARG B NH2 1 
ATOM 1761 N N   . LEU B 2 20  ? 24.480  6.279   52.409  1.00 58.14  ?  20  LEU B N   1 
ATOM 1762 C CA  . LEU B 2 20  ? 25.230  5.499   51.440  1.00 55.26  ?  20  LEU B CA  1 
ATOM 1763 C C   . LEU B 2 20  ? 26.681  5.372   51.884  1.00 55.21  ?  20  LEU B C   1 
ATOM 1764 O O   . LEU B 2 20  ? 27.247  6.293   52.478  1.00 57.44  ?  20  LEU B O   1 
ATOM 1765 C CB  . LEU B 2 20  ? 25.173  6.152   50.059  1.00 57.69  ?  20  LEU B CB  1 
ATOM 1766 C CG  . LEU B 2 20  ? 23.776  6.517   49.564  1.00 58.21  ?  20  LEU B CG  1 
ATOM 1767 C CD1 . LEU B 2 20  ? 23.847  7.175   48.195  1.00 52.42  ?  20  LEU B CD1 1 
ATOM 1768 C CD2 . LEU B 2 20  ? 22.886  5.290   49.541  1.00 59.54  ?  20  LEU B CD2 1 
ATOM 1769 N N   . SER B 2 21  ? 27.284  4.222   51.589  1.00 56.61  ?  21  SER B N   1 
ATOM 1770 C CA  . SER B 2 21  ? 28.679  3.979   51.924  1.00 54.33  ?  21  SER B CA  1 
ATOM 1771 C C   . SER B 2 21  ? 29.428  3.490   50.690  1.00 57.75  ?  21  SER B C   1 
ATOM 1772 O O   . SER B 2 21  ? 28.843  2.925   49.765  1.00 50.91  ?  21  SER B O   1 
ATOM 1773 C CB  . SER B 2 21  ? 28.817  2.978   53.085  1.00 56.24  ?  21  SER B CB  1 
ATOM 1774 O OG  . SER B 2 21  ? 28.108  1.775   52.836  1.00 61.44  ?  21  SER B OG  1 
ATOM 1775 N N   . CYS B 2 22  ? 30.744  3.708   50.709  1.00 60.22  ?  22  CYS B N   1 
ATOM 1776 C CA  . CYS B 2 22  ? 31.644  3.434   49.588  1.00 51.03  ?  22  CYS B CA  1 
ATOM 1777 C C   . CYS B 2 22  ? 32.950  2.895   50.160  1.00 61.01  ?  22  CYS B C   1 
ATOM 1778 O O   . CYS B 2 22  ? 33.771  3.666   50.661  1.00 65.44  ?  22  CYS B O   1 
ATOM 1779 C CB  . CYS B 2 22  ? 31.894  4.697   48.773  1.00 54.09  ?  22  CYS B CB  1 
ATOM 1780 S SG  . CYS B 2 22  ? 33.133  4.516   47.463  1.00 75.87  ?  22  CYS B SG  1 
ATOM 1781 N N   . ALA B 2 23  ? 33.150  1.584   50.072  1.00 66.43  ?  23  ALA B N   1 
ATOM 1782 C CA  . ALA B 2 23  ? 34.361  0.952   50.577  1.00 66.44  ?  23  ALA B CA  1 
ATOM 1783 C C   . ALA B 2 23  ? 35.414  0.914   49.478  1.00 58.81  ?  23  ALA B C   1 
ATOM 1784 O O   . ALA B 2 23  ? 35.118  0.532   48.343  1.00 60.52  ?  23  ALA B O   1 
ATOM 1785 C CB  . ALA B 2 23  ? 34.066  -0.462  51.079  1.00 62.73  ?  23  ALA B CB  1 
ATOM 1786 N N   . ALA B 2 24  ? 36.630  1.334   49.811  1.00 60.02  ?  24  ALA B N   1 
ATOM 1787 C CA  . ALA B 2 24  ? 37.740  1.326   48.872  1.00 64.51  ?  24  ALA B CA  1 
ATOM 1788 C C   . ALA B 2 24  ? 38.601  0.086   49.083  1.00 74.06  ?  24  ALA B C   1 
ATOM 1789 O O   . ALA B 2 24  ? 38.773  -0.393  50.208  1.00 66.68  ?  24  ALA B O   1 
ATOM 1790 C CB  . ALA B 2 24  ? 38.594  2.585   49.020  1.00 61.37  ?  24  ALA B CB  1 
ATOM 1791 N N   . SER B 2 25  ? 39.151  -0.423  47.982  1.00 74.67  ?  25  SER B N   1 
ATOM 1792 C CA  . SER B 2 25  ? 40.013  -1.599  48.010  1.00 66.89  ?  25  SER B CA  1 
ATOM 1793 C C   . SER B 2 25  ? 41.198  -1.355  47.090  1.00 75.81  ?  25  SER B C   1 
ATOM 1794 O O   . SER B 2 25  ? 41.015  -1.035  45.910  1.00 82.14  ?  25  SER B O   1 
ATOM 1795 C CB  . SER B 2 25  ? 39.241  -2.849  47.581  1.00 67.47  ?  25  SER B CB  1 
ATOM 1796 O OG  . SER B 2 25  ? 38.031  -2.965  48.309  1.00 73.15  ?  25  SER B OG  1 
ATOM 1797 N N   . GLY B 2 26  ? 42.408  -1.483  47.634  1.00 69.13  ?  26  GLY B N   1 
ATOM 1798 C CA  . GLY B 2 26  ? 43.632  -1.298  46.880  1.00 71.22  ?  26  GLY B CA  1 
ATOM 1799 C C   . GLY B 2 26  ? 44.357  -0.001  47.166  1.00 73.18  ?  26  GLY B C   1 
ATOM 1800 O O   . GLY B 2 26  ? 45.508  0.154   46.737  1.00 75.31  ?  26  GLY B O   1 
ATOM 1801 N N   . PHE B 2 27  ? 43.728  0.928   47.880  1.00 68.30  ?  27  PHE B N   1 
ATOM 1802 C CA  . PHE B 2 27  ? 44.350  2.198   48.225  1.00 68.58  ?  27  PHE B CA  1 
ATOM 1803 C C   . PHE B 2 27  ? 43.603  2.774   49.417  1.00 72.63  ?  27  PHE B C   1 
ATOM 1804 O O   . PHE B 2 27  ? 42.564  2.253   49.832  1.00 77.58  ?  27  PHE B O   1 
ATOM 1805 C CB  . PHE B 2 27  ? 44.333  3.183   47.047  1.00 77.02  ?  27  PHE B CB  1 
ATOM 1806 C CG  . PHE B 2 27  ? 42.975  3.781   46.768  1.00 76.07  ?  27  PHE B CG  1 
ATOM 1807 C CD1 . PHE B 2 27  ? 42.001  3.055   46.102  1.00 74.14  ?  27  PHE B CD1 1 
ATOM 1808 C CD2 . PHE B 2 27  ? 42.674  5.072   47.180  1.00 72.86  ?  27  PHE B CD2 1 
ATOM 1809 C CE1 . PHE B 2 27  ? 40.757  3.608   45.853  1.00 75.04  ?  27  PHE B CE1 1 
ATOM 1810 C CE2 . PHE B 2 27  ? 41.430  5.627   46.933  1.00 68.77  ?  27  PHE B CE2 1 
ATOM 1811 C CZ  . PHE B 2 27  ? 40.472  4.897   46.269  1.00 66.12  ?  27  PHE B CZ  1 
ATOM 1812 N N   . SER B 2 28  ? 44.152  3.848   49.976  1.00 68.89  ?  28  SER B N   1 
ATOM 1813 C CA  . SER B 2 28  ? 43.535  4.538   51.101  1.00 67.54  ?  28  SER B CA  1 
ATOM 1814 C C   . SER B 2 28  ? 42.914  5.838   50.600  1.00 69.35  ?  28  SER B C   1 
ATOM 1815 O O   . SER B 2 28  ? 43.633  6.748   50.165  1.00 61.40  ?  28  SER B O   1 
ATOM 1816 C CB  . SER B 2 28  ? 44.556  4.806   52.208  1.00 70.03  ?  28  SER B CB  1 
ATOM 1817 O OG  . SER B 2 28  ? 45.680  5.510   51.711  1.00 78.79  ?  28  SER B OG  1 
ATOM 1818 N N   . LEU B 2 29  ? 41.585  5.938   50.705  1.00 69.74  ?  29  LEU B N   1 
ATOM 1819 C CA  . LEU B 2 29  ? 40.876  7.142   50.280  1.00 67.78  ?  29  LEU B CA  1 
ATOM 1820 C C   . LEU B 2 29  ? 41.292  8.372   51.073  1.00 64.44  ?  29  LEU B C   1 
ATOM 1821 O O   . LEU B 2 29  ? 40.973  9.493   50.665  1.00 63.29  ?  29  LEU B O   1 
ATOM 1822 C CB  . LEU B 2 29  ? 39.360  6.926   50.369  1.00 63.31  ?  29  LEU B CB  1 
ATOM 1823 C CG  . LEU B 2 29  ? 38.755  6.282   51.617  1.00 64.79  ?  29  LEU B CG  1 
ATOM 1824 C CD1 . LEU B 2 29  ? 38.536  7.313   52.715  1.00 66.95  ?  29  LEU B CD1 1 
ATOM 1825 C CD2 . LEU B 2 29  ? 37.456  5.579   51.267  1.00 61.47  ?  29  LEU B CD2 1 
ATOM 1826 N N   . SER B 2 30  ? 41.998  8.190   52.188  1.00 69.20  ?  30  SER B N   1 
ATOM 1827 C CA  . SER B 2 30  ? 42.478  9.314   52.977  1.00 71.71  ?  30  SER B CA  1 
ATOM 1828 C C   . SER B 2 30  ? 43.574  10.101  52.267  1.00 70.93  ?  30  SER B C   1 
ATOM 1829 O O   . SER B 2 30  ? 43.984  11.151  52.773  1.00 69.62  ?  30  SER B O   1 
ATOM 1830 C CB  . SER B 2 30  ? 42.985  8.805   54.325  1.00 67.82  ?  30  SER B CB  1 
ATOM 1831 O OG  . SER B 2 30  ? 42.033  7.935   54.918  1.00 74.88  ?  30  SER B OG  1 
ATOM 1832 N N   . SER B 2 31  ? 44.051  9.622   51.117  1.00 64.67  ?  31  SER B N   1 
ATOM 1833 C CA  . SER B 2 31  ? 45.109  10.277  50.359  1.00 63.33  ?  31  SER B CA  1 
ATOM 1834 C C   . SER B 2 31  ? 44.580  10.960  49.105  1.00 63.78  ?  31  SER B C   1 
ATOM 1835 O O   . SER B 2 31  ? 45.373  11.467  48.304  1.00 63.59  ?  31  SER B O   1 
ATOM 1836 C CB  . SER B 2 31  ? 46.189  9.266   49.971  1.00 63.30  ?  31  SER B CB  1 
ATOM 1837 O OG  . SER B 2 31  ? 46.451  8.364   51.026  1.00 69.80  ?  31  SER B OG  1 
ATOM 1838 N N   . TYR B 2 32  ? 43.265  10.984  48.912  1.00 60.55  ?  32  TYR B N   1 
ATOM 1839 C CA  . TYR B 2 32  ? 42.677  11.548  47.709  1.00 63.31  ?  32  TYR B CA  1 
ATOM 1840 C C   . TYR B 2 32  ? 41.447  12.364  48.074  1.00 63.04  ?  32  TYR B C   1 
ATOM 1841 O O   . TYR B 2 32  ? 40.816  12.152  49.112  1.00 65.47  ?  32  TYR B O   1 
ATOM 1842 C CB  . TYR B 2 32  ? 42.280  10.452  46.700  1.00 63.51  ?  32  TYR B CB  1 
ATOM 1843 C CG  . TYR B 2 32  ? 43.434  9.666   46.103  1.00 67.86  ?  32  TYR B CG  1 
ATOM 1844 C CD1 . TYR B 2 32  ? 43.944  9.989   44.845  1.00 67.45  ?  32  TYR B CD1 1 
ATOM 1845 C CD2 . TYR B 2 32  ? 44.002  8.593   46.787  1.00 60.36  ?  32  TYR B CD2 1 
ATOM 1846 C CE1 . TYR B 2 32  ? 44.991  9.269   44.288  1.00 69.71  ?  32  TYR B CE1 1 
ATOM 1847 C CE2 . TYR B 2 32  ? 45.051  7.869   46.242  1.00 63.89  ?  32  TYR B CE2 1 
ATOM 1848 C CZ  . TYR B 2 32  ? 45.541  8.210   44.991  1.00 70.86  ?  32  TYR B CZ  1 
ATOM 1849 O OH  . TYR B 2 32  ? 46.585  7.494   44.443  1.00 58.98  ?  32  TYR B OH  1 
ATOM 1850 N N   . TYR B 2 33  ? 41.123  13.318  47.204  1.00 63.22  ?  33  TYR B N   1 
ATOM 1851 C CA  . TYR B 2 33  ? 39.796  13.911  47.209  1.00 54.79  ?  33  TYR B CA  1 
ATOM 1852 C C   . TYR B 2 33  ? 38.780  12.839  46.842  1.00 58.56  ?  33  TYR B C   1 
ATOM 1853 O O   . TYR B 2 33  ? 39.044  11.975  46.000  1.00 60.17  ?  33  TYR B O   1 
ATOM 1854 C CB  . TYR B 2 33  ? 39.723  15.051  46.198  1.00 58.27  ?  33  TYR B CB  1 
ATOM 1855 C CG  . TYR B 2 33  ? 40.450  16.317  46.579  1.00 68.22  ?  33  TYR B CG  1 
ATOM 1856 C CD1 . TYR B 2 33  ? 39.780  17.539  46.601  1.00 68.39  ?  33  TYR B CD1 1 
ATOM 1857 C CD2 . TYR B 2 33  ? 41.809  16.306  46.877  1.00 65.78  ?  33  TYR B CD2 1 
ATOM 1858 C CE1 . TYR B 2 33  ? 40.433  18.709  46.926  1.00 64.24  ?  33  TYR B CE1 1 
ATOM 1859 C CE2 . TYR B 2 33  ? 42.472  17.471  47.209  1.00 70.42  ?  33  TYR B CE2 1 
ATOM 1860 C CZ  . TYR B 2 33  ? 41.778  18.672  47.231  1.00 73.14  ?  33  TYR B CZ  1 
ATOM 1861 O OH  . TYR B 2 33  ? 42.425  19.844  47.558  1.00 73.04  ?  33  TYR B OH  1 
ATOM 1862 N N   . MET B 2 34  ? 37.615  12.882  47.472  1.00 53.08  ?  34  MET B N   1 
ATOM 1863 C CA  . MET B 2 34  ? 36.566  11.926  47.149  1.00 51.15  ?  34  MET B CA  1 
ATOM 1864 C C   . MET B 2 34  ? 35.305  12.696  46.797  1.00 52.28  ?  34  MET B C   1 
ATOM 1865 O O   . MET B 2 34  ? 35.145  13.855  47.178  1.00 54.56  ?  34  MET B O   1 
ATOM 1866 C CB  . MET B 2 34  ? 36.322  10.934  48.295  1.00 46.17  ?  34  MET B CB  1 
ATOM 1867 C CG  . MET B 2 34  ? 37.496  9.972   48.529  1.00 52.22  ?  34  MET B CG  1 
ATOM 1868 S SD  . MET B 2 34  ? 38.068  9.069   47.060  1.00 56.97  ?  34  MET B SD  1 
ATOM 1869 C CE  . MET B 2 34  ? 36.693  7.957   46.768  1.00 45.75  ?  34  MET B CE  1 
ATOM 1870 N N   . THR B 2 35  ? 34.422  12.059  46.033  1.00 50.37  ?  35  THR B N   1 
ATOM 1871 C CA  . THR B 2 35  ? 33.282  12.774  45.485  1.00 45.39  ?  35  THR B CA  1 
ATOM 1872 C C   . THR B 2 35  ? 32.077  11.851  45.402  1.00 47.56  ?  35  THR B C   1 
ATOM 1873 O O   . THR B 2 35  ? 32.210  10.643  45.184  1.00 56.94  ?  35  THR B O   1 
ATOM 1874 C CB  . THR B 2 35  ? 33.623  13.330  44.095  1.00 52.18  ?  35  THR B CB  1 
ATOM 1875 O OG1 . THR B 2 35  ? 34.760  14.196  44.192  1.00 57.42  ?  35  THR B OG1 1 
ATOM 1876 C CG2 . THR B 2 35  ? 32.460  14.102  43.499  1.00 57.66  ?  35  THR B CG2 1 
ATOM 1877 N N   . TRP B 2 36  ? 30.901  12.435  45.602  1.00 41.98  ?  36  TRP B N   1 
ATOM 1878 C CA  . TRP B 2 36  ? 29.630  11.803  45.284  1.00 44.75  ?  36  TRP B CA  1 
ATOM 1879 C C   . TRP B 2 36  ? 29.007  12.546  44.108  1.00 54.31  ?  36  TRP B C   1 
ATOM 1880 O O   . TRP B 2 36  ? 28.917  13.785  44.135  1.00 51.16  ?  36  TRP B O   1 
ATOM 1881 C CB  . TRP B 2 36  ? 28.684  11.820  46.483  1.00 47.59  ?  36  TRP B CB  1 
ATOM 1882 C CG  . TRP B 2 36  ? 29.062  10.872  47.577  1.00 49.02  ?  36  TRP B CG  1 
ATOM 1883 C CD1 . TRP B 2 36  ? 29.785  11.162  48.695  1.00 47.61  ?  36  TRP B CD1 1 
ATOM 1884 C CD2 . TRP B 2 36  ? 28.711  9.488   47.673  1.00 50.57  ?  36  TRP B CD2 1 
ATOM 1885 N NE1 . TRP B 2 36  ? 29.920  10.043  49.473  1.00 49.15  ?  36  TRP B NE1 1 
ATOM 1886 C CE2 . TRP B 2 36  ? 29.269  9.000   48.869  1.00 51.25  ?  36  TRP B CE2 1 
ATOM 1887 C CE3 . TRP B 2 36  ? 27.986  8.611   46.861  1.00 47.67  ?  36  TRP B CE3 1 
ATOM 1888 C CZ2 . TRP B 2 36  ? 29.125  7.676   49.274  1.00 52.12  ?  36  TRP B CZ2 1 
ATOM 1889 C CZ3 . TRP B 2 36  ? 27.844  7.298   47.265  1.00 49.35  ?  36  TRP B CZ3 1 
ATOM 1890 C CH2 . TRP B 2 36  ? 28.410  6.842   48.459  1.00 50.96  ?  36  TRP B CH2 1 
ATOM 1891 N N   . VAL B 2 37  ? 28.571  11.788  43.092  1.00 51.23  ?  37  VAL B N   1 
ATOM 1892 C CA  . VAL B 2 37  ? 27.982  12.325  41.865  1.00 46.57  ?  37  VAL B CA  1 
ATOM 1893 C C   . VAL B 2 37  ? 26.717  11.540  41.548  1.00 46.93  ?  37  VAL B C   1 
ATOM 1894 O O   . VAL B 2 37  ? 26.746  10.309  41.512  1.00 48.55  ?  37  VAL B O   1 
ATOM 1895 C CB  . VAL B 2 37  ? 28.956  12.242  40.674  1.00 39.58  ?  37  VAL B CB  1 
ATOM 1896 C CG1 . VAL B 2 37  ? 28.214  12.477  39.374  1.00 44.67  ?  37  VAL B CG1 1 
ATOM 1897 C CG2 . VAL B 2 37  ? 30.089  13.234  40.831  1.00 46.66  ?  37  VAL B CG2 1 
ATOM 1898 N N   . ARG B 2 38  ? 25.612  12.239  41.309  1.00 49.36  ?  38  ARG B N   1 
ATOM 1899 C CA  . ARG B 2 38  ? 24.351  11.560  41.048  1.00 49.52  ?  38  ARG B CA  1 
ATOM 1900 C C   . ARG B 2 38  ? 23.944  11.684  39.585  1.00 50.50  ?  38  ARG B C   1 
ATOM 1901 O O   . ARG B 2 38  ? 24.475  12.503  38.828  1.00 52.76  ?  38  ARG B O   1 
ATOM 1902 C CB  . ARG B 2 38  ? 23.226  12.097  41.940  1.00 51.21  ?  38  ARG B CB  1 
ATOM 1903 C CG  . ARG B 2 38  ? 22.651  13.443  41.540  1.00 51.53  ?  38  ARG B CG  1 
ATOM 1904 C CD  . ARG B 2 38  ? 21.562  13.838  42.528  1.00 58.37  ?  38  ARG B CD  1 
ATOM 1905 N NE  . ARG B 2 38  ? 20.921  15.109  42.202  1.00 67.98  ?  38  ARG B NE  1 
ATOM 1906 C CZ  . ARG B 2 38  ? 19.947  15.655  42.924  1.00 67.73  ?  38  ARG B CZ  1 
ATOM 1907 N NH1 . ARG B 2 38  ? 19.414  16.814  42.562  1.00 70.14  ?  38  ARG B NH1 1 
ATOM 1908 N NH2 . ARG B 2 38  ? 19.504  15.036  44.011  1.00 65.50  ?  38  ARG B NH2 1 
ATOM 1909 N N   . GLN B 2 39  ? 22.990  10.838  39.202  1.00 46.43  ?  39  GLN B N   1 
ATOM 1910 C CA  . GLN B 2 39  ? 22.417  10.852  37.861  1.00 49.34  ?  39  GLN B CA  1 
ATOM 1911 C C   . GLN B 2 39  ? 20.964  10.422  37.966  1.00 50.04  ?  39  GLN B C   1 
ATOM 1912 O O   . GLN B 2 39  ? 20.692  9.276   38.333  1.00 50.79  ?  39  GLN B O   1 
ATOM 1913 C CB  . GLN B 2 39  ? 23.191  9.921   36.923  1.00 50.85  ?  39  GLN B CB  1 
ATOM 1914 C CG  . GLN B 2 39  ? 22.596  9.819   35.522  1.00 58.42  ?  39  GLN B CG  1 
ATOM 1915 C CD  . GLN B 2 39  ? 23.428  8.958   34.572  1.00 55.87  ?  39  GLN B CD  1 
ATOM 1916 O OE1 . GLN B 2 39  ? 24.039  7.970   34.977  1.00 52.80  ?  39  GLN B OE1 1 
ATOM 1917 N NE2 . GLN B 2 39  ? 23.454  9.343   33.298  1.00 54.82  ?  39  GLN B NE2 1 
ATOM 1918 N N   . ALA B 2 40  ? 20.037  11.328  37.659  1.00 45.69  ?  40  ALA B N   1 
ATOM 1919 C CA  . ALA B 2 40  ? 18.627  10.972  37.683  1.00 44.08  ?  40  ALA B CA  1 
ATOM 1920 C C   . ALA B 2 40  ? 18.317  10.078  36.482  1.00 56.08  ?  40  ALA B C   1 
ATOM 1921 O O   . ALA B 2 40  ? 19.066  10.069  35.501  1.00 58.17  ?  40  ALA B O   1 
ATOM 1922 C CB  . ALA B 2 40  ? 17.762  12.228  37.678  1.00 43.10  ?  40  ALA B CB  1 
ATOM 1923 N N   . PRO B 2 41  ? 17.226  9.309   36.537  1.00 59.06  ?  41  PRO B N   1 
ATOM 1924 C CA  . PRO B 2 41  ? 16.923  8.377   35.436  1.00 57.14  ?  41  PRO B CA  1 
ATOM 1925 C C   . PRO B 2 41  ? 16.792  9.082   34.091  1.00 62.33  ?  41  PRO B C   1 
ATOM 1926 O O   . PRO B 2 41  ? 16.028  10.039  33.941  1.00 60.68  ?  41  PRO B O   1 
ATOM 1927 C CB  . PRO B 2 41  ? 15.594  7.744   35.863  1.00 50.72  ?  41  PRO B CB  1 
ATOM 1928 C CG  . PRO B 2 41  ? 15.578  7.863   37.344  1.00 62.80  ?  41  PRO B CG  1 
ATOM 1929 C CD  . PRO B 2 41  ? 16.273  9.166   37.653  1.00 55.18  ?  41  PRO B CD  1 
ATOM 1930 N N   . GLY B 2 42  ? 17.548  8.590   33.110  1.00 67.90  ?  42  GLY B N   1 
ATOM 1931 C CA  . GLY B 2 42  ? 17.517  9.137   31.762  1.00 60.80  ?  42  GLY B CA  1 
ATOM 1932 C C   . GLY B 2 42  ? 18.017  10.559  31.641  1.00 64.96  ?  42  GLY B C   1 
ATOM 1933 O O   . GLY B 2 42  ? 17.621  11.267  30.710  1.00 69.33  ?  42  GLY B O   1 
ATOM 1934 N N   . LYS B 2 43  ? 18.885  11.002  32.556  1.00 64.87  ?  43  LYS B N   1 
ATOM 1935 C CA  . LYS B 2 43  ? 19.405  12.366  32.509  1.00 61.17  ?  43  LYS B CA  1 
ATOM 1936 C C   . LYS B 2 43  ? 20.924  12.376  32.668  1.00 58.56  ?  43  LYS B C   1 
ATOM 1937 O O   . LYS B 2 43  ? 21.565  11.318  32.651  1.00 56.00  ?  43  LYS B O   1 
ATOM 1938 C CB  . LYS B 2 43  ? 18.730  13.252  33.566  1.00 55.61  ?  43  LYS B CB  1 
ATOM 1939 C CG  . LYS B 2 43  ? 17.215  13.362  33.376  1.00 55.18  ?  43  LYS B CG  1 
ATOM 1940 C CD  . LYS B 2 43  ? 16.592  14.566  34.067  1.00 62.04  ?  43  LYS B CD  1 
ATOM 1941 C CE  . LYS B 2 43  ? 16.984  15.862  33.345  1.00 77.18  ?  43  LYS B CE  1 
ATOM 1942 N NZ  . LYS B 2 43  ? 16.275  17.080  33.851  1.00 67.84  ?  43  LYS B NZ  1 
ATOM 1943 N N   . GLY B 2 44  ? 21.515  13.570  32.794  1.00 55.62  ?  44  GLY B N   1 
ATOM 1944 C CA  . GLY B 2 44  ? 22.956  13.708  32.849  1.00 58.03  ?  44  GLY B CA  1 
ATOM 1945 C C   . GLY B 2 44  ? 23.540  13.548  34.249  1.00 59.80  ?  44  GLY B C   1 
ATOM 1946 O O   . GLY B 2 44  ? 22.852  13.252  35.227  1.00 56.40  ?  44  GLY B O   1 
ATOM 1947 N N   . LEU B 2 45  ? 24.860  13.725  34.322  1.00 54.81  ?  45  LEU B N   1 
ATOM 1948 C CA  . LEU B 2 45  ? 25.580  13.617  35.584  1.00 57.50  ?  45  LEU B CA  1 
ATOM 1949 C C   . LEU B 2 45  ? 25.536  14.934  36.346  1.00 56.58  ?  45  LEU B C   1 
ATOM 1950 O O   . LEU B 2 45  ? 25.824  15.996  35.785  1.00 57.88  ?  45  LEU B O   1 
ATOM 1951 C CB  . LEU B 2 45  ? 27.030  13.202  35.340  1.00 55.21  ?  45  LEU B CB  1 
ATOM 1952 C CG  . LEU B 2 45  ? 27.234  11.787  34.808  1.00 53.87  ?  45  LEU B CG  1 
ATOM 1953 C CD1 . LEU B 2 45  ? 28.715  11.513  34.613  1.00 55.79  ?  45  LEU B CD1 1 
ATOM 1954 C CD2 . LEU B 2 45  ? 26.617  10.774  35.757  1.00 57.55  ?  45  LEU B CD2 1 
ATOM 1955 N N   . GLU B 2 46  ? 25.237  14.856  37.639  1.00 56.06  ?  46  GLU B N   1 
ATOM 1956 C CA  . GLU B 2 46  ? 25.089  16.033  38.485  1.00 53.60  ?  46  GLU B CA  1 
ATOM 1957 C C   . GLU B 2 46  ? 26.000  15.882  39.695  1.00 53.75  ?  46  GLU B C   1 
ATOM 1958 O O   . GLU B 2 46  ? 25.839  14.946  40.485  1.00 50.23  ?  46  GLU B O   1 
ATOM 1959 C CB  . GLU B 2 46  ? 23.628  16.212  38.905  1.00 56.04  ?  46  GLU B CB  1 
ATOM 1960 C CG  . GLU B 2 46  ? 23.248  17.616  39.317  1.00 54.84  ?  46  GLU B CG  1 
ATOM 1961 C CD  . GLU B 2 46  ? 21.786  17.719  39.714  1.00 63.00  ?  46  GLU B CD  1 
ATOM 1962 O OE1 . GLU B 2 46  ? 21.176  16.676  40.040  1.00 55.59  ?  46  GLU B OE1 1 
ATOM 1963 O OE2 . GLU B 2 46  ? 21.241  18.842  39.692  1.00 74.93  ?  46  GLU B OE2 1 
ATOM 1964 N N   . TRP B 2 47  ? 26.959  16.796  39.824  1.00 58.81  ?  47  TRP B N   1 
ATOM 1965 C CA  . TRP B 2 47  ? 27.889  16.792  40.946  1.00 55.68  ?  47  TRP B CA  1 
ATOM 1966 C C   . TRP B 2 47  ? 27.150  17.059  42.253  1.00 61.94  ?  47  TRP B C   1 
ATOM 1967 O O   . TRP B 2 47  ? 26.346  17.992  42.345  1.00 64.09  ?  47  TRP B O   1 
ATOM 1968 C CB  . TRP B 2 47  ? 28.969  17.848  40.716  1.00 64.12  ?  47  TRP B CB  1 
ATOM 1969 C CG  . TRP B 2 47  ? 29.867  18.084  41.882  1.00 68.11  ?  47  TRP B CG  1 
ATOM 1970 C CD1 . TRP B 2 47  ? 30.942  17.333  42.248  1.00 71.08  ?  47  TRP B CD1 1 
ATOM 1971 C CD2 . TRP B 2 47  ? 29.783  19.158  42.831  1.00 68.99  ?  47  TRP B CD2 1 
ATOM 1972 N NE1 . TRP B 2 47  ? 31.530  17.866  43.373  1.00 71.89  ?  47  TRP B NE1 1 
ATOM 1973 C CE2 . TRP B 2 47  ? 30.837  18.986  43.750  1.00 68.08  ?  47  TRP B CE2 1 
ATOM 1974 C CE3 . TRP B 2 47  ? 28.917  20.245  42.993  1.00 72.38  ?  47  TRP B CE3 1 
ATOM 1975 C CZ2 . TRP B 2 47  ? 31.051  19.859  44.816  1.00 66.16  ?  47  TRP B CZ2 1 
ATOM 1976 C CZ3 . TRP B 2 47  ? 29.132  21.113  44.055  1.00 73.95  ?  47  TRP B CZ3 1 
ATOM 1977 C CH2 . TRP B 2 47  ? 30.190  20.913  44.951  1.00 70.00  ?  47  TRP B CH2 1 
ATOM 1978 N N   . VAL B 2 48  ? 27.423  16.238  43.268  1.00 57.44  ?  48  VAL B N   1 
ATOM 1979 C CA  . VAL B 2 48  ? 26.741  16.319  44.559  1.00 58.92  ?  48  VAL B CA  1 
ATOM 1980 C C   . VAL B 2 48  ? 27.656  16.871  45.652  1.00 63.40  ?  48  VAL B C   1 
ATOM 1981 O O   . VAL B 2 48  ? 27.334  17.870  46.297  1.00 63.31  ?  48  VAL B O   1 
ATOM 1982 C CB  . VAL B 2 48  ? 26.144  14.955  44.965  1.00 58.40  ?  48  VAL B CB  1 
ATOM 1983 C CG1 . VAL B 2 48  ? 25.433  15.070  46.309  1.00 58.23  ?  48  VAL B CG1 1 
ATOM 1984 C CG2 . VAL B 2 48  ? 25.200  14.459  43.892  1.00 55.97  ?  48  VAL B CG2 1 
ATOM 1985 N N   . SER B 2 49  ? 28.785  16.211  45.904  1.00 66.98  ?  49  SER B N   1 
ATOM 1986 C CA  . SER B 2 49  ? 29.587  16.616  47.055  1.00 58.71  ?  49  SER B CA  1 
ATOM 1987 C C   . SER B 2 49  ? 31.037  16.202  46.864  1.00 55.01  ?  49  SER B C   1 
ATOM 1988 O O   . SER B 2 49  ? 31.337  15.257  46.134  1.00 63.61  ?  49  SER B O   1 
ATOM 1989 C CB  . SER B 2 49  ? 29.030  16.011  48.347  1.00 59.60  ?  49  SER B CB  1 
ATOM 1990 O OG  . SER B 2 49  ? 29.813  16.391  49.463  1.00 63.84  ?  49  SER B OG  1 
ATOM 1991 N N   . VAL B 2 50  ? 31.931  16.901  47.562  1.00 50.73  ?  50  VAL B N   1 
ATOM 1992 C CA  . VAL B 2 50  ? 33.359  16.604  47.536  1.00 54.59  ?  50  VAL B CA  1 
ATOM 1993 C C   . VAL B 2 50  ? 33.903  16.688  48.955  1.00 60.66  ?  50  VAL B C   1 
ATOM 1994 O O   . VAL B 2 50  ? 33.530  17.580  49.723  1.00 63.82  ?  50  VAL B O   1 
ATOM 1995 C CB  . VAL B 2 50  ? 34.120  17.564  46.600  1.00 51.50  ?  50  VAL B CB  1 
ATOM 1996 C CG1 . VAL B 2 50  ? 35.573  17.700  47.014  1.00 50.98  ?  50  VAL B CG1 1 
ATOM 1997 C CG2 . VAL B 2 50  ? 34.042  17.068  45.179  1.00 65.03  ?  50  VAL B CG2 1 
ATOM 1998 N N   . ILE B 2 51  ? 34.781  15.755  49.308  1.00 54.98  ?  51  ILE B N   1 
ATOM 1999 C CA  . ILE B 2 51  ? 35.518  15.814  50.562  1.00 60.85  ?  51  ILE B CA  1 
ATOM 2000 C C   . ILE B 2 51  ? 37.006  15.877  50.253  1.00 58.87  ?  51  ILE B C   1 
ATOM 2001 O O   . ILE B 2 51  ? 37.503  15.196  49.345  1.00 58.44  ?  51  ILE B O   1 
ATOM 2002 C CB  . ILE B 2 51  ? 35.190  14.638  51.507  1.00 62.11  ?  51  ILE B CB  1 
ATOM 2003 C CG1 . ILE B 2 51  ? 35.844  14.880  52.872  1.00 56.54  ?  51  ILE B CG1 1 
ATOM 2004 C CG2 . ILE B 2 51  ? 35.625  13.305  50.908  1.00 50.40  ?  51  ILE B CG2 1 
ATOM 2005 C CD1 . ILE B 2 51  ? 35.478  13.853  53.925  1.00 59.59  ?  51  ILE B CD1 1 
ATOM 2006 N N   . ASN B 2 52  ? 37.702  16.721  51.007  1.00 64.20  ?  52  ASN B N   1 
ATOM 2007 C CA  . ASN B 2 52  ? 39.103  17.035  50.817  1.00 66.93  ?  52  ASN B CA  1 
ATOM 2008 C C   . ASN B 2 52  ? 39.984  15.975  51.472  1.00 66.79  ?  52  ASN B C   1 
ATOM 2009 O O   . ASN B 2 52  ? 39.515  15.096  52.199  1.00 66.56  ?  52  ASN B O   1 
ATOM 2010 C CB  . ASN B 2 52  ? 39.411  18.407  51.415  1.00 74.13  ?  52  ASN B CB  1 
ATOM 2011 C CG  . ASN B 2 52  ? 40.676  19.016  50.861  1.00 81.04  ?  52  ASN B CG  1 
ATOM 2012 O OD1 . ASN B 2 52  ? 41.579  18.303  50.410  1.00 78.44  ?  52  ASN B OD1 1 
ATOM 2013 N ND2 . ASN B 2 52  ? 40.761  20.342  50.908  1.00 80.35  ?  52  ASN B ND2 1 
ATOM 2014 N N   . VAL B 2 53  ? 41.291  16.097  51.237  1.00 66.02  ?  53  VAL B N   1 
ATOM 2015 C CA  . VAL B 2 53  ? 42.241  15.212  51.895  1.00 62.74  ?  53  VAL B CA  1 
ATOM 2016 C C   . VAL B 2 53  ? 42.411  15.614  53.358  1.00 68.97  ?  53  VAL B C   1 
ATOM 2017 O O   . VAL B 2 53  ? 42.743  14.772  54.204  1.00 64.26  ?  53  VAL B O   1 
ATOM 2018 C CB  . VAL B 2 53  ? 43.578  15.218  51.128  1.00 59.13  ?  53  VAL B CB  1 
ATOM 2019 C CG1 . VAL B 2 53  ? 44.295  16.551  51.293  1.00 63.45  ?  53  VAL B CG1 1 
ATOM 2020 C CG2 . VAL B 2 53  ? 44.460  14.056  51.546  1.00 62.34  ?  53  VAL B CG2 1 
ATOM 2021 N N   . TYR B 2 54  ? 42.167  16.890  53.682  1.00 69.18  ?  54  TYR B N   1 
ATOM 2022 C CA  . TYR B 2 54  ? 42.190  17.358  55.064  1.00 64.94  ?  54  TYR B CA  1 
ATOM 2023 C C   . TYR B 2 54  ? 40.893  17.070  55.807  1.00 64.20  ?  54  TYR B C   1 
ATOM 2024 O O   . TYR B 2 54  ? 40.877  17.122  57.044  1.00 62.67  ?  54  TYR B O   1 
ATOM 2025 C CB  . TYR B 2 54  ? 42.463  18.862  55.112  1.00 63.02  ?  54  TYR B CB  1 
ATOM 2026 C CG  . TYR B 2 54  ? 43.661  19.313  54.312  1.00 65.84  ?  54  TYR B CG  1 
ATOM 2027 C CD1 . TYR B 2 54  ? 44.943  19.217  54.836  1.00 64.91  ?  54  TYR B CD1 1 
ATOM 2028 C CD2 . TYR B 2 54  ? 43.510  19.847  53.037  1.00 67.77  ?  54  TYR B CD2 1 
ATOM 2029 C CE1 . TYR B 2 54  ? 46.043  19.635  54.112  1.00 72.78  ?  54  TYR B CE1 1 
ATOM 2030 C CE2 . TYR B 2 54  ? 44.605  20.267  52.302  1.00 65.92  ?  54  TYR B CE2 1 
ATOM 2031 C CZ  . TYR B 2 54  ? 45.869  20.159  52.844  1.00 73.89  ?  54  TYR B CZ  1 
ATOM 2032 O OH  . TYR B 2 54  ? 46.966  20.575  52.125  1.00 74.77  ?  54  TYR B OH  1 
ATOM 2033 N N   . GLY B 2 55  ? 39.809  16.787  55.086  1.00 64.58  ?  55  GLY B N   1 
ATOM 2034 C CA  . GLY B 2 55  ? 38.488  16.662  55.669  1.00 61.19  ?  55  GLY B CA  1 
ATOM 2035 C C   . GLY B 2 55  ? 37.545  17.797  55.328  1.00 65.29  ?  55  GLY B C   1 
ATOM 2036 O O   . GLY B 2 55  ? 36.397  17.784  55.791  1.00 62.68  ?  55  GLY B O   1 
ATOM 2037 N N   . GLY B 2 56  ? 37.986  18.775  54.538  1.00 63.88  ?  56  GLY B N   1 
ATOM 2038 C CA  . GLY B 2 56  ? 37.111  19.872  54.158  1.00 69.20  ?  56  GLY B CA  1 
ATOM 2039 C C   . GLY B 2 56  ? 36.035  19.413  53.187  1.00 75.21  ?  56  GLY B C   1 
ATOM 2040 O O   . GLY B 2 56  ? 36.295  18.672  52.239  1.00 72.42  ?  56  GLY B O   1 
ATOM 2041 N N   . THR B 2 57  ? 34.807  19.858  53.437  1.00 75.51  ?  57  THR B N   1 
ATOM 2042 C CA  . THR B 2 57  ? 33.635  19.407  52.699  1.00 67.92  ?  57  THR B CA  1 
ATOM 2043 C C   . THR B 2 57  ? 33.064  20.534  51.846  1.00 72.30  ?  57  THR B C   1 
ATOM 2044 O O   . THR B 2 57  ? 32.792  21.626  52.353  1.00 81.01  ?  57  THR B O   1 
ATOM 2045 C CB  . THR B 2 57  ? 32.566  18.885  53.663  1.00 68.65  ?  57  THR B CB  1 
ATOM 2046 O OG1 . THR B 2 57  ? 32.172  19.931  54.560  1.00 68.57  ?  57  THR B OG1 1 
ATOM 2047 C CG2 . THR B 2 57  ? 33.106  17.719  54.473  1.00 69.74  ?  57  THR B CG2 1 
ATOM 2048 N N   . TYR B 2 58  ? 32.897  20.269  50.551  1.00 74.64  ?  58  TYR B N   1 
ATOM 2049 C CA  . TYR B 2 58  ? 32.238  21.183  49.626  1.00 77.46  ?  58  TYR B CA  1 
ATOM 2050 C C   . TYR B 2 58  ? 30.960  20.527  49.127  1.00 72.64  ?  58  TYR B C   1 
ATOM 2051 O O   . TYR B 2 58  ? 30.962  19.343  48.774  1.00 70.06  ?  58  TYR B O   1 
ATOM 2052 C CB  . TYR B 2 58  ? 33.124  21.543  48.425  1.00 78.66  ?  58  TYR B CB  1 
ATOM 2053 C CG  . TYR B 2 58  ? 34.331  22.396  48.740  1.00 90.08  ?  58  TYR B CG  1 
ATOM 2054 C CD1 . TYR B 2 58  ? 34.556  22.873  50.025  1.00 85.39  ?  58  TYR B CD1 1 
ATOM 2055 C CD2 . TYR B 2 58  ? 35.241  22.737  47.742  1.00 96.65  ?  58  TYR B CD2 1 
ATOM 2056 C CE1 . TYR B 2 58  ? 35.656  23.653  50.313  1.00 95.83  ?  58  TYR B CE1 1 
ATOM 2057 C CE2 . TYR B 2 58  ? 36.347  23.520  48.020  1.00 100.47 ?  58  TYR B CE2 1 
ATOM 2058 C CZ  . TYR B 2 58  ? 36.548  23.976  49.308  1.00 100.39 ?  58  TYR B CZ  1 
ATOM 2059 O OH  . TYR B 2 58  ? 37.644  24.756  49.600  1.00 101.78 ?  58  TYR B OH  1 
ATOM 2060 N N   . TYR B 2 59  ? 29.877  21.289  49.102  1.00 80.22  ?  59  TYR B N   1 
ATOM 2061 C CA  . TYR B 2 59  ? 28.573  20.806  48.675  1.00 75.30  ?  59  TYR B CA  1 
ATOM 2062 C C   . TYR B 2 59  ? 28.071  21.670  47.523  1.00 78.40  ?  59  TYR B C   1 
ATOM 2063 O O   . TYR B 2 59  ? 28.718  22.638  47.116  1.00 81.62  ?  59  TYR B O   1 
ATOM 2064 C CB  . TYR B 2 59  ? 27.582  20.813  49.842  1.00 77.95  ?  59  TYR B CB  1 
ATOM 2065 C CG  . TYR B 2 59  ? 27.995  19.949  51.014  1.00 74.41  ?  59  TYR B CG  1 
ATOM 2066 C CD1 . TYR B 2 59  ? 27.557  18.634  51.117  1.00 74.22  ?  59  TYR B CD1 1 
ATOM 2067 C CD2 . TYR B 2 59  ? 28.814  20.445  52.016  1.00 67.58  ?  59  TYR B CD2 1 
ATOM 2068 C CE1 . TYR B 2 59  ? 27.925  17.838  52.182  1.00 69.71  ?  59  TYR B CE1 1 
ATOM 2069 C CE2 . TYR B 2 59  ? 29.188  19.656  53.083  1.00 64.57  ?  59  TYR B CE2 1 
ATOM 2070 C CZ  . TYR B 2 59  ? 28.738  18.352  53.164  1.00 65.98  ?  59  TYR B CZ  1 
ATOM 2071 O OH  . TYR B 2 59  ? 29.103  17.554  54.228  1.00 65.41  ?  59  TYR B OH  1 
ATOM 2072 N N   . ALA B 2 60  ? 26.897  21.323  47.009  1.00 82.08  ?  60  ALA B N   1 
ATOM 2073 C CA  . ALA B 2 60  ? 26.266  22.079  45.938  1.00 85.02  ?  60  ALA B CA  1 
ATOM 2074 C C   . ALA B 2 60  ? 25.168  22.971  46.509  1.00 83.77  ?  60  ALA B C   1 
ATOM 2075 O O   . ALA B 2 60  ? 24.772  22.848  47.670  1.00 84.12  ?  60  ALA B O   1 
ATOM 2076 C CB  . ALA B 2 60  ? 25.705  21.137  44.867  1.00 71.43  ?  60  ALA B CB  1 
ATOM 2077 N N   . SER B 2 61  ? 24.676  23.885  45.673  1.00 84.63  ?  61  SER B N   1 
ATOM 2078 C CA  . SER B 2 61  ? 23.675  24.839  46.138  1.00 84.81  ?  61  SER B CA  1 
ATOM 2079 C C   . SER B 2 61  ? 22.396  24.129  46.568  1.00 80.37  ?  61  SER B C   1 
ATOM 2080 O O   . SER B 2 61  ? 21.893  24.351  47.675  1.00 80.36  ?  61  SER B O   1 
ATOM 2081 C CB  . SER B 2 61  ? 23.392  25.871  45.043  1.00 87.69  ?  61  SER B CB  1 
ATOM 2082 O OG  . SER B 2 61  ? 23.051  25.249  43.812  1.00 81.43  ?  61  SER B OG  1 
ATOM 2083 N N   . TRP B 2 62  ? 21.868  23.250  45.711  1.00 80.83  ?  62  TRP B N   1 
ATOM 2084 C CA  . TRP B 2 62  ? 20.617  22.560  46.010  1.00 76.37  ?  62  TRP B CA  1 
ATOM 2085 C C   . TRP B 2 62  ? 20.754  21.585  47.171  1.00 79.27  ?  62  TRP B C   1 
ATOM 2086 O O   . TRP B 2 62  ? 19.743  21.218  47.781  1.00 79.10  ?  62  TRP B O   1 
ATOM 2087 C CB  . TRP B 2 62  ? 20.116  21.824  44.766  1.00 73.22  ?  62  TRP B CB  1 
ATOM 2088 C CG  . TRP B 2 62  ? 21.196  21.074  44.041  1.00 78.01  ?  62  TRP B CG  1 
ATOM 2089 C CD1 . TRP B 2 62  ? 22.004  21.550  43.045  1.00 79.92  ?  62  TRP B CD1 1 
ATOM 2090 C CD2 . TRP B 2 62  ? 21.581  19.713  44.251  1.00 70.96  ?  62  TRP B CD2 1 
ATOM 2091 N NE1 . TRP B 2 62  ? 22.871  20.567  42.627  1.00 70.19  ?  62  TRP B NE1 1 
ATOM 2092 C CE2 . TRP B 2 62  ? 22.631  19.431  43.354  1.00 70.92  ?  62  TRP B CE2 1 
ATOM 2093 C CE3 . TRP B 2 62  ? 21.139  18.705  45.110  1.00 67.07  ?  62  TRP B CE3 1 
ATOM 2094 C CZ2 . TRP B 2 62  ? 23.246  18.186  43.296  1.00 70.63  ?  62  TRP B CZ2 1 
ATOM 2095 C CZ3 . TRP B 2 62  ? 21.752  17.471  45.052  1.00 68.76  ?  62  TRP B CZ3 1 
ATOM 2096 C CH2 . TRP B 2 62  ? 22.792  17.220  44.150  1.00 69.46  ?  62  TRP B CH2 1 
ATOM 2097 N N   . ALA B 2 63  ? 21.974  21.152  47.482  1.00 79.48  ?  63  ALA B N   1 
ATOM 2098 C CA  . ALA B 2 63  ? 22.213  20.278  48.621  1.00 78.29  ?  63  ALA B CA  1 
ATOM 2099 C C   . ALA B 2 63  ? 23.243  20.905  49.546  1.00 90.70  ?  63  ALA B C   1 
ATOM 2100 O O   . ALA B 2 63  ? 24.340  20.364  49.722  1.00 99.08  ?  63  ALA B O   1 
ATOM 2101 C CB  . ALA B 2 63  ? 22.683  18.897  48.166  1.00 78.98  ?  63  ALA B CB  1 
ATOM 2102 N N   . LYS B 2 64  ? 22.906  22.048  50.133  1.00 88.92  ?  64  LYS B N   1 
ATOM 2103 C CA  . LYS B 2 64  ? 23.755  22.716  51.107  1.00 83.80  ?  64  LYS B CA  1 
ATOM 2104 C C   . LYS B 2 64  ? 23.149  22.492  52.483  1.00 87.92  ?  64  LYS B C   1 
ATOM 2105 O O   . LYS B 2 64  ? 21.958  22.749  52.688  1.00 86.51  ?  64  LYS B O   1 
ATOM 2106 C CB  . LYS B 2 64  ? 23.878  24.211  50.798  1.00 93.65  ?  64  LYS B CB  1 
ATOM 2107 C CG  . LYS B 2 64  ? 25.143  24.875  51.338  1.00 100.12 ?  64  LYS B CG  1 
ATOM 2108 C CD  . LYS B 2 64  ? 26.393  24.255  50.715  1.00 98.30  ?  64  LYS B CD  1 
ATOM 2109 C CE  . LYS B 2 64  ? 27.677  24.847  51.285  1.00 98.14  ?  64  LYS B CE  1 
ATOM 2110 N NZ  . LYS B 2 64  ? 27.807  26.300  50.974  1.00 99.57  ?  64  LYS B NZ  1 
ATOM 2111 N N   . GLY B 2 65  ? 23.952  21.967  53.407  1.00 88.24  ?  65  GLY B N   1 
ATOM 2112 C CA  . GLY B 2 65  ? 23.469  21.615  54.725  1.00 80.81  ?  65  GLY B CA  1 
ATOM 2113 C C   . GLY B 2 65  ? 22.463  20.487  54.770  1.00 78.37  ?  65  GLY B C   1 
ATOM 2114 O O   . GLY B 2 65  ? 22.125  20.029  55.867  1.00 80.81  ?  65  GLY B O   1 
ATOM 2115 N N   . ARG B 2 66  ? 21.960  20.031  53.624  1.00 84.80  ?  66  ARG B N   1 
ATOM 2116 C CA  . ARG B 2 66  ? 21.005  18.932  53.568  1.00 80.58  ?  66  ARG B CA  1 
ATOM 2117 C C   . ARG B 2 66  ? 21.696  17.573  53.548  1.00 80.92  ?  66  ARG B C   1 
ATOM 2118 O O   . ARG B 2 66  ? 21.210  16.620  54.170  1.00 77.60  ?  66  ARG B O   1 
ATOM 2119 C CB  . ARG B 2 66  ? 20.103  19.092  52.343  1.00 73.76  ?  66  ARG B CB  1 
ATOM 2120 C CG  . ARG B 2 66  ? 18.798  18.323  52.417  1.00 71.77  ?  66  ARG B CG  1 
ATOM 2121 C CD  . ARG B 2 66  ? 17.751  18.956  51.514  1.00 78.74  ?  66  ARG B CD  1 
ATOM 2122 N NE  . ARG B 2 66  ? 18.279  19.249  50.185  1.00 83.12  ?  66  ARG B NE  1 
ATOM 2123 C CZ  . ARG B 2 66  ? 18.181  18.433  49.141  1.00 79.98  ?  66  ARG B CZ  1 
ATOM 2124 N NH1 . ARG B 2 66  ? 18.698  18.792  47.974  1.00 82.14  ?  66  ARG B NH1 1 
ATOM 2125 N NH2 . ARG B 2 66  ? 17.571  17.261  49.261  1.00 71.56  ?  66  ARG B NH2 1 
ATOM 2126 N N   . PHE B 2 67  ? 22.815  17.462  52.837  1.00 76.30  ?  67  PHE B N   1 
ATOM 2127 C CA  . PHE B 2 67  ? 23.604  16.242  52.789  1.00 69.13  ?  67  PHE B CA  1 
ATOM 2128 C C   . PHE B 2 67  ? 24.905  16.436  53.556  1.00 63.52  ?  67  PHE B C   1 
ATOM 2129 O O   . PHE B 2 67  ? 25.334  17.563  53.819  1.00 70.57  ?  67  PHE B O   1 
ATOM 2130 C CB  . PHE B 2 67  ? 23.911  15.840  51.343  1.00 72.98  ?  67  PHE B CB  1 
ATOM 2131 C CG  . PHE B 2 67  ? 22.691  15.543  50.523  1.00 68.15  ?  67  PHE B CG  1 
ATOM 2132 C CD1 . PHE B 2 67  ? 22.770  15.498  49.145  1.00 69.32  ?  67  PHE B CD1 1 
ATOM 2133 C CD2 . PHE B 2 67  ? 21.463  15.333  51.127  1.00 68.96  ?  67  PHE B CD2 1 
ATOM 2134 C CE1 . PHE B 2 67  ? 21.651  15.234  48.384  1.00 76.49  ?  67  PHE B CE1 1 
ATOM 2135 C CE2 . PHE B 2 67  ? 20.342  15.071  50.372  1.00 69.59  ?  67  PHE B CE2 1 
ATOM 2136 C CZ  . PHE B 2 67  ? 20.435  15.019  49.000  1.00 75.83  ?  67  PHE B CZ  1 
ATOM 2137 N N   . THR B 2 68  ? 25.539  15.318  53.900  1.00 64.08  ?  68  THR B N   1 
ATOM 2138 C CA  . THR B 2 68  ? 26.785  15.343  54.662  1.00 68.70  ?  68  THR B CA  1 
ATOM 2139 C C   . THR B 2 68  ? 27.708  14.245  54.156  1.00 64.70  ?  68  THR B C   1 
ATOM 2140 O O   . THR B 2 68  ? 27.367  13.061  54.242  1.00 58.29  ?  68  THR B O   1 
ATOM 2141 C CB  . THR B 2 68  ? 26.518  15.154  56.160  1.00 68.15  ?  68  THR B CB  1 
ATOM 2142 O OG1 . THR B 2 68  ? 25.663  16.200  56.636  1.00 68.42  ?  68  THR B OG1 1 
ATOM 2143 C CG2 . THR B 2 68  ? 27.824  15.179  56.939  1.00 57.76  ?  68  THR B CG2 1 
ATOM 2144 N N   . ILE B 2 69  ? 28.889  14.635  53.670  1.00 61.49  ?  69  ILE B N   1 
ATOM 2145 C CA  . ILE B 2 69  ? 29.907  13.701  53.197  1.00 59.16  ?  69  ILE B CA  1 
ATOM 2146 C C   . ILE B 2 69  ? 30.948  13.513  54.291  1.00 63.86  ?  69  ILE B C   1 
ATOM 2147 O O   . ILE B 2 69  ? 31.304  14.465  54.998  1.00 72.09  ?  69  ILE B O   1 
ATOM 2148 C CB  . ILE B 2 69  ? 30.555  14.201  51.892  1.00 61.53  ?  69  ILE B CB  1 
ATOM 2149 C CG1 . ILE B 2 69  ? 31.521  13.159  51.330  1.00 58.49  ?  69  ILE B CG1 1 
ATOM 2150 C CG2 . ILE B 2 69  ? 31.277  15.522  52.115  1.00 60.32  ?  69  ILE B CG2 1 
ATOM 2151 C CD1 . ILE B 2 69  ? 32.065  13.522  49.967  1.00 55.98  ?  69  ILE B CD1 1 
ATOM 2152 N N   . SER B 2 70  ? 31.437  12.284  54.442  1.00 60.51  ?  70  SER B N   1 
ATOM 2153 C CA  . SER B 2 70  ? 32.401  11.986  55.494  1.00 57.18  ?  70  SER B CA  1 
ATOM 2154 C C   . SER B 2 70  ? 33.237  10.781  55.089  1.00 61.10  ?  70  SER B C   1 
ATOM 2155 O O   . SER B 2 70  ? 32.927  10.083  54.124  1.00 59.46  ?  70  SER B O   1 
ATOM 2156 C CB  . SER B 2 70  ? 31.697  11.725  56.829  1.00 57.62  ?  70  SER B CB  1 
ATOM 2157 O OG  . SER B 2 70  ? 30.712  10.711  56.686  1.00 51.14  ?  70  SER B OG  1 
ATOM 2158 N N   . ARG B 2 71  ? 34.294  10.521  55.854  1.00 64.58  ?  71  ARG B N   1 
ATOM 2159 C CA  . ARG B 2 71  ? 35.110  9.345   55.592  1.00 62.04  ?  71  ARG B CA  1 
ATOM 2160 C C   . ARG B 2 71  ? 35.682  8.805   56.896  1.00 61.09  ?  71  ARG B C   1 
ATOM 2161 O O   . ARG B 2 71  ? 36.120  9.566   57.763  1.00 55.49  ?  71  ARG B O   1 
ATOM 2162 C CB  . ARG B 2 71  ? 36.251  9.642   54.610  1.00 58.82  ?  71  ARG B CB  1 
ATOM 2163 C CG  . ARG B 2 71  ? 37.210  10.711  55.081  1.00 63.50  ?  71  ARG B CG  1 
ATOM 2164 C CD  . ARG B 2 71  ? 38.615  10.421  54.596  1.00 65.74  ?  71  ARG B CD  1 
ATOM 2165 N NE  . ARG B 2 71  ? 39.546  11.476  54.976  1.00 61.86  ?  71  ARG B NE  1 
ATOM 2166 C CZ  . ARG B 2 71  ? 39.979  12.422  54.150  1.00 66.28  ?  71  ARG B CZ  1 
ATOM 2167 N NH1 . ARG B 2 71  ? 39.571  12.444  52.884  1.00 68.98  ?  71  ARG B NH1 1 
ATOM 2168 N NH2 . ARG B 2 71  ? 40.827  13.340  54.589  1.00 67.18  ?  71  ARG B NH2 1 
ATOM 2169 N N   . ASP B 2 72  ? 35.674  7.483   57.015  1.00 67.28  ?  72  ASP B N   1 
ATOM 2170 C CA  . ASP B 2 72  ? 36.290  6.777   58.128  1.00 71.39  ?  72  ASP B CA  1 
ATOM 2171 C C   . ASP B 2 72  ? 37.621  6.212   57.650  1.00 70.30  ?  72  ASP B C   1 
ATOM 2172 O O   . ASP B 2 72  ? 37.653  5.378   56.736  1.00 72.18  ?  72  ASP B O   1 
ATOM 2173 C CB  . ASP B 2 72  ? 35.380  5.664   58.652  1.00 73.55  ?  72  ASP B CB  1 
ATOM 2174 C CG  . ASP B 2 72  ? 35.765  5.203   60.049  1.00 78.15  ?  72  ASP B CG  1 
ATOM 2175 O OD1 . ASP B 2 72  ? 36.975  5.078   60.337  1.00 76.04  ?  72  ASP B OD1 1 
ATOM 2176 O OD2 . ASP B 2 72  ? 34.850  4.985   60.870  1.00 80.76  ?  72  ASP B OD2 1 
ATOM 2177 N N   . ASN B 2 73  ? 38.714  6.698   58.245  1.00 70.15  ?  73  ASN B N   1 
ATOM 2178 C CA  . ASN B 2 73  ? 40.047  6.274   57.830  1.00 73.41  ?  73  ASN B CA  1 
ATOM 2179 C C   . ASN B 2 73  ? 40.382  4.876   58.329  1.00 71.09  ?  73  ASN B C   1 
ATOM 2180 O O   . ASN B 2 73  ? 41.096  4.132   57.647  1.00 73.58  ?  73  ASN B O   1 
ATOM 2181 C CB  . ASN B 2 73  ? 41.092  7.274   58.312  1.00 67.39  ?  73  ASN B CB  1 
ATOM 2182 C CG  . ASN B 2 73  ? 40.753  8.692   57.922  1.00 70.12  ?  73  ASN B CG  1 
ATOM 2183 O OD1 . ASN B 2 73  ? 40.960  9.091   56.778  1.00 72.42  ?  73  ASN B OD1 1 
ATOM 2184 N ND2 . ASN B 2 73  ? 40.233  9.466   58.870  1.00 75.70  ?  73  ASN B ND2 1 
ATOM 2185 N N   . SER B 2 74  ? 39.898  4.507   59.514  1.00 71.16  ?  74  SER B N   1 
ATOM 2186 C CA  . SER B 2 74  ? 40.130  3.154   60.005  1.00 73.87  ?  74  SER B CA  1 
ATOM 2187 C C   . SER B 2 74  ? 39.459  2.129   59.101  1.00 77.73  ?  74  SER B C   1 
ATOM 2188 O O   . SER B 2 74  ? 40.106  1.194   58.613  1.00 80.67  ?  74  SER B O   1 
ATOM 2189 C CB  . SER B 2 74  ? 39.622  3.026   61.441  1.00 79.18  ?  74  SER B CB  1 
ATOM 2190 O OG  . SER B 2 74  ? 38.247  3.365   61.529  1.00 77.36  ?  74  SER B OG  1 
ATOM 2191 N N   . LYS B 2 75  ? 38.160  2.297   58.854  1.00 73.40  ?  75  LYS B N   1 
ATOM 2192 C CA  . LYS B 2 75  ? 37.444  1.428   57.930  1.00 69.48  ?  75  LYS B CA  1 
ATOM 2193 C C   . LYS B 2 75  ? 37.730  1.737   56.466  1.00 70.84  ?  75  LYS B C   1 
ATOM 2194 O O   . LYS B 2 75  ? 37.307  0.960   55.603  1.00 65.07  ?  75  LYS B O   1 
ATOM 2195 C CB  . LYS B 2 75  ? 35.937  1.494   58.184  1.00 73.24  ?  75  LYS B CB  1 
ATOM 2196 C CG  . LYS B 2 75  ? 35.487  0.791   59.455  1.00 71.08  ?  75  LYS B CG  1 
ATOM 2197 C CD  . LYS B 2 75  ? 33.976  0.846   59.597  1.00 72.10  ?  75  LYS B CD  1 
ATOM 2198 C CE  . LYS B 2 75  ? 33.493  0.033   60.782  1.00 82.19  ?  75  LYS B CE  1 
ATOM 2199 N NZ  . LYS B 2 75  ? 33.840  -1.411  60.648  1.00 81.38  ?  75  LYS B NZ  1 
ATOM 2200 N N   . ASN B 2 76  ? 38.393  2.854   56.165  1.00 73.42  ?  76  ASN B N   1 
ATOM 2201 C CA  . ASN B 2 76  ? 38.715  3.236   54.789  1.00 70.03  ?  76  ASN B CA  1 
ATOM 2202 C C   . ASN B 2 76  ? 37.450  3.228   53.930  1.00 66.02  ?  76  ASN B C   1 
ATOM 2203 O O   . ASN B 2 76  ? 37.314  2.462   52.976  1.00 67.36  ?  76  ASN B O   1 
ATOM 2204 C CB  . ASN B 2 76  ? 39.803  2.320   54.215  1.00 66.56  ?  76  ASN B CB  1 
ATOM 2205 C CG  . ASN B 2 76  ? 40.327  2.791   52.868  1.00 67.98  ?  76  ASN B CG  1 
ATOM 2206 O OD1 . ASN B 2 76  ? 40.898  3.875   52.751  1.00 68.87  ?  76  ASN B OD1 1 
ATOM 2207 N ND2 . ASN B 2 76  ? 40.165  1.955   51.849  1.00 65.70  ?  76  ASN B ND2 1 
ATOM 2208 N N   . THR B 2 77  ? 36.500  4.086   54.312  1.00 66.56  ?  77  THR B N   1 
ATOM 2209 C CA  . THR B 2 77  ? 35.185  4.098   53.680  1.00 65.00  ?  77  THR B CA  1 
ATOM 2210 C C   . THR B 2 77  ? 34.641  5.516   53.606  1.00 62.98  ?  77  THR B C   1 
ATOM 2211 O O   . THR B 2 77  ? 34.748  6.278   54.569  1.00 67.93  ?  77  THR B O   1 
ATOM 2212 C CB  . THR B 2 77  ? 34.191  3.217   54.455  1.00 64.88  ?  77  THR B CB  1 
ATOM 2213 O OG1 . THR B 2 77  ? 34.712  1.888   54.578  1.00 64.26  ?  77  THR B OG1 1 
ATOM 2214 C CG2 . THR B 2 77  ? 32.844  3.167   53.747  1.00 63.00  ?  77  THR B CG2 1 
ATOM 2215 N N   . LEU B 2 78  ? 34.031  5.853   52.472  1.00 55.48  ?  78  LEU B N   1 
ATOM 2216 C CA  . LEU B 2 78  ? 33.346  7.124   52.286  1.00 55.28  ?  78  LEU B CA  1 
ATOM 2217 C C   . LEU B 2 78  ? 31.862  6.966   52.604  1.00 56.64  ?  78  LEU B C   1 
ATOM 2218 O O   . LEU B 2 78  ? 31.285  5.893   52.422  1.00 53.35  ?  78  LEU B O   1 
ATOM 2219 C CB  . LEU B 2 78  ? 33.532  7.620   50.853  1.00 54.04  ?  78  LEU B CB  1 
ATOM 2220 C CG  . LEU B 2 78  ? 33.164  9.066   50.542  1.00 55.45  ?  78  LEU B CG  1 
ATOM 2221 C CD1 . LEU B 2 78  ? 34.155  9.991   51.217  1.00 60.83  ?  78  LEU B CD1 1 
ATOM 2222 C CD2 . LEU B 2 78  ? 33.136  9.311   49.041  1.00 55.58  ?  78  LEU B CD2 1 
ATOM 2223 N N   . TYR B 2 79  ? 31.241  8.052   53.071  1.00 53.75  ?  79  TYR B N   1 
ATOM 2224 C CA  . TYR B 2 79  ? 29.849  8.043   53.502  1.00 48.26  ?  79  TYR B CA  1 
ATOM 2225 C C   . TYR B 2 79  ? 29.139  9.295   53.008  1.00 54.34  ?  79  TYR B C   1 
ATOM 2226 O O   . TYR B 2 79  ? 29.733  10.379  52.961  1.00 56.05  ?  79  TYR B O   1 
ATOM 2227 C CB  . TYR B 2 79  ? 29.727  7.970   55.035  1.00 50.64  ?  79  TYR B CB  1 
ATOM 2228 C CG  . TYR B 2 79  ? 30.289  6.711   55.654  1.00 58.68  ?  79  TYR B CG  1 
ATOM 2229 C CD1 . TYR B 2 79  ? 29.568  5.522   55.628  1.00 56.56  ?  79  TYR B CD1 1 
ATOM 2230 C CD2 . TYR B 2 79  ? 31.542  6.707   56.255  1.00 56.08  ?  79  TYR B CD2 1 
ATOM 2231 C CE1 . TYR B 2 79  ? 30.074  4.369   56.182  1.00 57.45  ?  79  TYR B CE1 1 
ATOM 2232 C CE2 . TYR B 2 79  ? 32.059  5.555   56.815  1.00 61.00  ?  79  TYR B CE2 1 
ATOM 2233 C CZ  . TYR B 2 79  ? 31.321  4.386   56.778  1.00 67.49  ?  79  TYR B CZ  1 
ATOM 2234 O OH  . TYR B 2 79  ? 31.825  3.227   57.334  1.00 72.12  ?  79  TYR B OH  1 
ATOM 2235 N N   . LEU B 2 80  ? 27.870  9.129   52.633  1.00 50.52  ?  80  LEU B N   1 
ATOM 2236 C CA  . LEU B 2 80  ? 26.981  10.237  52.292  1.00 49.88  ?  80  LEU B CA  1 
ATOM 2237 C C   . LEU B 2 80  ? 25.671  10.063  53.049  1.00 59.64  ?  80  LEU B C   1 
ATOM 2238 O O   . LEU B 2 80  ? 24.921  9.119   52.780  1.00 60.33  ?  80  LEU B O   1 
ATOM 2239 C CB  . LEU B 2 80  ? 26.722  10.305  50.788  1.00 58.08  ?  80  LEU B CB  1 
ATOM 2240 C CG  . LEU B 2 80  ? 25.947  11.543  50.324  1.00 55.28  ?  80  LEU B CG  1 
ATOM 2241 C CD1 . LEU B 2 80  ? 26.783  12.803  50.511  1.00 48.13  ?  80  LEU B CD1 1 
ATOM 2242 C CD2 . LEU B 2 80  ? 25.494  11.396  48.883  1.00 51.50  ?  80  LEU B CD2 1 
ATOM 2243 N N   . GLN B 2 81  ? 25.402  10.961  53.998  1.00 64.30  ?  81  GLN B N   1 
ATOM 2244 C CA  . GLN B 2 81  ? 24.157  10.967  54.759  1.00 60.50  ?  81  GLN B CA  1 
ATOM 2245 C C   . GLN B 2 81  ? 23.206  11.998  54.159  1.00 61.90  ?  81  GLN B C   1 
ATOM 2246 O O   . GLN B 2 81  ? 23.572  13.168  54.002  1.00 66.64  ?  81  GLN B O   1 
ATOM 2247 C CB  . GLN B 2 81  ? 24.420  11.274  56.237  1.00 63.98  ?  81  GLN B CB  1 
ATOM 2248 C CG  . GLN B 2 81  ? 23.164  11.411  57.101  1.00 64.57  ?  81  GLN B CG  1 
ATOM 2249 C CD  . GLN B 2 81  ? 22.535  10.075  57.479  1.00 58.89  ?  81  GLN B CD  1 
ATOM 2250 O OE1 . GLN B 2 81  ? 23.223  9.147   57.904  1.00 55.69  ?  81  GLN B OE1 1 
ATOM 2251 N NE2 . GLN B 2 81  ? 21.218  9.974   57.323  1.00 55.48  ?  81  GLN B NE2 1 
ATOM 2252 N N   . MET B 2 82  ? 21.996  11.556  53.821  1.00 62.39  ?  82  MET B N   1 
ATOM 2253 C CA  . MET B 2 82  ? 20.971  12.372  53.182  1.00 65.25  ?  82  MET B CA  1 
ATOM 2254 C C   . MET B 2 82  ? 19.778  12.450  54.125  1.00 67.64  ?  82  MET B C   1 
ATOM 2255 O O   . MET B 2 82  ? 19.288  11.414  54.585  1.00 70.87  ?  82  MET B O   1 
ATOM 2256 C CB  . MET B 2 82  ? 20.573  11.760  51.834  1.00 61.78  ?  82  MET B CB  1 
ATOM 2257 C CG  . MET B 2 82  ? 21.760  11.542  50.897  1.00 65.35  ?  82  MET B CG  1 
ATOM 2258 S SD  . MET B 2 82  ? 21.377  10.681  49.350  1.00 76.42  ?  82  MET B SD  1 
ATOM 2259 C CE  . MET B 2 82  ? 20.953  9.042   49.941  1.00 67.45  ?  82  MET B CE  1 
ATOM 2260 N N   . ASN B 2 83  ? 19.304  13.666  54.415  1.00 71.82  ?  83  ASN B N   1 
ATOM 2261 C CA  . ASN B 2 83  ? 18.290  13.829  55.454  1.00 79.27  ?  83  ASN B CA  1 
ATOM 2262 C C   . ASN B 2 83  ? 16.960  14.379  54.961  1.00 78.90  ?  83  ASN B C   1 
ATOM 2263 O O   . ASN B 2 83  ? 15.906  13.870  55.362  1.00 85.17  ?  83  ASN B O   1 
ATOM 2264 C CB  . ASN B 2 83  ? 18.836  14.729  56.570  1.00 77.69  ?  83  ASN B CB  1 
ATOM 2265 C CG  . ASN B 2 83  ? 20.168  14.247  57.097  1.00 77.17  ?  83  ASN B CG  1 
ATOM 2266 O OD1 . ASN B 2 83  ? 20.230  13.285  57.864  1.00 72.40  ?  83  ASN B OD1 1 
ATOM 2267 N ND2 . ASN B 2 83  ? 21.246  14.910  56.683  1.00 75.94  ?  83  ASN B ND2 1 
ATOM 2268 N N   . SER B 2 84  ? 16.960  15.415  54.132  1.00 77.63  ?  84  SER B N   1 
ATOM 2269 C CA  . SER B 2 84  ? 15.691  15.984  53.696  1.00 82.26  ?  84  SER B CA  1 
ATOM 2270 C C   . SER B 2 84  ? 15.451  15.672  52.226  1.00 78.40  ?  84  SER B C   1 
ATOM 2271 O O   . SER B 2 84  ? 15.434  16.576  51.383  1.00 79.03  ?  84  SER B O   1 
ATOM 2272 C CB  . SER B 2 84  ? 15.659  17.488  53.964  1.00 83.18  ?  84  SER B CB  1 
ATOM 2273 O OG  . SER B 2 84  ? 15.853  17.754  55.345  1.00 78.02  ?  84  SER B OG  1 
ATOM 2274 N N   . LEU B 2 85  ? 15.277  14.388  51.915  1.00 74.66  ?  85  LEU B N   1 
ATOM 2275 C CA  . LEU B 2 85  ? 15.161  13.961  50.527  1.00 78.68  ?  85  LEU B CA  1 
ATOM 2276 C C   . LEU B 2 85  ? 13.804  14.333  49.942  1.00 75.80  ?  85  LEU B C   1 
ATOM 2277 O O   . LEU B 2 85  ? 12.766  14.219  50.600  1.00 73.97  ?  85  LEU B O   1 
ATOM 2278 C CB  . LEU B 2 85  ? 15.375  12.450  50.424  1.00 71.05  ?  85  LEU B CB  1 
ATOM 2279 C CG  . LEU B 2 85  ? 16.808  11.983  50.689  1.00 66.48  ?  85  LEU B CG  1 
ATOM 2280 C CD1 . LEU B 2 85  ? 16.889  10.468  50.744  1.00 64.22  ?  85  LEU B CD1 1 
ATOM 2281 C CD2 . LEU B 2 85  ? 17.737  12.541  49.625  1.00 72.01  ?  85  LEU B CD2 1 
ATOM 2282 N N   . ARG B 2 86  ? 13.827  14.769  48.685  1.00 73.47  ?  86  ARG B N   1 
ATOM 2283 C CA  . ARG B 2 86  ? 12.652  15.154  47.919  1.00 78.52  ?  86  ARG B CA  1 
ATOM 2284 C C   . ARG B 2 86  ? 12.507  14.240  46.706  1.00 81.00  ?  86  ARG B C   1 
ATOM 2285 O O   . ARG B 2 86  ? 13.375  13.413  46.412  1.00 80.67  ?  86  ARG B O   1 
ATOM 2286 C CB  . ARG B 2 86  ? 12.739  16.620  47.473  1.00 82.23  ?  86  ARG B CB  1 
ATOM 2287 C CG  . ARG B 2 86  ? 13.395  17.553  48.481  1.00 86.14  ?  86  ARG B CG  1 
ATOM 2288 C CD  . ARG B 2 86  ? 13.942  18.796  47.784  1.00 89.83  ?  86  ARG B CD  1 
ATOM 2289 N NE  . ARG B 2 86  ? 14.606  19.717  48.705  1.00 91.87  ?  86  ARG B NE  1 
ATOM 2290 C CZ  . ARG B 2 86  ? 15.322  20.769  48.318  1.00 89.97  ?  86  ARG B CZ  1 
ATOM 2291 N NH1 . ARG B 2 86  ? 15.478  21.026  47.025  1.00 93.40  ?  86  ARG B NH1 1 
ATOM 2292 N NH2 . ARG B 2 86  ? 15.893  21.557  49.221  1.00 85.73  ?  86  ARG B NH2 1 
ATOM 2293 N N   . ALA B 2 87  ? 11.389  14.402  45.992  1.00 83.86  ?  87  ALA B N   1 
ATOM 2294 C CA  . ALA B 2 87  ? 11.137  13.576  44.813  1.00 80.42  ?  87  ALA B CA  1 
ATOM 2295 C C   . ALA B 2 87  ? 12.178  13.809  43.724  1.00 78.01  ?  87  ALA B C   1 
ATOM 2296 O O   . ALA B 2 87  ? 12.472  12.898  42.944  1.00 77.18  ?  87  ALA B O   1 
ATOM 2297 C CB  . ALA B 2 87  ? 9.733   13.841  44.267  1.00 83.15  ?  87  ALA B CB  1 
ATOM 2298 N N   . GLU B 2 88  ? 12.734  15.016  43.637  1.00 77.95  ?  88  GLU B N   1 
ATOM 2299 C CA  . GLU B 2 88  ? 13.774  15.282  42.652  1.00 77.89  ?  88  GLU B CA  1 
ATOM 2300 C C   . GLU B 2 88  ? 15.133  14.729  43.075  1.00 75.58  ?  88  GLU B C   1 
ATOM 2301 O O   . GLU B 2 88  ? 16.126  14.979  42.383  1.00 78.93  ?  88  GLU B O   1 
ATOM 2302 C CB  . GLU B 2 88  ? 13.898  16.787  42.376  1.00 80.35  ?  88  GLU B CB  1 
ATOM 2303 C CG  . GLU B 2 88  ? 14.443  17.611  43.546  1.00 87.82  ?  88  GLU B CG  1 
ATOM 2304 C CD  . GLU B 2 88  ? 13.364  18.339  44.328  1.00 92.50  ?  88  GLU B CD  1 
ATOM 2305 O OE1 . GLU B 2 88  ? 13.594  19.513  44.704  1.00 84.45  ?  88  GLU B OE1 1 
ATOM 2306 O OE2 . GLU B 2 88  ? 12.294  17.739  44.566  1.00 97.43  ?  88  GLU B OE2 1 
ATOM 2307 N N   . ASP B 2 89  ? 15.206  13.997  44.191  1.00 70.96  ?  89  ASP B N   1 
ATOM 2308 C CA  . ASP B 2 89  ? 16.457  13.397  44.640  1.00 67.84  ?  89  ASP B CA  1 
ATOM 2309 C C   . ASP B 2 89  ? 16.618  11.940  44.223  1.00 61.21  ?  89  ASP B C   1 
ATOM 2310 O O   . ASP B 2 89  ? 17.704  11.381  44.415  1.00 53.45  ?  89  ASP B O   1 
ATOM 2311 C CB  . ASP B 2 89  ? 16.590  13.494  46.167  1.00 66.33  ?  89  ASP B CB  1 
ATOM 2312 C CG  . ASP B 2 89  ? 16.860  14.909  46.645  1.00 75.84  ?  89  ASP B CG  1 
ATOM 2313 O OD1 . ASP B 2 89  ? 16.068  15.419  47.467  1.00 81.55  ?  89  ASP B OD1 1 
ATOM 2314 O OD2 . ASP B 2 89  ? 17.852  15.519  46.188  1.00 73.03  ?  89  ASP B OD2 1 
ATOM 2315 N N   . THR B 2 90  ? 15.586  11.315  43.659  1.00 57.41  ?  90  THR B N   1 
ATOM 2316 C CA  . THR B 2 90  ? 15.730  9.946   43.179  1.00 57.19  ?  90  THR B CA  1 
ATOM 2317 C C   . THR B 2 90  ? 16.737  9.925   42.041  1.00 48.89  ?  90  THR B C   1 
ATOM 2318 O O   . THR B 2 90  ? 16.608  10.685  41.078  1.00 53.59  ?  90  THR B O   1 
ATOM 2319 C CB  . THR B 2 90  ? 14.388  9.388   42.713  1.00 57.44  ?  90  THR B CB  1 
ATOM 2320 O OG1 . THR B 2 90  ? 14.186  9.733   41.339  1.00 66.86  ?  90  THR B OG1 1 
ATOM 2321 C CG2 . THR B 2 90  ? 13.261  9.984   43.530  1.00 62.88  ?  90  THR B CG2 1 
ATOM 2322 N N   . ALA B 2 91  ? 17.753  9.080   42.169  1.00 46.94  ?  91  ALA B N   1 
ATOM 2323 C CA  . ALA B 2 91  ? 18.856  9.058   41.218  1.00 44.01  ?  91  ALA B CA  1 
ATOM 2324 C C   . ALA B 2 91  ? 19.760  7.880   41.551  1.00 54.18  ?  91  ALA B C   1 
ATOM 2325 O O   . ALA B 2 91  ? 19.632  7.250   42.604  1.00 48.15  ?  91  ALA B O   1 
ATOM 2326 C CB  . ALA B 2 91  ? 19.656  10.360  41.254  1.00 41.52  ?  91  ALA B CB  1 
ATOM 2327 N N   . VAL B 2 92  ? 20.682  7.593   40.639  1.00 52.77  ?  92  VAL B N   1 
ATOM 2328 C CA  . VAL B 2 92  ? 21.776  6.672   40.911  1.00 54.42  ?  92  VAL B CA  1 
ATOM 2329 C C   . VAL B 2 92  ? 22.946  7.495   41.432  1.00 55.60  ?  92  VAL B C   1 
ATOM 2330 O O   . VAL B 2 92  ? 23.395  8.434   40.766  1.00 55.33  ?  92  VAL B O   1 
ATOM 2331 C CB  . VAL B 2 92  ? 22.173  5.877   39.658  1.00 53.54  ?  92  VAL B CB  1 
ATOM 2332 C CG1 . VAL B 2 92  ? 23.376  4.998   39.962  1.00 48.55  ?  92  VAL B CG1 1 
ATOM 2333 C CG2 . VAL B 2 92  ? 21.005  5.030   39.167  1.00 49.77  ?  92  VAL B CG2 1 
ATOM 2334 N N   . TYR B 2 93  ? 23.421  7.166   42.630  1.00 54.45  ?  93  TYR B N   1 
ATOM 2335 C CA  . TYR B 2 93  ? 24.534  7.870   43.252  1.00 54.76  ?  93  TYR B CA  1 
ATOM 2336 C C   . TYR B 2 93  ? 25.813  7.060   43.083  1.00 53.36  ?  93  TYR B C   1 
ATOM 2337 O O   . TYR B 2 93  ? 25.834  5.852   43.369  1.00 50.55  ?  93  TYR B O   1 
ATOM 2338 C CB  . TYR B 2 93  ? 24.252  8.133   44.733  1.00 57.74  ?  93  TYR B CB  1 
ATOM 2339 C CG  . TYR B 2 93  ? 23.197  9.190   44.945  1.00 51.15  ?  93  TYR B CG  1 
ATOM 2340 C CD1 . TYR B 2 93  ? 23.550  10.504  45.206  1.00 45.31  ?  93  TYR B CD1 1 
ATOM 2341 C CD2 . TYR B 2 93  ? 21.846  8.874   44.861  1.00 50.28  ?  93  TYR B CD2 1 
ATOM 2342 C CE1 . TYR B 2 93  ? 22.587  11.474  45.384  1.00 46.78  ?  93  TYR B CE1 1 
ATOM 2343 C CE2 . TYR B 2 93  ? 20.876  9.835   45.043  1.00 47.59  ?  93  TYR B CE2 1 
ATOM 2344 C CZ  . TYR B 2 93  ? 21.252  11.133  45.303  1.00 47.46  ?  93  TYR B CZ  1 
ATOM 2345 O OH  . TYR B 2 93  ? 20.287  12.096  45.479  1.00 58.21  ?  93  TYR B OH  1 
ATOM 2346 N N   . TYR B 2 94  ? 26.874  7.744   42.641  1.00 51.32  ?  94  TYR B N   1 
ATOM 2347 C CA  . TYR B 2 94  ? 28.179  7.176   42.343  1.00 53.67  ?  94  TYR B CA  1 
ATOM 2348 C C   . TYR B 2 94  ? 29.216  7.761   43.287  1.00 48.79  ?  94  TYR B C   1 
ATOM 2349 O O   . TYR B 2 94  ? 29.182  8.954   43.612  1.00 52.27  ?  94  TYR B O   1 
ATOM 2350 C CB  . TYR B 2 94  ? 28.631  7.473   40.896  1.00 50.74  ?  94  TYR B CB  1 
ATOM 2351 C CG  . TYR B 2 94  ? 27.824  6.827   39.788  1.00 52.46  ?  94  TYR B CG  1 
ATOM 2352 C CD1 . TYR B 2 94  ? 26.805  7.524   39.154  1.00 55.85  ?  94  TYR B CD1 1 
ATOM 2353 C CD2 . TYR B 2 94  ? 28.103  5.536   39.353  1.00 51.38  ?  94  TYR B CD2 1 
ATOM 2354 C CE1 . TYR B 2 94  ? 26.071  6.949   38.132  1.00 58.90  ?  94  TYR B CE1 1 
ATOM 2355 C CE2 . TYR B 2 94  ? 27.374  4.949   38.325  1.00 52.55  ?  94  TYR B CE2 1 
ATOM 2356 C CZ  . TYR B 2 94  ? 26.356  5.663   37.720  1.00 55.85  ?  94  TYR B CZ  1 
ATOM 2357 O OH  . TYR B 2 94  ? 25.612  5.107   36.701  1.00 47.88  ?  94  TYR B OH  1 
ATOM 2358 N N   . CYS B 2 95  ? 30.146  6.910   43.691  1.00 53.79  ?  95  CYS B N   1 
ATOM 2359 C CA  . CYS B 2 95  ? 31.303  7.275   44.491  1.00 53.11  ?  95  CYS B CA  1 
ATOM 2360 C C   . CYS B 2 95  ? 32.512  7.334   43.569  1.00 50.09  ?  95  CYS B C   1 
ATOM 2361 O O   . CYS B 2 95  ? 32.716  6.425   42.759  1.00 55.05  ?  95  CYS B O   1 
ATOM 2362 C CB  . CYS B 2 95  ? 31.508  6.237   45.596  1.00 48.65  ?  95  CYS B CB  1 
ATOM 2363 S SG  . CYS B 2 95  ? 33.094  6.269   46.419  1.00 69.55  ?  95  CYS B SG  1 
ATOM 2364 N N   . ALA B 2 96  ? 33.285  8.414   43.650  1.00 43.60  ?  96  ALA B N   1 
ATOM 2365 C CA  . ALA B 2 96  ? 34.386  8.594   42.714  1.00 47.44  ?  96  ALA B CA  1 
ATOM 2366 C C   . ALA B 2 96  ? 35.611  9.166   43.415  1.00 53.21  ?  96  ALA B C   1 
ATOM 2367 O O   . ALA B 2 96  ? 35.506  9.920   44.389  1.00 52.76  ?  96  ALA B O   1 
ATOM 2368 C CB  . ALA B 2 96  ? 33.980  9.491   41.542  1.00 49.36  ?  96  ALA B CB  1 
ATOM 2369 N N   . ARG B 2 97  ? 36.779  8.808   42.889  1.00 48.55  ?  97  ARG B N   1 
ATOM 2370 C CA  . ARG B 2 97  ? 38.064  9.256   43.402  1.00 54.05  ?  97  ARG B CA  1 
ATOM 2371 C C   . ARG B 2 97  ? 38.611  10.322  42.467  1.00 57.97  ?  97  ARG B C   1 
ATOM 2372 O O   . ARG B 2 97  ? 38.676  10.114  41.252  1.00 61.79  ?  97  ARG B O   1 
ATOM 2373 C CB  . ARG B 2 97  ? 39.047  8.086   43.503  1.00 52.05  ?  97  ARG B CB  1 
ATOM 2374 C CG  . ARG B 2 97  ? 40.345  8.407   44.231  1.00 59.86  ?  97  ARG B CG  1 
ATOM 2375 C CD  . ARG B 2 97  ? 41.559  8.038   43.404  1.00 61.19  ?  97  ARG B CD  1 
ATOM 2376 N NE  . ARG B 2 97  ? 41.668  6.602   43.173  1.00 68.35  ?  97  ARG B NE  1 
ATOM 2377 C CZ  . ARG B 2 97  ? 42.664  6.031   42.502  1.00 70.66  ?  97  ARG B CZ  1 
ATOM 2378 N NH1 . ARG B 2 97  ? 42.686  4.719   42.330  1.00 71.56  ?  97  ARG B NH1 1 
ATOM 2379 N NH2 . ARG B 2 97  ? 43.641  6.772   42.000  1.00 73.25  ?  97  ARG B NH2 1 
ATOM 2380 N N   . GLU B 2 98  ? 38.977  11.467  43.028  1.00 61.40  ?  98  GLU B N   1 
ATOM 2381 C CA  . GLU B 2 98  ? 39.499  12.578  42.251  1.00 60.62  ?  98  GLU B CA  1 
ATOM 2382 C C   . GLU B 2 98  ? 41.008  12.661  42.417  1.00 66.17  ?  98  GLU B C   1 
ATOM 2383 O O   . GLU B 2 98  ? 41.516  12.613  43.542  1.00 77.00  ?  98  GLU B O   1 
ATOM 2384 C CB  . GLU B 2 98  ? 38.833  13.888  42.671  1.00 62.81  ?  98  GLU B CB  1 
ATOM 2385 C CG  . GLU B 2 98  ? 39.238  15.075  41.826  1.00 75.07  ?  98  GLU B CG  1 
ATOM 2386 C CD  . GLU B 2 98  ? 38.432  16.310  42.149  1.00 80.28  ?  98  GLU B CD  1 
ATOM 2387 O OE1 . GLU B 2 98  ? 37.551  16.222  43.035  1.00 73.52  ?  98  GLU B OE1 1 
ATOM 2388 O OE2 . GLU B 2 98  ? 38.669  17.357  41.505  1.00 89.17  ?  98  GLU B OE2 1 
ATOM 2389 N N   . ASP B 2 99  ? 41.718  12.755  41.300  1.00 69.23  ?  99  ASP B N   1 
ATOM 2390 C CA  . ASP B 2 99  ? 43.176  12.846  41.274  1.00 76.02  ?  99  ASP B CA  1 
ATOM 2391 C C   . ASP B 2 99  ? 43.509  14.284  40.868  1.00 80.31  ?  99  ASP B C   1 
ATOM 2392 O O   . ASP B 2 99  ? 43.702  14.583  39.689  1.00 77.38  ?  99  ASP B O   1 
ATOM 2393 C CB  . ASP B 2 99  ? 43.769  11.801  40.322  1.00 76.60  ?  99  ASP B CB  1 
ATOM 2394 C CG  . ASP B 2 99  ? 45.278  11.670  40.450  1.00 82.71  ?  99  ASP B CG  1 
ATOM 2395 O OD1 . ASP B 2 99  ? 45.969  12.702  40.569  1.00 85.11  ?  99  ASP B OD1 1 
ATOM 2396 O OD2 . ASP B 2 99  ? 45.772  10.522  40.454  1.00 83.50  ?  99  ASP B OD2 1 
ATOM 2397 N N   . VAL B 2 100 ? 43.577  15.174  41.864  1.00 87.69  ?  100 VAL B N   1 
ATOM 2398 C CA  . VAL B 2 100 ? 43.846  16.590  41.612  1.00 87.09  ?  100 VAL B CA  1 
ATOM 2399 C C   . VAL B 2 100 ? 45.329  16.892  41.430  1.00 86.80  ?  100 VAL B C   1 
ATOM 2400 O O   . VAL B 2 100 ? 45.674  17.940  40.871  1.00 86.17  ?  100 VAL B O   1 
ATOM 2401 C CB  . VAL B 2 100 ? 43.303  17.461  42.760  1.00 79.92  ?  100 VAL B CB  1 
ATOM 2402 C CG1 . VAL B 2 100 ? 43.048  18.890  42.285  1.00 84.03  ?  100 VAL B CG1 1 
ATOM 2403 C CG2 . VAL B 2 100 ? 42.042  16.851  43.352  1.00 72.25  ?  100 VAL B CG2 1 
ATOM 2404 N N   . ALA B 2 101 ? 46.218  16.005  41.878  1.00 91.25  ?  101 ALA B N   1 
ATOM 2405 C CA  . ALA B 2 101 ? 47.649  16.267  41.784  1.00 92.52  ?  101 ALA B CA  1 
ATOM 2406 C C   . ALA B 2 101 ? 48.238  15.938  40.417  1.00 96.62  ?  101 ALA B C   1 
ATOM 2407 O O   . ALA B 2 101 ? 49.336  16.414  40.104  1.00 98.33  ?  101 ALA B O   1 
ATOM 2408 C CB  . ALA B 2 101 ? 48.396  15.471  42.858  1.00 90.03  ?  101 ALA B CB  1 
ATOM 2409 N N   . VAL B 2 102 ? 47.544  15.151  39.596  1.00 88.14  ?  102 VAL B N   1 
ATOM 2410 C CA  . VAL B 2 102 ? 48.092  14.722  38.313  1.00 88.24  ?  102 VAL B CA  1 
ATOM 2411 C C   . VAL B 2 102 ? 47.084  14.930  37.190  1.00 89.06  ?  102 VAL B C   1 
ATOM 2412 O O   . VAL B 2 102 ? 47.319  15.711  36.261  1.00 86.67  ?  102 VAL B O   1 
ATOM 2413 C CB  . VAL B 2 102 ? 48.541  13.249  38.370  1.00 85.85  ?  102 VAL B CB  1 
ATOM 2414 C CG1 . VAL B 2 102 ? 48.947  12.763  36.987  1.00 85.19  ?  102 VAL B CG1 1 
ATOM 2415 C CG2 . VAL B 2 102 ? 49.689  13.078  39.354  1.00 85.06  ?  102 VAL B CG2 1 
ATOM 2416 N N   . TYR B 2 103 ? 45.947  14.242  37.279  1.00 90.75  ?  103 TYR B N   1 
ATOM 2417 C CA  . TYR B 2 103 ? 44.982  14.223  36.186  1.00 78.06  ?  103 TYR B CA  1 
ATOM 2418 C C   . TYR B 2 103 ? 44.063  15.438  36.198  1.00 78.79  ?  103 TYR B C   1 
ATOM 2419 O O   . TYR B 2 103 ? 43.584  15.851  35.136  1.00 78.51  ?  103 TYR B O   1 
ATOM 2420 C CB  . TYR B 2 103 ? 44.139  12.949  36.270  1.00 73.91  ?  103 TYR B CB  1 
ATOM 2421 C CG  . TYR B 2 103 ? 44.870  11.680  35.887  1.00 82.58  ?  103 TYR B CG  1 
ATOM 2422 C CD1 . TYR B 2 103 ? 44.707  11.111  34.631  1.00 84.45  ?  103 TYR B CD1 1 
ATOM 2423 C CD2 . TYR B 2 103 ? 45.714  11.040  36.790  1.00 88.09  ?  103 TYR B CD2 1 
ATOM 2424 C CE1 . TYR B 2 103 ? 45.369  9.946   34.278  1.00 86.56  ?  103 TYR B CE1 1 
ATOM 2425 C CE2 . TYR B 2 103 ? 46.380  9.874   36.447  1.00 91.07  ?  103 TYR B CE2 1 
ATOM 2426 C CZ  . TYR B 2 103 ? 46.203  9.333   35.189  1.00 94.45  ?  103 TYR B CZ  1 
ATOM 2427 O OH  . TYR B 2 103 ? 46.859  8.176   34.836  1.00 106.01 ?  103 TYR B OH  1 
ATOM 2428 N N   . MET B 2 104 ? 43.805  16.013  37.375  1.00 78.84  ?  104 MET B N   1 
ATOM 2429 C CA  . MET B 2 104 ? 42.763  17.027  37.547  1.00 75.09  ?  104 MET B CA  1 
ATOM 2430 C C   . MET B 2 104 ? 41.421  16.513  37.025  1.00 71.26  ?  104 MET B C   1 
ATOM 2431 O O   . MET B 2 104 ? 40.625  17.254  36.446  1.00 75.54  ?  104 MET B O   1 
ATOM 2432 C CB  . MET B 2 104 ? 43.147  18.353  36.880  1.00 79.75  ?  104 MET B CB  1 
ATOM 2433 C CG  . MET B 2 104 ? 44.301  19.095  37.549  1.00 80.27  ?  104 MET B CG  1 
ATOM 2434 S SD  . MET B 2 104 ? 45.925  18.417  37.157  1.00 90.31  ?  104 MET B SD  1 
ATOM 2435 C CE  . MET B 2 104 ? 46.999  19.560  38.025  1.00 73.53  ?  104 MET B CE  1 
ATOM 2436 N N   . ALA B 2 105 ? 41.172  15.223  37.234  1.00 71.49  ?  105 ALA B N   1 
ATOM 2437 C CA  . ALA B 2 105 ? 39.978  14.563  36.726  1.00 66.62  ?  105 ALA B CA  1 
ATOM 2438 C C   . ALA B 2 105 ? 39.590  13.453  37.696  1.00 64.40  ?  105 ALA B C   1 
ATOM 2439 O O   . ALA B 2 105 ? 40.134  13.348  38.799  1.00 63.46  ?  105 ALA B O   1 
ATOM 2440 C CB  . ALA B 2 105 ? 40.217  14.026  35.309  1.00 66.13  ?  105 ALA B CB  1 
ATOM 2441 N N   . ILE B 2 106 ? 38.658  12.607  37.273  1.00 62.71  ?  106 ILE B N   1 
ATOM 2442 C CA  . ILE B 2 106 ? 38.173  11.489  38.073  1.00 55.09  ?  106 ILE B CA  1 
ATOM 2443 C C   . ILE B 2 106 ? 38.691  10.219  37.418  1.00 56.47  ?  106 ILE B C   1 
ATOM 2444 O O   . ILE B 2 106 ? 38.298  9.890   36.292  1.00 58.85  ?  106 ILE B O   1 
ATOM 2445 C CB  . ILE B 2 106 ? 36.643  11.484  38.169  1.00 47.65  ?  106 ILE B CB  1 
ATOM 2446 C CG1 . ILE B 2 106 ? 36.154  12.755  38.868  1.00 47.94  ?  106 ILE B CG1 1 
ATOM 2447 C CG2 . ILE B 2 106 ? 36.162  10.260  38.892  1.00 46.79  ?  106 ILE B CG2 1 
ATOM 2448 C CD1 . ILE B 2 106 ? 34.645  12.853  38.964  1.00 37.78  ?  106 ILE B CD1 1 
ATOM 2449 N N   . ASP B 2 107 ? 39.573  9.500   38.115  1.00 55.24  ?  107 ASP B N   1 
ATOM 2450 C CA  . ASP B 2 107 ? 40.213  8.325   37.543  1.00 51.39  ?  107 ASP B CA  1 
ATOM 2451 C C   . ASP B 2 107 ? 39.614  7.015   38.027  1.00 52.77  ?  107 ASP B C   1 
ATOM 2452 O O   . ASP B 2 107 ? 39.949  5.966   37.472  1.00 62.46  ?  107 ASP B O   1 
ATOM 2453 C CB  . ASP B 2 107 ? 41.716  8.330   37.846  1.00 51.08  ?  107 ASP B CB  1 
ATOM 2454 C CG  . ASP B 2 107 ? 42.013  8.209   39.324  1.00 67.34  ?  107 ASP B CG  1 
ATOM 2455 O OD1 . ASP B 2 107 ? 43.131  7.778   39.671  1.00 71.85  ?  107 ASP B OD1 1 
ATOM 2456 O OD2 . ASP B 2 107 ? 41.120  8.508   40.142  1.00 69.30  ?  107 ASP B OD2 1 
ATOM 2457 N N   . LEU B 2 108 ? 38.743  7.045   39.034  1.00 50.27  ?  108 LEU B N   1 
ATOM 2458 C CA  . LEU B 2 108 ? 38.187  5.822   39.598  1.00 52.26  ?  108 LEU B CA  1 
ATOM 2459 C C   . LEU B 2 108 ? 36.749  6.069   40.024  1.00 48.76  ?  108 LEU B C   1 
ATOM 2460 O O   . LEU B 2 108 ? 36.466  7.068   40.680  1.00 55.51  ?  108 LEU B O   1 
ATOM 2461 C CB  . LEU B 2 108 ? 39.020  5.345   40.792  1.00 54.34  ?  108 LEU B CB  1 
ATOM 2462 C CG  . LEU B 2 108 ? 38.476  4.103   41.496  1.00 56.91  ?  108 LEU B CG  1 
ATOM 2463 C CD1 . LEU B 2 108 ? 38.348  2.970   40.506  1.00 64.07  ?  108 LEU B CD1 1 
ATOM 2464 C CD2 . LEU B 2 108 ? 39.357  3.697   42.666  1.00 56.35  ?  108 LEU B CD2 1 
ATOM 2465 N N   . TRP B 2 109 ? 35.850  5.169   39.650  1.00 47.64  ?  109 TRP B N   1 
ATOM 2466 C CA  . TRP B 2 109 ? 34.445  5.237   40.024  1.00 45.06  ?  109 TRP B CA  1 
ATOM 2467 C C   . TRP B 2 109 ? 34.027  3.946   40.712  1.00 53.11  ?  109 TRP B C   1 
ATOM 2468 O O   . TRP B 2 109 ? 34.791  2.983   40.808  1.00 63.63  ?  109 TRP B O   1 
ATOM 2469 C CB  . TRP B 2 109 ? 33.550  5.460   38.802  1.00 46.67  ?  109 TRP B CB  1 
ATOM 2470 C CG  . TRP B 2 109 ? 33.800  6.719   38.050  1.00 44.96  ?  109 TRP B CG  1 
ATOM 2471 C CD1 . TRP B 2 109 ? 34.905  7.024   37.310  1.00 46.48  ?  109 TRP B CD1 1 
ATOM 2472 C CD2 . TRP B 2 109 ? 32.896  7.819   37.892  1.00 49.36  ?  109 TRP B CD2 1 
ATOM 2473 N NE1 . TRP B 2 109 ? 34.761  8.258   36.730  1.00 50.94  ?  109 TRP B NE1 1 
ATOM 2474 C CE2 . TRP B 2 109 ? 33.535  8.769   37.071  1.00 54.15  ?  109 TRP B CE2 1 
ATOM 2475 C CE3 . TRP B 2 109 ? 31.617  8.103   38.382  1.00 52.93  ?  109 TRP B CE3 1 
ATOM 2476 C CZ2 . TRP B 2 109 ? 32.938  9.985   36.728  1.00 54.50  ?  109 TRP B CZ2 1 
ATOM 2477 C CZ3 . TRP B 2 109 ? 31.024  9.309   38.038  1.00 54.83  ?  109 TRP B CZ3 1 
ATOM 2478 C CH2 . TRP B 2 109 ? 31.684  10.233  37.218  1.00 50.97  ?  109 TRP B CH2 1 
ATOM 2479 N N   . GLY B 2 110 ? 32.778  3.930   41.179  1.00 49.44  ?  110 GLY B N   1 
ATOM 2480 C CA  . GLY B 2 110 ? 32.139  2.716   41.623  1.00 51.13  ?  110 GLY B CA  1 
ATOM 2481 C C   . GLY B 2 110 ? 30.843  2.508   40.855  1.00 58.56  ?  110 GLY B C   1 
ATOM 2482 O O   . GLY B 2 110 ? 30.361  3.403   40.149  1.00 62.16  ?  110 GLY B O   1 
ATOM 2483 N N   . GLN B 2 111 ? 30.309  1.296   40.957  1.00 55.72  ?  111 GLN B N   1 
ATOM 2484 C CA  . GLN B 2 111 ? 28.978  1.054   40.427  1.00 48.62  ?  111 GLN B CA  1 
ATOM 2485 C C   . GLN B 2 111 ? 27.996  1.866   41.253  1.00 59.15  ?  111 GLN B C   1 
ATOM 2486 O O   . GLN B 2 111 ? 28.200  2.080   42.452  1.00 67.45  ?  111 GLN B O   1 
ATOM 2487 C CB  . GLN B 2 111 ? 28.627  -0.435  40.463  1.00 53.96  ?  111 GLN B CB  1 
ATOM 2488 C CG  . GLN B 2 111 ? 27.836  -0.910  41.687  1.00 56.97  ?  111 GLN B CG  1 
ATOM 2489 C CD  . GLN B 2 111 ? 28.618  -0.831  42.985  1.00 57.18  ?  111 GLN B CD  1 
ATOM 2490 O OE1 . GLN B 2 111 ? 29.837  -0.659  42.980  1.00 61.79  ?  111 GLN B OE1 1 
ATOM 2491 N NE2 . GLN B 2 111 ? 27.917  -0.957  44.107  1.00 53.38  ?  111 GLN B NE2 1 
ATOM 2492 N N   . GLY B 2 112 ? 26.971  2.373   40.613  1.00 56.62  ?  112 GLY B N   1 
ATOM 2493 C CA  . GLY B 2 112 ? 26.053  3.235   41.321  1.00 61.86  ?  112 GLY B CA  1 
ATOM 2494 C C   . GLY B 2 112 ? 25.105  2.469   42.224  1.00 62.20  ?  112 GLY B C   1 
ATOM 2495 O O   . GLY B 2 112 ? 24.982  1.246   42.155  1.00 61.23  ?  112 GLY B O   1 
ATOM 2496 N N   . THR B 2 113 ? 24.446  3.204   43.116  1.00 61.00  ?  113 THR B N   1 
ATOM 2497 C CA  . THR B 2 113 ? 23.323  2.662   43.869  1.00 57.57  ?  113 THR B CA  1 
ATOM 2498 C C   . THR B 2 113 ? 22.111  3.552   43.640  1.00 57.07  ?  113 THR B C   1 
ATOM 2499 O O   . THR B 2 113 ? 22.224  4.780   43.654  1.00 57.72  ?  113 THR B O   1 
ATOM 2500 C CB  . THR B 2 113 ? 23.621  2.546   45.372  1.00 62.93  ?  113 THR B CB  1 
ATOM 2501 O OG1 . THR B 2 113 ? 24.431  3.650   45.803  1.00 62.88  ?  113 THR B OG1 1 
ATOM 2502 C CG2 . THR B 2 113 ? 24.331  1.229   45.677  1.00 64.28  ?  113 THR B CG2 1 
ATOM 2503 N N   . LEU B 2 114 ? 20.960  2.934   43.399  1.00 54.16  ?  114 LEU B N   1 
ATOM 2504 C CA  . LEU B 2 114 ? 19.746  3.670   43.075  1.00 53.60  ?  114 LEU B CA  1 
ATOM 2505 C C   . LEU B 2 114 ? 19.005  4.036   44.353  1.00 55.11  ?  114 LEU B C   1 
ATOM 2506 O O   . LEU B 2 114 ? 18.588  3.153   45.108  1.00 59.29  ?  114 LEU B O   1 
ATOM 2507 C CB  . LEU B 2 114 ? 18.841  2.857   42.153  1.00 57.40  ?  114 LEU B CB  1 
ATOM 2508 C CG  . LEU B 2 114 ? 17.526  3.559   41.802  1.00 58.26  ?  114 LEU B CG  1 
ATOM 2509 C CD1 . LEU B 2 114 ? 17.779  4.791   40.947  1.00 55.74  ?  114 LEU B CD1 1 
ATOM 2510 C CD2 . LEU B 2 114 ? 16.582  2.613   41.088  1.00 56.52  ?  114 LEU B CD2 1 
ATOM 2511 N N   . VAL B 2 115 ? 18.826  5.333   44.579  1.00 59.50  ?  115 VAL B N   1 
ATOM 2512 C CA  . VAL B 2 115 ? 18.016  5.856   45.670  1.00 52.34  ?  115 VAL B CA  1 
ATOM 2513 C C   . VAL B 2 115 ? 16.710  6.347   45.061  1.00 51.12  ?  115 VAL B C   1 
ATOM 2514 O O   . VAL B 2 115 ? 16.714  7.201   44.164  1.00 49.35  ?  115 VAL B O   1 
ATOM 2515 C CB  . VAL B 2 115 ? 18.743  6.985   46.419  1.00 52.50  ?  115 VAL B CB  1 
ATOM 2516 C CG1 . VAL B 2 115 ? 17.863  7.548   47.527  1.00 57.68  ?  115 VAL B CG1 1 
ATOM 2517 C CG2 . VAL B 2 115 ? 20.069  6.489   46.978  1.00 50.53  ?  115 VAL B CG2 1 
ATOM 2518 N N   . THR B 2 116 ? 15.600  5.768   45.511  1.00 49.70  ?  116 THR B N   1 
ATOM 2519 C CA  . THR B 2 116 ? 14.265  6.114   45.041  1.00 55.07  ?  116 THR B CA  1 
ATOM 2520 C C   . THR B 2 116 ? 13.505  6.780   46.179  1.00 54.74  ?  116 THR B C   1 
ATOM 2521 O O   . THR B 2 116 ? 13.215  6.138   47.193  1.00 56.70  ?  116 THR B O   1 
ATOM 2522 C CB  . THR B 2 116 ? 13.512  4.876   44.550  1.00 50.87  ?  116 THR B CB  1 
ATOM 2523 O OG1 . THR B 2 116 ? 14.232  4.276   43.468  1.00 60.96  ?  116 THR B OG1 1 
ATOM 2524 C CG2 . THR B 2 116 ? 12.112  5.247   44.074  1.00 46.16  ?  116 THR B CG2 1 
ATOM 2525 N N   . VAL B 2 117 ? 13.172  8.051   46.004  1.00 54.42  ?  117 VAL B N   1 
ATOM 2526 C CA  . VAL B 2 117 ? 12.400  8.802   46.985  1.00 62.54  ?  117 VAL B CA  1 
ATOM 2527 C C   . VAL B 2 117 ? 10.954  8.797   46.510  1.00 55.02  ?  117 VAL B C   1 
ATOM 2528 O O   . VAL B 2 117 ? 10.611  9.452   45.522  1.00 59.80  ?  117 VAL B O   1 
ATOM 2529 C CB  . VAL B 2 117 ? 12.937  10.230  47.163  1.00 69.31  ?  117 VAL B CB  1 
ATOM 2530 C CG1 . VAL B 2 117 ? 12.175  10.957  48.267  1.00 70.15  ?  117 VAL B CG1 1 
ATOM 2531 C CG2 . VAL B 2 117 ? 14.426  10.201  47.476  1.00 64.15  ?  117 VAL B CG2 1 
ATOM 2532 N N   . SER B 2 118 ? 10.107  8.054   47.216  1.00 57.68  ?  118 SER B N   1 
ATOM 2533 C CA  . SER B 2 118 ? 8.705   7.914   46.854  1.00 60.01  ?  118 SER B CA  1 
ATOM 2534 C C   . SER B 2 118 ? 7.907   7.521   48.086  1.00 69.62  ?  118 SER B C   1 
ATOM 2535 O O   . SER B 2 118 ? 8.448   6.988   49.060  1.00 70.08  ?  118 SER B O   1 
ATOM 2536 C CB  . SER B 2 118 ? 8.507   6.866   45.754  1.00 58.25  ?  118 SER B CB  1 
ATOM 2537 O OG  . SER B 2 118 ? 7.168   6.399   45.743  1.00 57.99  ?  118 SER B OG  1 
ATOM 2538 N N   . SER B 2 119 ? 6.606   7.793   48.026  1.00 72.05  ?  119 SER B N   1 
ATOM 2539 C CA  . SER B 2 119 ? 5.698   7.427   49.102  1.00 74.44  ?  119 SER B CA  1 
ATOM 2540 C C   . SER B 2 119 ? 5.076   6.049   48.914  1.00 71.88  ?  119 SER B C   1 
ATOM 2541 O O   . SER B 2 119 ? 4.391   5.566   49.823  1.00 71.63  ?  119 SER B O   1 
ATOM 2542 C CB  . SER B 2 119 ? 4.594   8.482   49.227  1.00 77.29  ?  119 SER B CB  1 
ATOM 2543 O OG  . SER B 2 119 ? 3.933   8.663   47.985  1.00 82.74  ?  119 SER B OG  1 
ATOM 2544 N N   . ALA B 2 120 ? 5.316   5.399   47.776  1.00 72.99  ?  120 ALA B N   1 
ATOM 2545 C CA  . ALA B 2 120 ? 4.818   4.051   47.544  1.00 67.77  ?  120 ALA B CA  1 
ATOM 2546 C C   . ALA B 2 120 ? 5.520   3.054   48.465  1.00 70.36  ?  120 ALA B C   1 
ATOM 2547 O O   . ALA B 2 120 ? 6.530   3.357   49.109  1.00 72.35  ?  120 ALA B O   1 
ATOM 2548 C CB  . ALA B 2 120 ? 5.010   3.653   46.084  1.00 69.32  ?  120 ALA B CB  1 
ATOM 2549 N N   . SER B 2 121 ? 4.957   1.852   48.544  1.00 66.99  ?  121 SER B N   1 
ATOM 2550 C CA  . SER B 2 121 ? 5.514   0.800   49.381  1.00 65.20  ?  121 SER B CA  1 
ATOM 2551 C C   . SER B 2 121 ? 6.234   -0.249  48.538  1.00 67.79  ?  121 SER B C   1 
ATOM 2552 O O   . SER B 2 121 ? 5.914   -0.475  47.367  1.00 65.72  ?  121 SER B O   1 
ATOM 2553 C CB  . SER B 2 121 ? 4.427   0.140   50.232  1.00 59.40  ?  121 SER B CB  1 
ATOM 2554 O OG  . SER B 2 121 ? 3.300   -0.210  49.449  1.00 73.78  ?  121 SER B OG  1 
ATOM 2555 N N   . THR B 2 122 ? 7.226   -0.878  49.160  1.00 66.68  ?  122 THR B N   1 
ATOM 2556 C CA  . THR B 2 122 ? 8.025   -1.913  48.520  1.00 62.18  ?  122 THR B CA  1 
ATOM 2557 C C   . THR B 2 122 ? 7.197   -3.165  48.246  1.00 67.35  ?  122 THR B C   1 
ATOM 2558 O O   . THR B 2 122 ? 6.432   -3.617  49.106  1.00 67.22  ?  122 THR B O   1 
ATOM 2559 C CB  . THR B 2 122 ? 9.224   -2.253  49.404  1.00 64.41  ?  122 THR B CB  1 
ATOM 2560 O OG1 . THR B 2 122 ? 10.096  -1.120  49.480  1.00 77.80  ?  122 THR B OG1 1 
ATOM 2561 C CG2 . THR B 2 122 ? 9.995   -3.409  48.831  1.00 65.94  ?  122 THR B CG2 1 
ATOM 2562 N N   . LYS B 2 123 ? 7.341   -3.718  47.039  1.00 62.29  ?  123 LYS B N   1 
ATOM 2563 C CA  . LYS B 2 123 ? 6.635   -4.928  46.638  1.00 61.34  ?  123 LYS B CA  1 
ATOM 2564 C C   . LYS B 2 123 ? 7.594   -5.834  45.879  1.00 60.65  ?  123 LYS B C   1 
ATOM 2565 O O   . LYS B 2 123 ? 8.355   -5.369  45.026  1.00 63.13  ?  123 LYS B O   1 
ATOM 2566 C CB  . LYS B 2 123 ? 5.414   -4.625  45.760  1.00 59.43  ?  123 LYS B CB  1 
ATOM 2567 C CG  . LYS B 2 123 ? 4.662   -5.874  45.310  1.00 54.61  ?  123 LYS B CG  1 
ATOM 2568 C CD  . LYS B 2 123 ? 3.315   -5.528  44.700  1.00 60.49  ?  123 LYS B CD  1 
ATOM 2569 C CE  . LYS B 2 123 ? 2.449   -6.769  44.517  1.00 62.37  ?  123 LYS B CE  1 
ATOM 2570 N NZ  . LYS B 2 123 ? 3.052   -7.760  43.573  1.00 64.13  ?  123 LYS B NZ  1 
ATOM 2571 N N   . GLY B 2 124 ? 7.560   -7.124  46.205  1.00 56.59  ?  124 GLY B N   1 
ATOM 2572 C CA  . GLY B 2 124 ? 8.340   -8.120  45.512  1.00 55.57  ?  124 GLY B CA  1 
ATOM 2573 C C   . GLY B 2 124 ? 7.752   -8.519  44.174  1.00 57.08  ?  124 GLY B C   1 
ATOM 2574 O O   . GLY B 2 124 ? 6.553   -8.367  43.921  1.00 59.36  ?  124 GLY B O   1 
ATOM 2575 N N   . PRO B 2 125 ? 8.594   -9.046  43.288  1.00 57.51  ?  125 PRO B N   1 
ATOM 2576 C CA  . PRO B 2 125 ? 8.148   -9.396  41.938  1.00 57.59  ?  125 PRO B CA  1 
ATOM 2577 C C   . PRO B 2 125 ? 7.562   -10.796 41.831  1.00 55.95  ?  125 PRO B C   1 
ATOM 2578 O O   . PRO B 2 125 ? 7.905   -11.712 42.580  1.00 50.79  ?  125 PRO B O   1 
ATOM 2579 C CB  . PRO B 2 125 ? 9.450   -9.308  41.132  1.00 58.33  ?  125 PRO B CB  1 
ATOM 2580 C CG  . PRO B 2 125 ? 10.492  -9.755  42.109  1.00 49.80  ?  125 PRO B CG  1 
ATOM 2581 C CD  . PRO B 2 125 ? 10.045  -9.246  43.459  1.00 59.00  ?  125 PRO B CD  1 
ATOM 2582 N N   . SER B 2 126 ? 6.673   -10.952 40.853  1.00 56.96  ?  126 SER B N   1 
ATOM 2583 C CA  . SER B 2 126 ? 6.199   -12.260 40.417  1.00 62.34  ?  126 SER B CA  1 
ATOM 2584 C C   . SER B 2 126 ? 6.986   -12.682 39.181  1.00 59.44  ?  126 SER B C   1 
ATOM 2585 O O   . SER B 2 126 ? 7.114   -11.908 38.228  1.00 59.35  ?  126 SER B O   1 
ATOM 2586 C CB  . SER B 2 126 ? 4.701   -12.235 40.109  1.00 62.15  ?  126 SER B CB  1 
ATOM 2587 O OG  . SER B 2 126 ? 3.939   -12.061 41.289  1.00 61.83  ?  126 SER B OG  1 
ATOM 2588 N N   . VAL B 2 127 ? 7.511   -13.903 39.196  1.00 58.62  ?  127 VAL B N   1 
ATOM 2589 C CA  . VAL B 2 127 ? 8.383   -14.396 38.135  1.00 58.92  ?  127 VAL B CA  1 
ATOM 2590 C C   . VAL B 2 127 ? 7.679   -15.559 37.448  1.00 60.67  ?  127 VAL B C   1 
ATOM 2591 O O   . VAL B 2 127 ? 7.576   -16.656 38.014  1.00 67.08  ?  127 VAL B O   1 
ATOM 2592 C CB  . VAL B 2 127 ? 9.756   -14.815 38.672  1.00 59.52  ?  127 VAL B CB  1 
ATOM 2593 C CG1 . VAL B 2 127 ? 10.658  -15.248 37.531  1.00 58.45  ?  127 VAL B CG1 1 
ATOM 2594 C CG2 . VAL B 2 127 ? 10.387  -13.664 39.446  1.00 52.67  ?  127 VAL B CG2 1 
ATOM 2595 N N   . PHE B 2 128 ? 7.205   -15.326 36.222  1.00 61.56  ?  128 PHE B N   1 
ATOM 2596 C CA  . PHE B 2 128 ? 6.529   -16.341 35.431  1.00 63.56  ?  128 PHE B CA  1 
ATOM 2597 C C   . PHE B 2 128 ? 7.445   -16.850 34.319  1.00 64.20  ?  128 PHE B C   1 
ATOM 2598 O O   . PHE B 2 128 ? 8.352   -16.135 33.881  1.00 63.54  ?  128 PHE B O   1 
ATOM 2599 C CB  . PHE B 2 128 ? 5.237   -15.788 34.818  1.00 63.19  ?  128 PHE B CB  1 
ATOM 2600 C CG  . PHE B 2 128 ? 4.293   -15.217 35.829  1.00 69.34  ?  128 PHE B CG  1 
ATOM 2601 C CD1 . PHE B 2 128 ? 3.720   -16.028 36.797  1.00 77.50  ?  128 PHE B CD1 1 
ATOM 2602 C CD2 . PHE B 2 128 ? 3.972   -13.870 35.814  1.00 67.93  ?  128 PHE B CD2 1 
ATOM 2603 C CE1 . PHE B 2 128 ? 2.849   -15.501 37.740  1.00 73.81  ?  128 PHE B CE1 1 
ATOM 2604 C CE2 . PHE B 2 128 ? 3.100   -13.337 36.749  1.00 66.79  ?  128 PHE B CE2 1 
ATOM 2605 C CZ  . PHE B 2 128 ? 2.538   -14.152 37.712  1.00 68.51  ?  128 PHE B CZ  1 
ATOM 2606 N N   . PRO B 2 129 ? 7.236   -18.075 33.832  1.00 61.50  ?  129 PRO B N   1 
ATOM 2607 C CA  . PRO B 2 129 ? 8.121   -18.610 32.792  1.00 56.11  ?  129 PRO B CA  1 
ATOM 2608 C C   . PRO B 2 129 ? 7.649   -18.280 31.385  1.00 59.74  ?  129 PRO B C   1 
ATOM 2609 O O   . PRO B 2 129 ? 6.463   -18.358 31.057  1.00 64.81  ?  129 PRO B O   1 
ATOM 2610 C CB  . PRO B 2 129 ? 8.052   -20.121 33.040  1.00 56.06  ?  129 PRO B CB  1 
ATOM 2611 C CG  . PRO B 2 129 ? 6.653   -20.329 33.525  1.00 55.13  ?  129 PRO B CG  1 
ATOM 2612 C CD  . PRO B 2 129 ? 6.280   -19.091 34.311  1.00 65.36  ?  129 PRO B CD  1 
ATOM 2613 N N   . LEU B 2 130 ? 8.599   -17.869 30.548  1.00 56.61  ?  130 LEU B N   1 
ATOM 2614 C CA  . LEU B 2 130 ? 8.408   -17.778 29.106  1.00 61.56  ?  130 LEU B CA  1 
ATOM 2615 C C   . LEU B 2 130 ? 8.995   -19.071 28.551  1.00 61.79  ?  130 LEU B C   1 
ATOM 2616 O O   . LEU B 2 130 ? 10.198  -19.170 28.295  1.00 56.61  ?  130 LEU B O   1 
ATOM 2617 C CB  . LEU B 2 130 ? 9.086   -16.539 28.535  1.00 58.32  ?  130 LEU B CB  1 
ATOM 2618 C CG  . LEU B 2 130 ? 8.623   -15.213 29.136  1.00 58.64  ?  130 LEU B CG  1 
ATOM 2619 C CD1 . LEU B 2 130 ? 9.246   -14.041 28.398  1.00 51.38  ?  130 LEU B CD1 1 
ATOM 2620 C CD2 . LEU B 2 130 ? 7.100   -15.121 29.156  1.00 59.86  ?  130 LEU B CD2 1 
ATOM 2621 N N   . ALA B 2 131 ? 8.136   -20.091 28.428  1.00 63.50  ?  131 ALA B N   1 
ATOM 2622 C CA  . ALA B 2 131 ? 8.566   -21.459 28.179  1.00 58.29  ?  131 ALA B CA  1 
ATOM 2623 C C   . ALA B 2 131 ? 8.963   -21.649 26.718  1.00 61.07  ?  131 ALA B C   1 
ATOM 2624 O O   . ALA B 2 131 ? 8.308   -21.112 25.821  1.00 61.93  ?  131 ALA B O   1 
ATOM 2625 C CB  . ALA B 2 131 ? 7.456   -22.440 28.541  1.00 64.52  ?  131 ALA B CB  1 
ATOM 2626 N N   . PRO B 2 132 ? 10.037  -22.396 26.461  1.00 67.28  ?  132 PRO B N   1 
ATOM 2627 C CA  . PRO B 2 132 ? 10.395  -22.744 25.081  1.00 65.02  ?  132 PRO B CA  1 
ATOM 2628 C C   . PRO B 2 132 ? 9.397   -23.721 24.484  1.00 67.07  ?  132 PRO B C   1 
ATOM 2629 O O   . PRO B 2 132 ? 8.847   -24.581 25.174  1.00 75.50  ?  132 PRO B O   1 
ATOM 2630 C CB  . PRO B 2 132 ? 11.780  -23.383 25.224  1.00 62.27  ?  132 PRO B CB  1 
ATOM 2631 C CG  . PRO B 2 132 ? 11.797  -23.917 26.611  1.00 60.87  ?  132 PRO B CG  1 
ATOM 2632 C CD  . PRO B 2 132 ? 11.004  -22.934 27.432  1.00 61.84  ?  132 PRO B CD  1 
ATOM 2633 N N   . SER B 2 133 ? 9.175   -23.593 23.184  1.00 78.23  ?  133 SER B N   1 
ATOM 2634 C CA  . SER B 2 133 ? 8.185   -24.400 22.490  1.00 89.04  ?  133 SER B CA  1 
ATOM 2635 C C   . SER B 2 133 ? 8.875   -25.580 21.801  1.00 92.41  ?  133 SER B C   1 
ATOM 2636 O O   . SER B 2 133 ? 10.029  -25.911 22.094  1.00 86.16  ?  133 SER B O   1 
ATOM 2637 C CB  . SER B 2 133 ? 7.394   -23.530 21.505  1.00 91.16  ?  133 SER B CB  1 
ATOM 2638 O OG  . SER B 2 133 ? 8.158   -23.203 20.357  1.00 85.11  ?  133 SER B OG  1 
ATOM 2639 N N   . SER B 2 134 ? 8.152   -26.249 20.903  1.00 104.42 ?  134 SER B N   1 
ATOM 2640 C CA  . SER B 2 134 ? 8.665   -27.442 20.234  1.00 104.71 ?  134 SER B CA  1 
ATOM 2641 C C   . SER B 2 134 ? 9.787   -27.076 19.259  1.00 95.43  ?  134 SER B C   1 
ATOM 2642 O O   . SER B 2 134 ? 10.189  -25.914 19.128  1.00 98.55  ?  134 SER B O   1 
ATOM 2643 C CB  . SER B 2 134 ? 7.538   -28.162 19.498  1.00 98.09  ?  134 SER B CB  1 
ATOM 2644 O OG  . SER B 2 134 ? 8.042   -29.209 18.686  1.00 92.31  ?  134 SER B OG  1 
ATOM 2645 N N   . LYS B 2 135 ? 10.274  -28.078 18.525  1.00 91.26  ?  135 LYS B N   1 
ATOM 2646 C CA  . LYS B 2 135 ? 11.374  -27.816 17.606  1.00 95.53  ?  135 LYS B CA  1 
ATOM 2647 C C   . LYS B 2 135 ? 10.814  -27.261 16.302  1.00 95.52  ?  135 LYS B C   1 
ATOM 2648 O O   . LYS B 2 135 ? 11.079  -27.794 15.217  1.00 92.28  ?  135 LYS B O   1 
ATOM 2649 C CB  . LYS B 2 135 ? 12.215  -29.075 17.342  1.00 92.02  ?  135 LYS B CB  1 
ATOM 2650 C CG  . LYS B 2 135 ? 13.046  -29.547 18.531  1.00 90.09  ?  135 LYS B CG  1 
ATOM 2651 C CD  . LYS B 2 135 ? 14.112  -30.546 18.094  1.00 92.57  ?  135 LYS B CD  1 
ATOM 2652 C CE  . LYS B 2 135 ? 14.907  -31.080 19.280  1.00 89.40  ?  135 LYS B CE  1 
ATOM 2653 N NZ  . LYS B 2 135 ? 15.892  -32.136 18.888  1.00 78.54  ?  135 LYS B NZ  1 
ATOM 2654 N N   . SER B 2 136 ? 10.028  -26.185 16.414  1.00 90.68  ?  136 SER B N   1 
ATOM 2655 C CA  . SER B 2 136 ? 9.527   -25.414 15.284  1.00 87.49  ?  136 SER B CA  1 
ATOM 2656 C C   . SER B 2 136 ? 10.019  -23.974 15.372  1.00 90.78  ?  136 SER B C   1 
ATOM 2657 O O   . SER B 2 136 ? 9.390   -23.051 14.850  1.00 76.04  ?  136 SER B O   1 
ATOM 2658 C CB  . SER B 2 136 ? 7.999   -25.477 15.217  1.00 86.67  ?  136 SER B CB  1 
ATOM 2659 O OG  . SER B 2 136 ? 7.406   -24.912 16.377  1.00 97.44  ?  136 SER B OG  1 
ATOM 2660 N N   . THR B 2 137 ? 11.156  -23.792 16.031  1.00 93.33  ?  137 THR B N   1 
ATOM 2661 C CA  . THR B 2 137 ? 11.680  -22.493 16.437  1.00 88.96  ?  137 THR B CA  1 
ATOM 2662 C C   . THR B 2 137 ? 12.880  -22.140 15.561  1.00 84.44  ?  137 THR B C   1 
ATOM 2663 O O   . THR B 2 137 ? 14.024  -22.425 15.915  1.00 87.08  ?  137 THR B O   1 
ATOM 2664 C CB  . THR B 2 137 ? 12.060  -22.533 17.913  1.00 87.92  ?  137 THR B CB  1 
ATOM 2665 O OG1 . THR B 2 137 ? 12.764  -23.755 18.182  1.00 90.03  ?  137 THR B OG1 1 
ATOM 2666 C CG2 . THR B 2 137 ? 10.815  -22.475 18.785  1.00 87.96  ?  137 THR B CG2 1 
ATOM 2667 N N   . SER B 2 138 ? 12.602  -21.532 14.405  1.00 84.26  ?  138 SER B N   1 
ATOM 2668 C CA  . SER B 2 138 ? 13.609  -20.976 13.504  1.00 86.32  ?  138 SER B CA  1 
ATOM 2669 C C   . SER B 2 138 ? 14.870  -21.828 13.420  1.00 79.17  ?  138 SER B C   1 
ATOM 2670 O O   . SER B 2 138 ? 15.986  -21.296 13.493  1.00 84.36  ?  138 SER B O   1 
ATOM 2671 C CB  . SER B 2 138 ? 13.971  -19.539 13.939  1.00 88.90  ?  138 SER B CB  1 
ATOM 2672 O OG  . SER B 2 138 ? 14.989  -19.521 14.923  1.00 89.95  ?  138 SER B OG  1 
ATOM 2673 N N   . GLY B 2 139 ? 14.708  -23.137 13.290  1.00 70.15  ?  139 GLY B N   1 
ATOM 2674 C CA  . GLY B 2 139 ? 15.839  -24.025 13.098  1.00 69.08  ?  139 GLY B CA  1 
ATOM 2675 C C   . GLY B 2 139 ? 16.248  -24.729 14.382  1.00 70.78  ?  139 GLY B C   1 
ATOM 2676 O O   . GLY B 2 139 ? 15.399  -25.236 15.125  1.00 70.37  ?  139 GLY B O   1 
ATOM 2677 N N   . GLY B 2 140 ? 17.552  -24.741 14.645  1.00 67.81  ?  140 GLY B N   1 
ATOM 2678 C CA  . GLY B 2 140 ? 18.143  -25.359 15.803  1.00 67.17  ?  140 GLY B CA  1 
ATOM 2679 C C   . GLY B 2 140 ? 18.251  -24.495 17.036  1.00 65.84  ?  140 GLY B C   1 
ATOM 2680 O O   . GLY B 2 140 ? 18.738  -24.976 18.065  1.00 68.43  ?  140 GLY B O   1 
ATOM 2681 N N   . THR B 2 141 ? 17.822  -23.236 16.974  1.00 67.27  ?  141 THR B N   1 
ATOM 2682 C CA  . THR B 2 141 ? 17.870  -22.333 18.114  1.00 69.92  ?  141 THR B CA  1 
ATOM 2683 C C   . THR B 2 141 ? 16.478  -22.175 18.715  1.00 69.35  ?  141 THR B C   1 
ATOM 2684 O O   . THR B 2 141 ? 15.472  -22.170 18.007  1.00 68.95  ?  141 THR B O   1 
ATOM 2685 C CB  . THR B 2 141 ? 18.403  -20.954 17.693  1.00 62.12  ?  141 THR B CB  1 
ATOM 2686 O OG1 . THR B 2 141 ? 19.655  -21.098 17.011  1.00 64.00  ?  141 THR B OG1 1 
ATOM 2687 C CG2 . THR B 2 141 ? 18.601  -20.050 18.912  1.00 64.68  ?  141 THR B CG2 1 
ATOM 2688 N N   . ALA B 2 142 ? 16.429  -22.045 20.038  1.00 64.79  ?  142 ALA B N   1 
ATOM 2689 C CA  . ALA B 2 142 ? 15.185  -21.842 20.764  1.00 61.29  ?  142 ALA B CA  1 
ATOM 2690 C C   . ALA B 2 142 ? 15.266  -20.584 21.625  1.00 60.66  ?  142 ALA B C   1 
ATOM 2691 O O   . ALA B 2 142 ? 16.350  -20.115 21.982  1.00 61.58  ?  142 ALA B O   1 
ATOM 2692 C CB  . ALA B 2 142 ? 14.839  -23.056 21.637  1.00 61.99  ?  142 ALA B CB  1 
ATOM 2693 N N   . ALA B 2 143 ? 14.097  -20.031 21.946  1.00 58.78  ?  143 ALA B N   1 
ATOM 2694 C CA  . ALA B 2 143 ? 13.983  -18.850 22.795  1.00 55.45  ?  143 ALA B CA  1 
ATOM 2695 C C   . ALA B 2 143 ? 13.229  -19.194 24.075  1.00 57.44  ?  143 ALA B C   1 
ATOM 2696 O O   . ALA B 2 143 ? 12.152  -19.797 24.024  1.00 57.37  ?  143 ALA B O   1 
ATOM 2697 C CB  . ALA B 2 143 ? 13.271  -17.714 22.063  1.00 50.89  ?  143 ALA B CB  1 
ATOM 2698 N N   . LEU B 2 144 ? 13.808  -18.838 25.221  1.00 50.16  ?  144 LEU B N   1 
ATOM 2699 C CA  . LEU B 2 144 ? 13.138  -19.003 26.503  1.00 56.46  ?  144 LEU B CA  1 
ATOM 2700 C C   . LEU B 2 144 ? 13.459  -17.800 27.379  1.00 53.07  ?  144 LEU B C   1 
ATOM 2701 O O   . LEU B 2 144 ? 14.379  -17.030 27.092  1.00 52.37  ?  144 LEU B O   1 
ATOM 2702 C CB  . LEU B 2 144 ? 13.536  -20.324 27.185  1.00 57.35  ?  144 LEU B CB  1 
ATOM 2703 C CG  . LEU B 2 144 ? 15.014  -20.590 27.475  1.00 54.53  ?  144 LEU B CG  1 
ATOM 2704 C CD1 . LEU B 2 144 ? 15.358  -20.213 28.904  1.00 53.03  ?  144 LEU B CD1 1 
ATOM 2705 C CD2 . LEU B 2 144 ? 15.363  -22.043 27.203  1.00 45.32  ?  144 LEU B CD2 1 
ATOM 2706 N N   . GLY B 2 145 ? 12.692  -17.632 28.450  1.00 59.44  ?  145 GLY B N   1 
ATOM 2707 C CA  . GLY B 2 145 ? 12.962  -16.506 29.323  1.00 57.89  ?  145 GLY B CA  1 
ATOM 2708 C C   . GLY B 2 145 ? 12.112  -16.505 30.574  1.00 55.51  ?  145 GLY B C   1 
ATOM 2709 O O   . GLY B 2 145 ? 11.407  -17.467 30.880  1.00 54.58  ?  145 GLY B O   1 
ATOM 2710 N N   . CYS B 2 146 ? 12.207  -15.393 31.305  1.00 66.22  ?  146 CYS B N   1 
ATOM 2711 C CA  . CYS B 2 146 ? 11.443  -15.155 32.525  1.00 61.08  ?  146 CYS B CA  1 
ATOM 2712 C C   . CYS B 2 146 ? 10.778  -13.791 32.441  1.00 57.14  ?  146 CYS B C   1 
ATOM 2713 O O   . CYS B 2 146 ? 11.408  -12.811 32.030  1.00 56.55  ?  146 CYS B O   1 
ATOM 2714 C CB  . CYS B 2 146 ? 12.335  -15.239 33.778  1.00 51.38  ?  146 CYS B CB  1 
ATOM 2715 S SG  . CYS B 2 146 ? 12.736  -16.941 34.254  1.00 69.15  ?  146 CYS B SG  1 
ATOM 2716 N N   . LEU B 2 147 ? 9.500   -13.737 32.818  1.00 57.08  ?  147 LEU B N   1 
ATOM 2717 C CA  . LEU B 2 147 ? 8.738   -12.495 32.899  1.00 60.54  ?  147 LEU B CA  1 
ATOM 2718 C C   . LEU B 2 147 ? 8.675   -12.054 34.360  1.00 57.18  ?  147 LEU B C   1 
ATOM 2719 O O   . LEU B 2 147 ? 8.058   -12.729 35.192  1.00 59.99  ?  147 LEU B O   1 
ATOM 2720 C CB  . LEU B 2 147 ? 7.342   -12.687 32.309  1.00 56.00  ?  147 LEU B CB  1 
ATOM 2721 C CG  . LEU B 2 147 ? 6.315   -11.578 32.520  1.00 51.93  ?  147 LEU B CG  1 
ATOM 2722 C CD1 . LEU B 2 147 ? 6.791   -10.287 31.890  1.00 54.84  ?  147 LEU B CD1 1 
ATOM 2723 C CD2 . LEU B 2 147 ? 4.977   -11.995 31.934  1.00 50.59  ?  147 LEU B CD2 1 
ATOM 2724 N N   . VAL B 2 148 ? 9.338   -10.944 34.674  1.00 53.08  ?  148 VAL B N   1 
ATOM 2725 C CA  . VAL B 2 148 ? 9.372   -10.384 36.022  1.00 52.13  ?  148 VAL B CA  1 
ATOM 2726 C C   . VAL B 2 148 ? 8.380   -9.229  36.083  1.00 54.58  ?  148 VAL B C   1 
ATOM 2727 O O   . VAL B 2 148 ? 8.645   -8.141  35.555  1.00 51.62  ?  148 VAL B O   1 
ATOM 2728 C CB  . VAL B 2 148 ? 10.781  -9.914  36.399  1.00 54.45  ?  148 VAL B CB  1 
ATOM 2729 C CG1 . VAL B 2 148 ? 10.818  -9.477  37.850  1.00 51.55  ?  148 VAL B CG1 1 
ATOM 2730 C CG2 . VAL B 2 148 ? 11.797  -11.014 36.136  1.00 61.43  ?  148 VAL B CG2 1 
ATOM 2731 N N   . LYS B 2 149 ? 7.254   -9.443  36.763  1.00 55.29  ?  149 LYS B N   1 
ATOM 2732 C CA  . LYS B 2 149 ? 6.125   -8.527  36.730  1.00 57.63  ?  149 LYS B CA  1 
ATOM 2733 C C   . LYS B 2 149 ? 5.749   -8.059  38.133  1.00 62.41  ?  149 LYS B C   1 
ATOM 2734 O O   . LYS B 2 149 ? 5.915   -8.785  39.118  1.00 60.57  ?  149 LYS B O   1 
ATOM 2735 C CB  . LYS B 2 149 ? 4.902   -9.192  36.072  1.00 56.66  ?  149 LYS B CB  1 
ATOM 2736 C CG  . LYS B 2 149 ? 3.892   -8.204  35.504  1.00 63.85  ?  149 LYS B CG  1 
ATOM 2737 C CD  . LYS B 2 149 ? 2.562   -8.871  35.172  1.00 61.34  ?  149 LYS B CD  1 
ATOM 2738 C CE  . LYS B 2 149 ? 1.613   -7.894  34.480  1.00 66.98  ?  149 LYS B CE  1 
ATOM 2739 N NZ  . LYS B 2 149 ? 0.897   -7.008  35.439  1.00 66.62  ?  149 LYS B NZ  1 
ATOM 2740 N N   . ASP B 2 150 ? 5.237   -6.828  38.203  1.00 62.27  ?  150 ASP B N   1 
ATOM 2741 C CA  . ASP B 2 150 ? 4.605   -6.262  39.396  1.00 65.58  ?  150 ASP B CA  1 
ATOM 2742 C C   . ASP B 2 150 ? 5.581   -6.209  40.578  1.00 62.99  ?  150 ASP B C   1 
ATOM 2743 O O   . ASP B 2 150 ? 5.452   -6.929  41.571  1.00 63.48  ?  150 ASP B O   1 
ATOM 2744 C CB  . ASP B 2 150 ? 3.341   -7.053  39.762  1.00 63.63  ?  150 ASP B CB  1 
ATOM 2745 C CG  . ASP B 2 150 ? 2.298   -7.034  38.656  1.00 65.90  ?  150 ASP B CG  1 
ATOM 2746 O OD1 . ASP B 2 150 ? 2.300   -6.080  37.846  1.00 63.37  ?  150 ASP B OD1 1 
ATOM 2747 O OD2 . ASP B 2 150 ? 1.459   -7.961  38.612  1.00 68.58  ?  150 ASP B OD2 1 
ATOM 2748 N N   . TYR B 2 151 ? 6.567   -5.324  40.442  1.00 56.99  ?  151 TYR B N   1 
ATOM 2749 C CA  . TYR B 2 151 ? 7.527   -5.067  41.506  1.00 54.90  ?  151 TYR B CA  1 
ATOM 2750 C C   . TYR B 2 151 ? 7.758   -3.568  41.643  1.00 61.75  ?  151 TYR B C   1 
ATOM 2751 O O   . TYR B 2 151 ? 7.462   -2.786  40.736  1.00 63.67  ?  151 TYR B O   1 
ATOM 2752 C CB  . TYR B 2 151 ? 8.857   -5.798  41.257  1.00 56.54  ?  151 TYR B CB  1 
ATOM 2753 C CG  . TYR B 2 151 ? 9.717   -5.232  40.142  1.00 57.75  ?  151 TYR B CG  1 
ATOM 2754 C CD1 . TYR B 2 151 ? 9.595   -5.702  38.839  1.00 56.50  ?  151 TYR B CD1 1 
ATOM 2755 C CD2 . TYR B 2 151 ? 10.650  -4.234  40.391  1.00 54.02  ?  151 TYR B CD2 1 
ATOM 2756 C CE1 . TYR B 2 151 ? 10.377  -5.194  37.815  1.00 51.18  ?  151 TYR B CE1 1 
ATOM 2757 C CE2 . TYR B 2 151 ? 11.438  -3.724  39.371  1.00 60.36  ?  151 TYR B CE2 1 
ATOM 2758 C CZ  . TYR B 2 151 ? 11.297  -4.211  38.086  1.00 55.01  ?  151 TYR B CZ  1 
ATOM 2759 O OH  . TYR B 2 151 ? 12.080  -3.701  37.075  1.00 48.91  ?  151 TYR B OH  1 
ATOM 2760 N N   . PHE B 2 152 ? 8.296   -3.173  42.801  1.00 60.71  ?  152 PHE B N   1 
ATOM 2761 C CA  . PHE B 2 152 ? 8.597   -1.772  43.083  1.00 58.16  ?  152 PHE B CA  1 
ATOM 2762 C C   . PHE B 2 152 ? 9.474   -1.674  44.324  1.00 60.85  ?  152 PHE B C   1 
ATOM 2763 O O   . PHE B 2 152 ? 9.198   -2.336  45.333  1.00 64.24  ?  152 PHE B O   1 
ATOM 2764 C CB  . PHE B 2 152 ? 7.318   -0.954  43.279  1.00 56.12  ?  152 PHE B CB  1 
ATOM 2765 C CG  . PHE B 2 152 ? 7.560   0.526   43.398  1.00 59.37  ?  152 PHE B CG  1 
ATOM 2766 C CD1 . PHE B 2 152 ? 7.832   1.102   44.628  1.00 60.89  ?  152 PHE B CD1 1 
ATOM 2767 C CD2 . PHE B 2 152 ? 7.516   1.344   42.277  1.00 63.51  ?  152 PHE B CD2 1 
ATOM 2768 C CE1 . PHE B 2 152 ? 8.061   2.459   44.738  1.00 58.79  ?  152 PHE B CE1 1 
ATOM 2769 C CE2 . PHE B 2 152 ? 7.740   2.707   42.381  1.00 62.43  ?  152 PHE B CE2 1 
ATOM 2770 C CZ  . PHE B 2 152 ? 8.013   3.265   43.611  1.00 57.65  ?  152 PHE B CZ  1 
ATOM 2771 N N   . PRO B 2 153 ? 10.524  -0.840  44.305  1.00 57.20  ?  153 PRO B N   1 
ATOM 2772 C CA  . PRO B 2 153 ? 10.942  -0.033  43.160  1.00 52.20  ?  153 PRO B CA  1 
ATOM 2773 C C   . PRO B 2 153 ? 12.036  -0.712  42.347  1.00 54.43  ?  153 PRO B C   1 
ATOM 2774 O O   . PRO B 2 153 ? 12.313  -1.891  42.550  1.00 55.59  ?  153 PRO B O   1 
ATOM 2775 C CB  . PRO B 2 153 ? 11.492  1.217   43.826  1.00 55.68  ?  153 PRO B CB  1 
ATOM 2776 C CG  . PRO B 2 153 ? 12.163  0.658   45.049  1.00 52.09  ?  153 PRO B CG  1 
ATOM 2777 C CD  . PRO B 2 153 ? 11.320  -0.518  45.502  1.00 54.63  ?  153 PRO B CD  1 
ATOM 2778 N N   . GLU B 2 154 ? 12.651  0.037   41.438  1.00 54.66  ?  154 GLU B N   1 
ATOM 2779 C CA  . GLU B 2 154 ? 13.850  -0.436  40.772  1.00 52.96  ?  154 GLU B CA  1 
ATOM 2780 C C   . GLU B 2 154 ? 14.988  -0.509  41.792  1.00 54.50  ?  154 GLU B C   1 
ATOM 2781 O O   . GLU B 2 154 ? 14.958  0.191   42.807  1.00 65.29  ?  154 GLU B O   1 
ATOM 2782 C CB  . GLU B 2 154 ? 14.216  0.503   39.621  1.00 55.77  ?  154 GLU B CB  1 
ATOM 2783 C CG  . GLU B 2 154 ? 13.322  0.394   38.383  1.00 62.03  ?  154 GLU B CG  1 
ATOM 2784 C CD  . GLU B 2 154 ? 13.947  -0.436  37.262  1.00 66.29  ?  154 GLU B CD  1 
ATOM 2785 O OE1 . GLU B 2 154 ? 14.229  -1.642  37.475  1.00 60.71  ?  154 GLU B OE1 1 
ATOM 2786 O OE2 . GLU B 2 154 ? 14.153  0.133   36.165  1.00 56.55  ?  154 GLU B OE2 1 
ATOM 2787 N N   . PRO B 2 155 ? 16.007  -1.354  41.556  1.00 54.73  ?  155 PRO B N   1 
ATOM 2788 C CA  . PRO B 2 155 ? 16.216  -2.198  40.383  1.00 53.24  ?  155 PRO B CA  1 
ATOM 2789 C C   . PRO B 2 155 ? 15.953  -3.670  40.641  1.00 51.56  ?  155 PRO B C   1 
ATOM 2790 O O   . PRO B 2 155 ? 15.782  -4.098  41.782  1.00 55.31  ?  155 PRO B O   1 
ATOM 2791 C CB  . PRO B 2 155 ? 17.697  -1.983  40.085  1.00 45.81  ?  155 PRO B CB  1 
ATOM 2792 C CG  . PRO B 2 155 ? 18.303  -1.890  41.460  1.00 45.65  ?  155 PRO B CG  1 
ATOM 2793 C CD  . PRO B 2 155 ? 17.228  -1.305  42.382  1.00 50.47  ?  155 PRO B CD  1 
ATOM 2794 N N   . VAL B 2 156 ? 15.933  -4.438  39.559  1.00 57.87  ?  156 VAL B N   1 
ATOM 2795 C CA  . VAL B 2 156 ? 15.910  -5.892  39.606  1.00 52.22  ?  156 VAL B CA  1 
ATOM 2796 C C   . VAL B 2 156 ? 17.109  -6.379  38.810  1.00 49.78  ?  156 VAL B C   1 
ATOM 2797 O O   . VAL B 2 156 ? 17.482  -5.770  37.801  1.00 45.33  ?  156 VAL B O   1 
ATOM 2798 C CB  . VAL B 2 156 ? 14.585  -6.460  39.049  1.00 48.97  ?  156 VAL B CB  1 
ATOM 2799 C CG1 . VAL B 2 156 ? 14.752  -7.885  38.559  1.00 52.71  ?  156 VAL B CG1 1 
ATOM 2800 C CG2 . VAL B 2 156 ? 13.498  -6.394  40.114  1.00 54.81  ?  156 VAL B CG2 1 
ATOM 2801 N N   . THR B 2 157 ? 17.735  -7.449  39.291  1.00 52.91  ?  157 THR B N   1 
ATOM 2802 C CA  . THR B 2 157 ? 18.870  -8.077  38.635  1.00 48.64  ?  157 THR B CA  1 
ATOM 2803 C C   . THR B 2 157 ? 18.480  -9.492  38.248  1.00 53.32  ?  157 THR B C   1 
ATOM 2804 O O   . THR B 2 157 ? 17.985  -10.253 39.086  1.00 61.52  ?  157 THR B O   1 
ATOM 2805 C CB  . THR B 2 157 ? 20.098  -8.099  39.550  1.00 57.80  ?  157 THR B CB  1 
ATOM 2806 O OG1 . THR B 2 157 ? 20.645  -6.781  39.643  1.00 55.06  ?  157 THR B OG1 1 
ATOM 2807 C CG2 . THR B 2 157 ? 21.156  -9.049  39.006  1.00 68.08  ?  157 THR B CG2 1 
ATOM 2808 N N   . VAL B 2 158 ? 18.696  -9.842  36.987  1.00 49.82  ?  158 VAL B N   1 
ATOM 2809 C CA  . VAL B 2 158 ? 18.422  -11.181 36.486  1.00 47.81  ?  158 VAL B CA  1 
ATOM 2810 C C   . VAL B 2 158 ? 19.730  -11.781 35.994  1.00 49.37  ?  158 VAL B C   1 
ATOM 2811 O O   . VAL B 2 158 ? 20.590  -11.072 35.462  1.00 55.38  ?  158 VAL B O   1 
ATOM 2812 C CB  . VAL B 2 158 ? 17.352  -11.179 35.373  1.00 47.50  ?  158 VAL B CB  1 
ATOM 2813 C CG1 . VAL B 2 158 ? 17.008  -12.602 34.959  1.00 51.42  ?  158 VAL B CG1 1 
ATOM 2814 C CG2 . VAL B 2 158 ? 16.101  -10.463 35.849  1.00 49.96  ?  158 VAL B CG2 1 
ATOM 2815 N N   . SER B 2 159 ? 19.900  -13.078 36.228  1.00 54.15  ?  159 SER B N   1 
ATOM 2816 C CA  . SER B 2 159 ? 21.024  -13.833 35.699  1.00 51.47  ?  159 SER B CA  1 
ATOM 2817 C C   . SER B 2 159 ? 20.522  -15.236 35.410  1.00 53.76  ?  159 SER B C   1 
ATOM 2818 O O   . SER B 2 159 ? 19.456  -15.636 35.884  1.00 57.88  ?  159 SER B O   1 
ATOM 2819 C CB  . SER B 2 159 ? 22.209  -13.857 36.671  1.00 49.62  ?  159 SER B CB  1 
ATOM 2820 O OG  . SER B 2 159 ? 21.990  -14.794 37.713  1.00 54.88  ?  159 SER B OG  1 
ATOM 2821 N N   . TRP B 2 160 ? 21.279  -15.976 34.603  1.00 52.40  ?  160 TRP B N   1 
ATOM 2822 C CA  . TRP B 2 160 ? 20.887  -17.316 34.187  1.00 52.69  ?  160 TRP B CA  1 
ATOM 2823 C C   . TRP B 2 160 ? 21.928  -18.334 34.629  1.00 53.77  ?  160 TRP B C   1 
ATOM 2824 O O   . TRP B 2 160 ? 23.123  -18.163 34.364  1.00 52.53  ?  160 TRP B O   1 
ATOM 2825 C CB  . TRP B 2 160 ? 20.683  -17.375 32.674  1.00 51.02  ?  160 TRP B CB  1 
ATOM 2826 C CG  . TRP B 2 160 ? 19.434  -16.676 32.227  1.00 49.19  ?  160 TRP B CG  1 
ATOM 2827 C CD1 . TRP B 2 160 ? 19.306  -15.357 31.885  1.00 49.34  ?  160 TRP B CD1 1 
ATOM 2828 C CD2 . TRP B 2 160 ? 18.136  -17.257 32.079  1.00 44.82  ?  160 TRP B CD2 1 
ATOM 2829 N NE1 . TRP B 2 160 ? 18.007  -15.085 31.529  1.00 47.58  ?  160 TRP B NE1 1 
ATOM 2830 C CE2 . TRP B 2 160 ? 17.269  -16.235 31.639  1.00 46.86  ?  160 TRP B CE2 1 
ATOM 2831 C CE3 . TRP B 2 160 ? 17.624  -18.542 32.268  1.00 48.45  ?  160 TRP B CE3 1 
ATOM 2832 C CZ2 . TRP B 2 160 ? 15.919  -16.461 31.387  1.00 46.32  ?  160 TRP B CZ2 1 
ATOM 2833 C CZ3 . TRP B 2 160 ? 16.282  -18.764 32.019  1.00 52.26  ?  160 TRP B CZ3 1 
ATOM 2834 C CH2 . TRP B 2 160 ? 15.445  -17.727 31.585  1.00 52.40  ?  160 TRP B CH2 1 
ATOM 2835 N N   . ASN B 2 161 ? 21.464  -19.393 35.294  1.00 52.78  ?  161 ASN B N   1 
ATOM 2836 C CA  . ASN B 2 161 ? 22.330  -20.446 35.820  1.00 52.90  ?  161 ASN B CA  1 
ATOM 2837 C C   . ASN B 2 161 ? 23.453  -19.854 36.665  1.00 55.21  ?  161 ASN B C   1 
ATOM 2838 O O   . ASN B 2 161 ? 24.632  -20.168 36.490  1.00 52.74  ?  161 ASN B O   1 
ATOM 2839 C CB  . ASN B 2 161 ? 22.885  -21.315 34.693  1.00 56.42  ?  161 ASN B CB  1 
ATOM 2840 C CG  . ASN B 2 161 ? 21.802  -22.090 33.977  1.00 56.85  ?  161 ASN B CG  1 
ATOM 2841 O OD1 . ASN B 2 161 ? 20.626  -22.005 34.335  1.00 55.87  ?  161 ASN B OD1 1 
ATOM 2842 N ND2 . ASN B 2 161 ? 22.190  -22.855 32.962  1.00 60.54  ?  161 ASN B ND2 1 
ATOM 2843 N N   . SER B 2 162 ? 23.064  -18.959 37.578  1.00 57.61  ?  162 SER B N   1 
ATOM 2844 C CA  . SER B 2 162 ? 23.970  -18.374 38.565  1.00 50.29  ?  162 SER B CA  1 
ATOM 2845 C C   . SER B 2 162 ? 25.155  -17.669 37.911  1.00 51.42  ?  162 SER B C   1 
ATOM 2846 O O   . SER B 2 162 ? 26.242  -17.599 38.488  1.00 52.51  ?  162 SER B O   1 
ATOM 2847 C CB  . SER B 2 162 ? 24.452  -19.436 39.555  1.00 46.87  ?  162 SER B CB  1 
ATOM 2848 O OG  . SER B 2 162 ? 23.386  -19.852 40.388  1.00 51.65  ?  162 SER B OG  1 
ATOM 2849 N N   . GLY B 2 163 ? 24.962  -17.153 36.696  1.00 51.92  ?  163 GLY B N   1 
ATOM 2850 C CA  . GLY B 2 163 ? 26.018  -16.472 35.974  1.00 48.78  ?  163 GLY B CA  1 
ATOM 2851 C C   . GLY B 2 163 ? 26.763  -17.321 34.967  1.00 54.62  ?  163 GLY B C   1 
ATOM 2852 O O   . GLY B 2 163 ? 27.726  -16.827 34.365  1.00 50.12  ?  163 GLY B O   1 
ATOM 2853 N N   . ALA B 2 164 ? 26.371  -18.589 34.788  1.00 56.76  ?  164 ALA B N   1 
ATOM 2854 C CA  . ALA B 2 164 ? 27.051  -19.470 33.842  1.00 59.96  ?  164 ALA B CA  1 
ATOM 2855 C C   . ALA B 2 164 ? 26.589  -19.257 32.405  1.00 65.28  ?  164 ALA B C   1 
ATOM 2856 O O   . ALA B 2 164 ? 27.328  -19.586 31.471  1.00 66.25  ?  164 ALA B O   1 
ATOM 2857 C CB  . ALA B 2 164 ? 26.848  -20.934 34.235  1.00 52.12  ?  164 ALA B CB  1 
ATOM 2858 N N   . LEU B 2 165 ? 25.371  -18.756 32.208  1.00 60.12  ?  165 LEU B N   1 
ATOM 2859 C CA  . LEU B 2 165 ? 24.822  -18.484 30.883  1.00 59.25  ?  165 LEU B CA  1 
ATOM 2860 C C   . LEU B 2 165 ? 24.785  -16.974 30.681  1.00 59.61  ?  165 LEU B C   1 
ATOM 2861 O O   . LEU B 2 165 ? 24.029  -16.275 31.365  1.00 59.71  ?  165 LEU B O   1 
ATOM 2862 C CB  . LEU B 2 165 ? 23.434  -19.101 30.738  1.00 56.26  ?  165 LEU B CB  1 
ATOM 2863 C CG  . LEU B 2 165 ? 22.791  -19.071 29.350  1.00 59.35  ?  165 LEU B CG  1 
ATOM 2864 C CD1 . LEU B 2 165 ? 23.765  -19.553 28.289  1.00 55.46  ?  165 LEU B CD1 1 
ATOM 2865 C CD2 . LEU B 2 165 ? 21.530  -19.926 29.343  1.00 51.85  ?  165 LEU B CD2 1 
ATOM 2866 N N   . THR B 2 166 ? 25.597  -16.469 29.746  1.00 62.52  ?  166 THR B N   1 
ATOM 2867 C CA  . THR B 2 166 ? 25.665  -15.028 29.520  1.00 57.65  ?  166 THR B CA  1 
ATOM 2868 C C   . THR B 2 166 ? 25.475  -14.642 28.060  1.00 57.73  ?  166 THR B C   1 
ATOM 2869 O O   . THR B 2 166 ? 24.988  -13.545 27.772  1.00 60.34  ?  166 THR B O   1 
ATOM 2870 C CB  . THR B 2 166 ? 27.004  -14.462 30.002  1.00 57.16  ?  166 THR B CB  1 
ATOM 2871 O OG1 . THR B 2 166 ? 28.077  -15.130 29.327  1.00 56.49  ?  166 THR B OG1 1 
ATOM 2872 C CG2 . THR B 2 166 ? 27.157  -14.620 31.502  1.00 56.83  ?  166 THR B CG2 1 
ATOM 2873 N N   . SER B 2 167 ? 25.838  -15.525 27.132  1.00 65.20  ?  167 SER B N   1 
ATOM 2874 C CA  . SER B 2 167 ? 25.781  -15.192 25.712  1.00 59.95  ?  167 SER B CA  1 
ATOM 2875 C C   . SER B 2 167 ? 24.368  -15.348 25.165  1.00 57.21  ?  167 SER B C   1 
ATOM 2876 O O   . SER B 2 167 ? 23.685  -16.342 25.431  1.00 58.06  ?  167 SER B O   1 
ATOM 2877 C CB  . SER B 2 167 ? 26.739  -16.072 24.913  1.00 55.89  ?  167 SER B CB  1 
ATOM 2878 O OG  . SER B 2 167 ? 26.213  -17.379 24.775  1.00 69.27  ?  167 SER B OG  1 
ATOM 2879 N N   . GLY B 2 168 ? 23.938  -14.369 24.375  1.00 53.14  ?  168 GLY B N   1 
ATOM 2880 C CA  . GLY B 2 168 ? 22.589  -14.420 23.852  1.00 53.98  ?  168 GLY B CA  1 
ATOM 2881 C C   . GLY B 2 168 ? 21.522  -14.140 24.879  1.00 52.64  ?  168 GLY B C   1 
ATOM 2882 O O   . GLY B 2 168 ? 20.376  -14.564 24.704  1.00 49.59  ?  168 GLY B O   1 
ATOM 2883 N N   . VAL B 2 169 ? 21.882  -13.474 25.970  1.00 53.49  ?  169 VAL B N   1 
ATOM 2884 C CA  . VAL B 2 169 ? 20.954  -13.126 27.037  1.00 53.71  ?  169 VAL B CA  1 
ATOM 2885 C C   . VAL B 2 169 ? 20.598  -11.658 26.885  1.00 46.05  ?  169 VAL B C   1 
ATOM 2886 O O   . VAL B 2 169 ? 21.486  -10.813 26.717  1.00 47.59  ?  169 VAL B O   1 
ATOM 2887 C CB  . VAL B 2 169 ? 21.557  -13.402 28.425  1.00 55.30  ?  169 VAL B CB  1 
ATOM 2888 C CG1 . VAL B 2 169 ? 20.553  -13.048 29.518  1.00 51.76  ?  169 VAL B CG1 1 
ATOM 2889 C CG2 . VAL B 2 169 ? 21.997  -14.846 28.538  1.00 52.17  ?  169 VAL B CG2 1 
ATOM 2890 N N   . HIS B 2 170 ? 19.307  -11.354 26.913  1.00 44.28  ?  170 HIS B N   1 
ATOM 2891 C CA  . HIS B 2 170 ? 18.836  -9.976  26.841  1.00 54.40  ?  170 HIS B CA  1 
ATOM 2892 C C   . HIS B 2 170 ? 17.874  -9.735  27.997  1.00 54.61  ?  170 HIS B C   1 
ATOM 2893 O O   . HIS B 2 170 ? 16.809  -10.359 28.061  1.00 54.00  ?  170 HIS B O   1 
ATOM 2894 C CB  . HIS B 2 170 ? 18.171  -9.677  25.496  1.00 51.74  ?  170 HIS B CB  1 
ATOM 2895 C CG  . HIS B 2 170 ? 19.117  -9.697  24.332  1.00 57.18  ?  170 HIS B CG  1 
ATOM 2896 N ND1 . HIS B 2 170 ? 20.075  -8.723  24.135  1.00 56.71  ?  170 HIS B ND1 1 
ATOM 2897 C CD2 . HIS B 2 170 ? 19.243  -10.564 23.297  1.00 51.10  ?  170 HIS B CD2 1 
ATOM 2898 C CE1 . HIS B 2 170 ? 20.756  -8.996  23.035  1.00 56.73  ?  170 HIS B CE1 1 
ATOM 2899 N NE2 . HIS B 2 170 ? 20.270  -10.106 22.508  1.00 53.91  ?  170 HIS B NE2 1 
ATOM 2900 N N   . THR B 2 171 ? 18.276  -8.882  28.939  1.00 47.35  ?  171 THR B N   1 
ATOM 2901 C CA  . THR B 2 171 ? 17.402  -8.432  30.018  1.00 50.47  ?  171 THR B CA  1 
ATOM 2902 C C   . THR B 2 171 ? 16.898  -7.043  29.650  1.00 51.58  ?  171 THR B C   1 
ATOM 2903 O O   . THR B 2 171 ? 17.669  -6.077  29.651  1.00 58.23  ?  171 THR B O   1 
ATOM 2904 C CB  . THR B 2 171 ? 18.126  -8.412  31.360  1.00 55.01  ?  171 THR B CB  1 
ATOM 2905 O OG1 . THR B 2 171 ? 18.607  -9.728  31.666  1.00 57.37  ?  171 THR B OG1 1 
ATOM 2906 C CG2 . THR B 2 171 ? 17.184  -7.945  32.462  1.00 50.89  ?  171 THR B CG2 1 
ATOM 2907 N N   . PHE B 2 172 ? 15.615  -6.948  29.315  1.00 50.99  ?  172 PHE B N   1 
ATOM 2908 C CA  . PHE B 2 172 ? 15.073  -5.691  28.829  1.00 54.66  ?  172 PHE B CA  1 
ATOM 2909 C C   . PHE B 2 172 ? 14.925  -4.681  29.962  1.00 54.24  ?  172 PHE B C   1 
ATOM 2910 O O   . PHE B 2 172 ? 14.718  -5.056  31.118  1.00 54.20  ?  172 PHE B O   1 
ATOM 2911 C CB  . PHE B 2 172 ? 13.721  -5.907  28.161  1.00 55.18  ?  172 PHE B CB  1 
ATOM 2912 C CG  . PHE B 2 172 ? 13.805  -6.714  26.913  1.00 52.90  ?  172 PHE B CG  1 
ATOM 2913 C CD1 . PHE B 2 172 ? 13.598  -8.078  26.945  1.00 51.99  ?  172 PHE B CD1 1 
ATOM 2914 C CD2 . PHE B 2 172 ? 14.110  -6.113  25.711  1.00 53.30  ?  172 PHE B CD2 1 
ATOM 2915 C CE1 . PHE B 2 172 ? 13.682  -8.830  25.797  1.00 51.34  ?  172 PHE B CE1 1 
ATOM 2916 C CE2 . PHE B 2 172 ? 14.202  -6.860  24.563  1.00 58.14  ?  172 PHE B CE2 1 
ATOM 2917 C CZ  . PHE B 2 172 ? 13.983  -8.224  24.606  1.00 54.03  ?  172 PHE B CZ  1 
ATOM 2918 N N   . PRO B 2 173 ? 15.026  -3.391  29.653  1.00 60.09  ?  173 PRO B N   1 
ATOM 2919 C CA  . PRO B 2 173 ? 14.761  -2.373  30.670  1.00 54.31  ?  173 PRO B CA  1 
ATOM 2920 C C   . PRO B 2 173 ? 13.326  -2.460  31.168  1.00 56.21  ?  173 PRO B C   1 
ATOM 2921 O O   . PRO B 2 173 ? 12.429  -2.987  30.502  1.00 50.15  ?  173 PRO B O   1 
ATOM 2922 C CB  . PRO B 2 173 ? 15.015  -1.054  29.929  1.00 56.62  ?  173 PRO B CB  1 
ATOM 2923 C CG  . PRO B 2 173 ? 15.939  -1.424  28.810  1.00 55.45  ?  173 PRO B CG  1 
ATOM 2924 C CD  . PRO B 2 173 ? 15.518  -2.803  28.394  1.00 56.94  ?  173 PRO B CD  1 
ATOM 2925 N N   . ALA B 2 174 ? 13.120  -1.924  32.366  1.00 58.85  ?  174 ALA B N   1 
ATOM 2926 C CA  . ALA B 2 174 ? 11.824  -1.982  33.019  1.00 56.20  ?  174 ALA B CA  1 
ATOM 2927 C C   . ALA B 2 174 ? 10.876  -0.942  32.438  1.00 58.29  ?  174 ALA B C   1 
ATOM 2928 O O   . ALA B 2 174 ? 11.287  0.148   32.033  1.00 58.18  ?  174 ALA B O   1 
ATOM 2929 C CB  . ALA B 2 174 ? 11.982  -1.763  34.522  1.00 62.04  ?  174 ALA B CB  1 
ATOM 2930 N N   . VAL B 2 175 ? 9.589   -1.281  32.424  1.00 59.45  ?  175 VAL B N   1 
ATOM 2931 C CA  . VAL B 2 175 ? 8.541   -0.403  31.919  1.00 63.25  ?  175 VAL B CA  1 
ATOM 2932 C C   . VAL B 2 175 ? 7.569   -0.122  33.054  1.00 68.28  ?  175 VAL B C   1 
ATOM 2933 O O   . VAL B 2 175 ? 7.087   -1.053  33.711  1.00 73.55  ?  175 VAL B O   1 
ATOM 2934 C CB  . VAL B 2 175 ? 7.802   -1.025  30.719  1.00 68.08  ?  175 VAL B CB  1 
ATOM 2935 C CG1 . VAL B 2 175 ? 6.615   -0.160  30.320  1.00 68.30  ?  175 VAL B CG1 1 
ATOM 2936 C CG2 . VAL B 2 175 ? 8.750   -1.204  29.544  1.00 67.06  ?  175 VAL B CG2 1 
ATOM 2937 N N   . LEU B 2 176 ? 7.278   1.157   33.277  1.00 66.72  ?  176 LEU B N   1 
ATOM 2938 C CA  . LEU B 2 176 ? 6.342   1.568   34.317  1.00 69.11  ?  176 LEU B CA  1 
ATOM 2939 C C   . LEU B 2 176 ? 4.919   1.347   33.818  1.00 72.71  ?  176 LEU B C   1 
ATOM 2940 O O   . LEU B 2 176 ? 4.474   2.005   32.871  1.00 76.54  ?  176 LEU B O   1 
ATOM 2941 C CB  . LEU B 2 176 ? 6.580   3.027   34.695  1.00 68.51  ?  176 LEU B CB  1 
ATOM 2942 C CG  . LEU B 2 176 ? 5.875   3.536   35.953  1.00 67.11  ?  176 LEU B CG  1 
ATOM 2943 C CD1 . LEU B 2 176 ? 6.189   2.639   37.135  1.00 69.52  ?  176 LEU B CD1 1 
ATOM 2944 C CD2 . LEU B 2 176 ? 6.295   4.967   36.247  1.00 59.40  ?  176 LEU B CD2 1 
ATOM 2945 N N   . GLN B 2 177 ? 4.204   0.419   34.448  1.00 74.36  ?  177 GLN B N   1 
ATOM 2946 C CA  . GLN B 2 177 ? 2.831   0.141   34.062  1.00 76.57  ?  177 GLN B CA  1 
ATOM 2947 C C   . GLN B 2 177 ? 1.883   1.177   34.666  1.00 80.68  ?  177 GLN B C   1 
ATOM 2948 O O   . GLN B 2 177 ? 2.261   1.996   35.512  1.00 78.76  ?  177 GLN B O   1 
ATOM 2949 C CB  . GLN B 2 177 ? 2.426   -1.273  34.484  1.00 77.05  ?  177 GLN B CB  1 
ATOM 2950 C CG  . GLN B 2 177 ? 3.303   -2.376  33.901  1.00 74.32  ?  177 GLN B CG  1 
ATOM 2951 C CD  . GLN B 2 177 ? 2.896   -3.760  34.379  1.00 77.25  ?  177 GLN B CD  1 
ATOM 2952 O OE1 . GLN B 2 177 ? 2.664   -4.667  33.577  1.00 79.86  ?  177 GLN B OE1 1 
ATOM 2953 N NE2 . GLN B 2 177 ? 2.801   -3.927  35.693  1.00 74.06  ?  177 GLN B NE2 1 
ATOM 2954 N N   . SER B 2 178 ? 0.632   1.146   34.195  1.00 76.07  ?  178 SER B N   1 
ATOM 2955 C CA  . SER B 2 178 ? -0.386  2.058   34.708  1.00 79.14  ?  178 SER B CA  1 
ATOM 2956 C C   . SER B 2 178 ? -0.572  1.915   36.212  1.00 81.03  ?  178 SER B C   1 
ATOM 2957 O O   . SER B 2 178 ? -0.963  2.878   36.882  1.00 84.17  ?  178 SER B O   1 
ATOM 2958 C CB  . SER B 2 178 ? -1.719  1.806   34.005  1.00 77.46  ?  178 SER B CB  1 
ATOM 2959 O OG  . SER B 2 178 ? -2.105  0.448   34.142  1.00 77.87  ?  178 SER B OG  1 
ATOM 2960 N N   . SER B 2 179 ? -0.299  0.731   36.761  1.00 81.55  ?  179 SER B N   1 
ATOM 2961 C CA  . SER B 2 179 ? -0.531  0.466   38.176  1.00 82.02  ?  179 SER B CA  1 
ATOM 2962 C C   . SER B 2 179 ? 0.553   1.037   39.079  1.00 80.05  ?  179 SER B C   1 
ATOM 2963 O O   . SER B 2 179 ? 0.465   0.873   40.301  1.00 77.14  ?  179 SER B O   1 
ATOM 2964 C CB  . SER B 2 179 ? -0.647  -1.041  38.415  1.00 76.19  ?  179 SER B CB  1 
ATOM 2965 O OG  . SER B 2 179 ? 0.554   -1.707  38.059  1.00 80.99  ?  179 SER B OG  1 
ATOM 2966 N N   . GLY B 2 180 ? 1.554   1.712   38.519  1.00 76.99  ?  180 GLY B N   1 
ATOM 2967 C CA  . GLY B 2 180 ? 2.673   2.199   39.294  1.00 75.75  ?  180 GLY B CA  1 
ATOM 2968 C C   . GLY B 2 180 ? 3.735   1.170   39.607  1.00 70.72  ?  180 GLY B C   1 
ATOM 2969 O O   . GLY B 2 180 ? 4.722   1.509   40.272  1.00 65.54  ?  180 GLY B O   1 
ATOM 2970 N N   . LEU B 2 181 ? 3.578   -0.066  39.145  1.00 72.93  ?  181 LEU B N   1 
ATOM 2971 C CA  . LEU B 2 181 ? 4.571   -1.111  39.332  1.00 69.16  ?  181 LEU B CA  1 
ATOM 2972 C C   . LEU B 2 181 ? 5.346   -1.344  38.040  1.00 72.28  ?  181 LEU B C   1 
ATOM 2973 O O   . LEU B 2 181 ? 4.852   -1.102  36.935  1.00 75.05  ?  181 LEU B O   1 
ATOM 2974 C CB  . LEU B 2 181 ? 3.913   -2.418  39.784  1.00 72.57  ?  181 LEU B CB  1 
ATOM 2975 C CG  . LEU B 2 181 ? 3.129   -2.412  41.099  1.00 75.48  ?  181 LEU B CG  1 
ATOM 2976 C CD1 . LEU B 2 181 ? 2.502   -3.778  41.351  1.00 66.78  ?  181 LEU B CD1 1 
ATOM 2977 C CD2 . LEU B 2 181 ? 4.024   -2.005  42.259  1.00 61.15  ?  181 LEU B CD2 1 
ATOM 2978 N N   . TYR B 2 182 ? 6.568   -1.848  38.194  1.00 68.77  ?  182 TYR B N   1 
ATOM 2979 C CA  . TYR B 2 182 ? 7.443   -2.104  37.061  1.00 66.05  ?  182 TYR B CA  1 
ATOM 2980 C C   . TYR B 2 182 ? 7.259   -3.528  36.546  1.00 64.82  ?  182 TYR B C   1 
ATOM 2981 O O   . TYR B 2 182 ? 6.650   -4.381  37.196  1.00 66.35  ?  182 TYR B O   1 
ATOM 2982 C CB  . TYR B 2 182 ? 8.904   -1.872  37.444  1.00 61.33  ?  182 TYR B CB  1 
ATOM 2983 C CG  . TYR B 2 182 ? 9.283   -0.419  37.606  1.00 65.93  ?  182 TYR B CG  1 
ATOM 2984 C CD1 . TYR B 2 182 ? 9.160   0.227   38.833  1.00 64.85  ?  182 TYR B CD1 1 
ATOM 2985 C CD2 . TYR B 2 182 ? 9.762   0.311   36.524  1.00 62.97  ?  182 TYR B CD2 1 
ATOM 2986 C CE1 . TYR B 2 182 ? 9.514   1.565   38.977  1.00 64.64  ?  182 TYR B CE1 1 
ATOM 2987 C CE2 . TYR B 2 182 ? 10.114  1.640   36.658  1.00 66.47  ?  182 TYR B CE2 1 
ATOM 2988 C CZ  . TYR B 2 182 ? 9.988   2.261   37.882  1.00 61.51  ?  182 TYR B CZ  1 
ATOM 2989 O OH  . TYR B 2 182 ? 10.341  3.580   38.000  1.00 58.17  ?  182 TYR B OH  1 
ATOM 2990 N N   . SER B 2 183 ? 7.818   -3.782  35.364  1.00 64.82  ?  183 SER B N   1 
ATOM 2991 C CA  . SER B 2 183 ? 7.740   -5.092  34.732  1.00 59.79  ?  183 SER B CA  1 
ATOM 2992 C C   . SER B 2 183 ? 8.775   -5.155  33.619  1.00 56.62  ?  183 SER B C   1 
ATOM 2993 O O   . SER B 2 183 ? 8.998   -4.165  32.920  1.00 61.96  ?  183 SER B O   1 
ATOM 2994 C CB  . SER B 2 183 ? 6.337   -5.368  34.178  1.00 58.91  ?  183 SER B CB  1 
ATOM 2995 O OG  . SER B 2 183 ? 6.332   -6.528  33.365  1.00 64.56  ?  183 SER B OG  1 
ATOM 2996 N N   . LEU B 2 184 ? 9.418   -6.313  33.479  1.00 53.45  ?  184 LEU B N   1 
ATOM 2997 C CA  . LEU B 2 184 ? 10.386  -6.528  32.413  1.00 49.11  ?  184 LEU B CA  1 
ATOM 2998 C C   . LEU B 2 184 ? 10.447  -8.016  32.092  1.00 53.50  ?  184 LEU B C   1 
ATOM 2999 O O   . LEU B 2 184 ? 9.727   -8.833  32.673  1.00 57.01  ?  184 LEU B O   1 
ATOM 3000 C CB  . LEU B 2 184 ? 11.766  -5.975  32.792  1.00 46.45  ?  184 LEU B CB  1 
ATOM 3001 C CG  . LEU B 2 184 ? 12.545  -6.549  33.981  1.00 52.80  ?  184 LEU B CG  1 
ATOM 3002 C CD1 . LEU B 2 184 ? 13.451  -7.702  33.588  1.00 49.82  ?  184 LEU B CD1 1 
ATOM 3003 C CD2 . LEU B 2 184 ? 13.360  -5.448  34.647  1.00 55.33  ?  184 LEU B CD2 1 
ATOM 3004 N N   . SER B 2 185 ? 11.302  -8.356  31.131  1.00 55.59  ?  185 SER B N   1 
ATOM 3005 C CA  . SER B 2 185 ? 11.569  -9.739  30.767  1.00 50.86  ?  185 SER B CA  1 
ATOM 3006 C C   . SER B 2 185 ? 13.063  -9.911  30.548  1.00 52.63  ?  185 SER B C   1 
ATOM 3007 O O   . SER B 2 185 ? 13.799  -8.947  30.320  1.00 51.58  ?  185 SER B O   1 
ATOM 3008 C CB  . SER B 2 185 ? 10.793  -10.174 29.518  1.00 43.49  ?  185 SER B CB  1 
ATOM 3009 O OG  . SER B 2 185 ? 9.421   -10.347 29.821  1.00 46.12  ?  185 SER B OG  1 
ATOM 3010 N N   . SER B 2 186 ? 13.509  -11.156 30.664  1.00 50.71  ?  186 SER B N   1 
ATOM 3011 C CA  . SER B 2 186 ? 14.883  -11.525 30.363  1.00 50.08  ?  186 SER B CA  1 
ATOM 3012 C C   . SER B 2 186 ? 14.850  -12.798 29.535  1.00 50.66  ?  186 SER B C   1 
ATOM 3013 O O   . SER B 2 186 ? 14.345  -13.824 30.000  1.00 53.29  ?  186 SER B O   1 
ATOM 3014 C CB  . SER B 2 186 ? 15.699  -11.724 31.640  1.00 48.83  ?  186 SER B CB  1 
ATOM 3015 O OG  . SER B 2 186 ? 17.077  -11.858 31.342  1.00 51.24  ?  186 SER B OG  1 
ATOM 3016 N N   . VAL B 2 187 ? 15.344  -12.726 28.301  1.00 48.23  ?  187 VAL B N   1 
ATOM 3017 C CA  . VAL B 2 187 ? 15.279  -13.854 27.379  1.00 51.58  ?  187 VAL B CA  1 
ATOM 3018 C C   . VAL B 2 187 ? 16.690  -14.294 27.016  1.00 50.31  ?  187 VAL B C   1 
ATOM 3019 O O   . VAL B 2 187 ? 17.637  -13.500 27.035  1.00 55.25  ?  187 VAL B O   1 
ATOM 3020 C CB  . VAL B 2 187 ? 14.472  -13.513 26.109  1.00 45.24  ?  187 VAL B CB  1 
ATOM 3021 C CG1 . VAL B 2 187 ? 13.009  -13.309 26.457  1.00 45.38  ?  187 VAL B CG1 1 
ATOM 3022 C CG2 . VAL B 2 187 ? 15.042  -12.277 25.435  1.00 38.07  ?  187 VAL B CG2 1 
ATOM 3023 N N   . VAL B 2 188 ? 16.828  -15.580 26.703  1.00 49.13  ?  188 VAL B N   1 
ATOM 3024 C CA  . VAL B 2 188 ? 18.096  -16.163 26.273  1.00 55.91  ?  188 VAL B CA  1 
ATOM 3025 C C   . VAL B 2 188 ? 17.814  -17.133 25.134  1.00 51.19  ?  188 VAL B C   1 
ATOM 3026 O O   . VAL B 2 188 ? 16.799  -17.838 25.144  1.00 50.04  ?  188 VAL B O   1 
ATOM 3027 C CB  . VAL B 2 188 ? 18.832  -16.867 27.439  1.00 57.32  ?  188 VAL B CB  1 
ATOM 3028 C CG1 . VAL B 2 188 ? 17.943  -17.918 28.093  1.00 50.19  ?  188 VAL B CG1 1 
ATOM 3029 C CG2 . VAL B 2 188 ? 20.135  -17.493 26.958  1.00 58.40  ?  188 VAL B CG2 1 
ATOM 3030 N N   . THR B 2 189 ? 18.705  -17.163 24.147  1.00 55.56  ?  189 THR B N   1 
ATOM 3031 C CA  . THR B 2 189 ? 18.617  -18.112 23.044  1.00 57.53  ?  189 THR B CA  1 
ATOM 3032 C C   . THR B 2 189 ? 19.613  -19.245 23.254  1.00 55.24  ?  189 THR B C   1 
ATOM 3033 O O   . THR B 2 189 ? 20.772  -19.005 23.611  1.00 54.37  ?  189 THR B O   1 
ATOM 3034 C CB  . THR B 2 189 ? 18.871  -17.438 21.691  1.00 53.77  ?  189 THR B CB  1 
ATOM 3035 O OG1 . THR B 2 189 ? 20.022  -16.588 21.774  1.00 56.84  ?  189 THR B OG1 1 
ATOM 3036 C CG2 . THR B 2 189 ? 17.665  -16.614 21.269  1.00 51.95  ?  189 THR B CG2 1 
ATOM 3037 N N   . VAL B 2 190 ? 19.150  -20.474 23.046  1.00 52.77  ?  190 VAL B N   1 
ATOM 3038 C CA  . VAL B 2 190 ? 19.967  -21.670 23.239  1.00 57.08  ?  190 VAL B CA  1 
ATOM 3039 C C   . VAL B 2 190 ? 19.744  -22.617 22.067  1.00 66.28  ?  190 VAL B C   1 
ATOM 3040 O O   . VAL B 2 190 ? 18.740  -22.527 21.354  1.00 64.43  ?  190 VAL B O   1 
ATOM 3041 C CB  . VAL B 2 190 ? 19.637  -22.389 24.561  1.00 59.08  ?  190 VAL B CB  1 
ATOM 3042 C CG1 . VAL B 2 190 ? 20.017  -21.524 25.752  1.00 58.39  ?  190 VAL B CG1 1 
ATOM 3043 C CG2 . VAL B 2 190 ? 18.159  -22.747 24.605  1.00 58.22  ?  190 VAL B CG2 1 
ATOM 3044 N N   . PRO B 2 191 ? 20.689  -23.530 21.843  1.00 63.94  ?  191 PRO B N   1 
ATOM 3045 C CA  . PRO B 2 191 ? 20.450  -24.586 20.853  1.00 57.01  ?  191 PRO B CA  1 
ATOM 3046 C C   . PRO B 2 191 ? 19.230  -25.408 21.238  1.00 61.23  ?  191 PRO B C   1 
ATOM 3047 O O   . PRO B 2 191 ? 19.012  -25.717 22.411  1.00 67.50  ?  191 PRO B O   1 
ATOM 3048 C CB  . PRO B 2 191 ? 21.734  -25.418 20.912  1.00 57.35  ?  191 PRO B CB  1 
ATOM 3049 C CG  . PRO B 2 191 ? 22.770  -24.465 21.411  1.00 57.24  ?  191 PRO B CG  1 
ATOM 3050 C CD  . PRO B 2 191 ? 22.067  -23.552 22.361  1.00 53.61  ?  191 PRO B CD  1 
ATOM 3051 N N   . SER B 2 192 ? 18.422  -25.761 20.236  1.00 62.82  ?  192 SER B N   1 
ATOM 3052 C CA  . SER B 2 192 ? 17.199  -26.505 20.519  1.00 62.35  ?  192 SER B CA  1 
ATOM 3053 C C   . SER B 2 192 ? 17.492  -27.891 21.079  1.00 70.18  ?  192 SER B C   1 
ATOM 3054 O O   . SER B 2 192 ? 16.718  -28.405 21.897  1.00 69.60  ?  192 SER B O   1 
ATOM 3055 C CB  . SER B 2 192 ? 16.340  -26.618 19.265  1.00 62.11  ?  192 SER B CB  1 
ATOM 3056 O OG  . SER B 2 192 ? 15.119  -27.267 19.567  1.00 66.00  ?  192 SER B OG  1 
ATOM 3057 N N   . SER B 2 193 ? 18.602  -28.509 20.668  1.00 72.26  ?  193 SER B N   1 
ATOM 3058 C CA  . SER B 2 193 ? 18.940  -29.830 21.185  1.00 67.19  ?  193 SER B CA  1 
ATOM 3059 C C   . SER B 2 193 ? 19.415  -29.793 22.634  1.00 65.14  ?  193 SER B C   1 
ATOM 3060 O O   . SER B 2 193 ? 19.615  -30.859 23.224  1.00 60.14  ?  193 SER B O   1 
ATOM 3061 C CB  . SER B 2 193 ? 20.000  -30.488 20.296  1.00 58.53  ?  193 SER B CB  1 
ATOM 3062 O OG  . SER B 2 193 ? 21.183  -29.712 20.235  1.00 56.98  ?  193 SER B OG  1 
ATOM 3063 N N   . SER B 2 194 ? 19.609  -28.601 23.216  1.00 67.86  ?  194 SER B N   1 
ATOM 3064 C CA  . SER B 2 194 ? 19.986  -28.503 24.625  1.00 65.41  ?  194 SER B CA  1 
ATOM 3065 C C   . SER B 2 194 ? 18.808  -28.768 25.551  1.00 65.72  ?  194 SER B C   1 
ATOM 3066 O O   . SER B 2 194 ? 19.005  -29.226 26.684  1.00 63.64  ?  194 SER B O   1 
ATOM 3067 C CB  . SER B 2 194 ? 20.554  -27.118 24.941  1.00 58.39  ?  194 SER B CB  1 
ATOM 3068 O OG  . SER B 2 194 ? 21.770  -26.874 24.261  1.00 68.43  ?  194 SER B OG  1 
ATOM 3069 N N   . LEU B 2 195 ? 17.587  -28.514 25.086  1.00 64.08  ?  195 LEU B N   1 
ATOM 3070 C CA  . LEU B 2 195 ? 16.412  -28.698 25.922  1.00 60.55  ?  195 LEU B CA  1 
ATOM 3071 C C   . LEU B 2 195 ? 16.241  -30.172 26.258  1.00 70.52  ?  195 LEU B C   1 
ATOM 3072 O O   . LEU B 2 195 ? 16.508  -31.048 25.432  1.00 77.29  ?  195 LEU B O   1 
ATOM 3073 C CB  . LEU B 2 195 ? 15.166  -28.157 25.213  1.00 59.85  ?  195 LEU B CB  1 
ATOM 3074 C CG  . LEU B 2 195 ? 15.283  -26.773 24.552  1.00 66.24  ?  195 LEU B CG  1 
ATOM 3075 C CD1 . LEU B 2 195 ? 13.982  -26.341 23.880  1.00 52.88  ?  195 LEU B CD1 1 
ATOM 3076 C CD2 . LEU B 2 195 ? 15.737  -25.715 25.551  1.00 60.27  ?  195 LEU B CD2 1 
ATOM 3077 N N   . GLY B 2 196 ? 15.832  -30.448 27.490  1.00 67.43  ?  196 GLY B N   1 
ATOM 3078 C CA  . GLY B 2 196 ? 15.645  -31.825 27.914  1.00 71.56  ?  196 GLY B CA  1 
ATOM 3079 C C   . GLY B 2 196 ? 16.823  -32.394 28.679  1.00 76.24  ?  196 GLY B C   1 
ATOM 3080 O O   . GLY B 2 196 ? 16.641  -33.192 29.603  1.00 74.06  ?  196 GLY B O   1 
ATOM 3081 N N   . THR B 2 197 ? 18.038  -32.003 28.296  1.00 73.36  ?  197 THR B N   1 
ATOM 3082 C CA  . THR B 2 197 ? 19.237  -32.427 29.007  1.00 71.61  ?  197 THR B CA  1 
ATOM 3083 C C   . THR B 2 197 ? 19.883  -31.314 29.812  1.00 64.81  ?  197 THR B C   1 
ATOM 3084 O O   . THR B 2 197 ? 20.470  -31.590 30.858  1.00 73.13  ?  197 THR B O   1 
ATOM 3085 C CB  . THR B 2 197 ? 20.273  -33.002 28.031  1.00 68.81  ?  197 THR B CB  1 
ATOM 3086 O OG1 . THR B 2 197 ? 20.621  -32.013 27.054  1.00 67.12  ?  197 THR B OG1 1 
ATOM 3087 C CG2 . THR B 2 197 ? 19.714  -34.229 27.329  1.00 70.62  ?  197 THR B CG2 1 
ATOM 3088 N N   . GLN B 2 198 ? 19.789  -30.073 29.349  1.00 63.97  ?  198 GLN B N   1 
ATOM 3089 C CA  . GLN B 2 198 ? 20.334  -28.915 30.044  1.00 59.93  ?  198 GLN B CA  1 
ATOM 3090 C C   . GLN B 2 198 ? 19.204  -28.163 30.741  1.00 58.61  ?  198 GLN B C   1 
ATOM 3091 O O   . GLN B 2 198 ? 18.134  -27.964 30.156  1.00 60.94  ?  198 GLN B O   1 
ATOM 3092 C CB  . GLN B 2 198 ? 21.068  -27.997 29.065  1.00 56.21  ?  198 GLN B CB  1 
ATOM 3093 C CG  . GLN B 2 198 ? 21.563  -26.713 29.687  1.00 61.13  ?  198 GLN B CG  1 
ATOM 3094 C CD  . GLN B 2 198 ? 22.796  -26.925 30.538  1.00 63.29  ?  198 GLN B CD  1 
ATOM 3095 O OE1 . GLN B 2 198 ? 23.879  -27.199 30.021  1.00 57.46  ?  198 GLN B OE1 1 
ATOM 3096 N NE2 . GLN B 2 198 ? 22.633  -26.825 31.855  1.00 63.68  ?  198 GLN B NE2 1 
ATOM 3097 N N   . THR B 2 199 ? 19.422  -27.789 32.000  1.00 58.36  ?  199 THR B N   1 
ATOM 3098 C CA  . THR B 2 199 ? 18.433  -27.029 32.756  1.00 64.43  ?  199 THR B CA  1 
ATOM 3099 C C   . THR B 2 199 ? 18.718  -25.531 32.658  1.00 60.56  ?  199 THR B C   1 
ATOM 3100 O O   . THR B 2 199 ? 19.870  -25.099 32.539  1.00 56.29  ?  199 THR B O   1 
ATOM 3101 C CB  . THR B 2 199 ? 18.405  -27.457 34.226  1.00 65.77  ?  199 THR B CB  1 
ATOM 3102 O OG1 . THR B 2 199 ? 19.615  -27.044 34.874  1.00 61.06  ?  199 THR B OG1 1 
ATOM 3103 C CG2 . THR B 2 199 ? 18.260  -28.973 34.336  1.00 64.30  ?  199 THR B CG2 1 
ATOM 3104 N N   . TYR B 2 200 ? 17.647  -24.736 32.684  1.00 57.02  ?  200 TYR B N   1 
ATOM 3105 C CA  . TYR B 2 200 ? 17.749  -23.284 32.560  1.00 58.59  ?  200 TYR B CA  1 
ATOM 3106 C C   . TYR B 2 200 ? 16.985  -22.629 33.705  1.00 60.86  ?  200 TYR B C   1 
ATOM 3107 O O   . TYR B 2 200 ? 15.752  -22.718 33.766  1.00 61.26  ?  200 TYR B O   1 
ATOM 3108 C CB  . TYR B 2 200 ? 17.228  -22.820 31.199  1.00 50.36  ?  200 TYR B CB  1 
ATOM 3109 C CG  . TYR B 2 200 ? 18.099  -23.316 30.069  1.00 52.28  ?  200 TYR B CG  1 
ATOM 3110 C CD1 . TYR B 2 200 ? 19.331  -22.728 29.815  1.00 51.59  ?  200 TYR B CD1 1 
ATOM 3111 C CD2 . TYR B 2 200 ? 17.712  -24.402 29.285  1.00 48.05  ?  200 TYR B CD2 1 
ATOM 3112 C CE1 . TYR B 2 200 ? 20.141  -23.190 28.797  1.00 54.29  ?  200 TYR B CE1 1 
ATOM 3113 C CE2 . TYR B 2 200 ? 18.519  -24.871 28.266  1.00 44.82  ?  200 TYR B CE2 1 
ATOM 3114 C CZ  . TYR B 2 200 ? 19.732  -24.258 28.027  1.00 48.55  ?  200 TYR B CZ  1 
ATOM 3115 O OH  . TYR B 2 200 ? 20.548  -24.709 27.014  1.00 53.05  ?  200 TYR B OH  1 
ATOM 3116 N N   . ILE B 2 201 ? 17.715  -21.970 34.607  1.00 56.90  ?  201 ILE B N   1 
ATOM 3117 C CA  . ILE B 2 201 ? 17.136  -21.287 35.759  1.00 55.34  ?  201 ILE B CA  1 
ATOM 3118 C C   . ILE B 2 201 ? 17.506  -19.812 35.687  1.00 53.19  ?  201 ILE B C   1 
ATOM 3119 O O   . ILE B 2 201 ? 18.691  -19.466 35.604  1.00 51.46  ?  201 ILE B O   1 
ATOM 3120 C CB  . ILE B 2 201 ? 17.618  -21.890 37.091  1.00 52.31  ?  201 ILE B CB  1 
ATOM 3121 C CG1 . ILE B 2 201 ? 17.418  -23.404 37.111  1.00 54.36  ?  201 ILE B CG1 1 
ATOM 3122 C CG2 . ILE B 2 201 ? 16.889  -21.238 38.256  1.00 51.37  ?  201 ILE B CG2 1 
ATOM 3123 C CD1 . ILE B 2 201 ? 18.022  -24.068 38.329  1.00 49.25  ?  201 ILE B CD1 1 
ATOM 3124 N N   . CYS B 2 202 ? 16.497  -18.946 35.747  1.00 49.62  ?  202 CYS B N   1 
ATOM 3125 C CA  . CYS B 2 202 ? 16.730  -17.514 35.844  1.00 54.76  ?  202 CYS B CA  1 
ATOM 3126 C C   . CYS B 2 202 ? 16.770  -17.109 37.310  1.00 58.58  ?  202 CYS B C   1 
ATOM 3127 O O   . CYS B 2 202 ? 16.009  -17.628 38.132  1.00 58.62  ?  202 CYS B O   1 
ATOM 3128 C CB  . CYS B 2 202 ? 15.644  -16.725 35.108  1.00 58.06  ?  202 CYS B CB  1 
ATOM 3129 S SG  . CYS B 2 202 ? 13.993  -16.806 35.853  1.00 72.15  ?  202 CYS B SG  1 
ATOM 3130 N N   . ASN B 2 203 ? 17.669  -16.183 37.631  1.00 59.05  ?  203 ASN B N   1 
ATOM 3131 C CA  . ASN B 2 203 ? 17.931  -15.769 39.007  1.00 55.52  ?  203 ASN B CA  1 
ATOM 3132 C C   . ASN B 2 203 ? 17.524  -14.308 39.148  1.00 55.10  ?  203 ASN B C   1 
ATOM 3133 O O   . ASN B 2 203 ? 18.282  -13.408 38.776  1.00 57.44  ?  203 ASN B O   1 
ATOM 3134 C CB  . ASN B 2 203 ? 19.396  -15.976 39.374  1.00 55.00  ?  203 ASN B CB  1 
ATOM 3135 C CG  . ASN B 2 203 ? 19.932  -17.305 38.892  1.00 56.83  ?  203 ASN B CG  1 
ATOM 3136 O OD1 . ASN B 2 203 ? 20.914  -17.353 38.155  1.00 57.27  ?  203 ASN B OD1 1 
ATOM 3137 N ND2 . ASN B 2 203 ? 19.287  -18.396 39.301  1.00 55.55  ?  203 ASN B ND2 1 
ATOM 3138 N N   . VAL B 2 204 ? 16.323  -14.079 39.670  1.00 50.04  ?  204 VAL B N   1 
ATOM 3139 C CA  . VAL B 2 204 ? 15.806  -12.733 39.884  1.00 52.98  ?  204 VAL B CA  1 
ATOM 3140 C C   . VAL B 2 204 ? 16.182  -12.273 41.285  1.00 50.91  ?  204 VAL B C   1 
ATOM 3141 O O   . VAL B 2 204 ? 15.898  -12.960 42.272  1.00 52.85  ?  204 VAL B O   1 
ATOM 3142 C CB  . VAL B 2 204 ? 14.282  -12.695 39.680  1.00 57.29  ?  204 VAL B CB  1 
ATOM 3143 C CG1 . VAL B 2 204 ? 13.743  -11.301 39.947  1.00 49.64  ?  204 VAL B CG1 1 
ATOM 3144 C CG2 . VAL B 2 204 ? 13.932  -13.133 38.259  1.00 59.53  ?  204 VAL B CG2 1 
ATOM 3145 N N   . ASN B 2 205 ? 16.803  -11.101 41.375  1.00 54.40  ?  205 ASN B N   1 
ATOM 3146 C CA  . ASN B 2 205 ? 17.205  -10.512 42.646  1.00 56.04  ?  205 ASN B CA  1 
ATOM 3147 C C   . ASN B 2 205 ? 16.571  -9.135  42.765  1.00 56.03  ?  205 ASN B C   1 
ATOM 3148 O O   . ASN B 2 205 ? 16.595  -8.353  41.808  1.00 56.71  ?  205 ASN B O   1 
ATOM 3149 C CB  . ASN B 2 205 ? 18.730  -10.412 42.755  1.00 59.22  ?  205 ASN B CB  1 
ATOM 3150 C CG  . ASN B 2 205 ? 19.208  -10.285 44.194  1.00 67.35  ?  205 ASN B CG  1 
ATOM 3151 O OD1 . ASN B 2 205 ? 18.633  -9.547  44.995  1.00 71.48  ?  205 ASN B OD1 1 
ATOM 3152 N ND2 . ASN B 2 205 ? 20.264  -11.020 44.529  1.00 76.62  ?  205 ASN B ND2 1 
ATOM 3153 N N   . HIS B 2 206 ? 15.979  -8.849  43.935  1.00 58.95  ?  206 HIS B N   1 
ATOM 3154 C CA  . HIS B 2 206 ? 15.278  -7.581  44.182  1.00 58.01  ?  206 HIS B CA  1 
ATOM 3155 C C   . HIS B 2 206 ? 15.704  -7.092  45.567  1.00 59.71  ?  206 HIS B C   1 
ATOM 3156 O O   . HIS B 2 206 ? 14.958  -7.202  46.543  1.00 65.49  ?  206 HIS B O   1 
ATOM 3157 C CB  . HIS B 2 206 ? 13.763  -7.753  44.071  1.00 58.34  ?  206 HIS B CB  1 
ATOM 3158 C CG  . HIS B 2 206 ? 12.993  -6.477  44.209  1.00 57.14  ?  206 HIS B CG  1 
ATOM 3159 N ND1 . HIS B 2 206 ? 12.004  -6.301  45.153  1.00 56.78  ?  206 HIS B ND1 1 
ATOM 3160 C CD2 . HIS B 2 206 ? 13.074  -5.309  43.528  1.00 59.52  ?  206 HIS B CD2 1 
ATOM 3161 C CE1 . HIS B 2 206 ? 11.502  -5.084  45.040  1.00 57.52  ?  206 HIS B CE1 1 
ATOM 3162 N NE2 . HIS B 2 206 ? 12.136  -4.460  44.064  1.00 56.22  ?  206 HIS B NE2 1 
ATOM 3163 N N   . LYS B 2 207 ? 16.920  -6.553  45.642  1.00 59.39  ?  207 LYS B N   1 
ATOM 3164 C CA  . LYS B 2 207 ? 17.469  -6.111  46.921  1.00 58.09  ?  207 LYS B CA  1 
ATOM 3165 C C   . LYS B 2 207 ? 16.589  -5.121  47.678  1.00 57.25  ?  207 LYS B C   1 
ATOM 3166 O O   . LYS B 2 207 ? 16.548  -5.210  48.917  1.00 63.83  ?  207 LYS B O   1 
ATOM 3167 C CB  . LYS B 2 207 ? 18.872  -5.521  46.711  1.00 61.38  ?  207 LYS B CB  1 
ATOM 3168 C CG  . LYS B 2 207 ? 19.949  -6.552  46.429  1.00 70.95  ?  207 LYS B CG  1 
ATOM 3169 C CD  . LYS B 2 207 ? 21.325  -5.903  46.389  1.00 85.95  ?  207 LYS B CD  1 
ATOM 3170 C CE  . LYS B 2 207 ? 22.419  -6.928  46.127  1.00 96.54  ?  207 LYS B CE  1 
ATOM 3171 N NZ  . LYS B 2 207 ? 23.769  -6.295  46.107  1.00 96.51  ?  207 LYS B NZ  1 
ATOM 3172 N N   . PRO B 2 208 ? 15.877  -4.183  47.040  1.00 53.02  ?  208 PRO B N   1 
ATOM 3173 C CA  . PRO B 2 208 ? 14.961  -3.325  47.813  1.00 59.77  ?  208 PRO B CA  1 
ATOM 3174 C C   . PRO B 2 208 ? 13.955  -4.078  48.681  1.00 60.67  ?  208 PRO B C   1 
ATOM 3175 O O   . PRO B 2 208 ? 13.490  -3.524  49.687  1.00 63.49  ?  208 PRO B O   1 
ATOM 3176 C CB  . PRO B 2 208 ? 14.272  -2.501  46.719  1.00 59.00  ?  208 PRO B CB  1 
ATOM 3177 C CG  . PRO B 2 208 ? 15.323  -2.342  45.697  1.00 59.22  ?  208 PRO B CG  1 
ATOM 3178 C CD  . PRO B 2 208 ? 16.089  -3.643  45.683  1.00 60.54  ?  208 PRO B CD  1 
ATOM 3179 N N   . SER B 2 209 ? 13.594  -5.313  48.333  1.00 57.64  ?  209 SER B N   1 
ATOM 3180 C CA  . SER B 2 209 ? 12.711  -6.110  49.179  1.00 56.94  ?  209 SER B CA  1 
ATOM 3181 C C   . SER B 2 209 ? 13.412  -7.343  49.729  1.00 55.57  ?  209 SER B C   1 
ATOM 3182 O O   . SER B 2 209 ? 12.753  -8.200  50.326  1.00 53.96  ?  209 SER B O   1 
ATOM 3183 C CB  . SER B 2 209 ? 11.448  -6.528  48.422  1.00 53.18  ?  209 SER B CB  1 
ATOM 3184 O OG  . SER B 2 209 ? 11.734  -7.487  47.422  1.00 66.37  ?  209 SER B OG  1 
ATOM 3185 N N   . ASN B 2 210 ? 14.725  -7.456  49.530  1.00 56.39  ?  210 ASN B N   1 
ATOM 3186 C CA  . ASN B 2 210 ? 15.500  -8.605  49.989  1.00 62.04  ?  210 ASN B CA  1 
ATOM 3187 C C   . ASN B 2 210 ? 14.879  -9.915  49.505  1.00 63.71  ?  210 ASN B C   1 
ATOM 3188 O O   . ASN B 2 210 ? 14.818  -10.909 50.232  1.00 63.61  ?  210 ASN B O   1 
ATOM 3189 C CB  . ASN B 2 210 ? 15.649  -8.585  51.512  1.00 66.45  ?  210 ASN B CB  1 
ATOM 3190 C CG  . ASN B 2 210 ? 16.242  -7.275  52.025  1.00 71.48  ?  210 ASN B CG  1 
ATOM 3191 O OD1 . ASN B 2 210 ? 17.462  -7.106  52.065  1.00 78.13  ?  210 ASN B OD1 1 
ATOM 3192 N ND2 . ASN B 2 210 ? 15.375  -6.342  52.424  1.00 60.25  ?  210 ASN B ND2 1 
ATOM 3193 N N   . THR B 2 211 ? 14.420  -9.915  48.256  1.00 62.81  ?  211 THR B N   1 
ATOM 3194 C CA  . THR B 2 211 ? 13.777  -11.069 47.644  1.00 65.30  ?  211 THR B CA  1 
ATOM 3195 C C   . THR B 2 211 ? 14.661  -11.603 46.525  1.00 62.74  ?  211 THR B C   1 
ATOM 3196 O O   . THR B 2 211 ? 15.236  -10.831 45.751  1.00 63.93  ?  211 THR B O   1 
ATOM 3197 C CB  . THR B 2 211 ? 12.398  -10.704 47.077  1.00 62.09  ?  211 THR B CB  1 
ATOM 3198 O OG1 . THR B 2 211 ? 11.594  -10.102 48.100  1.00 58.15  ?  211 THR B OG1 1 
ATOM 3199 C CG2 . THR B 2 211 ? 11.688  -11.940 46.539  1.00 61.46  ?  211 THR B CG2 1 
ATOM 3200 N N   . LYS B 2 212 ? 14.756  -12.925 46.439  1.00 52.06  ?  212 LYS B N   1 
ATOM 3201 C CA  . LYS B 2 212 ? 15.537  -13.582 45.401  1.00 56.65  ?  212 LYS B CA  1 
ATOM 3202 C C   . LYS B 2 212 ? 14.734  -14.770 44.892  1.00 60.75  ?  212 LYS B C   1 
ATOM 3203 O O   . LYS B 2 212 ? 14.309  -15.618 45.683  1.00 63.39  ?  212 LYS B O   1 
ATOM 3204 C CB  . LYS B 2 212 ? 16.904  -14.018 45.943  1.00 60.23  ?  212 LYS B CB  1 
ATOM 3205 C CG  . LYS B 2 212 ? 17.865  -14.568 44.899  1.00 69.56  ?  212 LYS B CG  1 
ATOM 3206 C CD  . LYS B 2 212 ? 19.254  -14.794 45.492  1.00 79.25  ?  212 LYS B CD  1 
ATOM 3207 C CE  . LYS B 2 212 ? 20.233  -15.317 44.446  1.00 87.16  ?  212 LYS B CE  1 
ATOM 3208 N NZ  . LYS B 2 212 ? 19.842  -16.668 43.946  1.00 79.68  ?  212 LYS B NZ  1 
ATOM 3209 N N   . VAL B 2 213 ? 14.501  -14.817 43.581  1.00 53.73  ?  213 VAL B N   1 
ATOM 3210 C CA  . VAL B 2 213 ? 13.682  -15.852 42.960  1.00 54.79  ?  213 VAL B CA  1 
ATOM 3211 C C   . VAL B 2 213 ? 14.536  -16.646 41.982  1.00 52.43  ?  213 VAL B C   1 
ATOM 3212 O O   . VAL B 2 213 ? 15.213  -16.066 41.124  1.00 53.38  ?  213 VAL B O   1 
ATOM 3213 C CB  . VAL B 2 213 ? 12.461  -15.254 42.237  1.00 50.41  ?  213 VAL B CB  1 
ATOM 3214 C CG1 . VAL B 2 213 ? 11.621  -16.363 41.628  1.00 55.24  ?  213 VAL B CG1 1 
ATOM 3215 C CG2 . VAL B 2 213 ? 11.635  -14.404 43.187  1.00 44.82  ?  213 VAL B CG2 1 
ATOM 3216 N N   . ASP B 2 214 ? 14.478  -17.968 42.090  1.00 52.52  ?  214 ASP B N   1 
ATOM 3217 C CA  . ASP B 2 214 ? 15.119  -18.869 41.140  1.00 55.85  ?  214 ASP B CA  1 
ATOM 3218 C C   . ASP B 2 214 ? 14.020  -19.704 40.495  1.00 54.50  ?  214 ASP B C   1 
ATOM 3219 O O   . ASP B 2 214 ? 13.407  -20.547 41.156  1.00 61.22  ?  214 ASP B O   1 
ATOM 3220 C CB  . ASP B 2 214 ? 16.173  -19.745 41.820  1.00 53.20  ?  214 ASP B CB  1 
ATOM 3221 C CG  . ASP B 2 214 ? 17.225  -18.932 42.550  1.00 59.98  ?  214 ASP B CG  1 
ATOM 3222 O OD1 . ASP B 2 214 ? 17.113  -18.793 43.787  1.00 76.26  ?  214 ASP B OD1 1 
ATOM 3223 O OD2 . ASP B 2 214 ? 18.161  -18.424 41.890  1.00 57.05  ?  214 ASP B OD2 1 
ATOM 3224 N N   . LYS B 2 215 ? 13.749  -19.444 39.221  1.00 50.96  ?  215 LYS B N   1 
ATOM 3225 C CA  . LYS B 2 215 ? 12.701  -20.128 38.473  1.00 59.76  ?  215 LYS B CA  1 
ATOM 3226 C C   . LYS B 2 215 ? 13.349  -20.991 37.397  1.00 62.45  ?  215 LYS B C   1 
ATOM 3227 O O   . LYS B 2 215 ? 14.054  -20.471 36.525  1.00 61.35  ?  215 LYS B O   1 
ATOM 3228 C CB  . LYS B 2 215 ? 11.745  -19.115 37.844  1.00 63.12  ?  215 LYS B CB  1 
ATOM 3229 C CG  . LYS B 2 215 ? 10.498  -19.699 37.208  1.00 61.14  ?  215 LYS B CG  1 
ATOM 3230 C CD  . LYS B 2 215 ? 9.701   -20.504 38.219  1.00 66.15  ?  215 LYS B CD  1 
ATOM 3231 C CE  . LYS B 2 215 ? 8.255   -20.688 37.768  1.00 72.61  ?  215 LYS B CE  1 
ATOM 3232 N NZ  . LYS B 2 215 ? 8.090   -21.763 36.748  1.00 73.08  ?  215 LYS B NZ  1 
ATOM 3233 N N   . LYS B 2 216 ? 13.111  -22.299 37.454  1.00 63.51  ?  216 LYS B N   1 
ATOM 3234 C CA  . LYS B 2 216 ? 13.602  -23.207 36.421  1.00 68.35  ?  216 LYS B CA  1 
ATOM 3235 C C   . LYS B 2 216 ? 12.627  -23.182 35.247  1.00 65.13  ?  216 LYS B C   1 
ATOM 3236 O O   . LYS B 2 216 ? 11.469  -23.590 35.386  1.00 65.91  ?  216 LYS B O   1 
ATOM 3237 C CB  . LYS B 2 216 ? 13.768  -24.617 36.982  1.00 63.62  ?  216 LYS B CB  1 
ATOM 3238 C CG  . LYS B 2 216 ? 14.249  -25.637 35.960  1.00 68.79  ?  216 LYS B CG  1 
ATOM 3239 C CD  . LYS B 2 216 ? 14.421  -27.021 36.583  1.00 79.94  ?  216 LYS B CD  1 
ATOM 3240 C CE  . LYS B 2 216 ? 14.811  -28.065 35.541  1.00 77.37  ?  216 LYS B CE  1 
ATOM 3241 N NZ  . LYS B 2 216 ? 14.860  -29.442 36.111  1.00 80.81  ?  216 LYS B NZ  1 
ATOM 3242 N N   . VAL B 2 217 ? 13.075  -22.682 34.099  1.00 61.03  ?  217 VAL B N   1 
ATOM 3243 C CA  . VAL B 2 217 ? 12.230  -22.645 32.908  1.00 67.78  ?  217 VAL B CA  1 
ATOM 3244 C C   . VAL B 2 217 ? 12.289  -23.996 32.203  1.00 69.46  ?  217 VAL B C   1 
ATOM 3245 O O   . VAL B 2 217 ? 13.364  -24.444 31.789  1.00 67.77  ?  217 VAL B O   1 
ATOM 3246 C CB  . VAL B 2 217 ? 12.652  -21.518 31.957  1.00 60.02  ?  217 VAL B CB  1 
ATOM 3247 C CG1 . VAL B 2 217 ? 11.704  -21.463 30.775  1.00 59.35  ?  217 VAL B CG1 1 
ATOM 3248 C CG2 . VAL B 2 217 ? 12.680  -20.186 32.683  1.00 61.20  ?  217 VAL B CG2 1 
ATOM 3249 N N   . GLU B 2 218 ? 11.130  -24.639 32.054  1.00 66.76  ?  218 GLU B N   1 
ATOM 3250 C CA  . GLU B 2 218 ? 11.036  -25.946 31.428  1.00 64.55  ?  218 GLU B CA  1 
ATOM 3251 C C   . GLU B 2 218 ? 10.181  -25.867 30.169  1.00 67.32  ?  218 GLU B C   1 
ATOM 3252 O O   . GLU B 2 218 ? 9.252   -25.055 30.093  1.00 65.35  ?  218 GLU B O   1 
ATOM 3253 C CB  . GLU B 2 218 ? 10.439  -26.984 32.389  1.00 70.49  ?  218 GLU B CB  1 
ATOM 3254 C CG  . GLU B 2 218 ? 11.319  -27.295 33.595  1.00 74.19  ?  218 GLU B CG  1 
ATOM 3255 C CD  . GLU B 2 218 ? 10.774  -28.426 34.454  1.00 80.22  ?  218 GLU B CD  1 
ATOM 3256 O OE1 . GLU B 2 218 ? 9.535   -28.534 34.578  1.00 79.36  ?  218 GLU B OE1 1 
ATOM 3257 O OE2 . GLU B 2 218 ? 11.587  -29.206 35.003  1.00 80.90  ?  218 GLU B OE2 1 
ATOM 3258 N N   . PRO B 2 219 ? 10.468  -26.700 29.168  1.00 70.82  ?  219 PRO B N   1 
ATOM 3259 C CA  . PRO B 2 219 ? 9.663   -26.691 27.940  1.00 69.65  ?  219 PRO B CA  1 
ATOM 3260 C C   . PRO B 2 219 ? 8.209   -27.058 28.201  1.00 75.22  ?  219 PRO B C   1 
ATOM 3261 O O   . PRO B 2 219 ? 7.900   -27.905 29.044  1.00 74.70  ?  219 PRO B O   1 
ATOM 3262 C CB  . PRO B 2 219 ? 10.354  -27.736 27.058  1.00 65.30  ?  219 PRO B CB  1 
ATOM 3263 C CG  . PRO B 2 219 ? 11.751  -27.808 27.582  1.00 62.57  ?  219 PRO B CG  1 
ATOM 3264 C CD  . PRO B 2 219 ? 11.633  -27.595 29.058  1.00 67.71  ?  219 PRO B CD  1 
ATOM 3265 N N   . LYS B 2 220 ? 7.315   -26.414 27.457  1.00 78.02  ?  220 LYS B N   1 
ATOM 3266 C CA  . LYS B 2 220 ? 5.885   -26.694 27.505  1.00 88.07  ?  220 LYS B CA  1 
ATOM 3267 C C   . LYS B 2 220 ? 5.535   -27.563 26.300  1.00 100.75 ?  220 LYS B C   1 
ATOM 3268 O O   . LYS B 2 220 ? 5.782   -27.169 25.155  1.00 98.49  ?  220 LYS B O   1 
ATOM 3269 C CB  . LYS B 2 220 ? 5.076   -25.394 27.518  1.00 81.20  ?  220 LYS B CB  1 
ATOM 3270 C CG  . LYS B 2 220 ? 3.599   -25.554 27.869  1.00 87.11  ?  220 LYS B CG  1 
ATOM 3271 C CD  . LYS B 2 220 ? 3.025   -24.264 28.451  1.00 79.32  ?  220 LYS B CD  1 
ATOM 3272 C CE  . LYS B 2 220 ? 3.677   -23.936 29.799  1.00 83.02  ?  220 LYS B CE  1 
ATOM 3273 N NZ  . LYS B 2 220 ? 3.169   -22.684 30.437  1.00 72.35  ?  220 LYS B NZ  1 
ATOM 3274 N N   . SER B 2 221 ? 4.984   -28.748 26.557  1.00 109.58 ?  221 SER B N   1 
ATOM 3275 C CA  . SER B 2 221 ? 4.757   -29.731 25.504  1.00 121.25 ?  221 SER B CA  1 
ATOM 3276 C C   . SER B 2 221 ? 3.464   -29.418 24.745  1.00 124.17 ?  221 SER B C   1 
ATOM 3277 O O   . SER B 2 221 ? 2.851   -28.359 24.911  1.00 121.29 ?  221 SER B O   1 
ATOM 3278 C CB  . SER B 2 221 ? 4.743   -31.139 26.095  1.00 124.82 ?  221 SER B CB  1 
ATOM 3279 O OG  . SER B 2 221 ? 4.322   -32.096 25.140  1.00 124.25 ?  221 SER B OG  1 
ATOM 3280 N N   . CYS B 2 222 ? 3.035   -30.355 23.897  1.00 128.15 ?  222 CYS B N   1 
ATOM 3281 C CA  . CYS B 2 222 ? 1.783   -30.255 23.157  1.00 132.41 ?  222 CYS B CA  1 
ATOM 3282 C C   . CYS B 2 222 ? 1.013   -31.565 23.251  1.00 138.85 ?  222 CYS B C   1 
ATOM 3283 O O   . CYS B 2 222 ? 1.600   -32.649 23.176  1.00 137.36 ?  222 CYS B O   1 
ATOM 3284 C CB  . CYS B 2 222 ? 2.036   -29.903 21.676  1.00 132.79 ?  222 CYS B CB  1 
ATOM 3285 S SG  . CYS B 2 222 ? 0.544   -29.865 20.636  1.00 147.86 ?  222 CYS B SG  1 
ATOM 3286 N N   . GLY B 2 223 ? -0.302  -31.456 23.422  1.00 138.30 ?  223 GLY B N   1 
ATOM 3287 C CA  . GLY B 2 223 ? -1.161  -32.621 23.523  1.00 132.28 ?  223 GLY B CA  1 
ATOM 3288 C C   . GLY B 2 223 ? -2.482  -32.331 24.209  1.00 125.86 ?  223 GLY B C   1 
ATOM 3289 O O   . GLY B 2 223 ? -2.514  -31.981 25.390  1.00 118.77 ?  223 GLY B O   1 
ATOM 3290 N N   . ALA C 1 1   ? -4.934  8.327   5.675   1.00 90.33  ?  1   ALA C N   1 
ATOM 3291 C CA  . ALA C 1 1   ? -5.110  7.322   6.714   1.00 82.56  ?  1   ALA C CA  1 
ATOM 3292 C C   . ALA C 1 1   ? -4.426  7.758   8.002   1.00 86.27  ?  1   ALA C C   1 
ATOM 3293 O O   . ALA C 1 1   ? -4.558  7.102   9.036   1.00 91.59  ?  1   ALA C O   1 
ATOM 3294 C CB  . ALA C 1 1   ? -4.564  5.976   6.252   1.00 87.67  ?  1   ALA C CB  1 
ATOM 3295 N N   . ILE C 1 2   ? -3.697  8.870   7.942   1.00 80.74  ?  2   ILE C N   1 
ATOM 3296 C CA  . ILE C 1 2   ? -2.926  9.362   9.075   1.00 81.67  ?  2   ILE C CA  1 
ATOM 3297 C C   . ILE C 1 2   ? -3.343  10.792  9.402   1.00 83.17  ?  2   ILE C C   1 
ATOM 3298 O O   . ILE C 1 2   ? -3.624  11.593  8.503   1.00 82.14  ?  2   ILE C O   1 
ATOM 3299 C CB  . ILE C 1 2   ? -1.412  9.278   8.793   1.00 75.77  ?  2   ILE C CB  1 
ATOM 3300 C CG1 . ILE C 1 2   ? -0.613  9.633   10.039  1.00 81.87  ?  2   ILE C CG1 1 
ATOM 3301 C CG2 . ILE C 1 2   ? -1.009  10.172  7.638   1.00 74.51  ?  2   ILE C CG2 1 
ATOM 3302 C CD1 . ILE C 1 2   ? 0.819   9.348   9.861   1.00 85.77  ?  2   ILE C CD1 1 
ATOM 3303 N N   . GLN C 1 3   ? -3.390  11.102  10.700  1.00 80.00  ?  3   GLN C N   1 
ATOM 3304 C CA  . GLN C 1 3   ? -3.770  12.417  11.198  1.00 74.27  ?  3   GLN C CA  1 
ATOM 3305 C C   . GLN C 1 3   ? -2.770  12.869  12.250  1.00 68.05  ?  3   GLN C C   1 
ATOM 3306 O O   . GLN C 1 3   ? -2.318  12.069  13.074  1.00 72.05  ?  3   GLN C O   1 
ATOM 3307 C CB  . GLN C 1 3   ? -5.188  12.419  11.791  1.00 70.02  ?  3   GLN C CB  1 
ATOM 3308 C CG  . GLN C 1 3   ? -6.294  12.205  10.764  1.00 86.43  ?  3   GLN C CG  1 
ATOM 3309 C CD  . GLN C 1 3   ? -6.446  10.754  10.336  1.00 89.63  ?  3   GLN C CD  1 
ATOM 3310 O OE1 . GLN C 1 3   ? -6.484  9.849   11.170  1.00 94.20  ?  3   GLN C OE1 1 
ATOM 3311 N NE2 . GLN C 1 3   ? -6.528  10.527  9.027   1.00 86.83  ?  3   GLN C NE2 1 
ATOM 3312 N N   . MET C 1 4   ? -2.423  14.149  12.215  1.00 60.87  ?  4   MET C N   1 
ATOM 3313 C CA  . MET C 1 4   ? -1.529  14.751  13.195  1.00 62.61  ?  4   MET C CA  1 
ATOM 3314 C C   . MET C 1 4   ? -2.315  15.738  14.049  1.00 58.27  ?  4   MET C C   1 
ATOM 3315 O O   . MET C 1 4   ? -2.820  16.743  13.538  1.00 58.25  ?  4   MET C O   1 
ATOM 3316 C CB  . MET C 1 4   ? -0.354  15.439  12.502  1.00 64.72  ?  4   MET C CB  1 
ATOM 3317 C CG  . MET C 1 4   ? 0.600   14.468  11.826  1.00 62.59  ?  4   MET C CG  1 
ATOM 3318 S SD  . MET C 1 4   ? 1.414   13.385  13.015  1.00 69.53  ?  4   MET C SD  1 
ATOM 3319 C CE  . MET C 1 4   ? 1.589   11.897  12.051  1.00 71.60  ?  4   MET C CE  1 
ATOM 3320 N N   . THR C 1 5   ? -2.418  15.456  15.345  1.00 58.28  ?  5   THR C N   1 
ATOM 3321 C CA  . THR C 1 5   ? -3.112  16.341  16.275  1.00 54.05  ?  5   THR C CA  1 
ATOM 3322 C C   . THR C 1 5   ? -2.072  17.180  17.003  1.00 52.67  ?  5   THR C C   1 
ATOM 3323 O O   . THR C 1 5   ? -1.328  16.667  17.840  1.00 55.51  ?  5   THR C O   1 
ATOM 3324 C CB  . THR C 1 5   ? -3.964  15.554  17.264  1.00 47.60  ?  5   THR C CB  1 
ATOM 3325 O OG1 . THR C 1 5   ? -4.911  14.755  16.546  1.00 53.01  ?  5   THR C OG1 1 
ATOM 3326 C CG2 . THR C 1 5   ? -4.709  16.505  18.182  1.00 49.89  ?  5   THR C CG2 1 
ATOM 3327 N N   . GLN C 1 6   ? -2.018  18.464  16.679  1.00 58.90  ?  6   GLN C N   1 
ATOM 3328 C CA  . GLN C 1 6   ? -1.053  19.370  17.276  1.00 53.58  ?  6   GLN C CA  1 
ATOM 3329 C C   . GLN C 1 6   ? -1.719  20.152  18.398  1.00 54.16  ?  6   GLN C C   1 
ATOM 3330 O O   . GLN C 1 6   ? -2.916  20.445  18.347  1.00 55.78  ?  6   GLN C O   1 
ATOM 3331 C CB  . GLN C 1 6   ? -0.481  20.329  16.232  1.00 51.38  ?  6   GLN C CB  1 
ATOM 3332 C CG  . GLN C 1 6   ? 0.821   20.972  16.653  1.00 50.63  ?  6   GLN C CG  1 
ATOM 3333 C CD  . GLN C 1 6   ? 1.451   21.779  15.549  1.00 50.07  ?  6   GLN C CD  1 
ATOM 3334 O OE1 . GLN C 1 6   ? 1.156   21.580  14.369  1.00 56.54  ?  6   GLN C OE1 1 
ATOM 3335 N NE2 . GLN C 1 6   ? 2.334   22.694  15.922  1.00 47.37  ?  6   GLN C NE2 1 
ATOM 3336 N N   . SER C 1 7   ? -0.932  20.474  19.425  1.00 52.87  ?  7   SER C N   1 
ATOM 3337 C CA  . SER C 1 7   ? -1.462  21.189  20.566  1.00 52.75  ?  7   SER C CA  1 
ATOM 3338 C C   . SER C 1 7   ? -0.351  21.985  21.239  1.00 53.01  ?  7   SER C C   1 
ATOM 3339 O O   . SER C 1 7   ? 0.801   21.520  21.286  1.00 54.75  ?  7   SER C O   1 
ATOM 3340 C CB  . SER C 1 7   ? -2.117  20.235  21.571  1.00 53.77  ?  7   SER C CB  1 
ATOM 3341 O OG  . SER C 1 7   ? -2.877  20.948  22.533  1.00 59.19  ?  7   SER C OG  1 
ATOM 3342 N N   . PRO C 1 8   ? -0.645  23.205  21.711  1.00 52.78  ?  8   PRO C N   1 
ATOM 3343 C CA  . PRO C 1 8   ? -1.943  23.853  21.509  1.00 58.31  ?  8   PRO C CA  1 
ATOM 3344 C C   . PRO C 1 8   ? -1.967  24.636  20.202  1.00 52.28  ?  8   PRO C C   1 
ATOM 3345 O O   . PRO C 1 8   ? -0.950  24.679  19.510  1.00 50.60  ?  8   PRO C O   1 
ATOM 3346 C CB  . PRO C 1 8   ? -2.046  24.790  22.710  1.00 51.11  ?  8   PRO C CB  1 
ATOM 3347 C CG  . PRO C 1 8   ? -0.636  25.199  22.940  1.00 49.79  ?  8   PRO C CG  1 
ATOM 3348 C CD  . PRO C 1 8   ? 0.217   23.991  22.608  1.00 49.20  ?  8   PRO C CD  1 
ATOM 3349 N N   . SER C 1 9   ? -3.110  25.241  19.870  1.00 52.49  ?  9   SER C N   1 
ATOM 3350 C CA  . SER C 1 9   ? -3.186  26.065  18.667  1.00 48.24  ?  9   SER C CA  1 
ATOM 3351 C C   . SER C 1 9   ? -2.379  27.346  18.821  1.00 52.80  ?  9   SER C C   1 
ATOM 3352 O O   . SER C 1 9   ? -1.858  27.873  17.831  1.00 52.77  ?  9   SER C O   1 
ATOM 3353 C CB  . SER C 1 9   ? -4.638  26.412  18.352  1.00 44.42  ?  9   SER C CB  1 
ATOM 3354 O OG  . SER C 1 9   ? -5.436  25.245  18.291  1.00 58.87  ?  9   SER C OG  1 
ATOM 3355 N N   . SER C 1 10  ? -2.255  27.849  20.047  1.00 54.79  ?  10  SER C N   1 
ATOM 3356 C CA  . SER C 1 10  ? -1.557  29.100  20.300  1.00 53.72  ?  10  SER C CA  1 
ATOM 3357 C C   . SER C 1 10  ? -1.127  29.141  21.759  1.00 61.52  ?  10  SER C C   1 
ATOM 3358 O O   . SER C 1 10  ? -1.701  28.463  22.616  1.00 62.58  ?  10  SER C O   1 
ATOM 3359 C CB  . SER C 1 10  ? -2.449  30.299  19.966  1.00 51.94  ?  10  SER C CB  1 
ATOM 3360 O OG  . SER C 1 10  ? -3.695  30.191  20.639  1.00 50.75  ?  10  SER C OG  1 
ATOM 3361 N N   . LEU C 1 11  ? -0.115  29.964  22.030  1.00 54.03  ?  11  LEU C N   1 
ATOM 3362 C CA  . LEU C 1 11  ? 0.419   30.116  23.374  1.00 52.75  ?  11  LEU C CA  1 
ATOM 3363 C C   . LEU C 1 11  ? 1.250   31.390  23.421  1.00 57.14  ?  11  LEU C C   1 
ATOM 3364 O O   . LEU C 1 11  ? 1.856   31.783  22.421  1.00 52.83  ?  11  LEU C O   1 
ATOM 3365 C CB  . LEU C 1 11  ? 1.255   28.894  23.788  1.00 56.61  ?  11  LEU C CB  1 
ATOM 3366 C CG  . LEU C 1 11  ? 2.551   28.546  23.041  1.00 55.73  ?  11  LEU C CG  1 
ATOM 3367 C CD1 . LEU C 1 11  ? 3.775   29.164  23.713  1.00 48.83  ?  11  LEU C CD1 1 
ATOM 3368 C CD2 . LEU C 1 11  ? 2.715   27.034  22.900  1.00 48.18  ?  11  LEU C CD2 1 
ATOM 3369 N N   . SER C 1 12  ? 1.269   32.026  24.593  1.00 59.97  ?  12  SER C N   1 
ATOM 3370 C CA  . SER C 1 12  ? 2.042   33.238  24.827  1.00 56.62  ?  12  SER C CA  1 
ATOM 3371 C C   . SER C 1 12  ? 3.195   32.944  25.776  1.00 63.98  ?  12  SER C C   1 
ATOM 3372 O O   . SER C 1 12  ? 3.037   32.197  26.749  1.00 62.36  ?  12  SER C O   1 
ATOM 3373 C CB  . SER C 1 12  ? 1.167   34.351  25.416  1.00 60.28  ?  12  SER C CB  1 
ATOM 3374 O OG  . SER C 1 12  ? 0.172   34.775  24.501  1.00 65.41  ?  12  SER C OG  1 
ATOM 3375 N N   . ALA C 1 13  ? 4.350   33.547  25.496  1.00 67.03  ?  13  ALA C N   1 
ATOM 3376 C CA  . ALA C 1 13  ? 5.522   33.398  26.349  1.00 71.36  ?  13  ALA C CA  1 
ATOM 3377 C C   . ALA C 1 13  ? 6.407   34.628  26.201  1.00 72.43  ?  13  ALA C C   1 
ATOM 3378 O O   . ALA C 1 13  ? 6.252   35.422  25.268  1.00 70.53  ?  13  ALA C O   1 
ATOM 3379 C CB  . ALA C 1 13  ? 6.311   32.125  26.015  1.00 58.00  ?  13  ALA C CB  1 
ATOM 3380 N N   . SER C 1 14  ? 7.331   34.784  27.143  1.00 70.55  ?  14  SER C N   1 
ATOM 3381 C CA  . SER C 1 14  ? 8.281   35.887  27.135  1.00 70.36  ?  14  SER C CA  1 
ATOM 3382 C C   . SER C 1 14  ? 9.636   35.430  26.604  1.00 70.32  ?  14  SER C C   1 
ATOM 3383 O O   . SER C 1 14  ? 9.911   34.237  26.461  1.00 73.81  ?  14  SER C O   1 
ATOM 3384 C CB  . SER C 1 14  ? 8.426   36.484  28.536  1.00 66.93  ?  14  SER C CB  1 
ATOM 3385 O OG  . SER C 1 14  ? 7.221   37.111  28.938  1.00 73.70  ?  14  SER C OG  1 
ATOM 3386 N N   . VAL C 1 15  ? 10.487  36.410  26.302  1.00 70.55  ?  15  VAL C N   1 
ATOM 3387 C CA  . VAL C 1 15  ? 11.821  36.124  25.788  1.00 69.86  ?  15  VAL C CA  1 
ATOM 3388 C C   . VAL C 1 15  ? 12.632  35.429  26.872  1.00 73.83  ?  15  VAL C C   1 
ATOM 3389 O O   . VAL C 1 15  ? 12.903  36.008  27.930  1.00 78.73  ?  15  VAL C O   1 
ATOM 3390 C CB  . VAL C 1 15  ? 12.520  37.406  25.321  1.00 75.66  ?  15  VAL C CB  1 
ATOM 3391 C CG1 . VAL C 1 15  ? 13.910  37.081  24.797  1.00 80.27  ?  15  VAL C CG1 1 
ATOM 3392 C CG2 . VAL C 1 15  ? 11.691  38.111  24.258  1.00 77.34  ?  15  VAL C CG2 1 
ATOM 3393 N N   . GLY C 1 16  ? 13.032  34.189  26.607  1.00 74.18  ?  16  GLY C N   1 
ATOM 3394 C CA  . GLY C 1 16  ? 13.791  33.394  27.549  1.00 70.46  ?  16  GLY C CA  1 
ATOM 3395 C C   . GLY C 1 16  ? 13.047  32.206  28.113  1.00 71.13  ?  16  GLY C C   1 
ATOM 3396 O O   . GLY C 1 16  ? 13.685  31.321  28.698  1.00 75.78  ?  16  GLY C O   1 
ATOM 3397 N N   . ASP C 1 17  ? 11.729  32.143  27.951  1.00 63.12  ?  17  ASP C N   1 
ATOM 3398 C CA  . ASP C 1 17  ? 10.975  31.018  28.475  1.00 62.37  ?  17  ASP C CA  1 
ATOM 3399 C C   . ASP C 1 17  ? 11.242  29.755  27.662  1.00 69.57  ?  17  ASP C C   1 
ATOM 3400 O O   . ASP C 1 17  ? 11.773  29.791  26.548  1.00 68.87  ?  17  ASP C O   1 
ATOM 3401 C CB  . ASP C 1 17  ? 9.478   31.316  28.481  1.00 63.70  ?  17  ASP C CB  1 
ATOM 3402 C CG  . ASP C 1 17  ? 9.101   32.373  29.491  1.00 69.57  ?  17  ASP C CG  1 
ATOM 3403 O OD1 . ASP C 1 17  ? 8.372   33.313  29.114  1.00 72.62  ?  17  ASP C OD1 1 
ATOM 3404 O OD2 . ASP C 1 17  ? 9.543   32.272  30.657  1.00 71.82  ?  17  ASP C OD2 1 
ATOM 3405 N N   . ARG C 1 18  ? 10.887  28.623  28.254  1.00 73.41  ?  18  ARG C N   1 
ATOM 3406 C CA  . ARG C 1 18  ? 10.976  27.328  27.598  1.00 71.06  ?  18  ARG C CA  1 
ATOM 3407 C C   . ARG C 1 18  ? 9.577   26.926  27.152  1.00 68.16  ?  18  ARG C C   1 
ATOM 3408 O O   . ARG C 1 18  ? 8.654   26.870  27.972  1.00 65.25  ?  18  ARG C O   1 
ATOM 3409 C CB  . ARG C 1 18  ? 11.579  26.280  28.533  1.00 69.71  ?  18  ARG C CB  1 
ATOM 3410 C CG  . ARG C 1 18  ? 11.573  24.882  27.959  1.00 76.57  ?  18  ARG C CG  1 
ATOM 3411 C CD  . ARG C 1 18  ? 11.958  23.846  28.996  1.00 80.76  ?  18  ARG C CD  1 
ATOM 3412 N NE  . ARG C 1 18  ? 11.819  22.498  28.459  1.00 79.47  ?  18  ARG C NE  1 
ATOM 3413 C CZ  . ARG C 1 18  ? 11.829  21.395  29.196  1.00 87.30  ?  18  ARG C CZ  1 
ATOM 3414 N NH1 . ARG C 1 18  ? 11.970  21.481  30.513  1.00 101.19 ?  18  ARG C NH1 1 
ATOM 3415 N NH2 . ARG C 1 18  ? 11.692  20.209  28.615  1.00 82.91  ?  18  ARG C NH2 1 
ATOM 3416 N N   . VAL C 1 19  ? 9.413   26.672  25.857  1.00 67.00  ?  19  VAL C N   1 
ATOM 3417 C CA  . VAL C 1 19  ? 8.098   26.357  25.315  1.00 65.05  ?  19  VAL C CA  1 
ATOM 3418 C C   . VAL C 1 19  ? 8.108   24.953  24.724  1.00 62.00  ?  19  VAL C C   1 
ATOM 3419 O O   . VAL C 1 19  ? 9.131   24.464  24.224  1.00 64.36  ?  19  VAL C O   1 
ATOM 3420 C CB  . VAL C 1 19  ? 7.638   27.396  24.261  1.00 66.21  ?  19  VAL C CB  1 
ATOM 3421 C CG1 . VAL C 1 19  ? 7.557   28.790  24.872  1.00 61.84  ?  19  VAL C CG1 1 
ATOM 3422 C CG2 . VAL C 1 19  ? 8.568   27.394  23.069  1.00 66.46  ?  19  VAL C CG2 1 
ATOM 3423 N N   . THR C 1 20  ? 6.941   24.310  24.781  1.00 52.13  ?  20  THR C N   1 
ATOM 3424 C CA  . THR C 1 20  ? 6.757   22.920  24.386  1.00 51.44  ?  20  THR C CA  1 
ATOM 3425 C C   . THR C 1 20  ? 5.519   22.828  23.508  1.00 51.54  ?  20  THR C C   1 
ATOM 3426 O O   . THR C 1 20  ? 4.445   23.295  23.902  1.00 52.73  ?  20  THR C O   1 
ATOM 3427 C CB  . THR C 1 20  ? 6.592   22.011  25.624  1.00 60.34  ?  20  THR C CB  1 
ATOM 3428 O OG1 . THR C 1 20  ? 7.805   21.988  26.388  1.00 58.82  ?  20  THR C OG1 1 
ATOM 3429 C CG2 . THR C 1 20  ? 6.217   20.589  25.230  1.00 56.04  ?  20  THR C CG2 1 
ATOM 3430 N N   . ILE C 1 21  ? 5.662   22.211  22.335  1.00 49.77  ?  21  ILE C N   1 
ATOM 3431 C CA  . ILE C 1 21  ? 4.552   21.937  21.427  1.00 49.98  ?  21  ILE C CA  1 
ATOM 3432 C C   . ILE C 1 21  ? 4.481   20.435  21.219  1.00 51.49  ?  21  ILE C C   1 
ATOM 3433 O O   . ILE C 1 21  ? 5.517   19.780  21.068  1.00 53.13  ?  21  ILE C O   1 
ATOM 3434 C CB  . ILE C 1 21  ? 4.708   22.659  20.072  1.00 51.78  ?  21  ILE C CB  1 
ATOM 3435 C CG1 . ILE C 1 21  ? 5.122   24.118  20.269  1.00 48.12  ?  21  ILE C CG1 1 
ATOM 3436 C CG2 . ILE C 1 21  ? 3.432   22.564  19.265  1.00 53.05  ?  21  ILE C CG2 1 
ATOM 3437 C CD1 . ILE C 1 21  ? 5.395   24.845  18.968  1.00 52.82  ?  21  ILE C CD1 1 
ATOM 3438 N N   . THR C 1 22  ? 3.269   19.885  21.207  1.00 54.29  ?  22  THR C N   1 
ATOM 3439 C CA  . THR C 1 22  ? 3.101   18.444  21.105  1.00 58.10  ?  22  THR C CA  1 
ATOM 3440 C C   . THR C 1 22  ? 2.308   18.084  19.855  1.00 55.46  ?  22  THR C C   1 
ATOM 3441 O O   . THR C 1 22  ? 1.444   18.841  19.409  1.00 60.44  ?  22  THR C O   1 
ATOM 3442 C CB  . THR C 1 22  ? 2.423   17.876  22.368  1.00 59.00  ?  22  THR C CB  1 
ATOM 3443 O OG1 . THR C 1 22  ? 1.261   18.652  22.694  1.00 54.92  ?  22  THR C OG1 1 
ATOM 3444 C CG2 . THR C 1 22  ? 3.395   17.905  23.544  1.00 47.37  ?  22  THR C CG2 1 
ATOM 3445 N N   . CYS C 1 23  ? 2.645   16.931  19.278  1.00 57.39  ?  23  CYS C N   1 
ATOM 3446 C CA  . CYS C 1 23  ? 2.015   16.416  18.065  1.00 60.87  ?  23  CYS C CA  1 
ATOM 3447 C C   . CYS C 1 23  ? 1.772   14.925  18.269  1.00 55.45  ?  23  CYS C C   1 
ATOM 3448 O O   . CYS C 1 23  ? 2.706   14.182  18.575  1.00 53.53  ?  23  CYS C O   1 
ATOM 3449 C CB  . CYS C 1 23  ? 2.904   16.674  16.837  1.00 64.95  ?  23  CYS C CB  1 
ATOM 3450 S SG  . CYS C 1 23  ? 2.160   16.443  15.176  1.00 82.66  ?  23  CYS C SG  1 
ATOM 3451 N N   . GLN C 1 24  ? 0.523   14.490  18.141  1.00 56.26  ?  24  GLN C N   1 
ATOM 3452 C CA  . GLN C 1 24  ? 0.154   13.093  18.335  1.00 54.87  ?  24  GLN C CA  1 
ATOM 3453 C C   . GLN C 1 24  ? -0.225  12.455  17.005  1.00 62.77  ?  24  GLN C C   1 
ATOM 3454 O O   . GLN C 1 24  ? -1.001  13.030  16.230  1.00 61.83  ?  24  GLN C O   1 
ATOM 3455 C CB  . GLN C 1 24  ? -0.997  12.956  19.329  1.00 54.19  ?  24  GLN C CB  1 
ATOM 3456 C CG  . GLN C 1 24  ? -1.408  11.511  19.579  1.00 57.55  ?  24  GLN C CG  1 
ATOM 3457 C CD  . GLN C 1 24  ? -2.152  11.327  20.890  1.00 58.99  ?  24  GLN C CD  1 
ATOM 3458 O OE1 . GLN C 1 24  ? -1.723  11.820  21.938  1.00 58.95  ?  24  GLN C OE1 1 
ATOM 3459 N NE2 . GLN C 1 24  ? -3.279  10.618  20.838  1.00 53.03  ?  24  GLN C NE2 1 
ATOM 3460 N N   . ALA C 1 25  ? 0.305   11.258  16.760  1.00 61.07  ?  25  ALA C N   1 
ATOM 3461 C CA  . ALA C 1 25  ? 0.052   10.536  15.525  1.00 64.98  ?  25  ALA C CA  1 
ATOM 3462 C C   . ALA C 1 25  ? -1.122  9.580   15.692  1.00 67.03  ?  25  ALA C C   1 
ATOM 3463 O O   . ALA C 1 25  ? -1.330  8.992   16.758  1.00 66.04  ?  25  ALA C O   1 
ATOM 3464 C CB  . ALA C 1 25  ? 1.295   9.757   15.091  1.00 68.07  ?  25  ALA C CB  1 
ATOM 3465 N N   . SER C 1 26  ? -1.882  9.418   14.609  1.00 68.81  ?  26  SER C N   1 
ATOM 3466 C CA  . SER C 1 26  ? -3.046  8.540   14.635  1.00 63.04  ?  26  SER C CA  1 
ATOM 3467 C C   . SER C 1 26  ? -2.626  7.083   14.788  1.00 64.27  ?  26  SER C C   1 
ATOM 3468 O O   . SER C 1 26  ? -3.217  6.335   15.576  1.00 62.26  ?  26  SER C O   1 
ATOM 3469 C CB  . SER C 1 26  ? -3.873  8.749   13.365  1.00 70.56  ?  26  SER C CB  1 
ATOM 3470 O OG  . SER C 1 26  ? -5.087  8.023   13.411  1.00 78.78  ?  26  SER C OG  1 
ATOM 3471 N N   . GLN C 1 27  ? -1.627  6.655   14.018  1.00 72.41  ?  27  GLN C N   1 
ATOM 3472 C CA  . GLN C 1 27  ? -1.023  5.337   14.106  1.00 71.49  ?  27  GLN C CA  1 
ATOM 3473 C C   . GLN C 1 27  ? 0.432   5.491   14.562  1.00 75.75  ?  27  GLN C C   1 
ATOM 3474 O O   . GLN C 1 27  ? 0.776   6.500   15.201  1.00 75.68  ?  27  GLN C O   1 
ATOM 3475 C CB  . GLN C 1 27  ? -1.175  4.630   12.764  1.00 71.14  ?  27  GLN C CB  1 
ATOM 3476 C CG  . GLN C 1 27  ? -2.612  4.476   12.306  1.00 75.45  ?  27  GLN C CG  1 
ATOM 3477 C CD  . GLN C 1 27  ? -2.709  3.851   10.936  1.00 80.91  ?  27  GLN C CD  1 
ATOM 3478 O OE1 . GLN C 1 27  ? -2.075  2.832   10.662  1.00 84.09  ?  27  GLN C OE1 1 
ATOM 3479 N NE2 . GLN C 1 27  ? -3.497  4.463   10.059  1.00 86.78  ?  27  GLN C NE2 1 
ATOM 3480 N N   . SER C 1 28  ? 1.279   4.524   14.216  1.00 83.02  ?  28  SER C N   1 
ATOM 3481 C CA  . SER C 1 28  ? 2.696   4.538   14.561  1.00 80.97  ?  28  SER C CA  1 
ATOM 3482 C C   . SER C 1 28  ? 3.501   4.777   13.291  1.00 76.85  ?  28  SER C C   1 
ATOM 3483 O O   . SER C 1 28  ? 3.407   3.992   12.340  1.00 71.78  ?  28  SER C O   1 
ATOM 3484 C CB  . SER C 1 28  ? 3.111   3.226   15.230  1.00 72.92  ?  28  SER C CB  1 
ATOM 3485 O OG  . SER C 1 28  ? 4.515   3.165   15.428  1.00 68.29  ?  28  SER C OG  1 
ATOM 3486 N N   . ILE C 1 29  ? 4.259   5.878   13.263  1.00 75.43  ?  29  ILE C N   1 
ATOM 3487 C CA  . ILE C 1 29  ? 5.065   6.206   12.093  1.00 74.89  ?  29  ILE C CA  1 
ATOM 3488 C C   . ILE C 1 29  ? 6.553   5.924   12.256  1.00 86.83  ?  29  ILE C C   1 
ATOM 3489 O O   . ILE C 1 29  ? 7.292   6.024   11.263  1.00 94.77  ?  29  ILE C O   1 
ATOM 3490 C CB  . ILE C 1 29  ? 4.879   7.683   11.703  1.00 74.91  ?  29  ILE C CB  1 
ATOM 3491 C CG1 . ILE C 1 29  ? 4.848   8.561   12.951  1.00 78.88  ?  29  ILE C CG1 1 
ATOM 3492 C CG2 . ILE C 1 29  ? 3.624   7.841   10.920  1.00 84.34  ?  29  ILE C CG2 1 
ATOM 3493 C CD1 . ILE C 1 29  ? 4.583   10.025  12.654  1.00 73.70  ?  29  ILE C CD1 1 
ATOM 3494 N N   . SER C 1 30  ? 7.020   5.586   13.457  1.00 87.25  ?  30  SER C N   1 
ATOM 3495 C CA  . SER C 1 30  ? 8.422   5.237   13.703  1.00 86.93  ?  30  SER C CA  1 
ATOM 3496 C C   . SER C 1 30  ? 9.457   6.285   13.263  1.00 88.19  ?  30  SER C C   1 
ATOM 3497 O O   . SER C 1 30  ? 10.217  6.094   12.313  1.00 93.91  ?  30  SER C O   1 
ATOM 3498 C CB  . SER C 1 30  ? 8.743   3.879   13.074  1.00 85.16  ?  30  SER C CB  1 
ATOM 3499 O OG  . SER C 1 30  ? 7.971   2.862   13.688  1.00 89.43  ?  30  SER C OG  1 
ATOM 3500 N N   . ASN C 1 31  ? 9.450   7.409   13.985  1.00 75.71  ?  31  ASN C N   1 
ATOM 3501 C CA  . ASN C 1 31  ? 10.377  8.527   13.782  1.00 75.12  ?  31  ASN C CA  1 
ATOM 3502 C C   . ASN C 1 31  ? 10.161  9.381   12.534  1.00 81.40  ?  31  ASN C C   1 
ATOM 3503 O O   . ASN C 1 31  ? 10.810  10.423  12.403  1.00 82.84  ?  31  ASN C O   1 
ATOM 3504 C CB  . ASN C 1 31  ? 11.828  8.025   13.746  1.00 77.50  ?  31  ASN C CB  1 
ATOM 3505 C CG  . ASN C 1 31  ? 12.419  7.813   15.132  1.00 91.60  ?  31  ASN C CG  1 
ATOM 3506 O OD1 . ASN C 1 31  ? 11.694  7.711   16.123  1.00 92.93  ?  31  ASN C OD1 1 
ATOM 3507 N ND2 . ASN C 1 31  ? 13.748  7.739   15.204  1.00 93.08  ?  31  ASN C ND2 1 
ATOM 3508 N N   . GLN C 1 32  ? 9.280   8.989   11.610  1.00 79.68  ?  32  GLN C N   1 
ATOM 3509 C CA  . GLN C 1 32  ? 9.104   9.771   10.380  1.00 81.17  ?  32  GLN C CA  1 
ATOM 3510 C C   . GLN C 1 32  ? 8.194   10.973  10.654  1.00 78.96  ?  32  GLN C C   1 
ATOM 3511 O O   . GLN C 1 32  ? 7.067   11.078  10.163  1.00 74.15  ?  32  GLN C O   1 
ATOM 3512 C CB  . GLN C 1 32  ? 8.568   8.900   9.253   1.00 88.17  ?  32  GLN C CB  1 
ATOM 3513 C CG  . GLN C 1 32  ? 9.424   7.682   8.943   1.00 89.73  ?  32  GLN C CG  1 
ATOM 3514 C CD  . GLN C 1 32  ? 9.018   6.996   7.647   1.00 97.49  ?  32  GLN C CD  1 
ATOM 3515 O OE1 . GLN C 1 32  ? 8.822   7.646   6.616   1.00 98.60  ?  32  GLN C OE1 1 
ATOM 3516 N NE2 . GLN C 1 32  ? 8.880   5.676   7.697   1.00 97.21  ?  32  GLN C NE2 1 
ATOM 3517 N N   . LEU C 1 33  ? 8.722   11.906  11.449  1.00 74.38  ?  33  LEU C N   1 
ATOM 3518 C CA  . LEU C 1 33  ? 8.045   13.155  11.768  1.00 70.55  ?  33  LEU C CA  1 
ATOM 3519 C C   . LEU C 1 33  ? 9.045   14.300  11.725  1.00 75.03  ?  33  LEU C C   1 
ATOM 3520 O O   . LEU C 1 33  ? 10.176  14.158  12.198  1.00 76.93  ?  33  LEU C O   1 
ATOM 3521 C CB  . LEU C 1 33  ? 7.382   13.094  13.151  1.00 65.01  ?  33  LEU C CB  1 
ATOM 3522 C CG  . LEU C 1 33  ? 6.555   14.322  13.531  1.00 63.40  ?  33  LEU C CG  1 
ATOM 3523 C CD1 . LEU C 1 33  ? 5.180   13.925  14.045  1.00 60.73  ?  33  LEU C CD1 1 
ATOM 3524 C CD2 . LEU C 1 33  ? 7.301   15.167  14.553  1.00 55.50  ?  33  LEU C CD2 1 
ATOM 3525 N N   . SER C 1 34  ? 8.620   15.435  11.164  1.00 75.61  ?  34  SER C N   1 
ATOM 3526 C CA  . SER C 1 34  ? 9.473   16.611  11.043  1.00 69.42  ?  34  SER C CA  1 
ATOM 3527 C C   . SER C 1 34  ? 8.750   17.849  11.560  1.00 67.18  ?  34  SER C C   1 
ATOM 3528 O O   . SER C 1 34  ? 7.520   17.934  11.517  1.00 68.82  ?  34  SER C O   1 
ATOM 3529 C CB  . SER C 1 34  ? 9.921   16.833  9.588   1.00 67.00  ?  34  SER C CB  1 
ATOM 3530 O OG  . SER C 1 34  ? 8.854   16.633  8.679   1.00 63.75  ?  34  SER C OG  1 
ATOM 3531 N N   . TRP C 1 35  ? 9.534   18.799  12.069  1.00 63.66  ?  35  TRP C N   1 
ATOM 3532 C CA  . TRP C 1 35  ? 9.038   20.066  12.600  1.00 62.41  ?  35  TRP C CA  1 
ATOM 3533 C C   . TRP C 1 35  ? 9.545   21.220  11.742  1.00 62.53  ?  35  TRP C C   1 
ATOM 3534 O O   . TRP C 1 35  ? 10.743  21.284  11.433  1.00 62.39  ?  35  TRP C O   1 
ATOM 3535 C CB  . TRP C 1 35  ? 9.480   20.279  14.050  1.00 63.37  ?  35  TRP C CB  1 
ATOM 3536 C CG  . TRP C 1 35  ? 8.874   19.340  15.051  1.00 65.75  ?  35  TRP C CG  1 
ATOM 3537 C CD1 . TRP C 1 35  ? 9.433   18.195  15.541  1.00 62.11  ?  35  TRP C CD1 1 
ATOM 3538 C CD2 . TRP C 1 35  ? 7.605   19.479  15.706  1.00 66.86  ?  35  TRP C CD2 1 
ATOM 3539 N NE1 . TRP C 1 35  ? 8.588   17.605  16.449  1.00 60.33  ?  35  TRP C NE1 1 
ATOM 3540 C CE2 . TRP C 1 35  ? 7.459   18.371  16.570  1.00 60.09  ?  35  TRP C CE2 1 
ATOM 3541 C CE3 . TRP C 1 35  ? 6.577   20.425  15.641  1.00 62.30  ?  35  TRP C CE3 1 
ATOM 3542 C CZ2 . TRP C 1 35  ? 6.325   18.185  17.365  1.00 53.71  ?  35  TRP C CZ2 1 
ATOM 3543 C CZ3 . TRP C 1 35  ? 5.452   20.239  16.433  1.00 61.98  ?  35  TRP C CZ3 1 
ATOM 3544 C CH2 . TRP C 1 35  ? 5.337   19.126  17.284  1.00 57.01  ?  35  TRP C CH2 1 
ATOM 3545 N N   . TYR C 1 36  ? 8.637   22.145  11.403  1.00 58.16  ?  36  TYR C N   1 
ATOM 3546 C CA  . TYR C 1 36  ? 8.912   23.285  10.538  1.00 64.43  ?  36  TYR C CA  1 
ATOM 3547 C C   . TYR C 1 36  ? 8.470   24.581  11.205  1.00 61.91  ?  36  TYR C C   1 
ATOM 3548 O O   . TYR C 1 36  ? 7.550   24.591  12.028  1.00 59.91  ?  36  TYR C O   1 
ATOM 3549 C CB  . TYR C 1 36  ? 8.186   23.169  9.187   1.00 61.88  ?  36  TYR C CB  1 
ATOM 3550 C CG  . TYR C 1 36  ? 8.448   21.887  8.438   1.00 63.55  ?  36  TYR C CG  1 
ATOM 3551 C CD1 . TYR C 1 36  ? 9.328   21.857  7.368   1.00 64.13  ?  36  TYR C CD1 1 
ATOM 3552 C CD2 . TYR C 1 36  ? 7.813   20.708  8.798   1.00 62.85  ?  36  TYR C CD2 1 
ATOM 3553 C CE1 . TYR C 1 36  ? 9.568   20.690  6.678   1.00 67.37  ?  36  TYR C CE1 1 
ATOM 3554 C CE2 . TYR C 1 36  ? 8.049   19.537  8.116   1.00 63.89  ?  36  TYR C CE2 1 
ATOM 3555 C CZ  . TYR C 1 36  ? 8.928   19.531  7.059   1.00 66.72  ?  36  TYR C CZ  1 
ATOM 3556 O OH  . TYR C 1 36  ? 9.165   18.363  6.377   1.00 69.58  ?  36  TYR C OH  1 
ATOM 3557 N N   . GLN C 1 37  ? 9.113   25.681  10.808  1.00 56.29  ?  37  GLN C N   1 
ATOM 3558 C CA  . GLN C 1 37  ? 8.793   27.019  11.289  1.00 59.10  ?  37  GLN C CA  1 
ATOM 3559 C C   . GLN C 1 37  ? 8.441   27.920  10.112  1.00 60.19  ?  37  GLN C C   1 
ATOM 3560 O O   . GLN C 1 37  ? 9.151   27.927  9.101   1.00 57.17  ?  37  GLN C O   1 
ATOM 3561 C CB  . GLN C 1 37  ? 9.971   27.622  12.051  1.00 62.43  ?  37  GLN C CB  1 
ATOM 3562 C CG  . GLN C 1 37  ? 9.766   29.072  12.442  1.00 58.54  ?  37  GLN C CG  1 
ATOM 3563 C CD  . GLN C 1 37  ? 11.061  29.751  12.834  1.00 65.42  ?  37  GLN C CD  1 
ATOM 3564 O OE1 . GLN C 1 37  ? 12.058  29.668  12.114  1.00 63.72  ?  37  GLN C OE1 1 
ATOM 3565 N NE2 . GLN C 1 37  ? 11.066  30.403  13.996  1.00 69.58  ?  37  GLN C NE2 1 
ATOM 3566 N N   . GLN C 1 38  ? 7.359   28.688  10.251  1.00 58.15  ?  38  GLN C N   1 
ATOM 3567 C CA  . GLN C 1 38  ? 6.887   29.597  9.215   1.00 59.72  ?  38  GLN C CA  1 
ATOM 3568 C C   . GLN C 1 38  ? 6.545   30.946  9.829   1.00 57.25  ?  38  GLN C C   1 
ATOM 3569 O O   . GLN C 1 38  ? 5.804   31.015  10.817  1.00 53.77  ?  38  GLN C O   1 
ATOM 3570 C CB  . GLN C 1 38  ? 5.662   29.039  8.485   1.00 61.51  ?  38  GLN C CB  1 
ATOM 3571 C CG  . GLN C 1 38  ? 5.197   29.921  7.334   1.00 56.26  ?  38  GLN C CG  1 
ATOM 3572 C CD  . GLN C 1 38  ? 3.884   29.466  6.734   1.00 54.99  ?  38  GLN C CD  1 
ATOM 3573 O OE1 . GLN C 1 38  ? 3.095   28.780  7.381   1.00 55.40  ?  38  GLN C OE1 1 
ATOM 3574 N NE2 . GLN C 1 38  ? 3.636   29.859  5.491   1.00 64.00  ?  38  GLN C NE2 1 
ATOM 3575 N N   . LYS C 1 39  ? 7.099   32.024  9.238   1.00 61.47  ?  39  LYS C N   1 
ATOM 3576 C CA  . LYS C 1 39  ? 6.842   33.418  9.558   1.00 62.22  ?  39  LYS C CA  1 
ATOM 3577 C C   . LYS C 1 39  ? 5.887   34.022  8.531   1.00 66.23  ?  39  LYS C C   1 
ATOM 3578 O O   . LYS C 1 39  ? 5.827   33.556  7.387   1.00 67.73  ?  39  LYS C O   1 
ATOM 3579 C CB  . LYS C 1 39  ? 8.155   34.209  9.584   1.00 60.25  ?  39  LYS C CB  1 
ATOM 3580 C CG  . LYS C 1 39  ? 9.084   33.806  10.722  1.00 59.69  ?  39  LYS C CG  1 
ATOM 3581 C CD  . LYS C 1 39  ? 10.469  34.408  10.564  1.00 69.53  ?  39  LYS C CD  1 
ATOM 3582 C CE  . LYS C 1 39  ? 11.253  34.356  11.876  1.00 79.07  ?  39  LYS C CE  1 
ATOM 3583 N NZ  . LYS C 1 39  ? 10.721  35.311  12.898  1.00 69.04  ?  39  LYS C NZ  1 
ATOM 3584 N N   . PRO C 1 40  ? 5.127   35.058  8.899   1.00 66.25  ?  40  PRO C N   1 
ATOM 3585 C CA  . PRO C 1 40  ? 4.097   35.576  7.985   1.00 68.66  ?  40  PRO C CA  1 
ATOM 3586 C C   . PRO C 1 40  ? 4.676   36.002  6.643   1.00 64.17  ?  40  PRO C C   1 
ATOM 3587 O O   . PRO C 1 40  ? 5.739   36.619  6.568   1.00 69.62  ?  40  PRO C O   1 
ATOM 3588 C CB  . PRO C 1 40  ? 3.505   36.765  8.752   1.00 65.48  ?  40  PRO C CB  1 
ATOM 3589 C CG  . PRO C 1 40  ? 4.499   37.076  9.833   1.00 67.08  ?  40  PRO C CG  1 
ATOM 3590 C CD  . PRO C 1 40  ? 5.112   35.764  10.190  1.00 64.60  ?  40  PRO C CD  1 
ATOM 3591 N N   . GLY C 1 41  ? 3.969   35.635  5.576   1.00 63.55  ?  41  GLY C N   1 
ATOM 3592 C CA  . GLY C 1 41  ? 4.377   35.952  4.224   1.00 64.87  ?  41  GLY C CA  1 
ATOM 3593 C C   . GLY C 1 41  ? 5.529   35.139  3.671   1.00 71.80  ?  41  GLY C C   1 
ATOM 3594 O O   . GLY C 1 41  ? 5.858   35.296  2.490   1.00 68.49  ?  41  GLY C O   1 
ATOM 3595 N N   . LYS C 1 42  ? 6.150   34.274  4.469   1.00 75.26  ?  42  LYS C N   1 
ATOM 3596 C CA  . LYS C 1 42  ? 7.310   33.503  4.044   1.00 70.37  ?  42  LYS C CA  1 
ATOM 3597 C C   . LYS C 1 42  ? 6.958   32.023  3.931   1.00 65.24  ?  42  LYS C C   1 
ATOM 3598 O O   . LYS C 1 42  ? 5.936   31.563  4.447   1.00 64.10  ?  42  LYS C O   1 
ATOM 3599 C CB  . LYS C 1 42  ? 8.482   33.698  5.016   1.00 65.33  ?  42  LYS C CB  1 
ATOM 3600 C CG  . LYS C 1 42  ? 8.900   35.154  5.194   1.00 65.23  ?  42  LYS C CG  1 
ATOM 3601 C CD  . LYS C 1 42  ? 9.285   35.777  3.857   1.00 77.61  ?  42  LYS C CD  1 
ATOM 3602 C CE  . LYS C 1 42  ? 9.597   37.263  3.988   1.00 80.34  ?  42  LYS C CE  1 
ATOM 3603 N NZ  . LYS C 1 42  ? 9.946   37.872  2.670   1.00 73.34  ?  42  LYS C NZ  1 
ATOM 3604 N N   . ALA C 1 43  ? 7.815   31.278  3.229   1.00 65.38  ?  43  ALA C N   1 
ATOM 3605 C CA  . ALA C 1 43  ? 7.627   29.837  3.149   1.00 63.52  ?  43  ALA C CA  1 
ATOM 3606 C C   . ALA C 1 43  ? 8.238   29.147  4.369   1.00 69.16  ?  43  ALA C C   1 
ATOM 3607 O O   . ALA C 1 43  ? 9.188   29.657  4.972   1.00 70.44  ?  43  ALA C O   1 
ATOM 3608 C CB  . ALA C 1 43  ? 8.256   29.283  1.878   1.00 66.38  ?  43  ALA C CB  1 
ATOM 3609 N N   . PRO C 1 44  ? 7.699   27.994  4.763   1.00 66.22  ?  44  PRO C N   1 
ATOM 3610 C CA  . PRO C 1 44  ? 8.213   27.311  5.954   1.00 62.56  ?  44  PRO C CA  1 
ATOM 3611 C C   . PRO C 1 44  ? 9.659   26.862  5.782   1.00 65.55  ?  44  PRO C C   1 
ATOM 3612 O O   . PRO C 1 44  ? 10.146  26.635  4.672   1.00 63.53  ?  44  PRO C O   1 
ATOM 3613 C CB  . PRO C 1 44  ? 7.270   26.111  6.108   1.00 62.55  ?  44  PRO C CB  1 
ATOM 3614 C CG  . PRO C 1 44  ? 6.014   26.523  5.414   1.00 59.06  ?  44  PRO C CG  1 
ATOM 3615 C CD  . PRO C 1 44  ? 6.477   27.353  4.246   1.00 66.87  ?  44  PRO C CD  1 
ATOM 3616 N N   . LYS C 1 45  ? 10.342  26.727  6.919   1.00 69.57  ?  45  LYS C N   1 
ATOM 3617 C CA  . LYS C 1 45  ? 11.728  26.279  6.988   1.00 68.12  ?  45  LYS C CA  1 
ATOM 3618 C C   . LYS C 1 45  ? 11.807  25.007  7.821   1.00 65.81  ?  45  LYS C C   1 
ATOM 3619 O O   . LYS C 1 45  ? 11.197  24.928  8.891   1.00 63.31  ?  45  LYS C O   1 
ATOM 3620 C CB  . LYS C 1 45  ? 12.621  27.366  7.596   1.00 65.31  ?  45  LYS C CB  1 
ATOM 3621 C CG  . LYS C 1 45  ? 14.059  26.936  7.830   1.00 78.67  ?  45  LYS C CG  1 
ATOM 3622 C CD  . LYS C 1 45  ? 14.860  28.013  8.555   1.00 85.58  ?  45  LYS C CD  1 
ATOM 3623 C CE  . LYS C 1 45  ? 16.275  27.529  8.868   1.00 92.51  ?  45  LYS C CE  1 
ATOM 3624 N NZ  . LYS C 1 45  ? 17.088  28.560  9.573   1.00 91.31  ?  45  LYS C NZ  1 
ATOM 3625 N N   . LEU C 1 46  ? 12.541  24.011  7.322   1.00 71.90  ?  46  LEU C N   1 
ATOM 3626 C CA  . LEU C 1 46  ? 12.695  22.741  8.032   1.00 68.85  ?  46  LEU C CA  1 
ATOM 3627 C C   . LEU C 1 46  ? 13.567  22.930  9.267   1.00 69.76  ?  46  LEU C C   1 
ATOM 3628 O O   . LEU C 1 46  ? 14.736  23.311  9.156   1.00 74.88  ?  46  LEU C O   1 
ATOM 3629 C CB  . LEU C 1 46  ? 13.295  21.684  7.105   1.00 71.92  ?  46  LEU C CB  1 
ATOM 3630 C CG  . LEU C 1 46  ? 13.470  20.213  7.534   1.00 71.40  ?  46  LEU C CG  1 
ATOM 3631 C CD1 . LEU C 1 46  ? 14.837  19.960  8.141   1.00 70.68  ?  46  LEU C CD1 1 
ATOM 3632 C CD2 . LEU C 1 46  ? 12.378  19.745  8.493   1.00 69.43  ?  46  LEU C CD2 1 
ATOM 3633 N N   . LEU C 1 47  ? 12.999  22.657  10.442  1.00 69.89  ?  47  LEU C N   1 
ATOM 3634 C CA  . LEU C 1 47  ? 13.712  22.754  11.710  1.00 66.65  ?  47  LEU C CA  1 
ATOM 3635 C C   . LEU C 1 47  ? 14.298  21.427  12.169  1.00 72.78  ?  47  LEU C C   1 
ATOM 3636 O O   . LEU C 1 47  ? 15.468  21.365  12.557  1.00 78.51  ?  47  LEU C O   1 
ATOM 3637 C CB  . LEU C 1 47  ? 12.786  23.282  12.807  1.00 63.15  ?  47  LEU C CB  1 
ATOM 3638 C CG  . LEU C 1 47  ? 12.401  24.752  12.768  1.00 66.22  ?  47  LEU C CG  1 
ATOM 3639 C CD1 . LEU C 1 47  ? 11.625  25.078  14.028  1.00 64.35  ?  47  LEU C CD1 1 
ATOM 3640 C CD2 . LEU C 1 47  ? 13.635  25.622  12.631  1.00 69.90  ?  47  LEU C CD2 1 
ATOM 3641 N N   . ILE C 1 48  ? 13.491  20.371  12.181  1.00 70.64  ?  48  ILE C N   1 
ATOM 3642 C CA  . ILE C 1 48  ? 13.904  19.091  12.746  1.00 67.87  ?  48  ILE C CA  1 
ATOM 3643 C C   . ILE C 1 48  ? 13.357  17.966  11.878  1.00 73.60  ?  48  ILE C C   1 
ATOM 3644 O O   . ILE C 1 48  ? 12.215  18.032  11.414  1.00 73.71  ?  48  ILE C O   1 
ATOM 3645 C CB  . ILE C 1 48  ? 13.432  18.957  14.213  1.00 69.60  ?  48  ILE C CB  1 
ATOM 3646 C CG1 . ILE C 1 48  ? 14.271  19.854  15.128  1.00 74.93  ?  48  ILE C CG1 1 
ATOM 3647 C CG2 . ILE C 1 48  ? 13.482  17.515  14.693  1.00 74.76  ?  48  ILE C CG2 1 
ATOM 3648 C CD1 . ILE C 1 48  ? 13.834  19.835  16.578  1.00 74.41  ?  48  ILE C CD1 1 
ATOM 3649 N N   . TYR C 1 49  ? 14.176  16.940  11.649  1.00 72.35  ?  49  TYR C N   1 
ATOM 3650 C CA  . TYR C 1 49  ? 13.764  15.738  10.938  1.00 74.49  ?  49  TYR C CA  1 
ATOM 3651 C C   . TYR C 1 49  ? 14.040  14.513  11.805  1.00 80.47  ?  49  TYR C C   1 
ATOM 3652 O O   . TYR C 1 49  ? 14.757  14.581  12.807  1.00 75.99  ?  49  TYR C O   1 
ATOM 3653 C CB  . TYR C 1 49  ? 14.485  15.607  9.589   1.00 77.12  ?  49  TYR C CB  1 
ATOM 3654 C CG  . TYR C 1 49  ? 15.960  15.301  9.707   1.00 79.06  ?  49  TYR C CG  1 
ATOM 3655 C CD1 . TYR C 1 49  ? 16.889  16.315  9.881   1.00 79.66  ?  49  TYR C CD1 1 
ATOM 3656 C CD2 . TYR C 1 49  ? 16.422  13.991  9.640   1.00 80.62  ?  49  TYR C CD2 1 
ATOM 3657 C CE1 . TYR C 1 49  ? 18.237  16.034  9.990   1.00 85.79  ?  49  TYR C CE1 1 
ATOM 3658 C CE2 . TYR C 1 49  ? 17.766  13.701  9.749   1.00 81.39  ?  49  TYR C CE2 1 
ATOM 3659 C CZ  . TYR C 1 49  ? 18.670  14.725  9.923   1.00 84.51  ?  49  TYR C CZ  1 
ATOM 3660 O OH  . TYR C 1 49  ? 20.011  14.442  10.033  1.00 83.64  ?  49  TYR C OH  1 
ATOM 3661 N N   . ASP C 1 50  ? 13.442  13.387  11.404  1.00 82.45  ?  50  ASP C N   1 
ATOM 3662 C CA  . ASP C 1 50  ? 13.589  12.096  12.085  1.00 79.46  ?  50  ASP C CA  1 
ATOM 3663 C C   . ASP C 1 50  ? 13.368  12.223  13.592  1.00 80.91  ?  50  ASP C C   1 
ATOM 3664 O O   . ASP C 1 50  ? 14.135  11.699  14.405  1.00 79.80  ?  50  ASP C O   1 
ATOM 3665 C CB  . ASP C 1 50  ? 14.953  11.469  11.787  1.00 83.91  ?  50  ASP C CB  1 
ATOM 3666 C CG  . ASP C 1 50  ? 14.934  10.589  10.548  1.00 88.93  ?  50  ASP C CG  1 
ATOM 3667 O OD1 . ASP C 1 50  ? 13.884  9.973   10.264  1.00 83.60  ?  50  ASP C OD1 1 
ATOM 3668 O OD2 . ASP C 1 50  ? 15.975  10.500  9.863   1.00 96.20  ?  50  ASP C OD2 1 
ATOM 3669 N N   . ALA C 1 51  ? 12.303  12.943  13.954  1.00 79.30  ?  51  ALA C N   1 
ATOM 3670 C CA  . ALA C 1 51  ? 11.842  13.118  15.330  1.00 73.34  ?  51  ALA C CA  1 
ATOM 3671 C C   . ALA C 1 51  ? 12.791  13.964  16.171  1.00 72.37  ?  51  ALA C C   1 
ATOM 3672 O O   . ALA C 1 51  ? 12.357  14.942  16.788  1.00 76.38  ?  51  ALA C O   1 
ATOM 3673 C CB  . ALA C 1 51  ? 11.609  11.766  16.011  1.00 74.18  ?  51  ALA C CB  1 
ATOM 3674 N N   . SER C 1 52  ? 14.081  13.615  16.209  1.00 71.62  ?  52  SER C N   1 
ATOM 3675 C CA  . SER C 1 52  ? 14.991  14.238  17.166  1.00 76.48  ?  52  SER C CA  1 
ATOM 3676 C C   . SER C 1 52  ? 16.307  14.699  16.542  1.00 73.89  ?  52  SER C C   1 
ATOM 3677 O O   . SER C 1 52  ? 17.265  14.977  17.272  1.00 70.06  ?  52  SER C O   1 
ATOM 3678 C CB  . SER C 1 52  ? 15.263  13.275  18.331  1.00 74.37  ?  52  SER C CB  1 
ATOM 3679 O OG  . SER C 1 52  ? 15.809  12.041  17.892  1.00 65.88  ?  52  SER C OG  1 
ATOM 3680 N N   . SER C 1 53  ? 16.370  14.840  15.222  1.00 72.02  ?  53  SER C N   1 
ATOM 3681 C CA  . SER C 1 53  ? 17.598  15.234  14.542  1.00 75.14  ?  53  SER C CA  1 
ATOM 3682 C C   . SER C 1 53  ? 17.516  16.698  14.132  1.00 75.28  ?  53  SER C C   1 
ATOM 3683 O O   . SER C 1 53  ? 16.502  17.134  13.580  1.00 82.03  ?  53  SER C O   1 
ATOM 3684 C CB  . SER C 1 53  ? 17.851  14.350  13.318  1.00 79.23  ?  53  SER C CB  1 
ATOM 3685 O OG  . SER C 1 53  ? 18.030  12.992  13.693  1.00 75.22  ?  53  SER C OG  1 
ATOM 3686 N N   . LEU C 1 54  ? 18.584  17.449  14.398  1.00 72.69  ?  54  LEU C N   1 
ATOM 3687 C CA  . LEU C 1 54  ? 18.630  18.865  14.056  1.00 74.62  ?  54  LEU C CA  1 
ATOM 3688 C C   . LEU C 1 54  ? 18.929  19.067  12.573  1.00 74.82  ?  54  LEU C C   1 
ATOM 3689 O O   . LEU C 1 54  ? 19.590  18.248  11.929  1.00 75.37  ?  54  LEU C O   1 
ATOM 3690 C CB  . LEU C 1 54  ? 19.683  19.587  14.896  1.00 77.08  ?  54  LEU C CB  1 
ATOM 3691 C CG  . LEU C 1 54  ? 19.183  20.266  16.173  1.00 81.59  ?  54  LEU C CG  1 
ATOM 3692 C CD1 . LEU C 1 54  ? 20.304  21.045  16.838  1.00 77.01  ?  54  LEU C CD1 1 
ATOM 3693 C CD2 . LEU C 1 54  ? 17.998  21.171  15.876  1.00 87.63  ?  54  LEU C CD2 1 
ATOM 3694 N N   . ALA C 1 55  ? 18.425  20.174  12.035  1.00 80.44  ?  55  ALA C N   1 
ATOM 3695 C CA  . ALA C 1 55  ? 18.652  20.532  10.640  1.00 83.35  ?  55  ALA C CA  1 
ATOM 3696 C C   . ALA C 1 55  ? 19.979  21.277  10.490  1.00 86.94  ?  55  ALA C C   1 
ATOM 3697 O O   . ALA C 1 55  ? 20.747  21.446  11.442  1.00 88.65  ?  55  ALA C O   1 
ATOM 3698 C CB  . ALA C 1 55  ? 17.486  21.358  10.108  1.00 73.78  ?  55  ALA C CB  1 
ATOM 3699 N N   . SER C 1 56  ? 20.253  21.748  9.277   1.00 88.36  ?  56  SER C N   1 
ATOM 3700 C CA  . SER C 1 56  ? 21.498  22.438  8.968   1.00 88.61  ?  56  SER C CA  1 
ATOM 3701 C C   . SER C 1 56  ? 21.343  23.929  9.246   1.00 90.33  ?  56  SER C C   1 
ATOM 3702 O O   . SER C 1 56  ? 20.563  24.613  8.575   1.00 90.83  ?  56  SER C O   1 
ATOM 3703 C CB  . SER C 1 56  ? 21.881  22.196  7.506   1.00 87.44  ?  56  SER C CB  1 
ATOM 3704 O OG  . SER C 1 56  ? 22.973  23.004  7.099   1.00 88.21  ?  56  SER C OG  1 
ATOM 3705 N N   . GLY C 1 57  ? 22.090  24.430  10.228  1.00 89.28  ?  57  GLY C N   1 
ATOM 3706 C CA  . GLY C 1 57  ? 22.086  25.846  10.537  1.00 87.89  ?  57  GLY C CA  1 
ATOM 3707 C C   . GLY C 1 57  ? 21.053  26.293  11.545  1.00 93.43  ?  57  GLY C C   1 
ATOM 3708 O O   . GLY C 1 57  ? 20.731  27.485  11.587  1.00 98.20  ?  57  GLY C O   1 
ATOM 3709 N N   . VAL C 1 58  ? 20.533  25.392  12.365  1.00 91.02  ?  58  VAL C N   1 
ATOM 3710 C CA  . VAL C 1 58  ? 19.517  25.708  13.366  1.00 88.75  ?  58  VAL C CA  1 
ATOM 3711 C C   . VAL C 1 58  ? 20.171  25.652  14.743  1.00 87.88  ?  58  VAL C C   1 
ATOM 3712 O O   . VAL C 1 58  ? 20.869  24.677  15.040  1.00 88.07  ?  58  VAL C O   1 
ATOM 3713 C CB  . VAL C 1 58  ? 18.316  24.744  13.292  1.00 90.12  ?  58  VAL C CB  1 
ATOM 3714 C CG1 . VAL C 1 58  ? 18.787  23.323  13.056  1.00 87.27  ?  58  VAL C CG1 1 
ATOM 3715 C CG2 . VAL C 1 58  ? 17.485  24.816  14.564  1.00 90.01  ?  58  VAL C CG2 1 
ATOM 3716 N N   . PRO C 1 59  ? 19.992  26.667  15.588  1.00 85.33  ?  59  PRO C N   1 
ATOM 3717 C CA  . PRO C 1 59  ? 20.653  26.666  16.899  1.00 85.36  ?  59  PRO C CA  1 
ATOM 3718 C C   . PRO C 1 59  ? 20.196  25.497  17.758  1.00 85.81  ?  59  PRO C C   1 
ATOM 3719 O O   . PRO C 1 59  ? 19.122  24.922  17.561  1.00 88.05  ?  59  PRO C O   1 
ATOM 3720 C CB  . PRO C 1 59  ? 20.237  28.009  17.512  1.00 86.46  ?  59  PRO C CB  1 
ATOM 3721 C CG  . PRO C 1 59  ? 19.011  28.418  16.750  1.00 83.36  ?  59  PRO C CG  1 
ATOM 3722 C CD  . PRO C 1 59  ? 19.197  27.886  15.367  1.00 83.33  ?  59  PRO C CD  1 
ATOM 3723 N N   . SER C 1 60  ? 21.034  25.155  18.738  1.00 81.46  ?  60  SER C N   1 
ATOM 3724 C CA  . SER C 1 60  ? 20.816  23.961  19.547  1.00 84.49  ?  60  SER C CA  1 
ATOM 3725 C C   . SER C 1 60  ? 19.606  24.068  20.463  1.00 86.94  ?  60  SER C C   1 
ATOM 3726 O O   . SER C 1 60  ? 19.183  23.046  21.017  1.00 83.73  ?  60  SER C O   1 
ATOM 3727 C CB  . SER C 1 60  ? 22.062  23.661  20.385  1.00 84.15  ?  60  SER C CB  1 
ATOM 3728 O OG  . SER C 1 60  ? 23.159  23.305  19.563  1.00 88.90  ?  60  SER C OG  1 
ATOM 3729 N N   . ARG C 1 61  ? 19.031  25.260  20.622  1.00 86.58  ?  61  ARG C N   1 
ATOM 3730 C CA  . ARG C 1 61  ? 17.890  25.440  21.513  1.00 87.81  ?  61  ARG C CA  1 
ATOM 3731 C C   . ARG C 1 61  ? 16.597  24.856  20.962  1.00 79.23  ?  61  ARG C C   1 
ATOM 3732 O O   . ARG C 1 61  ? 15.578  24.899  21.663  1.00 74.45  ?  61  ARG C O   1 
ATOM 3733 C CB  . ARG C 1 61  ? 17.715  26.926  21.819  1.00 87.06  ?  61  ARG C CB  1 
ATOM 3734 C CG  . ARG C 1 61  ? 17.811  27.791  20.588  1.00 85.17  ?  61  ARG C CG  1 
ATOM 3735 C CD  . ARG C 1 61  ? 17.898  29.252  20.953  1.00 83.36  ?  61  ARG C CD  1 
ATOM 3736 N NE  . ARG C 1 61  ? 17.964  30.085  19.759  1.00 85.18  ?  61  ARG C NE  1 
ATOM 3737 C CZ  . ARG C 1 61  ? 16.907  30.405  19.022  1.00 83.55  ?  61  ARG C CZ  1 
ATOM 3738 N NH1 . ARG C 1 61  ? 15.708  29.956  19.361  1.00 85.80  ?  61  ARG C NH1 1 
ATOM 3739 N NH2 . ARG C 1 61  ? 17.049  31.169  17.948  1.00 81.24  ?  61  ARG C NH2 1 
ATOM 3740 N N   . PHE C 1 62  ? 16.606  24.324  19.743  1.00 74.33  ?  62  PHE C N   1 
ATOM 3741 C CA  . PHE C 1 62  ? 15.492  23.551  19.209  1.00 75.24  ?  62  PHE C CA  1 
ATOM 3742 C C   . PHE C 1 62  ? 15.775  22.065  19.391  1.00 73.08  ?  62  PHE C C   1 
ATOM 3743 O O   . PHE C 1 62  ? 16.802  21.566  18.920  1.00 74.63  ?  62  PHE C O   1 
ATOM 3744 C CB  . PHE C 1 62  ? 15.272  23.853  17.726  1.00 76.77  ?  62  PHE C CB  1 
ATOM 3745 C CG  . PHE C 1 62  ? 14.735  25.228  17.452  1.00 76.36  ?  62  PHE C CG  1 
ATOM 3746 C CD1 . PHE C 1 62  ? 13.372  25.471  17.488  1.00 71.23  ?  62  PHE C CD1 1 
ATOM 3747 C CD2 . PHE C 1 62  ? 15.587  26.271  17.131  1.00 79.35  ?  62  PHE C CD2 1 
ATOM 3748 C CE1 . PHE C 1 62  ? 12.873  26.730  17.225  1.00 66.63  ?  62  PHE C CE1 1 
ATOM 3749 C CE2 . PHE C 1 62  ? 15.092  27.531  16.868  1.00 71.53  ?  62  PHE C CE2 1 
ATOM 3750 C CZ  . PHE C 1 62  ? 13.735  27.760  16.917  1.00 64.31  ?  62  PHE C CZ  1 
ATOM 3751 N N   . SER C 1 63  ? 14.852  21.354  20.038  1.00 67.80  ?  63  SER C N   1 
ATOM 3752 C CA  . SER C 1 63  ? 15.041  19.931  20.284  1.00 67.49  ?  63  SER C CA  1 
ATOM 3753 C C   . SER C 1 63  ? 13.750  19.176  20.001  1.00 66.45  ?  63  SER C C   1 
ATOM 3754 O O   . SER C 1 63  ? 12.649  19.711  20.149  1.00 64.86  ?  63  SER C O   1 
ATOM 3755 C CB  . SER C 1 63  ? 15.503  19.668  21.722  1.00 65.46  ?  63  SER C CB  1 
ATOM 3756 O OG  . SER C 1 63  ? 14.629  20.278  22.655  1.00 67.65  ?  63  SER C OG  1 
ATOM 3757 N N   . GLY C 1 64  ? 13.900  17.921  19.597  1.00 67.10  ?  64  GLY C N   1 
ATOM 3758 C CA  . GLY C 1 64  ? 12.761  17.074  19.312  1.00 67.16  ?  64  GLY C CA  1 
ATOM 3759 C C   . GLY C 1 64  ? 12.852  15.768  20.075  1.00 68.82  ?  64  GLY C C   1 
ATOM 3760 O O   . GLY C 1 64  ? 13.931  15.216  20.277  1.00 69.76  ?  64  GLY C O   1 
ATOM 3761 N N   . SER C 1 65  ? 11.688  15.275  20.490  1.00 69.43  ?  65  SER C N   1 
ATOM 3762 C CA  . SER C 1 65  ? 11.615  14.073  21.307  1.00 66.70  ?  65  SER C CA  1 
ATOM 3763 C C   . SER C 1 65  ? 10.445  13.210  20.867  1.00 66.49  ?  65  SER C C   1 
ATOM 3764 O O   . SER C 1 65  ? 9.413   13.716  20.425  1.00 71.76  ?  65  SER C O   1 
ATOM 3765 C CB  . SER C 1 65  ? 11.461  14.427  22.790  1.00 62.11  ?  65  SER C CB  1 
ATOM 3766 O OG  . SER C 1 65  ? 11.073  13.292  23.540  1.00 76.81  ?  65  SER C OG  1 
ATOM 3767 N N   . ARG C 1 66  ? 10.609  11.897  21.003  1.00 66.30  ?  66  ARG C N   1 
ATOM 3768 C CA  . ARG C 1 66  ? 9.564   10.947  20.654  1.00 62.28  ?  66  ARG C CA  1 
ATOM 3769 C C   . ARG C 1 66  ? 9.292   10.020  21.832  1.00 70.77  ?  66  ARG C C   1 
ATOM 3770 O O   . ARG C 1 66  ? 10.216  9.602   22.538  1.00 64.18  ?  66  ARG C O   1 
ATOM 3771 C CB  . ARG C 1 66  ? 9.935   10.124  19.418  1.00 64.37  ?  66  ARG C CB  1 
ATOM 3772 C CG  . ARG C 1 66  ? 8.857   9.125   19.014  1.00 67.22  ?  66  ARG C CG  1 
ATOM 3773 C CD  . ARG C 1 66  ? 9.451   7.909   18.333  1.00 70.33  ?  66  ARG C CD  1 
ATOM 3774 N NE  . ARG C 1 66  ? 8.427   6.954   17.924  1.00 75.06  ?  66  ARG C NE  1 
ATOM 3775 C CZ  . ARG C 1 66  ? 8.685   5.713   17.521  1.00 77.34  ?  66  ARG C CZ  1 
ATOM 3776 N NH1 . ARG C 1 66  ? 7.691   4.910   17.163  1.00 76.35  ?  66  ARG C NH1 1 
ATOM 3777 N NH2 . ARG C 1 66  ? 9.938   5.276   17.473  1.00 77.58  ?  66  ARG C NH2 1 
ATOM 3778 N N   . SER C 1 67  ? 8.013   9.714   22.039  1.00 67.03  ?  67  SER C N   1 
ATOM 3779 C CA  . SER C 1 67  ? 7.565   8.748   23.039  1.00 58.33  ?  67  SER C CA  1 
ATOM 3780 C C   . SER C 1 67  ? 6.368   8.027   22.426  1.00 61.67  ?  67  SER C C   1 
ATOM 3781 O O   . SER C 1 67  ? 5.241   8.529   22.477  1.00 60.70  ?  67  SER C O   1 
ATOM 3782 C CB  . SER C 1 67  ? 7.203   9.432   24.352  1.00 63.86  ?  67  SER C CB  1 
ATOM 3783 O OG  . SER C 1 67  ? 6.862   8.486   25.354  1.00 69.97  ?  67  SER C OG  1 
ATOM 3784 N N   . GLY C 1 68  ? 6.622   6.865   21.828  1.00 64.87  ?  68  GLY C N   1 
ATOM 3785 C CA  . GLY C 1 68  ? 5.587   6.135   21.123  1.00 63.05  ?  68  GLY C CA  1 
ATOM 3786 C C   . GLY C 1 68  ? 5.044   6.920   19.947  1.00 67.83  ?  68  GLY C C   1 
ATOM 3787 O O   . GLY C 1 68  ? 5.733   7.089   18.936  1.00 67.52  ?  68  GLY C O   1 
ATOM 3788 N N   . THR C 1 69  ? 3.820   7.428   20.079  1.00 64.97  ?  69  THR C N   1 
ATOM 3789 C CA  . THR C 1 69  ? 3.190   8.239   19.047  1.00 60.34  ?  69  THR C CA  1 
ATOM 3790 C C   . THR C 1 69  ? 3.159   9.719   19.393  1.00 64.48  ?  69  THR C C   1 
ATOM 3791 O O   . THR C 1 69  ? 2.595   10.506  18.625  1.00 71.66  ?  69  THR C O   1 
ATOM 3792 C CB  . THR C 1 69  ? 1.760   7.753   18.774  1.00 57.17  ?  69  THR C CB  1 
ATOM 3793 O OG1 . THR C 1 69  ? 0.983   7.839   19.974  1.00 58.76  ?  69  THR C OG1 1 
ATOM 3794 C CG2 . THR C 1 69  ? 1.763   6.322   18.280  1.00 64.51  ?  69  THR C CG2 1 
ATOM 3795 N N   . LYS C 1 70  ? 3.738   10.118  20.525  1.00 61.66  ?  70  LYS C N   1 
ATOM 3796 C CA  . LYS C 1 70  ? 3.746   11.507  20.969  1.00 59.34  ?  70  LYS C CA  1 
ATOM 3797 C C   . LYS C 1 70  ? 5.094   12.139  20.636  1.00 57.89  ?  70  LYS C C   1 
ATOM 3798 O O   . LYS C 1 70  ? 6.135   11.676  21.112  1.00 59.88  ?  70  LYS C O   1 
ATOM 3799 C CB  . LYS C 1 70  ? 3.475   11.583  22.474  1.00 60.16  ?  70  LYS C CB  1 
ATOM 3800 C CG  . LYS C 1 70  ? 3.272   12.984  23.033  1.00 60.58  ?  70  LYS C CG  1 
ATOM 3801 C CD  . LYS C 1 70  ? 2.929   12.930  24.523  1.00 74.47  ?  70  LYS C CD  1 
ATOM 3802 C CE  . LYS C 1 70  ? 1.615   12.184  24.781  1.00 73.60  ?  70  LYS C CE  1 
ATOM 3803 N NZ  . LYS C 1 70  ? 1.226   12.170  26.229  1.00 66.93  ?  70  LYS C NZ  1 
ATOM 3804 N N   . PHE C 1 71  ? 5.078   13.195  19.829  1.00 58.97  ?  71  PHE C N   1 
ATOM 3805 C CA  . PHE C 1 71  ? 6.285   13.919  19.457  1.00 62.18  ?  71  PHE C CA  1 
ATOM 3806 C C   . PHE C 1 71  ? 6.251   15.310  20.079  1.00 59.83  ?  71  PHE C C   1 
ATOM 3807 O O   . PHE C 1 71  ? 5.196   15.946  20.143  1.00 57.33  ?  71  PHE C O   1 
ATOM 3808 C CB  . PHE C 1 71  ? 6.418   14.010  17.935  1.00 56.32  ?  71  PHE C CB  1 
ATOM 3809 C CG  . PHE C 1 71  ? 6.494   12.672  17.260  1.00 52.67  ?  71  PHE C CG  1 
ATOM 3810 C CD1 . PHE C 1 71  ? 5.344   11.934  17.017  1.00 52.74  ?  71  PHE C CD1 1 
ATOM 3811 C CD2 . PHE C 1 71  ? 7.716   12.144  16.880  1.00 54.48  ?  71  PHE C CD2 1 
ATOM 3812 C CE1 . PHE C 1 71  ? 5.411   10.696  16.402  1.00 56.45  ?  71  PHE C CE1 1 
ATOM 3813 C CE2 . PHE C 1 71  ? 7.792   10.909  16.263  1.00 58.06  ?  71  PHE C CE2 1 
ATOM 3814 C CZ  . PHE C 1 71  ? 6.637   10.182  16.026  1.00 58.74  ?  71  PHE C CZ  1 
ATOM 3815 N N   . THR C 1 72  ? 7.406   15.776  20.540  1.00 62.63  ?  72  THR C N   1 
ATOM 3816 C CA  . THR C 1 72  ? 7.498   17.015  21.299  1.00 57.62  ?  72  THR C CA  1 
ATOM 3817 C C   . THR C 1 72  ? 8.603   17.891  20.734  1.00 60.12  ?  72  THR C C   1 
ATOM 3818 O O   . THR C 1 72  ? 9.747   17.444  20.592  1.00 60.28  ?  72  THR C O   1 
ATOM 3819 C CB  . THR C 1 72  ? 7.757   16.743  22.781  1.00 63.77  ?  72  THR C CB  1 
ATOM 3820 O OG1 . THR C 1 72  ? 6.586   16.165  23.372  1.00 71.96  ?  72  THR C OG1 1 
ATOM 3821 C CG2 . THR C 1 72  ? 8.104   18.040  23.507  1.00 60.43  ?  72  THR C CG2 1 
ATOM 3822 N N   . LEU C 1 73  ? 8.252   19.133  20.420  1.00 58.30  ?  73  LEU C N   1 
ATOM 3823 C CA  . LEU C 1 73  ? 9.203   20.153  20.008  1.00 59.09  ?  73  LEU C CA  1 
ATOM 3824 C C   . LEU C 1 73  ? 9.416   21.107  21.172  1.00 59.88  ?  73  LEU C C   1 
ATOM 3825 O O   . LEU C 1 73  ? 8.448   21.611  21.752  1.00 59.82  ?  73  LEU C O   1 
ATOM 3826 C CB  . LEU C 1 73  ? 8.692   20.911  18.783  1.00 64.02  ?  73  LEU C CB  1 
ATOM 3827 C CG  . LEU C 1 73  ? 9.475   22.142  18.326  1.00 59.98  ?  73  LEU C CG  1 
ATOM 3828 C CD1 . LEU C 1 73  ? 10.816  21.739  17.736  1.00 64.86  ?  73  LEU C CD1 1 
ATOM 3829 C CD2 . LEU C 1 73  ? 8.655   22.917  17.316  1.00 59.85  ?  73  LEU C CD2 1 
ATOM 3830 N N   . THR C 1 74  ? 10.676  21.314  21.542  1.00 62.33  ?  74  THR C N   1 
ATOM 3831 C CA  . THR C 1 74  ? 11.027  22.137  22.689  1.00 63.78  ?  74  THR C CA  1 
ATOM 3832 C C   . THR C 1 74  ? 11.970  23.251  22.259  1.00 62.46  ?  74  THR C C   1 
ATOM 3833 O O   . THR C 1 74  ? 13.006  22.988  21.635  1.00 61.42  ?  74  THR C O   1 
ATOM 3834 C CB  . THR C 1 74  ? 11.676  21.287  23.786  1.00 67.53  ?  74  THR C CB  1 
ATOM 3835 O OG1 . THR C 1 74  ? 10.735  20.308  24.252  1.00 71.46  ?  74  THR C OG1 1 
ATOM 3836 C CG2 . THR C 1 74  ? 12.112  22.163  24.951  1.00 64.21  ?  74  THR C CG2 1 
ATOM 3837 N N   . ILE C 1 75  ? 11.602  24.489  22.578  1.00 63.77  ?  75  ILE C N   1 
ATOM 3838 C CA  . ILE C 1 75  ? 12.509  25.630  22.483  1.00 65.53  ?  75  ILE C CA  1 
ATOM 3839 C C   . ILE C 1 75  ? 12.928  25.979  23.904  1.00 67.37  ?  75  ILE C C   1 
ATOM 3840 O O   . ILE C 1 75  ? 12.106  26.444  24.703  1.00 69.35  ?  75  ILE C O   1 
ATOM 3841 C CB  . ILE C 1 75  ? 11.860  26.829  21.783  1.00 70.69  ?  75  ILE C CB  1 
ATOM 3842 C CG1 . ILE C 1 75  ? 11.244  26.409  20.451  1.00 65.01  ?  75  ILE C CG1 1 
ATOM 3843 C CG2 . ILE C 1 75  ? 12.886  27.935  21.561  1.00 74.67  ?  75  ILE C CG2 1 
ATOM 3844 C CD1 . ILE C 1 75  ? 10.504  27.531  19.760  1.00 61.29  ?  75  ILE C CD1 1 
ATOM 3845 N N   . SER C 1 76  ? 14.206  25.752  24.223  1.00 75.22  ?  76  SER C N   1 
ATOM 3846 C CA  . SER C 1 76  ? 14.657  25.860  25.609  1.00 83.07  ?  76  SER C CA  1 
ATOM 3847 C C   . SER C 1 76  ? 14.748  27.314  26.060  1.00 81.35  ?  76  SER C C   1 
ATOM 3848 O O   . SER C 1 76  ? 14.241  27.675  27.128  1.00 82.62  ?  76  SER C O   1 
ATOM 3849 C CB  . SER C 1 76  ? 16.006  25.157  25.784  1.00 82.45  ?  76  SER C CB  1 
ATOM 3850 O OG  . SER C 1 76  ? 16.997  25.729  24.947  1.00 94.71  ?  76  SER C OG  1 
ATOM 3851 N N   . SER C 1 77  ? 15.395  28.162  25.266  1.00 80.87  ?  77  SER C N   1 
ATOM 3852 C CA  . SER C 1 77  ? 15.544  29.583  25.576  1.00 77.85  ?  77  SER C CA  1 
ATOM 3853 C C   . SER C 1 77  ? 14.930  30.373  24.425  1.00 83.10  ?  77  SER C C   1 
ATOM 3854 O O   . SER C 1 77  ? 15.533  30.501  23.354  1.00 87.54  ?  77  SER C O   1 
ATOM 3855 C CB  . SER C 1 77  ? 17.011  29.945  25.796  1.00 75.25  ?  77  SER C CB  1 
ATOM 3856 O OG  . SER C 1 77  ? 17.142  31.273  26.264  1.00 79.83  ?  77  SER C OG  1 
ATOM 3857 N N   . LEU C 1 78  ? 13.722  30.883  24.645  1.00 80.57  ?  78  LEU C N   1 
ATOM 3858 C CA  . LEU C 1 78  ? 13.007  31.612  23.606  1.00 79.21  ?  78  LEU C CA  1 
ATOM 3859 C C   . LEU C 1 78  ? 13.716  32.924  23.286  1.00 78.56  ?  78  LEU C C   1 
ATOM 3860 O O   . LEU C 1 78  ? 14.101  33.674  24.189  1.00 74.29  ?  78  LEU C O   1 
ATOM 3861 C CB  . LEU C 1 78  ? 11.570  31.874  24.049  1.00 73.13  ?  78  LEU C CB  1 
ATOM 3862 C CG  . LEU C 1 78  ? 10.562  32.123  22.935  1.00 67.31  ?  78  LEU C CG  1 
ATOM 3863 C CD1 . LEU C 1 78  ? 10.489  30.900  22.051  1.00 71.68  ?  78  LEU C CD1 1 
ATOM 3864 C CD2 . LEU C 1 78  ? 9.202   32.435  23.526  1.00 68.58  ?  78  LEU C CD2 1 
ATOM 3865 N N   . GLN C 1 79  ? 13.891  33.193  22.000  1.00 80.69  ?  79  GLN C N   1 
ATOM 3866 C CA  . GLN C 1 79  ? 14.521  34.398  21.485  1.00 81.12  ?  79  GLN C CA  1 
ATOM 3867 C C   . GLN C 1 79  ? 13.484  35.262  20.780  1.00 82.79  ?  79  GLN C C   1 
ATOM 3868 O O   . GLN C 1 79  ? 12.439  34.762  20.353  1.00 83.73  ?  79  GLN C O   1 
ATOM 3869 C CB  . GLN C 1 79  ? 15.650  34.046  20.504  1.00 81.21  ?  79  GLN C CB  1 
ATOM 3870 C CG  . GLN C 1 79  ? 16.768  33.218  21.112  1.00 82.25  ?  79  GLN C CG  1 
ATOM 3871 C CD  . GLN C 1 79  ? 17.407  33.901  22.301  1.00 83.94  ?  79  GLN C CD  1 
ATOM 3872 O OE1 . GLN C 1 79  ? 17.523  33.315  23.378  1.00 79.12  ?  79  GLN C OE1 1 
ATOM 3873 N NE2 . GLN C 1 79  ? 17.833  35.145  22.111  1.00 84.90  ?  79  GLN C NE2 1 
ATOM 3874 N N   . PRO C 1 80  ? 13.729  36.573  20.652  1.00 86.84  ?  80  PRO C N   1 
ATOM 3875 C CA  . PRO C 1 80  ? 12.739  37.443  19.989  1.00 81.09  ?  80  PRO C CA  1 
ATOM 3876 C C   . PRO C 1 80  ? 12.457  37.091  18.536  1.00 77.62  ?  80  PRO C C   1 
ATOM 3877 O O   . PRO C 1 80  ? 11.497  37.631  17.973  1.00 82.55  ?  80  PRO C O   1 
ATOM 3878 C CB  . PRO C 1 80  ? 13.365  38.841  20.111  1.00 81.26  ?  80  PRO C CB  1 
ATOM 3879 C CG  . PRO C 1 80  ? 14.824  38.586  20.276  1.00 79.94  ?  80  PRO C CG  1 
ATOM 3880 C CD  . PRO C 1 80  ? 14.885  37.349  21.133  1.00 86.20  ?  80  PRO C CD  1 
ATOM 3881 N N   . GLU C 1 81  ? 13.246  36.220  17.909  1.00 78.25  ?  81  GLU C N   1 
ATOM 3882 C CA  . GLU C 1 81  ? 13.035  35.865  16.512  1.00 74.70  ?  81  GLU C CA  1 
ATOM 3883 C C   . GLU C 1 81  ? 12.334  34.529  16.336  1.00 72.36  ?  81  GLU C C   1 
ATOM 3884 O O   . GLU C 1 81  ? 12.140  34.101  15.195  1.00 75.95  ?  81  GLU C O   1 
ATOM 3885 C CB  . GLU C 1 81  ? 14.372  35.820  15.767  1.00 80.28  ?  81  GLU C CB  1 
ATOM 3886 C CG  . GLU C 1 81  ? 15.354  34.823  16.362  1.00 80.31  ?  81  GLU C CG  1 
ATOM 3887 C CD  . GLU C 1 81  ? 16.251  35.437  17.420  1.00 87.69  ?  81  GLU C CD  1 
ATOM 3888 O OE1 . GLU C 1 81  ? 15.850  36.454  18.030  1.00 85.02  ?  81  GLU C OE1 1 
ATOM 3889 O OE2 . GLU C 1 81  ? 17.349  34.890  17.651  1.00 91.24  ?  81  GLU C OE2 1 
ATOM 3890 N N   . ASP C 1 82  ? 11.964  33.856  17.427  1.00 71.19  ?  82  ASP C N   1 
ATOM 3891 C CA  . ASP C 1 82  ? 11.311  32.557  17.333  1.00 73.63  ?  82  ASP C CA  1 
ATOM 3892 C C   . ASP C 1 82  ? 9.793   32.645  17.379  1.00 65.10  ?  82  ASP C C   1 
ATOM 3893 O O   . ASP C 1 82  ? 9.125   31.621  17.205  1.00 64.52  ?  82  ASP C O   1 
ATOM 3894 C CB  . ASP C 1 82  ? 11.797  31.630  18.452  1.00 73.97  ?  82  ASP C CB  1 
ATOM 3895 C CG  . ASP C 1 82  ? 13.300  31.477  18.469  1.00 75.68  ?  82  ASP C CG  1 
ATOM 3896 O OD1 . ASP C 1 82  ? 13.887  31.472  19.572  1.00 80.14  ?  82  ASP C OD1 1 
ATOM 3897 O OD2 . ASP C 1 82  ? 13.901  31.389  17.379  1.00 78.10  ?  82  ASP C OD2 1 
ATOM 3898 N N   . PHE C 1 83  ? 9.235   33.825  17.632  1.00 62.92  ?  83  PHE C N   1 
ATOM 3899 C CA  . PHE C 1 83  ? 7.794   34.018  17.534  1.00 65.44  ?  83  PHE C CA  1 
ATOM 3900 C C   . PHE C 1 83  ? 7.357   33.792  16.094  1.00 65.84  ?  83  PHE C C   1 
ATOM 3901 O O   . PHE C 1 83  ? 7.679   34.593  15.209  1.00 67.91  ?  83  PHE C O   1 
ATOM 3902 C CB  . PHE C 1 83  ? 7.405   35.408  18.035  1.00 68.80  ?  83  PHE C CB  1 
ATOM 3903 C CG  . PHE C 1 83  ? 7.852   35.675  19.440  1.00 64.37  ?  83  PHE C CG  1 
ATOM 3904 C CD1 . PHE C 1 83  ? 8.871   36.578  19.700  1.00 64.49  ?  83  PHE C CD1 1 
ATOM 3905 C CD2 . PHE C 1 83  ? 7.278   34.990  20.500  1.00 65.03  ?  83  PHE C CD2 1 
ATOM 3906 C CE1 . PHE C 1 83  ? 9.292   36.814  20.993  1.00 68.24  ?  83  PHE C CE1 1 
ATOM 3907 C CE2 . PHE C 1 83  ? 7.695   35.215  21.799  1.00 68.35  ?  83  PHE C CE2 1 
ATOM 3908 C CZ  . PHE C 1 83  ? 8.704   36.130  22.047  1.00 71.64  ?  83  PHE C CZ  1 
ATOM 3909 N N   . ALA C 1 84  ? 6.621   32.715  15.855  1.00 59.23  ?  84  ALA C N   1 
ATOM 3910 C CA  . ALA C 1 84  ? 6.271   32.268  14.511  1.00 52.38  ?  84  ALA C CA  1 
ATOM 3911 C C   . ALA C 1 84  ? 5.176   31.219  14.655  1.00 52.94  ?  84  ALA C C   1 
ATOM 3912 O O   . ALA C 1 84  ? 4.601   31.047  15.737  1.00 57.12  ?  84  ALA C O   1 
ATOM 3913 C CB  . ALA C 1 84  ? 7.499   31.725  13.778  1.00 54.94  ?  84  ALA C CB  1 
ATOM 3914 N N   . THR C 1 85  ? 4.895   30.496  13.578  1.00 56.13  ?  85  THR C N   1 
ATOM 3915 C CA  . THR C 1 85  ? 3.963   29.383  13.621  1.00 53.36  ?  85  THR C CA  1 
ATOM 3916 C C   . THR C 1 85  ? 4.745   28.117  13.312  1.00 56.77  ?  85  THR C C   1 
ATOM 3917 O O   . THR C 1 85  ? 5.571   28.100  12.397  1.00 62.20  ?  85  THR C O   1 
ATOM 3918 C CB  . THR C 1 85  ? 2.812   29.584  12.623  1.00 51.22  ?  85  THR C CB  1 
ATOM 3919 O OG1 . THR C 1 85  ? 2.123   30.805  12.921  1.00 54.80  ?  85  THR C OG1 1 
ATOM 3920 C CG2 . THR C 1 85  ? 1.820   28.434  12.693  1.00 50.62  ?  85  THR C CG2 1 
ATOM 3921 N N   . TYR C 1 86  ? 4.553   27.091  14.126  1.00 50.36  ?  86  TYR C N   1 
ATOM 3922 C CA  . TYR C 1 86  ? 5.285   25.844  13.981  1.00 54.57  ?  86  TYR C CA  1 
ATOM 3923 C C   . TYR C 1 86  ? 4.334   24.726  13.570  1.00 55.70  ?  86  TYR C C   1 
ATOM 3924 O O   . TYR C 1 86  ? 3.188   24.668  14.028  1.00 57.78  ?  86  TYR C O   1 
ATOM 3925 C CB  . TYR C 1 86  ? 6.033   25.505  15.274  1.00 55.19  ?  86  TYR C CB  1 
ATOM 3926 C CG  . TYR C 1 86  ? 7.090   26.542  15.613  1.00 56.37  ?  86  TYR C CG  1 
ATOM 3927 C CD1 . TYR C 1 86  ? 6.745   27.733  16.241  1.00 58.34  ?  86  TYR C CD1 1 
ATOM 3928 C CD2 . TYR C 1 86  ? 8.426   26.344  15.279  1.00 54.89  ?  86  TYR C CD2 1 
ATOM 3929 C CE1 . TYR C 1 86  ? 7.700   28.689  16.544  1.00 56.89  ?  86  TYR C CE1 1 
ATOM 3930 C CE2 . TYR C 1 86  ? 9.389   27.297  15.577  1.00 52.96  ?  86  TYR C CE2 1 
ATOM 3931 C CZ  . TYR C 1 86  ? 9.020   28.467  16.207  1.00 58.16  ?  86  TYR C CZ  1 
ATOM 3932 O OH  . TYR C 1 86  ? 9.968   29.420  16.507  1.00 60.08  ?  86  TYR C OH  1 
ATOM 3933 N N   . TYR C 1 87  ? 4.805   23.859  12.677  1.00 49.20  ?  87  TYR C N   1 
ATOM 3934 C CA  . TYR C 1 87  ? 3.993   22.779  12.137  1.00 53.21  ?  87  TYR C CA  1 
ATOM 3935 C C   . TYR C 1 87  ? 4.731   21.456  12.265  1.00 60.85  ?  87  TYR C C   1 
ATOM 3936 O O   . TYR C 1 87  ? 5.961   21.405  12.188  1.00 63.86  ?  87  TYR C O   1 
ATOM 3937 C CB  . TYR C 1 87  ? 3.635   23.000  10.656  1.00 55.22  ?  87  TYR C CB  1 
ATOM 3938 C CG  . TYR C 1 87  ? 2.728   24.172  10.385  1.00 48.71  ?  87  TYR C CG  1 
ATOM 3939 C CD1 . TYR C 1 87  ? 1.349   24.033  10.463  1.00 50.00  ?  87  TYR C CD1 1 
ATOM 3940 C CD2 . TYR C 1 87  ? 3.242   25.402  10.007  1.00 45.63  ?  87  TYR C CD2 1 
ATOM 3941 C CE1 . TYR C 1 87  ? 0.508   25.097  10.207  1.00 48.16  ?  87  TYR C CE1 1 
ATOM 3942 C CE2 . TYR C 1 87  ? 2.408   26.470  9.747   1.00 45.96  ?  87  TYR C CE2 1 
ATOM 3943 C CZ  . TYR C 1 87  ? 1.041   26.311  9.849   1.00 45.86  ?  87  TYR C CZ  1 
ATOM 3944 O OH  . TYR C 1 87  ? 0.195   27.367  9.590   1.00 49.15  ?  87  TYR C OH  1 
ATOM 3945 N N   . CYS C 1 88  ? 3.967   20.381  12.450  1.00 60.07  ?  88  CYS C N   1 
ATOM 3946 C CA  . CYS C 1 88  ? 4.503   19.032  12.349  1.00 65.52  ?  88  CYS C CA  1 
ATOM 3947 C C   . CYS C 1 88  ? 4.012   18.376  11.065  1.00 63.88  ?  88  CYS C C   1 
ATOM 3948 O O   . CYS C 1 88  ? 2.912   18.660  10.581  1.00 64.76  ?  88  CYS C O   1 
ATOM 3949 C CB  . CYS C 1 88  ? 4.133   18.159  13.565  1.00 61.98  ?  88  CYS C CB  1 
ATOM 3950 S SG  . CYS C 1 88  ? 2.420   18.205  14.173  1.00 62.85  ?  88  CYS C SG  1 
ATOM 3951 N N   . LEU C 1 89  ? 4.857   17.509  10.510  1.00 65.96  ?  89  LEU C N   1 
ATOM 3952 C CA  . LEU C 1 89  ? 4.565   16.767  9.288   1.00 65.38  ?  89  LEU C CA  1 
ATOM 3953 C C   . LEU C 1 89  ? 4.895   15.302  9.520   1.00 68.46  ?  89  LEU C C   1 
ATOM 3954 O O   . LEU C 1 89  ? 6.035   14.968  9.864   1.00 69.81  ?  89  LEU C O   1 
ATOM 3955 C CB  . LEU C 1 89  ? 5.362   17.315  8.102   1.00 63.05  ?  89  LEU C CB  1 
ATOM 3956 C CG  . LEU C 1 89  ? 5.213   16.537  6.800   1.00 63.76  ?  89  LEU C CG  1 
ATOM 3957 C CD1 . LEU C 1 89  ? 3.775   16.567  6.327   1.00 65.58  ?  89  LEU C CD1 1 
ATOM 3958 C CD2 . LEU C 1 89  ? 6.139   17.114  5.751   1.00 64.32  ?  89  LEU C CD2 1 
ATOM 3959 N N   . GLY C 1 90  ? 3.908   14.439  9.330   1.00 68.32  ?  90  GLY C N   1 
ATOM 3960 C CA  . GLY C 1 90  ? 4.075   13.008  9.532   1.00 70.92  ?  90  GLY C CA  1 
ATOM 3961 C C   . GLY C 1 90  ? 3.901   12.246  8.233   1.00 76.62  ?  90  GLY C C   1 
ATOM 3962 O O   . GLY C 1 90  ? 3.010   12.553  7.436   1.00 79.40  ?  90  GLY C O   1 
ATOM 3963 N N   . ILE C 1 91  ? 4.851   11.347  7.975   1.00 81.58  ?  91  ILE C N   1 
ATOM 3964 C CA  . ILE C 1 91  ? 4.823   10.522  6.742   1.00 80.07  ?  91  ILE C CA  1 
ATOM 3965 C C   . ILE C 1 91  ? 4.742   9.063   7.174   1.00 85.87  ?  91  ILE C C   1 
ATOM 3966 O O   . ILE C 1 91  ? 5.476   8.690   8.086   1.00 85.70  ?  91  ILE C O   1 
ATOM 3967 C CB  . ILE C 1 91  ? 6.077   10.805  5.907   1.00 82.10  ?  91  ILE C CB  1 
ATOM 3968 C CG1 . ILE C 1 91  ? 6.037   12.201  5.284   1.00 79.51  ?  91  ILE C CG1 1 
ATOM 3969 C CG2 . ILE C 1 91  ? 6.273   9.728   4.856   1.00 91.14  ?  91  ILE C CG2 1 
ATOM 3970 C CD1 . ILE C 1 91  ? 7.255   13.037  5.584   1.00 78.58  ?  91  ILE C CD1 1 
ATOM 3971 N N   . TYR C 1 92  ? 3.829   8.291   6.589   1.00 89.76  ?  92  TYR C N   1 
ATOM 3972 C CA  . TYR C 1 92  ? 3.591   6.887   6.996   1.00 91.21  ?  92  TYR C CA  1 
ATOM 3973 C C   . TYR C 1 92  ? 4.298   5.941   6.043   1.00 94.85  ?  92  TYR C C   1 
ATOM 3974 O O   . TYR C 1 92  ? 3.933   4.764   5.969   1.00 101.17 ?  92  TYR C O   1 
ATOM 3975 C CB  . TYR C 1 92  ? 2.100   6.610   6.887   1.00 85.48  ?  92  TYR C CB  1 
ATOM 3976 C CG  . TYR C 1 92  ? 1.610   5.249   7.306   1.00 96.39  ?  92  TYR C CG  1 
ATOM 3977 C CD1 . TYR C 1 92  ? 2.189   4.554   8.354   1.00 97.22  ?  92  TYR C CD1 1 
ATOM 3978 C CD2 . TYR C 1 92  ? 0.539   4.667   6.654   1.00 95.73  ?  92  TYR C CD2 1 
ATOM 3979 C CE1 . TYR C 1 92  ? 1.722   3.307   8.734   1.00 93.03  ?  92  TYR C CE1 1 
ATOM 3980 C CE2 . TYR C 1 92  ? 0.058   3.425   7.023   1.00 97.45  ?  92  TYR C CE2 1 
ATOM 3981 C CZ  . TYR C 1 92  ? 0.652   2.743   8.066   1.00 99.13  ?  92  TYR C CZ  1 
ATOM 3982 O OH  . TYR C 1 92  ? 0.165   1.520   8.417   1.00 100.36 ?  92  TYR C OH  1 
ATOM 3983 N N   . GLY C 1 93  ? 5.295   6.443   5.331   1.00 94.21  ?  93  GLY C N   1 
ATOM 3984 C CA  . GLY C 1 93  ? 5.950   5.606   4.317   1.00 97.51  ?  93  GLY C CA  1 
ATOM 3985 C C   . GLY C 1 93  ? 5.570   6.059   2.923   1.00 108.71 ?  93  GLY C C   1 
ATOM 3986 O O   . GLY C 1 93  ? 4.447   5.737   2.509   1.00 110.80 ?  93  GLY C O   1 
ATOM 3987 N N   . ASP C 1 94  ? 6.418   6.855   2.271   1.00 102.82 ?  94  ASP C N   1 
ATOM 3988 C CA  . ASP C 1 94  ? 6.206   7.245   0.852   1.00 98.97  ?  94  ASP C CA  1 
ATOM 3989 C C   . ASP C 1 94  ? 5.016   8.185   0.638   1.00 104.85 ?  94  ASP C C   1 
ATOM 3990 O O   . ASP C 1 94  ? 5.163   9.132   -0.148  1.00 104.47 ?  94  ASP C O   1 
ATOM 3991 C CB  . ASP C 1 94  ? 6.142   5.999   -0.040  1.00 106.91 ?  94  ASP C CB  1 
ATOM 3992 C CG  . ASP C 1 94  ? 7.457   5.262   -0.242  1.00 111.88 ?  94  ASP C CG  1 
ATOM 3993 O OD1 . ASP C 1 94  ? 8.516   5.838   0.066   1.00 108.66 ?  94  ASP C OD1 1 
ATOM 3994 O OD2 . ASP C 1 94  ? 7.408   4.106   -0.702  1.00 116.00 ?  94  ASP C OD2 1 
ATOM 3995 N N   . GLY C 1 95  ? 3.885   7.957   1.288   1.00 98.95  ?  95  GLY C N   1 
ATOM 3996 C CA  . GLY C 1 95  ? 2.720   8.753   0.964   1.00 96.73  ?  95  GLY C CA  1 
ATOM 3997 C C   . GLY C 1 95  ? 1.721   8.004   0.107   1.00 100.25 ?  95  GLY C C   1 
ATOM 3998 O O   . GLY C 1 95  ? 1.812   7.994   -1.125  1.00 103.21 ?  95  GLY C O   1 
ATOM 3999 N N   . ALA C 1 96  ? 0.770   7.352   0.769   1.00 91.48  ?  96  ALA C N   1 
ATOM 4000 C CA  . ALA C 1 96  ? -0.319  6.648   0.111   1.00 97.28  ?  96  ALA C CA  1 
ATOM 4001 C C   . ALA C 1 96  ? -1.466  6.551   1.105   1.00 108.30 ?  96  ALA C C   1 
ATOM 4002 O O   . ALA C 1 96  ? -1.240  6.478   2.317   1.00 108.37 ?  96  ALA C O   1 
ATOM 4003 C CB  . ALA C 1 96  ? 0.108   5.257   -0.371  1.00 94.20  ?  96  ALA C CB  1 
ATOM 4004 N N   . ASP C 1 97  ? -2.693  6.533   0.581   1.00 112.15 ?  97  ASP C N   1 
ATOM 4005 C CA  . ASP C 1 97  ? -3.901  6.589   1.407   1.00 107.86 ?  97  ASP C CA  1 
ATOM 4006 C C   . ASP C 1 97  ? -3.851  7.800   2.338   1.00 103.80 ?  97  ASP C C   1 
ATOM 4007 O O   . ASP C 1 97  ? -4.128  7.708   3.536   1.00 105.01 ?  97  ASP C O   1 
ATOM 4008 C CB  . ASP C 1 97  ? -4.106  5.293   2.201   1.00 107.36 ?  97  ASP C CB  1 
ATOM 4009 C CG  . ASP C 1 97  ? -4.198  4.066   1.311   1.00 114.81 ?  97  ASP C CG  1 
ATOM 4010 O OD1 . ASP C 1 97  ? -4.602  4.207   0.137   1.00 110.90 ?  97  ASP C OD1 1 
ATOM 4011 O OD2 . ASP C 1 97  ? -3.880  2.957   1.792   1.00 119.32 ?  97  ASP C OD2 1 
ATOM 4012 N N   . ASP C 1 98  ? -3.498  8.952   1.764   1.00 100.26 ?  98  ASP C N   1 
ATOM 4013 C CA  . ASP C 1 98  ? -3.265  10.187  2.514   1.00 92.97  ?  98  ASP C CA  1 
ATOM 4014 C C   . ASP C 1 98  ? -2.233  9.953   3.621   1.00 90.46  ?  98  ASP C C   1 
ATOM 4015 O O   . ASP C 1 98  ? -2.483  10.179  4.806   1.00 91.10  ?  98  ASP C O   1 
ATOM 4016 C CB  . ASP C 1 98  ? -4.574  10.749  3.084   1.00 91.63  ?  98  ASP C CB  1 
ATOM 4017 C CG  . ASP C 1 98  ? -5.628  11.003  2.012   1.00 91.13  ?  98  ASP C CG  1 
ATOM 4018 O OD1 . ASP C 1 98  ? -6.057  10.032  1.354   1.00 93.98  ?  98  ASP C OD1 1 
ATOM 4019 O OD2 . ASP C 1 98  ? -6.041  12.172  1.838   1.00 85.01  ?  98  ASP C OD2 1 
ATOM 4020 N N   . GLY C 1 99  ? -1.054  9.483   3.204   1.00 87.05  ?  99  GLY C N   1 
ATOM 4021 C CA  . GLY C 1 99  ? 0.023   9.170   4.128   1.00 78.86  ?  99  GLY C CA  1 
ATOM 4022 C C   . GLY C 1 99  ? 0.868   10.343  4.576   1.00 74.90  ?  99  GLY C C   1 
ATOM 4023 O O   . GLY C 1 99  ? 1.655   10.195  5.513   1.00 83.47  ?  99  GLY C O   1 
ATOM 4024 N N   . ILE C 1 100 ? 0.757   11.487  3.913   1.00 72.32  ?  100 ILE C N   1 
ATOM 4025 C CA  . ILE C 1 100 ? 1.436   12.711  4.322   1.00 71.99  ?  100 ILE C CA  1 
ATOM 4026 C C   . ILE C 1 100 ? 0.418   13.602  5.030   1.00 71.60  ?  100 ILE C C   1 
ATOM 4027 O O   . ILE C 1 100 ? -0.607  13.971  4.444   1.00 71.71  ?  100 ILE C O   1 
ATOM 4028 C CB  . ILE C 1 100 ? 2.082   13.417  3.120   1.00 71.69  ?  100 ILE C CB  1 
ATOM 4029 C CG1 . ILE C 1 100 ? 3.171   12.526  2.518   1.00 76.78  ?  100 ILE C CG1 1 
ATOM 4030 C CG2 . ILE C 1 100 ? 2.674   14.747  3.530   1.00 70.28  ?  100 ILE C CG2 1 
ATOM 4031 C CD1 . ILE C 1 100 ? 3.718   13.017  1.194   1.00 72.96  ?  100 ILE C CD1 1 
ATOM 4032 N N   . ALA C 1 101 ? 0.665   13.919  6.302   1.00 69.31  ?  101 ALA C N   1 
ATOM 4033 C CA  . ALA C 1 101 ? -0.295  14.667  7.108   1.00 64.52  ?  101 ALA C CA  1 
ATOM 4034 C C   . ALA C 1 101 ? 0.406   15.794  7.850   1.00 63.11  ?  101 ALA C C   1 
ATOM 4035 O O   . ALA C 1 101 ? 1.390   15.560  8.555   1.00 62.46  ?  101 ALA C O   1 
ATOM 4036 C CB  . ALA C 1 101 ? -1.014  13.756  8.107   1.00 65.72  ?  101 ALA C CB  1 
ATOM 4037 N N   . PHE C 1 102 ? -0.115  17.007  7.709   1.00 63.62  ?  102 PHE C N   1 
ATOM 4038 C CA  . PHE C 1 102 ? 0.408   18.159  8.427   1.00 56.64  ?  102 PHE C CA  1 
ATOM 4039 C C   . PHE C 1 102 ? -0.355  18.383  9.723   1.00 55.25  ?  102 PHE C C   1 
ATOM 4040 O O   . PHE C 1 102 ? -1.514  17.983  9.868   1.00 54.85  ?  102 PHE C O   1 
ATOM 4041 C CB  . PHE C 1 102 ? 0.334   19.421  7.568   1.00 54.68  ?  102 PHE C CB  1 
ATOM 4042 C CG  . PHE C 1 102 ? 1.520   19.621  6.673   1.00 53.49  ?  102 PHE C CG  1 
ATOM 4043 C CD1 . PHE C 1 102 ? 2.713   20.104  7.187   1.00 56.09  ?  102 PHE C CD1 1 
ATOM 4044 C CD2 . PHE C 1 102 ? 1.441   19.343  5.317   1.00 56.74  ?  102 PHE C CD2 1 
ATOM 4045 C CE1 . PHE C 1 102 ? 3.809   20.305  6.369   1.00 57.55  ?  102 PHE C CE1 1 
ATOM 4046 C CE2 . PHE C 1 102 ? 2.537   19.540  4.491   1.00 58.98  ?  102 PHE C CE2 1 
ATOM 4047 C CZ  . PHE C 1 102 ? 3.723   20.022  5.020   1.00 60.26  ?  102 PHE C CZ  1 
ATOM 4048 N N   . GLY C 1 103 ? 0.320   19.017  10.677  1.00 55.75  ?  103 GLY C N   1 
ATOM 4049 C CA  . GLY C 1 103 ? -0.329  19.414  11.903  1.00 56.19  ?  103 GLY C CA  1 
ATOM 4050 C C   . GLY C 1 103 ? -1.136  20.679  11.732  1.00 53.26  ?  103 GLY C C   1 
ATOM 4051 O O   . GLY C 1 103 ? -1.038  21.382  10.727  1.00 63.53  ?  103 GLY C O   1 
ATOM 4052 N N   . GLY C 1 104 ? -1.952  20.970  12.745  1.00 47.91  ?  104 GLY C N   1 
ATOM 4053 C CA  . GLY C 1 104 ? -2.785  22.158  12.697  1.00 49.86  ?  104 GLY C CA  1 
ATOM 4054 C C   . GLY C 1 104 ? -2.013  23.455  12.810  1.00 53.03  ?  104 GLY C C   1 
ATOM 4055 O O   . GLY C 1 104 ? -2.505  24.498  12.365  1.00 54.07  ?  104 GLY C O   1 
ATOM 4056 N N   . GLY C 1 105 ? -0.819  23.411  13.377  1.00 49.16  ?  105 GLY C N   1 
ATOM 4057 C CA  . GLY C 1 105 ? -0.015  24.598  13.567  1.00 45.65  ?  105 GLY C CA  1 
ATOM 4058 C C   . GLY C 1 105 ? -0.151  25.148  14.972  1.00 47.28  ?  105 GLY C C   1 
ATOM 4059 O O   . GLY C 1 105 ? -1.167  24.955  15.651  1.00 44.75  ?  105 GLY C O   1 
ATOM 4060 N N   . THR C 1 106 ? 0.912   25.802  15.438  1.00 47.60  ?  106 THR C N   1 
ATOM 4061 C CA  . THR C 1 106 ? 0.942   26.452  16.744  1.00 48.88  ?  106 THR C CA  1 
ATOM 4062 C C   . THR C 1 106 ? 1.543   27.835  16.568  1.00 50.67  ?  106 THR C C   1 
ATOM 4063 O O   . THR C 1 106 ? 2.692   27.957  16.136  1.00 54.92  ?  106 THR C O   1 
ATOM 4064 C CB  . THR C 1 106 ? 1.761   25.654  17.766  1.00 49.51  ?  106 THR C CB  1 
ATOM 4065 O OG1 . THR C 1 106 ? 1.161   24.369  17.976  1.00 54.41  ?  106 THR C OG1 1 
ATOM 4066 C CG2 . THR C 1 106 ? 1.825   26.397  19.088  1.00 49.01  ?  106 THR C CG2 1 
ATOM 4067 N N   . LYS C 1 107 ? 0.768   28.869  16.876  1.00 47.37  ?  107 LYS C N   1 
ATOM 4068 C CA  . LYS C 1 107 ? 1.241   30.243  16.780  1.00 50.18  ?  107 LYS C CA  1 
ATOM 4069 C C   . LYS C 1 107 ? 1.775   30.687  18.136  1.00 50.07  ?  107 LYS C C   1 
ATOM 4070 O O   . LYS C 1 107 ? 1.063   30.599  19.140  1.00 53.20  ?  107 LYS C O   1 
ATOM 4071 C CB  . LYS C 1 107 ? 0.117   31.167  16.307  1.00 54.49  ?  107 LYS C CB  1 
ATOM 4072 C CG  . LYS C 1 107 ? 0.551   32.607  16.060  1.00 53.40  ?  107 LYS C CG  1 
ATOM 4073 C CD  . LYS C 1 107 ? -0.556  33.397  15.396  1.00 51.10  ?  107 LYS C CD  1 
ATOM 4074 C CE  . LYS C 1 107 ? -0.075  34.764  14.957  1.00 59.84  ?  107 LYS C CE  1 
ATOM 4075 N NZ  . LYS C 1 107 ? -1.126  35.494  14.190  1.00 67.42  ?  107 LYS C NZ  1 
ATOM 4076 N N   . VAL C 1 108 ? 3.019   31.168  18.166  1.00 51.55  ?  108 VAL C N   1 
ATOM 4077 C CA  . VAL C 1 108 ? 3.711   31.505  19.409  1.00 57.48  ?  108 VAL C CA  1 
ATOM 4078 C C   . VAL C 1 108 ? 3.675   33.025  19.561  1.00 54.34  ?  108 VAL C C   1 
ATOM 4079 O O   . VAL C 1 108 ? 4.492   33.745  18.981  1.00 52.59  ?  108 VAL C O   1 
ATOM 4080 C CB  . VAL C 1 108 ? 5.145   30.968  19.414  1.00 58.49  ?  108 VAL C CB  1 
ATOM 4081 C CG1 . VAL C 1 108 ? 5.823   31.282  20.734  1.00 57.89  ?  108 VAL C CG1 1 
ATOM 4082 C CG2 . VAL C 1 108 ? 5.161   29.472  19.122  1.00 50.48  ?  108 VAL C CG2 1 
ATOM 4083 N N   . GLU C 1 109 ? 2.760   33.504  20.399  1.00 53.06  ?  109 GLU C N   1 
ATOM 4084 C CA  . GLU C 1 109 ? 2.550   34.920  20.672  1.00 58.59  ?  109 GLU C CA  1 
ATOM 4085 C C   . GLU C 1 109 ? 3.577   35.451  21.681  1.00 60.17  ?  109 GLU C C   1 
ATOM 4086 O O   . GLU C 1 109 ? 4.452   34.726  22.163  1.00 65.36  ?  109 GLU C O   1 
ATOM 4087 C CB  . GLU C 1 109 ? 1.122   35.139  21.174  1.00 60.92  ?  109 GLU C CB  1 
ATOM 4088 C CG  . GLU C 1 109 ? 0.013   34.499  20.317  1.00 55.20  ?  109 GLU C CG  1 
ATOM 4089 C CD  . GLU C 1 109 ? -0.377  35.331  19.098  1.00 65.47  ?  109 GLU C CD  1 
ATOM 4090 O OE1 . GLU C 1 109 ? 0.269   36.371  18.837  1.00 64.43  ?  109 GLU C OE1 1 
ATOM 4091 O OE2 . GLU C 1 109 ? -1.353  34.958  18.410  1.00 70.06  ?  109 GLU C OE2 1 
ATOM 4092 N N   . ILE C 1 110 ? 3.472   36.741  22.006  1.00 58.92  ?  110 ILE C N   1 
ATOM 4093 C CA  . ILE C 1 110 ? 4.393   37.414  22.920  1.00 64.98  ?  110 ILE C CA  1 
ATOM 4094 C C   . ILE C 1 110 ? 3.596   37.867  24.135  1.00 61.06  ?  110 ILE C C   1 
ATOM 4095 O O   . ILE C 1 110 ? 2.539   38.492  23.995  1.00 59.72  ?  110 ILE C O   1 
ATOM 4096 C CB  . ILE C 1 110 ? 5.095   38.621  22.274  1.00 60.90  ?  110 ILE C CB  1 
ATOM 4097 C CG1 . ILE C 1 110 ? 5.951   38.193  21.089  1.00 63.04  ?  110 ILE C CG1 1 
ATOM 4098 C CG2 . ILE C 1 110 ? 5.985   39.312  23.294  1.00 49.54  ?  110 ILE C CG2 1 
ATOM 4099 C CD1 . ILE C 1 110 ? 6.676   39.362  20.430  1.00 61.74  ?  110 ILE C CD1 1 
ATOM 4100 N N   . LYS C 1 111 ? 4.102   37.552  25.321  1.00 59.95  ?  111 LYS C N   1 
ATOM 4101 C CA  . LYS C 1 111 ? 3.414   37.882  26.557  1.00 64.40  ?  111 LYS C CA  1 
ATOM 4102 C C   . LYS C 1 111 ? 3.764   39.302  26.976  1.00 60.19  ?  111 LYS C C   1 
ATOM 4103 O O   . LYS C 1 111 ? 4.936   39.694  26.956  1.00 56.12  ?  111 LYS C O   1 
ATOM 4104 C CB  . LYS C 1 111 ? 3.792   36.890  27.660  1.00 67.72  ?  111 LYS C CB  1 
ATOM 4105 C CG  . LYS C 1 111 ? 3.083   37.110  28.993  1.00 67.67  ?  111 LYS C CG  1 
ATOM 4106 C CD  . LYS C 1 111 ? 1.767   36.341  29.073  1.00 77.09  ?  111 LYS C CD  1 
ATOM 4107 C CE  . LYS C 1 111 ? 1.166   36.435  30.475  1.00 89.07  ?  111 LYS C CE  1 
ATOM 4108 N NZ  . LYS C 1 111 ? -0.084  35.637  30.658  1.00 84.07  ?  111 LYS C NZ  1 
ATOM 4109 N N   . ARG C 1 112 ? 2.739   40.088  27.290  1.00 55.30  ?  112 ARG C N   1 
ATOM 4110 C CA  . ARG C 1 112 ? 2.933   41.432  27.806  1.00 55.20  ?  112 ARG C CA  1 
ATOM 4111 C C   . ARG C 1 112 ? 1.797   41.724  28.776  1.00 51.75  ?  112 ARG C C   1 
ATOM 4112 O O   . ARG C 1 112 ? 0.883   40.914  28.951  1.00 57.55  ?  112 ARG C O   1 
ATOM 4113 C CB  . ARG C 1 112 ? 2.986   42.455  26.671  1.00 65.76  ?  112 ARG C CB  1 
ATOM 4114 C CG  . ARG C 1 112 ? 1.662   42.646  25.961  1.00 58.84  ?  112 ARG C CG  1 
ATOM 4115 C CD  . ARG C 1 112 ? 1.679   43.915  25.149  1.00 56.95  ?  112 ARG C CD  1 
ATOM 4116 N NE  . ARG C 1 112 ? 1.963   45.114  25.939  1.00 58.80  ?  112 ARG C NE  1 
ATOM 4117 C CZ  . ARG C 1 112 ? 1.072   45.759  26.685  1.00 54.55  ?  112 ARG C CZ  1 
ATOM 4118 N NH1 . ARG C 1 112 ? 1.427   46.844  27.358  1.00 51.07  ?  112 ARG C NH1 1 
ATOM 4119 N NH2 . ARG C 1 112 ? -0.171  45.310  26.769  1.00 61.18  ?  112 ARG C NH2 1 
ATOM 4120 N N   . THR C 1 113 ? 1.828   42.909  29.371  1.00 55.46  ?  113 THR C N   1 
ATOM 4121 C CA  . THR C 1 113 ? 0.804   43.240  30.349  1.00 65.14  ?  113 THR C CA  1 
ATOM 4122 C C   . THR C 1 113 ? -0.523  43.551  29.659  1.00 60.73  ?  113 THR C C   1 
ATOM 4123 O O   . THR C 1 113 ? -0.575  43.923  28.484  1.00 56.33  ?  113 THR C O   1 
ATOM 4124 C CB  . THR C 1 113 ? 1.241   44.419  31.228  1.00 62.30  ?  113 THR C CB  1 
ATOM 4125 O OG1 . THR C 1 113 ? 1.422   45.590  30.419  1.00 66.07  ?  113 THR C OG1 1 
ATOM 4126 C CG2 . THR C 1 113 ? 2.543   44.098  31.946  1.00 55.57  ?  113 THR C CG2 1 
ATOM 4127 N N   . VAL C 1 114 ? -1.609  43.373  30.413  1.00 60.45  ?  114 VAL C N   1 
ATOM 4128 C CA  . VAL C 1 114 ? -2.942  43.665  29.903  1.00 54.78  ?  114 VAL C CA  1 
ATOM 4129 C C   . VAL C 1 114 ? -3.056  45.160  29.645  1.00 53.34  ?  114 VAL C C   1 
ATOM 4130 O O   . VAL C 1 114 ? -2.620  45.980  30.463  1.00 60.06  ?  114 VAL C O   1 
ATOM 4131 C CB  . VAL C 1 114 ? -4.009  43.174  30.893  1.00 53.65  ?  114 VAL C CB  1 
ATOM 4132 C CG1 . VAL C 1 114 ? -5.411  43.468  30.377  1.00 51.53  ?  114 VAL C CG1 1 
ATOM 4133 C CG2 . VAL C 1 114 ? -3.840  41.678  31.155  1.00 43.85  ?  114 VAL C CG2 1 
ATOM 4134 N N   . ALA C 1 115 ? -3.619  45.522  28.489  1.00 56.48  ?  115 ALA C N   1 
ATOM 4135 C CA  . ALA C 1 115 ? -3.808  46.915  28.099  1.00 52.54  ?  115 ALA C CA  1 
ATOM 4136 C C   . ALA C 1 115 ? -5.204  47.119  27.532  1.00 51.94  ?  115 ALA C C   1 
ATOM 4137 O O   . ALA C 1 115 ? -5.682  46.308  26.736  1.00 58.34  ?  115 ALA C O   1 
ATOM 4138 C CB  . ALA C 1 115 ? -2.772  47.361  27.056  1.00 43.24  ?  115 ALA C CB  1 
ATOM 4139 N N   . ALA C 1 116 ? -5.858  48.199  27.954  1.00 53.43  ?  116 ALA C N   1 
ATOM 4140 C CA  . ALA C 1 116 ? -7.188  48.500  27.450  1.00 51.29  ?  116 ALA C CA  1 
ATOM 4141 C C   . ALA C 1 116 ? -7.083  49.197  26.094  1.00 53.57  ?  116 ALA C C   1 
ATOM 4142 O O   . ALA C 1 116 ? -6.134  49.946  25.844  1.00 51.93  ?  116 ALA C O   1 
ATOM 4143 C CB  . ALA C 1 116 ? -7.953  49.381  28.428  1.00 45.53  ?  116 ALA C CB  1 
ATOM 4144 N N   . PRO C 1 117 ? -8.032  48.957  25.194  1.00 55.54  ?  117 PRO C N   1 
ATOM 4145 C CA  . PRO C 1 117 ? -7.958  49.584  23.876  1.00 50.91  ?  117 PRO C CA  1 
ATOM 4146 C C   . PRO C 1 117 ? -8.401  51.034  23.914  1.00 53.93  ?  117 PRO C C   1 
ATOM 4147 O O   . PRO C 1 117 ? -9.227  51.442  24.733  1.00 53.25  ?  117 PRO C O   1 
ATOM 4148 C CB  . PRO C 1 117 ? -8.937  48.753  23.042  1.00 48.32  ?  117 PRO C CB  1 
ATOM 4149 C CG  . PRO C 1 117 ? -9.960  48.324  24.029  1.00 49.03  ?  117 PRO C CG  1 
ATOM 4150 C CD  . PRO C 1 117 ? -9.215  48.086  25.322  1.00 54.15  ?  117 PRO C CD  1 
ATOM 4151 N N   . SER C 1 118 ? -7.859  51.807  22.979  1.00 55.40  ?  118 SER C N   1 
ATOM 4152 C CA  . SER C 1 118 ? -8.411  53.114  22.656  1.00 50.03  ?  118 SER C CA  1 
ATOM 4153 C C   . SER C 1 118 ? -9.468  52.884  21.582  1.00 53.83  ?  118 SER C C   1 
ATOM 4154 O O   . SER C 1 118 ? -9.166  52.302  20.537  1.00 52.04  ?  118 SER C O   1 
ATOM 4155 C CB  . SER C 1 118 ? -7.316  54.055  22.158  1.00 54.25  ?  118 SER C CB  1 
ATOM 4156 O OG  . SER C 1 118 ? -6.198  54.039  23.031  1.00 56.81  ?  118 SER C OG  1 
ATOM 4157 N N   . VAL C 1 119 ? -10.707 53.285  21.849  1.00 51.26  ?  119 VAL C N   1 
ATOM 4158 C CA  . VAL C 1 119 ? -11.831 52.969  20.971  1.00 45.99  ?  119 VAL C CA  1 
ATOM 4159 C C   . VAL C 1 119 ? -12.233 54.227  20.214  1.00 48.92  ?  119 VAL C C   1 
ATOM 4160 O O   . VAL C 1 119 ? -12.568 55.249  20.825  1.00 52.80  ?  119 VAL C O   1 
ATOM 4161 C CB  . VAL C 1 119 ? -13.025 52.398  21.747  1.00 45.01  ?  119 VAL C CB  1 
ATOM 4162 C CG1 . VAL C 1 119 ? -14.189 52.175  20.806  1.00 44.77  ?  119 VAL C CG1 1 
ATOM 4163 C CG2 . VAL C 1 119 ? -12.642 51.096  22.430  1.00 46.08  ?  119 VAL C CG2 1 
ATOM 4164 N N   . PHE C 1 120 ? -12.211 54.143  18.885  1.00 52.10  ?  120 PHE C N   1 
ATOM 4165 C CA  . PHE C 1 120 ? -12.688 55.204  18.010  1.00 46.96  ?  120 PHE C CA  1 
ATOM 4166 C C   . PHE C 1 120 ? -13.855 54.701  17.171  1.00 45.92  ?  120 PHE C C   1 
ATOM 4167 O O   . PHE C 1 120 ? -13.966 53.512  16.871  1.00 48.32  ?  120 PHE C O   1 
ATOM 4168 C CB  . PHE C 1 120 ? -11.583 55.697  17.073  1.00 43.16  ?  120 PHE C CB  1 
ATOM 4169 C CG  . PHE C 1 120 ? -10.357 56.187  17.776  1.00 50.95  ?  120 PHE C CG  1 
ATOM 4170 C CD1 . PHE C 1 120 ? -10.250 57.513  18.173  1.00 53.02  ?  120 PHE C CD1 1 
ATOM 4171 C CD2 . PHE C 1 120 ? -9.303  55.326  18.035  1.00 50.58  ?  120 PHE C CD2 1 
ATOM 4172 C CE1 . PHE C 1 120 ? -9.116  57.974  18.811  1.00 46.56  ?  120 PHE C CE1 1 
ATOM 4173 C CE2 . PHE C 1 120 ? -8.163  55.777  18.671  1.00 53.83  ?  120 PHE C CE2 1 
ATOM 4174 C CZ  . PHE C 1 120 ? -8.069  57.105  19.060  1.00 52.76  ?  120 PHE C CZ  1 
ATOM 4175 N N   . ILE C 1 121 ? -14.702 55.629  16.736  1.00 54.15  ?  121 ILE C N   1 
ATOM 4176 C CA  . ILE C 1 121 ? -15.823 55.307  15.863  1.00 52.71  ?  121 ILE C CA  1 
ATOM 4177 C C   . ILE C 1 121 ? -15.820 56.302  14.710  1.00 49.07  ?  121 ILE C C   1 
ATOM 4178 O O   . ILE C 1 121 ? -15.691 57.513  14.922  1.00 55.70  ?  121 ILE C O   1 
ATOM 4179 C CB  . ILE C 1 121 ? -17.174 55.316  16.612  1.00 50.55  ?  121 ILE C CB  1 
ATOM 4180 C CG1 . ILE C 1 121 ? -18.315 54.906  15.677  1.00 56.44  ?  121 ILE C CG1 1 
ATOM 4181 C CG2 . ILE C 1 121 ? -17.462 56.676  17.226  1.00 48.79  ?  121 ILE C CG2 1 
ATOM 4182 C CD1 . ILE C 1 121 ? -19.593 54.533  16.407  1.00 52.56  ?  121 ILE C CD1 1 
ATOM 4183 N N   . PHE C 1 122 ? -15.927 55.784  13.490  1.00 53.02  ?  122 PHE C N   1 
ATOM 4184 C CA  . PHE C 1 122 ? -15.914 56.586  12.278  1.00 51.91  ?  122 PHE C CA  1 
ATOM 4185 C C   . PHE C 1 122 ? -17.246 56.427  11.559  1.00 54.37  ?  122 PHE C C   1 
ATOM 4186 O O   . PHE C 1 122 ? -17.595 55.302  11.150  1.00 54.30  ?  122 PHE C O   1 
ATOM 4187 C CB  . PHE C 1 122 ? -14.766 56.169  11.357  1.00 51.72  ?  122 PHE C CB  1 
ATOM 4188 C CG  . PHE C 1 122 ? -13.403 56.301  11.975  1.00 52.30  ?  122 PHE C CG  1 
ATOM 4189 C CD1 . PHE C 1 122 ? -12.738 57.516  11.963  1.00 47.89  ?  122 PHE C CD1 1 
ATOM 4190 C CD2 . PHE C 1 122 ? -12.774 55.203  12.540  1.00 48.66  ?  122 PHE C CD2 1 
ATOM 4191 C CE1 . PHE C 1 122 ? -11.475 57.636  12.521  1.00 51.07  ?  122 PHE C CE1 1 
ATOM 4192 C CE2 . PHE C 1 122 ? -11.510 55.318  13.100  1.00 47.16  ?  122 PHE C CE2 1 
ATOM 4193 C CZ  . PHE C 1 122 ? -10.861 56.535  13.093  1.00 47.25  ?  122 PHE C CZ  1 
ATOM 4194 N N   . PRO C 1 123 ? -18.012 57.502  11.397  1.00 58.17  ?  123 PRO C N   1 
ATOM 4195 C CA  . PRO C 1 123 ? -19.223 57.448  10.569  1.00 55.17  ?  123 PRO C CA  1 
ATOM 4196 C C   . PRO C 1 123 ? -18.861 57.287  9.107   1.00 52.81  ?  123 PRO C C   1 
ATOM 4197 O O   . PRO C 1 123 ? -17.711 57.540  8.717   1.00 53.83  ?  123 PRO C O   1 
ATOM 4198 C CB  . PRO C 1 123 ? -19.889 58.811  10.826  1.00 56.74  ?  123 PRO C CB  1 
ATOM 4199 C CG  . PRO C 1 123 ? -19.253 59.330  12.086  1.00 54.40  ?  123 PRO C CG  1 
ATOM 4200 C CD  . PRO C 1 123 ? -17.858 58.797  12.077  1.00 53.55  ?  123 PRO C CD  1 
ATOM 4201 N N   . PRO C 1 124 ? -19.807 56.871  8.266   1.00 54.71  ?  124 PRO C N   1 
ATOM 4202 C CA  . PRO C 1 124 ? -19.529 56.809  6.827   1.00 54.25  ?  124 PRO C CA  1 
ATOM 4203 C C   . PRO C 1 124 ? -19.410 58.201  6.229   1.00 52.98  ?  124 PRO C C   1 
ATOM 4204 O O   . PRO C 1 124 ? -20.102 59.136  6.639   1.00 56.89  ?  124 PRO C O   1 
ATOM 4205 C CB  . PRO C 1 124 ? -20.740 56.059  6.263   1.00 53.77  ?  124 PRO C CB  1 
ATOM 4206 C CG  . PRO C 1 124 ? -21.823 56.320  7.245   1.00 56.71  ?  124 PRO C CG  1 
ATOM 4207 C CD  . PRO C 1 124 ? -21.158 56.383  8.588   1.00 55.00  ?  124 PRO C CD  1 
ATOM 4208 N N   . SER C 1 125 ? -18.514 58.333  5.259   1.00 55.40  ?  125 SER C N   1 
ATOM 4209 C CA  . SER C 1 125 ? -18.327 59.607  4.586   1.00 57.60  ?  125 SER C CA  1 
ATOM 4210 C C   . SER C 1 125 ? -19.469 59.865  3.612   1.00 58.66  ?  125 SER C C   1 
ATOM 4211 O O   . SER C 1 125 ? -20.233 58.964  3.255   1.00 59.44  ?  125 SER C O   1 
ATOM 4212 C CB  . SER C 1 125 ? -16.998 59.636  3.833   1.00 53.45  ?  125 SER C CB  1 
ATOM 4213 O OG  . SER C 1 125 ? -16.921 58.566  2.903   1.00 54.04  ?  125 SER C OG  1 
ATOM 4214 N N   . ASP C 1 126 ? -19.598 61.130  3.206   1.00 61.58  ?  126 ASP C N   1 
ATOM 4215 C CA  . ASP C 1 126 ? -20.574 61.474  2.177   1.00 60.70  ?  126 ASP C CA  1 
ATOM 4216 C C   . ASP C 1 126 ? -20.183 60.887  0.831   1.00 61.19  ?  126 ASP C C   1 
ATOM 4217 O O   . ASP C 1 126 ? -21.056 60.507  0.036   1.00 62.43  ?  126 ASP C O   1 
ATOM 4218 C CB  . ASP C 1 126 ? -20.723 62.989  2.080   1.00 61.22  ?  126 ASP C CB  1 
ATOM 4219 C CG  . ASP C 1 126 ? -20.974 63.628  3.426   1.00 75.02  ?  126 ASP C CG  1 
ATOM 4220 O OD1 . ASP C 1 126 ? -20.004 63.795  4.201   1.00 80.55  ?  126 ASP C OD1 1 
ATOM 4221 O OD2 . ASP C 1 126 ? -22.148 63.946  3.711   1.00 75.45  ?  126 ASP C OD2 1 
ATOM 4222 N N   . GLU C 1 127 ? -18.880 60.800  0.567   1.00 58.98  ?  127 GLU C N   1 
ATOM 4223 C CA  . GLU C 1 127 ? -18.414 60.201  -0.676  1.00 57.97  ?  127 GLU C CA  1 
ATOM 4224 C C   . GLU C 1 127 ? -18.934 58.778  -0.827  1.00 57.71  ?  127 GLU C C   1 
ATOM 4225 O O   . GLU C 1 127 ? -19.315 58.362  -1.928  1.00 60.26  ?  127 GLU C O   1 
ATOM 4226 C CB  . GLU C 1 127 ? -16.888 60.230  -0.711  1.00 59.46  ?  127 GLU C CB  1 
ATOM 4227 C CG  . GLU C 1 127 ? -16.278 59.734  -2.005  1.00 71.36  ?  127 GLU C CG  1 
ATOM 4228 C CD  . GLU C 1 127 ? -14.768 59.892  -2.028  1.00 78.08  ?  127 GLU C CD  1 
ATOM 4229 O OE1 . GLU C 1 127 ? -14.231 60.601  -1.139  1.00 70.70  ?  127 GLU C OE1 1 
ATOM 4230 O OE2 . GLU C 1 127 ? -14.130 59.316  -2.941  1.00 72.40  ?  127 GLU C OE2 1 
ATOM 4231 N N   . GLN C 1 128 ? -19.004 58.031  0.278   1.00 62.55  ?  128 GLN C N   1 
ATOM 4232 C CA  . GLN C 1 128 ? -19.548 56.679  0.225   1.00 59.89  ?  128 GLN C CA  1 
ATOM 4233 C C   . GLN C 1 128 ? -21.069 56.681  0.201   1.00 60.03  ?  128 GLN C C   1 
ATOM 4234 O O   . GLN C 1 128 ? -21.677 55.800  -0.416  1.00 60.76  ?  128 GLN C O   1 
ATOM 4235 C CB  . GLN C 1 128 ? -19.053 55.858  1.412   1.00 49.65  ?  128 GLN C CB  1 
ATOM 4236 C CG  . GLN C 1 128 ? -19.417 54.394  1.332   1.00 49.14  ?  128 GLN C CG  1 
ATOM 4237 C CD  . GLN C 1 128 ? -19.276 53.674  2.661   1.00 53.87  ?  128 GLN C CD  1 
ATOM 4238 O OE1 . GLN C 1 128 ? -19.591 52.491  2.767   1.00 56.81  ?  128 GLN C OE1 1 
ATOM 4239 N NE2 . GLN C 1 128 ? -18.803 54.387  3.686   1.00 52.37  ?  128 GLN C NE2 1 
ATOM 4240 N N   . LEU C 1 129 ? -21.698 57.663  0.847   1.00 58.91  ?  129 LEU C N   1 
ATOM 4241 C CA  . LEU C 1 129 ? -23.151 57.754  0.804   1.00 60.86  ?  129 LEU C CA  1 
ATOM 4242 C C   . LEU C 1 129 ? -23.655 58.036  -0.605  1.00 66.41  ?  129 LEU C C   1 
ATOM 4243 O O   . LEU C 1 129 ? -24.790 57.671  -0.939  1.00 64.58  ?  129 LEU C O   1 
ATOM 4244 C CB  . LEU C 1 129 ? -23.634 58.837  1.762   1.00 60.23  ?  129 LEU C CB  1 
ATOM 4245 C CG  . LEU C 1 129 ? -23.563 58.447  3.232   1.00 59.86  ?  129 LEU C CG  1 
ATOM 4246 C CD1 . LEU C 1 129 ? -23.918 59.625  4.125   1.00 56.82  ?  129 LEU C CD1 1 
ATOM 4247 C CD2 . LEU C 1 129 ? -24.496 57.276  3.472   1.00 62.98  ?  129 LEU C CD2 1 
ATOM 4248 N N   . LYS C 1 130 ? -22.829 58.674  -1.443  1.00 67.67  ?  130 LYS C N   1 
ATOM 4249 C CA  . LYS C 1 130 ? -23.227 58.945  -2.823  1.00 65.10  ?  130 LYS C CA  1 
ATOM 4250 C C   . LYS C 1 130 ? -23.528 57.676  -3.613  1.00 68.93  ?  130 LYS C C   1 
ATOM 4251 O O   . LYS C 1 130 ? -24.220 57.749  -4.635  1.00 72.00  ?  130 LYS C O   1 
ATOM 4252 C CB  . LYS C 1 130 ? -22.130 59.723  -3.559  1.00 65.40  ?  130 LYS C CB  1 
ATOM 4253 C CG  . LYS C 1 130 ? -22.008 61.199  -3.221  1.00 64.16  ?  130 LYS C CG  1 
ATOM 4254 C CD  . LYS C 1 130 ? -20.959 61.859  -4.120  1.00 61.53  ?  130 LYS C CD  1 
ATOM 4255 C CE  . LYS C 1 130 ? -20.852 63.365  -3.871  1.00 72.98  ?  130 LYS C CE  1 
ATOM 4256 N NZ  . LYS C 1 130 ? -20.473 63.684  -2.452  1.00 81.45  ?  130 LYS C NZ  1 
ATOM 4257 N N   . SER C 1 131 ? -23.036 56.519  -3.168  1.00 67.14  ?  131 SER C N   1 
ATOM 4258 C CA  . SER C 1 131 ? -23.184 55.268  -3.903  1.00 58.02  ?  131 SER C CA  1 
ATOM 4259 C C   . SER C 1 131 ? -24.206 54.325  -3.279  1.00 65.11  ?  131 SER C C   1 
ATOM 4260 O O   . SER C 1 131 ? -24.275 53.155  -3.670  1.00 71.37  ?  131 SER C O   1 
ATOM 4261 C CB  . SER C 1 131 ? -21.831 54.565  -4.029  1.00 61.67  ?  131 SER C CB  1 
ATOM 4262 O OG  . SER C 1 131 ? -21.306 54.222  -2.758  1.00 65.54  ?  131 SER C OG  1 
ATOM 4263 N N   . GLY C 1 132 ? -24.983 54.788  -2.303  1.00 65.18  ?  132 GLY C N   1 
ATOM 4264 C CA  . GLY C 1 132 ? -26.025 53.948  -1.750  1.00 61.31  ?  132 GLY C CA  1 
ATOM 4265 C C   . GLY C 1 132 ? -25.564 52.885  -0.782  1.00 65.09  ?  132 GLY C C   1 
ATOM 4266 O O   . GLY C 1 132 ? -26.232 51.854  -0.654  1.00 69.71  ?  132 GLY C O   1 
ATOM 4267 N N   . THR C 1 133 ? -24.427 53.085  -0.117  1.00 64.99  ?  133 THR C N   1 
ATOM 4268 C CA  . THR C 1 133 ? -23.938 52.161  0.900   1.00 64.26  ?  133 THR C CA  1 
ATOM 4269 C C   . THR C 1 133 ? -23.196 52.954  1.968   1.00 62.94  ?  133 THR C C   1 
ATOM 4270 O O   . THR C 1 133 ? -22.512 53.933  1.658   1.00 61.57  ?  133 THR C O   1 
ATOM 4271 C CB  . THR C 1 133 ? -23.026 51.084  0.291   1.00 59.89  ?  133 THR C CB  1 
ATOM 4272 O OG1 . THR C 1 133 ? -23.754 50.355  -0.704  1.00 69.84  ?  133 THR C OG1 1 
ATOM 4273 C CG2 . THR C 1 133 ? -22.539 50.112  1.347   1.00 52.61  ?  133 THR C CG2 1 
ATOM 4274 N N   . ALA C 1 134 ? -23.347 52.539  3.226   1.00 65.15  ?  134 ALA C N   1 
ATOM 4275 C CA  . ALA C 1 134 ? -22.733 53.218  4.364   1.00 63.58  ?  134 ALA C CA  1 
ATOM 4276 C C   . ALA C 1 134 ? -21.976 52.202  5.206   1.00 55.39  ?  134 ALA C C   1 
ATOM 4277 O O   . ALA C 1 134 ? -22.560 51.215  5.665   1.00 57.81  ?  134 ALA C O   1 
ATOM 4278 C CB  . ALA C 1 134 ? -23.782 53.935  5.218   1.00 62.24  ?  134 ALA C CB  1 
ATOM 4279 N N   . SER C 1 135 ? -20.683 52.449  5.408   1.00 51.29  ?  135 SER C N   1 
ATOM 4280 C CA  . SER C 1 135 ? -19.834 51.631  6.264   1.00 48.58  ?  135 SER C CA  1 
ATOM 4281 C C   . SER C 1 135 ? -19.413 52.461  7.469   1.00 49.52  ?  135 SER C C   1 
ATOM 4282 O O   . SER C 1 135 ? -18.722 53.477  7.325   1.00 48.90  ?  135 SER C O   1 
ATOM 4283 C CB  . SER C 1 135 ? -18.601 51.127  5.514   1.00 43.29  ?  135 SER C CB  1 
ATOM 4284 O OG  . SER C 1 135 ? -18.963 50.270  4.448   1.00 52.10  ?  135 SER C OG  1 
ATOM 4285 N N   . VAL C 1 136 ? -19.840 52.039  8.651   1.00 47.49  ?  136 VAL C N   1 
ATOM 4286 C CA  . VAL C 1 136 ? -19.420 52.669  9.896   1.00 50.21  ?  136 VAL C CA  1 
ATOM 4287 C C   . VAL C 1 136 ? -18.397 51.759  10.561  1.00 45.60  ?  136 VAL C C   1 
ATOM 4288 O O   . VAL C 1 136 ? -18.606 50.542  10.653  1.00 51.13  ?  136 VAL C O   1 
ATOM 4289 C CB  . VAL C 1 136 ? -20.628 52.961  10.804  1.00 49.31  ?  136 VAL C CB  1 
ATOM 4290 C CG1 . VAL C 1 136 ? -21.584 51.784  10.823  1.00 53.36  ?  136 VAL C CG1 1 
ATOM 4291 C CG2 . VAL C 1 136 ? -20.182 53.354  12.205  1.00 45.88  ?  136 VAL C CG2 1 
ATOM 4292 N N   . VAL C 1 137 ? -17.280 52.334  11.008  1.00 46.89  ?  137 VAL C N   1 
ATOM 4293 C CA  . VAL C 1 137 ? -16.126 51.552  11.449  1.00 48.59  ?  137 VAL C CA  1 
ATOM 4294 C C   . VAL C 1 137 ? -15.861 51.794  12.932  1.00 51.75  ?  137 VAL C C   1 
ATOM 4295 O O   . VAL C 1 137 ? -15.861 52.939  13.395  1.00 50.13  ?  137 VAL C O   1 
ATOM 4296 C CB  . VAL C 1 137 ? -14.873 51.884  10.619  1.00 47.02  ?  137 VAL C CB  1 
ATOM 4297 C CG1 . VAL C 1 137 ? -13.718 50.976  11.020  1.00 46.38  ?  137 VAL C CG1 1 
ATOM 4298 C CG2 . VAL C 1 137 ? -15.172 51.760  9.134   1.00 46.27  ?  137 VAL C CG2 1 
ATOM 4299 N N   . CYS C 1 138 ? -15.640 50.712  13.672  1.00 57.93  ?  138 CYS C N   1 
ATOM 4300 C CA  . CYS C 1 138 ? -15.282 50.748  15.085  1.00 56.44  ?  138 CYS C CA  1 
ATOM 4301 C C   . CYS C 1 138 ? -13.851 50.243  15.217  1.00 52.03  ?  138 CYS C C   1 
ATOM 4302 O O   . CYS C 1 138 ? -13.565 49.093  14.870  1.00 51.49  ?  138 CYS C O   1 
ATOM 4303 C CB  . CYS C 1 138 ? -16.243 49.880  15.901  1.00 54.12  ?  138 CYS C CB  1 
ATOM 4304 S SG  . CYS C 1 138 ? -16.058 49.900  17.704  1.00 58.08  ?  138 CYS C SG  1 
ATOM 4305 N N   . LEU C 1 139 ? -12.961 51.098  15.708  1.00 52.69  ?  139 LEU C N   1 
ATOM 4306 C CA  . LEU C 1 139 ? -11.543 50.789  15.832  1.00 53.48  ?  139 LEU C CA  1 
ATOM 4307 C C   . LEU C 1 139 ? -11.169 50.598  17.297  1.00 48.43  ?  139 LEU C C   1 
ATOM 4308 O O   . LEU C 1 139 ? -11.567 51.390  18.156  1.00 45.58  ?  139 LEU C O   1 
ATOM 4309 C CB  . LEU C 1 139 ? -10.681 51.900  15.221  1.00 50.46  ?  139 LEU C CB  1 
ATOM 4310 C CG  . LEU C 1 139 ? -9.198  51.878  15.610  1.00 49.14  ?  139 LEU C CG  1 
ATOM 4311 C CD1 . LEU C 1 139 ? -8.522  50.610  15.103  1.00 47.23  ?  139 LEU C CD1 1 
ATOM 4312 C CD2 . LEU C 1 139 ? -8.474  53.111  15.103  1.00 42.76  ?  139 LEU C CD2 1 
ATOM 4313 N N   . LEU C 1 140 ? -10.398 49.547  17.568  1.00 46.28  ?  140 LEU C N   1 
ATOM 4314 C CA  . LEU C 1 140 ? -9.854  49.236  18.884  1.00 42.70  ?  140 LEU C CA  1 
ATOM 4315 C C   . LEU C 1 140 ? -8.340  49.206  18.726  1.00 46.46  ?  140 LEU C C   1 
ATOM 4316 O O   . LEU C 1 140 ? -7.797  48.270  18.131  1.00 47.64  ?  140 LEU C O   1 
ATOM 4317 C CB  . LEU C 1 140 ? -10.369 47.891  19.396  1.00 45.08  ?  140 LEU C CB  1 
ATOM 4318 C CG  . LEU C 1 140 ? -11.811 47.654  19.858  1.00 49.29  ?  140 LEU C CG  1 
ATOM 4319 C CD1 . LEU C 1 140 ? -12.830 47.860  18.746  1.00 49.57  ?  140 LEU C CD1 1 
ATOM 4320 C CD2 . LEU C 1 140 ? -11.929 46.247  20.430  1.00 50.19  ?  140 LEU C CD2 1 
ATOM 4321 N N   . ASN C 1 141 ? -7.659  50.213  19.261  1.00 50.43  ?  141 ASN C N   1 
ATOM 4322 C CA  . ASN C 1 141 ? -6.231  50.399  19.041  1.00 54.49  ?  141 ASN C CA  1 
ATOM 4323 C C   . ASN C 1 141 ? -5.446  49.983  20.277  1.00 52.49  ?  141 ASN C C   1 
ATOM 4324 O O   . ASN C 1 141 ? -5.797  50.380  21.397  1.00 56.89  ?  141 ASN C O   1 
ATOM 4325 C CB  . ASN C 1 141 ? -5.927  51.864  18.705  1.00 51.64  ?  141 ASN C CB  1 
ATOM 4326 C CG  . ASN C 1 141 ? -4.743  52.022  17.766  1.00 53.24  ?  141 ASN C CG  1 
ATOM 4327 O OD1 . ASN C 1 141 ? -4.346  51.081  17.080  1.00 58.18  ?  141 ASN C OD1 1 
ATOM 4328 N ND2 . ASN C 1 141 ? -4.165  53.216  17.743  1.00 53.06  ?  141 ASN C ND2 1 
ATOM 4329 N N   . ASN C 1 142 ? -4.393  49.181  20.067  1.00 48.95  ?  142 ASN C N   1 
ATOM 4330 C CA  . ASN C 1 142 ? -3.343  48.940  21.053  1.00 52.77  ?  142 ASN C CA  1 
ATOM 4331 C C   . ASN C 1 142 ? -3.926  48.386  22.359  1.00 57.34  ?  142 ASN C C   1 
ATOM 4332 O O   . ASN C 1 142 ? -3.974  49.056  23.395  1.00 60.98  ?  142 ASN C O   1 
ATOM 4333 C CB  . ASN C 1 142 ? -2.528  50.220  21.282  1.00 62.81  ?  142 ASN C CB  1 
ATOM 4334 C CG  . ASN C 1 142 ? -1.821  50.699  20.016  1.00 60.06  ?  142 ASN C CG  1 
ATOM 4335 O OD1 . ASN C 1 142 ? -2.319  50.505  18.908  1.00 54.80  ?  142 ASN C OD1 1 
ATOM 4336 N ND2 . ASN C 1 142 ? -0.663  51.329  20.178  1.00 60.49  ?  142 ASN C ND2 1 
ATOM 4337 N N   . PHE C 1 143 ? -4.388  47.137  22.276  1.00 53.54  ?  143 PHE C N   1 
ATOM 4338 C CA  . PHE C 1 143 ? -4.902  46.414  23.434  1.00 54.76  ?  143 PHE C CA  1 
ATOM 4339 C C   . PHE C 1 143 ? -4.258  45.034  23.538  1.00 58.07  ?  143 PHE C C   1 
ATOM 4340 O O   . PHE C 1 143 ? -3.617  44.544  22.603  1.00 56.40  ?  143 PHE C O   1 
ATOM 4341 C CB  . PHE C 1 143 ? -6.431  46.282  23.378  1.00 55.25  ?  143 PHE C CB  1 
ATOM 4342 C CG  . PHE C 1 143 ? -6.928  45.441  22.238  1.00 59.11  ?  143 PHE C CG  1 
ATOM 4343 C CD1 . PHE C 1 143 ? -7.313  44.123  22.443  1.00 56.88  ?  143 PHE C CD1 1 
ATOM 4344 C CD2 . PHE C 1 143 ? -7.010  45.967  20.959  1.00 53.96  ?  143 PHE C CD2 1 
ATOM 4345 C CE1 . PHE C 1 143 ? -7.773  43.348  21.393  1.00 54.13  ?  143 PHE C CE1 1 
ATOM 4346 C CE2 . PHE C 1 143 ? -7.466  45.199  19.908  1.00 49.81  ?  143 PHE C CE2 1 
ATOM 4347 C CZ  . PHE C 1 143 ? -7.848  43.887  20.124  1.00 52.53  ?  143 PHE C CZ  1 
ATOM 4348 N N   . TYR C 1 144 ? -4.440  44.407  24.708  1.00 62.07  ?  144 TYR C N   1 
ATOM 4349 C CA  . TYR C 1 144 ? -3.969  43.055  24.995  1.00 58.85  ?  144 TYR C CA  1 
ATOM 4350 C C   . TYR C 1 144 ? -4.756  42.535  26.188  1.00 59.30  ?  144 TYR C C   1 
ATOM 4351 O O   . TYR C 1 144 ? -4.965  43.295  27.144  1.00 54.55  ?  144 TYR C O   1 
ATOM 4352 C CB  . TYR C 1 144 ? -2.466  43.048  25.306  1.00 55.94  ?  144 TYR C CB  1 
ATOM 4353 C CG  . TYR C 1 144 ? -1.860  41.671  25.419  1.00 58.78  ?  144 TYR C CG  1 
ATOM 4354 C CD1 . TYR C 1 144 ? -1.837  40.990  26.629  1.00 59.42  ?  144 TYR C CD1 1 
ATOM 4355 C CD2 . TYR C 1 144 ? -1.291  41.058  24.315  1.00 58.98  ?  144 TYR C CD2 1 
ATOM 4356 C CE1 . TYR C 1 144 ? -1.277  39.728  26.725  1.00 57.10  ?  144 TYR C CE1 1 
ATOM 4357 C CE2 . TYR C 1 144 ? -0.726  39.805  24.406  1.00 58.00  ?  144 TYR C CE2 1 
ATOM 4358 C CZ  . TYR C 1 144 ? -0.722  39.144  25.607  1.00 54.93  ?  144 TYR C CZ  1 
ATOM 4359 O OH  . TYR C 1 144 ? -0.158  37.892  25.679  1.00 63.49  ?  144 TYR C OH  1 
ATOM 4360 N N   . PRO C 1 145 ? -5.179  41.262  26.199  1.00 59.42  ?  145 PRO C N   1 
ATOM 4361 C CA  . PRO C 1 145 ? -4.940  40.231  25.190  1.00 57.23  ?  145 PRO C CA  1 
ATOM 4362 C C   . PRO C 1 145 ? -5.874  40.341  23.980  1.00 56.44  ?  145 PRO C C   1 
ATOM 4363 O O   . PRO C 1 145 ? -6.707  41.244  23.919  1.00 55.23  ?  145 PRO C O   1 
ATOM 4364 C CB  . PRO C 1 145 ? -5.185  38.937  25.966  1.00 47.86  ?  145 PRO C CB  1 
ATOM 4365 C CG  . PRO C 1 145 ? -6.219  39.303  26.947  1.00 49.63  ?  145 PRO C CG  1 
ATOM 4366 C CD  . PRO C 1 145 ? -5.940  40.732  27.343  1.00 56.48  ?  145 PRO C CD  1 
ATOM 4367 N N   . ARG C 1 146 ? -5.729  39.394  23.047  1.00 55.47  ?  146 ARG C N   1 
ATOM 4368 C CA  . ARG C 1 146 ? -6.444  39.421  21.774  1.00 54.36  ?  146 ARG C CA  1 
ATOM 4369 C C   . ARG C 1 146 ? -7.963  39.328  21.921  1.00 57.08  ?  146 ARG C C   1 
ATOM 4370 O O   . ARG C 1 146 ? -8.685  39.798  21.034  1.00 68.94  ?  146 ARG C O   1 
ATOM 4371 C CB  . ARG C 1 146 ? -5.904  38.294  20.884  1.00 60.29  ?  146 ARG C CB  1 
ATOM 4372 C CG  . ARG C 1 146 ? -6.392  38.310  19.442  1.00 66.59  ?  146 ARG C CG  1 
ATOM 4373 C CD  . ARG C 1 146 ? -5.861  37.118  18.652  1.00 64.09  ?  146 ARG C CD  1 
ATOM 4374 N NE  . ARG C 1 146 ? -6.411  37.087  17.300  1.00 71.65  ?  146 ARG C NE  1 
ATOM 4375 C CZ  . ARG C 1 146 ? -7.577  36.538  16.974  1.00 82.62  ?  146 ARG C CZ  1 
ATOM 4376 N NH1 . ARG C 1 146 ? -8.325  35.959  17.906  1.00 91.77  ?  146 ARG C NH1 1 
ATOM 4377 N NH2 . ARG C 1 146 ? -7.996  36.568  15.713  1.00 81.36  ?  146 ARG C NH2 1 
ATOM 4378 N N   . GLU C 1 147 ? -8.468  38.758  23.010  1.00 53.51  ?  147 GLU C N   1 
ATOM 4379 C CA  . GLU C 1 147 ? -9.910  38.609  23.175  1.00 56.93  ?  147 GLU C CA  1 
ATOM 4380 C C   . GLU C 1 147 ? -10.591 39.947  23.436  1.00 59.46  ?  147 GLU C C   1 
ATOM 4381 O O   . GLU C 1 147 ? -10.106 40.774  24.215  1.00 63.88  ?  147 GLU C O   1 
ATOM 4382 C CB  . GLU C 1 147 ? -10.230 37.642  24.317  1.00 64.38  ?  147 GLU C CB  1 
ATOM 4383 C CG  . GLU C 1 147 ? -9.560  36.284  24.224  1.00 73.25  ?  147 GLU C CG  1 
ATOM 4384 C CD  . GLU C 1 147 ? -10.058 35.478  23.032  1.00 92.24  ?  147 GLU C CD  1 
ATOM 4385 O OE1 . GLU C 1 147 ? -11.153 35.796  22.510  1.00 95.65  ?  147 GLU C OE1 1 
ATOM 4386 O OE2 . GLU C 1 147 ? -9.364  34.519  22.625  1.00 95.97  ?  147 GLU C OE2 1 
ATOM 4387 N N   . ALA C 1 148 ? -11.720 40.157  22.757  1.00 52.42  ?  148 ALA C N   1 
ATOM 4388 C CA  . ALA C 1 148 ? -12.533 41.354  22.916  1.00 49.34  ?  148 ALA C CA  1 
ATOM 4389 C C   . ALA C 1 148 ? -13.901 41.133  22.285  1.00 57.50  ?  148 ALA C C   1 
ATOM 4390 O O   . ALA C 1 148 ? -13.993 40.600  21.174  1.00 66.46  ?  148 ALA C O   1 
ATOM 4391 C CB  . ALA C 1 148 ? -11.842 42.567  22.292  1.00 51.61  ?  148 ALA C CB  1 
ATOM 4392 N N   . LYS C 1 149 ? -14.971 41.492  22.993  1.00 58.49  ?  149 LYS C N   1 
ATOM 4393 C CA  . LYS C 1 149 ? -16.336 41.308  22.501  1.00 62.25  ?  149 LYS C CA  1 
ATOM 4394 C C   . LYS C 1 149 ? -16.846 42.642  21.956  1.00 63.99  ?  149 LYS C C   1 
ATOM 4395 O O   . LYS C 1 149 ? -17.134 43.563  22.728  1.00 67.71  ?  149 LYS C O   1 
ATOM 4396 C CB  . LYS C 1 149 ? -17.243 40.774  23.607  1.00 67.42  ?  149 LYS C CB  1 
ATOM 4397 C CG  . LYS C 1 149 ? -18.646 40.398  23.153  1.00 66.10  ?  149 LYS C CG  1 
ATOM 4398 C CD  . LYS C 1 149 ? -19.428 39.791  24.311  1.00 76.57  ?  149 LYS C CD  1 
ATOM 4399 C CE  . LYS C 1 149 ? -20.897 39.603  23.970  1.00 78.88  ?  149 LYS C CE  1 
ATOM 4400 N NZ  . LYS C 1 149 ? -21.707 39.330  25.193  1.00 82.12  ?  149 LYS C NZ  1 
ATOM 4401 N N   . VAL C 1 150 ? -16.931 42.757  20.630  1.00 54.77  ?  150 VAL C N   1 
ATOM 4402 C CA  . VAL C 1 150 ? -17.347 43.990  19.961  1.00 55.62  ?  150 VAL C CA  1 
ATOM 4403 C C   . VAL C 1 150 ? -18.749 43.800  19.394  1.00 55.73  ?  150 VAL C C   1 
ATOM 4404 O O   . VAL C 1 150 ? -18.954 42.983  18.487  1.00 64.95  ?  150 VAL C O   1 
ATOM 4405 C CB  . VAL C 1 150 ? -16.364 44.388  18.851  1.00 52.73  ?  150 VAL C CB  1 
ATOM 4406 C CG1 . VAL C 1 150 ? -16.788 45.702  18.221  1.00 57.51  ?  150 VAL C CG1 1 
ATOM 4407 C CG2 . VAL C 1 150 ? -14.956 44.490  19.404  1.00 57.43  ?  150 VAL C CG2 1 
ATOM 4408 N N   . GLN C 1 151 ? -19.709 44.574  19.902  1.00 57.74  ?  151 GLN C N   1 
ATOM 4409 C CA  . GLN C 1 151 ? -21.090 44.514  19.444  1.00 60.06  ?  151 GLN C CA  1 
ATOM 4410 C C   . GLN C 1 151 ? -21.525 45.875  18.923  1.00 58.41  ?  151 GLN C C   1 
ATOM 4411 O O   . GLN C 1 151 ? -20.986 46.909  19.318  1.00 63.93  ?  151 GLN C O   1 
ATOM 4412 C CB  . GLN C 1 151 ? -22.038 44.077  20.561  1.00 66.68  ?  151 GLN C CB  1 
ATOM 4413 C CG  . GLN C 1 151 ? -21.817 42.671  21.058  1.00 70.09  ?  151 GLN C CG  1 
ATOM 4414 C CD  . GLN C 1 151 ? -22.838 42.287  22.101  1.00 76.27  ?  151 GLN C CD  1 
ATOM 4415 O OE1 . GLN C 1 151 ? -23.871 41.700  21.782  1.00 83.82  ?  151 GLN C OE1 1 
ATOM 4416 N NE2 . GLN C 1 151 ? -22.565 42.631  23.355  1.00 66.69  ?  151 GLN C NE2 1 
ATOM 4417 N N   . TRP C 1 152 ? -22.527 45.868  18.046  1.00 63.45  ?  152 TRP C N   1 
ATOM 4418 C CA  . TRP C 1 152 ? -23.037 47.080  17.416  1.00 64.99  ?  152 TRP C CA  1 
ATOM 4419 C C   . TRP C 1 152 ? -24.473 47.352  17.844  1.00 64.61  ?  152 TRP C C   1 
ATOM 4420 O O   . TRP C 1 152 ? -25.294 46.432  17.915  1.00 66.92  ?  152 TRP C O   1 
ATOM 4421 C CB  . TRP C 1 152 ? -22.990 46.969  15.888  1.00 64.42  ?  152 TRP C CB  1 
ATOM 4422 C CG  . TRP C 1 152 ? -21.637 47.146  15.274  1.00 56.83  ?  152 TRP C CG  1 
ATOM 4423 C CD1 . TRP C 1 152 ? -20.743 46.164  14.961  1.00 61.15  ?  152 TRP C CD1 1 
ATOM 4424 C CD2 . TRP C 1 152 ? -21.028 48.381  14.888  1.00 57.04  ?  152 TRP C CD2 1 
ATOM 4425 N NE1 . TRP C 1 152 ? -19.612 46.712  14.403  1.00 60.44  ?  152 TRP C NE1 1 
ATOM 4426 C CE2 . TRP C 1 152 ? -19.762 48.073  14.349  1.00 58.42  ?  152 TRP C CE2 1 
ATOM 4427 C CE3 . TRP C 1 152 ? -21.427 49.718  14.949  1.00 56.24  ?  152 TRP C CE3 1 
ATOM 4428 C CZ2 . TRP C 1 152 ? -18.896 49.053  13.871  1.00 53.43  ?  152 TRP C CZ2 1 
ATOM 4429 C CZ3 . TRP C 1 152 ? -20.566 50.687  14.479  1.00 55.55  ?  152 TRP C CZ3 1 
ATOM 4430 C CH2 . TRP C 1 152 ? -19.314 50.351  13.946  1.00 53.41  ?  152 TRP C CH2 1 
ATOM 4431 N N   . LYS C 1 153 ? -24.787 48.626  18.077  1.00 62.63  ?  153 LYS C N   1 
ATOM 4432 C CA  . LYS C 1 153 ? -26.139 49.060  18.399  1.00 67.42  ?  153 LYS C CA  1 
ATOM 4433 C C   . LYS C 1 153 ? -26.520 50.235  17.511  1.00 70.30  ?  153 LYS C C   1 
ATOM 4434 O O   . LYS C 1 153 ? -25.728 51.163  17.313  1.00 67.62  ?  153 LYS C O   1 
ATOM 4435 C CB  . LYS C 1 153 ? -26.271 49.465  19.875  1.00 69.00  ?  153 LYS C CB  1 
ATOM 4436 C CG  . LYS C 1 153 ? -26.025 48.342  20.875  1.00 67.86  ?  153 LYS C CG  1 
ATOM 4437 C CD  . LYS C 1 153 ? -26.341 48.804  22.292  1.00 74.60  ?  153 LYS C CD  1 
ATOM 4438 C CE  . LYS C 1 153 ? -25.920 47.781  23.338  1.00 73.73  ?  153 LYS C CE  1 
ATOM 4439 N NZ  . LYS C 1 153 ? -26.000 48.358  24.711  1.00 70.11  ?  153 LYS C NZ  1 
ATOM 4440 N N   . VAL C 1 154 ? -27.737 50.189  16.975  1.00 75.60  ?  154 VAL C N   1 
ATOM 4441 C CA  . VAL C 1 154 ? -28.303 51.295  16.210  1.00 73.29  ?  154 VAL C CA  1 
ATOM 4442 C C   . VAL C 1 154 ? -29.633 51.657  16.857  1.00 77.92  ?  154 VAL C C   1 
ATOM 4443 O O   . VAL C 1 154 ? -30.538 50.816  16.946  1.00 79.16  ?  154 VAL C O   1 
ATOM 4444 C CB  . VAL C 1 154 ? -28.470 50.955  14.714  1.00 71.89  ?  154 VAL C CB  1 
ATOM 4445 C CG1 . VAL C 1 154 ? -27.135 50.568  14.108  1.00 66.53  ?  154 VAL C CG1 1 
ATOM 4446 C CG2 . VAL C 1 154 ? -29.468 49.831  14.487  1.00 73.82  ?  154 VAL C CG2 1 
ATOM 4447 N N   . ASP C 1 155 ? -29.737 52.892  17.348  1.00 79.96  ?  155 ASP C N   1 
ATOM 4448 C CA  . ASP C 1 155 ? -30.872 53.305  18.174  1.00 81.67  ?  155 ASP C CA  1 
ATOM 4449 C C   . ASP C 1 155 ? -31.116 52.299  19.299  1.00 80.25  ?  155 ASP C C   1 
ATOM 4450 O O   . ASP C 1 155 ? -32.250 51.901  19.577  1.00 74.08  ?  155 ASP C O   1 
ATOM 4451 C CB  . ASP C 1 155 ? -32.124 53.509  17.320  1.00 72.40  ?  155 ASP C CB  1 
ATOM 4452 C CG  . ASP C 1 155 ? -32.057 54.779  16.500  1.00 79.10  ?  155 ASP C CG  1 
ATOM 4453 O OD1 . ASP C 1 155 ? -31.316 55.701  16.906  1.00 83.15  ?  155 ASP C OD1 1 
ATOM 4454 O OD2 . ASP C 1 155 ? -32.741 54.862  15.457  1.00 83.66  ?  155 ASP C OD2 1 
ATOM 4455 N N   . ASN C 1 156 ? -30.020 51.865  19.928  1.00 82.08  ?  156 ASN C N   1 
ATOM 4456 C CA  . ASN C 1 156 ? -30.027 50.891  21.026  1.00 86.15  ?  156 ASN C CA  1 
ATOM 4457 C C   . ASN C 1 156 ? -30.653 49.557  20.624  1.00 86.87  ?  156 ASN C C   1 
ATOM 4458 O O   . ASN C 1 156 ? -31.186 48.830  21.467  1.00 88.48  ?  156 ASN C O   1 
ATOM 4459 C CB  . ASN C 1 156 ? -30.716 51.442  22.275  1.00 81.49  ?  156 ASN C CB  1 
ATOM 4460 C CG  . ASN C 1 156 ? -30.279 50.721  23.533  1.00 87.70  ?  156 ASN C CG  1 
ATOM 4461 O OD1 . ASN C 1 156 ? -29.084 50.624  23.824  1.00 84.68  ?  156 ASN C OD1 1 
ATOM 4462 N ND2 . ASN C 1 156 ? -31.243 50.189  24.276  1.00 94.04  ?  156 ASN C ND2 1 
ATOM 4463 N N   . ALA C 1 157 ? -30.598 49.223  19.339  1.00 85.28  ?  157 ALA C N   1 
ATOM 4464 C CA  . ALA C 1 157 ? -31.030 47.926  18.835  1.00 82.36  ?  157 ALA C CA  1 
ATOM 4465 C C   . ALA C 1 157 ? -29.787 47.160  18.407  1.00 81.74  ?  157 ALA C C   1 
ATOM 4466 O O   . ALA C 1 157 ? -29.012 47.650  17.579  1.00 79.67  ?  157 ALA C O   1 
ATOM 4467 C CB  . ALA C 1 157 ? -32.007 48.081  17.669  1.00 81.56  ?  157 ALA C CB  1 
ATOM 4468 N N   . LEU C 1 158 ? -29.591 45.975  18.981  1.00 82.26  ?  158 LEU C N   1 
ATOM 4469 C CA  . LEU C 1 158 ? -28.370 45.221  18.736  1.00 78.46  ?  158 LEU C CA  1 
ATOM 4470 C C   . LEU C 1 158 ? -28.379 44.648  17.320  1.00 75.55  ?  158 LEU C C   1 
ATOM 4471 O O   . LEU C 1 158 ? -29.423 44.262  16.787  1.00 73.99  ?  158 LEU C O   1 
ATOM 4472 C CB  . LEU C 1 158 ? -28.218 44.106  19.773  1.00 78.50  ?  158 LEU C CB  1 
ATOM 4473 C CG  . LEU C 1 158 ? -26.888 43.352  19.848  1.00 79.17  ?  158 LEU C CG  1 
ATOM 4474 C CD1 . LEU C 1 158 ? -25.762 44.299  20.241  1.00 73.21  ?  158 LEU C CD1 1 
ATOM 4475 C CD2 . LEU C 1 158 ? -26.975 42.189  20.824  1.00 71.81  ?  158 LEU C CD2 1 
ATOM 4476 N N   . GLN C 1 159 ? -27.200 44.601  16.708  1.00 74.80  ?  159 GLN C N   1 
ATOM 4477 C CA  . GLN C 1 159 ? -27.050 44.157  15.331  1.00 72.56  ?  159 GLN C CA  1 
ATOM 4478 C C   . GLN C 1 159 ? -26.391 42.784  15.279  1.00 74.91  ?  159 GLN C C   1 
ATOM 4479 O O   . GLN C 1 159 ? -25.534 42.455  16.104  1.00 77.64  ?  159 GLN C O   1 
ATOM 4480 C CB  . GLN C 1 159 ? -26.211 45.158  14.528  1.00 71.28  ?  159 GLN C CB  1 
ATOM 4481 C CG  . GLN C 1 159 ? -26.860 46.516  14.339  1.00 68.53  ?  159 GLN C CG  1 
ATOM 4482 C CD  . GLN C 1 159 ? -28.186 46.433  13.603  1.00 80.84  ?  159 GLN C CD  1 
ATOM 4483 O OE1 . GLN C 1 159 ? -28.327 45.667  12.653  1.00 81.48  ?  159 GLN C OE1 1 
ATOM 4484 N NE2 . GLN C 1 159 ? -29.173 47.209  14.057  1.00 77.23  ?  159 GLN C NE2 1 
ATOM 4485 N N   . SER C 1 160 ? -26.793 41.991  14.285  1.00 73.68  ?  160 SER C N   1 
ATOM 4486 C CA  . SER C 1 160 ? -26.234 40.666  14.060  1.00 73.52  ?  160 SER C CA  1 
ATOM 4487 C C   . SER C 1 160 ? -26.294 40.364  12.572  1.00 71.82  ?  160 SER C C   1 
ATOM 4488 O O   . SER C 1 160 ? -27.217 40.797  11.876  1.00 66.02  ?  160 SER C O   1 
ATOM 4489 C CB  . SER C 1 160 ? -26.995 39.580  14.830  1.00 75.70  ?  160 SER C CB  1 
ATOM 4490 O OG  . SER C 1 160 ? -28.326 39.468  14.352  1.00 70.84  ?  160 SER C OG  1 
ATOM 4491 N N   . GLY C 1 161 ? -25.192 39.878  12.015  1.00 74.19  ?  161 GLY C N   1 
ATOM 4492 C CA  . GLY C 1 161 ? -25.154 39.533  10.579  1.00 74.02  ?  161 GLY C CA  1 
ATOM 4493 C C   . GLY C 1 161 ? -24.945 40.690  9.616   1.00 71.89  ?  161 GLY C C   1 
ATOM 4494 O O   . GLY C 1 161 ? -25.234 40.505  8.433   1.00 68.46  ?  161 GLY C O   1 
ATOM 4495 N N   . ASN C 1 162 ? -24.435 41.825  10.082  1.00 74.06  ?  162 ASN C N   1 
ATOM 4496 C CA  . ASN C 1 162 ? -24.147 42.954  9.170   1.00 60.55  ?  162 ASN C CA  1 
ATOM 4497 C C   . ASN C 1 162 ? -22.815 43.567  9.559   1.00 61.28  ?  162 ASN C C   1 
ATOM 4498 O O   . ASN C 1 162 ? -22.570 44.710  9.185   1.00 60.54  ?  162 ASN C O   1 
ATOM 4499 C CB  . ASN C 1 162 ? -25.267 43.984  9.186   1.00 67.00  ?  162 ASN C CB  1 
ATOM 4500 C CG  . ASN C 1 162 ? -25.611 44.508  10.555  1.00 79.82  ?  162 ASN C CG  1 
ATOM 4501 O OD1 . ASN C 1 162 ? -25.374 43.852  11.563  1.00 83.24  ?  162 ASN C OD1 1 
ATOM 4502 N ND2 . ASN C 1 162 ? -26.167 45.703  10.585  1.00 87.71  ?  162 ASN C ND2 1 
ATOM 4503 N N   . SER C 1 163 ? -21.985 42.801  10.254  1.00 61.05  ?  163 SER C N   1 
ATOM 4504 C CA  . SER C 1 163 ? -20.691 43.329  10.735  1.00 58.24  ?  163 SER C CA  1 
ATOM 4505 C C   . SER C 1 163 ? -19.575 42.369  10.351  1.00 53.63  ?  163 SER C C   1 
ATOM 4506 O O   . SER C 1 163 ? -19.868 41.194  10.150  1.00 50.70  ?  163 SER C O   1 
ATOM 4507 C CB  . SER C 1 163 ? -20.745 43.515  12.213  1.00 59.36  ?  163 SER C CB  1 
ATOM 4508 O OG  . SER C 1 163 ? -19.636 44.269  12.667  1.00 53.77  ?  163 SER C OG  1 
ATOM 4509 N N   . GLN C 1 164 ? -18.354 42.869  10.210  1.00 50.63  ?  164 GLN C N   1 
ATOM 4510 C CA  . GLN C 1 164 ? -17.229 41.958  9.970   1.00 45.96  ?  164 GLN C CA  1 
ATOM 4511 C C   . GLN C 1 164 ? -16.040 42.498  10.750  1.00 45.35  ?  164 GLN C C   1 
ATOM 4512 O O   . GLN C 1 164 ? -15.894 43.711  10.841  1.00 45.20  ?  164 GLN C O   1 
ATOM 4513 C CB  . GLN C 1 164 ? -16.955 41.853  8.478   1.00 50.70  ?  164 GLN C CB  1 
ATOM 4514 C CG  . GLN C 1 164 ? -17.500 40.588  7.838   1.00 52.68  ?  164 GLN C CG  1 
ATOM 4515 C CD  . GLN C 1 164 ? -17.318 40.616  6.342   1.00 60.09  ?  164 GLN C CD  1 
ATOM 4516 O OE1 . GLN C 1 164 ? -17.049 41.659  5.754   1.00 68.34  ?  164 GLN C OE1 1 
ATOM 4517 N NE2 . GLN C 1 164 ? -17.457 39.463  5.712   1.00 46.83  ?  164 GLN C NE2 1 
ATOM 4518 N N   . GLU C 1 165 ? -15.232 41.601  11.293  1.00 52.96  ?  165 GLU C N   1 
ATOM 4519 C CA  . GLU C 1 165 ? -14.112 41.971  12.140  1.00 47.00  ?  165 GLU C CA  1 
ATOM 4520 C C   . GLU C 1 165 ? -12.792 41.576  11.495  1.00 43.58  ?  165 GLU C C   1 
ATOM 4521 O O   . GLU C 1 165 ? -12.722 40.646  10.687  1.00 42.64  ?  165 GLU C O   1 
ATOM 4522 C CB  . GLU C 1 165 ? -14.221 41.329  13.525  1.00 43.42  ?  165 GLU C CB  1 
ATOM 4523 C CG  . GLU C 1 165 ? -15.345 41.877  14.386  1.00 46.72  ?  165 GLU C CG  1 
ATOM 4524 C CD  . GLU C 1 165 ? -15.314 41.304  15.794  1.00 60.44  ?  165 GLU C CD  1 
ATOM 4525 O OE1 . GLU C 1 165 ? -16.067 41.799  16.667  1.00 57.45  ?  165 GLU C OE1 1 
ATOM 4526 O OE2 . GLU C 1 165 ? -14.507 40.375  16.027  1.00 55.07  ?  165 GLU C OE2 1 
ATOM 4527 N N   . SER C 1 166 ? -11.753 42.332  11.825  1.00 46.83  ?  166 SER C N   1 
ATOM 4528 C CA  . SER C 1 166 ? -10.410 42.042  11.347  1.00 49.06  ?  166 SER C CA  1 
ATOM 4529 C C   . SER C 1 166 ? -9.411  42.414  12.436  1.00 53.16  ?  166 SER C C   1 
ATOM 4530 O O   . SER C 1 166 ? -9.538  43.469  13.069  1.00 44.04  ?  166 SER C O   1 
ATOM 4531 C CB  . SER C 1 166 ? -10.105 42.787  10.045  1.00 43.48  ?  166 SER C CB  1 
ATOM 4532 O OG  . SER C 1 166 ? -8.813  42.460  9.568   1.00 46.24  ?  166 SER C OG  1 
ATOM 4533 N N   . VAL C 1 167 ? -8.440  41.532  12.668  1.00 48.37  ?  167 VAL C N   1 
ATOM 4534 C CA  . VAL C 1 167 ? -7.436  41.689  13.713  1.00 43.70  ?  167 VAL C CA  1 
ATOM 4535 C C   . VAL C 1 167 ? -6.072  41.824  13.056  1.00 41.93  ?  167 VAL C C   1 
ATOM 4536 O O   . VAL C 1 167 ? -5.753  41.088  12.115  1.00 47.43  ?  167 VAL C O   1 
ATOM 4537 C CB  . VAL C 1 167 ? -7.442  40.490  14.686  1.00 49.99  ?  167 VAL C CB  1 
ATOM 4538 C CG1 . VAL C 1 167 ? -6.582  40.777  15.902  1.00 48.11  ?  167 VAL C CG1 1 
ATOM 4539 C CG2 . VAL C 1 167 ? -8.860  40.113  15.081  1.00 50.75  ?  167 VAL C CG2 1 
ATOM 4540 N N   . THR C 1 168 ? -5.263  42.750  13.554  1.00 39.29  ?  168 THR C N   1 
ATOM 4541 C CA  . THR C 1 168 ? -3.892  42.835  13.079  1.00 45.81  ?  168 THR C CA  1 
ATOM 4542 C C   . THR C 1 168 ? -3.013  41.796  13.764  1.00 49.52  ?  168 THR C C   1 
ATOM 4543 O O   . THR C 1 168 ? -3.387  41.185  14.767  1.00 53.44  ?  168 THR C O   1 
ATOM 4544 C CB  . THR C 1 168 ? -3.307  44.229  13.312  1.00 51.98  ?  168 THR C CB  1 
ATOM 4545 O OG1 . THR C 1 168 ? -3.331  44.538  14.715  1.00 51.77  ?  168 THR C OG1 1 
ATOM 4546 C CG2 . THR C 1 168 ? -4.079  45.277  12.525  1.00 44.19  ?  168 THR C CG2 1 
ATOM 4547 N N   . GLU C 1 169 ? -1.833  41.585  13.189  1.00 59.86  ?  169 GLU C N   1 
ATOM 4548 C CA  . GLU C 1 169 ? -0.819  40.801  13.870  1.00 53.19  ?  169 GLU C CA  1 
ATOM 4549 C C   . GLU C 1 169 ? -0.253  41.605  15.030  1.00 48.04  ?  169 GLU C C   1 
ATOM 4550 O O   . GLU C 1 169 ? -0.436  42.821  15.124  1.00 49.59  ?  169 GLU C O   1 
ATOM 4551 C CB  . GLU C 1 169 ? 0.298   40.387  12.909  1.00 51.21  ?  169 GLU C CB  1 
ATOM 4552 C CG  . GLU C 1 169 ? -0.199  39.520  11.778  1.00 52.89  ?  169 GLU C CG  1 
ATOM 4553 C CD  . GLU C 1 169 ? -0.865  38.258  12.288  1.00 63.01  ?  169 GLU C CD  1 
ATOM 4554 O OE1 . GLU C 1 169 ? -0.320  37.629  13.223  1.00 66.14  ?  169 GLU C OE1 1 
ATOM 4555 O OE2 . GLU C 1 169 ? -1.954  37.917  11.779  1.00 67.77  ?  169 GLU C OE2 1 
ATOM 4556 N N   . GLN C 1 170 ? 0.430   40.904  15.929  1.00 57.25  ?  170 GLN C N   1 
ATOM 4557 C CA  . GLN C 1 170 ? 0.972   41.535  17.123  1.00 56.07  ?  170 GLN C CA  1 
ATOM 4558 C C   . GLN C 1 170 ? 1.985   42.612  16.738  1.00 56.54  ?  170 GLN C C   1 
ATOM 4559 O O   . GLN C 1 170 ? 2.929   42.357  15.983  1.00 49.90  ?  170 GLN C O   1 
ATOM 4560 C CB  . GLN C 1 170 ? 1.604   40.464  18.012  1.00 54.26  ?  170 GLN C CB  1 
ATOM 4561 C CG  . GLN C 1 170 ? 1.931   40.903  19.421  1.00 63.47  ?  170 GLN C CG  1 
ATOM 4562 C CD  . GLN C 1 170 ? 2.208   39.728  20.349  1.00 61.23  ?  170 GLN C CD  1 
ATOM 4563 O OE1 . GLN C 1 170 ? 2.631   38.658  19.907  1.00 60.44  ?  170 GLN C OE1 1 
ATOM 4564 N NE2 . GLN C 1 170 ? 1.973   39.927  21.643  1.00 53.48  ?  170 GLN C NE2 1 
ATOM 4565 N N   . ASP C 1 171 ? 1.777   43.821  17.263  1.00 58.97  ?  171 ASP C N   1 
ATOM 4566 C CA  . ASP C 1 171 ? 2.591   44.973  16.890  1.00 62.15  ?  171 ASP C CA  1 
ATOM 4567 C C   . ASP C 1 171 ? 4.069   44.725  17.171  1.00 69.21  ?  171 ASP C C   1 
ATOM 4568 O O   . ASP C 1 171 ? 4.439   44.114  18.177  1.00 72.81  ?  171 ASP C O   1 
ATOM 4569 C CB  . ASP C 1 171 ? 2.115   46.222  17.638  1.00 66.61  ?  171 ASP C CB  1 
ATOM 4570 C CG  . ASP C 1 171 ? 2.722   47.509  17.083  1.00 75.06  ?  171 ASP C CG  1 
ATOM 4571 O OD1 . ASP C 1 171 ? 3.927   47.752  17.307  1.00 72.51  ?  171 ASP C OD1 1 
ATOM 4572 O OD2 . ASP C 1 171 ? 1.993   48.280  16.419  1.00 78.48  ?  171 ASP C OD2 1 
ATOM 4573 N N   . SER C 1 172 ? 4.919   45.212  16.266  1.00 75.41  ?  172 SER C N   1 
ATOM 4574 C CA  . SER C 1 172 ? 6.358   45.004  16.366  1.00 77.12  ?  172 SER C CA  1 
ATOM 4575 C C   . SER C 1 172 ? 7.017   45.894  17.411  1.00 74.89  ?  172 SER C C   1 
ATOM 4576 O O   . SER C 1 172 ? 8.210   45.719  17.687  1.00 73.79  ?  172 SER C O   1 
ATOM 4577 C CB  . SER C 1 172 ? 7.015   45.241  15.001  1.00 80.38  ?  172 SER C CB  1 
ATOM 4578 O OG  . SER C 1 172 ? 6.751   46.553  14.529  1.00 80.32  ?  172 SER C OG  1 
ATOM 4579 N N   . LYS C 1 173 ? 6.277   46.831  18.001  1.00 74.19  ?  173 LYS C N   1 
ATOM 4580 C CA  . LYS C 1 173 ? 6.820   47.742  18.999  1.00 75.17  ?  173 LYS C CA  1 
ATOM 4581 C C   . LYS C 1 173 ? 6.333   47.403  20.403  1.00 69.33  ?  173 LYS C C   1 
ATOM 4582 O O   . LYS C 1 173 ? 7.136   47.024  21.260  1.00 72.10  ?  173 LYS C O   1 
ATOM 4583 C CB  . LYS C 1 173 ? 6.462   49.194  18.637  1.00 73.28  ?  173 LYS C CB  1 
ATOM 4584 C CG  . LYS C 1 173 ? 7.046   49.676  17.313  1.00 77.88  ?  173 LYS C CG  1 
ATOM 4585 C CD  . LYS C 1 173 ? 8.561   49.836  17.396  1.00 84.12  ?  173 LYS C CD  1 
ATOM 4586 C CE  . LYS C 1 173 ? 9.141   50.392  16.098  1.00 92.96  ?  173 LYS C CE  1 
ATOM 4587 N NZ  . LYS C 1 173 ? 10.619  50.597  16.185  1.00 88.56  ?  173 LYS C NZ  1 
ATOM 4588 N N   . ASP C 1 174 ? 5.029   47.504  20.659  1.00 64.22  ?  174 ASP C N   1 
ATOM 4589 C CA  . ASP C 1 174 ? 4.474   47.284  21.988  1.00 63.55  ?  174 ASP C CA  1 
ATOM 4590 C C   . ASP C 1 174 ? 3.736   45.954  22.112  1.00 64.99  ?  174 ASP C C   1 
ATOM 4591 O O   . ASP C 1 174 ? 2.961   45.777  23.057  1.00 62.82  ?  174 ASP C O   1 
ATOM 4592 C CB  . ASP C 1 174 ? 3.547   48.441  22.365  1.00 59.82  ?  174 ASP C CB  1 
ATOM 4593 C CG  . ASP C 1 174 ? 2.422   48.624  21.375  1.00 65.83  ?  174 ASP C CG  1 
ATOM 4594 O OD1 . ASP C 1 174 ? 2.559   48.135  20.233  1.00 72.04  ?  174 ASP C OD1 1 
ATOM 4595 O OD2 . ASP C 1 174 ? 1.408   49.265  21.729  1.00 61.07  ?  174 ASP C OD2 1 
ATOM 4596 N N   . SER C 1 175 ? 3.936   45.033  21.168  1.00 64.21  ?  175 SER C N   1 
ATOM 4597 C CA  . SER C 1 175 ? 3.406   43.668  21.252  1.00 59.30  ?  175 SER C CA  1 
ATOM 4598 C C   . SER C 1 175 ? 1.893   43.656  21.460  1.00 57.44  ?  175 SER C C   1 
ATOM 4599 O O   . SER C 1 175 ? 1.345   42.787  22.139  1.00 61.03  ?  175 SER C O   1 
ATOM 4600 C CB  . SER C 1 175 ? 4.106   42.882  22.361  1.00 60.01  ?  175 SER C CB  1 
ATOM 4601 O OG  . SER C 1 175 ? 5.512   42.972  22.233  1.00 63.33  ?  175 SER C OG  1 
ATOM 4602 N N   . THR C 1 176 ? 1.211   44.599  20.838  1.00 63.54  ?  176 THR C N   1 
ATOM 4603 C CA  . THR C 1 176 ? -0.207  44.827  21.057  1.00 63.09  ?  176 THR C CA  1 
ATOM 4604 C C   . THR C 1 176 ? -1.007  44.470  19.798  1.00 60.47  ?  176 THR C C   1 
ATOM 4605 O O   . THR C 1 176 ? -0.455  44.084  18.761  1.00 52.43  ?  176 THR C O   1 
ATOM 4606 C CB  . THR C 1 176 ? -0.427  46.278  21.486  1.00 60.05  ?  176 THR C CB  1 
ATOM 4607 O OG1 . THR C 1 176 ? -1.661  46.383  22.202  1.00 61.47  ?  176 THR C OG1 1 
ATOM 4608 C CG2 . THR C 1 176 ? -0.450  47.189  20.269  1.00 59.91  ?  176 THR C CG2 1 
ATOM 4609 N N   . TYR C 1 177 ? -2.331  44.577  19.905  1.00 56.59  ?  177 TYR C N   1 
ATOM 4610 C CA  . TYR C 1 177 ? -3.239  44.222  18.827  1.00 51.43  ?  177 TYR C CA  1 
ATOM 4611 C C   . TYR C 1 177 ? -4.152  45.395  18.489  1.00 55.78  ?  177 TYR C C   1 
ATOM 4612 O O   . TYR C 1 177 ? -4.323  46.336  19.273  1.00 58.56  ?  177 TYR C O   1 
ATOM 4613 C CB  . TYR C 1 177 ? -4.101  42.996  19.183  1.00 52.66  ?  177 TYR C CB  1 
ATOM 4614 C CG  . TYR C 1 177 ? -3.332  41.699  19.326  1.00 53.55  ?  177 TYR C CG  1 
ATOM 4615 C CD1 . TYR C 1 177 ? -2.790  41.068  18.218  1.00 56.01  ?  177 TYR C CD1 1 
ATOM 4616 C CD2 . TYR C 1 177 ? -3.179  41.087  20.563  1.00 57.22  ?  177 TYR C CD2 1 
ATOM 4617 C CE1 . TYR C 1 177 ? -2.091  39.885  18.336  1.00 55.53  ?  177 TYR C CE1 1 
ATOM 4618 C CE2 . TYR C 1 177 ? -2.484  39.897  20.692  1.00 55.55  ?  177 TYR C CE2 1 
ATOM 4619 C CZ  . TYR C 1 177 ? -1.944  39.302  19.571  1.00 58.71  ?  177 TYR C CZ  1 
ATOM 4620 O OH  . TYR C 1 177 ? -1.250  38.122  19.679  1.00 62.88  ?  177 TYR C OH  1 
ATOM 4621 N N   . SER C 1 178 ? -4.736  45.331  17.295  1.00 55.75  ?  178 SER C N   1 
ATOM 4622 C CA  . SER C 1 178 ? -5.737  46.297  16.867  1.00 52.01  ?  178 SER C CA  1 
ATOM 4623 C C   . SER C 1 178 ? -6.855  45.570  16.136  1.00 47.73  ?  178 SER C C   1 
ATOM 4624 O O   . SER C 1 178 ? -6.605  44.654  15.349  1.00 50.12  ?  178 SER C O   1 
ATOM 4625 C CB  . SER C 1 178 ? -5.130  47.388  15.981  1.00 51.72  ?  178 SER C CB  1 
ATOM 4626 O OG  . SER C 1 178 ? -4.302  48.245  16.744  1.00 48.35  ?  178 SER C OG  1 
ATOM 4627 N N   . LEU C 1 179 ? -8.085  45.976  16.421  1.00 40.13  ?  179 LEU C N   1 
ATOM 4628 C CA  . LEU C 1 179 ? -9.281  45.309  15.940  1.00 43.56  ?  179 LEU C CA  1 
ATOM 4629 C C   . LEU C 1 179 ? -10.142 46.323  15.207  1.00 49.51  ?  179 LEU C C   1 
ATOM 4630 O O   . LEU C 1 179 ? -10.265 47.470  15.641  1.00 50.83  ?  179 LEU C O   1 
ATOM 4631 C CB  . LEU C 1 179 ? -10.059 44.687  17.118  1.00 51.09  ?  179 LEU C CB  1 
ATOM 4632 C CG  . LEU C 1 179 ? -11.266 43.761  16.925  1.00 47.56  ?  179 LEU C CG  1 
ATOM 4633 C CD1 . LEU C 1 179 ? -12.537 44.533  16.574  1.00 50.36  ?  179 LEU C CD1 1 
ATOM 4634 C CD2 . LEU C 1 179 ? -10.976 42.729  15.876  1.00 50.05  ?  179 LEU C CD2 1 
ATOM 4635 N N   . SER C 1 180 ? -10.747 45.902  14.100  1.00 54.78  ?  180 SER C N   1 
ATOM 4636 C CA  . SER C 1 180 ? -11.647 46.765  13.345  1.00 45.31  ?  180 SER C CA  1 
ATOM 4637 C C   . SER C 1 180 ? -12.947 46.016  13.095  1.00 51.02  ?  180 SER C C   1 
ATOM 4638 O O   . SER C 1 180 ? -12.931 44.843  12.700  1.00 52.52  ?  180 SER C O   1 
ATOM 4639 C CB  . SER C 1 180 ? -11.016 47.223  12.027  1.00 43.34  ?  180 SER C CB  1 
ATOM 4640 O OG  . SER C 1 180 ? -10.982 46.164  11.083  1.00 59.94  ?  180 SER C OG  1 
ATOM 4641 N N   . SER C 1 181 ? -14.064 46.681  13.371  1.00 47.83  ?  181 SER C N   1 
ATOM 4642 C CA  . SER C 1 181 ? -15.396 46.140  13.140  1.00 49.07  ?  181 SER C CA  1 
ATOM 4643 C C   . SER C 1 181 ? -16.102 47.048  12.145  1.00 55.12  ?  181 SER C C   1 
ATOM 4644 O O   . SER C 1 181 ? -16.292 48.238  12.414  1.00 55.81  ?  181 SER C O   1 
ATOM 4645 C CB  . SER C 1 181 ? -16.182 46.046  14.448  1.00 47.28  ?  181 SER C CB  1 
ATOM 4646 O OG  . SER C 1 181 ? -17.472 45.509  14.226  1.00 47.36  ?  181 SER C OG  1 
ATOM 4647 N N   . THR C 1 182 ? -16.453 46.508  10.986  1.00 55.42  ?  182 THR C N   1 
ATOM 4648 C CA  . THR C 1 182 ? -17.091 47.281  9.930   1.00 52.33  ?  182 THR C CA  1 
ATOM 4649 C C   . THR C 1 182 ? -18.547 46.861  9.805   1.00 51.58  ?  182 THR C C   1 
ATOM 4650 O O   . THR C 1 182 ? -18.836 45.691  9.522   1.00 53.01  ?  182 THR C O   1 
ATOM 4651 C CB  . THR C 1 182 ? -16.362 47.100  8.606   1.00 48.81  ?  182 THR C CB  1 
ATOM 4652 O OG1 . THR C 1 182 ? -14.956 47.269  8.826   1.00 53.86  ?  182 THR C OG1 1 
ATOM 4653 C CG2 . THR C 1 182 ? -16.846 48.138  7.615   1.00 49.84  ?  182 THR C CG2 1 
ATOM 4654 N N   . LEU C 1 183 ? -19.452 47.814  10.021  1.00 51.34  ?  183 LEU C N   1 
ATOM 4655 C CA  . LEU C 1 183 ? -20.884 47.600  9.884   1.00 53.22  ?  183 LEU C CA  1 
ATOM 4656 C C   . LEU C 1 183 ? -21.346 48.233  8.578   1.00 57.54  ?  183 LEU C C   1 
ATOM 4657 O O   . LEU C 1 183 ? -21.209 49.449  8.387   1.00 52.37  ?  183 LEU C O   1 
ATOM 4658 C CB  . LEU C 1 183 ? -21.632 48.209  11.068  1.00 50.82  ?  183 LEU C CB  1 
ATOM 4659 C CG  . LEU C 1 183 ? -23.147 48.015  11.094  1.00 53.99  ?  183 LEU C CG  1 
ATOM 4660 C CD1 . LEU C 1 183 ? -23.503 46.640  11.640  1.00 59.17  ?  183 LEU C CD1 1 
ATOM 4661 C CD2 . LEU C 1 183 ? -23.807 49.111  11.905  1.00 50.00  ?  183 LEU C CD2 1 
ATOM 4662 N N   . THR C 1 184 ? -21.899 47.411  7.690   1.00 59.45  ?  184 THR C N   1 
ATOM 4663 C CA  . THR C 1 184 ? -22.326 47.844  6.367   1.00 62.54  ?  184 THR C CA  1 
ATOM 4664 C C   . THR C 1 184 ? -23.847 47.863  6.297   1.00 59.31  ?  184 THR C C   1 
ATOM 4665 O O   . THR C 1 184 ? -24.515 46.948  6.788   1.00 58.60  ?  184 THR C O   1 
ATOM 4666 C CB  . THR C 1 184 ? -21.757 46.932  5.272   1.00 57.32  ?  184 THR C CB  1 
ATOM 4667 O OG1 . THR C 1 184 ? -21.891 45.564  5.673   1.00 58.55  ?  184 THR C OG1 1 
ATOM 4668 C CG2 . THR C 1 184 ? -20.284 47.245  5.027   1.00 55.13  ?  184 THR C CG2 1 
ATOM 4669 N N   . LEU C 1 185 ? -24.387 48.926  5.706   1.00 61.13  ?  185 LEU C N   1 
ATOM 4670 C CA  . LEU C 1 185 ? -25.822 49.082  5.530   1.00 61.17  ?  185 LEU C CA  1 
ATOM 4671 C C   . LEU C 1 185 ? -26.079 49.765  4.199   1.00 63.25  ?  185 LEU C C   1 
ATOM 4672 O O   . LEU C 1 185 ? -25.176 50.340  3.588   1.00 64.11  ?  185 LEU C O   1 
ATOM 4673 C CB  . LEU C 1 185 ? -26.447 49.909  6.660   1.00 70.17  ?  185 LEU C CB  1 
ATOM 4674 C CG  . LEU C 1 185 ? -26.382 49.384  8.091   1.00 60.08  ?  185 LEU C CG  1 
ATOM 4675 C CD1 . LEU C 1 185 ? -26.880 50.449  9.050   1.00 55.03  ?  185 LEU C CD1 1 
ATOM 4676 C CD2 . LEU C 1 185 ? -27.208 48.121  8.223   1.00 60.59  ?  185 LEU C CD2 1 
ATOM 4677 N N   . SER C 1 186 ? -27.335 49.725  3.765   1.00 70.36  ?  186 SER C N   1 
ATOM 4678 C CA  . SER C 1 186 ? -27.731 50.526  2.620   1.00 69.71  ?  186 SER C CA  1 
ATOM 4679 C C   . SER C 1 186 ? -27.895 51.977  3.048   1.00 68.37  ?  186 SER C C   1 
ATOM 4680 O O   . SER C 1 186 ? -28.032 52.282  4.235   1.00 75.06  ?  186 SER C O   1 
ATOM 4681 C CB  . SER C 1 186 ? -29.042 50.015  2.031   1.00 74.08  ?  186 SER C CB  1 
ATOM 4682 O OG  . SER C 1 186 ? -30.067 50.063  3.011   1.00 75.37  ?  186 SER C OG  1 
ATOM 4683 N N   . LYS C 1 187 ? -27.890 52.879  2.063   1.00 63.00  ?  187 LYS C N   1 
ATOM 4684 C CA  . LYS C 1 187 ? -28.053 54.296  2.374   1.00 63.09  ?  187 LYS C CA  1 
ATOM 4685 C C   . LYS C 1 187 ? -29.398 54.564  3.039   1.00 67.17  ?  187 LYS C C   1 
ATOM 4686 O O   . LYS C 1 187 ? -29.483 55.349  3.991   1.00 66.59  ?  187 LYS C O   1 
ATOM 4687 C CB  . LYS C 1 187 ? -27.904 55.138  1.109   1.00 65.27  ?  187 LYS C CB  1 
ATOM 4688 C CG  . LYS C 1 187 ? -28.116 56.625  1.338   1.00 66.64  ?  187 LYS C CG  1 
ATOM 4689 C CD  . LYS C 1 187 ? -27.903 57.416  0.067   1.00 58.35  ?  187 LYS C CD  1 
ATOM 4690 C CE  . LYS C 1 187 ? -28.145 58.895  0.298   1.00 62.14  ?  187 LYS C CE  1 
ATOM 4691 N NZ  . LYS C 1 187 ? -27.974 59.677  -0.960  1.00 79.69  ?  187 LYS C NZ  1 
ATOM 4692 N N   . ALA C 1 188 ? -30.458 53.910  2.560   1.00 73.81  ?  188 ALA C N   1 
ATOM 4693 C CA  . ALA C 1 188 ? -31.782 54.110  3.141   1.00 77.02  ?  188 ALA C CA  1 
ATOM 4694 C C   . ALA C 1 188 ? -31.828 53.635  4.589   1.00 77.96  ?  188 ALA C C   1 
ATOM 4695 O O   . ALA C 1 188 ? -32.336 54.342  5.470   1.00 84.07  ?  188 ALA C O   1 
ATOM 4696 C CB  . ALA C 1 188 ? -32.834 53.387  2.300   1.00 88.10  ?  188 ALA C CB  1 
ATOM 4697 N N   . ASP C 1 189 ? -31.300 52.435  4.856   1.00 78.10  ?  189 ASP C N   1 
ATOM 4698 C CA  . ASP C 1 189 ? -31.269 51.933  6.228   1.00 79.68  ?  189 ASP C CA  1 
ATOM 4699 C C   . ASP C 1 189 ? -30.435 52.828  7.133   1.00 75.06  ?  189 ASP C C   1 
ATOM 4700 O O   . ASP C 1 189 ? -30.722 52.942  8.330   1.00 77.66  ?  189 ASP C O   1 
ATOM 4701 C CB  . ASP C 1 189 ? -30.724 50.503  6.262   1.00 79.71  ?  189 ASP C CB  1 
ATOM 4702 C CG  . ASP C 1 189 ? -31.732 49.479  5.781   1.00 87.01  ?  189 ASP C CG  1 
ATOM 4703 O OD1 . ASP C 1 189 ? -32.890 49.870  5.512   1.00 92.95  ?  189 ASP C OD1 1 
ATOM 4704 O OD2 . ASP C 1 189 ? -31.366 48.285  5.681   1.00 76.16  ?  189 ASP C OD2 1 
ATOM 4705 N N   . TYR C 1 190 ? -29.420 53.492  6.578   1.00 71.70  ?  190 TYR C N   1 
ATOM 4706 C CA  . TYR C 1 190 ? -28.626 54.416  7.375   1.00 67.89  ?  190 TYR C CA  1 
ATOM 4707 C C   . TYR C 1 190 ? -29.414 55.679  7.692   1.00 75.96  ?  190 TYR C C   1 
ATOM 4708 O O   . TYR C 1 190 ? -29.343 56.193  8.815   1.00 78.24  ?  190 TYR C O   1 
ATOM 4709 C CB  . TYR C 1 190 ? -27.326 54.754  6.645   1.00 67.95  ?  190 TYR C CB  1 
ATOM 4710 C CG  . TYR C 1 190 ? -26.407 55.685  7.405   1.00 67.72  ?  190 TYR C CG  1 
ATOM 4711 C CD1 . TYR C 1 190 ? -25.728 55.252  8.536   1.00 65.27  ?  190 TYR C CD1 1 
ATOM 4712 C CD2 . TYR C 1 190 ? -26.203 56.991  6.979   1.00 65.68  ?  190 TYR C CD2 1 
ATOM 4713 C CE1 . TYR C 1 190 ? -24.884 56.095  9.233   1.00 66.29  ?  190 TYR C CE1 1 
ATOM 4714 C CE2 . TYR C 1 190 ? -25.360 57.841  7.667   1.00 69.21  ?  190 TYR C CE2 1 
ATOM 4715 C CZ  . TYR C 1 190 ? -24.703 57.389  8.796   1.00 70.04  ?  190 TYR C CZ  1 
ATOM 4716 O OH  . TYR C 1 190 ? -23.860 58.231  9.488   1.00 62.04  ?  190 TYR C OH  1 
ATOM 4717 N N   . GLU C 1 191 ? -30.186 56.185  6.724   1.00 74.27  ?  191 GLU C N   1 
ATOM 4718 C CA  . GLU C 1 191 ? -31.005 57.363  6.992   1.00 70.80  ?  191 GLU C CA  1 
ATOM 4719 C C   . GLU C 1 191 ? -32.168 57.045  7.923   1.00 76.58  ?  191 GLU C C   1 
ATOM 4720 O O   . GLU C 1 191 ? -32.710 57.958  8.553   1.00 75.99  ?  191 GLU C O   1 
ATOM 4721 C CB  . GLU C 1 191 ? -31.554 57.957  5.692   1.00 74.19  ?  191 GLU C CB  1 
ATOM 4722 C CG  . GLU C 1 191 ? -30.553 58.078  4.544   1.00 79.04  ?  191 GLU C CG  1 
ATOM 4723 C CD  . GLU C 1 191 ? -29.591 59.245  4.663   1.00 77.34  ?  191 GLU C CD  1 
ATOM 4724 O OE1 . GLU C 1 191 ? -29.200 59.593  5.799   1.00 75.37  ?  191 GLU C OE1 1 
ATOM 4725 O OE2 . GLU C 1 191 ? -29.216 59.800  3.604   1.00 70.63  ?  191 GLU C OE2 1 
ATOM 4726 N N   . LYS C 1 192 ? -32.557 55.772  8.027   1.00 77.36  ?  192 LYS C N   1 
ATOM 4727 C CA  . LYS C 1 192 ? -33.702 55.376  8.841   1.00 79.84  ?  192 LYS C CA  1 
ATOM 4728 C C   . LYS C 1 192 ? -33.450 55.461  10.346  1.00 79.39  ?  192 LYS C C   1 
ATOM 4729 O O   . LYS C 1 192 ? -34.376 55.169  11.111  1.00 76.49  ?  192 LYS C O   1 
ATOM 4730 C CB  . LYS C 1 192 ? -34.125 53.946  8.497   1.00 78.38  ?  192 LYS C CB  1 
ATOM 4731 C CG  . LYS C 1 192 ? -34.954 53.790  7.228   1.00 89.05  ?  192 LYS C CG  1 
ATOM 4732 C CD  . LYS C 1 192 ? -35.230 52.310  6.956   1.00 92.05  ?  192 LYS C CD  1 
ATOM 4733 C CE  . LYS C 1 192 ? -36.037 52.100  5.684   1.00 88.40  ?  192 LYS C CE  1 
ATOM 4734 N NZ  . LYS C 1 192 ? -37.424 52.629  5.814   1.00 95.11  ?  192 LYS C NZ  1 
ATOM 4735 N N   . HIS C 1 193 ? -32.256 55.845  10.801  1.00 77.55  ?  193 HIS C N   1 
ATOM 4736 C CA  . HIS C 1 193 ? -31.927 55.784  12.221  1.00 76.68  ?  193 HIS C CA  1 
ATOM 4737 C C   . HIS C 1 193 ? -31.143 57.027  12.616  1.00 79.08  ?  193 HIS C C   1 
ATOM 4738 O O   . HIS C 1 193 ? -30.897 57.919  11.795  1.00 76.40  ?  193 HIS C O   1 
ATOM 4739 C CB  . HIS C 1 193 ? -31.138 54.512  12.551  1.00 74.40  ?  193 HIS C CB  1 
ATOM 4740 C CG  . HIS C 1 193 ? -31.866 53.251  12.211  1.00 76.50  ?  193 HIS C CG  1 
ATOM 4741 N ND1 . HIS C 1 193 ? -33.077 52.915  12.777  1.00 73.66  ?  193 HIS C ND1 1 
ATOM 4742 C CD2 . HIS C 1 193 ? -31.568 52.256  11.341  1.00 78.69  ?  193 HIS C CD2 1 
ATOM 4743 C CE1 . HIS C 1 193 ? -33.486 51.761  12.282  1.00 81.08  ?  193 HIS C CE1 1 
ATOM 4744 N NE2 . HIS C 1 193 ? -32.590 51.341  11.407  1.00 79.52  ?  193 HIS C NE2 1 
ATOM 4745 N N   . LYS C 1 194 ? -30.725 57.068  13.887  1.00 76.34  ?  194 LYS C N   1 
ATOM 4746 C CA  . LYS C 1 194 ? -30.104 58.264  14.451  1.00 78.17  ?  194 LYS C CA  1 
ATOM 4747 C C   . LYS C 1 194 ? -28.838 57.970  15.250  1.00 69.13  ?  194 LYS C C   1 
ATOM 4748 O O   . LYS C 1 194 ? -27.777 58.529  14.957  1.00 68.96  ?  194 LYS C O   1 
ATOM 4749 C CB  . LYS C 1 194 ? -31.101 58.997  15.351  1.00 74.62  ?  194 LYS C CB  1 
ATOM 4750 C CG  . LYS C 1 194 ? -30.511 60.201  16.070  1.00 78.84  ?  194 LYS C CG  1 
ATOM 4751 C CD  . LYS C 1 194 ? -31.458 60.714  17.146  1.00 83.51  ?  194 LYS C CD  1 
ATOM 4752 C CE  . LYS C 1 194 ? -30.798 61.780  18.009  1.00 81.33  ?  194 LYS C CE  1 
ATOM 4753 N NZ  . LYS C 1 194 ? -31.646 62.146  19.175  1.00 71.78  ?  194 LYS C NZ  1 
ATOM 4754 N N   . VAL C 1 195 ? -28.934 57.115  16.265  1.00 69.63  ?  195 VAL C N   1 
ATOM 4755 C CA  . VAL C 1 195 ? -27.831 56.873  17.192  1.00 71.42  ?  195 VAL C CA  1 
ATOM 4756 C C   . VAL C 1 195 ? -27.136 55.574  16.807  1.00 65.52  ?  195 VAL C C   1 
ATOM 4757 O O   . VAL C 1 195 ? -27.771 54.515  16.743  1.00 68.91  ?  195 VAL C O   1 
ATOM 4758 C CB  . VAL C 1 195 ? -28.316 56.830  18.650  1.00 73.15  ?  195 VAL C CB  1 
ATOM 4759 C CG1 . VAL C 1 195 ? -27.139 56.611  19.594  1.00 65.53  ?  195 VAL C CG1 1 
ATOM 4760 C CG2 . VAL C 1 195 ? -29.053 58.115  19.005  1.00 70.78  ?  195 VAL C CG2 1 
ATOM 4761 N N   . TYR C 1 196 ? -25.826 55.647  16.581  1.00 62.64  ?  196 TYR C N   1 
ATOM 4762 C CA  . TYR C 1 196 ? -25.007 54.489  16.256  1.00 66.32  ?  196 TYR C CA  1 
ATOM 4763 C C   . TYR C 1 196 ? -23.928 54.350  17.319  1.00 63.09  ?  196 TYR C C   1 
ATOM 4764 O O   . TYR C 1 196 ? -23.406 55.352  17.814  1.00 60.50  ?  196 TYR C O   1 
ATOM 4765 C CB  . TYR C 1 196 ? -24.373 54.628  14.855  1.00 69.91  ?  196 TYR C CB  1 
ATOM 4766 C CG  . TYR C 1 196 ? -25.374 54.600  13.716  1.00 64.09  ?  196 TYR C CG  1 
ATOM 4767 C CD1 . TYR C 1 196 ? -25.613 53.427  13.012  1.00 64.78  ?  196 TYR C CD1 1 
ATOM 4768 C CD2 . TYR C 1 196 ? -26.085 55.738  13.352  1.00 65.62  ?  196 TYR C CD2 1 
ATOM 4769 C CE1 . TYR C 1 196 ? -26.534 53.383  11.978  1.00 68.48  ?  196 TYR C CE1 1 
ATOM 4770 C CE2 . TYR C 1 196 ? -27.008 55.706  12.318  1.00 68.25  ?  196 TYR C CE2 1 
ATOM 4771 C CZ  . TYR C 1 196 ? -27.228 54.524  11.633  1.00 72.50  ?  196 TYR C CZ  1 
ATOM 4772 O OH  . TYR C 1 196 ? -28.141 54.478  10.601  1.00 74.39  ?  196 TYR C OH  1 
ATOM 4773 N N   . ALA C 1 197 ? -23.606 53.110  17.683  1.00 63.88  ?  197 ALA C N   1 
ATOM 4774 C CA  . ALA C 1 197 ? -22.669 52.881  18.774  1.00 57.07  ?  197 ALA C CA  1 
ATOM 4775 C C   . ALA C 1 197 ? -22.045 51.503  18.637  1.00 61.23  ?  197 ALA C C   1 
ATOM 4776 O O   . ALA C 1 197 ? -22.674 50.570  18.132  1.00 66.21  ?  197 ALA C O   1 
ATOM 4777 C CB  . ALA C 1 197 ? -23.369 52.992  20.132  1.00 55.23  ?  197 ALA C CB  1 
ATOM 4778 N N   . CYS C 1 198 ? -20.804 51.382  19.098  1.00 55.16  ?  198 CYS C N   1 
ATOM 4779 C CA  . CYS C 1 198 ? -20.188 50.076  19.282  1.00 57.22  ?  198 CYS C CA  1 
ATOM 4780 C C   . CYS C 1 198 ? -19.752 49.941  20.731  1.00 58.68  ?  198 CYS C C   1 
ATOM 4781 O O   . CYS C 1 198 ? -19.158 50.866  21.304  1.00 58.53  ?  198 CYS C O   1 
ATOM 4782 C CB  . CYS C 1 198 ? -19.007 49.819  18.335  1.00 53.60  ?  198 CYS C CB  1 
ATOM 4783 S SG  . CYS C 1 198 ? -17.650 50.980  18.374  1.00 68.50  ?  198 CYS C SG  1 
ATOM 4784 N N   . GLU C 1 199 ? -20.069 48.793  21.313  1.00 56.17  ?  199 GLU C N   1 
ATOM 4785 C CA  . GLU C 1 199 ? -19.755 48.471  22.693  1.00 60.46  ?  199 GLU C CA  1 
ATOM 4786 C C   . GLU C 1 199 ? -18.649 47.425  22.678  1.00 62.11  ?  199 GLU C C   1 
ATOM 4787 O O   . GLU C 1 199 ? -18.793 46.368  22.047  1.00 58.82  ?  199 GLU C O   1 
ATOM 4788 C CB  . GLU C 1 199 ? -21.003 47.965  23.421  1.00 63.70  ?  199 GLU C CB  1 
ATOM 4789 C CG  . GLU C 1 199 ? -20.807 47.609  24.884  1.00 64.03  ?  199 GLU C CG  1 
ATOM 4790 C CD  . GLU C 1 199 ? -22.096 47.142  25.553  1.00 74.01  ?  199 GLU C CD  1 
ATOM 4791 O OE1 . GLU C 1 199 ? -23.122 47.005  24.852  1.00 73.46  ?  199 GLU C OE1 1 
ATOM 4792 O OE2 . GLU C 1 199 ? -22.084 46.911  26.784  1.00 77.83  ?  199 GLU C OE2 1 
ATOM 4793 N N   . VAL C 1 200 ? -17.531 47.749  23.323  1.00 55.87  ?  200 VAL C N   1 
ATOM 4794 C CA  . VAL C 1 200 ? -16.384 46.860  23.452  1.00 59.41  ?  200 VAL C CA  1 
ATOM 4795 C C   . VAL C 1 200 ? -16.326 46.382  24.897  1.00 66.48  ?  200 VAL C C   1 
ATOM 4796 O O   . VAL C 1 200 ? -16.202 47.194  25.824  1.00 67.03  ?  200 VAL C O   1 
ATOM 4797 C CB  . VAL C 1 200 ? -15.077 47.565  23.064  1.00 54.03  ?  200 VAL C CB  1 
ATOM 4798 C CG1 . VAL C 1 200 ? -13.893 46.652  23.314  1.00 55.35  ?  200 VAL C CG1 1 
ATOM 4799 C CG2 . VAL C 1 200 ? -15.123 48.009  21.614  1.00 58.85  ?  200 VAL C CG2 1 
ATOM 4800 N N   . THR C 1 201 ? -16.410 45.071  25.089  1.00 62.67  ?  201 THR C N   1 
ATOM 4801 C CA  . THR C 1 201 ? -16.303 44.458  26.404  1.00 58.81  ?  201 THR C CA  1 
ATOM 4802 C C   . THR C 1 201 ? -15.011 43.654  26.476  1.00 56.67  ?  201 THR C C   1 
ATOM 4803 O O   . THR C 1 201 ? -14.726 42.843  25.586  1.00 58.27  ?  201 THR C O   1 
ATOM 4804 C CB  . THR C 1 201 ? -17.512 43.566  26.690  1.00 64.51  ?  201 THR C CB  1 
ATOM 4805 O OG1 . THR C 1 201 ? -18.714 44.319  26.480  1.00 69.26  ?  201 THR C OG1 1 
ATOM 4806 C CG2 . THR C 1 201 ? -17.479 43.066  28.125  1.00 56.59  ?  201 THR C CG2 1 
ATOM 4807 N N   . GLN C 1 202 ? -14.235 43.883  27.536  1.00 54.42  ?  202 GLN C N   1 
ATOM 4808 C CA  . GLN C 1 202 ? -12.953 43.218  27.749  1.00 56.17  ?  202 GLN C CA  1 
ATOM 4809 C C   . GLN C 1 202 ? -12.885 42.888  29.244  1.00 65.10  ?  202 GLN C C   1 
ATOM 4810 O O   . GLN C 1 202 ? -12.328 43.644  30.046  1.00 66.11  ?  202 GLN C O   1 
ATOM 4811 C CB  . GLN C 1 202 ? -11.780 44.088  27.299  1.00 56.60  ?  202 GLN C CB  1 
ATOM 4812 C CG  . GLN C 1 202 ? -10.426 43.399  27.387  1.00 66.17  ?  202 GLN C CG  1 
ATOM 4813 C CD  . GLN C 1 202 ? -9.260  44.348  27.146  1.00 63.92  ?  202 GLN C CD  1 
ATOM 4814 O OE1 . GLN C 1 202 ? -9.348  45.541  27.432  1.00 66.90  ?  202 GLN C OE1 1 
ATOM 4815 N NE2 . GLN C 1 202 ? -8.159  43.816  26.626  1.00 62.48  ?  202 GLN C NE2 1 
ATOM 4816 N N   . GLY C 1 203 ? -13.475 41.751  29.617  1.00 63.94  ?  203 GLY C N   1 
ATOM 4817 C CA  . GLY C 1 203 ? -13.513 41.327  31.005  1.00 62.22  ?  203 GLY C CA  1 
ATOM 4818 C C   . GLY C 1 203 ? -14.627 41.955  31.820  1.00 65.67  ?  203 GLY C C   1 
ATOM 4819 O O   . GLY C 1 203 ? -15.811 41.708  31.563  1.00 65.28  ?  203 GLY C O   1 
ATOM 4820 N N   . THR C 1 204 ? -14.260 42.756  32.820  1.00 64.41  ?  204 THR C N   1 
ATOM 4821 C CA  . THR C 1 204 ? -15.217 43.431  33.689  1.00 66.65  ?  204 THR C CA  1 
ATOM 4822 C C   . THR C 1 204 ? -15.556 44.843  33.224  1.00 65.24  ?  204 THR C C   1 
ATOM 4823 O O   . THR C 1 204 ? -16.293 45.548  33.921  1.00 66.60  ?  204 THR C O   1 
ATOM 4824 C CB  . THR C 1 204 ? -14.682 43.490  35.122  1.00 73.59  ?  204 THR C CB  1 
ATOM 4825 O OG1 . THR C 1 204 ? -13.358 44.040  35.115  1.00 77.19  ?  204 THR C OG1 1 
ATOM 4826 C CG2 . THR C 1 204 ? -14.658 42.103  35.754  1.00 67.68  ?  204 THR C CG2 1 
ATOM 4827 N N   . THR C 1 205 ? -15.051 45.264  32.067  1.00 68.96  ?  205 THR C N   1 
ATOM 4828 C CA  . THR C 1 205 ? -15.258 46.607  31.539  1.00 63.96  ?  205 THR C CA  1 
ATOM 4829 C C   . THR C 1 205 ? -15.998 46.518  30.212  1.00 60.83  ?  205 THR C C   1 
ATOM 4830 O O   . THR C 1 205 ? -15.781 45.583  29.435  1.00 67.31  ?  205 THR C O   1 
ATOM 4831 C CB  . THR C 1 205 ? -13.922 47.338  31.342  1.00 64.10  ?  205 THR C CB  1 
ATOM 4832 O OG1 . THR C 1 205 ? -13.130 47.227  32.532  1.00 74.89  ?  205 THR C OG1 1 
ATOM 4833 C CG2 . THR C 1 205 ? -14.153 48.808  31.036  1.00 63.25  ?  205 THR C CG2 1 
ATOM 4834 N N   . SER C 1 206 ? -16.882 47.484  29.955  1.00 60.34  ?  206 SER C N   1 
ATOM 4835 C CA  . SER C 1 206 ? -17.682 47.483  28.729  1.00 58.40  ?  206 SER C CA  1 
ATOM 4836 C C   . SER C 1 206 ? -17.927 48.936  28.320  1.00 59.67  ?  206 SER C C   1 
ATOM 4837 O O   . SER C 1 206 ? -18.894 49.556  28.774  1.00 63.08  ?  206 SER C O   1 
ATOM 4838 C CB  . SER C 1 206 ? -18.983 46.725  28.961  1.00 57.92  ?  206 SER C CB  1 
ATOM 4839 O OG  . SER C 1 206 ? -19.706 46.528  27.766  1.00 64.56  ?  206 SER C OG  1 
ATOM 4840 N N   . VAL C 1 207 ? -17.088 49.450  27.419  1.00 58.73  ?  207 VAL C N   1 
ATOM 4841 C CA  . VAL C 1 207 ? -17.109 50.861  27.023  1.00 59.27  ?  207 VAL C CA  1 
ATOM 4842 C C   . VAL C 1 207 ? -17.798 51.005  25.673  1.00 54.82  ?  207 VAL C C   1 
ATOM 4843 O O   . VAL C 1 207 ? -17.505 50.253  24.738  1.00 64.50  ?  207 VAL C O   1 
ATOM 4844 C CB  . VAL C 1 207 ? -15.687 51.447  26.977  1.00 54.41  ?  207 VAL C CB  1 
ATOM 4845 C CG1 . VAL C 1 207 ? -14.737 50.502  26.266  1.00 57.30  ?  207 VAL C CG1 1 
ATOM 4846 C CG2 . VAL C 1 207 ? -15.693 52.799  26.290  1.00 58.69  ?  207 VAL C CG2 1 
ATOM 4847 N N   . THR C 1 208 ? -18.706 51.975  25.565  1.00 53.46  ?  208 THR C N   1 
ATOM 4848 C CA  . THR C 1 208 ? -19.490 52.196  24.355  1.00 56.59  ?  208 THR C CA  1 
ATOM 4849 C C   . THR C 1 208 ? -19.168 53.561  23.754  1.00 58.81  ?  208 THR C C   1 
ATOM 4850 O O   . THR C 1 208 ? -19.242 54.582  24.448  1.00 60.93  ?  208 THR C O   1 
ATOM 4851 C CB  . THR C 1 208 ? -20.991 52.110  24.650  1.00 55.49  ?  208 THR C CB  1 
ATOM 4852 O OG1 . THR C 1 208 ? -21.294 50.849  25.262  1.00 64.08  ?  208 THR C OG1 1 
ATOM 4853 C CG2 . THR C 1 208 ? -21.782 52.245  23.366  1.00 54.27  ?  208 THR C CG2 1 
ATOM 4854 N N   . LYS C 1 209 ? -18.828 53.581  22.465  1.00 56.22  ?  209 LYS C N   1 
ATOM 4855 C CA  . LYS C 1 209 ? -18.626 54.826  21.729  1.00 52.25  ?  209 LYS C CA  1 
ATOM 4856 C C   . LYS C 1 209 ? -19.740 55.009  20.709  1.00 51.26  ?  209 LYS C C   1 
ATOM 4857 O O   . LYS C 1 209 ? -20.103 54.061  20.004  1.00 61.17  ?  209 LYS C O   1 
ATOM 4858 C CB  . LYS C 1 209 ? -17.268 54.852  21.026  1.00 48.10  ?  209 LYS C CB  1 
ATOM 4859 C CG  . LYS C 1 209 ? -16.077 54.882  21.972  1.00 58.39  ?  209 LYS C CG  1 
ATOM 4860 C CD  . LYS C 1 209 ? -15.766 56.289  22.467  1.00 61.44  ?  209 LYS C CD  1 
ATOM 4861 C CE  . LYS C 1 209 ? -14.665 56.256  23.525  1.00 65.98  ?  209 LYS C CE  1 
ATOM 4862 N NZ  . LYS C 1 209 ? -14.384 57.592  24.132  1.00 71.24  ?  209 LYS C NZ  1 
ATOM 4863 N N   . SER C 1 210 ? -20.278 56.228  20.622  1.00 49.23  ?  210 SER C N   1 
ATOM 4864 C CA  . SER C 1 210 ? -21.468 56.484  19.819  1.00 54.06  ?  210 SER C CA  1 
ATOM 4865 C C   . SER C 1 210 ? -21.327 57.783  19.029  1.00 60.21  ?  210 SER C C   1 
ATOM 4866 O O   . SER C 1 210 ? -20.369 58.548  19.183  1.00 57.61  ?  210 SER C O   1 
ATOM 4867 C CB  . SER C 1 210 ? -22.732 56.546  20.684  1.00 48.89  ?  210 SER C CB  1 
ATOM 4868 O OG  . SER C 1 210 ? -22.686 57.646  21.577  1.00 57.50  ?  210 SER C OG  1 
ATOM 4869 N N   . PHE C 1 211 ? -22.294 57.991  18.140  1.00 59.04  ?  211 PHE C N   1 
ATOM 4870 C CA  . PHE C 1 211 ? -22.464 59.237  17.408  1.00 61.55  ?  211 PHE C CA  1 
ATOM 4871 C C   . PHE C 1 211 ? -23.868 59.269  16.815  1.00 66.28  ?  211 PHE C C   1 
ATOM 4872 O O   . PHE C 1 211 ? -24.483 58.225  16.580  1.00 67.10  ?  211 PHE C O   1 
ATOM 4873 C CB  . PHE C 1 211 ? -21.414 59.408  16.303  1.00 60.10  ?  211 PHE C CB  1 
ATOM 4874 C CG  . PHE C 1 211 ? -21.709 58.620  15.057  1.00 61.89  ?  211 PHE C CG  1 
ATOM 4875 C CD1 . PHE C 1 211 ? -21.313 57.298  14.949  1.00 57.76  ?  211 PHE C CD1 1 
ATOM 4876 C CD2 . PHE C 1 211 ? -22.378 59.202  13.993  1.00 62.60  ?  211 PHE C CD2 1 
ATOM 4877 C CE1 . PHE C 1 211 ? -21.581 56.572  13.813  1.00 58.72  ?  211 PHE C CE1 1 
ATOM 4878 C CE2 . PHE C 1 211 ? -22.653 58.478  12.855  1.00 64.73  ?  211 PHE C CE2 1 
ATOM 4879 C CZ  . PHE C 1 211 ? -22.252 57.161  12.762  1.00 62.76  ?  211 PHE C CZ  1 
ATOM 4880 N N   . ASN C 1 212 ? -24.367 60.478  16.578  1.00 72.89  ?  212 ASN C N   1 
ATOM 4881 C CA  . ASN C 1 212 ? -25.629 60.684  15.882  1.00 76.02  ?  212 ASN C CA  1 
ATOM 4882 C C   . ASN C 1 212 ? -25.339 61.244  14.494  1.00 79.46  ?  212 ASN C C   1 
ATOM 4883 O O   . ASN C 1 212 ? -24.354 61.958  14.288  1.00 81.93  ?  212 ASN C O   1 
ATOM 4884 C CB  . ASN C 1 212 ? -26.569 61.625  16.645  1.00 75.00  ?  212 ASN C CB  1 
ATOM 4885 C CG  . ASN C 1 212 ? -26.756 61.220  18.088  1.00 74.24  ?  212 ASN C CG  1 
ATOM 4886 O OD1 . ASN C 1 212 ? -26.476 60.084  18.466  1.00 77.66  ?  212 ASN C OD1 1 
ATOM 4887 N ND2 . ASN C 1 212 ? -27.243 62.147  18.904  1.00 78.32  ?  212 ASN C ND2 1 
ATOM 4888 N N   . ARG C 1 213 ? -26.246 60.968  13.565  1.00 77.38  ?  213 ARG C N   1 
ATOM 4889 C CA  . ARG C 1 213 ? -25.986 61.325  12.150  1.00 81.66  ?  213 ARG C CA  1 
ATOM 4890 C C   . ARG C 1 213 ? -25.770 62.825  11.955  1.00 82.08  ?  213 ARG C C   1 
ATOM 4891 O O   . ARG C 1 213 ? -24.648 63.201  11.591  1.00 77.39  ?  213 ARG C O   1 
ATOM 4892 C CB  . ARG C 1 213 ? -27.120 60.773  11.282  1.00 77.08  ?  213 ARG C CB  1 
ATOM 4893 C CG  . ARG C 1 213 ? -27.422 59.302  11.517  1.00 76.45  ?  213 ARG C CG  1 
ATOM 4894 C CD  . ARG C 1 213 ? -27.915 58.611  10.262  1.00 76.32  ?  213 ARG C CD  1 
ATOM 4895 N NE  . ARG C 1 213 ? -28.309 59.561  9.237   1.00 75.86  ?  213 ARG C NE  1 
ATOM 4896 C CZ  . ARG C 1 213 ? -29.528 60.066  9.115   1.00 77.73  ?  213 ARG C CZ  1 
ATOM 4897 N NH1 . ARG C 1 213 ? -30.480 59.710  9.959   1.00 78.32  ?  213 ARG C NH1 1 
ATOM 4898 N NH2 . ARG C 1 213 ? -29.792 60.928  8.152   1.00 75.55  ?  213 ARG C NH2 1 
ATOM 4899 N N   . GLY C 1 214 ? -26.819 63.615  12.155  1.00 84.68  ?  214 GLY C N   1 
ATOM 4900 C CA  . GLY C 1 214 ? -26.686 65.079  12.060  1.00 86.41  ?  214 GLY C CA  1 
ATOM 4901 C C   . GLY C 1 214 ? -26.078 65.615  13.336  1.00 98.43  ?  214 GLY C C   1 
ATOM 4902 O O   . GLY C 1 214 ? -26.843 65.922  14.268  1.00 104.85 ?  214 GLY C O   1 
ATOM 4903 N N   . GLU C 1 215 ? -24.753 65.696  13.388  1.00 101.62 ?  215 GLU C N   1 
ATOM 4904 C CA  . GLU C 1 215 ? -24.077 66.121  14.632  1.00 102.42 ?  215 GLU C CA  1 
ATOM 4905 C C   . GLU C 1 215 ? -22.608 66.345  14.307  1.00 108.68 ?  215 GLU C C   1 
ATOM 4906 O O   . GLU C 1 215 ? -22.164 65.889  13.238  1.00 105.40 ?  215 GLU C O   1 
ATOM 4907 C CB  . GLU C 1 215 ? -24.186 65.037  15.696  1.00 94.23  ?  215 GLU C CB  1 
ATOM 4908 C CG  . GLU C 1 215 ? -22.971 64.125  15.743  1.00 96.77  ?  215 GLU C CG  1 
ATOM 4909 C CD  . GLU C 1 215 ? -22.767 63.339  17.027  1.00 96.26  ?  215 GLU C CD  1 
ATOM 4910 O OE1 . GLU C 1 215 ? -23.766 62.861  17.596  1.00 97.89  ?  215 GLU C OE1 1 
ATOM 4911 O OE2 . GLU C 1 215 ? -21.605 63.204  17.451  1.00 84.96  ?  215 GLU C OE2 1 
ATOM 4912 N N   . CYS C 1 216 ? -21.891 67.019  15.201  1.00 116.16 ?  216 CYS C N   1 
ATOM 4913 C CA  . CYS C 1 216 ? -20.460 67.311  14.955  1.00 114.98 ?  216 CYS C CA  1 
ATOM 4914 C C   . CYS C 1 216 ? -19.882 67.999  16.194  1.00 109.39 ?  216 CYS C C   1 
ATOM 4915 O O   . CYS C 1 216 ? -18.999 67.387  16.827  1.00 98.86  ?  216 CYS C O   1 
ATOM 4916 C CB  . CYS C 1 216 ? -20.287 68.194  13.726  1.00 119.83 ?  216 CYS C CB  1 
ATOM 4917 S SG  . CYS C 1 216 ? -21.232 69.740  13.780  1.00 138.19 ?  216 CYS C SG  1 
ATOM 4918 N N   . GLU D 2 1   ? 21.575  28.690  -4.174  1.00 102.45 ?  1   GLU D N   1 
ATOM 4919 C CA  . GLU D 2 1   ? 22.054  28.115  -5.430  1.00 113.18 ?  1   GLU D CA  1 
ATOM 4920 C C   . GLU D 2 1   ? 21.217  26.902  -5.841  1.00 102.85 ?  1   GLU D C   1 
ATOM 4921 O O   . GLU D 2 1   ? 21.305  26.427  -6.973  1.00 97.84  ?  1   GLU D O   1 
ATOM 4922 C CB  . GLU D 2 1   ? 23.531  27.737  -5.313  1.00 117.51 ?  1   GLU D CB  1 
ATOM 4923 C CG  . GLU D 2 1   ? 24.451  28.940  -5.149  1.00 115.56 ?  1   GLU D CG  1 
ATOM 4924 C CD  . GLU D 2 1   ? 25.914  28.556  -5.079  1.00 113.44 ?  1   GLU D CD  1 
ATOM 4925 O OE1 . GLU D 2 1   ? 26.634  29.113  -4.222  1.00 109.33 ?  1   GLU D OE1 1 
ATOM 4926 O OE2 . GLU D 2 1   ? 26.340  27.690  -5.875  1.00 109.33 ?  1   GLU D OE2 1 
ATOM 4927 N N   . VAL D 2 2   ? 20.425  26.395  -4.900  1.00 101.70 ?  2   VAL D N   1 
ATOM 4928 C CA  . VAL D 2 2   ? 19.449  25.339  -5.150  1.00 96.38  ?  2   VAL D CA  1 
ATOM 4929 C C   . VAL D 2 2   ? 18.071  25.950  -4.921  1.00 96.92  ?  2   VAL D C   1 
ATOM 4930 O O   . VAL D 2 2   ? 17.750  26.363  -3.799  1.00 100.69 ?  2   VAL D O   1 
ATOM 4931 C CB  . VAL D 2 2   ? 19.687  24.119  -4.245  1.00 83.63  ?  2   VAL D CB  1 
ATOM 4932 C CG1 . VAL D 2 2   ? 18.831  22.949  -4.688  1.00 83.88  ?  2   VAL D CG1 1 
ATOM 4933 C CG2 . VAL D 2 2   ? 21.159  23.735  -4.257  1.00 80.93  ?  2   VAL D CG2 1 
ATOM 4934 N N   . GLN D 2 3   ? 17.262  26.030  -5.978  1.00 94.76  ?  3   GLN D N   1 
ATOM 4935 C CA  . GLN D 2 3   ? 16.023  26.794  -5.914  1.00 94.43  ?  3   GLN D CA  1 
ATOM 4936 C C   . GLN D 2 3   ? 14.890  26.069  -6.630  1.00 88.96  ?  3   GLN D C   1 
ATOM 4937 O O   . GLN D 2 3   ? 15.108  25.253  -7.533  1.00 85.43  ?  3   GLN D O   1 
ATOM 4938 C CB  . GLN D 2 3   ? 16.199  28.197  -6.518  1.00 96.86  ?  3   GLN D CB  1 
ATOM 4939 C CG  . GLN D 2 3   ? 16.820  29.215  -5.575  1.00 96.72  ?  3   GLN D CG  1 
ATOM 4940 C CD  . GLN D 2 3   ? 16.914  30.595  -6.194  1.00 102.80 ?  3   GLN D CD  1 
ATOM 4941 O OE1 . GLN D 2 3   ? 16.784  30.751  -7.409  1.00 101.96 ?  3   GLN D OE1 1 
ATOM 4942 N NE2 . GLN D 2 3   ? 17.150  31.605  -5.361  1.00 107.53 ?  3   GLN D NE2 1 
ATOM 4943 N N   . LEU D 2 4   ? 13.668  26.408  -6.212  1.00 83.08  ?  4   LEU D N   1 
ATOM 4944 C CA  . LEU D 2 4   ? 12.425  25.995  -6.859  1.00 75.66  ?  4   LEU D CA  1 
ATOM 4945 C C   . LEU D 2 4   ? 11.639  27.257  -7.185  1.00 71.95  ?  4   LEU D C   1 
ATOM 4946 O O   . LEU D 2 4   ? 11.193  27.966  -6.277  1.00 76.71  ?  4   LEU D O   1 
ATOM 4947 C CB  . LEU D 2 4   ? 11.608  25.073  -5.954  1.00 76.95  ?  4   LEU D CB  1 
ATOM 4948 C CG  . LEU D 2 4   ? 12.170  23.703  -5.585  1.00 74.48  ?  4   LEU D CG  1 
ATOM 4949 C CD1 . LEU D 2 4   ? 11.291  23.066  -4.527  1.00 71.57  ?  4   LEU D CD1 1 
ATOM 4950 C CD2 . LEU D 2 4   ? 12.263  22.809  -6.812  1.00 71.76  ?  4   LEU D CD2 1 
ATOM 4951 N N   . VAL D 2 5   ? 11.482  27.551  -8.472  1.00 74.16  ?  5   VAL D N   1 
ATOM 4952 C CA  . VAL D 2 5   ? 10.815  28.765  -8.928  1.00 80.07  ?  5   VAL D CA  1 
ATOM 4953 C C   . VAL D 2 5   ? 9.440   28.382  -9.455  1.00 78.41  ?  5   VAL D C   1 
ATOM 4954 O O   . VAL D 2 5   ? 9.331   27.628  -10.429 1.00 71.49  ?  5   VAL D O   1 
ATOM 4955 C CB  . VAL D 2 5   ? 11.633  29.483  -10.012 1.00 71.53  ?  5   VAL D CB  1 
ATOM 4956 C CG1 . VAL D 2 5   ? 11.070  30.873  -10.269 1.00 69.61  ?  5   VAL D CG1 1 
ATOM 4957 C CG2 . VAL D 2 5   ? 13.101  29.546  -9.618  1.00 69.80  ?  5   VAL D CG2 1 
ATOM 4958 N N   . GLU D 2 6   ? 8.393   28.928  -8.845  1.00 79.39  ?  6   GLU D N   1 
ATOM 4959 C CA  . GLU D 2 6   ? 7.027   28.598  -9.226  1.00 73.31  ?  6   GLU D CA  1 
ATOM 4960 C C   . GLU D 2 6   ? 6.430   29.692  -10.095 1.00 70.30  ?  6   GLU D C   1 
ATOM 4961 O O   . GLU D 2 6   ? 6.583   30.885  -9.814  1.00 71.06  ?  6   GLU D O   1 
ATOM 4962 C CB  . GLU D 2 6   ? 6.143   28.381  -8.002  1.00 67.92  ?  6   GLU D CB  1 
ATOM 4963 C CG  . GLU D 2 6   ? 6.588   27.248  -7.127  1.00 69.62  ?  6   GLU D CG  1 
ATOM 4964 C CD  . GLU D 2 6   ? 5.692   27.081  -5.931  1.00 67.89  ?  6   GLU D CD  1 
ATOM 4965 O OE1 . GLU D 2 6   ? 4.487   27.390  -6.047  1.00 63.63  ?  6   GLU D OE1 1 
ATOM 4966 O OE2 . GLU D 2 6   ? 6.198   26.647  -4.876  1.00 71.43  ?  6   GLU D OE2 1 
ATOM 4967 N N   . SER D 2 7   ? 5.733   29.268  -11.142 1.00 66.35  ?  7   SER D N   1 
ATOM 4968 C CA  . SER D 2 7   ? 5.045   30.160  -12.056 1.00 64.10  ?  7   SER D CA  1 
ATOM 4969 C C   . SER D 2 7   ? 3.648   29.616  -12.329 1.00 62.49  ?  7   SER D C   1 
ATOM 4970 O O   . SER D 2 7   ? 3.330   28.457  -12.034 1.00 56.62  ?  7   SER D O   1 
ATOM 4971 C CB  . SER D 2 7   ? 5.834   30.328  -13.362 1.00 68.32  ?  7   SER D CB  1 
ATOM 4972 O OG  . SER D 2 7   ? 6.145   29.067  -13.935 1.00 68.60  ?  7   SER D OG  1 
ATOM 4973 N N   . GLY D 2 8   ? 2.813   30.470  -12.913 1.00 64.07  ?  8   GLY D N   1 
ATOM 4974 C CA  . GLY D 2 8   ? 1.413   30.166  -13.102 1.00 50.69  ?  8   GLY D CA  1 
ATOM 4975 C C   . GLY D 2 8   ? 0.577   30.617  -11.923 1.00 59.09  ?  8   GLY D C   1 
ATOM 4976 O O   . GLY D 2 8   ? 1.078   31.007  -10.864 1.00 67.48  ?  8   GLY D O   1 
ATOM 4977 N N   . GLY D 2 9   ? -0.731  30.601  -12.129 1.00 54.36  ?  9   GLY D N   1 
ATOM 4978 C CA  . GLY D 2 9   ? -1.613  30.953  -11.038 1.00 59.63  ?  9   GLY D CA  1 
ATOM 4979 C C   . GLY D 2 9   ? -2.131  32.369  -11.083 1.00 57.48  ?  9   GLY D C   1 
ATOM 4980 O O   . GLY D 2 9   ? -1.414  33.296  -11.466 1.00 65.29  ?  9   GLY D O   1 
ATOM 4981 N N   . GLY D 2 10  ? -3.377  32.541  -10.664 1.00 56.07  ?  10  GLY D N   1 
ATOM 4982 C CA  . GLY D 2 10  ? -4.038  33.824  -10.705 1.00 51.42  ?  10  GLY D CA  1 
ATOM 4983 C C   . GLY D 2 10  ? -5.528  33.663  -10.505 1.00 53.19  ?  10  GLY D C   1 
ATOM 4984 O O   . GLY D 2 10  ? -5.960  32.846  -9.687  1.00 53.72  ?  10  GLY D O   1 
ATOM 4985 N N   . LEU D 2 11  ? -6.324  34.432  -11.241 1.00 52.68  ?  11  LEU D N   1 
ATOM 4986 C CA  . LEU D 2 11  ? -7.774  34.369  -11.129 1.00 48.08  ?  11  LEU D CA  1 
ATOM 4987 C C   . LEU D 2 11  ? -8.332  33.327  -12.091 1.00 44.10  ?  11  LEU D C   1 
ATOM 4988 O O   . LEU D 2 11  ? -7.906  33.241  -13.247 1.00 48.36  ?  11  LEU D O   1 
ATOM 4989 C CB  . LEU D 2 11  ? -8.400  35.741  -11.389 1.00 52.23  ?  11  LEU D CB  1 
ATOM 4990 C CG  . LEU D 2 11  ? -9.912  35.798  -11.169 1.00 51.94  ?  11  LEU D CG  1 
ATOM 4991 C CD1 . LEU D 2 11  ? -10.252 35.310  -9.780  1.00 50.35  ?  11  LEU D CD1 1 
ATOM 4992 C CD2 . LEU D 2 11  ? -10.441 37.199  -11.391 1.00 55.81  ?  11  LEU D CD2 1 
ATOM 4993 N N   . VAL D 2 12  ? -9.244  32.504  -11.587 1.00 44.66  ?  12  VAL D N   1 
ATOM 4994 C CA  . VAL D 2 12  ? -9.928  31.477  -12.364 1.00 44.43  ?  12  VAL D CA  1 
ATOM 4995 C C   . VAL D 2 12  ? -11.379 31.434  -11.905 1.00 47.83  ?  12  VAL D C   1 
ATOM 4996 O O   . VAL D 2 12  ? -11.660 31.507  -10.704 1.00 52.79  ?  12  VAL D O   1 
ATOM 4997 C CB  . VAL D 2 12  ? -9.259  30.091  -12.196 1.00 52.89  ?  12  VAL D CB  1 
ATOM 4998 C CG1 . VAL D 2 12  ? -10.079 29.007  -12.881 1.00 54.16  ?  12  VAL D CG1 1 
ATOM 4999 C CG2 . VAL D 2 12  ? -7.834  30.094  -12.736 1.00 53.01  ?  12  VAL D CG2 1 
ATOM 5000 N N   . GLN D 2 13  ? -12.302 31.348  -12.853 1.00 46.44  ?  13  GLN D N   1 
ATOM 5001 C CA  . GLN D 2 13  ? -13.704 31.226  -12.479 1.00 51.70  ?  13  GLN D CA  1 
ATOM 5002 C C   . GLN D 2 13  ? -14.029 29.793  -12.048 1.00 54.46  ?  13  GLN D C   1 
ATOM 5003 O O   . GLN D 2 13  ? -13.364 28.845  -12.476 1.00 53.60  ?  13  GLN D O   1 
ATOM 5004 C CB  . GLN D 2 13  ? -14.599 31.638  -13.634 1.00 53.72  ?  13  GLN D CB  1 
ATOM 5005 C CG  . GLN D 2 13  ? -14.533 33.112  -13.929 1.00 56.35  ?  13  GLN D CG  1 
ATOM 5006 C CD  . GLN D 2 13  ? -15.364 33.480  -15.123 1.00 67.81  ?  13  GLN D CD  1 
ATOM 5007 O OE1 . GLN D 2 13  ? -16.241 32.722  -15.534 1.00 69.00  ?  13  GLN D OE1 1 
ATOM 5008 N NE2 . GLN D 2 13  ? -15.089 34.645  -15.702 1.00 79.91  ?  13  GLN D NE2 1 
ATOM 5009 N N   . PRO D 2 14  ? -15.043 29.611  -11.194 1.00 54.56  ?  14  PRO D N   1 
ATOM 5010 C CA  . PRO D 2 14  ? -15.394 28.260  -10.737 1.00 52.69  ?  14  PRO D CA  1 
ATOM 5011 C C   . PRO D 2 14  ? -15.669 27.327  -11.906 1.00 54.58  ?  14  PRO D C   1 
ATOM 5012 O O   . PRO D 2 14  ? -16.300 27.708  -12.894 1.00 58.82  ?  14  PRO D O   1 
ATOM 5013 C CB  . PRO D 2 14  ? -16.655 28.487  -9.898  1.00 49.43  ?  14  PRO D CB  1 
ATOM 5014 C CG  . PRO D 2 14  ? -16.552 29.895  -9.448  1.00 50.24  ?  14  PRO D CG  1 
ATOM 5015 C CD  . PRO D 2 14  ? -15.898 30.636  -10.570 1.00 53.50  ?  14  PRO D CD  1 
ATOM 5016 N N   . GLY D 2 15  ? -15.179 26.094  -11.786 1.00 55.26  ?  15  GLY D N   1 
ATOM 5017 C CA  . GLY D 2 15  ? -15.205 25.157  -12.886 1.00 61.59  ?  15  GLY D CA  1 
ATOM 5018 C C   . GLY D 2 15  ? -14.095 25.339  -13.896 1.00 60.28  ?  15  GLY D C   1 
ATOM 5019 O O   . GLY D 2 15  ? -13.921 24.473  -14.766 1.00 62.08  ?  15  GLY D O   1 
ATOM 5020 N N   . GLY D 2 16  ? -13.341 26.438  -13.817 1.00 56.45  ?  16  GLY D N   1 
ATOM 5021 C CA  . GLY D 2 16  ? -12.243 26.667  -14.728 1.00 57.07  ?  16  GLY D CA  1 
ATOM 5022 C C   . GLY D 2 16  ? -11.010 25.858  -14.378 1.00 55.07  ?  16  GLY D C   1 
ATOM 5023 O O   . GLY D 2 16  ? -10.941 25.155  -13.370 1.00 55.45  ?  16  GLY D O   1 
ATOM 5024 N N   . SER D 2 17  ? -10.018 25.949  -15.254 1.00 58.31  ?  17  SER D N   1 
ATOM 5025 C CA  . SER D 2 17  ? -8.793  25.184  -15.112 1.00 56.43  ?  17  SER D CA  1 
ATOM 5026 C C   . SER D 2 17  ? -7.605  26.122  -14.959 1.00 55.46  ?  17  SER D C   1 
ATOM 5027 O O   . SER D 2 17  ? -7.661  27.304  -15.316 1.00 53.82  ?  17  SER D O   1 
ATOM 5028 C CB  . SER D 2 17  ? -8.584  24.254  -16.319 1.00 57.08  ?  17  SER D CB  1 
ATOM 5029 O OG  . SER D 2 17  ? -9.658  23.331  -16.432 1.00 55.91  ?  17  SER D OG  1 
ATOM 5030 N N   . LEU D 2 18  ? -6.514  25.566  -14.443 1.00 51.11  ?  18  LEU D N   1 
ATOM 5031 C CA  . LEU D 2 18  ? -5.285  26.319  -14.253 1.00 50.74  ?  18  LEU D CA  1 
ATOM 5032 C C   . LEU D 2 18  ? -4.135  25.328  -14.193 1.00 49.71  ?  18  LEU D C   1 
ATOM 5033 O O   . LEU D 2 18  ? -4.330  24.154  -13.885 1.00 51.16  ?  18  LEU D O   1 
ATOM 5034 C CB  . LEU D 2 18  ? -5.355  27.171  -12.983 1.00 56.49  ?  18  LEU D CB  1 
ATOM 5035 C CG  . LEU D 2 18  ? -4.209  28.137  -12.715 1.00 60.11  ?  18  LEU D CG  1 
ATOM 5036 C CD1 . LEU D 2 18  ? -4.042  29.117  -13.870 1.00 57.59  ?  18  LEU D CD1 1 
ATOM 5037 C CD2 . LEU D 2 18  ? -4.481  28.863  -11.418 1.00 64.04  ?  18  LEU D CD2 1 
ATOM 5038 N N   . ARG D 2 19  ? -2.934  25.801  -14.505 1.00 52.25  ?  19  ARG D N   1 
ATOM 5039 C CA  . ARG D 2 19  ? -1.757  24.942  -14.458 1.00 52.03  ?  19  ARG D CA  1 
ATOM 5040 C C   . ARG D 2 19  ? -0.619  25.697  -13.800 1.00 52.11  ?  19  ARG D C   1 
ATOM 5041 O O   . ARG D 2 19  ? -0.230  26.769  -14.273 1.00 57.06  ?  19  ARG D O   1 
ATOM 5042 C CB  . ARG D 2 19  ? -1.332  24.479  -15.854 1.00 48.13  ?  19  ARG D CB  1 
ATOM 5043 C CG  . ARG D 2 19  ? -0.425  23.258  -15.837 1.00 54.09  ?  19  ARG D CG  1 
ATOM 5044 C CD  . ARG D 2 19  ? 0.053   22.923  -17.234 1.00 61.59  ?  19  ARG D CD  1 
ATOM 5045 N NE  . ARG D 2 19  ? 1.092   23.855  -17.663 1.00 64.90  ?  19  ARG D NE  1 
ATOM 5046 C CZ  . ARG D 2 19  ? 1.633   23.864  -18.877 1.00 68.39  ?  19  ARG D CZ  1 
ATOM 5047 N NH1 . ARG D 2 19  ? 2.579   24.747  -19.178 1.00 66.52  ?  19  ARG D NH1 1 
ATOM 5048 N NH2 . ARG D 2 19  ? 1.210   23.007  -19.796 1.00 61.15  ?  19  ARG D NH2 1 
ATOM 5049 N N   . LEU D 2 20  ? -0.082  25.127  -12.729 1.00 52.33  ?  20  LEU D N   1 
ATOM 5050 C CA  . LEU D 2 20  ? 1.079   25.669  -12.044 1.00 56.16  ?  20  LEU D CA  1 
ATOM 5051 C C   . LEU D 2 20  ? 2.310   24.882  -12.457 1.00 56.83  ?  20  LEU D C   1 
ATOM 5052 O O   . LEU D 2 20  ? 2.228   23.675  -12.712 1.00 56.53  ?  20  LEU D O   1 
ATOM 5053 C CB  . LEU D 2 20  ? 0.908   25.602  -10.525 1.00 60.87  ?  20  LEU D CB  1 
ATOM 5054 C CG  . LEU D 2 20  ? -0.387  26.183  -9.951  1.00 63.59  ?  20  LEU D CG  1 
ATOM 5055 C CD1 . LEU D 2 20  ? -0.441  26.011  -8.443  1.00 56.96  ?  20  LEU D CD1 1 
ATOM 5056 C CD2 . LEU D 2 20  ? -0.524  27.645  -10.324 1.00 54.97  ?  20  LEU D CD2 1 
ATOM 5057 N N   . SER D 2 21  ? 3.443   25.574  -12.540 1.00 57.13  ?  21  SER D N   1 
ATOM 5058 C CA  . SER D 2 21  ? 4.709   24.953  -12.887 1.00 59.71  ?  21  SER D CA  1 
ATOM 5059 C C   . SER D 2 21  ? 5.754   25.333  -11.849 1.00 61.92  ?  21  SER D C   1 
ATOM 5060 O O   . SER D 2 21  ? 5.643   26.361  -11.176 1.00 60.02  ?  21  SER D O   1 
ATOM 5061 C CB  . SER D 2 21  ? 5.176   25.369  -14.284 1.00 55.92  ?  21  SER D CB  1 
ATOM 5062 O OG  . SER D 2 21  ? 5.225   26.778  -14.396 1.00 63.81  ?  21  SER D OG  1 
ATOM 5063 N N   . CYS D 2 22  ? 6.772   24.483  -11.726 1.00 61.82  ?  22  CYS D N   1 
ATOM 5064 C CA  . CYS D 2 22  ? 7.812   24.640  -10.710 1.00 64.39  ?  22  CYS D CA  1 
ATOM 5065 C C   . CYS D 2 22  ? 9.132   24.184  -11.328 1.00 67.85  ?  22  CYS D C   1 
ATOM 5066 O O   . CYS D 2 22  ? 9.356   22.984  -11.506 1.00 73.36  ?  22  CYS D O   1 
ATOM 5067 C CB  . CYS D 2 22  ? 7.464   23.845  -9.460  1.00 69.04  ?  22  CYS D CB  1 
ATOM 5068 S SG  . CYS D 2 22  ? 8.702   23.879  -8.162  1.00 84.72  ?  22  CYS D SG  1 
ATOM 5069 N N   . ALA D 2 23  ? 9.982   25.144  -11.685 1.00 74.39  ?  23  ALA D N   1 
ATOM 5070 C CA  . ALA D 2 23  ? 11.277  24.867  -12.294 1.00 78.05  ?  23  ALA D CA  1 
ATOM 5071 C C   . ALA D 2 23  ? 12.353  24.742  -11.223 1.00 81.24  ?  23  ALA D C   1 
ATOM 5072 O O   . ALA D 2 23  ? 12.468  25.603  -10.346 1.00 84.24  ?  23  ALA D O   1 
ATOM 5073 C CB  . ALA D 2 23  ? 11.646  25.973  -13.284 1.00 72.98  ?  23  ALA D CB  1 
ATOM 5074 N N   . ALA D 2 24  ? 13.152  23.682  -11.310 1.00 83.18  ?  24  ALA D N   1 
ATOM 5075 C CA  . ALA D 2 24  ? 14.233  23.439  -10.366 1.00 85.10  ?  24  ALA D CA  1 
ATOM 5076 C C   . ALA D 2 24  ? 15.562  23.928  -10.927 1.00 88.50  ?  24  ALA D C   1 
ATOM 5077 O O   . ALA D 2 24  ? 15.801  23.882  -12.137 1.00 93.00  ?  24  ALA D O   1 
ATOM 5078 C CB  . ALA D 2 24  ? 14.337  21.951  -10.028 1.00 77.58  ?  24  ALA D CB  1 
ATOM 5079 N N   . SER D 2 25  ? 16.425  24.410  -10.034 1.00 88.43  ?  25  SER D N   1 
ATOM 5080 C CA  . SER D 2 25  ? 17.759  24.860  -10.419 1.00 83.10  ?  25  SER D CA  1 
ATOM 5081 C C   . SER D 2 25  ? 18.752  24.370  -9.379  1.00 88.76  ?  25  SER D C   1 
ATOM 5082 O O   . SER D 2 25  ? 18.596  24.655  -8.187  1.00 93.69  ?  25  SER D O   1 
ATOM 5083 C CB  . SER D 2 25  ? 17.821  26.384  -10.550 1.00 87.28  ?  25  SER D CB  1 
ATOM 5084 O OG  . SER D 2 25  ? 17.719  27.014  -9.286  1.00 86.88  ?  25  SER D OG  1 
ATOM 5085 N N   . GLY D 2 26  ? 19.771  23.640  -9.825  1.00 85.37  ?  26  GLY D N   1 
ATOM 5086 C CA  . GLY D 2 26  ? 20.792  23.116  -8.940  1.00 85.07  ?  26  GLY D CA  1 
ATOM 5087 C C   . GLY D 2 26  ? 20.720  21.626  -8.697  1.00 89.46  ?  26  GLY D C   1 
ATOM 5088 O O   . GLY D 2 26  ? 21.636  21.078  -8.070  1.00 88.11  ?  26  GLY D O   1 
ATOM 5089 N N   . PHE D 2 27  ? 19.661  20.956  -9.147  1.00 92.49  ?  27  PHE D N   1 
ATOM 5090 C CA  . PHE D 2 27  ? 19.520  19.517  -8.961  1.00 84.08  ?  27  PHE D CA  1 
ATOM 5091 C C   . PHE D 2 27  ? 18.521  18.985  -9.979  1.00 80.27  ?  27  PHE D C   1 
ATOM 5092 O O   . PHE D 2 27  ? 17.868  19.745  -10.698 1.00 85.64  ?  27  PHE D O   1 
ATOM 5093 C CB  . PHE D 2 27  ? 19.093  19.172  -7.528  1.00 87.05  ?  27  PHE D CB  1 
ATOM 5094 C CG  . PHE D 2 27  ? 17.662  19.508  -7.222  1.00 87.44  ?  27  PHE D CG  1 
ATOM 5095 C CD1 . PHE D 2 27  ? 17.284  20.815  -6.961  1.00 81.06  ?  27  PHE D CD1 1 
ATOM 5096 C CD2 . PHE D 2 27  ? 16.695  18.515  -7.193  1.00 88.20  ?  27  PHE D CD2 1 
ATOM 5097 C CE1 . PHE D 2 27  ? 15.972  21.127  -6.679  1.00 81.27  ?  27  PHE D CE1 1 
ATOM 5098 C CE2 . PHE D 2 27  ? 15.379  18.822  -6.911  1.00 85.82  ?  27  PHE D CE2 1 
ATOM 5099 C CZ  . PHE D 2 27  ? 15.018  20.130  -6.652  1.00 81.73  ?  27  PHE D CZ  1 
ATOM 5100 N N   . SER D 2 28  ? 18.408  17.661  -10.024 1.00 78.57  ?  28  SER D N   1 
ATOM 5101 C CA  . SER D 2 28  ? 17.528  16.968  -10.956 1.00 85.88  ?  28  SER D CA  1 
ATOM 5102 C C   . SER D 2 28  ? 16.276  16.500  -10.223 1.00 85.31  ?  28  SER D C   1 
ATOM 5103 O O   . SER D 2 28  ? 16.369  15.728  -9.262  1.00 86.28  ?  28  SER D O   1 
ATOM 5104 C CB  . SER D 2 28  ? 18.252  15.783  -11.599 1.00 91.77  ?  28  SER D CB  1 
ATOM 5105 O OG  . SER D 2 28  ? 17.402  15.059  -12.474 1.00 85.38  ?  28  SER D OG  1 
ATOM 5106 N N   . LEU D 2 29  ? 15.111  16.979  -10.672 1.00 83.00  ?  29  LEU D N   1 
ATOM 5107 C CA  . LEU D 2 29  ? 13.846  16.572  -10.067 1.00 80.57  ?  29  LEU D CA  1 
ATOM 5108 C C   . LEU D 2 29  ? 13.571  15.084  -10.216 1.00 81.90  ?  29  LEU D C   1 
ATOM 5109 O O   . LEU D 2 29  ? 12.719  14.550  -9.498  1.00 78.71  ?  29  LEU D O   1 
ATOM 5110 C CB  . LEU D 2 29  ? 12.683  17.338  -10.697 1.00 77.80  ?  29  LEU D CB  1 
ATOM 5111 C CG  . LEU D 2 29  ? 12.570  18.836  -10.445 1.00 78.99  ?  29  LEU D CG  1 
ATOM 5112 C CD1 . LEU D 2 29  ? 11.389  19.399  -11.215 1.00 76.17  ?  29  LEU D CD1 1 
ATOM 5113 C CD2 . LEU D 2 29  ? 12.418  19.099  -8.963  1.00 81.01  ?  29  LEU D CD2 1 
ATOM 5114 N N   . SER D 2 30  ? 14.259  14.406  -11.135 1.00 84.84  ?  30  SER D N   1 
ATOM 5115 C CA  . SER D 2 30  ? 14.059  12.977  -11.327 1.00 84.94  ?  30  SER D CA  1 
ATOM 5116 C C   . SER D 2 30  ? 14.645  12.131  -10.203 1.00 86.06  ?  30  SER D C   1 
ATOM 5117 O O   . SER D 2 30  ? 14.376  10.927  -10.155 1.00 80.94  ?  30  SER D O   1 
ATOM 5118 C CB  . SER D 2 30  ? 14.671  12.552  -12.662 1.00 85.23  ?  30  SER D CB  1 
ATOM 5119 O OG  . SER D 2 30  ? 14.257  13.419  -13.704 1.00 91.99  ?  30  SER D OG  1 
ATOM 5120 N N   . SER D 2 31  ? 15.404  12.727  -9.285  1.00 83.85  ?  31  SER D N   1 
ATOM 5121 C CA  . SER D 2 31  ? 16.065  11.985  -8.220  1.00 84.67  ?  31  SER D CA  1 
ATOM 5122 C C   . SER D 2 31  ? 15.406  12.178  -6.860  1.00 87.08  ?  31  SER D C   1 
ATOM 5123 O O   . SER D 2 31  ? 15.944  11.705  -5.852  1.00 83.43  ?  31  SER D O   1 
ATOM 5124 C CB  . SER D 2 31  ? 17.545  12.374  -8.151  1.00 89.62  ?  31  SER D CB  1 
ATOM 5125 O OG  . SER D 2 31  ? 17.706  13.782  -8.068  1.00 94.19  ?  31  SER D OG  1 
ATOM 5126 N N   . TYR D 2 32  ? 14.264  12.865  -6.800  1.00 86.27  ?  32  TYR D N   1 
ATOM 5127 C CA  . TYR D 2 32  ? 13.588  13.132  -5.538  1.00 82.37  ?  32  TYR D CA  1 
ATOM 5128 C C   . TYR D 2 32  ? 12.084  12.961  -5.707  1.00 77.33  ?  32  TYR D C   1 
ATOM 5129 O O   . TYR D 2 32  ? 11.543  13.088  -6.807  1.00 77.91  ?  32  TYR D O   1 
ATOM 5130 C CB  . TYR D 2 32  ? 13.881  14.552  -5.026  1.00 78.88  ?  32  TYR D CB  1 
ATOM 5131 C CG  . TYR D 2 32  ? 15.322  14.817  -4.644  1.00 84.63  ?  32  TYR D CG  1 
ATOM 5132 C CD1 . TYR D 2 32  ? 15.809  14.440  -3.395  1.00 84.16  ?  32  TYR D CD1 1 
ATOM 5133 C CD2 . TYR D 2 32  ? 16.187  15.468  -5.521  1.00 83.42  ?  32  TYR D CD2 1 
ATOM 5134 C CE1 . TYR D 2 32  ? 17.123  14.689  -3.032  1.00 85.80  ?  32  TYR D CE1 1 
ATOM 5135 C CE2 . TYR D 2 32  ? 17.504  15.722  -5.168  1.00 87.77  ?  32  TYR D CE2 1 
ATOM 5136 C CZ  . TYR D 2 32  ? 17.967  15.330  -3.920  1.00 88.28  ?  32  TYR D CZ  1 
ATOM 5137 O OH  . TYR D 2 32  ? 19.275  15.577  -3.558  1.00 81.23  ?  32  TYR D OH  1 
ATOM 5138 N N   . TYR D 2 33  ? 11.411  12.664  -4.595  1.00 76.79  ?  33  TYR D N   1 
ATOM 5139 C CA  . TYR D 2 33  ? 9.967   12.843  -4.524  1.00 73.62  ?  33  TYR D CA  1 
ATOM 5140 C C   . TYR D 2 33  ? 9.640   14.328  -4.633  1.00 72.25  ?  33  TYR D C   1 
ATOM 5141 O O   . TYR D 2 33  ? 10.363  15.172  -4.096  1.00 69.32  ?  33  TYR D O   1 
ATOM 5142 C CB  . TYR D 2 33  ? 9.417   12.296  -3.204  1.00 75.53  ?  33  TYR D CB  1 
ATOM 5143 C CG  . TYR D 2 33  ? 9.348   10.787  -3.079  1.00 79.98  ?  33  TYR D CG  1 
ATOM 5144 C CD1 . TYR D 2 33  ? 8.140   10.153  -2.807  1.00 80.77  ?  33  TYR D CD1 1 
ATOM 5145 C CD2 . TYR D 2 33  ? 10.483  9.998   -3.218  1.00 79.30  ?  33  TYR D CD2 1 
ATOM 5146 C CE1 . TYR D 2 33  ? 8.062   8.777   -2.682  1.00 79.44  ?  33  TYR D CE1 1 
ATOM 5147 C CE2 . TYR D 2 33  ? 10.414  8.620   -3.093  1.00 80.14  ?  33  TYR D CE2 1 
ATOM 5148 C CZ  . TYR D 2 33  ? 9.200   8.016   -2.825  1.00 79.94  ?  33  TYR D CZ  1 
ATOM 5149 O OH  . TYR D 2 33  ? 9.121   6.648   -2.702  1.00 82.46  ?  33  TYR D OH  1 
ATOM 5150 N N   . MET D 2 34  ? 8.551   14.660  -5.327  1.00 67.59  ?  34  MET D N   1 
ATOM 5151 C CA  . MET D 2 34  ? 8.135   16.055  -5.413  1.00 62.14  ?  34  MET D CA  1 
ATOM 5152 C C   . MET D 2 34  ? 6.691   16.183  -4.959  1.00 62.96  ?  34  MET D C   1 
ATOM 5153 O O   . MET D 2 34  ? 5.903   15.248  -5.100  1.00 58.48  ?  34  MET D O   1 
ATOM 5154 C CB  . MET D 2 34  ? 8.291   16.625  -6.831  1.00 60.91  ?  34  MET D CB  1 
ATOM 5155 C CG  . MET D 2 34  ? 9.732   16.783  -7.271  1.00 63.66  ?  34  MET D CG  1 
ATOM 5156 S SD  . MET D 2 34  ? 10.720  17.695  -6.066  1.00 62.81  ?  34  MET D SD  1 
ATOM 5157 C CE  . MET D 2 34  ? 10.019  19.335  -6.199  1.00 67.96  ?  34  MET D CE  1 
ATOM 5158 N N   . THR D 2 35  ? 6.337   17.357  -4.435  1.00 63.56  ?  35  THR D N   1 
ATOM 5159 C CA  . THR D 2 35  ? 5.030   17.495  -3.812  1.00 64.15  ?  35  THR D CA  1 
ATOM 5160 C C   . THR D 2 35  ? 4.493   18.907  -4.007  1.00 60.16  ?  35  THR D C   1 
ATOM 5161 O O   . THR D 2 35  ? 5.252   19.875  -4.103  1.00 67.46  ?  35  THR D O   1 
ATOM 5162 C CB  . THR D 2 35  ? 5.093   17.132  -2.320  1.00 62.49  ?  35  THR D CB  1 
ATOM 5163 O OG1 . THR D 2 35  ? 3.785   17.221  -1.745  1.00 68.65  ?  35  THR D OG1 1 
ATOM 5164 C CG2 . THR D 2 35  ? 6.034   18.056  -1.577  1.00 63.05  ?  35  THR D CG2 1 
ATOM 5165 N N   . TRP D 2 36  ? 3.171   19.002  -4.103  1.00 56.47  ?  36  TRP D N   1 
ATOM 5166 C CA  . TRP D 2 36  ? 2.451   20.268  -4.040  1.00 59.73  ?  36  TRP D CA  1 
ATOM 5167 C C   . TRP D 2 36  ? 1.670   20.325  -2.737  1.00 57.97  ?  36  TRP D C   1 
ATOM 5168 O O   . TRP D 2 36  ? 0.976   19.360  -2.387  1.00 61.22  ?  36  TRP D O   1 
ATOM 5169 C CB  . TRP D 2 36  ? 1.496   20.434  -5.224  1.00 57.31  ?  36  TRP D CB  1 
ATOM 5170 C CG  . TRP D 2 36  ? 2.178   20.710  -6.517  1.00 56.46  ?  36  TRP D CG  1 
ATOM 5171 C CD1 . TRP D 2 36  ? 2.492   19.806  -7.483  1.00 54.49  ?  36  TRP D CD1 1 
ATOM 5172 C CD2 . TRP D 2 36  ? 2.640   21.980  -6.989  1.00 59.35  ?  36  TRP D CD2 1 
ATOM 5173 N NE1 . TRP D 2 36  ? 3.118   20.432  -8.529  1.00 54.60  ?  36  TRP D NE1 1 
ATOM 5174 C CE2 . TRP D 2 36  ? 3.222   21.768  -8.251  1.00 54.08  ?  36  TRP D CE2 1 
ATOM 5175 C CE3 . TRP D 2 36  ? 2.620   23.277  -6.465  1.00 60.27  ?  36  TRP D CE3 1 
ATOM 5176 C CZ2 . TRP D 2 36  ? 3.776   22.798  -9.000  1.00 55.38  ?  36  TRP D CZ2 1 
ATOM 5177 C CZ3 . TRP D 2 36  ? 3.169   24.299  -7.210  1.00 57.74  ?  36  TRP D CZ3 1 
ATOM 5178 C CH2 . TRP D 2 36  ? 3.740   24.054  -8.466  1.00 59.03  ?  36  TRP D CH2 1 
ATOM 5179 N N   . VAL D 2 37  ? 1.793   21.450  -2.027  1.00 56.62  ?  37  VAL D N   1 
ATOM 5180 C CA  . VAL D 2 37  ? 1.139   21.669  -0.739  1.00 54.91  ?  37  VAL D CA  1 
ATOM 5181 C C   . VAL D 2 37  ? 0.523   23.061  -0.730  1.00 51.82  ?  37  VAL D C   1 
ATOM 5182 O O   . VAL D 2 37  ? 1.204   24.045  -1.028  1.00 52.38  ?  37  VAL D O   1 
ATOM 5183 C CB  . VAL D 2 37  ? 2.127   21.517  0.433   1.00 54.96  ?  37  VAL D CB  1 
ATOM 5184 C CG1 . VAL D 2 37  ? 1.536   22.094  1.703   1.00 55.63  ?  37  VAL D CG1 1 
ATOM 5185 C CG2 . VAL D 2 37  ? 2.483   20.054  0.634   1.00 60.88  ?  37  VAL D CG2 1 
ATOM 5186 N N   . ARG D 2 38  ? -0.752  23.152  -0.369  1.00 50.84  ?  38  ARG D N   1 
ATOM 5187 C CA  . ARG D 2 38  ? -1.444  24.432  -0.383  1.00 47.99  ?  38  ARG D CA  1 
ATOM 5188 C C   . ARG D 2 38  ? -1.690  24.950  1.027   1.00 52.00  ?  38  ARG D C   1 
ATOM 5189 O O   . ARG D 2 38  ? -1.591  24.221  2.020   1.00 49.38  ?  38  ARG D O   1 
ATOM 5190 C CB  . ARG D 2 38  ? -2.774  24.326  -1.131  1.00 46.99  ?  38  ARG D CB  1 
ATOM 5191 C CG  . ARG D 2 38  ? -3.880  23.615  -0.378  1.00 43.15  ?  38  ARG D CG  1 
ATOM 5192 C CD  . ARG D 2 38  ? -5.105  23.524  -1.272  1.00 51.36  ?  38  ARG D CD  1 
ATOM 5193 N NE  . ARG D 2 38  ? -6.225  22.858  -0.621  1.00 60.07  ?  38  ARG D NE  1 
ATOM 5194 C CZ  . ARG D 2 38  ? -7.395  22.630  -1.209  1.00 61.19  ?  38  ARG D CZ  1 
ATOM 5195 N NH1 . ARG D 2 38  ? -8.361  22.013  -0.537  1.00 66.66  ?  38  ARG D NH1 1 
ATOM 5196 N NH2 . ARG D 2 38  ? -7.591  23.004  -2.468  1.00 45.79  ?  38  ARG D NH2 1 
ATOM 5197 N N   . GLN D 2 39  ? -2.001  26.242  1.096   1.00 54.27  ?  39  GLN D N   1 
ATOM 5198 C CA  . GLN D 2 39  ? -2.337  26.888  2.360   1.00 50.83  ?  39  GLN D CA  1 
ATOM 5199 C C   . GLN D 2 39  ? -3.320  28.012  2.073   1.00 51.17  ?  39  GLN D C   1 
ATOM 5200 O O   . GLN D 2 39  ? -2.978  28.966  1.367   1.00 48.89  ?  39  GLN D O   1 
ATOM 5201 C CB  . GLN D 2 39  ? -1.082  27.421  3.045   1.00 45.76  ?  39  GLN D CB  1 
ATOM 5202 C CG  . GLN D 2 39  ? -1.354  28.154  4.326   1.00 49.55  ?  39  GLN D CG  1 
ATOM 5203 C CD  . GLN D 2 39  ? -0.082  28.606  5.012   1.00 53.64  ?  39  GLN D CD  1 
ATOM 5204 O OE1 . GLN D 2 39  ? 0.899   28.971  4.360   1.00 54.97  ?  39  GLN D OE1 1 
ATOM 5205 N NE2 . GLN D 2 39  ? -0.086  28.568  6.336   1.00 56.42  ?  39  GLN D NE2 1 
ATOM 5206 N N   . ALA D 2 40  ? -4.543  27.883  2.584   1.00 50.10  ?  40  ALA D N   1 
ATOM 5207 C CA  . ALA D 2 40  ? -5.548  28.916  2.400   1.00 43.61  ?  40  ALA D CA  1 
ATOM 5208 C C   . ALA D 2 40  ? -5.239  30.116  3.292   1.00 50.11  ?  40  ALA D C   1 
ATOM 5209 O O   . ALA D 2 40  ? -4.481  30.000  4.257   1.00 48.49  ?  40  ALA D O   1 
ATOM 5210 C CB  . ALA D 2 40  ? -6.935  28.363  2.709   1.00 38.60  ?  40  ALA D CB  1 
ATOM 5211 N N   . PRO D 2 41  ? -5.788  31.290  2.972   1.00 60.04  ?  41  PRO D N   1 
ATOM 5212 C CA  . PRO D 2 41  ? -5.528  32.474  3.808   1.00 55.62  ?  41  PRO D CA  1 
ATOM 5213 C C   . PRO D 2 41  ? -5.954  32.240  5.250   1.00 53.04  ?  41  PRO D C   1 
ATOM 5214 O O   . PRO D 2 41  ? -7.071  31.793  5.526   1.00 52.04  ?  41  PRO D O   1 
ATOM 5215 C CB  . PRO D 2 41  ? -6.364  33.572  3.139   1.00 50.61  ?  41  PRO D CB  1 
ATOM 5216 C CG  . PRO D 2 41  ? -6.467  33.136  1.710   1.00 49.46  ?  41  PRO D CG  1 
ATOM 5217 C CD  . PRO D 2 41  ? -6.541  31.635  1.749   1.00 50.36  ?  41  PRO D CD  1 
ATOM 5218 N N   . GLY D 2 42  ? -5.033  32.508  6.171   1.00 56.29  ?  42  GLY D N   1 
ATOM 5219 C CA  . GLY D 2 42  ? -5.326  32.339  7.580   1.00 58.52  ?  42  GLY D CA  1 
ATOM 5220 C C   . GLY D 2 42  ? -5.590  30.911  8.000   1.00 59.22  ?  42  GLY D C   1 
ATOM 5221 O O   . GLY D 2 42  ? -6.313  30.682  8.975   1.00 67.01  ?  42  GLY D O   1 
ATOM 5222 N N   . LYS D 2 43  ? -5.034  29.938  7.287   1.00 51.32  ?  43  LYS D N   1 
ATOM 5223 C CA  . LYS D 2 43  ? -5.235  28.531  7.599   1.00 54.68  ?  43  LYS D CA  1 
ATOM 5224 C C   . LYS D 2 43  ? -3.892  27.814  7.621   1.00 49.05  ?  43  LYS D C   1 
ATOM 5225 O O   . LYS D 2 43  ? -2.833  28.414  7.422   1.00 48.78  ?  43  LYS D O   1 
ATOM 5226 C CB  . LYS D 2 43  ? -6.183  27.876  6.589   1.00 55.39  ?  43  LYS D CB  1 
ATOM 5227 C CG  . LYS D 2 43  ? -7.602  28.411  6.619   1.00 60.78  ?  43  LYS D CG  1 
ATOM 5228 C CD  . LYS D 2 43  ? -8.512  27.492  5.823   1.00 68.54  ?  43  LYS D CD  1 
ATOM 5229 C CE  . LYS D 2 43  ? -8.691  26.138  6.475   1.00 69.85  ?  43  LYS D CE  1 
ATOM 5230 N NZ  . LYS D 2 43  ? -9.686  25.334  5.708   1.00 78.91  ?  43  LYS D NZ  1 
ATOM 5231 N N   . GLY D 2 44  ? -3.949  26.506  7.854   1.00 40.78  ?  44  GLY D N   1 
ATOM 5232 C CA  . GLY D 2 44  ? -2.753  25.706  7.972   1.00 49.40  ?  44  GLY D CA  1 
ATOM 5233 C C   . GLY D 2 44  ? -2.270  25.159  6.641   1.00 56.96  ?  44  GLY D C   1 
ATOM 5234 O O   . GLY D 2 44  ? -2.821  25.425  5.571   1.00 57.63  ?  44  GLY D O   1 
ATOM 5235 N N   . LEU D 2 45  ? -1.210  24.364  6.729   1.00 52.68  ?  45  LEU D N   1 
ATOM 5236 C CA  . LEU D 2 45  ? -0.651  23.714  5.558   1.00 46.13  ?  45  LEU D CA  1 
ATOM 5237 C C   . LEU D 2 45  ? -1.471  22.471  5.261   1.00 51.01  ?  45  LEU D C   1 
ATOM 5238 O O   . LEU D 2 45  ? -1.834  21.727  6.175   1.00 55.69  ?  45  LEU D O   1 
ATOM 5239 C CB  . LEU D 2 45  ? 0.814   23.350  5.787   1.00 45.09  ?  45  LEU D CB  1 
ATOM 5240 C CG  . LEU D 2 45  ? 1.792   24.518  5.905   1.00 51.56  ?  45  LEU D CG  1 
ATOM 5241 C CD1 . LEU D 2 45  ? 3.194   24.000  6.139   1.00 52.30  ?  45  LEU D CD1 1 
ATOM 5242 C CD2 . LEU D 2 45  ? 1.747   25.393  4.655   1.00 56.07  ?  45  LEU D CD2 1 
ATOM 5243 N N   . GLU D 2 46  ? -1.804  22.278  3.988   1.00 51.41  ?  46  GLU D N   1 
ATOM 5244 C CA  . GLU D 2 46  ? -2.627  21.161  3.549   1.00 48.47  ?  46  GLU D CA  1 
ATOM 5245 C C   . GLU D 2 46  ? -1.900  20.453  2.414   1.00 58.86  ?  46  GLU D C   1 
ATOM 5246 O O   . GLU D 2 46  ? -1.641  21.054  1.365   1.00 60.70  ?  46  GLU D O   1 
ATOM 5247 C CB  . GLU D 2 46  ? -4.011  21.644  3.100   1.00 50.32  ?  46  GLU D CB  1 
ATOM 5248 C CG  . GLU D 2 46  ? -5.091  20.580  3.118   1.00 50.88  ?  46  GLU D CG  1 
ATOM 5249 C CD  . GLU D 2 46  ? -6.430  21.096  2.609   1.00 61.70  ?  46  GLU D CD  1 
ATOM 5250 O OE1 . GLU D 2 46  ? -6.443  22.120  1.884   1.00 60.11  ?  46  GLU D OE1 1 
ATOM 5251 O OE2 . GLU D 2 46  ? -7.468  20.474  2.931   1.00 60.61  ?  46  GLU D OE2 1 
ATOM 5252 N N   . TRP D 2 47  ? -1.560  19.190  2.627   1.00 59.26  ?  47  TRP D N   1 
ATOM 5253 C CA  . TRP D 2 47  ? -0.907  18.414  1.585   1.00 59.21  ?  47  TRP D CA  1 
ATOM 5254 C C   . TRP D 2 47  ? -1.861  18.232  0.412   1.00 62.33  ?  47  TRP D C   1 
ATOM 5255 O O   . TRP D 2 47  ? -3.038  17.918  0.610   1.00 67.69  ?  47  TRP D O   1 
ATOM 5256 C CB  . TRP D 2 47  ? -0.473  17.060  2.144   1.00 65.36  ?  47  TRP D CB  1 
ATOM 5257 C CG  . TRP D 2 47  ? 0.037   16.117  1.120   1.00 61.47  ?  47  TRP D CG  1 
ATOM 5258 C CD1 . TRP D 2 47  ? 1.287   16.098  0.574   1.00 64.45  ?  47  TRP D CD1 1 
ATOM 5259 C CD2 . TRP D 2 47  ? -0.683  15.035  0.519   1.00 68.66  ?  47  TRP D CD2 1 
ATOM 5260 N NE1 . TRP D 2 47  ? 1.388   15.075  -0.344  1.00 72.04  ?  47  TRP D NE1 1 
ATOM 5261 C CE2 . TRP D 2 47  ? 0.191   14.407  -0.395  1.00 69.85  ?  47  TRP D CE2 1 
ATOM 5262 C CE3 . TRP D 2 47  ? -1.984  14.539  0.657   1.00 71.28  ?  47  TRP D CE3 1 
ATOM 5263 C CZ2 . TRP D 2 47  ? -0.193  13.309  -1.161  1.00 64.38  ?  47  TRP D CZ2 1 
ATOM 5264 C CZ3 . TRP D 2 47  ? -2.364  13.447  -0.109  1.00 71.74  ?  47  TRP D CZ3 1 
ATOM 5265 C CH2 . TRP D 2 47  ? -1.472  12.846  -1.005  1.00 68.07  ?  47  TRP D CH2 1 
ATOM 5266 N N   . VAL D 2 48  ? -1.372  18.459  -0.809  1.00 61.40  ?  48  VAL D N   1 
ATOM 5267 C CA  . VAL D 2 48  ? -2.191  18.353  -2.019  1.00 59.50  ?  48  VAL D CA  1 
ATOM 5268 C C   . VAL D 2 48  ? -1.850  17.091  -2.805  1.00 65.76  ?  48  VAL D C   1 
ATOM 5269 O O   . VAL D 2 48  ? -2.714  16.245  -3.042  1.00 68.45  ?  48  VAL D O   1 
ATOM 5270 C CB  . VAL D 2 48  ? -2.066  19.610  -2.910  1.00 52.67  ?  48  VAL D CB  1 
ATOM 5271 C CG1 . VAL D 2 48  ? -2.928  19.453  -4.143  1.00 53.61  ?  48  VAL D CG1 1 
ATOM 5272 C CG2 . VAL D 2 48  ? -2.456  20.856  -2.160  1.00 56.25  ?  48  VAL D CG2 1 
ATOM 5273 N N   . SER D 2 49  ? -0.597  16.958  -3.240  1.00 67.63  ?  49  SER D N   1 
ATOM 5274 C CA  . SER D 2 49  ? -0.268  15.850  -4.134  1.00 68.04  ?  49  SER D CA  1 
ATOM 5275 C C   . SER D 2 49  ? 1.220   15.536  -4.059  1.00 66.82  ?  49  SER D C   1 
ATOM 5276 O O   . SER D 2 49  ? 2.032   16.387  -3.689  1.00 66.31  ?  49  SER D O   1 
ATOM 5277 C CB  . SER D 2 49  ? -0.675  16.169  -5.576  1.00 65.84  ?  49  SER D CB  1 
ATOM 5278 O OG  . SER D 2 49  ? -0.342  15.104  -6.444  1.00 66.36  ?  49  SER D OG  1 
ATOM 5279 N N   . VAL D 2 50  ? 1.569   14.299  -4.425  1.00 61.57  ?  50  VAL D N   1 
ATOM 5280 C CA  . VAL D 2 50  ? 2.962   13.860  -4.458  1.00 63.32  ?  50  VAL D CA  1 
ATOM 5281 C C   . VAL D 2 50  ? 3.198   13.020  -5.706  1.00 68.27  ?  50  VAL D C   1 
ATOM 5282 O O   . VAL D 2 50  ? 2.329   12.245  -6.125  1.00 71.82  ?  50  VAL D O   1 
ATOM 5283 C CB  . VAL D 2 50  ? 3.354   13.066  -3.191  1.00 68.30  ?  50  VAL D CB  1 
ATOM 5284 C CG1 . VAL D 2 50  ? 2.536   11.793  -3.072  1.00 72.93  ?  50  VAL D CG1 1 
ATOM 5285 C CG2 . VAL D 2 50  ? 4.842   12.740  -3.198  1.00 60.78  ?  50  VAL D CG2 1 
ATOM 5286 N N   . ILE D 2 51  ? 4.368   13.195  -6.319  1.00 67.13  ?  51  ILE D N   1 
ATOM 5287 C CA  . ILE D 2 51  ? 4.829   12.331  -7.396  1.00 66.73  ?  51  ILE D CA  1 
ATOM 5288 C C   . ILE D 2 51  ? 6.123   11.656  -6.957  1.00 67.84  ?  51  ILE D C   1 
ATOM 5289 O O   . ILE D 2 51  ? 7.025   12.293  -6.391  1.00 68.25  ?  51  ILE D O   1 
ATOM 5290 C CB  . ILE D 2 51  ? 5.017   13.089  -8.728  1.00 68.67  ?  51  ILE D CB  1 
ATOM 5291 C CG1 . ILE D 2 51  ? 5.298   12.096  -9.858  1.00 66.57  ?  51  ILE D CG1 1 
ATOM 5292 C CG2 . ILE D 2 51  ? 6.134   14.119  -8.633  1.00 63.02  ?  51  ILE D CG2 1 
ATOM 5293 C CD1 . ILE D 2 51  ? 5.374   12.723  -11.219 1.00 64.33  ?  51  ILE D CD1 1 
ATOM 5294 N N   . ASN D 2 52  ? 6.200   10.360  -7.242  1.00 72.94  ?  52  ASN D N   1 
ATOM 5295 C CA  . ASN D 2 52  ? 7.250   9.448   -6.830  1.00 78.54  ?  52  ASN D CA  1 
ATOM 5296 C C   . ASN D 2 52  ? 8.452   9.556   -7.767  1.00 80.71  ?  52  ASN D C   1 
ATOM 5297 O O   . ASN D 2 52  ? 8.432   10.268  -8.774  1.00 83.73  ?  52  ASN D O   1 
ATOM 5298 C CB  . ASN D 2 52  ? 6.701   8.018   -6.820  1.00 83.51  ?  52  ASN D CB  1 
ATOM 5299 C CG  . ASN D 2 52  ? 7.548   7.061   -6.010  1.00 90.46  ?  52  ASN D CG  1 
ATOM 5300 O OD1 . ASN D 2 52  ? 8.756   7.250   -5.860  1.00 93.70  ?  52  ASN D OD1 1 
ATOM 5301 N ND2 . ASN D 2 52  ? 6.914   6.018   -5.480  1.00 99.51  ?  52  ASN D ND2 1 
ATOM 5302 N N   . VAL D 2 53  ? 9.520   8.842   -7.413  1.00 79.72  ?  53  VAL D N   1 
ATOM 5303 C CA  . VAL D 2 53  ? 10.667  8.751   -8.308  1.00 81.50  ?  53  VAL D CA  1 
ATOM 5304 C C   . VAL D 2 53  ? 10.373  7.801   -9.465  1.00 84.35  ?  53  VAL D C   1 
ATOM 5305 O O   . VAL D 2 53  ? 10.953  7.941   -10.549 1.00 83.99  ?  53  VAL D O   1 
ATOM 5306 C CB  . VAL D 2 53  ? 11.926  8.331   -7.529  1.00 81.64  ?  53  VAL D CB  1 
ATOM 5307 C CG1 . VAL D 2 53  ? 11.812  6.893   -7.047  1.00 88.96  ?  53  VAL D CG1 1 
ATOM 5308 C CG2 . VAL D 2 53  ? 13.166  8.513   -8.387  1.00 76.32  ?  53  VAL D CG2 1 
ATOM 5309 N N   . TYR D 2 54  ? 9.458   6.845   -9.275  1.00 85.38  ?  54  TYR D N   1 
ATOM 5310 C CA  . TYR D 2 54  ? 9.065   5.964   -10.367 1.00 87.60  ?  54  TYR D CA  1 
ATOM 5311 C C   . TYR D 2 54  ? 8.064   6.621   -11.304 1.00 82.81  ?  54  TYR D C   1 
ATOM 5312 O O   . TYR D 2 54  ? 7.897   6.158   -12.437 1.00 77.89  ?  54  TYR D O   1 
ATOM 5313 C CB  . TYR D 2 54  ? 8.451   4.665   -9.829  1.00 92.36  ?  54  TYR D CB  1 
ATOM 5314 C CG  . TYR D 2 54  ? 9.245   3.973   -8.740  1.00 99.23  ?  54  TYR D CG  1 
ATOM 5315 C CD1 . TYR D 2 54  ? 10.335  3.166   -9.047  1.00 100.90 ?  54  TYR D CD1 1 
ATOM 5316 C CD2 . TYR D 2 54  ? 8.880   4.101   -7.400  1.00 103.86 ?  54  TYR D CD2 1 
ATOM 5317 C CE1 . TYR D 2 54  ? 11.054  2.526   -8.048  1.00 102.20 ?  54  TYR D CE1 1 
ATOM 5318 C CE2 . TYR D 2 54  ? 9.591   3.463   -6.394  1.00 100.09 ?  54  TYR D CE2 1 
ATOM 5319 C CZ  . TYR D 2 54  ? 10.676  2.676   -6.725  1.00 99.48  ?  54  TYR D CZ  1 
ATOM 5320 O OH  . TYR D 2 54  ? 11.385  2.039   -5.733  1.00 94.34  ?  54  TYR D OH  1 
ATOM 5321 N N   . GLY D 2 55  ? 7.398   7.684   -10.856 1.00 81.08  ?  55  GLY D N   1 
ATOM 5322 C CA  . GLY D 2 55  ? 6.318   8.301   -11.598 1.00 77.17  ?  55  GLY D CA  1 
ATOM 5323 C C   . GLY D 2 55  ? 4.949   8.061   -11.008 1.00 69.72  ?  55  GLY D C   1 
ATOM 5324 O O   . GLY D 2 55  ? 3.958   8.534   -11.576 1.00 62.52  ?  55  GLY D O   1 
ATOM 5325 N N   . GLY D 2 56  ? 4.859   7.334   -9.898  1.00 72.35  ?  56  GLY D N   1 
ATOM 5326 C CA  . GLY D 2 56  ? 3.568   7.096   -9.277  1.00 79.13  ?  56  GLY D CA  1 
ATOM 5327 C C   . GLY D 2 56  ? 3.040   8.357   -8.617  1.00 77.48  ?  56  GLY D C   1 
ATOM 5328 O O   . GLY D 2 56  ? 3.758   9.036   -7.873  1.00 73.14  ?  56  GLY D O   1 
ATOM 5329 N N   . THR D 2 57  ? 1.768   8.655   -8.859  1.00 76.62  ?  57  THR D N   1 
ATOM 5330 C CA  . THR D 2 57  ? 1.140   9.888   -8.404  1.00 73.14  ?  57  THR D CA  1 
ATOM 5331 C C   . THR D 2 57  ? 0.124   9.551   -7.323  1.00 76.68  ?  57  THR D C   1 
ATOM 5332 O O   . THR D 2 57  ? -0.795  8.759   -7.558  1.00 81.05  ?  57  THR D O   1 
ATOM 5333 C CB  . THR D 2 57  ? 0.459   10.603  -9.570  1.00 72.36  ?  57  THR D CB  1 
ATOM 5334 O OG1 . THR D 2 57  ? -0.541  9.743   -10.130 1.00 76.26  ?  57  THR D OG1 1 
ATOM 5335 C CG2 . THR D 2 57  ? 1.476   10.957  -10.650 1.00 63.74  ?  57  THR D CG2 1 
ATOM 5336 N N   . TYR D 2 58  ? 0.280   10.159  -6.148  1.00 78.56  ?  58  TYR D N   1 
ATOM 5337 C CA  . TYR D 2 58  ? -0.660  9.992   -5.049  1.00 79.75  ?  58  TYR D CA  1 
ATOM 5338 C C   . TYR D 2 58  ? -1.314  11.329  -4.724  1.00 73.22  ?  58  TYR D C   1 
ATOM 5339 O O   . TYR D 2 58  ? -0.636  12.361  -4.636  1.00 72.84  ?  58  TYR D O   1 
ATOM 5340 C CB  . TYR D 2 58  ? 0.035   9.418   -3.812  1.00 84.57  ?  58  TYR D CB  1 
ATOM 5341 C CG  . TYR D 2 58  ? 0.516   7.996   -4.000  1.00 90.19  ?  58  TYR D CG  1 
ATOM 5342 C CD1 . TYR D 2 58  ? -0.326  6.920   -3.758  1.00 91.60  ?  58  TYR D CD1 1 
ATOM 5343 C CD2 . TYR D 2 58  ? 1.812   7.730   -4.427  1.00 90.55  ?  58  TYR D CD2 1 
ATOM 5344 C CE1 . TYR D 2 58  ? 0.110   5.620   -3.931  1.00 90.69  ?  58  TYR D CE1 1 
ATOM 5345 C CE2 . TYR D 2 58  ? 2.257   6.433   -4.603  1.00 88.66  ?  58  TYR D CE2 1 
ATOM 5346 C CZ  . TYR D 2 58  ? 1.401   5.382   -4.352  1.00 90.07  ?  58  TYR D CZ  1 
ATOM 5347 O OH  . TYR D 2 58  ? 1.834   4.088   -4.524  1.00 99.04  ?  58  TYR D OH  1 
ATOM 5348 N N   . TYR D 2 59  ? -2.628  11.302  -4.532  1.00 70.89  ?  59  TYR D N   1 
ATOM 5349 C CA  . TYR D 2 59  ? -3.422  12.499  -4.294  1.00 73.25  ?  59  TYR D CA  1 
ATOM 5350 C C   . TYR D 2 59  ? -4.164  12.389  -2.966  1.00 76.74  ?  59  TYR D C   1 
ATOM 5351 O O   . TYR D 2 59  ? -4.072  11.388  -2.252  1.00 80.24  ?  59  TYR D O   1 
ATOM 5352 C CB  . TYR D 2 59  ? -4.405  12.728  -5.446  1.00 70.39  ?  59  TYR D CB  1 
ATOM 5353 C CG  . TYR D 2 59  ? -3.734  12.875  -6.789  1.00 66.69  ?  59  TYR D CG  1 
ATOM 5354 C CD1 . TYR D 2 59  ? -3.374  14.124  -7.273  1.00 63.55  ?  59  TYR D CD1 1 
ATOM 5355 C CD2 . TYR D 2 59  ? -3.447  11.764  -7.568  1.00 66.06  ?  59  TYR D CD2 1 
ATOM 5356 C CE1 . TYR D 2 59  ? -2.753  14.265  -8.499  1.00 66.34  ?  59  TYR D CE1 1 
ATOM 5357 C CE2 . TYR D 2 59  ? -2.831  11.893  -8.795  1.00 68.13  ?  59  TYR D CE2 1 
ATOM 5358 C CZ  . TYR D 2 59  ? -2.484  13.145  -9.257  1.00 65.78  ?  59  TYR D CZ  1 
ATOM 5359 O OH  . TYR D 2 59  ? -1.864  13.276  -10.479 1.00 60.29  ?  59  TYR D OH  1 
ATOM 5360 N N   . ALA D 2 60  ? -4.905  13.445  -2.641  1.00 79.79  ?  60  ALA D N   1 
ATOM 5361 C CA  . ALA D 2 60  ? -5.720  13.503  -1.439  1.00 75.31  ?  60  ALA D CA  1 
ATOM 5362 C C   . ALA D 2 60  ? -7.184  13.255  -1.788  1.00 78.54  ?  60  ALA D C   1 
ATOM 5363 O O   . ALA D 2 60  ? -7.585  13.268  -2.954  1.00 82.09  ?  60  ALA D O   1 
ATOM 5364 C CB  . ALA D 2 60  ? -5.550  14.852  -0.737  1.00 70.04  ?  60  ALA D CB  1 
ATOM 5365 N N   . SER D 2 61  ? -7.992  13.047  -0.746  1.00 76.37  ?  61  SER D N   1 
ATOM 5366 C CA  . SER D 2 61  ? -9.394  12.696  -0.950  1.00 75.52  ?  61  SER D CA  1 
ATOM 5367 C C   . SER D 2 61  ? -10.147 13.808  -1.673  1.00 78.23  ?  61  SER D C   1 
ATOM 5368 O O   . SER D 2 61  ? -10.839 13.559  -2.669  1.00 76.09  ?  61  SER D O   1 
ATOM 5369 C CB  . SER D 2 61  ? -10.048 12.375  0.395   1.00 79.15  ?  61  SER D CB  1 
ATOM 5370 O OG  . SER D 2 61  ? -9.849  13.426  1.328   1.00 73.28  ?  61  SER D OG  1 
ATOM 5371 N N   . TRP D 2 62  ? -10.011 15.048  -1.193  1.00 80.57  ?  62  TRP D N   1 
ATOM 5372 C CA  . TRP D 2 62  ? -10.743 16.176  -1.766  1.00 76.11  ?  62  TRP D CA  1 
ATOM 5373 C C   . TRP D 2 62  ? -10.302 16.520  -3.184  1.00 76.01  ?  62  TRP D C   1 
ATOM 5374 O O   . TRP D 2 62  ? -11.052 17.191  -3.902  1.00 77.63  ?  62  TRP D O   1 
ATOM 5375 C CB  . TRP D 2 62  ? -10.609 17.407  -0.866  1.00 70.31  ?  62  TRP D CB  1 
ATOM 5376 C CG  . TRP D 2 62  ? -9.225  17.628  -0.339  1.00 66.84  ?  62  TRP D CG  1 
ATOM 5377 C CD1 . TRP D 2 62  ? -8.705  17.154  0.833   1.00 68.51  ?  62  TRP D CD1 1 
ATOM 5378 C CD2 . TRP D 2 62  ? -8.176  18.358  -0.976  1.00 65.94  ?  62  TRP D CD2 1 
ATOM 5379 N NE1 . TRP D 2 62  ? -7.400  17.559  0.971   1.00 63.99  ?  62  TRP D NE1 1 
ATOM 5380 C CE2 . TRP D 2 62  ? -7.050  18.300  -0.129  1.00 66.59  ?  62  TRP D CE2 1 
ATOM 5381 C CE3 . TRP D 2 62  ? -8.080  19.067  -2.176  1.00 66.73  ?  62  TRP D CE3 1 
ATOM 5382 C CZ2 . TRP D 2 62  ? -5.845  18.921  -0.446  1.00 64.16  ?  62  TRP D CZ2 1 
ATOM 5383 C CZ3 . TRP D 2 62  ? -6.883  19.678  -2.493  1.00 66.93  ?  62  TRP D CZ3 1 
ATOM 5384 C CH2 . TRP D 2 62  ? -5.781  19.602  -1.632  1.00 67.55  ?  62  TRP D CH2 1 
ATOM 5385 N N   . ALA D 2 63  ? -9.116  16.094  -3.603  1.00 78.43  ?  63  ALA D N   1 
ATOM 5386 C CA  . ALA D 2 63  ? -8.627  16.324  -4.960  1.00 74.15  ?  63  ALA D CA  1 
ATOM 5387 C C   . ALA D 2 63  ? -8.288  14.982  -5.597  1.00 80.31  ?  63  ALA D C   1 
ATOM 5388 O O   . ALA D 2 63  ? -7.135  14.727  -5.951  1.00 84.68  ?  63  ALA D O   1 
ATOM 5389 C CB  . ALA D 2 63  ? -7.416  17.246  -4.959  1.00 71.72  ?  63  ALA D CB  1 
ATOM 5390 N N   . LYS D 2 64  ? -9.295  14.137  -5.776  1.00 81.91  ?  64  LYS D N   1 
ATOM 5391 C CA  . LYS D 2 64  ? -9.111  12.866  -6.460  1.00 86.33  ?  64  LYS D CA  1 
ATOM 5392 C C   . LYS D 2 64  ? -9.674  12.986  -7.867  1.00 81.33  ?  64  LYS D C   1 
ATOM 5393 O O   . LYS D 2 64  ? -10.820 13.413  -8.050  1.00 81.26  ?  64  LYS D O   1 
ATOM 5394 C CB  . LYS D 2 64  ? -9.779  11.714  -5.706  1.00 88.06  ?  64  LYS D CB  1 
ATOM 5395 C CG  . LYS D 2 64  ? -9.193  10.347  -6.055  1.00 83.23  ?  64  LYS D CG  1 
ATOM 5396 C CD  . LYS D 2 64  ? -7.715  10.258  -5.692  1.00 82.50  ?  64  LYS D CD  1 
ATOM 5397 C CE  . LYS D 2 64  ? -7.103  8.935   -6.141  1.00 85.74  ?  64  LYS D CE  1 
ATOM 5398 N NZ  . LYS D 2 64  ? -7.723  7.760   -5.465  1.00 92.50  ?  64  LYS D NZ  1 
ATOM 5399 N N   . GLY D 2 65  ? -8.845  12.667  -8.859  1.00 77.35  ?  65  GLY D N   1 
ATOM 5400 C CA  . GLY D 2 65  ? -9.224  12.825  -10.245 1.00 78.65  ?  65  GLY D CA  1 
ATOM 5401 C C   . GLY D 2 65  ? -9.447  14.251  -10.683 1.00 78.08  ?  65  GLY D C   1 
ATOM 5402 O O   . GLY D 2 65  ? -9.609  14.494  -11.886 1.00 77.55  ?  65  GLY D O   1 
ATOM 5403 N N   . ARG D 2 66  ? -9.462  15.204  -9.753  1.00 76.73  ?  66  ARG D N   1 
ATOM 5404 C CA  . ARG D 2 66  ? -9.666  16.608  -10.069 1.00 69.97  ?  66  ARG D CA  1 
ATOM 5405 C C   . ARG D 2 66  ? -8.361  17.301  -10.440 1.00 67.63  ?  66  ARG D C   1 
ATOM 5406 O O   . ARG D 2 66  ? -8.333  18.106  -11.379 1.00 63.10  ?  66  ARG D O   1 
ATOM 5407 C CB  . ARG D 2 66  ? -10.328 17.306  -8.878  1.00 73.12  ?  66  ARG D CB  1 
ATOM 5408 C CG  . ARG D 2 66  ? -11.058 18.579  -9.230  1.00 67.31  ?  66  ARG D CG  1 
ATOM 5409 C CD  . ARG D 2 66  ? -12.123 18.904  -8.208  1.00 67.09  ?  66  ARG D CD  1 
ATOM 5410 N NE  . ARG D 2 66  ? -11.609 18.814  -6.846  1.00 74.94  ?  66  ARG D NE  1 
ATOM 5411 C CZ  . ARG D 2 66  ? -11.135 19.849  -6.161  1.00 74.63  ?  66  ARG D CZ  1 
ATOM 5412 N NH1 . ARG D 2 66  ? -10.689 19.683  -4.923  1.00 77.34  ?  66  ARG D NH1 1 
ATOM 5413 N NH2 . ARG D 2 66  ? -11.111 21.053  -6.713  1.00 69.36  ?  66  ARG D NH2 1 
ATOM 5414 N N   . PHE D 2 67  ? -7.276  16.986  -9.734  1.00 67.50  ?  67  PHE D N   1 
ATOM 5415 C CA  . PHE D 2 67  ? -5.957  17.531  -10.016 1.00 62.78  ?  67  PHE D CA  1 
ATOM 5416 C C   . PHE D 2 67  ? -5.067  16.450  -10.615 1.00 58.00  ?  67  PHE D C   1 
ATOM 5417 O O   . PHE D 2 67  ? -5.342  15.254  -10.497 1.00 62.53  ?  67  PHE D O   1 
ATOM 5418 C CB  . PHE D 2 67  ? -5.292  18.094  -8.750  1.00 57.51  ?  67  PHE D CB  1 
ATOM 5419 C CG  . PHE D 2 67  ? -6.036  19.237  -8.118  1.00 59.05  ?  67  PHE D CG  1 
ATOM 5420 C CD1 . PHE D 2 67  ? -5.698  19.676  -6.847  1.00 62.14  ?  67  PHE D CD1 1 
ATOM 5421 C CD2 . PHE D 2 67  ? -7.053  19.891  -8.795  1.00 61.31  ?  67  PHE D CD2 1 
ATOM 5422 C CE1 . PHE D 2 67  ? -6.371  20.729  -6.256  1.00 56.13  ?  67  PHE D CE1 1 
ATOM 5423 C CE2 . PHE D 2 67  ? -7.732  20.943  -8.210  1.00 62.93  ?  67  PHE D CE2 1 
ATOM 5424 C CZ  . PHE D 2 67  ? -7.388  21.364  -6.938  1.00 62.99  ?  67  PHE D CZ  1 
ATOM 5425 N N   . THR D 2 68  ? -3.981  16.889  -11.247 1.00 49.70  ?  68  THR D N   1 
ATOM 5426 C CA  . THR D 2 68  ? -3.032  15.983  -11.884 1.00 56.10  ?  68  THR D CA  1 
ATOM 5427 C C   . THR D 2 68  ? -1.625  16.522  -11.688 1.00 51.53  ?  68  THR D C   1 
ATOM 5428 O O   . THR D 2 68  ? -1.336  17.657  -12.069 1.00 47.66  ?  68  THR D O   1 
ATOM 5429 C CB  . THR D 2 68  ? -3.327  15.811  -13.379 1.00 64.41  ?  68  THR D CB  1 
ATOM 5430 O OG1 . THR D 2 68  ? -4.643  15.270  -13.556 1.00 66.04  ?  68  THR D OG1 1 
ATOM 5431 C CG2 . THR D 2 68  ? -2.307  14.869  -14.012 1.00 56.16  ?  68  THR D CG2 1 
ATOM 5432 N N   . ILE D 2 69  ? -0.758  15.723  -11.081 1.00 56.92  ?  69  ILE D N   1 
ATOM 5433 C CA  . ILE D 2 69  ? 0.643   16.085  -10.905 1.00 55.80  ?  69  ILE D CA  1 
ATOM 5434 C C   . ILE D 2 69  ? 1.467   15.378  -11.974 1.00 53.82  ?  69  ILE D C   1 
ATOM 5435 O O   . ILE D 2 69  ? 1.173   14.236  -12.350 1.00 57.85  ?  69  ILE D O   1 
ATOM 5436 C CB  . ILE D 2 69  ? 1.132   15.744  -9.482  1.00 63.42  ?  69  ILE D CB  1 
ATOM 5437 C CG1 . ILE D 2 69  ? 2.562   16.248  -9.260  1.00 58.61  ?  69  ILE D CG1 1 
ATOM 5438 C CG2 . ILE D 2 69  ? 1.016   14.252  -9.204  1.00 62.13  ?  69  ILE D CG2 1 
ATOM 5439 C CD1 . ILE D 2 69  ? 3.033   16.112  -7.844  1.00 55.14  ?  69  ILE D CD1 1 
ATOM 5440 N N   . SER D 2 70  ? 2.478   16.070  -12.495 1.00 59.23  ?  70  SER D N   1 
ATOM 5441 C CA  . SER D 2 70  ? 3.307   15.518  -13.560 1.00 57.50  ?  70  SER D CA  1 
ATOM 5442 C C   . SER D 2 70  ? 4.676   16.185  -13.522 1.00 65.13  ?  70  SER D C   1 
ATOM 5443 O O   . SER D 2 70  ? 4.882   17.182  -12.829 1.00 69.51  ?  70  SER D O   1 
ATOM 5444 C CB  . SER D 2 70  ? 2.649   15.713  -14.929 1.00 58.41  ?  70  SER D CB  1 
ATOM 5445 O OG  . SER D 2 70  ? 2.331   17.082  -15.140 1.00 57.54  ?  70  SER D OG  1 
ATOM 5446 N N   . ARG D 2 71  ? 5.619   15.634  -14.282 1.00 66.95  ?  71  ARG D N   1 
ATOM 5447 C CA  . ARG D 2 71  ? 6.938   16.248  -14.360 1.00 68.99  ?  71  ARG D CA  1 
ATOM 5448 C C   . ARG D 2 71  ? 7.559   15.990  -15.723 1.00 67.35  ?  71  ARG D C   1 
ATOM 5449 O O   . ARG D 2 71  ? 7.438   14.895  -16.277 1.00 69.80  ?  71  ARG D O   1 
ATOM 5450 C CB  . ARG D 2 71  ? 7.872   15.749  -13.244 1.00 68.44  ?  71  ARG D CB  1 
ATOM 5451 C CG  . ARG D 2 71  ? 8.103   14.249  -13.210 1.00 69.39  ?  71  ARG D CG  1 
ATOM 5452 C CD  . ARG D 2 71  ? 9.491   13.907  -12.688 1.00 72.50  ?  71  ARG D CD  1 
ATOM 5453 N NE  . ARG D 2 71  ? 9.666   12.462  -12.560 1.00 77.40  ?  71  ARG D NE  1 
ATOM 5454 C CZ  . ARG D 2 71  ? 9.589   11.800  -11.410 1.00 80.93  ?  71  ARG D CZ  1 
ATOM 5455 N NH1 . ARG D 2 71  ? 9.351   12.455  -10.280 1.00 79.13  ?  71  ARG D NH1 1 
ATOM 5456 N NH2 . ARG D 2 71  ? 9.756   10.484  -11.387 1.00 78.49  ?  71  ARG D NH2 1 
ATOM 5457 N N   . ASP D 2 72  ? 8.205   17.022  -16.259 1.00 72.94  ?  72  ASP D N   1 
ATOM 5458 C CA  . ASP D 2 72  ? 8.979   16.932  -17.491 1.00 74.57  ?  72  ASP D CA  1 
ATOM 5459 C C   . ASP D 2 72  ? 10.452  16.873  -17.105 1.00 76.34  ?  72  ASP D C   1 
ATOM 5460 O O   . ASP D 2 72  ? 11.010  17.855  -16.597 1.00 68.05  ?  72  ASP D O   1 
ATOM 5461 C CB  . ASP D 2 72  ? 8.687   18.125  -18.399 1.00 74.71  ?  72  ASP D CB  1 
ATOM 5462 C CG  . ASP D 2 72  ? 9.123   17.892  -19.828 1.00 77.92  ?  72  ASP D CG  1 
ATOM 5463 O OD1 . ASP D 2 72  ? 10.205  17.304  -20.032 1.00 80.18  ?  72  ASP D OD1 1 
ATOM 5464 O OD2 . ASP D 2 72  ? 8.384   18.302  -20.748 1.00 80.88  ?  72  ASP D OD2 1 
ATOM 5465 N N   . ASN D 2 73  ? 11.082  15.726  -17.364 1.00 79.46  ?  73  ASN D N   1 
ATOM 5466 C CA  . ASN D 2 73  ? 12.469  15.527  -16.962 1.00 80.65  ?  73  ASN D CA  1 
ATOM 5467 C C   . ASN D 2 73  ? 13.429  16.281  -17.871 1.00 83.87  ?  73  ASN D C   1 
ATOM 5468 O O   . ASN D 2 73  ? 14.452  16.795  -17.404 1.00 85.70  ?  73  ASN D O   1 
ATOM 5469 C CB  . ASN D 2 73  ? 12.795  14.038  -16.965 1.00 80.37  ?  73  ASN D CB  1 
ATOM 5470 C CG  . ASN D 2 73  ? 11.782  13.229  -16.195 1.00 82.45  ?  73  ASN D CG  1 
ATOM 5471 O OD1 . ASN D 2 73  ? 11.826  13.162  -14.967 1.00 91.90  ?  73  ASN D OD1 1 
ATOM 5472 N ND2 . ASN D 2 73  ? 10.837  12.630  -16.912 1.00 79.22  ?  73  ASN D ND2 1 
ATOM 5473 N N   . SER D 2 74  ? 13.119  16.353  -19.169 1.00 80.68  ?  74  SER D N   1 
ATOM 5474 C CA  . SER D 2 74  ? 13.945  17.133  -20.084 1.00 79.64  ?  74  SER D CA  1 
ATOM 5475 C C   . SER D 2 74  ? 13.889  18.614  -19.729 1.00 75.85  ?  74  SER D C   1 
ATOM 5476 O O   . SER D 2 74  ? 14.927  19.266  -19.566 1.00 74.61  ?  74  SER D O   1 
ATOM 5477 C CB  . SER D 2 74  ? 13.506  16.892  -21.532 1.00 83.52  ?  74  SER D CB  1 
ATOM 5478 O OG  . SER D 2 74  ? 12.136  17.201  -21.720 1.00 88.70  ?  74  SER D OG  1 
ATOM 5479 N N   . LYS D 2 75  ? 12.679  19.158  -19.587 1.00 73.66  ?  75  LYS D N   1 
ATOM 5480 C CA  . LYS D 2 75  ? 12.518  20.539  -19.151 1.00 77.73  ?  75  LYS D CA  1 
ATOM 5481 C C   . LYS D 2 75  ? 12.813  20.717  -17.665 1.00 77.48  ?  75  LYS D C   1 
ATOM 5482 O O   . LYS D 2 75  ? 12.979  21.859  -17.218 1.00 67.31  ?  75  LYS D O   1 
ATOM 5483 C CB  . LYS D 2 75  ? 11.093  21.011  -19.451 1.00 72.37  ?  75  LYS D CB  1 
ATOM 5484 C CG  . LYS D 2 75  ? 10.792  21.196  -20.926 1.00 80.37  ?  75  LYS D CG  1 
ATOM 5485 C CD  . LYS D 2 75  ? 9.373   21.699  -21.146 1.00 77.64  ?  75  LYS D CD  1 
ATOM 5486 C CE  . LYS D 2 75  ? 9.120   21.997  -22.615 1.00 81.53  ?  75  LYS D CE  1 
ATOM 5487 N NZ  . LYS D 2 75  ? 10.034  23.059  -23.123 1.00 89.16  ?  75  LYS D NZ  1 
ATOM 5488 N N   . ASN D 2 76  ? 12.895  19.619  -16.910 1.00 77.80  ?  76  ASN D N   1 
ATOM 5489 C CA  . ASN D 2 76  ? 13.174  19.627  -15.473 1.00 75.69  ?  76  ASN D CA  1 
ATOM 5490 C C   . ASN D 2 76  ? 12.201  20.551  -14.739 1.00 74.08  ?  76  ASN D C   1 
ATOM 5491 O O   . ASN D 2 76  ? 12.578  21.565  -14.147 1.00 69.66  ?  76  ASN D O   1 
ATOM 5492 C CB  . ASN D 2 76  ? 14.633  20.003  -15.196 1.00 70.94  ?  76  ASN D CB  1 
ATOM 5493 C CG  . ASN D 2 76  ? 15.029  19.780  -13.747 1.00 74.25  ?  76  ASN D CG  1 
ATOM 5494 O OD1 . ASN D 2 76  ? 15.009  18.651  -13.253 1.00 76.86  ?  76  ASN D OD1 1 
ATOM 5495 N ND2 . ASN D 2 76  ? 15.424  20.850  -13.068 1.00 79.40  ?  76  ASN D ND2 1 
ATOM 5496 N N   . THR D 2 77  ? 10.918  20.198  -14.821 1.00 74.13  ?  77  THR D N   1 
ATOM 5497 C CA  . THR D 2 77  ? 9.873   21.032  -14.246 1.00 69.93  ?  77  THR D CA  1 
ATOM 5498 C C   . THR D 2 77  ? 8.747   20.156  -13.710 1.00 71.33  ?  77  THR D C   1 
ATOM 5499 O O   . THR D 2 77  ? 8.360   19.171  -14.342 1.00 68.07  ?  77  THR D O   1 
ATOM 5500 C CB  . THR D 2 77  ? 9.323   22.024  -15.281 1.00 75.20  ?  77  THR D CB  1 
ATOM 5501 O OG1 . THR D 2 77  ? 10.398  22.805  -15.822 1.00 77.98  ?  77  THR D OG1 1 
ATOM 5502 C CG2 . THR D 2 77  ? 8.307   22.966  -14.641 1.00 71.35  ?  77  THR D CG2 1 
ATOM 5503 N N   . LEU D 2 78  ? 8.229   20.523  -12.539 1.00 70.11  ?  78  LEU D N   1 
ATOM 5504 C CA  . LEU D 2 78  ? 7.047   19.894  -11.968 1.00 66.27  ?  78  LEU D CA  1 
ATOM 5505 C C   . LEU D 2 78  ? 5.808   20.687  -12.366 1.00 61.47  ?  78  LEU D C   1 
ATOM 5506 O O   . LEU D 2 78  ? 5.865   21.902  -12.556 1.00 60.02  ?  78  LEU D O   1 
ATOM 5507 C CB  . LEU D 2 78  ? 7.152   19.823  -10.443 1.00 69.32  ?  78  LEU D CB  1 
ATOM 5508 C CG  . LEU D 2 78  ? 6.140   18.969  -9.672  1.00 66.16  ?  78  LEU D CG  1 
ATOM 5509 C CD1 . LEU D 2 78  ? 6.358   17.492  -9.931  1.00 60.72  ?  78  LEU D CD1 1 
ATOM 5510 C CD2 . LEU D 2 78  ? 6.204   19.277  -8.179  1.00 62.68  ?  78  LEU D CD2 1 
ATOM 5511 N N   . TYR D 2 79  ? 4.680   19.993  -12.478 1.00 61.23  ?  79  TYR D N   1 
ATOM 5512 C CA  . TYR D 2 79  ? 3.446   20.613  -12.932 1.00 61.47  ?  79  TYR D CA  1 
ATOM 5513 C C   . TYR D 2 79  ? 2.286   20.118  -12.088 1.00 53.83  ?  79  TYR D C   1 
ATOM 5514 O O   . TYR D 2 79  ? 2.226   18.935  -11.732 1.00 50.40  ?  79  TYR D O   1 
ATOM 5515 C CB  . TYR D 2 79  ? 3.141   20.300  -14.409 1.00 62.02  ?  79  TYR D CB  1 
ATOM 5516 C CG  . TYR D 2 79  ? 4.168   20.785  -15.408 1.00 64.79  ?  79  TYR D CG  1 
ATOM 5517 C CD1 . TYR D 2 79  ? 4.227   22.120  -15.781 1.00 61.47  ?  79  TYR D CD1 1 
ATOM 5518 C CD2 . TYR D 2 79  ? 5.053   19.896  -16.007 1.00 68.25  ?  79  TYR D CD2 1 
ATOM 5519 C CE1 . TYR D 2 79  ? 5.162   22.561  -16.702 1.00 67.96  ?  79  TYR D CE1 1 
ATOM 5520 C CE2 . TYR D 2 79  ? 5.988   20.327  -16.929 1.00 69.43  ?  79  TYR D CE2 1 
ATOM 5521 C CZ  . TYR D 2 79  ? 6.039   21.660  -17.274 1.00 69.18  ?  79  TYR D CZ  1 
ATOM 5522 O OH  . TYR D 2 79  ? 6.971   22.091  -18.193 1.00 71.93  ?  79  TYR D OH  1 
ATOM 5523 N N   . LEU D 2 80  ? 1.354   21.027  -11.804 1.00 47.13  ?  80  LEU D N   1 
ATOM 5524 C CA  . LEU D 2 80  ? 0.092   20.689  -11.155 1.00 47.24  ?  80  LEU D CA  1 
ATOM 5525 C C   . LEU D 2 80  ? -1.013  21.287  -12.011 1.00 48.33  ?  80  LEU D C   1 
ATOM 5526 O O   . LEU D 2 80  ? -1.128  22.512  -12.110 1.00 50.94  ?  80  LEU D O   1 
ATOM 5527 C CB  . LEU D 2 80  ? 0.030   21.216  -9.716  1.00 57.10  ?  80  LEU D CB  1 
ATOM 5528 C CG  . LEU D 2 80  ? -1.156  20.770  -8.848  1.00 50.69  ?  80  LEU D CG  1 
ATOM 5529 C CD1 . LEU D 2 80  ? -1.090  19.272  -8.572  1.00 53.48  ?  80  LEU D CD1 1 
ATOM 5530 C CD2 . LEU D 2 80  ? -1.197  21.539  -7.535  1.00 45.78  ?  80  LEU D CD2 1 
ATOM 5531 N N   . GLN D 2 81  ? -1.792  20.423  -12.654 1.00 50.61  ?  81  GLN D N   1 
ATOM 5532 C CA  . GLN D 2 81  ? -2.926  20.814  -13.478 1.00 50.32  ?  81  GLN D CA  1 
ATOM 5533 C C   . GLN D 2 81  ? -4.181  20.671  -12.632 1.00 49.71  ?  81  GLN D C   1 
ATOM 5534 O O   . GLN D 2 81  ? -4.416  19.611  -12.043 1.00 51.11  ?  81  GLN D O   1 
ATOM 5535 C CB  . GLN D 2 81  ? -3.016  19.944  -14.734 1.00 52.92  ?  81  GLN D CB  1 
ATOM 5536 C CG  . GLN D 2 81  ? -4.248  20.203  -15.594 1.00 57.30  ?  81  GLN D CG  1 
ATOM 5537 C CD  . GLN D 2 81  ? -4.130  21.455  -16.455 1.00 60.56  ?  81  GLN D CD  1 
ATOM 5538 O OE1 . GLN D 2 81  ? -3.113  21.677  -17.121 1.00 58.65  ?  81  GLN D OE1 1 
ATOM 5539 N NE2 . GLN D 2 81  ? -5.173  22.282  -16.441 1.00 57.47  ?  81  GLN D NE2 1 
ATOM 5540 N N   . MET D 2 82  ? -4.960  21.741  -12.540 1.00 49.34  ?  82  MET D N   1 
ATOM 5541 C CA  . MET D 2 82  ? -6.164  21.768  -11.727 1.00 57.55  ?  82  MET D CA  1 
ATOM 5542 C C   . MET D 2 82  ? -7.371  22.032  -12.615 1.00 54.95  ?  82  MET D C   1 
ATOM 5543 O O   . MET D 2 82  ? -7.415  23.037  -13.333 1.00 55.36  ?  82  MET D O   1 
ATOM 5544 C CB  . MET D 2 82  ? -6.046  22.831  -10.630 1.00 55.86  ?  82  MET D CB  1 
ATOM 5545 C CG  . MET D 2 82  ? -4.842  22.635  -9.724  1.00 50.38  ?  82  MET D CG  1 
ATOM 5546 S SD  . MET D 2 82  ? -4.599  23.966  -8.534  1.00 64.93  ?  82  MET D SD  1 
ATOM 5547 C CE  . MET D 2 82  ? -4.121  25.310  -9.611  1.00 59.11  ?  82  MET D CE  1 
ATOM 5548 N N   . ASN D 2 83  ? -8.338  21.125  -12.564 1.00 55.20  ?  83  ASN D N   1 
ATOM 5549 C CA  . ASN D 2 83  ? -9.553  21.186  -13.354 1.00 55.46  ?  83  ASN D CA  1 
ATOM 5550 C C   . ASN D 2 83  ? -10.737 21.196  -12.398 1.00 58.83  ?  83  ASN D C   1 
ATOM 5551 O O   . ASN D 2 83  ? -10.637 20.726  -11.265 1.00 66.02  ?  83  ASN D O   1 
ATOM 5552 C CB  . ASN D 2 83  ? -9.649  20.002  -14.321 1.00 56.01  ?  83  ASN D CB  1 
ATOM 5553 C CG  . ASN D 2 83  ? -8.394  19.837  -15.165 1.00 61.99  ?  83  ASN D CG  1 
ATOM 5554 O OD1 . ASN D 2 83  ? -8.170  20.581  -16.124 1.00 62.81  ?  83  ASN D OD1 1 
ATOM 5555 N ND2 . ASN D 2 83  ? -7.567  18.855  -14.812 1.00 60.66  ?  83  ASN D ND2 1 
ATOM 5556 N N   . SER D 2 84  ? -11.859 21.736  -12.859 1.00 62.35  ?  84  SER D N   1 
ATOM 5557 C CA  . SER D 2 84  ? -13.081 21.851  -12.058 1.00 65.25  ?  84  SER D CA  1 
ATOM 5558 C C   . SER D 2 84  ? -12.794 22.454  -10.679 1.00 65.05  ?  84  SER D C   1 
ATOM 5559 O O   . SER D 2 84  ? -13.054 21.855  -9.632  1.00 63.79  ?  84  SER D O   1 
ATOM 5560 C CB  . SER D 2 84  ? -13.763 20.485  -11.924 1.00 56.81  ?  84  SER D CB  1 
ATOM 5561 O OG  . SER D 2 84  ? -14.075 19.945  -13.196 1.00 67.16  ?  84  SER D OG  1 
ATOM 5562 N N   . LEU D 2 85  ? -12.275 23.679  -10.699 1.00 60.69  ?  85  LEU D N   1 
ATOM 5563 C CA  . LEU D 2 85  ? -11.880 24.361  -9.473  1.00 58.57  ?  85  LEU D CA  1 
ATOM 5564 C C   . LEU D 2 85  ? -13.102 24.875  -8.722  1.00 58.55  ?  85  LEU D C   1 
ATOM 5565 O O   . LEU D 2 85  ? -14.086 25.310  -9.326  1.00 65.90  ?  85  LEU D O   1 
ATOM 5566 C CB  . LEU D 2 85  ? -10.930 25.513  -9.790  1.00 54.82  ?  85  LEU D CB  1 
ATOM 5567 C CG  . LEU D 2 85  ? -9.538  25.081  -10.239 1.00 51.90  ?  85  LEU D CG  1 
ATOM 5568 C CD1 . LEU D 2 85  ? -8.715  26.267  -10.709 1.00 49.14  ?  85  LEU D CD1 1 
ATOM 5569 C CD2 . LEU D 2 85  ? -8.853  24.373  -9.087  1.00 57.96  ?  85  LEU D CD2 1 
ATOM 5570 N N   . ARG D 2 86  ? -13.038 24.822  -7.400  1.00 57.46  ?  86  ARG D N   1 
ATOM 5571 C CA  . ARG D 2 86  ? -14.130 25.282  -6.558  1.00 64.00  ?  86  ARG D CA  1 
ATOM 5572 C C   . ARG D 2 86  ? -13.684 26.490  -5.742  1.00 64.93  ?  86  ARG D C   1 
ATOM 5573 O O   . ARG D 2 86  ? -12.501 26.839  -5.691  1.00 61.90  ?  86  ARG D O   1 
ATOM 5574 C CB  . ARG D 2 86  ? -14.606 24.164  -5.620  1.00 71.47  ?  86  ARG D CB  1 
ATOM 5575 C CG  . ARG D 2 86  ? -14.552 22.756  -6.205  1.00 74.62  ?  86  ARG D CG  1 
ATOM 5576 C CD  . ARG D 2 86  ? -14.506 21.715  -5.084  1.00 74.53  ?  86  ARG D CD  1 
ATOM 5577 N NE  . ARG D 2 86  ? -14.414 20.345  -5.584  1.00 81.96  ?  86  ARG D NE  1 
ATOM 5578 C CZ  . ARG D 2 86  ? -14.192 19.283  -4.811  1.00 83.44  ?  86  ARG D CZ  1 
ATOM 5579 N NH1 . ARG D 2 86  ? -14.037 19.437  -3.504  1.00 83.74  ?  86  ARG D NH1 1 
ATOM 5580 N NH2 . ARG D 2 86  ? -14.120 18.068  -5.343  1.00 82.13  ?  86  ARG D NH2 1 
ATOM 5581 N N   . ALA D 2 87  ? -14.657 27.113  -5.072  1.00 66.60  ?  87  ALA D N   1 
ATOM 5582 C CA  . ALA D 2 87  ? -14.363 28.304  -4.280  1.00 52.77  ?  87  ALA D CA  1 
ATOM 5583 C C   . ALA D 2 87  ? -13.435 28.000  -3.116  1.00 54.90  ?  87  ALA D C   1 
ATOM 5584 O O   . ALA D 2 87  ? -12.626 28.848  -2.733  1.00 57.15  ?  87  ALA D O   1 
ATOM 5585 C CB  . ALA D 2 87  ? -15.661 28.927  -3.767  1.00 48.80  ?  87  ALA D CB  1 
ATOM 5586 N N   . GLU D 2 88  ? -13.523 26.802  -2.547  1.00 66.13  ?  88  GLU D N   1 
ATOM 5587 C CA  . GLU D 2 88  ? -12.672 26.407  -1.429  1.00 55.06  ?  88  GLU D CA  1 
ATOM 5588 C C   . GLU D 2 88  ? -11.259 26.015  -1.860  1.00 58.72  ?  88  GLU D C   1 
ATOM 5589 O O   . GLU D 2 88  ? -10.480 25.552  -1.020  1.00 53.79  ?  88  GLU D O   1 
ATOM 5590 C CB  . GLU D 2 88  ? -13.325 25.258  -0.658  1.00 49.60  ?  88  GLU D CB  1 
ATOM 5591 C CG  . GLU D 2 88  ? -13.423 23.966  -1.447  1.00 69.87  ?  88  GLU D CG  1 
ATOM 5592 C CD  . GLU D 2 88  ? -14.798 23.750  -2.060  1.00 78.17  ?  88  GLU D CD  1 
ATOM 5593 O OE1 . GLU D 2 88  ? -15.292 22.601  -2.023  1.00 85.86  ?  88  GLU D OE1 1 
ATOM 5594 O OE2 . GLU D 2 88  ? -15.383 24.727  -2.579  1.00 74.31  ?  88  GLU D OE2 1 
ATOM 5595 N N   . ASP D 2 89  ? -10.906 26.185  -3.136  1.00 56.23  ?  89  ASP D N   1 
ATOM 5596 C CA  . ASP D 2 89  ? -9.563  25.875  -3.606  1.00 49.85  ?  89  ASP D CA  1 
ATOM 5597 C C   . ASP D 2 89  ? -8.644  27.088  -3.651  1.00 46.82  ?  89  ASP D C   1 
ATOM 5598 O O   . ASP D 2 89  ? -7.454  26.929  -3.947  1.00 40.90  ?  89  ASP D O   1 
ATOM 5599 C CB  . ASP D 2 89  ? -9.611  25.237  -4.996  1.00 52.95  ?  89  ASP D CB  1 
ATOM 5600 C CG  . ASP D 2 89  ? -10.181 23.841  -4.971  1.00 64.11  ?  89  ASP D CG  1 
ATOM 5601 O OD1 . ASP D 2 89  ? -11.160 23.590  -5.708  1.00 63.17  ?  89  ASP D OD1 1 
ATOM 5602 O OD2 . ASP D 2 89  ? -9.652  22.999  -4.207  1.00 68.68  ?  89  ASP D OD2 1 
ATOM 5603 N N   . THR D 2 90  ? -9.159  28.288  -3.393  1.00 49.19  ?  90  THR D N   1 
ATOM 5604 C CA  . THR D 2 90  ? -8.301  29.464  -3.369  1.00 51.34  ?  90  THR D CA  1 
ATOM 5605 C C   . THR D 2 90  ? -7.309  29.338  -2.223  1.00 42.38  ?  90  THR D C   1 
ATOM 5606 O O   . THR D 2 90  ? -7.695  29.095  -1.077  1.00 43.37  ?  90  THR D O   1 
ATOM 5607 C CB  . THR D 2 90  ? -9.128  30.745  -3.229  1.00 50.01  ?  90  THR D CB  1 
ATOM 5608 O OG1 . THR D 2 90  ? -9.344  31.031  -1.846  1.00 56.11  ?  90  THR D OG1 1 
ATOM 5609 C CG2 . THR D 2 90  ? -10.475 30.569  -3.888  1.00 49.15  ?  90  THR D CG2 1 
ATOM 5610 N N   . ALA D 2 91  ? -6.027  29.478  -2.544  1.00 40.52  ?  91  ALA D N   1 
ATOM 5611 C CA  . ALA D 2 91  ? -4.956  29.254  -1.581  1.00 41.53  ?  91  ALA D CA  1 
ATOM 5612 C C   . ALA D 2 91  ? -3.642  29.674  -2.219  1.00 43.17  ?  91  ALA D C   1 
ATOM 5613 O O   . ALA D 2 91  ? -3.577  29.977  -3.412  1.00 41.03  ?  91  ALA D O   1 
ATOM 5614 C CB  . ALA D 2 91  ? -4.886  27.785  -1.145  1.00 41.69  ?  91  ALA D CB  1 
ATOM 5615 N N   . VAL D 2 92  ? -2.597  29.714  -1.404  1.00 44.33  ?  92  VAL D N   1 
ATOM 5616 C CA  . VAL D 2 92  ? -1.237  29.834  -1.910  1.00 49.36  ?  92  VAL D CA  1 
ATOM 5617 C C   . VAL D 2 92  ? -0.697  28.420  -2.083  1.00 51.97  ?  92  VAL D C   1 
ATOM 5618 O O   . VAL D 2 92  ? -0.707  27.625  -1.135  1.00 54.93  ?  92  VAL D O   1 
ATOM 5619 C CB  . VAL D 2 92  ? -0.359  30.666  -0.964  1.00 46.07  ?  92  VAL D CB  1 
ATOM 5620 C CG1 . VAL D 2 92  ? 1.073   30.684  -1.446  1.00 47.06  ?  92  VAL D CG1 1 
ATOM 5621 C CG2 . VAL D 2 92  ? -0.887  32.089  -0.882  1.00 41.22  ?  92  VAL D CG2 1 
ATOM 5622 N N   . TYR D 2 93  ? -0.267  28.088  -3.297  1.00 46.04  ?  93  TYR D N   1 
ATOM 5623 C CA  . TYR D 2 93  ? 0.252   26.760  -3.599  1.00 52.83  ?  93  TYR D CA  1 
ATOM 5624 C C   . TYR D 2 93  ? 1.771   26.798  -3.607  1.00 54.68  ?  93  TYR D C   1 
ATOM 5625 O O   . TYR D 2 93  ? 2.373   27.707  -4.199  1.00 55.27  ?  93  TYR D O   1 
ATOM 5626 C CB  . TYR D 2 93  ? -0.280  26.239  -4.939  1.00 52.10  ?  93  TYR D CB  1 
ATOM 5627 C CG  . TYR D 2 93  ? -1.743  25.876  -4.876  1.00 45.24  ?  93  TYR D CG  1 
ATOM 5628 C CD1 . TYR D 2 93  ? -2.143  24.568  -4.649  1.00 38.63  ?  93  TYR D CD1 1 
ATOM 5629 C CD2 . TYR D 2 93  ? -2.726  26.852  -5.007  1.00 44.79  ?  93  TYR D CD2 1 
ATOM 5630 C CE1 . TYR D 2 93  ? -3.483  24.237  -4.568  1.00 40.26  ?  93  TYR D CE1 1 
ATOM 5631 C CE2 . TYR D 2 93  ? -4.068  26.533  -4.929  1.00 44.13  ?  93  TYR D CE2 1 
ATOM 5632 C CZ  . TYR D 2 93  ? -4.442  25.224  -4.706  1.00 42.83  ?  93  TYR D CZ  1 
ATOM 5633 O OH  . TYR D 2 93  ? -5.779  24.907  -4.626  1.00 41.90  ?  93  TYR D OH  1 
ATOM 5634 N N   . TYR D 2 94  ? 2.378   25.815  -2.932  1.00 52.05  ?  94  TYR D N   1 
ATOM 5635 C CA  . TYR D 2 94  ? 3.815   25.677  -2.784  1.00 54.12  ?  94  TYR D CA  1 
ATOM 5636 C C   . TYR D 2 94  ? 4.273   24.390  -3.447  1.00 58.01  ?  94  TYR D C   1 
ATOM 5637 O O   . TYR D 2 94  ? 3.603   23.352  -3.364  1.00 55.80  ?  94  TYR D O   1 
ATOM 5638 C CB  . TYR D 2 94  ? 4.259   25.622  -1.316  1.00 54.62  ?  94  TYR D CB  1 
ATOM 5639 C CG  . TYR D 2 94  ? 4.050   26.866  -0.487  1.00 54.27  ?  94  TYR D CG  1 
ATOM 5640 C CD1 . TYR D 2 94  ? 2.942   26.988  0.339   1.00 50.56  ?  94  TYR D CD1 1 
ATOM 5641 C CD2 . TYR D 2 94  ? 4.983   27.889  -0.485  1.00 57.19  ?  94  TYR D CD2 1 
ATOM 5642 C CE1 . TYR D 2 94  ? 2.752   28.106  1.116   1.00 52.77  ?  94  TYR D CE1 1 
ATOM 5643 C CE2 . TYR D 2 94  ? 4.801   29.016  0.291   1.00 62.09  ?  94  TYR D CE2 1 
ATOM 5644 C CZ  . TYR D 2 94  ? 3.682   29.119  1.092   1.00 60.08  ?  94  TYR D CZ  1 
ATOM 5645 O OH  . TYR D 2 94  ? 3.482   30.234  1.875   1.00 64.07  ?  94  TYR D OH  1 
ATOM 5646 N N   . CYS D 2 95  ? 5.433   24.474  -4.074  1.00 66.26  ?  95  CYS D N   1 
ATOM 5647 C CA  . CYS D 2 95  ? 6.133   23.339  -4.645  1.00 65.18  ?  95  CYS D CA  1 
ATOM 5648 C C   . CYS D 2 95  ? 7.277   22.972  -3.713  1.00 66.83  ?  95  CYS D C   1 
ATOM 5649 O O   . CYS D 2 95  ? 8.059   23.842  -3.318  1.00 70.23  ?  95  CYS D O   1 
ATOM 5650 C CB  . CYS D 2 95  ? 6.647   23.714  -6.033  1.00 68.61  ?  95  CYS D CB  1 
ATOM 5651 S SG  . CYS D 2 95  ? 7.905   22.671  -6.739  1.00 89.99  ?  95  CYS D SG  1 
ATOM 5652 N N   . ALA D 2 96  ? 7.376   21.695  -3.357  1.00 65.57  ?  96  ALA D N   1 
ATOM 5653 C CA  . ALA D 2 96  ? 8.337   21.284  -2.349  1.00 67.85  ?  96  ALA D CA  1 
ATOM 5654 C C   . ALA D 2 96  ? 9.018   19.989  -2.761  1.00 70.46  ?  96  ALA D C   1 
ATOM 5655 O O   . ALA D 2 96  ? 8.436   19.144  -3.452  1.00 63.98  ?  96  ALA D O   1 
ATOM 5656 C CB  . ALA D 2 96  ? 7.668   21.116  -0.978  1.00 65.93  ?  96  ALA D CB  1 
ATOM 5657 N N   . ARG D 2 97  ? 10.267  19.848  -2.322  1.00 75.66  ?  97  ARG D N   1 
ATOM 5658 C CA  . ARG D 2 97  ? 11.067  18.657  -2.579  1.00 76.44  ?  97  ARG D CA  1 
ATOM 5659 C C   . ARG D 2 97  ? 11.155  17.820  -1.309  1.00 71.68  ?  97  ARG D C   1 
ATOM 5660 O O   . ARG D 2 97  ? 11.508  18.334  -0.242  1.00 78.68  ?  97  ARG D O   1 
ATOM 5661 C CB  . ARG D 2 97  ? 12.471  19.025  -3.065  1.00 78.91  ?  97  ARG D CB  1 
ATOM 5662 C CG  . ARG D 2 97  ? 13.286  17.825  -3.527  1.00 79.90  ?  97  ARG D CG  1 
ATOM 5663 C CD  . ARG D 2 97  ? 14.650  17.752  -2.845  1.00 85.08  ?  97  ARG D CD  1 
ATOM 5664 N NE  . ARG D 2 97  ? 15.531  18.855  -3.220  1.00 86.57  ?  97  ARG D NE  1 
ATOM 5665 C CZ  . ARG D 2 97  ? 16.783  18.987  -2.794  1.00 85.39  ?  97  ARG D CZ  1 
ATOM 5666 N NH1 . ARG D 2 97  ? 17.513  20.023  -3.188  1.00 81.07  ?  97  ARG D NH1 1 
ATOM 5667 N NH2 . ARG D 2 97  ? 17.307  18.082  -1.975  1.00 88.13  ?  97  ARG D NH2 1 
ATOM 5668 N N   . GLU D 2 98  ? 10.839  16.536  -1.430  1.00 70.58  ?  98  GLU D N   1 
ATOM 5669 C CA  . GLU D 2 98  ? 10.870  15.610  -0.307  1.00 79.13  ?  98  GLU D CA  1 
ATOM 5670 C C   . GLU D 2 98  ? 12.154  14.794  -0.369  1.00 83.81  ?  98  GLU D C   1 
ATOM 5671 O O   . GLU D 2 98  ? 12.468  14.197  -1.405  1.00 87.35  ?  98  GLU D O   1 
ATOM 5672 C CB  . GLU D 2 98  ? 9.651   14.687  -0.333  1.00 76.48  ?  98  GLU D CB  1 
ATOM 5673 C CG  . GLU D 2 98  ? 9.553   13.749  0.850   1.00 73.36  ?  98  GLU D CG  1 
ATOM 5674 C CD  . GLU D 2 98  ? 8.271   12.945  0.838   1.00 80.99  ?  98  GLU D CD  1 
ATOM 5675 O OE1 . GLU D 2 98  ? 7.455   13.133  -0.087  1.00 76.51  ?  98  GLU D OE1 1 
ATOM 5676 O OE2 . GLU D 2 98  ? 8.079   12.113  1.746   1.00 95.71  ?  98  GLU D OE2 1 
ATOM 5677 N N   . ASP D 2 99  ? 12.878  14.747  0.743   1.00 85.96  ?  99  ASP D N   1 
ATOM 5678 C CA  . ASP D 2 99  ? 14.166  14.063  0.823   1.00 89.17  ?  99  ASP D CA  1 
ATOM 5679 C C   . ASP D 2 99  ? 13.969  12.769  1.608   1.00 92.14  ?  99  ASP D C   1 
ATOM 5680 O O   . ASP D 2 99  ? 14.178  12.719  2.822   1.00 91.98  ?  99  ASP D O   1 
ATOM 5681 C CB  . ASP D 2 99  ? 15.219  14.975  1.471   1.00 92.08  ?  99  ASP D CB  1 
ATOM 5682 C CG  . ASP D 2 99  ? 16.634  14.420  1.370   1.00 94.39  ?  99  ASP D CG  1 
ATOM 5683 O OD1 . ASP D 2 99  ? 16.830  13.199  1.566   1.00 98.79  ?  99  ASP D OD1 1 
ATOM 5684 O OD2 . ASP D 2 99  ? 17.554  15.215  1.079   1.00 94.94  ?  99  ASP D OD2 1 
ATOM 5685 N N   . VAL D 2 100 ? 13.559  11.718  0.901   1.00 88.85  ?  100 VAL D N   1 
ATOM 5686 C CA  . VAL D 2 100 ? 13.380  10.415  1.526   1.00 94.63  ?  100 VAL D CA  1 
ATOM 5687 C C   . VAL D 2 100 ? 14.745  9.740   1.558   1.00 103.34 ?  100 VAL D C   1 
ATOM 5688 O O   . VAL D 2 100 ? 15.710  10.254  0.976   1.00 99.59  ?  100 VAL D O   1 
ATOM 5689 C CB  . VAL D 2 100 ? 12.332  9.565   0.786   1.00 88.78  ?  100 VAL D CB  1 
ATOM 5690 C CG1 . VAL D 2 100 ? 11.686  8.565   1.738   1.00 87.07  ?  100 VAL D CG1 1 
ATOM 5691 C CG2 . VAL D 2 100 ? 11.278  10.459  0.164   1.00 87.89  ?  100 VAL D CG2 1 
ATOM 5692 N N   . ALA D 2 101 ? 14.835  8.607   2.266   1.00 105.24 ?  101 ALA D N   1 
ATOM 5693 C CA  . ALA D 2 101 ? 16.055  7.820   2.446   1.00 105.19 ?  101 ALA D CA  1 
ATOM 5694 C C   . ALA D 2 101 ? 17.063  8.493   3.378   1.00 101.08 ?  101 ALA D C   1 
ATOM 5695 O O   . ALA D 2 101 ? 17.992  7.835   3.858   1.00 98.18  ?  101 ALA D O   1 
ATOM 5696 C CB  . ALA D 2 101 ? 16.713  7.503   1.096   1.00 95.48  ?  101 ALA D CB  1 
ATOM 5697 N N   . VAL D 2 102 ? 16.905  9.791   3.642   1.00 99.50  ?  102 VAL D N   1 
ATOM 5698 C CA  . VAL D 2 102 ? 17.854  10.502  4.494   1.00 104.63 ?  102 VAL D CA  1 
ATOM 5699 C C   . VAL D 2 102 ? 17.104  11.308  5.549   1.00 104.72 ?  102 VAL D C   1 
ATOM 5700 O O   . VAL D 2 102 ? 17.203  11.024  6.749   1.00 97.19  ?  102 VAL D O   1 
ATOM 5701 C CB  . VAL D 2 102 ? 18.776  11.415  3.662   1.00 104.65 ?  102 VAL D CB  1 
ATOM 5702 C CG1 . VAL D 2 102 ? 19.653  12.261  4.578   1.00 106.24 ?  102 VAL D CG1 1 
ATOM 5703 C CG2 . VAL D 2 102 ? 19.633  10.593  2.710   1.00 101.11 ?  102 VAL D CG2 1 
ATOM 5704 N N   . TYR D 2 103 ? 16.358  12.325  5.111   1.00 101.19 ?  103 TYR D N   1 
ATOM 5705 C CA  . TYR D 2 103 ? 15.639  13.206  6.026   1.00 91.51  ?  103 TYR D CA  1 
ATOM 5706 C C   . TYR D 2 103 ? 14.246  12.696  6.385   1.00 89.85  ?  103 TYR D C   1 
ATOM 5707 O O   . TYR D 2 103 ? 13.775  12.948  7.502   1.00 81.98  ?  103 TYR D O   1 
ATOM 5708 C CB  . TYR D 2 103 ? 15.528  14.612  5.425   1.00 85.99  ?  103 TYR D CB  1 
ATOM 5709 C CG  . TYR D 2 103 ? 16.787  15.452  5.523   1.00 94.96  ?  103 TYR D CG  1 
ATOM 5710 C CD1 . TYR D 2 103 ? 16.905  16.438  6.502   1.00 97.76  ?  103 TYR D CD1 1 
ATOM 5711 C CD2 . TYR D 2 103 ? 17.847  15.278  4.640   1.00 98.44  ?  103 TYR D CD2 1 
ATOM 5712 C CE1 . TYR D 2 103 ? 18.042  17.222  6.608   1.00 89.71  ?  103 TYR D CE1 1 
ATOM 5713 C CE2 . TYR D 2 103 ? 18.995  16.059  4.738   1.00 100.89 ?  103 TYR D CE2 1 
ATOM 5714 C CZ  . TYR D 2 103 ? 19.084  17.030  5.725   1.00 95.29  ?  103 TYR D CZ  1 
ATOM 5715 O OH  . TYR D 2 103 ? 20.213  17.811  5.834   1.00 85.36  ?  103 TYR D OH  1 
ATOM 5716 N N   . MET D 2 104 ? 13.588  11.979  5.468   1.00 90.43  ?  104 MET D N   1 
ATOM 5717 C CA  . MET D 2 104 ? 12.168  11.630  5.589   1.00 85.79  ?  104 MET D CA  1 
ATOM 5718 C C   . MET D 2 104 ? 11.318  12.877  5.828   1.00 88.71  ?  104 MET D C   1 
ATOM 5719 O O   . MET D 2 104 ? 10.317  12.847  6.549   1.00 89.91  ?  104 MET D O   1 
ATOM 5720 C CB  . MET D 2 104 ? 11.930  10.596  6.694   1.00 88.43  ?  104 MET D CB  1 
ATOM 5721 C CG  . MET D 2 104 ? 12.507  9.216   6.419   1.00 95.16  ?  104 MET D CG  1 
ATOM 5722 S SD  . MET D 2 104 ? 14.285  9.129   6.711   1.00 115.80 ?  104 MET D SD  1 
ATOM 5723 C CE  . MET D 2 104 ? 14.603  7.396   6.382   1.00 108.67 ?  104 MET D CE  1 
ATOM 5724 N N   . ALA D 2 105 ? 11.713  13.987  5.208   1.00 80.99  ?  105 ALA D N   1 
ATOM 5725 C CA  . ALA D 2 105 ? 11.063  15.268  5.442   1.00 71.13  ?  105 ALA D CA  1 
ATOM 5726 C C   . ALA D 2 105 ? 11.163  16.114  4.178   1.00 78.39  ?  105 ALA D C   1 
ATOM 5727 O O   . ALA D 2 105 ? 11.537  15.625  3.108   1.00 85.54  ?  105 ALA D O   1 
ATOM 5728 C CB  . ALA D 2 105 ? 11.689  15.973  6.649   1.00 76.21  ?  105 ALA D CB  1 
ATOM 5729 N N   . ILE D 2 106 ? 10.827  17.394  4.307   1.00 71.91  ?  106 ILE D N   1 
ATOM 5730 C CA  . ILE D 2 106 ? 10.864  18.351  3.209   1.00 71.85  ?  106 ILE D CA  1 
ATOM 5731 C C   . ILE D 2 106 ? 11.992  19.334  3.492   1.00 75.25  ?  106 ILE D C   1 
ATOM 5732 O O   . ILE D 2 106 ? 11.936  20.099  4.463   1.00 67.07  ?  106 ILE D O   1 
ATOM 5733 C CB  . ILE D 2 106 ? 9.522   19.074  3.041   1.00 70.55  ?  106 ILE D CB  1 
ATOM 5734 C CG1 . ILE D 2 106 ? 8.421   18.065  2.711   1.00 64.78  ?  106 ILE D CG1 1 
ATOM 5735 C CG2 . ILE D 2 106 ? 9.624   20.140  1.961   1.00 69.13  ?  106 ILE D CG2 1 
ATOM 5736 C CD1 . ILE D 2 106 ? 7.056   18.680  2.574   1.00 59.76  ?  106 ILE D CD1 1 
ATOM 5737 N N   . ASP D 2 107 ? 13.016  19.318  2.639   1.00 82.17  ?  107 ASP D N   1 
ATOM 5738 C CA  . ASP D 2 107 ? 14.204  20.140  2.825   1.00 77.05  ?  107 ASP D CA  1 
ATOM 5739 C C   . ASP D 2 107 ? 14.238  21.376  1.934   1.00 74.97  ?  107 ASP D C   1 
ATOM 5740 O O   . ASP D 2 107 ? 15.113  22.225  2.124   1.00 77.49  ?  107 ASP D O   1 
ATOM 5741 C CB  . ASP D 2 107 ? 15.469  19.301  2.581   1.00 79.57  ?  107 ASP D CB  1 
ATOM 5742 C CG  . ASP D 2 107 ? 15.553  18.765  1.156   1.00 85.89  ?  107 ASP D CG  1 
ATOM 5743 O OD1 . ASP D 2 107 ? 14.504  18.690  0.479   1.00 81.01  ?  107 ASP D OD1 1 
ATOM 5744 O OD2 . ASP D 2 107 ? 16.669  18.415  0.714   1.00 86.41  ?  107 ASP D OD2 1 
ATOM 5745 N N   . LEU D 2 108 ? 13.331  21.497  0.965   1.00 76.35  ?  108 LEU D N   1 
ATOM 5746 C CA  . LEU D 2 108 ? 13.370  22.620  0.035   1.00 79.50  ?  108 LEU D CA  1 
ATOM 5747 C C   . LEU D 2 108 ? 11.962  23.026  -0.378  1.00 76.81  ?  108 LEU D C   1 
ATOM 5748 O O   . LEU D 2 108 ? 11.147  22.170  -0.744  1.00 73.52  ?  108 LEU D O   1 
ATOM 5749 C CB  . LEU D 2 108 ? 14.202  22.273  -1.207  1.00 80.72  ?  108 LEU D CB  1 
ATOM 5750 C CG  . LEU D 2 108 ? 14.268  23.357  -2.286  1.00 80.37  ?  108 LEU D CG  1 
ATOM 5751 C CD1 . LEU D 2 108 ? 14.812  24.655  -1.707  1.00 80.56  ?  108 LEU D CD1 1 
ATOM 5752 C CD2 . LEU D 2 108 ? 15.107  22.900  -3.471  1.00 82.53  ?  108 LEU D CD2 1 
ATOM 5753 N N   . TRP D 2 109 ? 11.698  24.332  -0.342  1.00 69.89  ?  109 TRP D N   1 
ATOM 5754 C CA  . TRP D 2 109 ? 10.432  24.910  -0.765  1.00 65.90  ?  109 TRP D CA  1 
ATOM 5755 C C   . TRP D 2 109 ? 10.666  25.944  -1.858  1.00 73.06  ?  109 TRP D C   1 
ATOM 5756 O O   . TRP D 2 109 ? 11.795  26.339  -2.149  1.00 77.17  ?  109 TRP D O   1 
ATOM 5757 C CB  . TRP D 2 109 ? 9.702   25.588  0.403   1.00 66.85  ?  109 TRP D CB  1 
ATOM 5758 C CG  . TRP D 2 109 ? 9.347   24.694  1.541   1.00 66.66  ?  109 TRP D CG  1 
ATOM 5759 C CD1 . TRP D 2 109 ? 10.204  24.132  2.442   1.00 68.44  ?  109 TRP D CD1 1 
ATOM 5760 C CD2 . TRP D 2 109 ? 8.033   24.270  1.917   1.00 61.18  ?  109 TRP D CD2 1 
ATOM 5761 N NE1 . TRP D 2 109 ? 9.504   23.377  3.351   1.00 71.73  ?  109 TRP D NE1 1 
ATOM 5762 C CE2 . TRP D 2 109 ? 8.168   23.446  3.050   1.00 65.31  ?  109 TRP D CE2 1 
ATOM 5763 C CE3 . TRP D 2 109 ? 6.756   24.504  1.403   1.00 59.45  ?  109 TRP D CE3 1 
ATOM 5764 C CZ2 . TRP D 2 109 ? 7.075   22.856  3.675   1.00 60.89  ?  109 TRP D CZ2 1 
ATOM 5765 C CZ3 . TRP D 2 109 ? 5.675   23.919  2.024   1.00 56.46  ?  109 TRP D CZ3 1 
ATOM 5766 C CH2 . TRP D 2 109 ? 5.840   23.107  3.149   1.00 61.22  ?  109 TRP D CH2 1 
ATOM 5767 N N   . GLY D 2 110 ? 9.557   26.409  -2.437  1.00 71.31  ?  110 GLY D N   1 
ATOM 5768 C CA  . GLY D 2 110 ? 9.574   27.559  -3.310  1.00 60.50  ?  110 GLY D CA  1 
ATOM 5769 C C   . GLY D 2 110 ? 8.584   28.590  -2.797  1.00 71.12  ?  110 GLY D C   1 
ATOM 5770 O O   . GLY D 2 110 ? 7.753   28.304  -1.931  1.00 71.37  ?  110 GLY D O   1 
ATOM 5771 N N   . GLN D 2 111 ? 8.697   29.803  -3.328  1.00 77.63  ?  111 GLN D N   1 
ATOM 5772 C CA  . GLN D 2 111 ? 7.710   30.825  -3.010  1.00 70.90  ?  111 GLN D CA  1 
ATOM 5773 C C   . GLN D 2 111 ? 6.360   30.404  -3.575  1.00 74.21  ?  111 GLN D C   1 
ATOM 5774 O O   . GLN D 2 111 ? 6.280   29.778  -4.637  1.00 81.37  ?  111 GLN D O   1 
ATOM 5775 C CB  . GLN D 2 111 ? 8.141   32.188  -3.565  1.00 64.23  ?  111 GLN D CB  1 
ATOM 5776 C CG  . GLN D 2 111 ? 7.599   32.538  -4.946  1.00 72.05  ?  111 GLN D CG  1 
ATOM 5777 C CD  . GLN D 2 111 ? 8.154   31.643  -6.047  1.00 80.72  ?  111 GLN D CD  1 
ATOM 5778 O OE1 . GLN D 2 111 ? 9.131   30.916  -5.845  1.00 81.94  ?  111 GLN D OE1 1 
ATOM 5779 N NE2 . GLN D 2 111 ? 7.526   31.691  -7.219  1.00 76.98  ?  111 GLN D NE2 1 
ATOM 5780 N N   . GLY D 2 112 ? 5.299   30.700  -2.838  1.00 65.20  ?  112 GLY D N   1 
ATOM 5781 C CA  . GLY D 2 112 ? 3.989   30.262  -3.261  1.00 65.65  ?  112 GLY D CA  1 
ATOM 5782 C C   . GLY D 2 112 ? 3.416   31.112  -4.383  1.00 63.64  ?  112 GLY D C   1 
ATOM 5783 O O   . GLY D 2 112 ? 3.878   32.216  -4.661  1.00 63.87  ?  112 GLY D O   1 
ATOM 5784 N N   . THR D 2 113 ? 2.381   30.578  -5.033  1.00 58.63  ?  113 THR D N   1 
ATOM 5785 C CA  . THR D 2 113 ? 1.580   31.339  -5.986  1.00 55.82  ?  113 THR D CA  1 
ATOM 5786 C C   . THR D 2 113 ? 0.122   31.322  -5.551  1.00 52.23  ?  113 THR D C   1 
ATOM 5787 O O   . THR D 2 113 ? -0.400  30.275  -5.156  1.00 55.63  ?  113 THR D O   1 
ATOM 5788 C CB  . THR D 2 113 ? 1.704   30.785  -7.412  1.00 61.40  ?  113 THR D CB  1 
ATOM 5789 O OG1 . THR D 2 113 ? 1.839   29.358  -7.364  1.00 69.12  ?  113 THR D OG1 1 
ATOM 5790 C CG2 . THR D 2 113 ? 2.890   31.404  -8.146  1.00 63.69  ?  113 THR D CG2 1 
ATOM 5791 N N   . LEU D 2 114 ? -0.531  32.481  -5.621  1.00 39.68  ?  114 LEU D N   1 
ATOM 5792 C CA  . LEU D 2 114 ? -1.900  32.632  -5.140  1.00 40.81  ?  114 LEU D CA  1 
ATOM 5793 C C   . LEU D 2 114 ? -2.879  32.253  -6.245  1.00 45.27  ?  114 LEU D C   1 
ATOM 5794 O O   . LEU D 2 114 ? -2.881  32.869  -7.315  1.00 56.39  ?  114 LEU D O   1 
ATOM 5795 C CB  . LEU D 2 114 ? -2.165  34.065  -4.680  1.00 38.05  ?  114 LEU D CB  1 
ATOM 5796 C CG  . LEU D 2 114 ? -3.583  34.344  -4.161  1.00 41.59  ?  114 LEU D CG  1 
ATOM 5797 C CD1 . LEU D 2 114 ? -3.839  33.639  -2.824  1.00 32.68  ?  114 LEU D CD1 1 
ATOM 5798 C CD2 . LEU D 2 114 ? -3.888  35.836  -4.064  1.00 44.05  ?  114 LEU D CD2 1 
ATOM 5799 N N   . VAL D 2 115 ? -3.700  31.239  -5.991  1.00 43.80  ?  115 VAL D N   1 
ATOM 5800 C CA  . VAL D 2 115 ? -4.790  30.855  -6.878  1.00 45.90  ?  115 VAL D CA  1 
ATOM 5801 C C   . VAL D 2 115 ? -6.097  31.277  -6.221  1.00 51.31  ?  115 VAL D C   1 
ATOM 5802 O O   . VAL D 2 115 ? -6.428  30.806  -5.124  1.00 52.12  ?  115 VAL D O   1 
ATOM 5803 C CB  . VAL D 2 115 ? -4.783  29.349  -7.165  1.00 47.06  ?  115 VAL D CB  1 
ATOM 5804 C CG1 . VAL D 2 115 ? -5.959  28.986  -8.053  1.00 45.52  ?  115 VAL D CG1 1 
ATOM 5805 C CG2 . VAL D 2 115 ? -3.466  28.940  -7.799  1.00 48.28  ?  115 VAL D CG2 1 
ATOM 5806 N N   . THR D 2 116 ? -6.840  32.159  -6.892  1.00 54.60  ?  116 THR D N   1 
ATOM 5807 C CA  . THR D 2 116 ? -8.129  32.660  -6.419  1.00 49.35  ?  116 THR D CA  1 
ATOM 5808 C C   . THR D 2 116 ? -9.207  32.130  -7.359  1.00 52.18  ?  116 THR D C   1 
ATOM 5809 O O   . THR D 2 116 ? -9.217  32.465  -8.548  1.00 57.66  ?  116 THR D O   1 
ATOM 5810 C CB  . THR D 2 116 ? -8.149  34.188  -6.383  1.00 43.91  ?  116 THR D CB  1 
ATOM 5811 O OG1 . THR D 2 116 ? -7.120  34.672  -5.511  1.00 47.42  ?  116 THR D OG1 1 
ATOM 5812 C CG2 . THR D 2 116 ? -9.494  34.690  -5.896  1.00 44.28  ?  116 THR D CG2 1 
ATOM 5813 N N   . VAL D 2 117 ? -10.084 31.277  -6.845  1.00 51.50  ?  117 VAL D N   1 
ATOM 5814 C CA  . VAL D 2 117 ? -11.207 30.742  -7.608  1.00 53.00  ?  117 VAL D CA  1 
ATOM 5815 C C   . VAL D 2 117 ? -12.466 31.486  -7.179  1.00 54.21  ?  117 VAL D C   1 
ATOM 5816 O O   . VAL D 2 117 ? -12.951 31.309  -6.055  1.00 51.59  ?  117 VAL D O   1 
ATOM 5817 C CB  . VAL D 2 117 ? -11.362 29.229  -7.413  1.00 52.87  ?  117 VAL D CB  1 
ATOM 5818 C CG1 . VAL D 2 117 ? -12.485 28.708  -8.284  1.00 50.45  ?  117 VAL D CG1 1 
ATOM 5819 C CG2 . VAL D 2 117 ? -10.060 28.510  -7.732  1.00 48.06  ?  117 VAL D CG2 1 
ATOM 5820 N N   . SER D 2 118 ? -12.993 32.327  -8.069  1.00 55.59  ?  118 SER D N   1 
ATOM 5821 C CA  . SER D 2 118 ? -14.208 33.087  -7.801  1.00 51.39  ?  118 SER D CA  1 
ATOM 5822 C C   . SER D 2 118 ? -14.827 33.514  -9.122  1.00 56.72  ?  118 SER D C   1 
ATOM 5823 O O   . SER D 2 118 ? -14.143 33.609  -10.146 1.00 56.58  ?  118 SER D O   1 
ATOM 5824 C CB  . SER D 2 118 ? -13.921 34.311  -6.928  1.00 54.24  ?  118 SER D CB  1 
ATOM 5825 O OG  . SER D 2 118 ? -14.952 35.275  -7.051  1.00 56.67  ?  118 SER D OG  1 
ATOM 5826 N N   . SER D 2 119 ? -16.135 33.776  -9.089  1.00 60.48  ?  119 SER D N   1 
ATOM 5827 C CA  . SER D 2 119 ? -16.839 34.270  -10.269 1.00 57.11  ?  119 SER D CA  1 
ATOM 5828 C C   . SER D 2 119 ? -16.880 35.792  -10.330 1.00 54.33  ?  119 SER D C   1 
ATOM 5829 O O   . SER D 2 119 ? -17.404 36.344  -11.304 1.00 64.24  ?  119 SER D O   1 
ATOM 5830 C CB  . SER D 2 119 ? -18.265 33.699  -10.350 1.00 48.68  ?  119 SER D CB  1 
ATOM 5831 O OG  . SER D 2 119 ? -19.017 33.964  -9.181  1.00 63.93  ?  119 SER D OG  1 
ATOM 5832 N N   . ALA D 2 120 ? -16.354 36.481  -9.319  1.00 48.50  ?  120 ALA D N   1 
ATOM 5833 C CA  . ALA D 2 120 ? -16.283 37.932  -9.374  1.00 54.20  ?  120 ALA D CA  1 
ATOM 5834 C C   . ALA D 2 120 ? -15.293 38.380  -10.448 1.00 58.20  ?  120 ALA D C   1 
ATOM 5835 O O   . ALA D 2 120 ? -14.458 37.609  -10.930 1.00 58.23  ?  120 ALA D O   1 
ATOM 5836 C CB  . ALA D 2 120 ? -15.875 38.505  -8.018  1.00 46.46  ?  120 ALA D CB  1 
ATOM 5837 N N   . SER D 2 121 ? -15.385 39.654  -10.810 1.00 56.57  ?  121 SER D N   1 
ATOM 5838 C CA  . SER D 2 121 ? -14.527 40.244  -11.825 1.00 55.83  ?  121 SER D CA  1 
ATOM 5839 C C   . SER D 2 121 ? -13.457 41.095  -11.160 1.00 55.64  ?  121 SER D C   1 
ATOM 5840 O O   . SER D 2 121 ? -13.653 41.615  -10.059 1.00 48.98  ?  121 SER D O   1 
ATOM 5841 C CB  . SER D 2 121 ? -15.333 41.106  -12.797 1.00 53.88  ?  121 SER D CB  1 
ATOM 5842 O OG  . SER D 2 121 ? -16.563 40.490  -13.126 1.00 59.69  ?  121 SER D OG  1 
ATOM 5843 N N   . THR D 2 122 ? -12.323 41.243  -11.842 1.00 56.56  ?  122 THR D N   1 
ATOM 5844 C CA  . THR D 2 122 ? -11.260 42.066  -11.289 1.00 54.56  ?  122 THR D CA  1 
ATOM 5845 C C   . THR D 2 122 ? -11.749 43.502  -11.194 1.00 54.27  ?  122 THR D C   1 
ATOM 5846 O O   . THR D 2 122 ? -12.280 44.056  -12.160 1.00 62.88  ?  122 THR D O   1 
ATOM 5847 C CB  . THR D 2 122 ? -10.005 41.982  -12.158 1.00 54.58  ?  122 THR D CB  1 
ATOM 5848 O OG1 . THR D 2 122 ? -9.459  40.661  -12.099 1.00 56.82  ?  122 THR D OG1 1 
ATOM 5849 C CG2 . THR D 2 122 ? -8.958  42.974  -11.682 1.00 59.44  ?  122 THR D CG2 1 
ATOM 5850 N N   . LYS D 2 123 ? -11.591 44.094  -10.017 1.00 51.47  ?  123 LYS D N   1 
ATOM 5851 C CA  . LYS D 2 123 ? -12.082 45.436  -9.759  1.00 50.38  ?  123 LYS D CA  1 
ATOM 5852 C C   . LYS D 2 123 ? -11.092 46.184  -8.885  1.00 51.65  ?  123 LYS D C   1 
ATOM 5853 O O   . LYS D 2 123 ? -10.563 45.628  -7.918  1.00 50.81  ?  123 LYS D O   1 
ATOM 5854 C CB  . LYS D 2 123 ? -13.462 45.399  -9.081  1.00 48.23  ?  123 LYS D CB  1 
ATOM 5855 C CG  . LYS D 2 123 ? -14.063 46.763  -8.780  1.00 48.93  ?  123 LYS D CG  1 
ATOM 5856 C CD  . LYS D 2 123 ? -15.529 46.635  -8.411  1.00 49.20  ?  123 LYS D CD  1 
ATOM 5857 C CE  . LYS D 2 123 ? -16.227 47.984  -8.408  1.00 60.61  ?  123 LYS D CE  1 
ATOM 5858 N NZ  . LYS D 2 123 ? -17.713 47.826  -8.411  1.00 64.78  ?  123 LYS D NZ  1 
ATOM 5859 N N   . GLY D 2 124 ? -10.842 47.441  -9.236  1.00 47.71  ?  124 GLY D N   1 
ATOM 5860 C CA  . GLY D 2 124 ? -10.056 48.310  -8.404  1.00 45.01  ?  124 GLY D CA  1 
ATOM 5861 C C   . GLY D 2 124 ? -10.906 48.750  -7.231  1.00 47.42  ?  124 GLY D C   1 
ATOM 5862 O O   . GLY D 2 124 ? -12.142 48.719  -7.284  1.00 42.00  ?  124 GLY D O   1 
ATOM 5863 N N   . PRO D 2 125 ? -10.260 49.153  -6.140  1.00 45.95  ?  125 PRO D N   1 
ATOM 5864 C CA  . PRO D 2 125 ? -10.991 49.502  -4.923  1.00 44.39  ?  125 PRO D CA  1 
ATOM 5865 C C   . PRO D 2 125 ? -11.459 50.946  -4.930  1.00 42.01  ?  125 PRO D C   1 
ATOM 5866 O O   . PRO D 2 125 ? -10.887 51.813  -5.592  1.00 39.99  ?  125 PRO D O   1 
ATOM 5867 C CB  . PRO D 2 125 ? -9.937  49.293  -3.829  1.00 44.15  ?  125 PRO D CB  1 
ATOM 5868 C CG  . PRO D 2 125 ? -8.666  49.691  -4.500  1.00 44.27  ?  125 PRO D CG  1 
ATOM 5869 C CD  . PRO D 2 125 ? -8.803  49.255  -5.950  1.00 47.51  ?  125 PRO D CD  1 
ATOM 5870 N N   . SER D 2 126 ? -12.517 51.194  -4.168  1.00 39.82  ?  126 SER D N   1 
ATOM 5871 C CA  . SER D 2 126 ? -12.939 52.549  -3.849  1.00 43.13  ?  126 SER D CA  1 
ATOM 5872 C C   . SER D 2 126 ? -12.354 52.916  -2.491  1.00 45.03  ?  126 SER D C   1 
ATOM 5873 O O   . SER D 2 126 ? -12.415 52.116  -1.549  1.00 48.09  ?  126 SER D O   1 
ATOM 5874 C CB  . SER D 2 126 ? -14.462 52.666  -3.834  1.00 47.45  ?  126 SER D CB  1 
ATOM 5875 O OG  . SER D 2 126 ? -14.990 52.514  -5.139  1.00 48.64  ?  126 SER D OG  1 
ATOM 5876 N N   . VAL D 2 127 ? -11.748 54.096  -2.399  1.00 36.12  ?  127 VAL D N   1 
ATOM 5877 C CA  . VAL D 2 127 ? -11.021 54.502  -1.201  1.00 37.30  ?  127 VAL D CA  1 
ATOM 5878 C C   . VAL D 2 127 ? -11.721 55.705  -0.583  1.00 39.25  ?  127 VAL D C   1 
ATOM 5879 O O   . VAL D 2 127 ? -11.627 56.825  -1.103  1.00 43.80  ?  127 VAL D O   1 
ATOM 5880 C CB  . VAL D 2 127 ? -9.552  54.813  -1.503  1.00 37.33  ?  127 VAL D CB  1 
ATOM 5881 C CG1 . VAL D 2 127 ? -8.818  55.127  -0.218  1.00 41.56  ?  127 VAL D CG1 1 
ATOM 5882 C CG2 . VAL D 2 127 ? -8.906  53.639  -2.223  1.00 35.32  ?  127 VAL D CG2 1 
ATOM 5883 N N   . PHE D 2 128 ? -12.403 55.481  0.580   1.00 46.43  ?  128 PHE D N   1 
ATOM 5884 C CA  . PHE D 2 128 ? -13.106 56.541  1.290   1.00 48.23  ?  128 PHE D CA  1 
ATOM 5885 C C   . PHE D 2 128 ? -12.314 56.975  2.519   1.00 45.78  ?  128 PHE D C   1 
ATOM 5886 O O   . PHE D 2 128 ? -11.485 56.217  3.025   1.00 49.15  ?  128 PHE D O   1 
ATOM 5887 C CB  . PHE D 2 128 ? -14.504 56.072  1.707   1.00 43.07  ?  128 PHE D CB  1 
ATOM 5888 C CG  . PHE D 2 128 ? -15.340 55.594  0.554   1.00 53.32  ?  128 PHE D CG  1 
ATOM 5889 C CD1 . PHE D 2 128 ? -15.732 56.472  -0.447  1.00 61.83  ?  128 PHE D CD1 1 
ATOM 5890 C CD2 . PHE D 2 128 ? -15.717 54.270  0.453   1.00 50.83  ?  128 PHE D CD2 1 
ATOM 5891 C CE1 . PHE D 2 128 ? -16.494 56.032  -1.524  1.00 56.97  ?  128 PHE D CE1 1 
ATOM 5892 C CE2 . PHE D 2 128 ? -16.473 53.829  -0.619  1.00 49.32  ?  128 PHE D CE2 1 
ATOM 5893 C CZ  . PHE D 2 128 ? -16.864 54.712  -1.605  1.00 50.50  ?  128 PHE D CZ  1 
ATOM 5894 N N   . PRO D 2 129 ? -12.494 58.205  3.004   1.00 50.51  ?  129 PRO D N   1 
ATOM 5895 C CA  . PRO D 2 129 ? -11.731 58.651  4.175   1.00 49.59  ?  129 PRO D CA  1 
ATOM 5896 C C   . PRO D 2 129 ? -12.448 58.383  5.490   1.00 46.50  ?  129 PRO D C   1 
ATOM 5897 O O   . PRO D 2 129 ? -13.648 58.626  5.639   1.00 49.96  ?  129 PRO D O   1 
ATOM 5898 C CB  . PRO D 2 129 ? -11.605 60.160  3.933   1.00 47.00  ?  129 PRO D CB  1 
ATOM 5899 C CG  . PRO D 2 129 ? -12.885 60.505  3.242   1.00 44.80  ?  129 PRO D CG  1 
ATOM 5900 C CD  . PRO D 2 129 ? -13.263 59.308  2.398   1.00 47.14  ?  129 PRO D CD  1 
ATOM 5901 N N   . LEU D 2 130 ? -11.693 57.867  6.460   1.00 48.50  ?  130 LEU D N   1 
ATOM 5902 C CA  . LEU D 2 130 ? -12.119 57.818  7.857   1.00 56.16  ?  130 LEU D CA  1 
ATOM 5903 C C   . LEU D 2 130 ? -11.498 59.051  8.507   1.00 53.94  ?  130 LEU D C   1 
ATOM 5904 O O   . LEU D 2 130 ? -10.387 59.006  9.041   1.00 49.20  ?  130 LEU D O   1 
ATOM 5905 C CB  . LEU D 2 130 ? -11.678 56.517  8.519   1.00 50.14  ?  130 LEU D CB  1 
ATOM 5906 C CG  . LEU D 2 130 ? -12.209 55.240  7.867   1.00 48.37  ?  130 LEU D CG  1 
ATOM 5907 C CD1 . LEU D 2 130 ? -11.798 54.014  8.663   1.00 44.02  ?  130 LEU D CD1 1 
ATOM 5908 C CD2 . LEU D 2 130 ? -13.724 55.314  7.743   1.00 45.12  ?  130 LEU D CD2 1 
ATOM 5909 N N   . ALA D 2 131 ? -12.235 60.158  8.447   1.00 53.85  ?  131 ALA D N   1 
ATOM 5910 C CA  . ALA D 2 131 ? -11.669 61.464  8.737   1.00 62.74  ?  131 ALA D CA  1 
ATOM 5911 C C   . ALA D 2 131 ? -11.473 61.642  10.239  1.00 63.09  ?  131 ALA D C   1 
ATOM 5912 O O   . ALA D 2 131 ? -12.320 61.211  11.031  1.00 60.40  ?  131 ALA D O   1 
ATOM 5913 C CB  . ALA D 2 131 ? -12.578 62.568  8.194   1.00 67.49  ?  131 ALA D CB  1 
ATOM 5914 N N   . PRO D 2 132 ? -10.388 62.292  10.663  1.00 63.49  ?  132 PRO D N   1 
ATOM 5915 C CA  . PRO D 2 132 ? -10.194 62.537  12.092  1.00 66.13  ?  132 PRO D CA  1 
ATOM 5916 C C   . PRO D 2 132 ? -11.248 63.489  12.624  1.00 72.67  ?  132 PRO D C   1 
ATOM 5917 O O   . PRO D 2 132 ? -11.622 64.464  11.971  1.00 81.27  ?  132 PRO D O   1 
ATOM 5918 C CB  . PRO D 2 132 ? -8.794  63.155  12.159  1.00 60.93  ?  132 PRO D CB  1 
ATOM 5919 C CG  . PRO D 2 132 ? -8.607  63.780  10.819  1.00 64.77  ?  132 PRO D CG  1 
ATOM 5920 C CD  . PRO D 2 132 ? -9.307  62.877  9.852   1.00 65.31  ?  132 PRO D CD  1 
ATOM 5921 N N   . SER D 2 133 ? -11.722 63.198  13.824  1.00 73.88  ?  133 SER D N   1 
ATOM 5922 C CA  . SER D 2 133 ? -12.800 63.952  14.432  1.00 86.88  ?  133 SER D CA  1 
ATOM 5923 C C   . SER D 2 133 ? -12.228 64.909  15.472  1.00 97.27  ?  133 SER D C   1 
ATOM 5924 O O   . SER D 2 133 ? -11.012 65.116  15.566  1.00 94.19  ?  133 SER D O   1 
ATOM 5925 C CB  . SER D 2 133 ? -13.822 63.000  15.057  1.00 91.56  ?  133 SER D CB  1 
ATOM 5926 O OG  . SER D 2 133 ? -13.328 62.444  16.270  1.00 82.05  ?  133 SER D OG  1 
ATOM 5927 N N   . SER D 2 134 ? -13.115 65.500  16.267  1.00 97.10  ?  134 SER D N   1 
ATOM 5928 C CA  . SER D 2 134 ? -12.715 66.466  17.278  1.00 92.36  ?  134 SER D CA  1 
ATOM 5929 C C   . SER D 2 134 ? -13.273 66.046  18.631  1.00 94.71  ?  134 SER D C   1 
ATOM 5930 O O   . SER D 2 134 ? -12.559 65.487  19.469  1.00 91.28  ?  134 SER D O   1 
ATOM 5931 C CB  . SER D 2 134 ? -13.199 67.871  16.906  1.00 95.16  ?  134 SER D CB  1 
ATOM 5932 O OG  . SER D 2 134 ? -12.750 68.254  15.614  1.00 97.69  ?  134 SER D OG  1 
ATOM 5933 N N   . LYS D 2 135 ? -14.555 66.316  18.842  1.00 96.76  ?  135 LYS D N   1 
ATOM 5934 C CA  . LYS D 2 135 ? -15.219 66.032  20.107  1.00 84.51  ?  135 LYS D CA  1 
ATOM 5935 C C   . LYS D 2 135 ? -15.840 64.640  20.160  1.00 76.12  ?  135 LYS D C   1 
ATOM 5936 O O   . LYS D 2 135 ? -16.949 64.468  20.664  1.00 74.18  ?  135 LYS D O   1 
ATOM 5937 C CB  . LYS D 2 135 ? -16.264 67.110  20.356  1.00 86.55  ?  135 LYS D CB  1 
ATOM 5938 C CG  . LYS D 2 135 ? -15.575 68.450  20.536  1.00 95.10  ?  135 LYS D CG  1 
ATOM 5939 C CD  . LYS D 2 135 ? -16.442 69.551  21.083  1.00 90.23  ?  135 LYS D CD  1 
ATOM 5940 C CE  . LYS D 2 135 ? -15.622 70.829  21.094  1.00 85.00  ?  135 LYS D CE  1 
ATOM 5941 N NZ  . LYS D 2 135 ? -16.394 72.027  21.483  1.00 86.41  ?  135 LYS D NZ  1 
ATOM 5942 N N   . GLY D 2 139 ? -8.336  62.712  23.150  1.00 81.68  ?  139 GLY D N   1 
ATOM 5943 C CA  . GLY D 2 139 ? -7.179  63.077  23.949  1.00 86.54  ?  139 GLY D CA  1 
ATOM 5944 C C   . GLY D 2 139 ? -6.208  63.962  23.196  1.00 91.75  ?  139 GLY D C   1 
ATOM 5945 O O   . GLY D 2 139 ? -6.617  64.905  22.512  1.00 95.10  ?  139 GLY D O   1 
ATOM 5946 N N   . GLY D 2 140 ? -4.912  63.676  23.325  1.00 90.26  ?  140 GLY D N   1 
ATOM 5947 C CA  . GLY D 2 140 ? -3.937  64.446  22.581  1.00 88.87  ?  140 GLY D CA  1 
ATOM 5948 C C   . GLY D 2 140 ? -3.574  63.868  21.236  1.00 77.28  ?  140 GLY D C   1 
ATOM 5949 O O   . GLY D 2 140 ? -2.919  64.542  20.434  1.00 73.13  ?  140 GLY D O   1 
ATOM 5950 N N   . THR D 2 141 ? -3.998  62.637  20.958  1.00 78.89  ?  141 THR D N   1 
ATOM 5951 C CA  . THR D 2 141 ? -3.796  61.986  19.671  1.00 75.70  ?  141 THR D CA  1 
ATOM 5952 C C   . THR D 2 141 ? -5.131  61.842  18.954  1.00 72.48  ?  141 THR D C   1 
ATOM 5953 O O   . THR D 2 141 ? -6.184  61.715  19.588  1.00 68.46  ?  141 THR D O   1 
ATOM 5954 C CB  . THR D 2 141 ? -3.148  60.602  19.818  1.00 67.37  ?  141 THR D CB  1 
ATOM 5955 O OG1 . THR D 2 141 ? -4.033  59.728  20.530  1.00 72.49  ?  141 THR D OG1 1 
ATOM 5956 C CG2 . THR D 2 141 ? -1.819  60.701  20.560  1.00 65.40  ?  141 THR D CG2 1 
ATOM 5957 N N   . ALA D 2 142 ? -5.081  61.857  17.624  1.00 68.81  ?  142 ALA D N   1 
ATOM 5958 C CA  . ALA D 2 142 ? -6.265  61.649  16.806  1.00 63.68  ?  142 ALA D CA  1 
ATOM 5959 C C   . ALA D 2 142 ? -6.051  60.440  15.905  1.00 58.63  ?  142 ALA D C   1 
ATOM 5960 O O   . ALA D 2 142 ? -4.916  60.086  15.570  1.00 55.48  ?  142 ALA D O   1 
ATOM 5961 C CB  . ALA D 2 142 ? -6.591  62.883  15.967  1.00 61.82  ?  142 ALA D CB  1 
ATOM 5962 N N   . ALA D 2 143 ? -7.155  59.807  15.515  1.00 56.41  ?  143 ALA D N   1 
ATOM 5963 C CA  . ALA D 2 143 ? -7.129  58.614  14.678  1.00 52.94  ?  143 ALA D CA  1 
ATOM 5964 C C   . ALA D 2 143 ? -7.796  58.917  13.348  1.00 51.60  ?  143 ALA D C   1 
ATOM 5965 O O   . ALA D 2 143 ? -8.928  59.409  13.317  1.00 54.58  ?  143 ALA D O   1 
ATOM 5966 C CB  . ALA D 2 143 ? -7.838  57.446  15.367  1.00 52.23  ?  143 ALA D CB  1 
ATOM 5967 N N   . LEU D 2 144 ? -7.104  58.604  12.256  1.00 45.68  ?  144 LEU D N   1 
ATOM 5968 C CA  . LEU D 2 144 ? -7.638  58.801  10.917  1.00 52.00  ?  144 LEU D CA  1 
ATOM 5969 C C   . LEU D 2 144 ? -7.253  57.608  10.057  1.00 52.25  ?  144 LEU D C   1 
ATOM 5970 O O   . LEU D 2 144 ? -6.381  56.812  10.416  1.00 54.81  ?  144 LEU D O   1 
ATOM 5971 C CB  . LEU D 2 144 ? -7.126  60.108  10.297  1.00 50.42  ?  144 LEU D CB  1 
ATOM 5972 C CG  . LEU D 2 144 ? -5.609  60.266  10.173  1.00 47.94  ?  144 LEU D CG  1 
ATOM 5973 C CD1 . LEU D 2 144 ? -5.123  59.856  8.786   1.00 53.33  ?  144 LEU D CD1 1 
ATOM 5974 C CD2 . LEU D 2 144 ? -5.201  61.689  10.482  1.00 54.20  ?  144 LEU D CD2 1 
ATOM 5975 N N   . GLY D 2 145 ? -7.899  57.481  8.908   1.00 47.33  ?  145 GLY D N   1 
ATOM 5976 C CA  . GLY D 2 145 ? -7.555  56.350  8.078   1.00 51.89  ?  145 GLY D CA  1 
ATOM 5977 C C   . GLY D 2 145 ? -8.242  56.357  6.734   1.00 51.19  ?  145 GLY D C   1 
ATOM 5978 O O   . GLY D 2 145 ? -8.890  57.327  6.340   1.00 51.17  ?  145 GLY D O   1 
ATOM 5979 N N   . CYS D 2 146 ? -8.099  55.230  6.047   1.00 51.48  ?  146 CYS D N   1 
ATOM 5980 C CA  . CYS D 2 146 ? -8.686  55.000  4.741   1.00 47.00  ?  146 CYS D CA  1 
ATOM 5981 C C   . CYS D 2 146 ? -9.473  53.705  4.777   1.00 44.05  ?  146 CYS D C   1 
ATOM 5982 O O   . CYS D 2 146 ? -9.004  52.702  5.319   1.00 48.20  ?  146 CYS D O   1 
ATOM 5983 C CB  . CYS D 2 146 ? -7.606  54.917  3.653   1.00 41.00  ?  146 CYS D CB  1 
ATOM 5984 S SG  . CYS D 2 146 ? -6.956  56.522  3.217   1.00 71.83  ?  146 CYS D SG  1 
ATOM 5985 N N   . LEU D 2 147 ? -10.678 53.740  4.224   1.00 43.33  ?  147 LEU D N   1 
ATOM 5986 C CA  . LEU D 2 147 ? -11.492 52.550  4.029   1.00 49.59  ?  147 LEU D CA  1 
ATOM 5987 C C   . LEU D 2 147 ? -11.333 52.137  2.570   1.00 48.61  ?  147 LEU D C   1 
ATOM 5988 O O   . LEU D 2 147 ? -11.794 52.844  1.668   1.00 45.52  ?  147 LEU D O   1 
ATOM 5989 C CB  . LEU D 2 147 ? -12.953 52.821  4.377   1.00 45.86  ?  147 LEU D CB  1 
ATOM 5990 C CG  . LEU D 2 147 ? -13.943 51.731  3.963   1.00 50.60  ?  147 LEU D CG  1 
ATOM 5991 C CD1 . LEU D 2 147 ? -13.645 50.402  4.651   1.00 46.86  ?  147 LEU D CD1 1 
ATOM 5992 C CD2 . LEU D 2 147 ? -15.358 52.188  4.264   1.00 52.15  ?  147 LEU D CD2 1 
ATOM 5993 N N   . VAL D 2 148 ? -10.660 51.014  2.344   1.00 45.67  ?  148 VAL D N   1 
ATOM 5994 C CA  . VAL D 2 148 ? -10.423 50.480  1.007   1.00 47.32  ?  148 VAL D CA  1 
ATOM 5995 C C   . VAL D 2 148 ? -11.444 49.372  0.780   1.00 51.03  ?  148 VAL D C   1 
ATOM 5996 O O   . VAL D 2 148 ? -11.321 48.276  1.342   1.00 53.54  ?  148 VAL D O   1 
ATOM 5997 C CB  . VAL D 2 148 ? -8.985  49.965  0.864   1.00 45.10  ?  148 VAL D CB  1 
ATOM 5998 C CG1 . VAL D 2 148 ? -8.715  49.530  -0.548  1.00 45.83  ?  148 VAL D CG1 1 
ATOM 5999 C CG2 . VAL D 2 148 ? -7.998  51.043  1.288   1.00 43.34  ?  148 VAL D CG2 1 
ATOM 6000 N N   . LYS D 2 149 ? -12.452 49.636  -0.050  1.00 45.71  ?  149 LYS D N   1 
ATOM 6001 C CA  . LYS D 2 149 ? -13.605 48.755  -0.145  1.00 49.59  ?  149 LYS D CA  1 
ATOM 6002 C C   . LYS D 2 149 ? -13.835 48.275  -1.574  1.00 50.34  ?  149 LYS D C   1 
ATOM 6003 O O   . LYS D 2 149 ? -13.535 48.976  -2.550  1.00 48.92  ?  149 LYS D O   1 
ATOM 6004 C CB  . LYS D 2 149 ? -14.872 49.465  0.375   1.00 44.77  ?  149 LYS D CB  1 
ATOM 6005 C CG  . LYS D 2 149 ? -15.958 48.503  0.844   1.00 51.37  ?  149 LYS D CG  1 
ATOM 6006 C CD  . LYS D 2 149 ? -17.289 49.204  1.055   1.00 47.71  ?  149 LYS D CD  1 
ATOM 6007 C CE  . LYS D 2 149 ? -18.318 48.256  1.659   1.00 48.94  ?  149 LYS D CE  1 
ATOM 6008 N NZ  . LYS D 2 149 ? -18.959 47.394  0.629   1.00 51.04  ?  149 LYS D NZ  1 
ATOM 6009 N N   . ASP D 2 150 ? -14.371 47.058  -1.676  1.00 47.78  ?  150 ASP D N   1 
ATOM 6010 C CA  . ASP D 2 150 ? -14.881 46.492  -2.925  1.00 53.20  ?  150 ASP D CA  1 
ATOM 6011 C C   . ASP D 2 150 ? -13.781 46.417  -3.989  1.00 48.74  ?  150 ASP D C   1 
ATOM 6012 O O   . ASP D 2 150 ? -13.780 47.140  -4.987  1.00 52.89  ?  150 ASP D O   1 
ATOM 6013 C CB  . ASP D 2 150 ? -16.095 47.286  -3.421  1.00 48.43  ?  150 ASP D CB  1 
ATOM 6014 C CG  . ASP D 2 150 ? -17.262 47.227  -2.449  1.00 51.28  ?  150 ASP D CG  1 
ATOM 6015 O OD1 . ASP D 2 150 ? -17.364 46.228  -1.705  1.00 51.44  ?  150 ASP D OD1 1 
ATOM 6016 O OD2 . ASP D 2 150 ? -18.072 48.178  -2.419  1.00 57.72  -1 150 ASP D OD2 1 
ATOM 6017 N N   . TYR D 2 151 ? -12.841 45.505  -3.746  1.00 45.29  ?  151 TYR D N   1 
ATOM 6018 C CA  . TYR D 2 151 ? -11.773 45.234  -4.692  1.00 45.65  ?  151 TYR D CA  1 
ATOM 6019 C C   . TYR D 2 151 ? -11.620 43.733  -4.861  1.00 47.77  ?  151 TYR D C   1 
ATOM 6020 O O   . TYR D 2 151 ? -12.062 42.944  -4.020  1.00 53.14  ?  151 TYR D O   1 
ATOM 6021 C CB  . TYR D 2 151 ? -10.438 45.867  -4.254  1.00 51.93  ?  151 TYR D CB  1 
ATOM 6022 C CG  . TYR D 2 151 ? -9.719  45.208  -3.089  1.00 48.82  ?  151 TYR D CG  1 
ATOM 6023 C CD1 . TYR D 2 151 ? -9.911  45.645  -1.789  1.00 46.81  ?  151 TYR D CD1 1 
ATOM 6024 C CD2 . TYR D 2 151 ? -8.821  44.169  -3.301  1.00 50.13  ?  151 TYR D CD2 1 
ATOM 6025 C CE1 . TYR D 2 151 ? -9.243  45.051  -0.732  1.00 47.70  ?  151 TYR D CE1 1 
ATOM 6026 C CE2 . TYR D 2 151 ? -8.151  43.573  -2.249  1.00 49.64  ?  151 TYR D CE2 1 
ATOM 6027 C CZ  . TYR D 2 151 ? -8.363  44.018  -0.968  1.00 49.70  ?  151 TYR D CZ  1 
ATOM 6028 O OH  . TYR D 2 151 ? -7.695  43.418  0.077   1.00 49.54  ?  151 TYR D OH  1 
ATOM 6029 N N   . PHE D 2 152 ? -10.984 43.345  -5.965  1.00 47.70  ?  152 PHE D N   1 
ATOM 6030 C CA  . PHE D 2 152 ? -10.797 41.930  -6.266  1.00 50.62  ?  152 PHE D CA  1 
ATOM 6031 C C   . PHE D 2 152 ? -9.799  41.741  -7.405  1.00 54.04  ?  152 PHE D C   1 
ATOM 6032 O O   . PHE D 2 152 ? -9.862  42.456  -8.413  1.00 52.80  ?  152 PHE D O   1 
ATOM 6033 C CB  . PHE D 2 152 ? -12.139 41.285  -6.625  1.00 46.17  ?  152 PHE D CB  1 
ATOM 6034 C CG  . PHE D 2 152 ? -12.073 39.799  -6.773  1.00 52.17  ?  152 PHE D CG  1 
ATOM 6035 C CD1 . PHE D 2 152 ? -11.752 39.227  -7.996  1.00 53.37  ?  152 PHE D CD1 1 
ATOM 6036 C CD2 . PHE D 2 152 ? -12.327 38.968  -5.685  1.00 50.85  ?  152 PHE D CD2 1 
ATOM 6037 C CE1 . PHE D 2 152 ? -11.687 37.866  -8.134  1.00 51.88  ?  152 PHE D CE1 1 
ATOM 6038 C CE2 . PHE D 2 152 ? -12.263 37.600  -5.809  1.00 42.87  ?  152 PHE D CE2 1 
ATOM 6039 C CZ  . PHE D 2 152 ? -11.939 37.046  -7.037  1.00 57.01  ?  152 PHE D CZ  1 
ATOM 6040 N N   . PRO D 2 153 ? -8.862  40.791  -7.287  1.00 53.63  ?  153 PRO D N   1 
ATOM 6041 C CA  . PRO D 2 153 ? -8.661  39.952  -6.105  1.00 49.30  ?  153 PRO D CA  1 
ATOM 6042 C C   . PRO D 2 153 ? -7.586  40.513  -5.172  1.00 49.86  ?  153 PRO D C   1 
ATOM 6043 O O   . PRO D 2 153 ? -7.157  41.655  -5.344  1.00 45.20  ?  153 PRO D O   1 
ATOM 6044 C CB  . PRO D 2 153 ? -8.205  38.631  -6.713  1.00 49.84  ?  153 PRO D CB  1 
ATOM 6045 C CG  . PRO D 2 153 ? -7.381  39.065  -7.886  1.00 47.95  ?  153 PRO D CG  1 
ATOM 6046 C CD  . PRO D 2 153 ? -8.042  40.326  -8.423  1.00 48.61  ?  153 PRO D CD  1 
ATOM 6047 N N   . GLU D 2 154 ? -7.157  39.706  -4.201  1.00 51.06  ?  154 GLU D N   1 
ATOM 6048 C CA  . GLU D 2 154 ? -6.000  40.047  -3.390  1.00 49.25  ?  154 GLU D CA  1 
ATOM 6049 C C   . GLU D 2 154 ? -4.732  40.003  -4.246  1.00 56.45  ?  154 GLU D C   1 
ATOM 6050 O O   . GLU D 2 154 ? -4.675  39.281  -5.248  1.00 57.42  ?  154 GLU D O   1 
ATOM 6051 C CB  . GLU D 2 154 ? -5.870  39.078  -2.216  1.00 43.71  ?  154 GLU D CB  1 
ATOM 6052 C CG  . GLU D 2 154 ? -6.877  39.266  -1.086  1.00 47.06  ?  154 GLU D CG  1 
ATOM 6053 C CD  . GLU D 2 154 ? -6.305  40.060  0.084   1.00 56.44  ?  154 GLU D CD  1 
ATOM 6054 O OE1 . GLU D 2 154 ? -5.949  41.247  -0.099  1.00 52.70  ?  154 GLU D OE1 1 
ATOM 6055 O OE2 . GLU D 2 154 ? -6.176  39.480  1.184   1.00 56.11  -1 154 GLU D OE2 1 
ATOM 6056 N N   . PRO D 2 155 ? -3.677  40.744  -3.853  1.00 52.63  ?  155 PRO D N   1 
ATOM 6057 C CA  . PRO D 2 155 ? -3.516  41.577  -2.660  1.00 52.07  ?  155 PRO D CA  1 
ATOM 6058 C C   . PRO D 2 155 ? -3.550  43.083  -2.922  1.00 48.15  ?  155 PRO D C   1 
ATOM 6059 O O   . PRO D 2 155 ? -3.500  43.505  -4.075  1.00 49.75  ?  155 PRO D O   1 
ATOM 6060 C CB  . PRO D 2 155 ? -2.134  41.165  -2.167  1.00 51.12  ?  155 PRO D CB  1 
ATOM 6061 C CG  . PRO D 2 155 ? -1.369  40.962  -3.448  1.00 40.32  ?  155 PRO D CG  1 
ATOM 6062 C CD  . PRO D 2 155 ? -2.374  40.513  -4.503  1.00 55.39  ?  155 PRO D CD  1 
ATOM 6063 N N   . VAL D 2 156 ? -3.618  43.874  -1.848  1.00 46.84  ?  156 VAL D N   1 
ATOM 6064 C CA  . VAL D 2 156 ? -3.476  45.326  -1.901  1.00 47.65  ?  156 VAL D CA  1 
ATOM 6065 C C   . VAL D 2 156 ? -2.352  45.742  -0.968  1.00 50.22  ?  156 VAL D C   1 
ATOM 6066 O O   . VAL D 2 156 ? -2.116  45.131  0.078   1.00 48.28  ?  156 VAL D O   1 
ATOM 6067 C CB  . VAL D 2 156 ? -4.750  46.110  -1.513  1.00 43.70  ?  156 VAL D CB  1 
ATOM 6068 C CG1 . VAL D 2 156 ? -5.762  46.141  -2.645  1.00 53.31  ?  156 VAL D CG1 1 
ATOM 6069 C CG2 . VAL D 2 156 ? -5.340  45.543  -0.254  1.00 49.23  ?  156 VAL D CG2 1 
ATOM 6070 N N   . THR D 2 157 ? -1.660  46.802  -1.362  1.00 54.89  ?  157 THR D N   1 
ATOM 6071 C CA  . THR D 2 157 ? -0.593  47.394  -0.575  1.00 50.81  ?  157 THR D CA  1 
ATOM 6072 C C   . THR D 2 157 ? -1.018  48.798  -0.186  1.00 50.11  ?  157 THR D C   1 
ATOM 6073 O O   . THR D 2 157 ? -1.444  49.578  -1.040  1.00 59.53  ?  157 THR D O   1 
ATOM 6074 C CB  . THR D 2 157 ? 0.718   47.425  -1.362  1.00 53.88  ?  157 THR D CB  1 
ATOM 6075 O OG1 . THR D 2 157 ? 1.260   46.102  -1.428  1.00 57.78  ?  157 THR D OG1 1 
ATOM 6076 C CG2 . THR D 2 157 ? 1.719   48.362  -0.698  1.00 59.91  ?  157 THR D CG2 1 
ATOM 6077 N N   . VAL D 2 158 ? -0.935  49.110  1.099   1.00 48.60  ?  158 VAL D N   1 
ATOM 6078 C CA  . VAL D 2 158 ? -1.277  50.434  1.591   1.00 55.00  ?  158 VAL D CA  1 
ATOM 6079 C C   . VAL D 2 158 ? -0.049  51.044  2.249   1.00 57.95  ?  158 VAL D C   1 
ATOM 6080 O O   . VAL D 2 158 ? 0.732   50.347  2.904   1.00 57.29  ?  158 VAL D O   1 
ATOM 6081 C CB  . VAL D 2 158 ? -2.466  50.391  2.570   1.00 51.51  ?  158 VAL D CB  1 
ATOM 6082 C CG1 . VAL D 2 158 ? -2.876  51.800  2.963   1.00 55.28  ?  158 VAL D CG1 1 
ATOM 6083 C CG2 . VAL D 2 158 ? -3.631  49.652  1.941   1.00 52.54  ?  158 VAL D CG2 1 
ATOM 6084 N N   . SER D 2 159 ? 0.139   52.340  2.033   1.00 58.91  ?  159 SER D N   1 
ATOM 6085 C CA  . SER D 2 159 ? 1.176   53.093  2.711   1.00 57.29  ?  159 SER D CA  1 
ATOM 6086 C C   . SER D 2 159 ? 0.663   54.509  2.903   1.00 59.80  ?  159 SER D C   1 
ATOM 6087 O O   . SER D 2 159 ? -0.268  54.946  2.223   1.00 59.83  ?  159 SER D O   1 
ATOM 6088 C CB  . SER D 2 159 ? 2.494   53.082  1.930   1.00 52.74  ?  159 SER D CB  1 
ATOM 6089 O OG  . SER D 2 159 ? 2.454   53.996  0.850   1.00 58.35  ?  159 SER D OG  1 
ATOM 6090 N N   . TRP D 2 160 ? 1.291   55.227  3.827   1.00 58.22  ?  160 TRP D N   1 
ATOM 6091 C CA  . TRP D 2 160 ? 0.889   56.580  4.178   1.00 56.66  ?  160 TRP D CA  1 
ATOM 6092 C C   . TRP D 2 160 ? 2.033   57.535  3.882   1.00 60.68  ?  160 TRP D C   1 
ATOM 6093 O O   . TRP D 2 160 ? 3.166   57.304  4.317   1.00 64.64  ?  160 TRP D O   1 
ATOM 6094 C CB  . TRP D 2 160 ? 0.483   56.665  5.650   1.00 61.08  ?  160 TRP D CB  1 
ATOM 6095 C CG  . TRP D 2 160 ? -0.846  56.042  5.935   1.00 57.65  ?  160 TRP D CG  1 
ATOM 6096 C CD1 . TRP D 2 160 ? -1.095  54.738  6.257   1.00 51.41  ?  160 TRP D CD1 1 
ATOM 6097 C CD2 . TRP D 2 160 ? -2.114  56.704  5.926   1.00 51.18  ?  160 TRP D CD2 1 
ATOM 6098 N NE1 . TRP D 2 160 ? -2.442  54.551  6.450   1.00 50.10  ?  160 TRP D NE1 1 
ATOM 6099 C CE2 . TRP D 2 160 ? -3.089  55.743  6.249   1.00 50.47  ?  160 TRP D CE2 1 
ATOM 6100 C CE3 . TRP D 2 160 ? -2.519  58.019  5.679   1.00 51.10  ?  160 TRP D CE3 1 
ATOM 6101 C CZ2 . TRP D 2 160 ? -4.444  56.055  6.327   1.00 52.42  ?  160 TRP D CZ2 1 
ATOM 6102 C CZ3 . TRP D 2 160 ? -3.862  58.327  5.758   1.00 48.57  ?  160 TRP D CZ3 1 
ATOM 6103 C CH2 . TRP D 2 160 ? -4.809  57.350  6.075   1.00 50.58  ?  160 TRP D CH2 1 
ATOM 6104 N N   . ASN D 2 161 ? 1.731   58.599  3.139   1.00 66.99  ?  161 ASN D N   1 
ATOM 6105 C CA  . ASN D 2 161 ? 2.719   59.597  2.727   1.00 65.44  ?  161 ASN D CA  1 
ATOM 6106 C C   . ASN D 2 161 ? 3.931   58.952  2.052   1.00 62.05  ?  161 ASN D C   1 
ATOM 6107 O O   . ASN D 2 161 ? 5.083   59.241  2.378   1.00 66.77  ?  161 ASN D O   1 
ATOM 6108 C CB  . ASN D 2 161 ? 3.135   60.462  3.917   1.00 56.17  ?  161 ASN D CB  1 
ATOM 6109 C CG  . ASN D 2 161 ? 2.000   61.325  4.422   1.00 58.03  ?  161 ASN D CG  1 
ATOM 6110 O OD1 . ASN D 2 161 ? 0.905   61.324  3.854   1.00 54.13  ?  161 ASN D OD1 1 
ATOM 6111 N ND2 . ASN D 2 161 ? 2.244   62.050  5.509   1.00 62.73  ?  161 ASN D ND2 1 
ATOM 6112 N N   . SER D 2 162 ? 3.654   58.056  1.102   1.00 59.60  ?  162 SER D N   1 
ATOM 6113 C CA  . SER D 2 162 ? 4.677   57.434  0.255   1.00 64.12  ?  162 SER D CA  1 
ATOM 6114 C C   . SER D 2 162 ? 5.753   56.720  1.066   1.00 67.57  ?  162 SER D C   1 
ATOM 6115 O O   . SER D 2 162 ? 6.891   56.578  0.610   1.00 69.10  ?  162 SER D O   1 
ATOM 6116 C CB  . SER D 2 162 ? 5.319   58.457  -0.687  1.00 67.06  ?  162 SER D CB  1 
ATOM 6117 O OG  . SER D 2 162 ? 4.413   58.861  -1.701  1.00 74.30  ?  162 SER D OG  1 
ATOM 6118 N N   . GLY D 2 163 ? 5.402   56.253  2.263   1.00 65.84  ?  163 GLY D N   1 
ATOM 6119 C CA  . GLY D 2 163 ? 6.336   55.581  3.140   1.00 62.44  ?  163 GLY D CA  1 
ATOM 6120 C C   . GLY D 2 163 ? 6.963   56.460  4.202   1.00 72.63  ?  163 GLY D C   1 
ATOM 6121 O O   . GLY D 2 163 ? 7.765   55.960  5.001   1.00 84.08  ?  163 GLY D O   1 
ATOM 6122 N N   . ALA D 2 164 ? 6.607   57.747  4.254   1.00 65.23  ?  164 ALA D N   1 
ATOM 6123 C CA  . ALA D 2 164 ? 7.186   58.645  5.246   1.00 68.40  ?  164 ALA D CA  1 
ATOM 6124 C C   . ALA D 2 164 ? 6.523   58.498  6.608   1.00 68.71  ?  164 ALA D C   1 
ATOM 6125 O O   . ALA D 2 164 ? 7.144   58.810  7.631   1.00 72.11  ?  164 ALA D O   1 
ATOM 6126 C CB  . ALA D 2 164 ? 7.077   60.094  4.772   1.00 66.95  ?  164 ALA D CB  1 
ATOM 6127 N N   . LEU D 2 165 ? 5.273   58.044  6.641   1.00 64.13  ?  165 LEU D N   1 
ATOM 6128 C CA  . LEU D 2 165 ? 4.526   57.840  7.875   1.00 60.39  ?  165 LEU D CA  1 
ATOM 6129 C C   . LEU D 2 165 ? 4.432   56.340  8.116   1.00 69.46  ?  165 LEU D C   1 
ATOM 6130 O O   . LEU D 2 165 ? 3.796   55.621  7.338   1.00 66.57  ?  165 LEU D O   1 
ATOM 6131 C CB  . LEU D 2 165 ? 3.145   58.480  7.786   1.00 52.29  ?  165 LEU D CB  1 
ATOM 6132 C CG  . LEU D 2 165 ? 2.319   58.519  9.065   1.00 59.25  ?  165 LEU D CG  1 
ATOM 6133 C CD1 . LEU D 2 165 ? 3.149   59.050  10.223  1.00 64.37  ?  165 LEU D CD1 1 
ATOM 6134 C CD2 . LEU D 2 165 ? 1.084   59.378  8.852   1.00 62.02  ?  165 LEU D CD2 1 
ATOM 6135 N N   . THR D 2 166 ? 5.081   55.870  9.181   1.00 71.35  ?  166 THR D N   1 
ATOM 6136 C CA  . THR D 2 166 ? 5.112   54.446  9.493   1.00 69.71  ?  166 THR D CA  1 
ATOM 6137 C C   . THR D 2 166 ? 4.697   54.182  10.936  1.00 72.99  ?  166 THR D C   1 
ATOM 6138 O O   . THR D 2 166 ? 4.213   53.091  11.256  1.00 68.17  ?  166 THR D O   1 
ATOM 6139 C CB  . THR D 2 166 ? 6.507   53.872  9.239   1.00 73.86  ?  166 THR D CB  1 
ATOM 6140 O OG1 . THR D 2 166 ? 7.463   54.574  10.042  1.00 82.69  ?  166 THR D OG1 1 
ATOM 6141 C CG2 . THR D 2 166 ? 6.885   54.021  7.772   1.00 65.48  ?  166 THR D CG2 1 
ATOM 6142 N N   . SER D 2 167 ? 4.883   55.166  11.811  1.00 70.21  ?  167 SER D N   1 
ATOM 6143 C CA  . SER D 2 167 ? 4.596   54.982  13.226  1.00 72.75  ?  167 SER D CA  1 
ATOM 6144 C C   . SER D 2 167 ? 3.103   55.120  13.496  1.00 67.32  ?  167 SER D C   1 
ATOM 6145 O O   . SER D 2 167 ? 2.449   56.045  13.007  1.00 70.78  ?  167 SER D O   1 
ATOM 6146 C CB  . SER D 2 167 ? 5.374   56.003  14.059  1.00 73.42  ?  167 SER D CB  1 
ATOM 6147 O OG  . SER D 2 167 ? 5.092   55.872  15.441  1.00 75.44  ?  167 SER D OG  1 
ATOM 6148 N N   . GLY D 2 168 ? 2.568   54.193  14.289  1.00 67.45  ?  168 GLY D N   1 
ATOM 6149 C CA  . GLY D 2 168 ? 1.151   54.198  14.588  1.00 61.53  ?  168 GLY D CA  1 
ATOM 6150 C C   . GLY D 2 168 ? 0.261   53.796  13.437  1.00 60.40  ?  168 GLY D C   1 
ATOM 6151 O O   . GLY D 2 168 ? -0.925  54.135  13.440  1.00 62.57  ?  168 GLY D O   1 
ATOM 6152 N N   . VAL D 2 169 ? 0.797   53.086  12.445  1.00 56.56  ?  169 VAL D N   1 
ATOM 6153 C CA  . VAL D 2 169 ? 0.047   52.689  11.257  1.00 52.94  ?  169 VAL D CA  1 
ATOM 6154 C C   . VAL D 2 169 ? -0.361  51.232  11.386  1.00 48.85  ?  169 VAL D C   1 
ATOM 6155 O O   . VAL D 2 169 ? 0.489   50.358  11.591  1.00 50.89  ?  169 VAL D O   1 
ATOM 6156 C CB  . VAL D 2 169 ? 0.876   52.905  9.981   1.00 56.42  ?  169 VAL D CB  1 
ATOM 6157 C CG1 . VAL D 2 169 ? 0.082   52.484  8.753   1.00 54.50  ?  169 VAL D CG1 1 
ATOM 6158 C CG2 . VAL D 2 169 ? 1.311   54.357  9.873   1.00 60.47  ?  169 VAL D CG2 1 
ATOM 6159 N N   . HIS D 2 170 ? -1.653  50.964  11.216  1.00 49.46  ?  170 HIS D N   1 
ATOM 6160 C CA  . HIS D 2 170 ? -2.187  49.607  11.264  1.00 49.85  ?  170 HIS D CA  1 
ATOM 6161 C C   . HIS D 2 170 ? -3.027  49.379  10.014  1.00 49.29  ?  170 HIS D C   1 
ATOM 6162 O O   . HIS D 2 170 ? -4.056  50.037  9.820   1.00 49.39  ?  170 HIS D O   1 
ATOM 6163 C CB  . HIS D 2 170 ? -2.996  49.384  12.539  1.00 47.91  ?  170 HIS D CB  1 
ATOM 6164 C CG  . HIS D 2 170 ? -2.165  49.440  13.784  1.00 53.24  ?  170 HIS D CG  1 
ATOM 6165 N ND1 . HIS D 2 170 ? -2.581  50.081  14.933  1.00 53.13  ?  170 HIS D ND1 1 
ATOM 6166 C CD2 . HIS D 2 170 ? -0.930  48.953  14.051  1.00 53.84  ?  170 HIS D CD2 1 
ATOM 6167 C CE1 . HIS D 2 170 ? -1.641  49.979  15.856  1.00 55.85  ?  170 HIS D CE1 1 
ATOM 6168 N NE2 . HIS D 2 170 ? -0.627  49.301  15.346  1.00 57.18  ?  170 HIS D NE2 1 
ATOM 6169 N N   . THR D 2 171 ? -2.554  48.490  9.143   1.00 44.54  ?  171 THR D N   1 
ATOM 6170 C CA  . THR D 2 171 ? -3.287  48.073  7.952   1.00 42.24  ?  171 THR D CA  1 
ATOM 6171 C C   . THR D 2 171 ? -3.931  46.723  8.243   1.00 43.26  ?  171 THR D C   1 
ATOM 6172 O O   . THR D 2 171 ? -3.237  45.705  8.342   1.00 47.67  ?  171 THR D O   1 
ATOM 6173 C CB  . THR D 2 171 ? -2.359  47.987  6.745   1.00 42.80  ?  171 THR D CB  1 
ATOM 6174 O OG1 . THR D 2 171 ? -1.732  49.259  6.531   1.00 44.67  ?  171 THR D OG1 1 
ATOM 6175 C CG2 . THR D 2 171 ? -3.141  47.597  5.504   1.00 44.03  ?  171 THR D CG2 1 
ATOM 6176 N N   . PHE D 2 172 ? -5.250  46.712  8.381   1.00 40.14  ?  172 PHE D N   1 
ATOM 6177 C CA  . PHE D 2 172 ? -5.930  45.490  8.770   1.00 42.70  ?  172 PHE D CA  1 
ATOM 6178 C C   . PHE D 2 172 ? -5.920  44.475  7.629   1.00 45.86  ?  172 PHE D C   1 
ATOM 6179 O O   . PHE D 2 172 ? -5.876  44.844  6.454   1.00 44.96  ?  172 PHE D O   1 
ATOM 6180 C CB  . PHE D 2 172 ? -7.364  45.791  9.183   1.00 43.09  ?  172 PHE D CB  1 
ATOM 6181 C CG  . PHE D 2 172 ? -7.460  46.579  10.440  1.00 47.70  ?  172 PHE D CG  1 
ATOM 6182 C CD1 . PHE D 2 172 ? -7.537  47.954  10.408  1.00 48.43  ?  172 PHE D CD1 1 
ATOM 6183 C CD2 . PHE D 2 172 ? -7.446  45.940  11.667  1.00 51.42  ?  172 PHE D CD2 1 
ATOM 6184 C CE1 . PHE D 2 172 ? -7.616  48.682  11.583  1.00 50.22  ?  172 PHE D CE1 1 
ATOM 6185 C CE2 . PHE D 2 172 ? -7.524  46.661  12.843  1.00 51.11  ?  172 PHE D CE2 1 
ATOM 6186 C CZ  . PHE D 2 172 ? -7.608  48.034  12.800  1.00 47.32  ?  172 PHE D CZ  1 
ATOM 6187 N N   . PRO D 2 173 ? -5.933  43.184  7.953   1.00 54.02  ?  173 PRO D N   1 
ATOM 6188 C CA  . PRO D 2 173 ? -6.048  42.172  6.901   1.00 45.62  ?  173 PRO D CA  1 
ATOM 6189 C C   . PRO D 2 173 ? -7.365  42.319  6.161   1.00 43.80  ?  173 PRO D C   1 
ATOM 6190 O O   . PRO D 2 173 ? -8.336  42.892  6.666   1.00 36.12  ?  173 PRO D O   1 
ATOM 6191 C CB  . PRO D 2 173 ? -5.982  40.842  7.667   1.00 36.45  ?  173 PRO D CB  1 
ATOM 6192 C CG  . PRO D 2 173 ? -5.257  41.175  8.924   1.00 47.16  ?  173 PRO D CG  1 
ATOM 6193 C CD  . PRO D 2 173 ? -5.684  42.579  9.275   1.00 48.53  ?  173 PRO D CD  1 
ATOM 6194 N N   . ALA D 2 174 ? -7.382  41.783  4.943   1.00 45.37  ?  174 ALA D N   1 
ATOM 6195 C CA  . ALA D 2 174 ? -8.552  41.865  4.087   1.00 44.62  ?  174 ALA D CA  1 
ATOM 6196 C C   . ALA D 2 174 ? -9.597  40.841  4.512   1.00 44.49  ?  174 ALA D C   1 
ATOM 6197 O O   . ALA D 2 174 ? -9.275  39.752  4.991   1.00 46.74  ?  174 ALA D O   1 
ATOM 6198 C CB  . ALA D 2 174 ? -8.161  41.638  2.630   1.00 52.65  ?  174 ALA D CB  1 
ATOM 6199 N N   . VAL D 2 175 ? -10.861 41.210  4.342   1.00 45.70  ?  175 VAL D N   1 
ATOM 6200 C CA  . VAL D 2 175 ? -11.990 40.359  4.690   1.00 47.65  ?  175 VAL D CA  1 
ATOM 6201 C C   . VAL D 2 175 ? -12.846 40.159  3.449   1.00 51.53  ?  175 VAL D C   1 
ATOM 6202 O O   . VAL D 2 175 ? -13.170 41.127  2.751   1.00 58.05  ?  175 VAL D O   1 
ATOM 6203 C CB  . VAL D 2 175 ? -12.810 40.960  5.846   1.00 53.19  ?  175 VAL D CB  1 
ATOM 6204 C CG1 . VAL D 2 175 ? -14.068 40.148  6.080   1.00 56.47  ?  175 VAL D CG1 1 
ATOM 6205 C CG2 . VAL D 2 175 ? -11.966 40.988  7.111   1.00 48.78  ?  175 VAL D CG2 1 
ATOM 6206 N N   . LEU D 2 176 ? -13.204 38.909  3.170   1.00 51.02  ?  176 LEU D N   1 
ATOM 6207 C CA  . LEU D 2 176 ? -14.044 38.606  2.019   1.00 50.73  ?  176 LEU D CA  1 
ATOM 6208 C C   . LEU D 2 176 ? -15.487 38.972  2.351   1.00 48.27  ?  176 LEU D C   1 
ATOM 6209 O O   . LEU D 2 176 ? -16.083 38.399  3.270   1.00 45.62  ?  176 LEU D O   1 
ATOM 6210 C CB  . LEU D 2 176 ? -13.919 37.130  1.639   1.00 40.14  ?  176 LEU D CB  1 
ATOM 6211 C CG  . LEU D 2 176 ? -14.504 36.699  0.291   1.00 45.40  ?  176 LEU D CG  1 
ATOM 6212 C CD1 . LEU D 2 176 ? -13.941 37.548  -0.849  1.00 47.48  ?  176 LEU D CD1 1 
ATOM 6213 C CD2 . LEU D 2 176 ? -14.242 35.225  0.038   1.00 37.58  ?  176 LEU D CD2 1 
ATOM 6214 N N   . GLN D 2 177 ? -16.035 39.950  1.633   1.00 50.26  ?  177 GLN D N   1 
ATOM 6215 C CA  . GLN D 2 177 ? -17.413 40.344  1.874   1.00 54.48  ?  177 GLN D CA  1 
ATOM 6216 C C   . GLN D 2 177 ? -18.369 39.371  1.192   1.00 53.46  ?  177 GLN D C   1 
ATOM 6217 O O   . GLN D 2 177 ? -17.994 38.605  0.300   1.00 54.38  ?  177 GLN D O   1 
ATOM 6218 C CB  . GLN D 2 177 ? -17.671 41.763  1.368   1.00 57.12  ?  177 GLN D CB  1 
ATOM 6219 C CG  . GLN D 2 177 ? -16.797 42.834  1.988   1.00 50.78  ?  177 GLN D CG  1 
ATOM 6220 C CD  . GLN D 2 177 ? -17.063 44.201  1.375   1.00 57.00  ?  177 GLN D CD  1 
ATOM 6221 O OE1 . GLN D 2 177 ? -17.344 45.173  2.081   1.00 64.50  ?  177 GLN D OE1 1 
ATOM 6222 N NE2 . GLN D 2 177 ? -16.961 44.282  0.053   1.00 49.98  ?  177 GLN D NE2 1 
ATOM 6223 N N   . SER D 2 178 ? -19.643 39.457  1.585   1.00 52.85  ?  178 SER D N   1 
ATOM 6224 C CA  . SER D 2 178 ? -20.655 38.575  1.015   1.00 48.49  ?  178 SER D CA  1 
ATOM 6225 C C   . SER D 2 178 ? -20.721 38.690  -0.503  1.00 46.91  ?  178 SER D C   1 
ATOM 6226 O O   . SER D 2 178 ? -21.116 37.733  -1.173  1.00 54.22  ?  178 SER D O   1 
ATOM 6227 C CB  . SER D 2 178 ? -22.018 38.879  1.636   1.00 44.53  ?  178 SER D CB  1 
ATOM 6228 O OG  . SER D 2 178 ? -22.346 40.252  1.504   1.00 59.19  ?  178 SER D OG  1 
ATOM 6229 N N   . SER D 2 179 ? -20.339 39.839  -1.061  1.00 48.09  ?  179 SER D N   1 
ATOM 6230 C CA  . SER D 2 179 ? -20.425 40.073  -2.500  1.00 48.58  ?  179 SER D CA  1 
ATOM 6231 C C   . SER D 2 179 ? -19.289 39.433  -3.286  1.00 47.78  ?  179 SER D C   1 
ATOM 6232 O O   . SER D 2 179 ? -19.231 39.617  -4.505  1.00 43.38  ?  179 SER D O   1 
ATOM 6233 C CB  . SER D 2 179 ? -20.433 41.573  -2.801  1.00 47.72  ?  179 SER D CB  1 
ATOM 6234 O OG  . SER D 2 179 ? -19.220 42.172  -2.375  1.00 47.43  ?  179 SER D OG  1 
ATOM 6235 N N   . GLY D 2 180 ? -18.377 38.714  -2.635  1.00 50.95  ?  180 GLY D N   1 
ATOM 6236 C CA  . GLY D 2 180 ? -17.216 38.192  -3.324  1.00 49.34  ?  180 GLY D CA  1 
ATOM 6237 C C   . GLY D 2 180 ? -16.108 39.198  -3.543  1.00 50.02  ?  180 GLY D C   1 
ATOM 6238 O O   . GLY D 2 180 ? -15.097 38.857  -4.176  1.00 48.56  ?  180 GLY D O   1 
ATOM 6239 N N   . LEU D 2 181 ? -16.275 40.428  -3.067  1.00 47.09  ?  181 LEU D N   1 
ATOM 6240 C CA  . LEU D 2 181 ? -15.261 41.465  -3.145  1.00 46.33  ?  181 LEU D CA  1 
ATOM 6241 C C   . LEU D 2 181 ? -14.618 41.653  -1.776  1.00 49.70  ?  181 LEU D C   1 
ATOM 6242 O O   . LEU D 2 181 ? -15.221 41.356  -0.741  1.00 52.24  ?  181 LEU D O   1 
ATOM 6243 C CB  . LEU D 2 181 ? -15.878 42.778  -3.632  1.00 51.55  ?  181 LEU D CB  1 
ATOM 6244 C CG  . LEU D 2 181 ? -16.545 42.724  -5.014  1.00 44.54  ?  181 LEU D CG  1 
ATOM 6245 C CD1 . LEU D 2 181 ? -17.185 44.051  -5.366  1.00 39.49  ?  181 LEU D CD1 1 
ATOM 6246 C CD2 . LEU D 2 181 ? -15.545 42.316  -6.079  1.00 39.60  ?  181 LEU D CD2 1 
ATOM 6247 N N   . TYR D 2 182 ? -13.385 42.150  -1.776  1.00 49.08  ?  182 TYR D N   1 
ATOM 6248 C CA  . TYR D 2 182 ? -12.636 42.341  -0.544  1.00 45.96  ?  182 TYR D CA  1 
ATOM 6249 C C   . TYR D 2 182 ? -12.843 43.750  -0.002  1.00 47.70  ?  182 TYR D C   1 
ATOM 6250 O O   . TYR D 2 182 ? -13.432 44.614  -0.653  1.00 53.18  ?  182 TYR D O   1 
ATOM 6251 C CB  . TYR D 2 182 ? -11.153 42.059  -0.772  1.00 48.88  ?  182 TYR D CB  1 
ATOM 6252 C CG  . TYR D 2 182 ? -10.863 40.592  -0.963  1.00 55.16  ?  182 TYR D CG  1 
ATOM 6253 C CD1 . TYR D 2 182 ? -10.917 40.015  -2.225  1.00 48.63  ?  182 TYR D CD1 1 
ATOM 6254 C CD2 . TYR D 2 182 ? -10.553 39.777  0.121   1.00 49.82  ?  182 TYR D CD2 1 
ATOM 6255 C CE1 . TYR D 2 182 ? -10.666 38.670  -2.401  1.00 52.21  ?  182 TYR D CE1 1 
ATOM 6256 C CE2 . TYR D 2 182 ? -10.297 38.430  -0.048  1.00 47.09  ?  182 TYR D CE2 1 
ATOM 6257 C CZ  . TYR D 2 182 ? -10.356 37.883  -1.311  1.00 52.19  ?  182 TYR D CZ  1 
ATOM 6258 O OH  . TYR D 2 182 ? -10.102 36.542  -1.497  1.00 56.09  ?  182 TYR D OH  1 
ATOM 6259 N N   . SER D 2 183 ? -12.385 43.962  1.230   1.00 49.77  ?  183 SER D N   1 
ATOM 6260 C CA  . SER D 2 183 ? -12.503 45.254  1.892   1.00 46.69  ?  183 SER D CA  1 
ATOM 6261 C C   . SER D 2 183 ? -11.608 45.254  3.122   1.00 44.83  ?  183 SER D C   1 
ATOM 6262 O O   . SER D 2 183 ? -11.515 44.237  3.815   1.00 44.46  ?  183 SER D O   1 
ATOM 6263 C CB  . SER D 2 183 ? -13.962 45.531  2.282   1.00 44.98  ?  183 SER D CB  1 
ATOM 6264 O OG  . SER D 2 183 ? -14.073 46.655  3.122   1.00 50.70  ?  183 SER D OG  1 
ATOM 6265 N N   . LEU D 2 184 ? -10.935 46.379  3.373   1.00 44.94  ?  184 LEU D N   1 
ATOM 6266 C CA  . LEU D 2 184 ? -10.115 46.534  4.571   1.00 46.23  ?  184 LEU D CA  1 
ATOM 6267 C C   . LEU D 2 184 ? -9.996  48.013  4.917   1.00 45.73  ?  184 LEU D C   1 
ATOM 6268 O O   . LEU D 2 184 ? -10.522 48.885  4.217   1.00 47.71  ?  184 LEU D O   1 
ATOM 6269 C CB  . LEU D 2 184 ? -8.727  45.906  4.399   1.00 41.69  ?  184 LEU D CB  1 
ATOM 6270 C CG  . LEU D 2 184 ? -7.770  46.460  3.344   1.00 45.71  ?  184 LEU D CG  1 
ATOM 6271 C CD1 . LEU D 2 184 ? -6.891  47.570  3.885   1.00 45.85  ?  184 LEU D CD1 1 
ATOM 6272 C CD2 . LEU D 2 184 ? -6.912  45.329  2.830   1.00 49.24  ?  184 LEU D CD2 1 
ATOM 6273 N N   . SER D 2 185 ? -9.260  48.288  5.992   1.00 42.30  ?  185 SER D N   1 
ATOM 6274 C CA  . SER D 2 185 ? -8.976  49.647  6.427   1.00 40.76  ?  185 SER D CA  1 
ATOM 6275 C C   . SER D 2 185 ? -7.506  49.765  6.795   1.00 41.61  ?  185 SER D C   1 
ATOM 6276 O O   . SER D 2 185 ? -6.838  48.780  7.116   1.00 45.27  ?  185 SER D O   1 
ATOM 6277 C CB  . SER D 2 185 ? -9.832  50.064  7.631   1.00 37.42  ?  185 SER D CB  1 
ATOM 6278 O OG  . SER D 2 185 ? -11.176 50.287  7.252   1.00 47.62  ?  185 SER D OG  1 
ATOM 6279 N N   . SER D 2 186 ? -7.009  50.996  6.737   1.00 47.33  ?  186 SER D N   1 
ATOM 6280 C CA  . SER D 2 186 ? -5.658  51.322  7.174   1.00 52.96  ?  186 SER D CA  1 
ATOM 6281 C C   . SER D 2 186 ? -5.741  52.584  8.018   1.00 48.17  ?  186 SER D C   1 
ATOM 6282 O O   . SER D 2 186 ? -6.111  53.644  7.507   1.00 47.12  ?  186 SER D O   1 
ATOM 6283 C CB  . SER D 2 186 ? -4.729  51.519  5.973   1.00 46.05  ?  186 SER D CB  1 
ATOM 6284 O OG  . SER D 2 186 ? -3.378  51.611  6.383   1.00 56.12  ?  186 SER D OG  1 
ATOM 6285 N N   . VAL D 2 187 ? -5.412  52.475  9.303   1.00 48.75  ?  187 VAL D N   1 
ATOM 6286 C CA  . VAL D 2 187 ? -5.595  53.586  10.233  1.00 52.33  ?  187 VAL D CA  1 
ATOM 6287 C C   . VAL D 2 187 ? -4.254  54.029  10.803  1.00 46.92  ?  187 VAL D C   1 
ATOM 6288 O O   . VAL D 2 187 ? -3.313  53.240  10.935  1.00 48.00  ?  187 VAL D O   1 
ATOM 6289 C CB  . VAL D 2 187 ? -6.572  53.224  11.371  1.00 48.30  ?  187 VAL D CB  1 
ATOM 6290 C CG1 . VAL D 2 187 ? -7.974  53.041  10.818  1.00 43.88  ?  187 VAL D CG1 1 
ATOM 6291 C CG2 . VAL D 2 187 ? -6.105  51.966  12.085  1.00 46.93  ?  187 VAL D CG2 1 
ATOM 6292 N N   . VAL D 2 188 ? -4.179  55.311  11.149  1.00 51.86  ?  188 VAL D N   1 
ATOM 6293 C CA  . VAL D 2 188 ? -2.984  55.899  11.745  1.00 56.16  ?  188 VAL D CA  1 
ATOM 6294 C C   . VAL D 2 188 ? -3.404  56.819  12.879  1.00 51.95  ?  188 VAL D C   1 
ATOM 6295 O O   . VAL D 2 188 ? -4.436  57.496  12.802  1.00 47.03  ?  188 VAL D O   1 
ATOM 6296 C CB  . VAL D 2 188 ? -2.136  56.687  10.720  1.00 58.77  ?  188 VAL D CB  1 
ATOM 6297 C CG1 . VAL D 2 188 ? -0.792  57.077  11.329  1.00 55.85  ?  188 VAL D CG1 1 
ATOM 6298 C CG2 . VAL D 2 188 ? -1.927  55.889  9.454   1.00 59.03  ?  188 VAL D CG2 1 
ATOM 6299 N N   . THR D 2 189 ? -2.604  56.826  13.940  1.00 57.59  ?  189 THR D N   1 
ATOM 6300 C CA  . THR D 2 189 ? -2.754  57.760  15.045  1.00 55.10  ?  189 THR D CA  1 
ATOM 6301 C C   . THR D 2 189 ? -1.706  58.851  14.888  1.00 55.98  ?  189 THR D C   1 
ATOM 6302 O O   . THR D 2 189 ? -0.535  58.561  14.617  1.00 54.51  ?  189 THR D O   1 
ATOM 6303 C CB  . THR D 2 189 ? -2.603  57.054  16.392  1.00 53.59  ?  189 THR D CB  1 
ATOM 6304 O OG1 . THR D 2 189 ? -1.485  56.157  16.344  1.00 58.08  ?  189 THR D OG1 1 
ATOM 6305 C CG2 . THR D 2 189 ? -3.866  56.281  16.733  1.00 51.15  ?  189 THR D CG2 1 
ATOM 6306 N N   . VAL D 2 190 ? -2.135  60.101  15.033  1.00 62.64  ?  190 VAL D N   1 
ATOM 6307 C CA  . VAL D 2 190 ? -1.267  61.258  14.824  1.00 64.82  ?  190 VAL D CA  1 
ATOM 6308 C C   . VAL D 2 190 ? -1.500  62.261  15.938  1.00 69.15  ?  190 VAL D C   1 
ATOM 6309 O O   . VAL D 2 190 ? -2.528  62.217  16.634  1.00 66.24  ?  190 VAL D O   1 
ATOM 6310 C CB  . VAL D 2 190 ? -1.516  61.922  13.454  1.00 66.20  ?  190 VAL D CB  1 
ATOM 6311 C CG1 . VAL D 2 190 ? -1.131  60.981  12.322  1.00 61.99  ?  190 VAL D CG1 1 
ATOM 6312 C CG2 . VAL D 2 190 ? -2.972  62.347  13.330  1.00 64.10  ?  190 VAL D CG2 1 
ATOM 6313 N N   . PRO D 2 191 ? -0.545  63.167  16.156  1.00 74.42  ?  191 PRO D N   1 
ATOM 6314 C CA  . PRO D 2 191 ? -0.769  64.262  17.107  1.00 72.20  ?  191 PRO D CA  1 
ATOM 6315 C C   . PRO D 2 191 ? -1.963  65.111  16.693  1.00 75.44  ?  191 PRO D C   1 
ATOM 6316 O O   . PRO D 2 191 ? -2.175  65.380  15.508  1.00 71.62  ?  191 PRO D O   1 
ATOM 6317 C CB  . PRO D 2 191 ? 0.537   65.061  17.041  1.00 71.95  ?  191 PRO D CB  1 
ATOM 6318 C CG  . PRO D 2 191 ? 1.554   64.088  16.580  1.00 65.44  ?  191 PRO D CG  1 
ATOM 6319 C CD  . PRO D 2 191 ? 0.838   63.164  15.640  1.00 69.67  ?  191 PRO D CD  1 
ATOM 6320 N N   . SER D 2 192 ? -2.748  65.534  17.688  1.00 73.08  ?  192 SER D N   1 
ATOM 6321 C CA  . SER D 2 192 ? -3.946  66.316  17.399  1.00 72.56  ?  192 SER D CA  1 
ATOM 6322 C C   . SER D 2 192 ? -3.603  67.661  16.759  1.00 81.19  ?  192 SER D C   1 
ATOM 6323 O O   . SER D 2 192 ? -4.373  68.168  15.933  1.00 79.84  ?  192 SER D O   1 
ATOM 6324 C CB  . SER D 2 192 ? -4.760  66.508  18.682  1.00 71.95  ?  192 SER D CB  1 
ATOM 6325 O OG  . SER D 2 192 ? -5.978  67.180  18.424  1.00 83.40  ?  192 SER D OG  1 
ATOM 6326 N N   . SER D 2 193 ? -2.457  68.251  17.115  1.00 81.11  ?  193 SER D N   1 
ATOM 6327 C CA  . SER D 2 193 ? -2.040  69.521  16.525  1.00 79.77  ?  193 SER D CA  1 
ATOM 6328 C C   . SER D 2 193 ? -1.518  69.377  15.098  1.00 78.38  ?  193 SER D C   1 
ATOM 6329 O O   . SER D 2 193 ? -1.260  70.397  14.447  1.00 74.54  ?  193 SER D O   1 
ATOM 6330 C CB  . SER D 2 193 ? -0.974  70.188  17.399  1.00 72.54  ?  193 SER D CB  1 
ATOM 6331 O OG  . SER D 2 193 ? 0.175   69.371  17.532  1.00 70.10  ?  193 SER D OG  1 
ATOM 6332 N N   . SER D 2 194 ? -1.351  68.150  14.597  1.00 79.86  ?  194 SER D N   1 
ATOM 6333 C CA  . SER D 2 194 ? -0.891  67.946  13.226  1.00 81.21  ?  194 SER D CA  1 
ATOM 6334 C C   . SER D 2 194 ? -1.971  68.229  12.193  1.00 80.34  ?  194 SER D C   1 
ATOM 6335 O O   . SER D 2 194 ? -1.640  68.516  11.036  1.00 79.72  ?  194 SER D O   1 
ATOM 6336 C CB  . SER D 2 194 ? -0.386  66.515  13.027  1.00 71.90  ?  194 SER D CB  1 
ATOM 6337 O OG  . SER D 2 194 ? 0.761   66.246  13.811  1.00 82.61  ?  194 SER D OG  1 
ATOM 6338 N N   . LEU D 2 195 ? -3.241  68.129  12.572  1.00 77.14  ?  195 LEU D N   1 
ATOM 6339 C CA  . LEU D 2 195 ? -4.328  68.364  11.634  1.00 79.05  ?  195 LEU D CA  1 
ATOM 6340 C C   . LEU D 2 195 ? -4.383  69.834  11.215  1.00 83.49  ?  195 LEU D C   1 
ATOM 6341 O O   . LEU D 2 195 ? -4.181  70.741  12.029  1.00 83.67  ?  195 LEU D O   1 
ATOM 6342 C CB  . LEU D 2 195 ? -5.654  67.935  12.264  1.00 75.86  ?  195 LEU D CB  1 
ATOM 6343 C CG  . LEU D 2 195 ? -5.614  66.574  12.973  1.00 76.26  ?  195 LEU D CG  1 
ATOM 6344 C CD1 . LEU D 2 195 ? -6.971  66.202  13.568  1.00 71.06  ?  195 LEU D CD1 1 
ATOM 6345 C CD2 . LEU D 2 195 ? -5.116  65.475  12.042  1.00 72.23  ?  195 LEU D CD2 1 
ATOM 6346 N N   . GLY D 2 196 ? -4.659  70.064  9.934   1.00 82.19  ?  196 GLY D N   1 
ATOM 6347 C CA  . GLY D 2 196 ? -4.756  71.410  9.398   1.00 90.15  ?  196 GLY D CA  1 
ATOM 6348 C C   . GLY D 2 196 ? -3.506  71.905  8.699   1.00 90.03  ?  196 GLY D C   1 
ATOM 6349 O O   . GLY D 2 196 ? -3.592  72.613  7.690   1.00 86.22  ?  196 GLY D O   1 
ATOM 6350 N N   . THR D 2 197 ? -2.335  71.536  9.219   1.00 87.02  ?  197 THR D N   1 
ATOM 6351 C CA  . THR D 2 197 ? -1.069  71.894  8.593   1.00 90.10  ?  197 THR D CA  1 
ATOM 6352 C C   . THR D 2 197 ? -0.369  70.721  7.923   1.00 87.21  ?  197 THR D C   1 
ATOM 6353 O O   . THR D 2 197 ? 0.260   70.909  6.877   1.00 79.67  ?  197 THR D O   1 
ATOM 6354 C CB  . THR D 2 197 ? -0.118  72.525  9.623   1.00 88.06  ?  197 THR D CB  1 
ATOM 6355 O OG1 . THR D 2 197 ? 0.101   71.610  10.704  1.00 85.53  ?  197 THR D OG1 1 
ATOM 6356 C CG2 . THR D 2 197 ? -0.697  73.825  10.170  1.00 88.84  ?  197 THR D CG2 1 
ATOM 6357 N N   . GLN D 2 198 ? -0.507  69.513  8.463   1.00 84.86  ?  198 GLN D N   1 
ATOM 6358 C CA  . GLN D 2 198 ? 0.124   68.326  7.900   1.00 81.30  ?  198 GLN D CA  1 
ATOM 6359 C C   . GLN D 2 198 ? -0.896  67.542  7.088   1.00 71.40  ?  198 GLN D C   1 
ATOM 6360 O O   . GLN D 2 198 ? -1.998  67.258  7.571   1.00 69.42  ?  198 GLN D O   1 
ATOM 6361 C CB  . GLN D 2 198 ? 0.700   67.438  9.004   1.00 75.83  ?  198 GLN D CB  1 
ATOM 6362 C CG  . GLN D 2 198 ? 1.263   66.114  8.515   1.00 66.28  ?  198 GLN D CG  1 
ATOM 6363 C CD  . GLN D 2 198 ? 2.607   66.272  7.844   1.00 61.92  ?  198 GLN D CD  1 
ATOM 6364 O OE1 . GLN D 2 198 ? 3.601   66.585  8.496   1.00 59.81  ?  198 GLN D OE1 1 
ATOM 6365 N NE2 . GLN D 2 198 ? 2.649   66.047  6.539   1.00 61.50  ?  198 GLN D NE2 1 
ATOM 6366 N N   . THR D 2 199 ? -0.516  67.170  5.872   1.00 68.21  ?  199 THR D N   1 
ATOM 6367 C CA  . THR D 2 199 ? -1.406  66.414  5.007   1.00 73.32  ?  199 THR D CA  1 
ATOM 6368 C C   . THR D 2 199 ? -1.153  64.920  5.173   1.00 70.47  ?  199 THR D C   1 
ATOM 6369 O O   . THR D 2 199 ? -0.021  64.476  5.393   1.00 66.34  ?  199 THR D O   1 
ATOM 6370 C CB  . THR D 2 199 ? -1.226  66.825  3.543   1.00 69.32  ?  199 THR D CB  1 
ATOM 6371 O OG1 . THR D 2 199 ? 0.056   66.394  3.070   1.00 64.85  ?  199 THR D OG1 1 
ATOM 6372 C CG2 . THR D 2 199 ? -1.327  68.341  3.405   1.00 68.06  ?  199 THR D CG2 1 
ATOM 6373 N N   . TYR D 2 200 ? -2.228  64.145  5.069   1.00 68.23  ?  200 TYR D N   1 
ATOM 6374 C CA  . TYR D 2 200 ? -2.175  62.700  5.259   1.00 64.26  ?  200 TYR D CA  1 
ATOM 6375 C C   . TYR D 2 200 ? -2.814  62.028  4.053   1.00 59.16  ?  200 TYR D C   1 
ATOM 6376 O O   . TYR D 2 200 ? -4.025  62.152  3.832   1.00 56.69  ?  200 TYR D O   1 
ATOM 6377 C CB  . TYR D 2 200 ? -2.871  62.289  6.554   1.00 59.49  ?  200 TYR D CB  1 
ATOM 6378 C CG  . TYR D 2 200 ? -2.164  62.774  7.794   1.00 65.55  ?  200 TYR D CG  1 
ATOM 6379 C CD1 . TYR D 2 200 ? -0.987  62.171  8.219   1.00 68.16  ?  200 TYR D CD1 1 
ATOM 6380 C CD2 . TYR D 2 200 ? -2.681  63.821  8.554   1.00 68.24  ?  200 TYR D CD2 1 
ATOM 6381 C CE1 . TYR D 2 200 ? -0.335  62.600  9.358   1.00 72.75  ?  200 TYR D CE1 1 
ATOM 6382 C CE2 . TYR D 2 200 ? -2.037  64.258  9.699   1.00 65.45  ?  200 TYR D CE2 1 
ATOM 6383 C CZ  . TYR D 2 200 ? -0.863  63.643  10.093  1.00 70.41  ?  200 TYR D CZ  1 
ATOM 6384 O OH  . TYR D 2 200 ? -0.206  64.059  11.226  1.00 69.42  ?  200 TYR D OH  1 
ATOM 6385 N N   . ILE D 2 201 ? -1.998  61.324  3.277   1.00 48.85  ?  201 ILE D N   1 
ATOM 6386 C CA  . ILE D 2 201 ? -2.442  60.624  2.082   1.00 59.54  ?  201 ILE D CA  1 
ATOM 6387 C C   . ILE D 2 201 ? -2.108  59.150  2.249   1.00 61.28  ?  201 ILE D C   1 
ATOM 6388 O O   . ILE D 2 201 ? -0.964  58.802  2.565   1.00 60.95  ?  201 ILE D O   1 
ATOM 6389 C CB  . ILE D 2 201 ? -1.778  61.183  0.808   1.00 63.24  ?  201 ILE D CB  1 
ATOM 6390 C CG1 . ILE D 2 201 ? -1.909  62.705  0.743   1.00 58.47  ?  201 ILE D CG1 1 
ATOM 6391 C CG2 . ILE D 2 201 ? -2.398  60.553  -0.435  1.00 58.57  ?  201 ILE D CG2 1 
ATOM 6392 C CD1 . ILE D 2 201 ? -1.124  63.323  -0.391  1.00 53.62  ?  201 ILE D CD1 1 
ATOM 6393 N N   . CYS D 2 202 ? -3.105  58.290  2.061   1.00 59.12  ?  202 CYS D N   1 
ATOM 6394 C CA  . CYS D 2 202 ? -2.870  56.855  1.991   1.00 59.84  ?  202 CYS D CA  1 
ATOM 6395 C C   . CYS D 2 202 ? -2.662  56.458  0.534   1.00 63.04  ?  202 CYS D C   1 
ATOM 6396 O O   . CYS D 2 202 ? -3.282  57.026  -0.370  1.00 60.42  ?  202 CYS D O   1 
ATOM 6397 C CB  . CYS D 2 202 ? -4.029  56.072  2.616   1.00 57.11  ?  202 CYS D CB  1 
ATOM 6398 S SG  . CYS D 2 202 ? -5.594  56.190  1.747   1.00 65.72  ?  202 CYS D SG  1 
ATOM 6399 N N   . ASN D 2 203 ? -1.750  55.511  0.309   1.00 60.31  ?  203 ASN D N   1 
ATOM 6400 C CA  . ASN D 2 203 ? -1.333  55.116  -1.037  1.00 61.10  ?  203 ASN D CA  1 
ATOM 6401 C C   . ASN D 2 203 ? -1.737  53.664  -1.263  1.00 65.59  ?  203 ASN D C   1 
ATOM 6402 O O   . ASN D 2 203 ? -0.999  52.743  -0.897  1.00 67.24  ?  203 ASN D O   1 
ATOM 6403 C CB  . ASN D 2 203 ? 0.169   55.294  -1.205  1.00 63.28  ?  203 ASN D CB  1 
ATOM 6404 C CG  . ASN D 2 203 ? 0.668   56.577  -0.587  1.00 66.49  ?  203 ASN D CG  1 
ATOM 6405 O OD1 . ASN D 2 203 ? 1.547   56.558  0.275   1.00 61.87  ?  203 ASN D OD1 1 
ATOM 6406 N ND2 . ASN D 2 203 ? 0.097   57.702  -1.009  1.00 71.55  ?  203 ASN D ND2 1 
ATOM 6407 N N   . VAL D 2 204 ? -2.885  53.457  -1.894  1.00 56.68  ?  204 VAL D N   1 
ATOM 6408 C CA  . VAL D 2 204 ? -3.394  52.114  -2.142  1.00 54.75  ?  204 VAL D CA  1 
ATOM 6409 C C   . VAL D 2 204 ? -2.895  51.644  -3.499  1.00 51.79  ?  204 VAL D C   1 
ATOM 6410 O O   . VAL D 2 204 ? -3.018  52.361  -4.498  1.00 57.08  ?  204 VAL D O   1 
ATOM 6411 C CB  . VAL D 2 204 ? -4.929  52.088  -2.071  1.00 54.84  ?  204 VAL D CB  1 
ATOM 6412 C CG1 . VAL D 2 204 ? -5.446  50.679  -2.292  1.00 49.21  ?  204 VAL D CG1 1 
ATOM 6413 C CG2 . VAL D 2 204 ? -5.405  52.656  -0.738  1.00 56.30  ?  204 VAL D CG2 1 
ATOM 6414 N N   . ASN D 2 205 ? -2.312  50.448  -3.532  1.00 51.09  ?  205 ASN D N   1 
ATOM 6415 C CA  . ASN D 2 205 ? -1.797  49.840  -4.752  1.00 51.19  ?  205 ASN D CA  1 
ATOM 6416 C C   . ASN D 2 205 ? -2.473  48.491  -4.945  1.00 56.42  ?  205 ASN D C   1 
ATOM 6417 O O   . ASN D 2 205 ? -2.553  47.693  -4.004  1.00 57.56  ?  205 ASN D O   1 
ATOM 6418 C CB  . ASN D 2 205 ? -0.275  49.676  -4.682  1.00 50.30  ?  205 ASN D CB  1 
ATOM 6419 C CG  . ASN D 2 205 ? 0.361   49.482  -6.050  1.00 61.39  ?  205 ASN D CG  1 
ATOM 6420 O OD1 . ASN D 2 205 ? -0.147  48.736  -6.893  1.00 58.42  ?  205 ASN D OD1 1 
ATOM 6421 N ND2 . ASN D 2 205 ? 1.484   50.153  -6.274  1.00 68.47  ?  205 ASN D ND2 1 
ATOM 6422 N N   . HIS D 2 206 ? -2.974  48.241  -6.171  1.00 52.41  ?  206 HIS D N   1 
ATOM 6423 C CA  . HIS D 2 206 ? -3.717  47.020  -6.500  1.00 51.28  ?  206 HIS D CA  1 
ATOM 6424 C C   . HIS D 2 206 ? -3.228  46.525  -7.866  1.00 54.33  ?  206 HIS D C   1 
ATOM 6425 O O   . HIS D 2 206 ? -3.908  46.677  -8.888  1.00 57.43  ?  206 HIS D O   1 
ATOM 6426 C CB  . HIS D 2 206 ? -5.227  47.269  -6.488  1.00 50.80  ?  206 HIS D CB  1 
ATOM 6427 C CG  . HIS D 2 206 ? -6.050  46.038  -6.720  1.00 50.28  ?  206 HIS D CG  1 
ATOM 6428 N ND1 . HIS D 2 206 ? -6.947  45.929  -7.762  1.00 52.42  ?  206 HIS D ND1 1 
ATOM 6429 C CD2 . HIS D 2 206 ? -6.127  44.872  -6.037  1.00 52.31  ?  206 HIS D CD2 1 
ATOM 6430 C CE1 . HIS D 2 206 ? -7.530  44.745  -7.719  1.00 52.08  ?  206 HIS D CE1 1 
ATOM 6431 N NE2 . HIS D 2 206 ? -7.051  44.083  -6.681  1.00 57.02  ?  206 HIS D NE2 1 
ATOM 6432 N N   . LYS D 2 207 ? -2.041  45.918  -7.869  1.00 50.13  ?  207 LYS D N   1 
ATOM 6433 C CA  . LYS D 2 207 ? -1.431  45.445  -9.110  1.00 52.73  ?  207 LYS D CA  1 
ATOM 6434 C C   . LYS D 2 207 ? -2.318  44.520  -9.937  1.00 60.20  ?  207 LYS D C   1 
ATOM 6435 O O   . LYS D 2 207 ? -2.229  44.585  -11.177 1.00 60.18  ?  207 LYS D O   1 
ATOM 6436 C CB  . LYS D 2 207 ? -0.092  44.760  -8.797  1.00 51.27  ?  207 LYS D CB  1 
ATOM 6437 C CG  . LYS D 2 207 ? 1.005   45.741  -8.413  1.00 65.84  ?  207 LYS D CG  1 
ATOM 6438 C CD  . LYS D 2 207 ? 2.352   45.062  -8.237  1.00 77.57  ?  207 LYS D CD  1 
ATOM 6439 C CE  . LYS D 2 207 ? 3.422   46.077  -7.852  1.00 82.56  ?  207 LYS D CE  1 
ATOM 6440 N NZ  . LYS D 2 207 ? 4.762   45.452  -7.667  1.00 95.32  ?  207 LYS D NZ  1 
ATOM 6441 N N   . PRO D 2 208 ? -3.160  43.650  -9.359  1.00 56.16  ?  208 PRO D N   1 
ATOM 6442 C CA  . PRO D 2 208 ? -4.070  42.858  -10.204 1.00 58.38  ?  208 PRO D CA  1 
ATOM 6443 C C   . PRO D 2 208 ? -4.931  43.677  -11.163 1.00 54.10  ?  208 PRO D C   1 
ATOM 6444 O O   . PRO D 2 208 ? -5.315  43.157  -12.219 1.00 58.37  ?  208 PRO D O   1 
ATOM 6445 C CB  . PRO D 2 208 ? -4.921  42.112  -9.171  1.00 51.38  ?  208 PRO D CB  1 
ATOM 6446 C CG  . PRO D 2 208 ? -3.998  41.895  -8.055  1.00 51.65  ?  208 PRO D CG  1 
ATOM 6447 C CD  . PRO D 2 208 ? -3.134  43.125  -7.979  1.00 55.51  ?  208 PRO D CD  1 
ATOM 6448 N N   . SER D 2 209 ? -5.242  44.935  -10.852 1.00 53.87  ?  209 SER D N   1 
ATOM 6449 C CA  . SER D 2 209 ? -6.001  45.771  -11.777 1.00 55.20  ?  209 SER D CA  1 
ATOM 6450 C C   . SER D 2 209 ? -5.194  46.957  -12.286 1.00 58.26  ?  209 SER D C   1 
ATOM 6451 O O   . SER D 2 209 ? -5.761  47.840  -12.944 1.00 55.31  ?  209 SER D O   1 
ATOM 6452 C CB  . SER D 2 209 ? -7.302  46.267  -11.135 1.00 56.32  ?  209 SER D CB  1 
ATOM 6453 O OG  . SER D 2 209 ? -7.062  47.223  -10.118 1.00 56.47  ?  209 SER D OG  1 
ATOM 6454 N N   . ASN D 2 210 ? -3.894  47.006  -11.984 1.00 59.54  ?  210 ASN D N   1 
ATOM 6455 C CA  . ASN D 2 210 ? -3.021  48.104  -12.400 1.00 60.88  ?  210 ASN D CA  1 
ATOM 6456 C C   . ASN D 2 210 ? -3.615  49.454  -12.005 1.00 57.45  ?  210 ASN D C   1 
ATOM 6457 O O   . ASN D 2 210 ? -3.596  50.414  -12.776 1.00 59.09  ?  210 ASN D O   1 
ATOM 6458 C CB  . ASN D 2 210 ? -2.742  48.047  -13.906 1.00 66.99  ?  210 ASN D CB  1 
ATOM 6459 C CG  . ASN D 2 210 ? -2.174  46.704  -14.353 1.00 61.84  ?  210 ASN D CG  1 
ATOM 6460 O OD1 . ASN D 2 210 ? -0.965  46.474  -14.287 1.00 62.53  ?  210 ASN D OD1 1 
ATOM 6461 N ND2 . ASN D 2 210 ? -3.048  45.819  -14.827 1.00 46.44  ?  210 ASN D ND2 1 
ATOM 6462 N N   . THR D 2 211 ? -4.180  49.512  -10.800 1.00 58.46  ?  211 THR D N   1 
ATOM 6463 C CA  . THR D 2 211 ? -4.824  50.705  -10.265 1.00 60.62  ?  211 THR D CA  1 
ATOM 6464 C C   . THR D 2 211 ? -4.061  51.202  -9.045  1.00 59.49  ?  211 THR D C   1 
ATOM 6465 O O   . THR D 2 211 ? -3.574  50.402  -8.239  1.00 57.61  ?  211 THR D O   1 
ATOM 6466 C CB  . THR D 2 211 ? -6.287  50.425  -9.888  1.00 61.52  ?  211 THR D CB  1 
ATOM 6467 O OG1 . THR D 2 211 ? -6.975  49.871  -11.018 1.00 65.57  ?  211 THR D OG1 1 
ATOM 6468 C CG2 . THR D 2 211 ? -6.991  51.703  -9.440  1.00 54.64  ?  211 THR D CG2 1 
ATOM 6469 N N   . LYS D 2 212 ? -3.937  52.523  -8.920  1.00 56.41  ?  212 LYS D N   1 
ATOM 6470 C CA  . LYS D 2 212 ? -3.291  53.138  -7.766  1.00 55.13  ?  212 LYS D CA  1 
ATOM 6471 C C   . LYS D 2 212 ? -4.102  54.356  -7.353  1.00 59.43  ?  212 LYS D C   1 
ATOM 6472 O O   . LYS D 2 212 ? -4.338  55.249  -8.173  1.00 60.73  ?  212 LYS D O   1 
ATOM 6473 C CB  . LYS D 2 212 ? -1.842  53.526  -8.076  1.00 55.52  ?  212 LYS D CB  1 
ATOM 6474 C CG  . LYS D 2 212 ? -1.058  54.024  -6.869  1.00 58.15  ?  212 LYS D CG  1 
ATOM 6475 C CD  . LYS D 2 212 ? 0.417   54.207  -7.200  1.00 59.96  ?  212 LYS D CD  1 
ATOM 6476 C CE  . LYS D 2 212 ? 1.210   54.668  -5.984  1.00 62.80  ?  212 LYS D CE  1 
ATOM 6477 N NZ  . LYS D 2 212 ? 0.791   56.023  -5.516  1.00 63.85  ?  212 LYS D NZ  1 
ATOM 6478 N N   . VAL D 2 213 ? -4.523  54.394  -6.089  1.00 52.93  ?  213 VAL D N   1 
ATOM 6479 C CA  . VAL D 2 213 ? -5.373  55.458  -5.563  1.00 53.01  ?  213 VAL D CA  1 
ATOM 6480 C C   . VAL D 2 213 ? -4.624  56.189  -4.462  1.00 54.63  ?  213 VAL D C   1 
ATOM 6481 O O   . VAL D 2 213 ? -4.060  55.556  -3.563  1.00 64.56  ?  213 VAL D O   1 
ATOM 6482 C CB  . VAL D 2 213 ? -6.708  54.912  -5.030  1.00 51.41  ?  213 VAL D CB  1 
ATOM 6483 C CG1 . VAL D 2 213 ? -7.560  56.049  -4.492  1.00 44.85  ?  213 VAL D CG1 1 
ATOM 6484 C CG2 . VAL D 2 213 ? -7.448  54.158  -6.125  1.00 54.80  ?  213 VAL D CG2 1 
ATOM 6485 N N   . ASP D 2 214 ? -4.619  57.517  -4.532  1.00 58.73  ?  214 ASP D N   1 
ATOM 6486 C CA  . ASP D 2 214 ? -4.057  58.360  -3.483  1.00 58.82  ?  214 ASP D CA  1 
ATOM 6487 C C   . ASP D 2 214 ? -5.175  59.241  -2.942  1.00 56.43  ?  214 ASP D C   1 
ATOM 6488 O O   . ASP D 2 214 ? -5.639  60.156  -3.629  1.00 59.87  ?  214 ASP D O   1 
ATOM 6489 C CB  . ASP D 2 214 ? -2.896  59.206  -4.006  1.00 61.84  ?  214 ASP D CB  1 
ATOM 6490 C CG  . ASP D 2 214 ? -1.820  58.372  -4.673  1.00 68.75  ?  214 ASP D CG  1 
ATOM 6491 O OD1 . ASP D 2 214 ? -1.792  58.344  -5.926  1.00 71.23  ?  214 ASP D OD1 1 
ATOM 6492 O OD2 . ASP D 2 214 ? -0.997  57.764  -3.946  1.00 62.69  -1 214 ASP D OD2 1 
ATOM 6493 N N   . LYS D 2 215 ? -5.610  58.964  -1.719  1.00 53.54  ?  215 LYS D N   1 
ATOM 6494 C CA  . LYS D 2 215 ? -6.685  59.710  -1.081  1.00 57.11  ?  215 LYS D CA  1 
ATOM 6495 C C   . LYS D 2 215 ? -6.106  60.531  0.059   1.00 61.58  ?  215 LYS D C   1 
ATOM 6496 O O   . LYS D 2 215 ? -5.519  59.980  0.998   1.00 64.92  ?  215 LYS D O   1 
ATOM 6497 C CB  . LYS D 2 215 ? -7.782  58.780  -0.561  1.00 53.82  ?  215 LYS D CB  1 
ATOM 6498 C CG  . LYS D 2 215 ? -8.995  59.511  -0.006  1.00 48.66  ?  215 LYS D CG  1 
ATOM 6499 C CD  . LYS D 2 215 ? -9.595  60.446  -1.039  1.00 64.08  ?  215 LYS D CD  1 
ATOM 6500 C CE  . LYS D 2 215 ? -11.019 60.846  -0.680  1.00 66.42  ?  215 LYS D CE  1 
ATOM 6501 N NZ  . LYS D 2 215 ? -11.055 61.921  0.357   1.00 67.06  ?  215 LYS D NZ  1 
ATOM 6502 N N   . LYS D 2 216 ? -6.272  61.844  -0.025  1.00 59.29  ?  216 LYS D N   1 
ATOM 6503 C CA  . LYS D 2 216 ? -5.859  62.737  1.045   1.00 60.99  ?  216 LYS D CA  1 
ATOM 6504 C C   . LYS D 2 216 ? -6.956  62.744  2.101   1.00 63.82  ?  216 LYS D C   1 
ATOM 6505 O O   . LYS D 2 216 ? -8.085  63.167  1.830   1.00 63.71  ?  216 LYS D O   1 
ATOM 6506 C CB  . LYS D 2 216 ? -5.601  64.138  0.499   1.00 61.55  ?  216 LYS D CB  1 
ATOM 6507 C CG  . LYS D 2 216 ? -5.220  65.159  1.553   1.00 63.91  ?  216 LYS D CG  1 
ATOM 6508 C CD  . LYS D 2 216 ? -4.979  66.531  0.940   1.00 66.18  ?  216 LYS D CD  1 
ATOM 6509 C CE  . LYS D 2 216 ? -4.708  67.576  2.017   1.00 71.21  ?  216 LYS D CE  1 
ATOM 6510 N NZ  . LYS D 2 216 ? -4.578  68.948  1.457   1.00 70.93  ?  216 LYS D NZ  1 
ATOM 6511 N N   . VAL D 2 217 ? -6.650  62.226  3.286   1.00 62.42  ?  217 VAL D N   1 
ATOM 6512 C CA  . VAL D 2 217 ? -7.597  62.281  4.392   1.00 64.27  ?  217 VAL D CA  1 
ATOM 6513 C C   . VAL D 2 217 ? -7.458  63.643  5.052   1.00 65.20  ?  217 VAL D C   1 
ATOM 6514 O O   . VAL D 2 217 ? -6.364  64.032  5.474   1.00 66.37  ?  217 VAL D O   1 
ATOM 6515 C CB  . VAL D 2 217 ? -7.371  61.147  5.398   1.00 60.71  ?  217 VAL D CB  1 
ATOM 6516 C CG1 . VAL D 2 217 ? -8.418  61.228  6.497   1.00 53.22  ?  217 VAL D CG1 1 
ATOM 6517 C CG2 . VAL D 2 217 ? -7.457  59.802  4.696   1.00 54.79  ?  217 VAL D CG2 1 
ATOM 6518 N N   . GLU D 2 218 ? -8.560  64.375  5.123   1.00 70.20  ?  218 GLU D N   1 
ATOM 6519 C CA  . GLU D 2 218 ? -8.547  65.723  5.648   1.00 75.58  ?  218 GLU D CA  1 
ATOM 6520 C C   . GLU D 2 218 ? -9.381  65.816  6.917   1.00 74.60  ?  218 GLU D C   1 
ATOM 6521 O O   . GLU D 2 218 ? -10.315 65.031  7.111   1.00 73.09  ?  218 GLU D O   1 
ATOM 6522 C CB  . GLU D 2 218 ? -9.083  66.716  4.610   1.00 76.61  ?  218 GLU D CB  1 
ATOM 6523 C CG  . GLU D 2 218 ? -8.201  66.839  3.393   1.00 72.17  ?  218 GLU D CG  1 
ATOM 6524 C CD  . GLU D 2 218 ? -8.658  67.933  2.462   1.00 82.39  ?  218 GLU D CD  1 
ATOM 6525 O OE1 . GLU D 2 218 ? -9.886  68.137  2.344   1.00 87.96  ?  218 GLU D OE1 1 
ATOM 6526 O OE2 . GLU D 2 218 ? -7.785  68.596  1.862   1.00 87.56  -1 218 GLU D OE2 1 
ATOM 6527 N N   . PRO D 2 219 ? -9.084  66.774  7.815   1.00 83.15  ?  219 PRO D N   1 
ATOM 6528 C CA  . PRO D 2 219 ? -9.789  66.848  9.064   1.00 82.52  ?  219 PRO D CA  1 
ATOM 6529 C C   . PRO D 2 219 ? -11.209 67.290  8.786   1.00 84.82  ?  219 PRO D C   1 
ATOM 6530 O O   . PRO D 2 219 ? -11.383 68.199  8.034   1.00 93.36  ?  219 PRO D O   1 
ATOM 6531 C CB  . PRO D 2 219 ? -9.118  68.000  9.806   1.00 75.57  ?  219 PRO D CB  1 
ATOM 6532 C CG  . PRO D 2 219 ? -7.774  68.133  9.158   1.00 82.34  ?  219 PRO D CG  1 
ATOM 6533 C CD  . PRO D 2 219 ? -8.057  67.821  7.708   1.00 85.56  ?  219 PRO D CD  1 
ATOM 6534 N N   . LYS D 2 220 ? -12.175 66.599  9.353   1.00 81.67  ?  220 LYS D N   1 
ATOM 6535 C CA  . LYS D 2 220 ? -13.538 67.137  9.227   1.00 89.94  ?  220 LYS D CA  1 
ATOM 6536 C C   . LYS D 2 220 ? -13.526 68.381  10.098  1.00 102.95 ?  220 LYS D C   1 
ATOM 6537 O O   . LYS D 2 220 ? -12.674 68.454  10.986  1.00 113.60 ?  220 LYS D O   1 
ATOM 6538 C CB  . LYS D 2 220 ? -14.578 66.149  9.745   1.00 93.69  ?  220 LYS D CB  1 
ATOM 6539 C CG  . LYS D 2 220 ? -14.727 64.869  8.933   1.00 96.81  ?  220 LYS D CG  1 
ATOM 6540 C CD  . LYS D 2 220 ? -15.754 63.911  9.503   1.00 94.60  ?  220 LYS D CD  1 
ATOM 6541 C CE  . LYS D 2 220 ? -15.922 62.648  8.684   1.00 96.14  ?  220 LYS D CE  1 
ATOM 6542 N NZ  . LYS D 2 220 ? -16.916 61.725  9.282   1.00 75.89  ?  220 LYS D NZ  1 
ATOM 6543 N N   . SER D 2 221 ? -14.411 69.335  9.844   1.00 115.29 ?  221 SER D N   1 
ATOM 6544 C CA  . SER D 2 221 ? -14.512 70.520  10.730  1.00 120.41 ?  221 SER D CA  1 
ATOM 6545 C C   . SER D 2 221 ? -15.998 70.844  10.565  1.00 127.08 ?  221 SER D C   1 
ATOM 6546 O O   . SER D 2 221 ? -16.342 71.442  9.528   1.00 124.29 ?  221 SER D O   1 
ATOM 6547 C CB  . SER D 2 221 ? -13.542 71.579  10.312  1.00 118.41 ?  221 SER D CB  1 
ATOM 6548 O OG  . SER D 2 221 ? -13.735 71.921  8.949   1.00 118.27 ?  221 SER D OG  1 
ATOM 6549 N N   . CYS D 2 222 ? -16.830 70.444  11.532  1.00 131.99 ?  222 CYS D N   1 
ATOM 6550 C CA  . CYS D 2 222 ? -18.274 70.814  11.568  1.00 132.74 ?  222 CYS D CA  1 
ATOM 6551 C C   . CYS D 2 222 ? -19.292 70.133  10.650  1.00 132.41 ?  222 CYS D C   1 
ATOM 6552 O O   . CYS D 2 222 ? -20.267 70.800  10.259  1.00 126.64 ?  222 CYS D O   1 
ATOM 6553 C CB  . CYS D 2 222 ? -18.489 72.322  11.516  1.00 129.43 ?  222 CYS D CB  1 
ATOM 6554 S SG  . CYS D 2 222 ? -18.024 73.169  13.047  1.00 140.11 ?  222 CYS D SG  1 
ATOM 6555 N N   . GLY D 2 223 ? -19.065 68.860  10.320  1.00 130.79 ?  223 GLY D N   1 
ATOM 6556 C CA  . GLY D 2 223 ? -20.037 68.107  9.505   1.00 124.60 ?  223 GLY D CA  1 
ATOM 6557 C C   . GLY D 2 223 ? -19.166 67.171  8.692   1.00 115.07 ?  223 GLY D C   1 
ATOM 6558 O O   . GLY D 2 223 ? -19.752 66.316  8.000   1.00 101.57 ?  223 GLY D O   1 
# 
