data_9OZ0
# 
_entry.id   9OZ0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9OZ0         pdb_00009oz0 10.2210/pdb9oz0/pdb 
WWPDB D_1000296716 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OZ0 
_pdbx_database_status.recvd_initial_deposition_date   2025-06-04 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
TargetTrack IDP95774 unspecified . 
TargetTrack IDP95776 unspecified . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexei.savchenko@ucalgary.ca 
_pdbx_contact_author.name_first         Alexei 
_pdbx_contact_author.name_last          Savchenko 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5256-9237 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stogios, P.J.'                                                1 ? 
'Borek, D.'                                                    2 ? 
'Skarina, T.'                                                  3 ? 
'Osipiuk, J.'                                                  4 ? 
'Di Leo, R.'                                                   5 ? 
'Savchenko, A.'                                                6 ? 
'Joachimiak, A.'                                               7 ? 
'Satchell, K.J.F.'                                             8 ? 
'Center for Structural Biology of Infectious Diseases (CSBID)' 9 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of T6SS effector-immunity complex PA3907-PA3908 from Pseudomonas aeruginosa' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Stogios, P.J.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 'Immunity protein 52 domain-containing protein' 27516.570 1 ? ? ? ? 
2 polymer     man 'Tox-REase-5 domain-containing protein'         21014.881 1 ? ? ? ? 
3 non-polymer syn 'CITRIC ACID'                                   192.124   1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                 24.305    1 ? ? ? ? 
5 water       nat water                                           18.015    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 yes 
;(MSE)TDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKAL
SRDRRTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWG
(MSE)LAPHAYFVHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREP(MSE)DETRREHFERVGEA
DIKL(MSE)ELGYLPPLRG
;
;MTDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKALSRDR
RTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWGMLAPHAYF
VHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREPMDETRREHFERVGEADIKLMELGYLPPLRG
;
A IDP95774 
2 'polypeptide(L)' no yes 
;QGRDKDCVECPPSRGE(MSE)AIANNGKGHS(MSE)SDLSARYQQWVTNFPFPHEWFWSGTWWDGFDEPRCTLLEAKANY
AFLFVPLLGVPRPWARAKVKSDLLQKAEVHSDKARPTPPVFVEWHFLQRIVYEYCAAEYLR(MSE)GLANLKAFWNP
(MSE)PGTDEHDDYQETRAKEQEE(MSE)KRFCEENPGYCA
;
;QGRDKDCVECPPSRGEMAIANNGKGHSMSDLSARYQQWVTNFPFPHEWFWSGTWWDGFDEPRCTLLEAKANYAFLFVPLL
GVPRPWARAKVKSDLLQKAEVHSDKARPTPPVFVEWHFLQRIVYEYCAAEYLRMGLANLKAFWNPMPGTDEHDDYQETRA
KEQEEMKRFCEENPGYCA
;
B IDP95776 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CITRIC ACID'   CIT 
4 'MAGNESIUM ION' MG  
5 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MSE n 
1 2   THR n 
1 3   ASP n 
1 4   ALA n 
1 5   LYS n 
1 6   ALA n 
1 7   PHE n 
1 8   ARG n 
1 9   ARG n 
1 10  TYR n 
1 11  ILE n 
1 12  PHE n 
1 13  GLU n 
1 14  LEU n 
1 15  TYR n 
1 16  PHE n 
1 17  ASP n 
1 18  PRO n 
1 19  ALA n 
1 20  ARG n 
1 21  LEU n 
1 22  LEU n 
1 23  GLU n 
1 24  LEU n 
1 25  ASP n 
1 26  ASP n 
1 27  ASP n 
1 28  GLN n 
1 29  HIS n 
1 30  LEU n 
1 31  GLN n 
1 32  ARG n 
1 33  ILE n 
1 34  GLU n 
1 35  ARG n 
1 36  PHE n 
1 37  LEU n 
1 38  ASP n 
1 39  ALA n 
1 40  LEU n 
1 41  ALA n 
1 42  PRO n 
1 43  LEU n 
1 44  HIS n 
1 45  PRO n 
1 46  VAL n 
1 47  LEU n 
1 48  GLU n 
1 49  ASN n 
1 50  TRP n 
1 51  TYR n 
1 52  LEU n 
1 53  CYS n 
1 54  GLY n 
1 55  ASP n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ASP n 
1 60  ALA n 
1 61  LEU n 
1 62  SER n 
1 63  HIS n 
1 64  ASN n 
1 65  VAL n 
1 66  THR n 
1 67  GLU n 
1 68  HIS n 
1 69  ARG n 
1 70  GLN n 
1 71  ASP n 
1 72  LEU n 
1 73  ALA n 
1 74  LYS n 
1 75  ALA n 
1 76  LEU n 
1 77  SER n 
1 78  ARG n 
1 79  ASP n 
1 80  ARG n 
1 81  ARG n 
1 82  THR n 
1 83  ARG n 
1 84  ALA n 
1 85  VAL n 
1 86  GLU n 
1 87  LEU n 
1 88  VAL n 
1 89  LEU n 
1 90  TRP n 
1 91  ASN n 
1 92  GLY n 
1 93  GLU n 
1 94  GLU n 
1 95  ASP n 
1 96  PRO n 
1 97  LEU n 
1 98  LYS n 
1 99  GLY n 
1 100 GLY n 
1 101 LEU n 
1 102 SER n 
1 103 LEU n 
1 104 ASP n 
1 105 TYR n 
1 106 GLU n 
1 107 ALA n 
1 108 SER n 
1 109 GLY n 
1 110 ARG n 
1 111 ALA n 
1 112 VAL n 
1 113 SER n 
1 114 SER n 
1 115 ARG n 
1 116 LEU n 
1 117 GLN n 
1 118 LEU n 
1 119 GLU n 
1 120 ASP n 
1 121 ALA n 
1 122 GLY n 
1 123 SER n 
1 124 LEU n 
1 125 LEU n 
1 126 GLN n 
1 127 VAL n 
1 128 PHE n 
1 129 ASP n 
1 130 ALA n 
1 131 PRO n 
1 132 ALA n 
1 133 SER n 
1 134 SER n 
1 135 PHE n 
1 136 VAL n 
1 137 ALA n 
1 138 ILE n 
1 139 PHE n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLU n 
1 145 ILE n 
1 146 TRP n 
1 147 PRO n 
1 148 GLU n 
1 149 THR n 
1 150 THR n 
1 151 TRP n 
1 152 GLY n 
1 153 MSE n 
1 154 LEU n 
1 155 ALA n 
1 156 PRO n 
1 157 HIS n 
1 158 ALA n 
1 159 TYR n 
1 160 PHE n 
1 161 VAL n 
1 162 HIS n 
1 163 GLN n 
1 164 ARG n 
1 165 THR n 
1 166 PHE n 
1 167 PRO n 
1 168 ASP n 
1 169 ARG n 
1 170 ARG n 
1 171 SER n 
1 172 ILE n 
1 173 GLY n 
1 174 TRP n 
1 175 ILE n 
1 176 GLY n 
1 177 PHE n 
1 178 CYS n 
1 179 PRO n 
1 180 HIS n 
1 181 PRO n 
1 182 LEU n 
1 183 ARG n 
1 184 ALA n 
1 185 THR n 
1 186 ASP n 
1 187 PHE n 
1 188 PRO n 
1 189 ALA n 
1 190 ALA n 
1 191 THR n 
1 192 GLU n 
1 193 LEU n 
1 194 VAL n 
1 195 ASP n 
1 196 ILE n 
1 197 PRO n 
1 198 GLY n 
1 199 ARG n 
1 200 GLY n 
1 201 THR n 
1 202 LEU n 
1 203 LEU n 
1 204 LEU n 
1 205 ASN n 
1 206 GLY n 
1 207 ARG n 
1 208 GLU n 
1 209 PRO n 
1 210 MSE n 
1 211 ASP n 
1 212 GLU n 
1 213 THR n 
1 214 ARG n 
1 215 ARG n 
1 216 GLU n 
1 217 HIS n 
1 218 PHE n 
1 219 GLU n 
1 220 ARG n 
1 221 VAL n 
1 222 GLY n 
1 223 GLU n 
1 224 ALA n 
1 225 ASP n 
1 226 ILE n 
1 227 LYS n 
1 228 LEU n 
1 229 MSE n 
1 230 GLU n 
1 231 LEU n 
1 232 GLY n 
1 233 TYR n 
1 234 LEU n 
1 235 PRO n 
1 236 PRO n 
1 237 LEU n 
1 238 ARG n 
1 239 GLY n 
2 1   GLN n 
2 2   GLY n 
2 3   ARG n 
2 4   ASP n 
2 5   LYS n 
2 6   ASP n 
2 7   CYS n 
2 8   VAL n 
2 9   GLU n 
2 10  CYS n 
2 11  PRO n 
2 12  PRO n 
2 13  SER n 
2 14  ARG n 
2 15  GLY n 
2 16  GLU n 
2 17  MSE n 
2 18  ALA n 
2 19  ILE n 
2 20  ALA n 
2 21  ASN n 
2 22  ASN n 
2 23  GLY n 
2 24  LYS n 
2 25  GLY n 
2 26  HIS n 
2 27  SER n 
2 28  MSE n 
2 29  SER n 
2 30  ASP n 
2 31  LEU n 
2 32  SER n 
2 33  ALA n 
2 34  ARG n 
2 35  TYR n 
2 36  GLN n 
2 37  GLN n 
2 38  TRP n 
2 39  VAL n 
2 40  THR n 
2 41  ASN n 
2 42  PHE n 
2 43  PRO n 
2 44  PHE n 
2 45  PRO n 
2 46  HIS n 
2 47  GLU n 
2 48  TRP n 
2 49  PHE n 
2 50  TRP n 
2 51  SER n 
2 52  GLY n 
2 53  THR n 
2 54  TRP n 
2 55  TRP n 
2 56  ASP n 
2 57  GLY n 
2 58  PHE n 
2 59  ASP n 
2 60  GLU n 
2 61  PRO n 
2 62  ARG n 
2 63  CYS n 
2 64  THR n 
2 65  LEU n 
2 66  LEU n 
2 67  GLU n 
2 68  ALA n 
2 69  LYS n 
2 70  ALA n 
2 71  ASN n 
2 72  TYR n 
2 73  ALA n 
2 74  PHE n 
2 75  LEU n 
2 76  PHE n 
2 77  VAL n 
2 78  PRO n 
2 79  LEU n 
2 80  LEU n 
2 81  GLY n 
2 82  VAL n 
2 83  PRO n 
2 84  ARG n 
2 85  PRO n 
2 86  TRP n 
2 87  ALA n 
2 88  ARG n 
2 89  ALA n 
2 90  LYS n 
2 91  VAL n 
2 92  LYS n 
2 93  SER n 
2 94  ASP n 
2 95  LEU n 
2 96  LEU n 
2 97  GLN n 
2 98  LYS n 
2 99  ALA n 
2 100 GLU n 
2 101 VAL n 
2 102 HIS n 
2 103 SER n 
2 104 ASP n 
2 105 LYS n 
2 106 ALA n 
2 107 ARG n 
2 108 PRO n 
2 109 THR n 
2 110 PRO n 
2 111 PRO n 
2 112 VAL n 
2 113 PHE n 
2 114 VAL n 
2 115 GLU n 
2 116 TRP n 
2 117 HIS n 
2 118 PHE n 
2 119 LEU n 
2 120 GLN n 
2 121 ARG n 
2 122 ILE n 
2 123 VAL n 
2 124 TYR n 
2 125 GLU n 
2 126 TYR n 
2 127 CYS n 
2 128 ALA n 
2 129 ALA n 
2 130 GLU n 
2 131 TYR n 
2 132 LEU n 
2 133 ARG n 
2 134 MSE n 
2 135 GLY n 
2 136 LEU n 
2 137 ALA n 
2 138 ASN n 
2 139 LEU n 
2 140 LYS n 
2 141 ALA n 
2 142 PHE n 
2 143 TRP n 
2 144 ASN n 
2 145 PRO n 
2 146 MSE n 
2 147 PRO n 
2 148 GLY n 
2 149 THR n 
2 150 ASP n 
2 151 GLU n 
2 152 HIS n 
2 153 ASP n 
2 154 ASP n 
2 155 TYR n 
2 156 GLN n 
2 157 GLU n 
2 158 THR n 
2 159 ARG n 
2 160 ALA n 
2 161 LYS n 
2 162 GLU n 
2 163 GLN n 
2 164 GLU n 
2 165 GLU n 
2 166 MSE n 
2 167 LYS n 
2 168 ARG n 
2 169 PHE n 
2 170 CYS n 
2 171 GLU n 
2 172 GLU n 
2 173 ASN n 
2 174 PRO n 
2 175 GLY n 
2 176 TYR n 
2 177 CYS n 
2 178 ALA 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' 1 239 ? ? PA3908 ? ? ? ? ? ? 'Pseudomonas aeruginosa' 287 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? -Magic ? ? ? ? ? ? plasmid ? ? ? pETDuet-1 ? ? 
2 1 sample 'Biological sequence' 1 178 ? ? PA3907 ? ? ? ? ? ? 'Pseudomonas aeruginosa' 287 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? -Magic ? ? ? ? ? ? plasmid ? ? ? pETDuet-1 ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CIT non-polymer         . 'CITRIC ACID'    ? 'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ? 'C6 H15 N2 O2 1' 147.195 
MG  non-polymer         . 'MAGNESIUM ION'  ? 'Mg 2'           24.305  
MSE 'L-peptide linking' n SELENOMETHIONINE ? 'C5 H11 N O2 Se' 196.106 
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   MSE 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  HIS 29  29  29  HIS HIS A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  TRP 50  50  50  TRP TRP A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  CYS 53  53  53  CYS CYS A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 TRP 146 146 146 TRP TRP A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 TRP 151 151 151 TRP TRP A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 MSE 153 153 153 MSE MSE A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 HIS 157 157 157 HIS HIS A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 TRP 174 174 174 TRP TRP A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 MSE 210 210 210 MSE MSE A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LYS 227 227 227 LYS ALA A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 MSE 229 229 229 MSE MSE A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 TYR 233 233 233 TYR TYR A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
B 2 1   GLN 1   84  84  GLN GLN B . n 
B 2 2   GLY 2   85  85  GLY GLY B . n 
B 2 3   ARG 3   86  86  ARG ARG B . n 
B 2 4   ASP 4   87  87  ASP ASP B . n 
B 2 5   LYS 5   88  88  LYS LYS B . n 
B 2 6   ASP 6   89  89  ASP ASP B . n 
B 2 7   CYS 7   90  90  CYS CYS B . n 
B 2 8   VAL 8   91  91  VAL VAL B . n 
B 2 9   GLU 9   92  92  GLU GLU B . n 
B 2 10  CYS 10  93  93  CYS CYS B . n 
B 2 11  PRO 11  94  94  PRO PRO B . n 
B 2 12  PRO 12  95  95  PRO PRO B . n 
B 2 13  SER 13  96  96  SER SER B . n 
B 2 14  ARG 14  97  97  ARG ARG B . n 
B 2 15  GLY 15  98  98  GLY GLY B . n 
B 2 16  GLU 16  99  99  GLU GLU B . n 
B 2 17  MSE 17  100 100 MSE MSE B . n 
B 2 18  ALA 18  101 101 ALA ALA B . n 
B 2 19  ILE 19  102 102 ILE ILE B . n 
B 2 20  ALA 20  103 103 ALA ALA B . n 
B 2 21  ASN 21  104 104 ASN ASN B . n 
B 2 22  ASN 22  105 105 ASN ASN B . n 
B 2 23  GLY 23  106 106 GLY ALA B . n 
B 2 24  LYS 24  107 107 LYS LYS B . n 
B 2 25  GLY 25  108 108 GLY GLY B . n 
B 2 26  HIS 26  109 109 HIS HIS B . n 
B 2 27  SER 27  110 110 SER SER B . n 
B 2 28  MSE 28  111 111 MSE MSE B . n 
B 2 29  SER 29  112 112 SER SER B . n 
B 2 30  ASP 30  113 113 ASP ASP B . n 
B 2 31  LEU 31  114 114 LEU LEU B . n 
B 2 32  SER 32  115 115 SER SER B . n 
B 2 33  ALA 33  116 116 ALA ALA B . n 
B 2 34  ARG 34  117 117 ARG ARG B . n 
B 2 35  TYR 35  118 118 TYR TYR B . n 
B 2 36  GLN 36  119 119 GLN GLN B . n 
B 2 37  GLN 37  120 120 GLN GLN B . n 
B 2 38  TRP 38  121 121 TRP TRP B . n 
B 2 39  VAL 39  122 122 VAL VAL B . n 
B 2 40  THR 40  123 123 THR THR B . n 
B 2 41  ASN 41  124 124 ASN ASN B . n 
B 2 42  PHE 42  125 125 PHE PHE B . n 
B 2 43  PRO 43  126 126 PRO PRO B . n 
B 2 44  PHE 44  127 127 PHE PHE B . n 
B 2 45  PRO 45  128 128 PRO PRO B . n 
B 2 46  HIS 46  129 129 HIS HIS B . n 
B 2 47  GLU 47  130 130 GLU GLU B . n 
B 2 48  TRP 48  131 131 TRP TRP B . n 
B 2 49  PHE 49  132 132 PHE PHE B . n 
B 2 50  TRP 50  133 133 TRP TRP B . n 
B 2 51  SER 51  134 134 SER SER B . n 
B 2 52  GLY 52  135 135 GLY GLY B . n 
B 2 53  THR 53  136 136 THR THR B . n 
B 2 54  TRP 54  137 137 TRP TRP B . n 
B 2 55  TRP 55  138 138 TRP TRP B . n 
B 2 56  ASP 56  139 139 ASP ASP B . n 
B 2 57  GLY 57  140 140 GLY GLY B . n 
B 2 58  PHE 58  141 141 PHE PHE B . n 
B 2 59  ASP 59  142 142 ASP ASP B . n 
B 2 60  GLU 60  143 143 GLU GLU B . n 
B 2 61  PRO 61  144 144 PRO PRO B . n 
B 2 62  ARG 62  145 145 ARG ARG B . n 
B 2 63  CYS 63  146 146 CYS CYS B . n 
B 2 64  THR 64  147 147 THR THR B . n 
B 2 65  LEU 65  148 148 LEU LEU B . n 
B 2 66  LEU 66  149 149 LEU LEU B . n 
B 2 67  GLU 67  150 150 GLU GLU B . n 
B 2 68  ALA 68  151 151 ALA ALA B . n 
B 2 69  LYS 69  152 152 LYS LYS B . n 
B 2 70  ALA 70  153 153 ALA ALA B . n 
B 2 71  ASN 71  154 154 ASN ASN B . n 
B 2 72  TYR 72  155 155 TYR TYR B . n 
B 2 73  ALA 73  156 156 ALA ALA B . n 
B 2 74  PHE 74  157 157 PHE PHE B . n 
B 2 75  LEU 75  158 158 LEU LEU B . n 
B 2 76  PHE 76  159 159 PHE PHE B . n 
B 2 77  VAL 77  160 160 VAL VAL B . n 
B 2 78  PRO 78  161 161 PRO PRO B . n 
B 2 79  LEU 79  162 162 LEU LEU B . n 
B 2 80  LEU 80  163 163 LEU LEU B . n 
B 2 81  GLY 81  164 164 GLY GLY B . n 
B 2 82  VAL 82  165 165 VAL VAL B . n 
B 2 83  PRO 83  166 166 PRO PRO B . n 
B 2 84  ARG 84  167 167 ARG ARG B . n 
B 2 85  PRO 85  168 168 PRO PRO B . n 
B 2 86  TRP 86  169 169 TRP TRP B . n 
B 2 87  ALA 87  170 170 ALA ALA B . n 
B 2 88  ARG 88  171 171 ARG ARG B . n 
B 2 89  ALA 89  172 172 ALA ALA B . n 
B 2 90  LYS 90  173 173 LYS LYS B . n 
B 2 91  VAL 91  174 174 VAL VAL B . n 
B 2 92  LYS 92  175 175 LYS LYS B . n 
B 2 93  SER 93  176 176 SER SER B . n 
B 2 94  ASP 94  177 177 ASP ASP B . n 
B 2 95  LEU 95  178 178 LEU LEU B . n 
B 2 96  LEU 96  179 179 LEU LEU B . n 
B 2 97  GLN 97  180 180 GLN GLN B . n 
B 2 98  LYS 98  181 181 LYS LYS B . n 
B 2 99  ALA 99  182 182 ALA ALA B . n 
B 2 100 GLU 100 183 183 GLU GLU B . n 
B 2 101 VAL 101 184 184 VAL VAL B . n 
B 2 102 HIS 102 185 185 HIS HIS B . n 
B 2 103 SER 103 186 186 SER SER B . n 
B 2 104 ASP 104 187 187 ASP ASP B . n 
B 2 105 LYS 105 188 188 LYS LYS B . n 
B 2 106 ALA 106 189 189 ALA ALA B . n 
B 2 107 ARG 107 190 190 ARG ARG B . n 
B 2 108 PRO 108 191 191 PRO PRO B . n 
B 2 109 THR 109 192 192 THR THR B . n 
B 2 110 PRO 110 193 193 PRO PRO B . n 
B 2 111 PRO 111 194 194 PRO PRO B . n 
B 2 112 VAL 112 195 195 VAL VAL B . n 
B 2 113 PHE 113 196 196 PHE PHE B . n 
B 2 114 VAL 114 197 197 VAL VAL B . n 
B 2 115 GLU 115 198 198 GLU GLU B . n 
B 2 116 TRP 116 199 199 TRP TRP B . n 
B 2 117 HIS 117 200 200 HIS HIS B . n 
B 2 118 PHE 118 201 201 PHE PHE B . n 
B 2 119 LEU 119 202 202 LEU LEU B . n 
B 2 120 GLN 120 203 203 GLN GLN B . n 
B 2 121 ARG 121 204 204 ARG ARG B . n 
B 2 122 ILE 122 205 205 ILE ILE B . n 
B 2 123 VAL 123 206 206 VAL VAL B . n 
B 2 124 TYR 124 207 207 TYR TYR B . n 
B 2 125 GLU 125 208 208 GLU GLU B . n 
B 2 126 TYR 126 209 209 TYR TYR B . n 
B 2 127 CYS 127 210 210 CYS CYS B . n 
B 2 128 ALA 128 211 211 ALA ALA B . n 
B 2 129 ALA 129 212 212 ALA ALA B . n 
B 2 130 GLU 130 213 213 GLU GLU B . n 
B 2 131 TYR 131 214 214 TYR TYR B . n 
B 2 132 LEU 132 215 215 LEU LEU B . n 
B 2 133 ARG 133 216 216 ARG ARG B . n 
B 2 134 MSE 134 217 217 MSE MSE B . n 
B 2 135 GLY 135 218 218 GLY GLY B . n 
B 2 136 LEU 136 219 219 LEU LEU B . n 
B 2 137 ALA 137 220 220 ALA ALA B . n 
B 2 138 ASN 138 221 221 ASN ASN B . n 
B 2 139 LEU 139 222 222 LEU LEU B . n 
B 2 140 LYS 140 223 223 LYS LYS B . n 
B 2 141 ALA 141 224 224 ALA ALA B . n 
B 2 142 PHE 142 225 225 PHE PHE B . n 
B 2 143 TRP 143 226 226 TRP TRP B . n 
B 2 144 ASN 144 227 227 ASN ASN B . n 
B 2 145 PRO 145 228 228 PRO PRO B . n 
B 2 146 MSE 146 229 229 MSE MSE B . n 
B 2 147 PRO 147 230 230 PRO PRO B . n 
B 2 148 GLY 148 231 231 GLY GLY B . n 
B 2 149 THR 149 232 232 THR THR B . n 
B 2 150 ASP 150 233 233 ASP ASP B . n 
B 2 151 GLU 151 234 234 GLU GLU B . n 
B 2 152 HIS 152 235 235 HIS HIS B . n 
B 2 153 ASP 153 236 236 ASP ASP B . n 
B 2 154 ASP 154 237 237 ASP ASP B . n 
B 2 155 TYR 155 238 238 TYR TYR B . n 
B 2 156 GLN 156 239 239 GLN GLN B . n 
B 2 157 GLU 157 240 240 GLU GLU B . n 
B 2 158 THR 158 241 241 THR THR B . n 
B 2 159 ARG 159 242 242 ARG ARG B . n 
B 2 160 ALA 160 243 243 ALA ALA B . n 
B 2 161 LYS 161 244 244 LYS LYS B . n 
B 2 162 GLU 162 245 245 GLU GLU B . n 
B 2 163 GLN 163 246 246 GLN GLN B . n 
B 2 164 GLU 164 247 247 GLU GLU B . n 
B 2 165 GLU 165 248 248 GLU GLU B . n 
B 2 166 MSE 166 249 249 MSE MSE B . n 
B 2 167 LYS 167 250 250 LYS LYS B . n 
B 2 168 ARG 168 251 251 ARG ARG B . n 
B 2 169 PHE 169 252 252 PHE PHE B . n 
B 2 170 CYS 170 253 ?   ?   ?   B . n 
B 2 171 GLU 171 254 ?   ?   ?   B . n 
B 2 172 GLU 172 255 ?   ?   ?   B . n 
B 2 173 ASN 173 256 ?   ?   ?   B . n 
B 2 174 PRO 174 257 ?   ?   ?   B . n 
B 2 175 GLY 175 258 ?   ?   ?   B . n 
B 2 176 TYR 176 259 ?   ?   ?   B . n 
B 2 177 CYS 177 260 ?   ?   ?   B . n 
B 2 178 ALA 178 261 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CIT 1 301 2 CIT CIT B . 
D 4 MG  1 302 1 MG  MG  B . 
E 5 HOH 1 401 1 HOH HOH B . 
E 5 HOH 2 402 2 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 227 ? CG ? A LYS 227 CG 
2 1 Y 1 A LYS 227 ? CD ? A LYS 227 CD 
3 1 Y 1 A LYS 227 ? CE ? A LYS 227 CE 
4 1 Y 1 A LYS 227 ? NZ ? A LYS 227 NZ 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(dev_3092: ???)' ? 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                 ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .                 ? 3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .                 ? 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .                 ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OZ0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     167.329 
_cell.length_a_esd                 ? 
_cell.length_b                     167.329 
_cell.length_b_esd                 ? 
_cell.length_c                     167.329 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9OZ0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                213 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9OZ0 
_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             4.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          69.69 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG3350 25%, KCl 0.1M, NaCl 0.1M, MgCl2 10mM, Hepes 0.1M pH 7.5, 10mM NH4Citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-03-01 
_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   0.97929 
_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                        'APS BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97929 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9OZ0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.87 
_reflns.d_resolution_low                               30.00 
_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                                     18909 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.2 
_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                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.097 
_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                                    2.87 
_reflns_shell.d_res_low                                     2.92 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             925 
_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                               9.3 
_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                               0.458 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.528 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.337 
_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                                 9OZ0 
_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                            2.871 
_refine.ls_d_res_low                             29.580 
_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                     18870 
_refine.ls_number_reflns_R_free                  944 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2305 
_refine.ls_R_factor_R_free                       0.2855 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2277 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_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                 28.32 
_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                            0.38 
_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                       2.871 
_refine_hist.d_res_low                        29.580 
_refine_hist.number_atoms_solvent             2 
_refine_hist.number_atoms_total               3311 
_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        3295 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003 ? 3407 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.686 ? 4632 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 6.762 ? 2019 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 473  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 612  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.871  3.0217 . . 131 2494 100.00 . . . . 0.3224 . . . . . . . . . . . . . . . 0.3467 
'X-RAY DIFFRACTION' 3.0217 3.2108 . . 132 2507 100.00 . . . . 0.3073 . . . . . . . . . . . . . . . 0.3591 
'X-RAY DIFFRACTION' 3.2108 3.4584 . . 132 2514 100.00 . . . . 0.2700 . . . . . . . . . . . . . . . 0.3266 
'X-RAY DIFFRACTION' 3.4584 3.8058 . . 133 2531 100.00 . . . . 0.2479 . . . . . . . . . . . . . . . 0.3032 
'X-RAY DIFFRACTION' 3.8058 4.3550 . . 135 2540 100.00 . . . . 0.2156 . . . . . . . . . . . . . . . 0.3227 
'X-RAY DIFFRACTION' 4.3550 5.4811 . . 136 2595 100.00 . . . . 0.1957 . . . . . . . . . . . . . . . 0.2264 
'X-RAY DIFFRACTION' 5.4811 29.58  . . 145 2745 100.00 . . . . 0.2127 . . . . . . . . . . . . . . . 0.2674 
# 
_struct.entry_id                     9OZ0 
_struct.title                        
'Crystal structure of T6SS effector-immunity complex PA3907-PA3908 from Pseudomonas aeruginosa' 
_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        9OZ0 
_struct_keywords.text            
;effector, immunity, complex, type 6, T6SS, secretion system, Structural Genomics, Center for Structural Biology of Infectious Diseases, CSBID, UNKNOWN FUNCTION
;
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q9HXA5_PSEAE Q9HXA5 ? 1 
;MTDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKALSRDR
RTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWGMLAPHAYF
VHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREPMDETRREHFERVGEADIKLMELGYLPPLRG
;
1  
2 UNP Q9HXA6_PSEAE Q9HXA6 ? 2 
;QGRDKDCVECPPSRGEMAIANNGKGHSMSDLSARYQQWVTNFPFPHEWFWSGTWWDGFDEPRCTLLEAKANYAFLFVPLL
GVPRPWARAKVKSDLLQKAEVHSDKARPTPPVFVEWHFLQRIVYEYCAAEYLRMGLANLKAFWNPMPGTDEHDDYQETRA
KEQEEMKRFCEENPGYCA
;
84 
# 
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 9OZ0 A 1 ? 239 ? Q9HXA5 1  ? 239 ? 1  239 
2 2 9OZ0 B 1 ? 178 ? Q9HXA6 84 ? 261 ? 84 261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2980  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  19530 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 17  ? LEU A 22  ? ASP A 17  LEU A 22  1 ? 6  
HELX_P HELX_P2  AA2 ASP A 25  ? ALA A 41  ? ASP A 25  ALA A 41  1 ? 17 
HELX_P HELX_P3  AA3 PRO A 42  ? GLU A 48  ? PRO A 42  GLU A 48  5 ? 7  
HELX_P HELX_P4  AA4 SER A 56  ? LEU A 61  ? SER A 56  LEU A 61  1 ? 6  
HELX_P HELX_P5  AA5 HIS A 68  ? LEU A 72  ? HIS A 68  LEU A 72  5 ? 5  
HELX_P HELX_P6  AA6 ASP A 95  ? GLY A 99  ? ASP A 95  GLY A 99  5 ? 5  
HELX_P HELX_P7  AA7 ARG A 110 ? VAL A 112 ? ARG A 110 VAL A 112 5 ? 3  
HELX_P HELX_P8  AA8 ALA A 121 ? GLN A 126 ? ALA A 121 GLN A 126 1 ? 6  
HELX_P HELX_P9  AA9 ALA A 130 ? TRP A 146 ? ALA A 130 TRP A 146 1 ? 17 
HELX_P HELX_P10 AB1 HIS A 157 ? ARG A 164 ? HIS A 157 ARG A 164 1 ? 8  
HELX_P HELX_P11 AB2 ARG A 214 ? LEU A 231 ? ARG A 214 LEU A 231 1 ? 18 
HELX_P HELX_P12 AB3 CYS B 10  ? GLY B 15  ? CYS B 93  GLY B 98  5 ? 6  
HELX_P HELX_P13 AB4 ASP B 30  ? ASN B 41  ? ASP B 113 ASN B 124 1 ? 12 
HELX_P HELX_P14 AB5 TYR B 72  ? PHE B 76  ? TYR B 155 PHE B 159 5 ? 5  
HELX_P HELX_P15 AB6 ARG B 84  ? TRP B 86  ? ARG B 167 TRP B 169 5 ? 3  
HELX_P HELX_P16 AB7 ALA B 87  ? LEU B 95  ? ALA B 170 LEU B 178 1 ? 9  
HELX_P HELX_P17 AB8 LEU B 96  ? ALA B 106 ? LEU B 179 ALA B 189 1 ? 11 
HELX_P HELX_P18 AB9 GLN B 120 ? GLY B 135 ? GLN B 203 GLY B 218 1 ? 16 
HELX_P HELX_P19 AC1 THR B 149 ? LYS B 161 ? THR B 232 LYS B 244 1 ? 13 
# 
_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 ?    ? B CYS 10  SG ? ? ? 1_555 B CYS 63  SG ? ? B CYS 93  B CYS 146 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
covale1  covale both ? A GLY 152 C  ? ? ? 1_555 A MSE 153 N  ? ? A GLY 152 A MSE 153 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2  covale both ? A MSE 153 C  ? ? ? 1_555 A LEU 154 N  ? ? A MSE 153 A LEU 154 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale3  covale both ? A PRO 209 C  ? ? ? 1_555 A MSE 210 N  ? ? A PRO 209 A MSE 210 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale4  covale both ? A MSE 210 C  ? ? ? 1_555 A ASP 211 N  ? ? A MSE 210 A ASP 211 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale5  covale both ? A LEU 228 C  ? ? ? 1_555 A MSE 229 N  ? ? A LEU 228 A MSE 229 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale6  covale both ? A MSE 229 C  ? ? ? 1_555 A GLU 230 N  ? ? A MSE 229 A GLU 230 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale7  covale both ? B GLU 16  C  ? ? ? 1_555 B MSE 17  N  ? ? B GLU 99  B MSE 100 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale8  covale both ? B MSE 17  C  ? ? ? 1_555 B ALA 18  N  ? ? B MSE 100 B ALA 101 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale9  covale both ? B SER 27  C  ? ? ? 1_555 B MSE 28  N  ? ? B SER 110 B MSE 111 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale10 covale both ? B MSE 28  C  ? ? ? 1_555 B SER 29  N  ? ? B MSE 111 B SER 112 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale11 covale both ? B ARG 133 C  ? ? ? 1_555 B MSE 134 N  ? ? B ARG 216 B MSE 217 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale12 covale both ? B MSE 134 C  ? ? ? 1_555 B GLY 135 N  ? ? B MSE 217 B GLY 218 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale13 covale both ? B PRO 145 C  ? ? ? 1_555 B MSE 146 N  ? ? B PRO 228 B MSE 229 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale14 covale both ? B MSE 146 C  ? ? ? 1_555 B PRO 147 N  ? ? B MSE 229 B PRO 230 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale15 covale both ? B GLU 165 C  ? ? ? 1_555 B MSE 166 N  ? ? B GLU 248 B MSE 249 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale16 covale both ? B MSE 166 C  ? ? ? 1_555 B LYS 167 N  ? ? B MSE 249 B LYS 250 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
metalc1  metalc ?    ? D MG  .   MG ? ? ? 1_555 E HOH .   O  ? ? B MG  302 B HOH 401 1_555 ? ? ? ? ? ? ? 2.858 ? ? 
metalc2  metalc ?    ? D MG  .   MG ? ? ? 1_555 E HOH .   O  ? ? B MG  302 B HOH 402 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     401 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   D 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     302 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     402 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 147.6 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 MSE A 153 ? .   . .  . MSE A 153 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
2 MSE A 210 ? .   . .  . MSE A 210 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
3 MSE A 229 ? .   . .  . MSE A 229 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
4 MSE B 17  ? .   . .  . MSE B 100 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
5 MSE B 28  ? .   . .  . MSE B 111 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
6 MSE B 134 ? .   . .  . MSE B 217 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
7 MSE B 146 ? .   . .  . MSE B 229 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
8 MSE B 166 ? .   . .  . MSE B 249 ? 1_555 .   . .   . .     .  .  MET 1 MSE Selenomethionine 'Named protein modification' 
9 CYS B 10  ? CYS B 63 ? CYS B 93  ? 1_555 CYS B 146 ? 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 GLU 119 A . ? GLU 119 A ASP 120 A ? ASP 120 A 1 -2.50 
2 PHE 44  B . ? PHE 127 B PRO 45  B ? PRO 128 B 1 -0.86 
3 ARG 107 B . ? ARG 190 B PRO 108 B ? PRO 191 B 1 1.72  
4 THR 109 B . ? THR 192 B PRO 110 B ? PRO 193 B 1 -0.04 
5 PRO 110 B . ? PRO 193 B PRO 111 B ? PRO 194 B 1 1.50  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 9 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? 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 TYR A 51  ? LEU A 52  ? TYR A 51  LEU A 52  
AA1 2 VAL A 85  ? TRP A 90  ? VAL A 85  TRP A 90  
AA1 3 LEU A 76  ? ARG A 78  ? LEU A 76  ARG A 78  
AA2 1 TYR A 51  ? LEU A 52  ? TYR A 51  LEU A 52  
AA2 2 VAL A 85  ? TRP A 90  ? VAL A 85  TRP A 90  
AA2 3 SER A 102 ? ALA A 107 ? SER A 102 ALA A 107 
AA2 4 SER A 114 ? GLU A 119 ? SER A 114 GLU A 119 
AA2 5 TYR A 10  ? PHE A 16  ? TYR A 10  PHE A 16  
AA2 6 THR A 149 ? PRO A 156 ? THR A 149 PRO A 156 
AA2 7 ILE A 175 ? CYS A 178 ? ILE A 175 CYS A 178 
AA2 8 GLY A 200 ? ASN A 205 ? GLY A 200 ASN A 205 
AA2 9 THR A 191 ? ILE A 196 ? THR A 191 ILE A 196 
AA3 1 GLU B 16  ? ILE B 19  ? GLU B 99  ILE B 102 
AA3 2 HIS B 46  ? TRP B 50  ? HIS B 129 TRP B 133 
AA3 3 THR B 53  ? TRP B 55  ? THR B 136 TRP B 138 
AA4 1 GLY B 57  ? ASP B 59  ? GLY B 140 ASP B 142 
AA4 2 THR B 64  ? LYS B 69  ? THR B 147 LYS B 152 
AA4 3 PHE B 113 ? PHE B 118 ? PHE B 196 PHE B 201 
AA4 4 LEU B 139 ? TRP B 143 ? LEU B 222 TRP B 226 
# 
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 TYR A 51  ? N TYR A 51  O TRP A 90  ? O TRP A 90  
AA1 2 3 O GLU A 86  ? O GLU A 86  N SER A 77  ? N SER A 77  
AA2 1 2 N TYR A 51  ? N TYR A 51  O TRP A 90  ? O TRP A 90  
AA2 2 3 N LEU A 89  ? N LEU A 89  O LEU A 103 ? O LEU A 103 
AA2 3 4 N SER A 102 ? N SER A 102 O GLU A 119 ? O GLU A 119 
AA2 4 5 O LEU A 116 ? O LEU A 116 N LEU A 14  ? N LEU A 14  
AA2 5 6 N ILE A 11  ? N ILE A 11  O ALA A 155 ? O ALA A 155 
AA2 6 7 N GLY A 152 ? N GLY A 152 O PHE A 177 ? O PHE A 177 
AA2 7 8 N GLY A 176 ? N GLY A 176 O LEU A 203 ? O LEU A 203 
AA2 8 9 O LEU A 204 ? O LEU A 204 N GLU A 192 ? N GLU A 192 
AA3 1 2 N GLU B 16  ? N GLU B 99  O PHE B 49  ? O PHE B 132 
AA3 2 3 N TRP B 48  ? N TRP B 131 O TRP B 55  ? O TRP B 138 
AA4 1 2 N ASP B 59  ? N ASP B 142 O THR B 64  ? O THR B 147 
AA4 2 3 N LEU B 65  ? N LEU B 148 O GLU B 115 ? O GLU B 198 
AA4 3 4 N PHE B 118 ? N PHE B 201 O PHE B 142 ? O PHE B 225 
# 
_pdbx_entry_details.entry_id                   9OZ0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              204 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              204 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              204 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                129.70 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            14.40 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 6   ? ? -112.28 78.46   
2  1 VAL A 127 ? ? -149.30 -31.48  
3  1 ALA A 141 ? ? -56.48  -78.08  
4  1 ARG A 170 ? ? -70.93  -158.21 
5  1 PRO A 179 ? ? -77.59  33.83   
6  1 PRO A 188 ? ? -61.42  -178.52 
7  1 ALA A 190 ? ? -93.54  39.35   
8  1 ALA A 224 ? ? -59.15  -74.84  
9  1 ARG B 86  ? ? 54.70   84.72   
10 1 LYS B 88  ? ? 36.69   76.81   
11 1 CYS B 93  ? ? 54.59   81.07   
12 1 ASN B 105 ? ? -84.46  32.10   
13 1 LYS B 107 ? ? -84.18  -137.76 
14 1 HIS B 109 ? ? -88.94  -153.94 
15 1 SER B 110 ? ? 66.46   133.69  
16 1 PRO B 128 ? ? -103.29 40.03   
17 1 ALA B 153 ? ? -98.09  -84.67  
18 1 TYR B 155 ? ? -143.58 -3.63   
19 1 LEU B 179 ? ? -96.23  -64.58  
20 1 MSE B 249 ? ? -101.44 60.57   
21 1 LYS B 250 ? ? -158.57 -48.92  
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.initial_of_center     CSBID 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A MSE 153 A MSE 153 ? MET 'modified residue' 
2 A MSE 210 A MSE 210 ? MET 'modified residue' 
3 A MSE 229 A MSE 229 ? MET 'modified residue' 
4 B MSE 17  B MSE 100 ? MET 'modified residue' 
5 B MSE 28  B MSE 111 ? MET 'modified residue' 
6 B MSE 134 B MSE 217 ? MET 'modified residue' 
7 B MSE 146 B MSE 229 ? MET 'modified residue' 
8 B MSE 166 B MSE 249 ? MET 'modified residue' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -3.9855  -7.1630  45.6572 1.2345 ? 0.1842  ? 0.3474  ? 0.7348 ? 0.0459  ? 1.0481 ? 3.3076 ? 
-1.4670 ? 0.2072  ? 6.3907 ? -0.8068 ? 4.7765 ? -0.3673 ? -0.3393 ? -0.1238 ? 1.3071  ? 1.2837  ? -0.4711 ? -0.8262 ? -0.0996 ? 
-0.6239 ? 
2  'X-RAY DIFFRACTION' ? refined 7.7358   -15.0550 46.9121 1.0693 ? 0.1424  ? -0.0288 ? 0.5162 ? 0.1410  ? 0.7533 ? 7.1961 ? 
-1.9705 ? 0.1596  ? 2.8479 ? 4.1705  ? 7.6497 ? -0.4502 ? -0.5871 ? 0.4897  ? 1.1012  ? 0.4344  ? -0.0812 ? -0.2706 ? 0.0754  ? 
-0.0071 ? 
3  'X-RAY DIFFRACTION' ? refined 12.1455  -10.0936 39.2240 0.8981 ? 0.0260  ? 0.0079  ? 0.6149 ? 0.0982  ? 0.8488 ? 3.4504 ? 
-1.9472 ? -0.0571 ? 3.7776 ? 3.1972  ? 3.1623 ? 0.1487  ? -0.2261 ? 0.4840  ? 0.2148  ? 0.1361  ? -1.2800 ? -0.1922 ? 0.4888  ? 
-0.1937 ? 
4  'X-RAY DIFFRACTION' ? refined -0.7523  -11.6927 40.3955 1.0720 ? 0.0887  ? 0.2085  ? 0.5241 ? 0.2038  ? 0.8623 ? 4.0136 ? 
0.6725  ? 0.4096  ? 3.0486 ? -0.8260 ? 1.9086 ? -0.0014 ? -0.1807 ? 0.5233  ? 0.7725  ? 0.0141  ? 0.6969  ? -0.7665 ? -0.7149 ? 
-0.0226 ? 
5  'X-RAY DIFFRACTION' ? refined -5.3139  -18.3597 51.1036 1.0923 ? 0.1955  ? 0.3912  ? 0.9172 ? 0.3053  ? 0.9117 ? 4.2947 ? 
0.7321  ? 2.0537  ? 4.6870 ? 3.7227  ? 8.6446 ? 0.0709  ? 0.0589  ? 0.0434  ? 0.4918  ? 0.7472  ? 0.4316  ? -0.7079 ? -0.6046 ? 
-0.6631 ? 
6  'X-RAY DIFFRACTION' ? refined -13.6942 -6.2377  47.1299 1.3370 ? 0.3028  ? 0.7656  ? 1.0327 ? 0.2486  ? 1.4470 ? 2.3480 ? 
-0.6556 ? -1.2615 ? 3.6281 ? 0.7205  ? 5.6547 ? 0.1802  ? -0.4510 ? 0.1075  ? 0.8753  ? 0.5188  ? 0.7577  ? -0.0088 ? -1.1456 ? 
-0.4776 ? 
7  'X-RAY DIFFRACTION' ? refined -16.6801 -10.9254 57.6269 1.9713 ? 0.3237  ? 0.7770  ? 1.2412 ? 0.2690  ? 1.3151 ? 3.4264 ? 
-1.2664 ? 0.3749  ? 3.6745 ? 2.9521  ? 5.9947 ? -0.3055 ? -1.4041 ? 0.4709  ? 1.6849  ? 0.3179  ? 1.6561  ? 0.4761  ? -1.8306 ? 
-0.0354 ? 
8  'X-RAY DIFFRACTION' ? refined -21.1592 -4.6630  50.5196 1.6250 ? 0.6050  ? 1.1948  ? 1.6086 ? 0.6430  ? 2.0794 ? 1.9840 ? 
0.8526  ? 0.1448  ? 1.1008 ? -1.9984 ? 4.9324 ? -0.7646 ? -0.0732 ? 0.2362  ? 1.5362  ? 0.8301  ? 1.6342  ? -0.7879 ? -0.9429 ? 
-0.3147 ? 
9  'X-RAY DIFFRACTION' ? refined -8.3279  19.3816  21.6772 0.8836 ? -0.0183 ? 0.0006  ? 0.7020 ? 0.0271  ? 0.7050 ? 8.4930 ? 
-3.5623 ? -3.7186 ? 5.1881 ? 4.1985  ? 4.3445 ? 0.2285  ? -0.0937 ? 1.3135  ? -0.1628 ? 0.1386  ? -0.2829 ? -0.2720 ? -0.3636 ? 
-0.6468 ? 
10 'X-RAY DIFFRACTION' ? refined 7.3589   -3.5743  12.7380 1.3502 ? -0.0098 ? 0.1066  ? 0.9858 ? 0.2811  ? 1.3781 ? 4.3763 ? 
4.1577  ? 5.4447  ? 5.1834 ? 6.3775  ? 7.9710 ? 0.5593  ? 1.2716  ? -1.0266 ? 2.4344  ? -1.0750 ? -0.1989 ? 1.4562  ? 3.0241  ? 
0.6171  ? 
11 'X-RAY DIFFRACTION' ? refined -3.8007  -1.3494  18.5475 0.5259 ? -0.0174 ? -0.0179 ? 0.4757 ? -0.0444 ? 0.5423 ? 3.7849 ? 
0.0378  ? -0.9816 ? 4.4086 ? -2.6172 ? 3.8069 ? -0.0260 ? 0.4505  ? -0.4710 ? -0.4854 ? -0.1074 ? -0.2960 ? 0.4070  ? -0.1669 ? 
0.0726  ? 
12 'X-RAY DIFFRACTION' ? refined -7.9548  -3.0775  26.6547 0.4047 ? -0.0276 ? 0.0885  ? 0.4324 ? -0.0056 ? 0.5963 ? 1.7859 ? 
-1.4387 ? -1.3432 ? 4.6970 ? -1.9347 ? 3.0306 ? -0.1681 ? -0.0668 ? -0.1283 ? 0.5326  ? 0.1093  ? 0.5989  ? -0.0467 ? -0.5526 ? 
0.0527  ? 
13 'X-RAY DIFFRACTION' ? refined -17.7380 -14.8066 13.1204 1.2567 ? -0.4483 ? -0.1139 ? 1.9507 ? -0.0812 ? 1.3834 ? 4.4695 ? 
2.7214  ? -3.5658 ? 3.1768 ? -0.9619 ? 3.8030 ? -0.5970 ? 2.1074  ? -0.7235 ? 0.9339  ? -0.4055 ? 1.7741  ? 0.7188  ? -3.8318 ? 
0.5127  ? 
14 'X-RAY DIFFRACTION' ? refined -32.8460 -15.4868 17.3425 1.9984 ? -0.0337 ? 0.9219  ? 2.6576 ? 0.0557  ? 1.8514 ? 0.1178 ? 
-0.1752 ? 0.1407  ? 0.3548 ? -0.1501 ? 0.1427 ? 0.5968  ? -5.1108 ? 0.6386  ? -0.4411 ? 0.1509  ? 1.3293  ? -0.0348 ? 1.2637  ? 
-1.2699 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 5 through 25 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 26 through 56 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 57 through 90 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 91 through 119 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 120 through 145 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 146 through 178 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 179 through 214 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 215 through 239 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 84 through 102 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 103 through 113 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 114 through 167 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 168 through 232 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 233 through 243 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 244 through 252 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MSE 1   ? A MSE 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ASP 3   ? A ASP 3   
4  1 Y 1 A ALA 4   ? A ALA 4   
5  1 Y 1 B CYS 253 ? B CYS 170 
6  1 Y 1 B GLU 254 ? B GLU 171 
7  1 Y 1 B GLU 255 ? B GLU 172 
8  1 Y 1 B ASN 256 ? B ASN 173 
9  1 Y 1 B PRO 257 ? B PRO 174 
10 1 Y 1 B GLY 258 ? B GLY 175 
11 1 Y 1 B TYR 259 ? B TYR 176 
12 1 Y 1 B CYS 260 ? B CYS 177 
13 1 Y 1 B ALA 261 ? B ALA 178 
# 
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  
CIT C1   C  N N 74  
CIT O1   O  N N 75  
CIT O2   O  N N 76  
CIT C2   C  N N 77  
CIT C3   C  N N 78  
CIT O7   O  N N 79  
CIT C4   C  N N 80  
CIT C5   C  N N 81  
CIT O3   O  N N 82  
CIT O4   O  N N 83  
CIT C6   C  N N 84  
CIT O5   O  N N 85  
CIT O6   O  N N 86  
CIT HO2  H  N N 87  
CIT H21  H  N N 88  
CIT H22  H  N N 89  
CIT HO7  H  N N 90  
CIT H41  H  N N 91  
CIT H42  H  N N 92  
CIT HO4  H  N N 93  
CIT HO6  H  N N 94  
CYS N    N  N N 95  
CYS CA   C  N R 96  
CYS C    C  N N 97  
CYS O    O  N N 98  
CYS CB   C  N N 99  
CYS SG   S  N N 100 
CYS OXT  O  N N 101 
CYS H    H  N N 102 
CYS H2   H  N N 103 
CYS HA   H  N N 104 
CYS HB2  H  N N 105 
CYS HB3  H  N N 106 
CYS HG   H  N N 107 
CYS HXT  H  N N 108 
GLN N    N  N N 109 
GLN CA   C  N S 110 
GLN C    C  N N 111 
GLN O    O  N N 112 
GLN CB   C  N N 113 
GLN CG   C  N N 114 
GLN CD   C  N N 115 
GLN OE1  O  N N 116 
GLN NE2  N  N N 117 
GLN OXT  O  N N 118 
GLN H    H  N N 119 
GLN H2   H  N N 120 
GLN HA   H  N N 121 
GLN HB2  H  N N 122 
GLN HB3  H  N N 123 
GLN HG2  H  N N 124 
GLN HG3  H  N N 125 
GLN HE21 H  N N 126 
GLN HE22 H  N N 127 
GLN HXT  H  N N 128 
GLU N    N  N N 129 
GLU CA   C  N S 130 
GLU C    C  N N 131 
GLU O    O  N N 132 
GLU CB   C  N N 133 
GLU CG   C  N N 134 
GLU CD   C  N N 135 
GLU OE1  O  N N 136 
GLU OE2  O  N N 137 
GLU OXT  O  N N 138 
GLU H    H  N N 139 
GLU H2   H  N N 140 
GLU HA   H  N N 141 
GLU HB2  H  N N 142 
GLU HB3  H  N N 143 
GLU HG2  H  N N 144 
GLU HG3  H  N N 145 
GLU HE2  H  N N 146 
GLU HXT  H  N N 147 
GLY N    N  N N 148 
GLY CA   C  N N 149 
GLY C    C  N N 150 
GLY O    O  N N 151 
GLY OXT  O  N N 152 
GLY H    H  N N 153 
GLY H2   H  N N 154 
GLY HA2  H  N N 155 
GLY HA3  H  N N 156 
GLY HXT  H  N N 157 
HIS N    N  N N 158 
HIS CA   C  N S 159 
HIS C    C  N N 160 
HIS O    O  N N 161 
HIS CB   C  N N 162 
HIS CG   C  Y N 163 
HIS ND1  N  Y N 164 
HIS CD2  C  Y N 165 
HIS CE1  C  Y N 166 
HIS NE2  N  Y N 167 
HIS OXT  O  N N 168 
HIS H    H  N N 169 
HIS H2   H  N N 170 
HIS HA   H  N N 171 
HIS HB2  H  N N 172 
HIS HB3  H  N N 173 
HIS HD1  H  N N 174 
HIS HD2  H  N N 175 
HIS HE1  H  N N 176 
HIS HE2  H  N N 177 
HIS HXT  H  N N 178 
HOH O    O  N N 179 
HOH H1   H  N N 180 
HOH H2   H  N N 181 
ILE N    N  N N 182 
ILE CA   C  N S 183 
ILE C    C  N N 184 
ILE O    O  N N 185 
ILE CB   C  N S 186 
ILE CG1  C  N N 187 
ILE CG2  C  N N 188 
ILE CD1  C  N N 189 
ILE OXT  O  N N 190 
ILE H    H  N N 191 
ILE H2   H  N N 192 
ILE HA   H  N N 193 
ILE HB   H  N N 194 
ILE HG12 H  N N 195 
ILE HG13 H  N N 196 
ILE HG21 H  N N 197 
ILE HG22 H  N N 198 
ILE HG23 H  N N 199 
ILE HD11 H  N N 200 
ILE HD12 H  N N 201 
ILE HD13 H  N N 202 
ILE HXT  H  N N 203 
LEU N    N  N N 204 
LEU CA   C  N S 205 
LEU C    C  N N 206 
LEU O    O  N N 207 
LEU CB   C  N N 208 
LEU CG   C  N N 209 
LEU CD1  C  N N 210 
LEU CD2  C  N N 211 
LEU OXT  O  N N 212 
LEU H    H  N N 213 
LEU H2   H  N N 214 
LEU HA   H  N N 215 
LEU HB2  H  N N 216 
LEU HB3  H  N N 217 
LEU HG   H  N N 218 
LEU HD11 H  N N 219 
LEU HD12 H  N N 220 
LEU HD13 H  N N 221 
LEU HD21 H  N N 222 
LEU HD22 H  N N 223 
LEU HD23 H  N N 224 
LEU HXT  H  N N 225 
LYS N    N  N N 226 
LYS CA   C  N S 227 
LYS C    C  N N 228 
LYS O    O  N N 229 
LYS CB   C  N N 230 
LYS CG   C  N N 231 
LYS CD   C  N N 232 
LYS CE   C  N N 233 
LYS NZ   N  N N 234 
LYS OXT  O  N N 235 
LYS H    H  N N 236 
LYS H2   H  N N 237 
LYS HA   H  N N 238 
LYS HB2  H  N N 239 
LYS HB3  H  N N 240 
LYS HG2  H  N N 241 
LYS HG3  H  N N 242 
LYS HD2  H  N N 243 
LYS HD3  H  N N 244 
LYS HE2  H  N N 245 
LYS HE3  H  N N 246 
LYS HZ1  H  N N 247 
LYS HZ2  H  N N 248 
LYS HZ3  H  N N 249 
LYS HXT  H  N N 250 
MG  MG   MG N N 251 
MSE N    N  N N 252 
MSE CA   C  N S 253 
MSE C    C  N N 254 
MSE O    O  N N 255 
MSE OXT  O  N N 256 
MSE CB   C  N N 257 
MSE CG   C  N N 258 
MSE SE   SE N N 259 
MSE CE   C  N N 260 
MSE H    H  N N 261 
MSE H2   H  N N 262 
MSE HA   H  N N 263 
MSE HXT  H  N N 264 
MSE HB2  H  N N 265 
MSE HB3  H  N N 266 
MSE HG2  H  N N 267 
MSE HG3  H  N N 268 
MSE HE1  H  N N 269 
MSE HE2  H  N N 270 
MSE HE3  H  N N 271 
PHE N    N  N N 272 
PHE CA   C  N S 273 
PHE C    C  N N 274 
PHE O    O  N N 275 
PHE CB   C  N N 276 
PHE CG   C  Y N 277 
PHE CD1  C  Y N 278 
PHE CD2  C  Y N 279 
PHE CE1  C  Y N 280 
PHE CE2  C  Y N 281 
PHE CZ   C  Y N 282 
PHE OXT  O  N N 283 
PHE H    H  N N 284 
PHE H2   H  N N 285 
PHE HA   H  N N 286 
PHE HB2  H  N N 287 
PHE HB3  H  N N 288 
PHE HD1  H  N N 289 
PHE HD2  H  N N 290 
PHE HE1  H  N N 291 
PHE HE2  H  N N 292 
PHE HZ   H  N N 293 
PHE HXT  H  N N 294 
PRO N    N  N N 295 
PRO CA   C  N S 296 
PRO C    C  N N 297 
PRO O    O  N N 298 
PRO CB   C  N N 299 
PRO CG   C  N N 300 
PRO CD   C  N N 301 
PRO OXT  O  N N 302 
PRO H    H  N N 303 
PRO HA   H  N N 304 
PRO HB2  H  N N 305 
PRO HB3  H  N N 306 
PRO HG2  H  N N 307 
PRO HG3  H  N N 308 
PRO HD2  H  N N 309 
PRO HD3  H  N N 310 
PRO HXT  H  N N 311 
SER N    N  N N 312 
SER CA   C  N S 313 
SER C    C  N N 314 
SER O    O  N N 315 
SER CB   C  N N 316 
SER OG   O  N N 317 
SER OXT  O  N N 318 
SER H    H  N N 319 
SER H2   H  N N 320 
SER HA   H  N N 321 
SER HB2  H  N N 322 
SER HB3  H  N N 323 
SER HG   H  N N 324 
SER HXT  H  N N 325 
THR N    N  N N 326 
THR CA   C  N S 327 
THR C    C  N N 328 
THR O    O  N N 329 
THR CB   C  N R 330 
THR OG1  O  N N 331 
THR CG2  C  N N 332 
THR OXT  O  N N 333 
THR H    H  N N 334 
THR H2   H  N N 335 
THR HA   H  N N 336 
THR HB   H  N N 337 
THR HG1  H  N N 338 
THR HG21 H  N N 339 
THR HG22 H  N N 340 
THR HG23 H  N N 341 
THR HXT  H  N N 342 
TRP N    N  N N 343 
TRP CA   C  N S 344 
TRP C    C  N N 345 
TRP O    O  N N 346 
TRP CB   C  N N 347 
TRP CG   C  Y N 348 
TRP CD1  C  Y N 349 
TRP CD2  C  Y N 350 
TRP NE1  N  Y N 351 
TRP CE2  C  Y N 352 
TRP CE3  C  Y N 353 
TRP CZ2  C  Y N 354 
TRP CZ3  C  Y N 355 
TRP CH2  C  Y N 356 
TRP OXT  O  N N 357 
TRP H    H  N N 358 
TRP H2   H  N N 359 
TRP HA   H  N N 360 
TRP HB2  H  N N 361 
TRP HB3  H  N N 362 
TRP HD1  H  N N 363 
TRP HE1  H  N N 364 
TRP HE3  H  N N 365 
TRP HZ2  H  N N 366 
TRP HZ3  H  N N 367 
TRP HH2  H  N N 368 
TRP HXT  H  N N 369 
TYR N    N  N N 370 
TYR CA   C  N S 371 
TYR C    C  N N 372 
TYR O    O  N N 373 
TYR CB   C  N N 374 
TYR CG   C  Y N 375 
TYR CD1  C  Y N 376 
TYR CD2  C  Y N 377 
TYR CE1  C  Y N 378 
TYR CE2  C  Y N 379 
TYR CZ   C  Y N 380 
TYR OH   O  N N 381 
TYR OXT  O  N N 382 
TYR H    H  N N 383 
TYR H2   H  N N 384 
TYR HA   H  N N 385 
TYR HB2  H  N N 386 
TYR HB3  H  N N 387 
TYR HD1  H  N N 388 
TYR HD2  H  N N 389 
TYR HE1  H  N N 390 
TYR HE2  H  N N 391 
TYR HH   H  N N 392 
TYR HXT  H  N N 393 
VAL N    N  N N 394 
VAL CA   C  N S 395 
VAL C    C  N N 396 
VAL O    O  N N 397 
VAL CB   C  N N 398 
VAL CG1  C  N N 399 
VAL CG2  C  N N 400 
VAL OXT  O  N N 401 
VAL H    H  N N 402 
VAL H2   H  N N 403 
VAL HA   H  N N 404 
VAL HB   H  N N 405 
VAL HG11 H  N N 406 
VAL HG12 H  N N 407 
VAL HG13 H  N N 408 
VAL HG21 H  N N 409 
VAL HG22 H  N N 410 
VAL HG23 H  N N 411 
VAL HXT  H  N N 412 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MSE N   CA   sing N N 238 
MSE N   H    sing N N 239 
MSE N   H2   sing N N 240 
MSE CA  C    sing N N 241 
MSE CA  CB   sing N N 242 
MSE CA  HA   sing N N 243 
MSE C   O    doub N N 244 
MSE C   OXT  sing N N 245 
MSE OXT HXT  sing N N 246 
MSE CB  CG   sing N N 247 
MSE CB  HB2  sing N N 248 
MSE CB  HB3  sing N N 249 
MSE CG  SE   sing N N 250 
MSE CG  HG2  sing N N 251 
MSE CG  HG3  sing N N 252 
MSE SE  CE   sing N N 253 
MSE CE  HE1  sing N N 254 
MSE CE  HE2  sing N N 255 
MSE CE  HE3  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 
HHSN272200700058C 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00035 2 
# 
_atom_sites.entry_id                    9OZ0 
_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]   0.005976 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005976 
_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]   0.005976 
_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  
MG 
N  
O  
S  
SE 
# 
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   . LYS A 1 5   ? -11.853 -29.663 34.251 1.00 156.58 ? 5   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 5   ? -12.584 -29.444 35.493 1.00 153.14 ? 5   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 5   ? -13.428 -28.175 35.420 1.00 147.85 ? 5   LYS A C   1 
ATOM   4    O  O   . LYS A 1 5   ? -13.220 -27.328 34.550 1.00 143.04 ? 5   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 5   ? -11.619 -29.367 36.677 1.00 150.39 ? 5   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 5   ? -11.138 -30.720 37.173 1.00 149.48 ? 5   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 5   ? -12.292 -31.558 37.699 1.00 150.96 ? 5   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 5   ? -12.999 -30.867 38.854 1.00 148.82 ? 5   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 5   ? -14.186 -31.639 39.318 1.00 151.66 ? 5   LYS A NZ  1 
ATOM   10   N  N   . ALA A 1 6   ? -14.380 -28.049 36.342 1.00 141.81 ? 6   ALA A N   1 
ATOM   11   C  CA  . ALA A 1 6   ? -15.310 -26.923 36.376 1.00 131.30 ? 6   ALA A CA  1 
ATOM   12   C  C   . ALA A 1 6   ? -15.013 -26.082 37.616 1.00 125.19 ? 6   ALA A C   1 
ATOM   13   O  O   . ALA A 1 6   ? -15.708 -26.161 38.630 1.00 122.14 ? 6   ALA A O   1 
ATOM   14   C  CB  . ALA A 1 6   ? -16.757 -27.417 36.359 1.00 126.46 ? 6   ALA A CB  1 
ATOM   15   N  N   . PHE A 1 7   ? -13.964 -25.268 37.525 1.00 119.62 ? 7   PHE A N   1 
ATOM   16   C  CA  . PHE A 1 7   ? -13.636 -24.300 38.559 1.00 116.14 ? 7   PHE A CA  1 
ATOM   17   C  C   . PHE A 1 7   ? -14.176 -22.929 38.159 1.00 110.47 ? 7   PHE A C   1 
ATOM   18   O  O   . PHE A 1 7   ? -14.716 -22.737 37.067 1.00 106.34 ? 7   PHE A O   1 
ATOM   19   C  CB  . PHE A 1 7   ? -12.123 -24.263 38.812 1.00 115.78 ? 7   PHE A CB  1 
ATOM   20   C  CG  . PHE A 1 7   ? -11.366 -23.319 37.913 1.00 110.31 ? 7   PHE A CG  1 
ATOM   21   C  CD1 . PHE A 1 7   ? -10.507 -22.372 38.452 1.00 108.58 ? 7   PHE A CD1 1 
ATOM   22   C  CD2 . PHE A 1 7   ? -11.492 -23.389 36.536 1.00 108.59 ? 7   PHE A CD2 1 
ATOM   23   C  CE1 . PHE A 1 7   ? -9.802  -21.503 37.635 1.00 98.25  ? 7   PHE A CE1 1 
ATOM   24   C  CE2 . PHE A 1 7   ? -10.797 -22.521 35.720 1.00 105.20 ? 7   PHE A CE2 1 
ATOM   25   C  CZ  . PHE A 1 7   ? -9.947  -21.579 36.269 1.00 96.57  ? 7   PHE A CZ  1 
ATOM   26   N  N   . ARG A 1 8   ? -14.022 -21.962 39.056 1.00 109.93 ? 8   ARG A N   1 
ATOM   27   C  CA  . ARG A 1 8   ? -14.514 -20.611 38.837 1.00 112.15 ? 8   ARG A CA  1 
ATOM   28   C  C   . ARG A 1 8   ? -13.393 -19.613 39.079 1.00 105.59 ? 8   ARG A C   1 
ATOM   29   O  O   . ARG A 1 8   ? -12.562 -19.805 39.972 1.00 111.15 ? 8   ARG A O   1 
ATOM   30   C  CB  . ARG A 1 8   ? -15.708 -20.302 39.752 1.00 126.57 ? 8   ARG A CB  1 
ATOM   31   C  CG  . ARG A 1 8   ? -15.653 -21.010 41.095 1.00 142.15 ? 8   ARG A CG  1 
ATOM   32   C  CD  . ARG A 1 8   ? -16.727 -20.501 42.039 1.00 155.58 ? 8   ARG A CD  1 
ATOM   33   N  NE  . ARG A 1 8   ? -17.927 -20.071 41.333 1.00 166.21 ? 8   ARG A NE  1 
ATOM   34   C  CZ  . ARG A 1 8   ? -18.960 -20.865 41.075 1.00 176.20 ? 8   ARG A CZ  1 
ATOM   35   N  NH1 . ARG A 1 8   ? -18.936 -22.134 41.462 1.00 181.56 ? 8   ARG A NH1 1 
ATOM   36   N  NH2 . ARG A 1 8   ? -20.015 -20.390 40.428 1.00 184.86 ? 8   ARG A NH2 1 
ATOM   37   N  N   . ARG A 1 9   ? -13.368 -18.555 38.274 1.00 94.21  ? 9   ARG A N   1 
ATOM   38   C  CA  . ARG A 1 9   ? -12.369 -17.511 38.451 1.00 88.88  ? 9   ARG A CA  1 
ATOM   39   C  C   . ARG A 1 9   ? -12.628 -16.754 39.746 1.00 89.88  ? 9   ARG A C   1 
ATOM   40   O  O   . ARG A 1 9   ? -13.778 -16.515 40.125 1.00 90.57  ? 9   ARG A O   1 
ATOM   41   C  CB  . ARG A 1 9   ? -12.387 -16.547 37.268 1.00 77.94  ? 9   ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 9   ? -12.197 -17.207 35.918 1.00 82.41  ? 9   ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 9   ? -12.161 -16.163 34.817 1.00 82.49  ? 9   ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 9   ? -11.119 -15.169 35.051 1.00 83.60  ? 9   ARG A NE  1 
ATOM   45   C  CZ  . ARG A 1 9   ? -10.989 -14.046 34.354 1.00 83.19  ? 9   ARG A CZ  1 
ATOM   46   N  NH1 . ARG A 1 9   ? -11.839 -13.772 33.375 1.00 87.78  ? 9   ARG A NH1 1 
ATOM   47   N  NH2 . ARG A 1 9   ? -10.009 -13.199 34.635 1.00 82.85  ? 9   ARG A NH2 1 
ATOM   48   N  N   . TYR A 1 10  ? -11.549 -16.376 40.426 1.00 89.90  ? 10  TYR A N   1 
ATOM   49   C  CA  . TYR A 1 10  ? -11.646 -15.693 41.706 1.00 96.06  ? 10  TYR A CA  1 
ATOM   50   C  C   . TYR A 1 10  ? -10.629 -14.561 41.759 1.00 96.64  ? 10  TYR A C   1 
ATOM   51   O  O   . TYR A 1 10  ? -9.565  -14.633 41.139 1.00 99.16  ? 10  TYR A O   1 
ATOM   52   C  CB  . TYR A 1 10  ? -11.425 -16.669 42.871 1.00 102.31 ? 10  TYR A CB  1 
ATOM   53   C  CG  . TYR A 1 10  ? -12.696 -17.086 43.581 1.00 106.88 ? 10  TYR A CG  1 
ATOM   54   C  CD1 . TYR A 1 10  ? -13.440 -18.173 43.151 1.00 106.32 ? 10  TYR A CD1 1 
ATOM   55   C  CD2 . TYR A 1 10  ? -13.151 -16.386 44.681 1.00 108.02 ? 10  TYR A CD2 1 
ATOM   56   C  CE1 . TYR A 1 10  ? -14.602 -18.545 43.810 1.00 108.30 ? 10  TYR A CE1 1 
ATOM   57   C  CE2 . TYR A 1 10  ? -14.302 -16.751 45.348 1.00 108.21 ? 10  TYR A CE2 1 
ATOM   58   C  CZ  . TYR A 1 10  ? -15.026 -17.830 44.909 1.00 109.92 ? 10  TYR A CZ  1 
ATOM   59   O  OH  . TYR A 1 10  ? -16.178 -18.189 45.570 1.00 115.10 ? 10  TYR A OH  1 
ATOM   60   N  N   . ILE A 1 11  ? -10.968 -13.514 42.509 1.00 99.29  ? 11  ILE A N   1 
ATOM   61   C  CA  . ILE A 1 11  ? -10.127 -12.330 42.656 1.00 97.45  ? 11  ILE A CA  1 
ATOM   62   C  C   . ILE A 1 11  ? -9.536  -12.314 44.058 1.00 99.13  ? 11  ILE A C   1 
ATOM   63   O  O   . ILE A 1 11  ? -10.233 -12.578 45.045 1.00 100.59 ? 11  ILE A O   1 
ATOM   64   C  CB  . ILE A 1 11  ? -10.906 -11.026 42.380 1.00 93.51  ? 11  ILE A CB  1 
ATOM   65   C  CG1 . ILE A 1 11  ? -10.999 -10.748 40.880 1.00 91.37  ? 11  ILE A CG1 1 
ATOM   66   C  CG2 . ILE A 1 11  ? -10.234 -9.835  43.062 1.00 84.89  ? 11  ILE A CG2 1 
ATOM   67   C  CD1 . ILE A 1 11  ? -11.898 -11.632 40.141 1.00 94.58  ? 11  ILE A CD1 1 
ATOM   68   N  N   . PHE A 1 12  ? -8.244  -12.003 44.141 1.00 99.69  ? 12  PHE A N   1 
ATOM   69   C  CA  . PHE A 1 12  ? -7.560  -11.843 45.422 1.00 105.68 ? 12  PHE A CA  1 
ATOM   70   C  C   . PHE A 1 12  ? -6.599  -10.665 45.275 1.00 109.42 ? 12  PHE A C   1 
ATOM   71   O  O   . PHE A 1 12  ? -5.422  -10.853 44.958 1.00 109.80 ? 12  PHE A O   1 
ATOM   72   C  CB  . PHE A 1 12  ? -6.840  -13.123 45.817 1.00 105.64 ? 12  PHE A CB  1 
ATOM   73   C  CG  . PHE A 1 12  ? -6.195  -13.065 47.166 1.00 109.48 ? 12  PHE A CG  1 
ATOM   74   C  CD1 . PHE A 1 12  ? -6.618  -12.156 48.119 1.00 114.06 ? 12  PHE A CD1 1 
ATOM   75   C  CD2 . PHE A 1 12  ? -5.147  -13.908 47.474 1.00 113.04 ? 12  PHE A CD2 1 
ATOM   76   C  CE1 . PHE A 1 12  ? -6.016  -12.106 49.357 1.00 117.89 ? 12  PHE A CE1 1 
ATOM   77   C  CE2 . PHE A 1 12  ? -4.539  -13.857 48.710 1.00 117.38 ? 12  PHE A CE2 1 
ATOM   78   C  CZ  . PHE A 1 12  ? -4.975  -12.953 49.653 1.00 118.39 ? 12  PHE A CZ  1 
ATOM   79   N  N   . GLU A 1 13  ? -7.108  -9.455  45.498 1.00 108.77 ? 13  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 13  ? -6.291  -8.252  45.504 1.00 108.90 ? 13  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 13  ? -6.332  -7.609  46.879 1.00 113.46 ? 13  GLU A C   1 
ATOM   82   O  O   . GLU A 1 13  ? -7.367  -7.625  47.552 1.00 119.65 ? 13  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 13  ? -6.760  -7.222  44.481 1.00 111.59 ? 13  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 13  ? -7.367  -7.769  43.224 1.00 116.04 ? 13  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 13  ? -8.368  -6.803  42.630 1.00 121.14 ? 13  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 13  ? -8.473  -6.748  41.391 1.00 122.43 ? 13  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 13  ? -9.047  -6.093  43.401 1.00 118.72 ? 13  GLU A OE2 1 
ATOM   88   N  N   . LEU A 1 14  ? -5.208  -7.024  47.279 1.00 111.27 ? 14  LEU A N   1 
ATOM   89   C  CA  . LEU A 1 14  ? -5.137  -6.223  48.491 1.00 112.62 ? 14  LEU A CA  1 
ATOM   90   C  C   . LEU A 1 14  ? -4.523  -4.879  48.143 1.00 115.16 ? 14  LEU A C   1 
ATOM   91   O  O   . LEU A 1 14  ? -3.448  -4.822  47.540 1.00 125.61 ? 14  LEU A O   1 
ATOM   92   C  CB  . LEU A 1 14  ? -4.326  -6.918  49.588 1.00 113.47 ? 14  LEU A CB  1 
ATOM   93   C  CG  . LEU A 1 14  ? -5.289  -7.547  50.598 1.00 114.12 ? 14  LEU A CG  1 
ATOM   94   C  CD1 . LEU A 1 14  ? -5.888  -8.823  50.034 1.00 111.16 ? 14  LEU A CD1 1 
ATOM   95   C  CD2 . LEU A 1 14  ? -4.675  -7.793  51.978 1.00 115.18 ? 14  LEU A CD2 1 
ATOM   96   N  N   . TYR A 1 15  ? -5.210  -3.804  48.514 1.00 114.76 ? 15  TYR A N   1 
ATOM   97   C  CA  . TYR A 1 15  ? -4.749  -2.457  48.222 1.00 110.92 ? 15  TYR A CA  1 
ATOM   98   C  C   . TYR A 1 15  ? -3.985  -1.898  49.412 1.00 113.85 ? 15  TYR A C   1 
ATOM   99   O  O   . TYR A 1 15  ? -4.348  -2.137  50.568 1.00 116.48 ? 15  TYR A O   1 
ATOM   100  C  CB  . TYR A 1 15  ? -5.929  -1.547  47.878 1.00 108.50 ? 15  TYR A CB  1 
ATOM   101  C  CG  . TYR A 1 15  ? -6.675  -1.965  46.632 1.00 104.37 ? 15  TYR A CG  1 
ATOM   102  C  CD1 . TYR A 1 15  ? -7.718  -2.879  46.696 1.00 101.30 ? 15  TYR A CD1 1 
ATOM   103  C  CD2 . TYR A 1 15  ? -6.335  -1.445  45.390 1.00 106.38 ? 15  TYR A CD2 1 
ATOM   104  C  CE1 . TYR A 1 15  ? -8.401  -3.264  45.559 1.00 103.04 ? 15  TYR A CE1 1 
ATOM   105  C  CE2 . TYR A 1 15  ? -7.013  -1.823  44.246 1.00 107.52 ? 15  TYR A CE2 1 
ATOM   106  C  CZ  . TYR A 1 15  ? -8.045  -2.733  44.336 1.00 108.38 ? 15  TYR A CZ  1 
ATOM   107  O  OH  . TYR A 1 15  ? -8.724  -3.113  43.202 1.00 110.20 ? 15  TYR A OH  1 
ATOM   108  N  N   . PHE A 1 16  ? -2.919  -1.160  49.122 1.00 112.67 ? 16  PHE A N   1 
ATOM   109  C  CA  . PHE A 1 16  ? -2.097  -0.537  50.144 1.00 113.84 ? 16  PHE A CA  1 
ATOM   110  C  C   . PHE A 1 16  ? -2.050  0.969   49.919 1.00 112.41 ? 16  PHE A C   1 
ATOM   111  O  O   . PHE A 1 16  ? -2.344  1.465   48.827 1.00 108.02 ? 16  PHE A O   1 
ATOM   112  C  CB  . PHE A 1 16  ? -0.670  -1.113  50.157 1.00 115.55 ? 16  PHE A CB  1 
ATOM   113  C  CG  . PHE A 1 16  ? -0.599  -2.596  49.890 1.00 116.44 ? 16  PHE A CG  1 
ATOM   114  C  CD1 . PHE A 1 16  ? -0.586  -3.086  48.593 1.00 114.30 ? 16  PHE A CD1 1 
ATOM   115  C  CD2 . PHE A 1 16  ? -0.542  -3.499  50.941 1.00 116.34 ? 16  PHE A CD2 1 
ATOM   116  C  CE1 . PHE A 1 16  ? -0.513  -4.446  48.349 1.00 114.80 ? 16  PHE A CE1 1 
ATOM   117  C  CE2 . PHE A 1 16  ? -0.473  -4.859  50.705 1.00 114.86 ? 16  PHE A CE2 1 
ATOM   118  C  CZ  . PHE A 1 16  ? -0.459  -5.334  49.407 1.00 115.55 ? 16  PHE A CZ  1 
ATOM   119  N  N   . ASP A 1 17  ? -1.679  1.691   50.976 1.00 114.75 ? 17  ASP A N   1 
ATOM   120  C  CA  . ASP A 1 17  ? -1.583  3.145   50.954 1.00 118.86 ? 17  ASP A CA  1 
ATOM   121  C  C   . ASP A 1 17  ? -0.579  3.580   49.895 1.00 121.45 ? 17  ASP A C   1 
ATOM   122  O  O   . ASP A 1 17  ? 0.628   3.365   50.060 1.00 127.71 ? 17  ASP A O   1 
ATOM   123  C  CB  . ASP A 1 17  ? -1.179  3.675   52.332 1.00 126.34 ? 17  ASP A CB  1 
ATOM   124  C  CG  . ASP A 1 17  ? -1.309  5.182   52.442 1.00 130.64 ? 17  ASP A CG  1 
ATOM   125  O  OD1 . ASP A 1 17  ? -0.630  5.901   51.681 1.00 132.33 ? 17  ASP A OD1 1 
ATOM   126  O  OD2 . ASP A 1 17  ? -2.091  5.650   53.296 1.00 134.62 ? 17  ASP A OD2 1 
ATOM   127  N  N   . PRO A 1 18  ? -1.033  4.202   48.805 1.00 117.81 ? 18  PRO A N   1 
ATOM   128  C  CA  . PRO A 1 18  ? -0.091  4.563   47.736 1.00 116.37 ? 18  PRO A CA  1 
ATOM   129  C  C   . PRO A 1 18  ? 0.873   5.666   48.130 1.00 122.19 ? 18  PRO A C   1 
ATOM   130  O  O   . PRO A 1 18  ? 1.963   5.751   47.551 1.00 122.30 ? 18  PRO A O   1 
ATOM   131  C  CB  . PRO A 1 18  ? -1.015  5.001   46.592 1.00 110.94 ? 18  PRO A CB  1 
ATOM   132  C  CG  . PRO A 1 18  ? -2.240  5.499   47.283 1.00 112.20 ? 18  PRO A CG  1 
ATOM   133  C  CD  . PRO A 1 18  ? -2.409  4.633   48.503 1.00 114.58 ? 18  PRO A CD  1 
ATOM   134  N  N   . ALA A 1 19  ? 0.512   6.508   49.100 1.00 128.31 ? 19  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 19  ? 1.363   7.640   49.452 1.00 139.34 ? 19  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 19  ? 2.688   7.175   50.044 1.00 145.59 ? 19  ALA A C   1 
ATOM   137  O  O   . ALA A 1 19  ? 3.759   7.619   49.615 1.00 150.76 ? 19  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 19  ? 0.632   8.567   50.424 1.00 141.46 ? 19  ALA A CB  1 
ATOM   139  N  N   . ARG A 1 20  ? 2.639   6.277   51.026 1.00 145.04 ? 20  ARG A N   1 
ATOM   140  C  CA  . ARG A 1 20  ? 3.840   5.844   51.726 1.00 146.80 ? 20  ARG A CA  1 
ATOM   141  C  C   . ARG A 1 20  ? 4.315   4.457   51.310 1.00 140.74 ? 20  ARG A C   1 
ATOM   142  O  O   . ARG A 1 20  ? 5.299   3.964   51.870 1.00 144.84 ? 20  ARG A O   1 
ATOM   143  C  CB  . ARG A 1 20  ? 3.617   5.887   53.242 1.00 155.55 ? 20  ARG A CB  1 
ATOM   144  C  CG  . ARG A 1 20  ? 2.420   5.097   53.740 1.00 153.92 ? 20  ARG A CG  1 
ATOM   145  C  CD  . ARG A 1 20  ? 2.459   4.976   55.258 1.00 159.80 ? 20  ARG A CD  1 
ATOM   146  N  NE  . ARG A 1 20  ? 1.408   4.105   55.777 1.00 159.11 ? 20  ARG A NE  1 
ATOM   147  C  CZ  . ARG A 1 20  ? 1.511   3.400   56.899 1.00 160.20 ? 20  ARG A CZ  1 
ATOM   148  N  NH1 . ARG A 1 20  ? 2.622   3.457   57.621 1.00 165.18 ? 20  ARG A NH1 1 
ATOM   149  N  NH2 . ARG A 1 20  ? 0.506   2.633   57.299 1.00 155.63 ? 20  ARG A NH2 1 
ATOM   150  N  N   . LEU A 1 21  ? 3.647   3.814   50.350 1.00 131.84 ? 21  LEU A N   1 
ATOM   151  C  CA  . LEU A 1 21  ? 4.204   2.592   49.780 1.00 123.94 ? 21  LEU A CA  1 
ATOM   152  C  C   . LEU A 1 21  ? 5.365   2.906   48.847 1.00 121.32 ? 21  LEU A C   1 
ATOM   153  O  O   . LEU A 1 21  ? 6.275   2.084   48.690 1.00 121.22 ? 21  LEU A O   1 
ATOM   154  C  CB  . LEU A 1 21  ? 3.121   1.803   49.042 1.00 105.18 ? 21  LEU A CB  1 
ATOM   155  C  CG  . LEU A 1 21  ? 3.356   0.299   48.863 1.00 107.33 ? 21  LEU A CG  1 
ATOM   156  C  CD1 . LEU A 1 21  ? 3.423   -0.401  50.211 1.00 107.09 ? 21  LEU A CD1 1 
ATOM   157  C  CD2 . LEU A 1 21  ? 2.270   -0.322  47.997 1.00 97.63  ? 21  LEU A CD2 1 
ATOM   158  N  N   . LEU A 1 22  ? 5.353   4.088   48.225 1.00 121.69 ? 22  LEU A N   1 
ATOM   159  C  CA  . LEU A 1 22  ? 6.473   4.515   47.395 1.00 128.30 ? 22  LEU A CA  1 
ATOM   160  C  C   . LEU A 1 22  ? 7.707   4.848   48.219 1.00 137.93 ? 22  LEU A C   1 
ATOM   161  O  O   . LEU A 1 22  ? 8.822   4.798   47.689 1.00 149.38 ? 22  LEU A O   1 
ATOM   162  C  CB  . LEU A 1 22  ? 6.077   5.731   46.557 1.00 128.85 ? 22  LEU A CB  1 
ATOM   163  C  CG  . LEU A 1 22  ? 5.507   5.463   45.164 1.00 125.48 ? 22  LEU A CG  1 
ATOM   164  C  CD1 . LEU A 1 22  ? 4.058   5.028   45.262 1.00 122.04 ? 22  LEU A CD1 1 
ATOM   165  C  CD2 . LEU A 1 22  ? 5.644   6.698   44.287 1.00 124.63 ? 22  LEU A CD2 1 
ATOM   166  N  N   . GLU A 1 23  ? 7.533   5.186   49.499 1.00 137.77 ? 23  GLU A N   1 
ATOM   167  C  CA  . GLU A 1 23  ? 8.669   5.550   50.338 1.00 144.33 ? 23  GLU A CA  1 
ATOM   168  C  C   . GLU A 1 23  ? 9.638   4.392   50.530 1.00 141.87 ? 23  GLU A C   1 
ATOM   169  O  O   . GLU A 1 23  ? 10.820  4.626   50.804 1.00 147.91 ? 23  GLU A O   1 
ATOM   170  C  CB  . GLU A 1 23  ? 8.175   6.064   51.691 1.00 151.52 ? 23  GLU A CB  1 
ATOM   171  C  CG  . GLU A 1 23  ? 7.240   7.259   51.580 1.00 153.75 ? 23  GLU A CG  1 
ATOM   172  C  CD  . GLU A 1 23  ? 6.929   7.888   52.923 1.00 160.35 ? 23  GLU A CD  1 
ATOM   173  O  OE1 . GLU A 1 23  ? 7.773   7.786   53.839 1.00 165.64 ? 23  GLU A OE1 1 
ATOM   174  O  OE2 . GLU A 1 23  ? 5.842   8.488   53.061 1.00 160.47 ? 23  GLU A OE2 1 
ATOM   175  N  N   . LEU A 1 24  ? 9.172   3.156   50.386 1.00 141.14 ? 24  LEU A N   1 
ATOM   176  C  CA  . LEU A 1 24  ? 10.060  2.007   50.470 1.00 125.70 ? 24  LEU A CA  1 
ATOM   177  C  C   . LEU A 1 24  ? 10.956  1.950   49.239 1.00 132.81 ? 24  LEU A C   1 
ATOM   178  O  O   . LEU A 1 24  ? 10.475  2.044   48.106 1.00 131.90 ? 24  LEU A O   1 
ATOM   179  C  CB  . LEU A 1 24  ? 9.245   0.721   50.592 1.00 120.82 ? 24  LEU A CB  1 
ATOM   180  C  CG  . LEU A 1 24  ? 8.138   0.716   51.647 1.00 120.29 ? 24  LEU A CG  1 
ATOM   181  C  CD1 . LEU A 1 24  ? 6.975   -0.142  51.185 1.00 114.48 ? 24  LEU A CD1 1 
ATOM   182  C  CD2 . LEU A 1 24  ? 8.668   0.227   52.984 1.00 124.23 ? 24  LEU A CD2 1 
ATOM   183  N  N   . ASP A 1 25  ? 12.261  1.802   49.458 1.00 133.22 ? 25  ASP A N   1 
ATOM   184  C  CA  . ASP A 1 25  ? 13.180  1.651   48.342 1.00 135.89 ? 25  ASP A CA  1 
ATOM   185  C  C   . ASP A 1 25  ? 13.143  0.212   47.832 1.00 133.87 ? 25  ASP A C   1 
ATOM   186  O  O   . ASP A 1 25  ? 12.366  -0.624  48.302 1.00 123.31 ? 25  ASP A O   1 
ATOM   187  C  CB  . ASP A 1 25  ? 14.593  2.085   48.741 1.00 142.53 ? 25  ASP A CB  1 
ATOM   188  C  CG  . ASP A 1 25  ? 15.143  1.320   49.939 1.00 143.43 ? 25  ASP A CG  1 
ATOM   189  O  OD1 . ASP A 1 25  ? 14.701  0.183   50.202 1.00 139.25 ? 25  ASP A OD1 1 
ATOM   190  O  OD2 . ASP A 1 25  ? 16.034  1.866   50.623 1.00 148.36 ? 25  ASP A OD2 1 
ATOM   191  N  N   . ASP A 1 26  ? 14.002  -0.088  46.856 1.00 119.53 ? 26  ASP A N   1 
ATOM   192  C  CA  . ASP A 1 26  ? 14.020  -1.428  46.283 1.00 117.20 ? 26  ASP A CA  1 
ATOM   193  C  C   . ASP A 1 26  ? 14.552  -2.472  47.258 1.00 124.16 ? 26  ASP A C   1 
ATOM   194  O  O   . ASP A 1 26  ? 14.327  -3.668  47.046 1.00 132.45 ? 26  ASP A O   1 
ATOM   195  C  CB  . ASP A 1 26  ? 14.842  -1.442  44.992 1.00 118.51 ? 26  ASP A CB  1 
ATOM   196  C  CG  . ASP A 1 26  ? 16.093  -0.600  45.086 1.00 134.84 ? 26  ASP A CG  1 
ATOM   197  O  OD1 . ASP A 1 26  ? 16.391  -0.092  46.187 1.00 146.34 ? 26  ASP A OD1 1 
ATOM   198  O  OD2 . ASP A 1 26  ? 16.779  -0.446  44.053 1.00 141.52 ? 26  ASP A OD2 1 
ATOM   199  N  N   . ASP A 1 27  ? 15.241  -2.053  48.322 1.00 125.48 ? 27  ASP A N   1 
ATOM   200  C  CA  . ASP A 1 27  ? 15.742  -3.010  49.305 1.00 119.23 ? 27  ASP A CA  1 
ATOM   201  C  C   . ASP A 1 27  ? 14.611  -3.537  50.181 1.00 110.30 ? 27  ASP A C   1 
ATOM   202  O  O   . ASP A 1 27  ? 14.346  -4.743  50.217 1.00 104.76 ? 27  ASP A O   1 
ATOM   203  C  CB  . ASP A 1 27  ? 16.833  -2.362  50.162 1.00 129.83 ? 27  ASP A CB  1 
ATOM   204  C  CG  . ASP A 1 27  ? 17.656  -3.381  50.935 1.00 138.31 ? 27  ASP A CG  1 
ATOM   205  O  OD1 . ASP A 1 27  ? 18.890  -3.206  51.018 1.00 145.58 ? 27  ASP A OD1 1 
ATOM   206  O  OD2 . ASP A 1 27  ? 17.074  -4.353  51.463 1.00 138.80 ? 27  ASP A OD2 1 
ATOM   207  N  N   . GLN A 1 28  ? 13.937  -2.641  50.905 1.00 114.19 ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? 12.869  -3.076  51.799 1.00 109.17 ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? 11.679  -3.634  51.029 1.00 106.21 ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? 10.932  -4.459  51.564 1.00 104.60 ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? 12.434  -1.921  52.701 1.00 105.50 ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? 12.216  -0.611  51.973 1.00 108.90 ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 12.726  0.587   52.753 1.00 114.99 ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 13.933  0.807   52.859 1.00 115.48 ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? 11.806  1.367   53.306 1.00 115.34 ? 28  GLN A NE2 1 
ATOM   216  N  N   . HIS A 1 29  ? 11.487  -3.203  49.779 1.00 103.52 ? 29  HIS A N   1 
ATOM   217  C  CA  . HIS A 1 29  ? 10.436  -3.783  48.948 1.00 97.27  ? 29  HIS A CA  1 
ATOM   218  C  C   . HIS A 1 29  ? 10.660  -5.277  48.752 1.00 99.01  ? 29  HIS A C   1 
ATOM   219  O  O   . HIS A 1 29  ? 9.746   -6.087  48.946 1.00 99.25  ? 29  HIS A O   1 
ATOM   220  C  CB  . HIS A 1 29  ? 10.382  -3.070  47.595 1.00 97.66  ? 29  HIS A CB  1 
ATOM   221  C  CG  . HIS A 1 29  ? 9.349   -1.989  47.517 1.00 100.05 ? 29  HIS A CG  1 
ATOM   222  N  ND1 . HIS A 1 29  ? 8.007   -2.222  47.729 1.00 96.58  ? 29  HIS A ND1 1 
ATOM   223  C  CD2 . HIS A 1 29  ? 9.462   -0.668  47.240 1.00 102.95 ? 29  HIS A CD2 1 
ATOM   224  C  CE1 . HIS A 1 29  ? 7.339   -1.090  47.593 1.00 98.12  ? 29  HIS A CE1 1 
ATOM   225  N  NE2 . HIS A 1 29  ? 8.199   -0.132  47.296 1.00 104.09 ? 29  HIS A NE2 1 
ATOM   226  N  N   . LEU A 1 30  ? 11.881  -5.660  48.370 1.00 97.09  ? 30  LEU A N   1 
ATOM   227  C  CA  . LEU A 1 30  ? 12.183  -7.070  48.149 1.00 89.51  ? 30  LEU A CA  1 
ATOM   228  C  C   . LEU A 1 30  ? 12.057  -7.882  49.430 1.00 93.20  ? 30  LEU A C   1 
ATOM   229  O  O   . LEU A 1 30  ? 11.678  -9.058  49.385 1.00 93.38  ? 30  LEU A O   1 
ATOM   230  C  CB  . LEU A 1 30  ? 13.590  -7.217  47.570 1.00 86.35  ? 30  LEU A CB  1 
ATOM   231  C  CG  . LEU A 1 30  ? 13.787  -6.779  46.117 1.00 87.19  ? 30  LEU A CG  1 
ATOM   232  C  CD1 . LEU A 1 30  ? 15.262  -6.561  45.825 1.00 91.05  ? 30  LEU A CD1 1 
ATOM   233  C  CD2 . LEU A 1 30  ? 13.191  -7.797  45.156 1.00 79.60  ? 30  LEU A CD2 1 
ATOM   234  N  N   . GLN A 1 31  ? 12.372  -7.280  50.579 1.00 97.55  ? 31  GLN A N   1 
ATOM   235  C  CA  . GLN A 1 31  ? 12.320  -8.023  51.832 1.00 97.45  ? 31  GLN A CA  1 
ATOM   236  C  C   . GLN A 1 31  ? 10.893  -8.383  52.219 1.00 94.66  ? 31  GLN A C   1 
ATOM   237  O  O   . GLN A 1 31  ? 10.664  -9.443  52.809 1.00 97.25  ? 31  GLN A O   1 
ATOM   238  C  CB  . GLN A 1 31  ? 12.987  -7.225  52.950 1.00 105.29 ? 31  GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 31  ? 13.367  -8.058  54.160 1.00 109.75 ? 31  GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 31  ? 12.853  -7.465  55.457 1.00 119.24 ? 31  GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 31  ? 11.705  -7.026  55.543 1.00 119.51 ? 31  GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 31  ? 13.703  -7.453  56.478 1.00 123.66 ? 31  GLN A NE2 1 
ATOM   243  N  N   . ARG A 1 32  ? 9.923   -7.528  51.895 1.00 93.52  ? 32  ARG A N   1 
ATOM   244  C  CA  . ARG A 1 32  ? 8.540   -7.832  52.248 1.00 94.80  ? 32  ARG A CA  1 
ATOM   245  C  C   . ARG A 1 32  ? 7.973   -8.930  51.350 1.00 94.38  ? 32  ARG A C   1 
ATOM   246  O  O   . ARG A 1 32  ? 7.259   -9.822  51.814 1.00 95.14  ? 32  ARG A O   1 
ATOM   247  C  CB  . ARG A 1 32  ? 7.682   -6.568  52.166 1.00 100.51 ? 32  ARG A CB  1 
ATOM   248  C  CG  . ARG A 1 32  ? 8.287   -5.356  52.863 1.00 107.91 ? 32  ARG A CG  1 
ATOM   249  C  CD  . ARG A 1 32  ? 7.506   -4.955  54.097 1.00 108.30 ? 32  ARG A CD  1 
ATOM   250  N  NE  . ARG A 1 32  ? 6.330   -4.148  53.802 1.00 105.25 ? 32  ARG A NE  1 
ATOM   251  C  CZ  . ARG A 1 32  ? 6.145   -2.925  54.282 1.00 107.91 ? 32  ARG A CZ  1 
ATOM   252  N  NH1 . ARG A 1 32  ? 7.061   -2.382  55.069 1.00 107.76 ? 32  ARG A NH1 1 
ATOM   253  N  NH2 . ARG A 1 32  ? 5.052   -2.246  53.985 1.00 112.00 ? 32  ARG A NH2 1 
ATOM   254  N  N   . ILE A 1 33  ? 8.273   -8.873  50.052 1.00 93.14  ? 33  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 33  ? 7.898   -9.957  49.147 1.00 88.58  ? 33  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 33  ? 8.589   -11.247 49.565 1.00 92.42  ? 33  ILE A C   1 
ATOM   257  O  O   . ILE A 1 33  ? 7.990   -12.328 49.536 1.00 90.16  ? 33  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 33  ? 8.233   -9.581  47.689 1.00 83.07  ? 33  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 33  ? 7.321   -8.458  47.214 1.00 78.85  ? 33  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 33  ? 8.105   -10.800 46.785 1.00 80.12  ? 33  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 33  ? 5.879   -8.865  47.051 1.00 73.98  ? 33  ILE A CD1 1 
ATOM   262  N  N   . GLU A 1 34  ? 9.858   -11.152 49.975 1.00 96.45  ? 34  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 34  ? 10.583  -12.332 50.436 1.00 96.67  ? 34  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 34  ? 9.917   -12.937 51.665 1.00 96.86  ? 34  GLU A C   1 
ATOM   265  O  O   . GLU A 1 34  ? 9.758   -14.159 51.756 1.00 94.73  ? 34  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 34  ? 12.038  -11.966 50.730 1.00 103.21 ? 34  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 34  ? 12.928  -13.147 51.079 1.00 110.73 ? 34  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 34  ? 14.393  -12.763 51.179 1.00 117.12 ? 34  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 34  ? 14.723  -11.597 50.876 1.00 116.84 ? 34  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 34  ? 15.213  -13.626 51.560 1.00 118.56 ? 34  GLU A OE2 1 
ATOM   271  N  N   . ARG A 1 35  ? 9.510   -12.094 52.616 1.00 101.61 ? 35  ARG A N   1 
ATOM   272  C  CA  . ARG A 1 35  ? 8.817   -12.587 53.799 1.00 100.51 ? 35  ARG A CA  1 
ATOM   273  C  C   . ARG A 1 35  ? 7.416   -13.085 53.480 1.00 98.11  ? 35  ARG A C   1 
ATOM   274  O  O   . ARG A 1 35  ? 6.858   -13.864 54.258 1.00 99.81  ? 35  ARG A O   1 
ATOM   275  C  CB  . ARG A 1 35  ? 8.745   -11.494 54.864 1.00 100.68 ? 35  ARG A CB  1 
ATOM   276  C  CG  . ARG A 1 35  ? 10.086  -11.122 55.470 1.00 103.79 ? 35  ARG A CG  1 
ATOM   277  C  CD  . ARG A 1 35  ? 9.966   -9.865  56.311 1.00 112.98 ? 35  ARG A CD  1 
ATOM   278  N  NE  . ARG A 1 35  ? 8.875   -9.964  57.274 1.00 121.52 ? 35  ARG A NE  1 
ATOM   279  C  CZ  . ARG A 1 35  ? 8.268   -8.920  57.827 1.00 128.26 ? 35  ARG A CZ  1 
ATOM   280  N  NH1 . ARG A 1 35  ? 8.640   -7.687  57.510 1.00 128.52 ? 35  ARG A NH1 1 
ATOM   281  N  NH2 . ARG A 1 35  ? 7.283   -9.110  58.695 1.00 134.67 ? 35  ARG A NH2 1 
ATOM   282  N  N   . PHE A 1 36  ? 6.834   -12.650 52.360 1.00 94.91  ? 36  PHE A N   1 
ATOM   283  C  CA  . PHE A 1 36  ? 5.504   -13.116 51.988 1.00 92.42  ? 36  PHE A CA  1 
ATOM   284  C  C   . PHE A 1 36  ? 5.556   -14.492 51.335 1.00 91.71  ? 36  PHE A C   1 
ATOM   285  O  O   . PHE A 1 36  ? 4.729   -15.359 51.641 1.00 95.77  ? 36  PHE A O   1 
ATOM   286  C  CB  . PHE A 1 36  ? 4.835   -12.105 51.057 1.00 88.12  ? 36  PHE A CB  1 
ATOM   287  C  CG  . PHE A 1 36  ? 3.452   -12.499 50.631 1.00 86.82  ? 36  PHE A CG  1 
ATOM   288  C  CD1 . PHE A 1 36  ? 2.474   -12.766 51.575 1.00 90.03  ? 36  PHE A CD1 1 
ATOM   289  C  CD2 . PHE A 1 36  ? 3.127   -12.603 49.288 1.00 83.54  ? 36  PHE A CD2 1 
ATOM   290  C  CE1 . PHE A 1 36  ? 1.201   -13.133 51.187 1.00 87.55  ? 36  PHE A CE1 1 
ATOM   291  C  CE2 . PHE A 1 36  ? 1.853   -12.966 48.894 1.00 80.70  ? 36  PHE A CE2 1 
ATOM   292  C  CZ  . PHE A 1 36  ? 0.888   -13.230 49.845 1.00 84.86  ? 36  PHE A CZ  1 
ATOM   293  N  N   . LEU A 1 37  ? 6.517   -14.711 50.433 1.00 87.86  ? 37  LEU A N   1 
ATOM   294  C  CA  . LEU A 1 37  ? 6.668   -16.030 49.827 1.00 80.50  ? 37  LEU A CA  1 
ATOM   295  C  C   . LEU A 1 37  ? 7.108   -17.059 50.858 1.00 83.84  ? 37  LEU A C   1 
ATOM   296  O  O   . LEU A 1 37  ? 6.691   -18.222 50.799 1.00 85.69  ? 37  LEU A O   1 
ATOM   297  C  CB  . LEU A 1 37  ? 7.663   -15.970 48.670 1.00 71.69  ? 37  LEU A CB  1 
ATOM   298  C  CG  . LEU A 1 37  ? 7.341   -14.959 47.570 1.00 73.74  ? 37  LEU A CG  1 
ATOM   299  C  CD1 . LEU A 1 37  ? 8.551   -14.746 46.679 1.00 72.99  ? 37  LEU A CD1 1 
ATOM   300  C  CD2 . LEU A 1 37  ? 6.138   -15.415 46.758 1.00 75.03  ? 37  LEU A CD2 1 
ATOM   301  N  N   . ASP A 1 38  ? 7.956   -16.652 51.806 1.00 90.69  ? 38  ASP A N   1 
ATOM   302  C  CA  . ASP A 1 38  ? 8.280   -17.527 52.928 1.00 97.38  ? 38  ASP A CA  1 
ATOM   303  C  C   . ASP A 1 38  ? 7.032   -17.890 53.719 1.00 95.44  ? 38  ASP A C   1 
ATOM   304  O  O   . ASP A 1 38  ? 6.935   -19.000 54.254 1.00 93.17  ? 38  ASP A O   1 
ATOM   305  C  CB  . ASP A 1 38  ? 9.309   -16.859 53.842 1.00 107.28 ? 38  ASP A CB  1 
ATOM   306  C  CG  . ASP A 1 38  ? 10.696  -16.813 53.228 1.00 114.98 ? 38  ASP A CG  1 
ATOM   307  O  OD1 . ASP A 1 38  ? 10.877  -17.354 52.116 1.00 115.62 ? 38  ASP A OD1 1 
ATOM   308  O  OD2 . ASP A 1 38  ? 11.606  -16.235 53.860 1.00 118.28 ? 38  ASP A OD2 1 
ATOM   309  N  N   . ALA A 1 39  ? 6.068   -16.973 53.799 1.00 96.73  ? 39  ALA A N   1 
ATOM   310  C  CA  . ALA A 1 39  ? 4.812   -17.264 54.477 1.00 97.88  ? 39  ALA A CA  1 
ATOM   311  C  C   . ALA A 1 39  ? 3.910   -18.161 53.642 1.00 97.54  ? 39  ALA A C   1 
ATOM   312  O  O   . ALA A 1 39  ? 3.150   -18.956 54.201 1.00 99.41  ? 39  ALA A O   1 
ATOM   313  C  CB  . ALA A 1 39  ? 4.085   -15.963 54.818 1.00 91.19  ? 39  ALA A CB  1 
ATOM   314  N  N   . LEU A 1 40  ? 3.991   -18.054 52.314 1.00 91.56  ? 40  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 40  ? 3.129   -18.819 51.419 1.00 88.52  ? 40  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 40  ? 3.511   -20.290 51.350 1.00 98.47  ? 40  LEU A C   1 
ATOM   317  O  O   . LEU A 1 40  ? 2.636   -21.143 51.164 1.00 102.71 ? 40  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 40  ? 3.179   -18.221 50.014 1.00 79.86  ? 40  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 40  ? 2.266   -17.031 49.733 1.00 73.34  ? 40  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 40  ? 2.413   -16.570 48.291 1.00 66.81  ? 40  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 40  ? 0.816   -17.404 50.031 1.00 71.39  ? 40  LEU A CD2 1 
ATOM   322  N  N   . ALA A 1 41  ? 4.799   -20.598 51.486 1.00 97.57  ? 41  ALA A N   1 
ATOM   323  C  CA  . ALA A 1 41  ? 5.268   -21.965 51.276 1.00 93.02  ? 41  ALA A CA  1 
ATOM   324  C  C   . ALA A 1 41  ? 4.611   -23.002 52.184 1.00 99.86  ? 41  ALA A C   1 
ATOM   325  O  O   . ALA A 1 41  ? 4.246   -24.076 51.674 1.00 106.53 ? 41  ALA A O   1 
ATOM   326  C  CB  . ALA A 1 41  ? 6.795   -22.005 51.422 1.00 89.43  ? 41  ALA A CB  1 
ATOM   327  N  N   . PRO A 1 42  ? 4.431   -22.777 53.501 1.00 102.74 ? 42  PRO A N   1 
ATOM   328  C  CA  . PRO A 1 42  ? 3.883   -23.851 54.346 1.00 101.53 ? 42  PRO A CA  1 
ATOM   329  C  C   . PRO A 1 42  ? 2.392   -24.102 54.161 1.00 96.00  ? 42  PRO A C   1 
ATOM   330  O  O   . PRO A 1 42  ? 1.804   -24.872 54.925 1.00 101.56 ? 42  PRO A O   1 
ATOM   331  C  CB  . PRO A 1 42  ? 4.181   -23.364 55.772 1.00 107.03 ? 42  PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 42  ? 5.199   -22.280 55.623 1.00 109.52 ? 42  PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 42  ? 4.881   -21.638 54.319 1.00 105.37 ? 42  PRO A CD  1 
ATOM   334  N  N   . LEU A 1 43  ? 1.765   -23.476 53.166 1.00 92.46  ? 43  LEU A N   1 
ATOM   335  C  CA  . LEU A 1 43  ? 0.337   -23.665 52.929 1.00 94.59  ? 43  LEU A CA  1 
ATOM   336  C  C   . LEU A 1 43  ? 0.040   -24.745 51.902 1.00 92.86  ? 43  LEU A C   1 
ATOM   337  O  O   . LEU A 1 43  ? -0.941  -25.480 52.052 1.00 93.26  ? 43  LEU A O   1 
ATOM   338  C  CB  . LEU A 1 43  ? -0.311  -22.358 52.477 1.00 98.50  ? 43  LEU A CB  1 
ATOM   339  C  CG  . LEU A 1 43  ? -0.594  -21.398 53.625 1.00 106.04 ? 43  LEU A CG  1 
ATOM   340  C  CD1 . LEU A 1 43  ? 0.523   -20.394 53.746 1.00 104.20 ? 43  LEU A CD1 1 
ATOM   341  C  CD2 . LEU A 1 43  ? -1.926  -20.719 53.421 1.00 109.42 ? 43  LEU A CD2 1 
ATOM   342  N  N   . HIS A 1 44  ? 0.849   -24.847 50.851 1.00 90.83  ? 44  HIS A N   1 
ATOM   343  C  CA  . HIS A 1 44  ? 0.713   -25.944 49.905 1.00 89.62  ? 44  HIS A CA  1 
ATOM   344  C  C   . HIS A 1 44  ? 2.021   -26.112 49.151 1.00 91.33  ? 44  HIS A C   1 
ATOM   345  O  O   . HIS A 1 44  ? 2.717   -25.120 48.902 1.00 98.35  ? 44  HIS A O   1 
ATOM   346  C  CB  . HIS A 1 44  ? -0.443  -25.713 48.921 1.00 82.19  ? 44  HIS A CB  1 
ATOM   347  C  CG  . HIS A 1 44  ? -0.714  -26.905 48.064 1.00 85.49  ? 44  HIS A CG  1 
ATOM   348  N  ND1 . HIS A 1 44  ? -1.434  -27.990 48.514 1.00 92.53  ? 44  HIS A ND1 1 
ATOM   349  C  CD2 . HIS A 1 44  ? -0.289  -27.224 46.819 1.00 84.01  ? 44  HIS A CD2 1 
ATOM   350  C  CE1 . HIS A 1 44  ? -1.467  -28.915 47.572 1.00 96.67  ? 44  HIS A CE1 1 
ATOM   351  N  NE2 . HIS A 1 44  ? -0.779  -28.476 46.533 1.00 90.61  ? 44  HIS A NE2 1 
ATOM   352  N  N   . PRO A 1 45  ? 2.381   -27.345 48.771 1.00 84.73  ? 45  PRO A N   1 
ATOM   353  C  CA  . PRO A 1 45  ? 3.629   -27.547 48.015 1.00 81.06  ? 45  PRO A CA  1 
ATOM   354  C  C   . PRO A 1 45  ? 3.735   -26.721 46.745 1.00 82.65  ? 45  PRO A C   1 
ATOM   355  O  O   . PRO A 1 45  ? 4.854   -26.392 46.331 1.00 86.32  ? 45  PRO A O   1 
ATOM   356  C  CB  . PRO A 1 45  ? 3.599   -29.048 47.699 1.00 81.31  ? 45  PRO A CB  1 
ATOM   357  C  CG  . PRO A 1 45  ? 2.811   -29.638 48.809 1.00 85.39  ? 45  PRO A CG  1 
ATOM   358  C  CD  . PRO A 1 45  ? 1.770   -28.624 49.178 1.00 86.35  ? 45  PRO A CD  1 
ATOM   359  N  N   . VAL A 1 46  ? 2.613   -26.373 46.109 1.00 75.72  ? 46  VAL A N   1 
ATOM   360  C  CA  . VAL A 1 46  ? 2.686   -25.598 44.876 1.00 75.29  ? 46  VAL A CA  1 
ATOM   361  C  C   . VAL A 1 46  ? 3.122   -24.163 45.141 1.00 84.59  ? 46  VAL A C   1 
ATOM   362  O  O   . VAL A 1 46  ? 3.570   -23.474 44.215 1.00 83.47  ? 46  VAL A O   1 
ATOM   363  C  CB  . VAL A 1 46  ? 1.337   -25.637 44.132 1.00 72.68  ? 46  VAL A CB  1 
ATOM   364  C  CG1 . VAL A 1 46  ? 0.391   -24.576 44.671 1.00 75.03  ? 46  VAL A CG1 1 
ATOM   365  C  CG2 . VAL A 1 46  ? 1.552   -25.461 42.634 1.00 70.68  ? 46  VAL A CG2 1 
ATOM   366  N  N   . LEU A 1 47  ? 3.017   -23.695 46.383 1.00 85.41  ? 47  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 47  ? 3.456   -22.360 46.759 1.00 81.15  ? 47  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 47  ? 4.886   -22.339 47.287 1.00 84.49  ? 47  LEU A C   1 
ATOM   369  O  O   . LEU A 1 47  ? 5.317   -21.319 47.834 1.00 87.66  ? 47  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 47  ? 2.509   -21.772 47.807 1.00 79.26  ? 47  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 47  ? 1.011   -21.930 47.537 1.00 75.93  ? 47  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 47  ? 0.194   -21.457 48.733 1.00 71.99  ? 47  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 47  ? 0.613   -21.176 46.280 1.00 72.47  ? 47  LEU A CD2 1 
ATOM   374  N  N   . GLU A 1 48  ? 5.629   -23.437 47.131 1.00 81.60  ? 48  GLU A N   1 
ATOM   375  C  CA  . GLU A 1 48  ? 6.967   -23.518 47.705 1.00 82.12  ? 48  GLU A CA  1 
ATOM   376  C  C   . GLU A 1 48  ? 8.010   -22.854 46.817 1.00 89.02  ? 48  GLU A C   1 
ATOM   377  O  O   . GLU A 1 48  ? 8.945   -22.223 47.322 1.00 99.43  ? 48  GLU A O   1 
ATOM   378  C  CB  . GLU A 1 48  ? 7.343   -24.976 47.956 1.00 79.73  ? 48  GLU A CB  1 
ATOM   379  C  CG  . GLU A 1 48  ? 6.588   -25.615 49.102 1.00 85.68  ? 48  GLU A CG  1 
ATOM   380  C  CD  . GLU A 1 48  ? 7.013   -27.045 49.348 1.00 92.85  ? 48  GLU A CD  1 
ATOM   381  O  OE1 . GLU A 1 48  ? 6.326   -27.741 50.124 1.00 99.31  ? 48  GLU A OE1 1 
ATOM   382  O  OE2 . GLU A 1 48  ? 8.033   -27.474 48.768 1.00 93.41  ? 48  GLU A OE2 1 
ATOM   383  N  N   . ASN A 1 49  ? 7.874   -22.985 45.501 1.00 84.98  ? 49  ASN A N   1 
ATOM   384  C  CA  . ASN A 1 49  ? 8.856   -22.470 44.559 1.00 78.47  ? 49  ASN A CA  1 
ATOM   385  C  C   . ASN A 1 49  ? 8.223   -21.414 43.668 1.00 75.07  ? 49  ASN A C   1 
ATOM   386  O  O   . ASN A 1 49  ? 7.092   -21.579 43.199 1.00 83.44  ? 49  ASN A O   1 
ATOM   387  C  CB  . ASN A 1 49  ? 9.432   -23.596 43.705 1.00 76.74  ? 49  ASN A CB  1 
ATOM   388  C  CG  . ASN A 1 49  ? 9.964   -24.734 44.541 1.00 75.29  ? 49  ASN A CG  1 
ATOM   389  O  OD1 . ASN A 1 49  ? 9.222   -25.645 44.911 1.00 77.39  ? 49  ASN A OD1 1 
ATOM   390  N  ND2 . ASN A 1 49  ? 11.255  -24.685 44.855 1.00 70.76  ? 49  ASN A ND2 1 
ATOM   391  N  N   . TRP A 1 50  ? 8.962   -20.332 43.435 1.00 70.11  ? 50  TRP A N   1 
ATOM   392  C  CA  . TRP A 1 50  ? 8.499   -19.230 42.608 1.00 68.40  ? 50  TRP A CA  1 
ATOM   393  C  C   . TRP A 1 50  ? 9.574   -18.864 41.595 1.00 66.33  ? 50  TRP A C   1 
ATOM   394  O  O   . TRP A 1 50  ? 10.773  -18.976 41.867 1.00 62.63  ? 50  TRP A O   1 
ATOM   395  C  CB  . TRP A 1 50  ? 8.127   -18.014 43.465 1.00 66.83  ? 50  TRP A CB  1 
ATOM   396  C  CG  . TRP A 1 50  ? 6.928   -18.272 44.317 1.00 65.20  ? 50  TRP A CG  1 
ATOM   397  C  CD1 . TRP A 1 50  ? 6.908   -18.871 45.541 1.00 69.78  ? 50  TRP A CD1 1 
ATOM   398  C  CD2 . TRP A 1 50  ? 5.568   -17.958 44.000 1.00 64.11  ? 50  TRP A CD2 1 
ATOM   399  N  NE1 . TRP A 1 50  ? 5.619   -18.943 46.011 1.00 73.76  ? 50  TRP A NE1 1 
ATOM   400  C  CE2 . TRP A 1 50  ? 4.778   -18.389 45.083 1.00 71.10  ? 50  TRP A CE2 1 
ATOM   401  C  CE3 . TRP A 1 50  ? 4.942   -17.349 42.909 1.00 63.87  ? 50  TRP A CE3 1 
ATOM   402  C  CZ2 . TRP A 1 50  ? 3.394   -18.232 45.106 1.00 75.80  ? 50  TRP A CZ2 1 
ATOM   403  C  CZ3 . TRP A 1 50  ? 3.569   -17.196 42.931 1.00 68.51  ? 50  TRP A CZ3 1 
ATOM   404  C  CH2 . TRP A 1 50  ? 2.810   -17.635 44.022 1.00 74.46  ? 50  TRP A CH2 1 
ATOM   405  N  N   . TYR A 1 51  ? 9.130   -18.430 40.419 1.00 65.73  ? 51  TYR A N   1 
ATOM   406  C  CA  . TYR A 1 51  ? 10.017  -18.168 39.298 1.00 62.87  ? 51  TYR A CA  1 
ATOM   407  C  C   . TYR A 1 51  ? 9.754   -16.778 38.740 1.00 67.24  ? 51  TYR A C   1 
ATOM   408  O  O   . TYR A 1 51  ? 8.712   -16.169 38.996 1.00 70.71  ? 51  TYR A O   1 
ATOM   409  C  CB  . TYR A 1 51  ? 9.835   -19.202 38.174 1.00 54.72  ? 51  TYR A CB  1 
ATOM   410  C  CG  . TYR A 1 51  ? 10.125  -20.636 38.557 1.00 56.39  ? 51  TYR A CG  1 
ATOM   411  C  CD1 . TYR A 1 51  ? 9.247   -21.356 39.359 1.00 58.83  ? 51  TYR A CD1 1 
ATOM   412  C  CD2 . TYR A 1 51  ? 11.268  -21.279 38.096 1.00 58.97  ? 51  TYR A CD2 1 
ATOM   413  C  CE1 . TYR A 1 51  ? 9.507   -22.670 39.704 1.00 63.45  ? 51  TYR A CE1 1 
ATOM   414  C  CE2 . TYR A 1 51  ? 11.536  -22.593 38.435 1.00 62.65  ? 51  TYR A CE2 1 
ATOM   415  C  CZ  . TYR A 1 51  ? 10.652  -23.284 39.238 1.00 65.09  ? 51  TYR A CZ  1 
ATOM   416  O  OH  . TYR A 1 51  ? 10.915  -24.592 39.575 1.00 67.49  ? 51  TYR A OH  1 
ATOM   417  N  N   . LEU A 1 52  ? 10.717  -16.281 37.968 1.00 67.12  ? 52  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 52  ? 10.482  -15.089 37.168 1.00 68.04  ? 52  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 52  ? 9.566   -15.422 35.998 1.00 69.12  ? 52  LEU A C   1 
ATOM   420  O  O   . LEU A 1 52  ? 9.616   -16.517 35.433 1.00 77.93  ? 52  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 52  ? 11.797  -14.519 36.635 1.00 69.93  ? 52  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 52  ? 12.884  -14.082 37.615 1.00 70.77  ? 52  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 52  ? 13.992  -13.353 36.870 1.00 64.48  ? 52  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 52  ? 12.307  -13.208 38.703 1.00 74.49  ? 52  LEU A CD2 1 
ATOM   425  N  N   . CYS A 1 53  ? 8.723   -14.463 35.633 1.00 67.44  ? 53  CYS A N   1 
ATOM   426  C  CA  . CYS A 1 53  ? 7.901   -14.638 34.450 1.00 65.54  ? 53  CYS A CA  1 
ATOM   427  C  C   . CYS A 1 53  ? 8.758   -14.493 33.193 1.00 63.74  ? 53  CYS A C   1 
ATOM   428  O  O   . CYS A 1 53  ? 9.940   -14.139 33.247 1.00 58.68  ? 53  CYS A O   1 
ATOM   429  C  CB  . CYS A 1 53  ? 6.750   -13.634 34.444 1.00 69.74  ? 53  CYS A CB  1 
ATOM   430  S  SG  . CYS A 1 53  ? 5.393   -14.078 35.545 1.00 71.89  ? 53  CYS A SG  1 
ATOM   431  N  N   . GLY A 1 54  ? 8.150   -14.782 32.046 1.00 56.86  ? 54  GLY A N   1 
ATOM   432  C  CA  . GLY A 1 54  ? 8.868   -14.703 30.790 1.00 58.45  ? 54  GLY A CA  1 
ATOM   433  C  C   . GLY A 1 54  ? 7.921   -14.663 29.615 1.00 59.60  ? 54  GLY A C   1 
ATOM   434  O  O   . GLY A 1 54  ? 6.738   -14.999 29.729 1.00 62.63  ? 54  GLY A O   1 
ATOM   435  N  N   . ASP A 1 55  ? 8.461   -14.238 28.472 1.00 67.39  ? 55  ASP A N   1 
ATOM   436  C  CA  . ASP A 1 55  ? 7.678   -14.209 27.244 1.00 69.55  ? 55  ASP A CA  1 
ATOM   437  C  C   . ASP A 1 55  ? 7.338   -15.606 26.751 1.00 74.84  ? 55  ASP A C   1 
ATOM   438  O  O   . ASP A 1 55  ? 6.437   -15.753 25.919 1.00 81.52  ? 55  ASP A O   1 
ATOM   439  C  CB  . ASP A 1 55  ? 8.431   -13.439 26.159 1.00 77.08  ? 55  ASP A CB  1 
ATOM   440  C  CG  . ASP A 1 55  ? 8.424   -11.943 26.397 1.00 84.64  ? 55  ASP A CG  1 
ATOM   441  O  OD1 . ASP A 1 55  ? 8.261   -11.179 25.421 1.00 92.06  ? 55  ASP A OD1 1 
ATOM   442  O  OD2 . ASP A 1 55  ? 8.574   -11.534 27.566 1.00 86.46  ? 55  ASP A OD2 1 
ATOM   443  N  N   . SER A 1 56  ? 8.035   -16.628 27.242 1.00 74.37  ? 56  SER A N   1 
ATOM   444  C  CA  . SER A 1 56  ? 7.745   -18.011 26.904 1.00 67.82  ? 56  SER A CA  1 
ATOM   445  C  C   . SER A 1 56  ? 7.801   -18.846 28.173 1.00 72.08  ? 56  SER A C   1 
ATOM   446  O  O   . SER A 1 56  ? 8.412   -18.454 29.170 1.00 72.94  ? 56  SER A O   1 
ATOM   447  C  CB  . SER A 1 56  ? 8.729   -18.559 25.865 1.00 61.57  ? 56  SER A CB  1 
ATOM   448  O  OG  . SER A 1 56  ? 10.047  -18.571 26.382 1.00 60.69  ? 56  SER A OG  1 
ATOM   449  N  N   . LEU A 1 57  ? 7.143   -20.007 28.130 1.00 75.32  ? 57  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? 7.249   -20.946 29.242 1.00 66.72  ? 57  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? 8.695   -21.376 29.446 1.00 61.93  ? 57  LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? 9.156   -21.513 30.586 1.00 61.91  ? 57  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? 6.353   -22.161 28.996 1.00 66.65  ? 57  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? 6.520   -23.359 29.937 1.00 63.45  ? 57  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? 6.242   -22.959 31.380 1.00 67.13  ? 57  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? 5.614   -24.500 29.515 1.00 61.97  ? 57  LEU A CD2 1 
ATOM   457  N  N   . ARG A 1 58  ? 9.429   -21.580 28.349 1.00 61.81  ? 58  ARG A N   1 
ATOM   458  C  CA  . ARG A 1 58  ? 10.847  -21.907 28.455 1.00 66.66  ? 58  ARG A CA  1 
ATOM   459  C  C   . ARG A 1 58  ? 11.607  -20.808 29.184 1.00 64.50  ? 58  ARG A C   1 
ATOM   460  O  O   . ARG A 1 58  ? 12.514  -21.086 29.976 1.00 58.21  ? 58  ARG A O   1 
ATOM   461  C  CB  . ARG A 1 58  ? 11.435  -22.138 27.063 1.00 66.07  ? 58  ARG A CB  1 
ATOM   462  C  CG  . ARG A 1 58  ? 12.954  -22.192 27.021 1.00 65.27  ? 58  ARG A CG  1 
ATOM   463  C  CD  . ARG A 1 58  ? 13.443  -22.546 25.628 1.00 79.88  ? 58  ARG A CD  1 
ATOM   464  N  NE  . ARG A 1 58  ? 14.890  -22.727 25.580 1.00 90.20  ? 58  ARG A NE  1 
ATOM   465  C  CZ  . ARG A 1 58  ? 15.545  -23.227 24.536 1.00 94.09  ? 58  ARG A CZ  1 
ATOM   466  N  NH1 . ARG A 1 58  ? 14.881  -23.595 23.448 1.00 97.77  ? 58  ARG A NH1 1 
ATOM   467  N  NH2 . ARG A 1 58  ? 16.865  -23.357 24.578 1.00 87.16  ? 58  ARG A NH2 1 
ATOM   468  N  N   . ASP A 1 59  ? 11.234  -19.553 28.945 1.00 68.91  ? 59  ASP A N   1 
ATOM   469  C  CA  . ASP A 1 59  ? 11.916  -18.441 29.595 1.00 74.90  ? 59  ASP A CA  1 
ATOM   470  C  C   . ASP A 1 59  ? 11.504  -18.298 31.054 1.00 70.45  ? 59  ASP A C   1 
ATOM   471  O  O   . ASP A 1 59  ? 12.332  -17.951 31.903 1.00 75.95  ? 59  ASP A O   1 
ATOM   472  C  CB  . ASP A 1 59  ? 11.635  -17.147 28.836 1.00 91.80  ? 59  ASP A CB  1 
ATOM   473  C  CG  . ASP A 1 59  ? 12.884  -16.334 28.600 1.00 108.24 ? 59  ASP A CG  1 
ATOM   474  O  OD1 . ASP A 1 59  ? 13.573  -16.006 29.589 1.00 118.30 ? 59  ASP A OD1 1 
ATOM   475  O  OD2 . ASP A 1 59  ? 13.180  -16.028 27.427 1.00 112.49 ? 59  ASP A OD2 1 
ATOM   476  N  N   . ALA A 1 60  ? 10.237  -18.566 31.364 1.00 65.75  ? 60  ALA A N   1 
ATOM   477  C  CA  . ALA A 1 60  ? 9.722   -18.366 32.712 1.00 65.68  ? 60  ALA A CA  1 
ATOM   478  C  C   . ALA A 1 60  ? 10.100  -19.482 33.679 1.00 64.06  ? 60  ALA A C   1 
ATOM   479  O  O   . ALA A 1 60  ? 9.791   -19.371 34.871 1.00 62.27  ? 60  ALA A O   1 
ATOM   480  C  CB  . ALA A 1 60  ? 8.200   -18.218 32.668 1.00 53.20  ? 60  ALA A CB  1 
ATOM   481  N  N   . LEU A 1 61  ? 10.746  -20.547 33.208 1.00 63.15  ? 61  LEU A N   1 
ATOM   482  C  CA  . LEU A 1 61  ? 11.226  -21.615 34.075 1.00 66.71  ? 61  LEU A CA  1 
ATOM   483  C  C   . LEU A 1 61  ? 12.734  -21.563 34.279 1.00 70.13  ? 61  LEU A C   1 
ATOM   484  O  O   . LEU A 1 61  ? 13.304  -22.493 34.857 1.00 76.37  ? 61  LEU A O   1 
ATOM   485  C  CB  . LEU A 1 61  ? 10.828  -22.980 33.512 1.00 68.57  ? 61  LEU A CB  1 
ATOM   486  C  CG  . LEU A 1 61  ? 9.357   -23.385 33.623 1.00 61.72  ? 61  LEU A CG  1 
ATOM   487  C  CD1 . LEU A 1 61  ? 9.128   -24.708 32.922 1.00 56.80  ? 61  LEU A CD1 1 
ATOM   488  C  CD2 . LEU A 1 61  ? 8.935   -23.469 35.078 1.00 60.72  ? 61  LEU A CD2 1 
ATOM   489  N  N   . SER A 1 62  ? 13.389  -20.497 33.825 1.00 71.31  ? 62  SER A N   1 
ATOM   490  C  CA  . SER A 1 62  ? 14.841  -20.415 33.872 1.00 72.32  ? 62  SER A CA  1 
ATOM   491  C  C   . SER A 1 62  ? 15.376  -19.840 35.176 1.00 66.14  ? 62  SER A C   1 
ATOM   492  O  O   . SER A 1 62  ? 16.550  -20.062 35.495 1.00 68.22  ? 62  SER A O   1 
ATOM   493  C  CB  . SER A 1 62  ? 15.354  -19.571 32.701 1.00 79.00  ? 62  SER A CB  1 
ATOM   494  O  OG  . SER A 1 62  ? 15.000  -20.158 31.461 1.00 87.20  ? 62  SER A OG  1 
ATOM   495  N  N   . HIS A 1 63  ? 14.556  -19.115 35.937 1.00 62.44  ? 63  HIS A N   1 
ATOM   496  C  CA  . HIS A 1 63  ? 15.006  -18.423 37.147 1.00 68.60  ? 63  HIS A CA  1 
ATOM   497  C  C   . HIS A 1 63  ? 14.134  -18.830 38.331 1.00 66.23  ? 63  HIS A C   1 
ATOM   498  O  O   . HIS A 1 63  ? 13.114  -18.192 38.604 1.00 68.83  ? 63  HIS A O   1 
ATOM   499  C  CB  . HIS A 1 63  ? 14.982  -16.912 36.953 1.00 82.27  ? 63  HIS A CB  1 
ATOM   500  C  CG  . HIS A 1 63  ? 15.808  -16.433 35.802 1.00 94.44  ? 63  HIS A CG  1 
ATOM   501  N  ND1 . HIS A 1 63  ? 16.927  -15.647 35.970 1.00 99.09  ? 63  HIS A ND1 1 
ATOM   502  C  CD2 . HIS A 1 63  ? 15.670  -16.611 34.467 1.00 96.88  ? 63  HIS A CD2 1 
ATOM   503  C  CE1 . HIS A 1 63  ? 17.447  -15.367 34.788 1.00 101.51 ? 63  HIS A CE1 1 
ATOM   504  N  NE2 . HIS A 1 63  ? 16.705  -15.943 33.860 1.00 98.44  ? 63  HIS A NE2 1 
ATOM   505  N  N   . ASN A 1 64  ? 14.543  -19.877 39.040 1.00 65.70  ? 64  ASN A N   1 
ATOM   506  C  CA  . ASN A 1 64  ? 13.933  -20.205 40.322 1.00 69.52  ? 64  ASN A CA  1 
ATOM   507  C  C   . ASN A 1 64  ? 14.463  -19.231 41.368 1.00 79.13  ? 64  ASN A C   1 
ATOM   508  O  O   . ASN A 1 64  ? 15.658  -19.239 41.681 1.00 87.72  ? 64  ASN A O   1 
ATOM   509  C  CB  . ASN A 1 64  ? 14.240  -21.651 40.710 1.00 71.13  ? 64  ASN A CB  1 
ATOM   510  C  CG  . ASN A 1 64  ? 13.523  -22.090 41.980 1.00 75.99  ? 64  ASN A CG  1 
ATOM   511  O  OD1 . ASN A 1 64  ? 13.116  -21.268 42.799 1.00 77.75  ? 64  ASN A OD1 1 
ATOM   512  N  ND2 . ASN A 1 64  ? 13.372  -23.399 42.149 1.00 85.84  ? 64  ASN A ND2 1 
ATOM   513  N  N   . VAL A 1 65  ? 13.579  -18.391 41.907 1.00 80.05  ? 65  VAL A N   1 
ATOM   514  C  CA  . VAL A 1 65  ? 13.989  -17.402 42.897 1.00 81.34  ? 65  VAL A CA  1 
ATOM   515  C  C   . VAL A 1 65  ? 13.850  -17.901 44.335 1.00 82.92  ? 65  VAL A C   1 
ATOM   516  O  O   . VAL A 1 65  ? 14.450  -17.305 45.243 1.00 82.09  ? 65  VAL A O   1 
ATOM   517  C  CB  . VAL A 1 65  ? 13.212  -16.080 42.717 1.00 80.76  ? 65  VAL A CB  1 
ATOM   518  C  CG1 . VAL A 1 65  ? 13.180  -15.666 41.253 1.00 85.44  ? 65  VAL A CG1 1 
ATOM   519  C  CG2 . VAL A 1 65  ? 11.807  -16.207 43.270 1.00 84.85  ? 65  VAL A CG2 1 
ATOM   520  N  N   . THR A 1 66  ? 13.077  -18.962 44.573 1.00 79.21  ? 66  THR A N   1 
ATOM   521  C  CA  . THR A 1 66  ? 13.091  -19.586 45.891 1.00 70.88  ? 66  THR A CA  1 
ATOM   522  C  C   . THR A 1 66  ? 14.399  -20.333 46.117 1.00 80.81  ? 66  THR A C   1 
ATOM   523  O  O   . THR A 1 66  ? 15.001  -20.238 47.193 1.00 78.22  ? 66  THR A O   1 
ATOM   524  C  CB  . THR A 1 66  ? 11.897  -20.528 46.047 1.00 72.44  ? 66  THR A CB  1 
ATOM   525  O  OG1 . THR A 1 66  ? 10.697  -19.758 46.189 1.00 75.20  ? 66  THR A OG1 1 
ATOM   526  C  CG2 . THR A 1 66  ? 12.071  -21.415 47.277 1.00 73.52  ? 66  THR A CG2 1 
ATOM   527  N  N   . GLU A 1 67  ? 14.860  -21.071 45.105 1.00 81.32  ? 67  GLU A N   1 
ATOM   528  C  CA  . GLU A 1 67  ? 16.150  -21.743 45.201 1.00 80.28  ? 67  GLU A CA  1 
ATOM   529  C  C   . GLU A 1 67  ? 17.293  -20.738 45.196 1.00 81.47  ? 67  GLU A C   1 
ATOM   530  O  O   . GLU A 1 67  ? 18.282  -20.907 45.918 1.00 82.54  ? 67  GLU A O   1 
ATOM   531  C  CB  . GLU A 1 67  ? 16.302  -22.739 44.050 1.00 81.07  ? 67  GLU A CB  1 
ATOM   532  C  CG  . GLU A 1 67  ? 17.185  -23.932 44.363 1.00 90.13  ? 67  GLU A CG  1 
ATOM   533  C  CD  . GLU A 1 67  ? 17.568  -24.713 43.120 1.00 95.50  ? 67  GLU A CD  1 
ATOM   534  O  OE1 . GLU A 1 67  ? 17.294  -24.224 42.003 1.00 96.99  ? 67  GLU A OE1 1 
ATOM   535  O  OE2 . GLU A 1 67  ? 18.144  -25.813 43.261 1.00 98.98  ? 67  GLU A OE2 1 
ATOM   536  N  N   . HIS A 1 68  ? 17.174  -19.681 44.392 1.00 90.05  ? 68  HIS A N   1 
ATOM   537  C  CA  . HIS A 1 68  ? 18.198  -18.642 44.276 1.00 100.05 ? 68  HIS A CA  1 
ATOM   538  C  C   . HIS A 1 68  ? 17.536  -17.295 44.557 1.00 115.40 ? 68  HIS A C   1 
ATOM   539  O  O   . HIS A 1 68  ? 17.031  -16.635 43.645 1.00 127.72 ? 68  HIS A O   1 
ATOM   540  C  CB  . HIS A 1 68  ? 18.860  -18.672 42.900 1.00 92.83  ? 68  HIS A CB  1 
ATOM   541  C  CG  . HIS A 1 68  ? 19.433  -20.005 42.533 1.00 91.24  ? 68  HIS A CG  1 
ATOM   542  N  ND1 . HIS A 1 68  ? 20.573  -20.513 43.119 1.00 95.42  ? 68  HIS A ND1 1 
ATOM   543  C  CD2 . HIS A 1 68  ? 19.022  -20.937 41.641 1.00 88.45  ? 68  HIS A CD2 1 
ATOM   544  C  CE1 . HIS A 1 68  ? 20.839  -21.700 42.603 1.00 94.69  ? 68  HIS A CE1 1 
ATOM   545  N  NE2 . HIS A 1 68  ? 19.913  -21.981 41.704 1.00 91.79  ? 68  HIS A NE2 1 
ATOM   546  N  N   . ARG A 1 69  ? 17.554  -16.887 45.827 1.00 114.85 ? 69  ARG A N   1 
ATOM   547  C  CA  . ARG A 1 69  ? 16.955  -15.623 46.238 1.00 108.87 ? 69  ARG A CA  1 
ATOM   548  C  C   . ARG A 1 69  ? 17.744  -14.412 45.762 1.00 107.06 ? 69  ARG A C   1 
ATOM   549  O  O   . ARG A 1 69  ? 17.217  -13.295 45.811 1.00 100.66 ? 69  ARG A O   1 
ATOM   550  C  CB  . ARG A 1 69  ? 16.812  -15.595 47.759 1.00 108.84 ? 69  ARG A CB  1 
ATOM   551  C  CG  . ARG A 1 69  ? 16.157  -16.846 48.315 1.00 113.15 ? 69  ARG A CG  1 
ATOM   552  C  CD  . ARG A 1 69  ? 16.547  -17.105 49.759 1.00 121.93 ? 69  ARG A CD  1 
ATOM   553  N  NE  . ARG A 1 69  ? 15.509  -16.667 50.687 1.00 127.16 ? 69  ARG A NE  1 
ATOM   554  C  CZ  . ARG A 1 69  ? 14.373  -17.324 50.905 1.00 132.18 ? 69  ARG A CZ  1 
ATOM   555  N  NH1 . ARG A 1 69  ? 14.120  -18.455 50.259 1.00 130.52 ? 69  ARG A NH1 1 
ATOM   556  N  NH2 . ARG A 1 69  ? 13.487  -16.847 51.768 1.00 135.40 ? 69  ARG A NH2 1 
ATOM   557  N  N   . GLN A 1 70  ? 18.983  -14.601 45.300 1.00 115.24 ? 70  GLN A N   1 
ATOM   558  C  CA  . GLN A 1 70  ? 19.761  -13.494 44.760 1.00 117.74 ? 70  GLN A CA  1 
ATOM   559  C  C   . GLN A 1 70  ? 19.140  -12.918 43.495 1.00 109.64 ? 70  GLN A C   1 
ATOM   560  O  O   . GLN A 1 70  ? 19.424  -11.766 43.151 1.00 105.88 ? 70  GLN A O   1 
ATOM   561  C  CB  . GLN A 1 70  ? 21.197  -13.943 44.469 1.00 126.85 ? 70  GLN A CB  1 
ATOM   562  C  CG  . GLN A 1 70  ? 21.316  -15.298 43.766 1.00 136.62 ? 70  GLN A CG  1 
ATOM   563  C  CD  . GLN A 1 70  ? 21.200  -16.483 44.717 1.00 148.16 ? 70  GLN A CD  1 
ATOM   564  O  OE1 . GLN A 1 70  ? 20.295  -16.537 45.551 1.00 151.30 ? 70  GLN A OE1 1 
ATOM   565  N  NE2 . GLN A 1 70  ? 22.117  -17.439 44.592 1.00 153.87 ? 70  GLN A NE2 1 
ATOM   566  N  N   . ASP A 1 71  ? 18.314  -13.690 42.792 1.00 105.16 ? 71  ASP A N   1 
ATOM   567  C  CA  . ASP A 1 71  ? 17.665  -13.235 41.571 1.00 102.62 ? 71  ASP A CA  1 
ATOM   568  C  C   . ASP A 1 71  ? 16.271  -12.676 41.818 1.00 98.47  ? 71  ASP A C   1 
ATOM   569  O  O   . ASP A 1 71  ? 15.538  -12.424 40.855 1.00 106.00 ? 71  ASP A O   1 
ATOM   570  C  CB  . ASP A 1 71  ? 17.591  -14.377 40.554 1.00 105.76 ? 71  ASP A CB  1 
ATOM   571  C  CG  . ASP A 1 71  ? 18.962  -14.861 40.124 1.00 112.07 ? 71  ASP A CG  1 
ATOM   572  O  OD1 . ASP A 1 71  ? 19.918  -14.693 40.908 1.00 116.81 ? 71  ASP A OD1 1 
ATOM   573  O  OD2 . ASP A 1 71  ? 19.084  -15.407 39.007 1.00 113.14 ? 71  ASP A OD2 1 
ATOM   574  N  N   . LEU A 1 72  ? 15.881  -12.497 43.082 1.00 89.04  ? 72  LEU A N   1 
ATOM   575  C  CA  . LEU A 1 72  ? 14.611  -11.841 43.368 1.00 81.98  ? 72  LEU A CA  1 
ATOM   576  C  C   . LEU A 1 72  ? 14.653  -10.366 42.997 1.00 84.34  ? 72  LEU A C   1 
ATOM   577  O  O   . LEU A 1 72  ? 13.624  -9.795  42.619 1.00 85.26  ? 72  LEU A O   1 
ATOM   578  C  CB  . LEU A 1 72  ? 14.247  -12.008 44.843 1.00 79.36  ? 72  LEU A CB  1 
ATOM   579  C  CG  . LEU A 1 72  ? 12.842  -11.550 45.241 1.00 74.68  ? 72  LEU A CG  1 
ATOM   580  C  CD1 . LEU A 1 72  ? 11.791  -12.287 44.429 1.00 72.46  ? 72  LEU A CD1 1 
ATOM   581  C  CD2 . LEU A 1 72  ? 12.606  -11.745 46.730 1.00 71.24  ? 72  LEU A CD2 1 
ATOM   582  N  N   . ALA A 1 73  ? 15.826  -9.736  43.098 1.00 84.22  ? 73  ALA A N   1 
ATOM   583  C  CA  . ALA A 1 73  ? 15.960  -8.343  42.686 1.00 83.01  ? 73  ALA A CA  1 
ATOM   584  C  C   . ALA A 1 73  ? 15.717  -8.173  41.193 1.00 81.95  ? 73  ALA A C   1 
ATOM   585  O  O   . ALA A 1 73  ? 15.332  -7.086  40.746 1.00 92.66  ? 73  ALA A O   1 
ATOM   586  C  CB  . ALA A 1 73  ? 17.344  -7.815  43.062 1.00 76.15  ? 73  ALA A CB  1 
ATOM   587  N  N   . LYS A 1 74  ? 15.926  -9.232  40.410 1.00 75.88  ? 74  LYS A N   1 
ATOM   588  C  CA  . LYS A 1 74  ? 15.704  -9.158  38.971 1.00 80.40  ? 74  LYS A CA  1 
ATOM   589  C  C   . LYS A 1 74  ? 14.224  -9.094  38.616 1.00 81.23  ? 74  LYS A C   1 
ATOM   590  O  O   . LYS A 1 74  ? 13.887  -8.722  37.487 1.00 85.30  ? 74  LYS A O   1 
ATOM   591  C  CB  . LYS A 1 74  ? 16.365  -10.352 38.278 1.00 76.85  ? 74  LYS A CB  1 
ATOM   592  C  CG  . LYS A 1 74  ? 17.884  -10.354 38.387 1.00 77.37  ? 74  LYS A CG  1 
ATOM   593  C  CD  . LYS A 1 74  ? 18.499  -11.581 37.732 1.00 77.43  ? 74  LYS A CD  1 
ATOM   594  C  CE  . LYS A 1 74  ? 20.019  -11.523 37.788 1.00 81.35  ? 74  LYS A CE  1 
ATOM   595  N  NZ  . LYS A 1 74  ? 20.651  -12.755 37.241 1.00 82.32  ? 74  LYS A NZ  1 
ATOM   596  N  N   . ALA A 1 75  ? 13.335  -9.444  39.548 1.00 77.10  ? 75  ALA A N   1 
ATOM   597  C  CA  . ALA A 1 75  ? 11.905  -9.352  39.284 1.00 75.41  ? 75  ALA A CA  1 
ATOM   598  C  C   . ALA A 1 75  ? 11.390  -7.926  39.420 1.00 78.34  ? 75  ALA A C   1 
ATOM   599  O  O   . ALA A 1 75  ? 10.453  -7.538  38.712 1.00 78.48  ? 75  ALA A O   1 
ATOM   600  C  CB  . ALA A 1 75  ? 11.129  -10.268 40.231 1.00 72.02  ? 75  ALA A CB  1 
ATOM   601  N  N   . LEU A 1 76  ? 11.983  -7.139  40.310 1.00 81.54  ? 76  LEU A N   1 
ATOM   602  C  CA  . LEU A 1 76  ? 11.482  -5.811  40.628 1.00 83.23  ? 76  LEU A CA  1 
ATOM   603  C  C   . LEU A 1 76  ? 12.055  -4.791  39.652 1.00 82.94  ? 76  LEU A C   1 
ATOM   604  O  O   . LEU A 1 76  ? 13.271  -4.572  39.616 1.00 81.84  ? 76  LEU A O   1 
ATOM   605  C  CB  . LEU A 1 76  ? 11.835  -5.436  42.066 1.00 83.21  ? 76  LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 76  ? 11.325  -4.071  42.527 1.00 85.39  ? 76  LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 76  ? 10.100  -4.226  43.414 1.00 87.86  ? 76  LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 76  ? 12.422  -3.322  43.252 1.00 82.87  ? 76  LEU A CD2 1 
ATOM   609  N  N   . SER A 1 77  ? 11.180  -4.177  38.862 1.00 85.21  ? 77  SER A N   1 
ATOM   610  C  CA  . SER A 1 77  ? 11.548  -3.081  37.980 1.00 92.42  ? 77  SER A CA  1 
ATOM   611  C  C   . SER A 1 77  ? 11.086  -1.769  38.598 1.00 92.14  ? 77  SER A C   1 
ATOM   612  O  O   . SER A 1 77  ? 9.960   -1.668  39.095 1.00 90.36  ? 77  SER A O   1 
ATOM   613  C  CB  . SER A 1 77  ? 10.934  -3.262  36.590 1.00 97.01  ? 77  SER A CB  1 
ATOM   614  O  OG  . SER A 1 77  ? 10.669  -2.013  35.979 1.00 106.62 ? 77  SER A OG  1 
ATOM   615  N  N   . ARG A 1 78  ? 11.962  -0.768  38.577 1.00 92.68  ? 78  ARG A N   1 
ATOM   616  C  CA  . ARG A 1 78  ? 11.698  0.504   39.236 1.00 93.38  ? 78  ARG A CA  1 
ATOM   617  C  C   . ARG A 1 78  ? 11.951  1.651   38.270 1.00 95.77  ? 78  ARG A C   1 
ATOM   618  O  O   . ARG A 1 78  ? 12.993  1.694   37.608 1.00 94.48  ? 78  ARG A O   1 
ATOM   619  C  CB  . ARG A 1 78  ? 12.568  0.665   40.488 1.00 89.26  ? 78  ARG A CB  1 
ATOM   620  C  CG  . ARG A 1 78  ? 12.953  2.101   40.804 1.00 86.78  ? 78  ARG A CG  1 
ATOM   621  C  CD  . ARG A 1 78  ? 13.122  2.309   42.299 1.00 93.28  ? 78  ARG A CD  1 
ATOM   622  N  NE  . ARG A 1 78  ? 11.874  2.720   42.936 1.00 99.62  ? 78  ARG A NE  1 
ATOM   623  C  CZ  . ARG A 1 78  ? 11.660  2.696   44.247 1.00 103.81 ? 78  ARG A CZ  1 
ATOM   624  N  NH1 . ARG A 1 78  ? 12.612  2.275   45.067 1.00 106.64 ? 78  ARG A NH1 1 
ATOM   625  N  NH2 . ARG A 1 78  ? 10.492  3.086   44.739 1.00 103.18 ? 78  ARG A NH2 1 
ATOM   626  N  N   . ASP A 1 79  ? 10.992  2.570   38.190 1.00 97.08  ? 79  ASP A N   1 
ATOM   627  C  CA  . ASP A 1 79  ? 11.164  3.813   37.452 1.00 104.43 ? 79  ASP A CA  1 
ATOM   628  C  C   . ASP A 1 79  ? 11.779  4.849   38.384 1.00 103.15 ? 79  ASP A C   1 
ATOM   629  O  O   . ASP A 1 79  ? 11.271  5.082   39.484 1.00 94.39  ? 79  ASP A O   1 
ATOM   630  C  CB  . ASP A 1 79  ? 9.822   4.301   36.903 1.00 107.34 ? 79  ASP A CB  1 
ATOM   631  C  CG  . ASP A 1 79  ? 9.962   5.472   35.936 1.00 120.53 ? 79  ASP A CG  1 
ATOM   632  O  OD1 . ASP A 1 79  ? 9.092   5.607   35.051 1.00 124.86 ? 79  ASP A OD1 1 
ATOM   633  O  OD2 . ASP A 1 79  ? 10.922  6.263   36.058 1.00 129.61 ? 79  ASP A OD2 1 
ATOM   634  N  N   . ARG A 1 80  ? 12.879  5.462   37.943 1.00 109.60 ? 80  ARG A N   1 
ATOM   635  C  CA  . ARG A 1 80  ? 13.555  6.444   38.784 1.00 116.83 ? 80  ARG A CA  1 
ATOM   636  C  C   . ARG A 1 80  ? 12.780  7.753   38.865 1.00 120.34 ? 80  ARG A C   1 
ATOM   637  O  O   . ARG A 1 80  ? 12.845  8.447   39.886 1.00 121.93 ? 80  ARG A O   1 
ATOM   638  C  CB  . ARG A 1 80  ? 14.968  6.700   38.261 1.00 121.19 ? 80  ARG A CB  1 
ATOM   639  C  CG  . ARG A 1 80  ? 15.762  5.441   37.948 1.00 118.35 ? 80  ARG A CG  1 
ATOM   640  C  CD  . ARG A 1 80  ? 17.246  5.651   38.215 1.00 126.21 ? 80  ARG A CD  1 
ATOM   641  N  NE  . ARG A 1 80  ? 17.619  7.062   38.135 1.00 135.79 ? 80  ARG A NE  1 
ATOM   642  C  CZ  . ARG A 1 80  ? 18.268  7.609   37.112 1.00 140.88 ? 80  ARG A CZ  1 
ATOM   643  N  NH1 . ARG A 1 80  ? 18.623  6.863   36.074 1.00 141.42 ? 80  ARG A NH1 1 
ATOM   644  N  NH2 . ARG A 1 80  ? 18.564  8.902   37.127 1.00 142.04 ? 80  ARG A NH2 1 
ATOM   645  N  N   . ARG A 1 81  ? 12.039  8.104   37.812 1.00 122.77 ? 81  ARG A N   1 
ATOM   646  C  CA  . ARG A 1 81  ? 11.360  9.396   37.778 1.00 120.84 ? 81  ARG A CA  1 
ATOM   647  C  C   . ARG A 1 81  ? 10.146  9.411   38.701 1.00 109.96 ? 81  ARG A C   1 
ATOM   648  O  O   . ARG A 1 81  ? 10.017  10.293  39.559 1.00 103.82 ? 81  ARG A O   1 
ATOM   649  C  CB  . ARG A 1 81  ? 10.958  9.734   36.342 1.00 123.30 ? 81  ARG A CB  1 
ATOM   650  C  CG  . ARG A 1 81  ? 10.275  11.081  36.179 1.00 119.22 ? 81  ARG A CG  1 
ATOM   651  C  CD  . ARG A 1 81  ? 9.570   11.170  34.835 1.00 119.69 ? 81  ARG A CD  1 
ATOM   652  N  NE  . ARG A 1 81  ? 8.486   10.198  34.730 1.00 118.78 ? 81  ARG A NE  1 
ATOM   653  C  CZ  . ARG A 1 81  ? 7.206   10.517  34.568 1.00 116.39 ? 81  ARG A CZ  1 
ATOM   654  N  NH1 . ARG A 1 81  ? 6.842   11.788  34.486 1.00 117.68 ? 81  ARG A NH1 1 
ATOM   655  N  NH2 . ARG A 1 81  ? 6.289   9.562   34.485 1.00 111.96 ? 81  ARG A NH2 1 
ATOM   656  N  N   . THR A 1 82  ? 9.240   8.446   38.540 1.00 104.52 ? 82  THR A N   1 
ATOM   657  C  CA  . THR A 1 82  ? 8.036   8.389   39.358 1.00 103.15 ? 82  THR A CA  1 
ATOM   658  C  C   . THR A 1 82  ? 8.219   7.587   40.639 1.00 101.35 ? 82  THR A C   1 
ATOM   659  O  O   . THR A 1 82  ? 7.338   7.630   41.505 1.00 95.32  ? 82  THR A O   1 
ATOM   660  C  CB  . THR A 1 82  ? 6.868   7.799   38.555 1.00 105.72 ? 82  THR A CB  1 
ATOM   661  O  OG1 . THR A 1 82  ? 5.790   7.480   39.443 1.00 108.19 ? 82  THR A OG1 1 
ATOM   662  C  CG2 . THR A 1 82  ? 7.298   6.540   37.830 1.00 105.68 ? 82  THR A CG2 1 
ATOM   663  N  N   . ARG A 1 83  ? 9.330   6.860   40.773 1.00 105.53 ? 83  ARG A N   1 
ATOM   664  C  CA  . ARG A 1 83  ? 9.632   6.057   41.960 1.00 103.91 ? 83  ARG A CA  1 
ATOM   665  C  C   . ARG A 1 83  ? 8.617   4.935   42.169 1.00 95.42  ? 83  ARG A C   1 
ATOM   666  O  O   . ARG A 1 83  ? 8.399   4.479   43.294 1.00 89.87  ? 83  ARG A O   1 
ATOM   667  C  CB  . ARG A 1 83  ? 9.738   6.932   43.213 1.00 108.96 ? 83  ARG A CB  1 
ATOM   668  C  CG  . ARG A 1 83  ? 11.126  7.503   43.433 1.00 123.17 ? 83  ARG A CG  1 
ATOM   669  C  CD  . ARG A 1 83  ? 11.820  6.790   44.573 1.00 137.32 ? 83  ARG A CD  1 
ATOM   670  N  NE  . ARG A 1 83  ? 10.967  6.736   45.754 1.00 148.99 ? 83  ARG A NE  1 
ATOM   671  C  CZ  . ARG A 1 83  ? 11.412  6.527   46.988 1.00 157.39 ? 83  ARG A CZ  1 
ATOM   672  N  NH1 . ARG A 1 83  ? 12.705  6.344   47.211 1.00 161.69 ? 83  ARG A NH1 1 
ATOM   673  N  NH2 . ARG A 1 83  ? 10.559  6.500   47.998 1.00 162.24 ? 83  ARG A NH2 1 
ATOM   674  N  N   . ALA A 1 84  ? 7.996   4.475   41.087 1.00 95.49  ? 84  ALA A N   1 
ATOM   675  C  CA  . ALA A 1 84  ? 7.073   3.354   41.148 1.00 89.67  ? 84  ALA A CA  1 
ATOM   676  C  C   . ALA A 1 84  ? 7.816   2.047   40.905 1.00 91.11  ? 84  ALA A C   1 
ATOM   677  O  O   . ALA A 1 84  ? 8.776   1.988   40.132 1.00 91.76  ? 84  ALA A O   1 
ATOM   678  C  CB  . ALA A 1 84  ? 5.951   3.516   40.122 1.00 84.69  ? 84  ALA A CB  1 
ATOM   679  N  N   . VAL A 1 85  ? 7.361   0.993   41.579 1.00 89.82  ? 85  VAL A N   1 
ATOM   680  C  CA  . VAL A 1 85  ? 7.958   -0.329  41.452 1.00 87.69  ? 85  VAL A CA  1 
ATOM   681  C  C   . VAL A 1 85  ? 6.874   -1.336  41.103 1.00 81.39  ? 85  VAL A C   1 
ATOM   682  O  O   . VAL A 1 85  ? 5.695   -1.149  41.417 1.00 81.51  ? 85  VAL A O   1 
ATOM   683  C  CB  . VAL A 1 85  ? 8.696   -0.764  42.738 1.00 87.47  ? 85  VAL A CB  1 
ATOM   684  C  CG1 . VAL A 1 85  ? 9.929   0.084   42.954 1.00 92.29  ? 85  VAL A CG1 1 
ATOM   685  C  CG2 . VAL A 1 85  ? 7.772   -0.680  43.938 1.00 83.16  ? 85  VAL A CG2 1 
ATOM   686  N  N   . GLU A 1 86  ? 7.287   -2.412  40.440 1.00 79.45  ? 86  GLU A N   1 
ATOM   687  C  CA  . GLU A 1 86  ? 6.410   -3.539  40.174 1.00 75.41  ? 86  GLU A CA  1 
ATOM   688  C  C   . GLU A 1 86  ? 7.248   -4.807  40.190 1.00 73.59  ? 86  GLU A C   1 
ATOM   689  O  O   . GLU A 1 86  ? 8.438   -4.787  39.862 1.00 75.91  ? 86  GLU A O   1 
ATOM   690  C  CB  . GLU A 1 86  ? 5.666   -3.389  38.839 1.00 71.38  ? 86  GLU A CB  1 
ATOM   691  C  CG  . GLU A 1 86  ? 6.555   -3.381  37.610 1.00 74.43  ? 86  GLU A CG  1 
ATOM   692  C  CD  . GLU A 1 86  ? 5.806   -2.964  36.359 1.00 85.89  ? 86  GLU A CD  1 
ATOM   693  O  OE1 . GLU A 1 86  ? 5.586   -3.824  35.480 1.00 90.40  ? 86  GLU A OE1 1 
ATOM   694  O  OE2 . GLU A 1 86  ? 5.436   -1.775  36.255 1.00 91.39  ? 86  GLU A OE2 1 
ATOM   695  N  N   . LEU A 1 87  ? 6.618   -5.908  40.589 1.00 69.14  ? 87  LEU A N   1 
ATOM   696  C  CA  . LEU A 1 87  ? 7.304   -7.189  40.719 1.00 68.79  ? 87  LEU A CA  1 
ATOM   697  C  C   . LEU A 1 87  ? 6.306   -8.291  40.409 1.00 70.72  ? 87  LEU A C   1 
ATOM   698  O  O   . LEU A 1 87  ? 5.238   -8.348  41.026 1.00 68.43  ? 87  LEU A O   1 
ATOM   699  C  CB  . LEU A 1 87  ? 7.883   -7.355  42.126 1.00 68.90  ? 87  LEU A CB  1 
ATOM   700  C  CG  . LEU A 1 87  ? 8.581   -8.671  42.469 1.00 69.63  ? 87  LEU A CG  1 
ATOM   701  C  CD1 . LEU A 1 87  ? 9.881   -8.399  43.208 1.00 72.00  ? 87  LEU A CD1 1 
ATOM   702  C  CD2 . LEU A 1 87  ? 7.672   -9.562  43.300 1.00 65.74  ? 87  LEU A CD2 1 
ATOM   703  N  N   . VAL A 1 88  ? 6.647   -9.159  39.458 1.00 77.76  ? 88  VAL A N   1 
ATOM   704  C  CA  . VAL A 1 88  ? 5.753   -10.217 39.001 1.00 75.55  ? 88  VAL A CA  1 
ATOM   705  C  C   . VAL A 1 88  ? 6.491   -11.548 39.081 1.00 78.94  ? 88  VAL A C   1 
ATOM   706  O  O   . VAL A 1 88  ? 7.571   -11.699 38.498 1.00 90.25  ? 88  VAL A O   1 
ATOM   707  C  CB  . VAL A 1 88  ? 5.247   -9.965  37.571 1.00 70.53  ? 88  VAL A CB  1 
ATOM   708  C  CG1 . VAL A 1 88  ? 4.283   -11.057 37.152 1.00 70.89  ? 88  VAL A CG1 1 
ATOM   709  C  CG2 . VAL A 1 88  ? 4.581   -8.599  37.476 1.00 65.57  ? 88  VAL A CG2 1 
ATOM   710  N  N   . LEU A 1 89  ? 5.910   -12.505 39.801 1.00 73.07  ? 89  LEU A N   1 
ATOM   711  C  CA  . LEU A 1 89  ? 6.417   -13.867 39.884 1.00 67.88  ? 89  LEU A CA  1 
ATOM   712  C  C   . LEU A 1 89  ? 5.292   -14.833 39.539 1.00 68.08  ? 89  LEU A C   1 
ATOM   713  O  O   . LEU A 1 89  ? 4.140   -14.433 39.347 1.00 70.38  ? 89  LEU A O   1 
ATOM   714  C  CB  . LEU A 1 89  ? 6.979   -14.174 41.278 1.00 66.80  ? 89  LEU A CB  1 
ATOM   715  C  CG  . LEU A 1 89  ? 8.145   -13.307 41.754 1.00 71.70  ? 89  LEU A CG  1 
ATOM   716  C  CD1 . LEU A 1 89  ? 8.391   -13.518 43.239 1.00 58.99  ? 89  LEU A CD1 1 
ATOM   717  C  CD2 . LEU A 1 89  ? 9.405   -13.601 40.952 1.00 58.08  ? 89  LEU A CD2 1 
ATOM   718  N  N   . TRP A 1 90  ? 5.624   -16.120 39.457 1.00 70.93  ? 90  TRP A N   1 
ATOM   719  C  CA  . TRP A 1 90  ? 4.612   -17.125 39.162 1.00 74.37  ? 90  TRP A CA  1 
ATOM   720  C  C   . TRP A 1 90  ? 5.007   -18.459 39.780 1.00 83.37  ? 90  TRP A C   1 
ATOM   721  O  O   . TRP A 1 90  ? 6.118   -18.638 40.285 1.00 81.23  ? 90  TRP A O   1 
ATOM   722  C  CB  . TRP A 1 90  ? 4.372   -17.258 37.654 1.00 69.14  ? 90  TRP A CB  1 
ATOM   723  C  CG  . TRP A 1 90  ? 5.419   -18.016 36.906 1.00 65.61  ? 90  TRP A CG  1 
ATOM   724  C  CD1 . TRP A 1 90  ? 6.720   -17.653 36.721 1.00 65.33  ? 90  TRP A CD1 1 
ATOM   725  C  CD2 . TRP A 1 90  ? 5.244   -19.256 36.211 1.00 70.65  ? 90  TRP A CD2 1 
ATOM   726  N  NE1 . TRP A 1 90  ? 7.371   -18.597 35.964 1.00 64.50  ? 90  TRP A NE1 1 
ATOM   727  C  CE2 . TRP A 1 90  ? 6.487   -19.591 35.637 1.00 71.62  ? 90  TRP A CE2 1 
ATOM   728  C  CE3 . TRP A 1 90  ? 4.160   -20.119 36.024 1.00 73.94  ? 90  TRP A CE3 1 
ATOM   729  C  CZ2 . TRP A 1 90  ? 6.676   -20.754 34.892 1.00 76.45  ? 90  TRP A CZ2 1 
ATOM   730  C  CZ3 . TRP A 1 90  ? 4.349   -21.273 35.282 1.00 72.86  ? 90  TRP A CZ3 1 
ATOM   731  C  CH2 . TRP A 1 90  ? 5.597   -21.579 34.725 1.00 76.86  ? 90  TRP A CH2 1 
ATOM   732  N  N   . ASN A 1 91  ? 4.061   -19.401 39.722 1.00 90.55  ? 91  ASN A N   1 
ATOM   733  C  CA  . ASN A 1 91  ? 4.155   -20.641 40.488 1.00 83.33  ? 91  ASN A CA  1 
ATOM   734  C  C   . ASN A 1 91  ? 5.232   -21.576 39.959 1.00 79.98  ? 91  ASN A C   1 
ATOM   735  O  O   . ASN A 1 91  ? 5.803   -22.356 40.730 1.00 76.39  ? 91  ASN A O   1 
ATOM   736  C  CB  . ASN A 1 91  ? 2.809   -21.363 40.464 1.00 81.88  ? 91  ASN A CB  1 
ATOM   737  C  CG  . ASN A 1 91  ? 2.162   -21.430 41.822 1.00 94.46  ? 91  ASN A CG  1 
ATOM   738  O  OD1 . ASN A 1 91  ? 2.803   -21.171 42.838 1.00 113.53 ? 91  ASN A OD1 1 
ATOM   739  N  ND2 . ASN A 1 91  ? 0.884   -21.783 41.850 1.00 95.95  ? 91  ASN A ND2 1 
ATOM   740  N  N   . GLY A 1 92  ? 5.516   -21.525 38.660 1.00 78.43  ? 92  GLY A N   1 
ATOM   741  C  CA  . GLY A 1 92  ? 6.224   -22.594 37.999 1.00 75.15  ? 92  GLY A CA  1 
ATOM   742  C  C   . GLY A 1 92  ? 5.327   -23.714 37.518 1.00 74.65  ? 92  GLY A C   1 
ATOM   743  O  O   . GLY A 1 92  ? 5.792   -24.586 36.771 1.00 69.43  ? 92  GLY A O   1 
ATOM   744  N  N   . GLU A 1 93  ? 4.060   -23.717 37.925 1.00 72.69  ? 93  GLU A N   1 
ATOM   745  C  CA  . GLU A 1 93  ? 3.070   -24.666 37.438 1.00 73.12  ? 93  GLU A CA  1 
ATOM   746  C  C   . GLU A 1 93  ? 2.304   -24.032 36.285 1.00 78.48  ? 93  GLU A C   1 
ATOM   747  O  O   . GLU A 1 93  ? 1.740   -22.943 36.433 1.00 82.80  ? 93  GLU A O   1 
ATOM   748  C  CB  . GLU A 1 93  ? 2.111   -25.079 38.554 1.00 72.87  ? 93  GLU A CB  1 
ATOM   749  C  CG  . GLU A 1 93  ? 1.737   -26.555 38.541 1.00 79.35  ? 93  GLU A CG  1 
ATOM   750  C  CD  . GLU A 1 93  ? 1.237   -27.017 37.187 1.00 82.46  ? 93  GLU A CD  1 
ATOM   751  O  OE1 . GLU A 1 93  ? 1.742   -28.041 36.681 1.00 81.98  ? 93  GLU A OE1 1 
ATOM   752  O  OE2 . GLU A 1 93  ? 0.343   -26.352 36.626 1.00 85.05  ? 93  GLU A OE2 1 
ATOM   753  N  N   . GLU A 1 94  ? 2.285   -24.718 35.143 1.00 82.77  ? 94  GLU A N   1 
ATOM   754  C  CA  . GLU A 1 94  ? 1.691   -24.149 33.938 1.00 84.85  ? 94  GLU A CA  1 
ATOM   755  C  C   . GLU A 1 94  ? 0.166   -24.194 33.974 1.00 83.70  ? 94  GLU A C   1 
ATOM   756  O  O   . GLU A 1 94  ? -0.494  -23.253 33.521 1.00 84.72  ? 94  GLU A O   1 
ATOM   757  C  CB  . GLU A 1 94  ? 2.218   -24.887 32.707 1.00 92.43  ? 94  GLU A CB  1 
ATOM   758  C  CG  . GLU A 1 94  ? 1.588   -24.457 31.396 1.00 106.48 ? 94  GLU A CG  1 
ATOM   759  C  CD  . GLU A 1 94  ? 1.904   -25.413 30.263 1.00 113.27 ? 94  GLU A CD  1 
ATOM   760  O  OE1 . GLU A 1 94  ? 2.728   -26.328 30.471 1.00 112.44 ? 94  GLU A OE1 1 
ATOM   761  O  OE2 . GLU A 1 94  ? 1.329   -25.248 29.166 1.00 116.58 ? 94  GLU A OE2 1 
ATOM   762  N  N   . ASP A 1 95  ? -0.409  -25.269 34.511 1.00 83.71  ? 95  ASP A N   1 
ATOM   763  C  CA  . ASP A 1 95  ? -1.850  -25.483 34.441 1.00 79.67  ? 95  ASP A CA  1 
ATOM   764  C  C   . ASP A 1 95  ? -2.545  -24.775 35.596 1.00 81.97  ? 95  ASP A C   1 
ATOM   765  O  O   . ASP A 1 95  ? -2.232  -25.061 36.760 1.00 85.76  ? 95  ASP A O   1 
ATOM   766  C  CB  . ASP A 1 95  ? -2.170  -26.968 34.478 1.00 78.12  ? 95  ASP A CB  1 
ATOM   767  C  CG  . ASP A 1 95  ? -3.623  -27.264 34.158 1.00 86.48  ? 95  ASP A CG  1 
ATOM   768  O  OD1 . ASP A 1 95  ? -4.347  -26.340 33.732 1.00 91.67  ? 95  ASP A OD1 1 
ATOM   769  O  OD2 . ASP A 1 95  ? -4.042  -28.427 34.332 1.00 95.03  ? 95  ASP A OD2 1 
ATOM   770  N  N   . PRO A 1 96  ? -3.480  -23.859 35.332 1.00 77.04  ? 96  PRO A N   1 
ATOM   771  C  CA  . PRO A 1 96  ? -4.267  -23.283 36.435 1.00 79.43  ? 96  PRO A CA  1 
ATOM   772  C  C   . PRO A 1 96  ? -5.085  -24.312 37.194 1.00 84.14  ? 96  PRO A C   1 
ATOM   773  O  O   . PRO A 1 96  ? -5.379  -24.104 38.378 1.00 90.89  ? 96  PRO A O   1 
ATOM   774  C  CB  . PRO A 1 96  ? -5.166  -22.260 35.725 1.00 77.85  ? 96  PRO A CB  1 
ATOM   775  C  CG  . PRO A 1 96  ? -4.441  -21.932 34.459 1.00 73.67  ? 96  PRO A CG  1 
ATOM   776  C  CD  . PRO A 1 96  ? -3.754  -23.196 34.045 1.00 68.31  ? 96  PRO A CD  1 
ATOM   777  N  N   . LEU A 1 97  ? -5.465  -25.419 36.552 1.00 84.01  ? 97  LEU A N   1 
ATOM   778  C  CA  . LEU A 1 97  ? -6.249  -26.438 37.242 1.00 85.14  ? 97  LEU A CA  1 
ATOM   779  C  C   . LEU A 1 97  ? -5.440  -27.130 38.331 1.00 88.42  ? 97  LEU A C   1 
ATOM   780  O  O   . LEU A 1 97  ? -6.003  -27.546 39.350 1.00 92.91  ? 97  LEU A O   1 
ATOM   781  C  CB  . LEU A 1 97  ? -6.775  -27.466 36.242 1.00 83.35  ? 97  LEU A CB  1 
ATOM   782  C  CG  . LEU A 1 97  ? -7.760  -26.947 35.194 1.00 81.83  ? 97  LEU A CG  1 
ATOM   783  C  CD1 . LEU A 1 97  ? -8.047  -28.013 34.146 1.00 81.35  ? 97  LEU A CD1 1 
ATOM   784  C  CD2 . LEU A 1 97  ? -9.043  -26.484 35.863 1.00 83.65  ? 97  LEU A CD2 1 
ATOM   785  N  N   . LYS A 1 98  ? -4.129  -27.260 38.138 1.00 90.35  ? 98  LYS A N   1 
ATOM   786  C  CA  . LYS A 1 98  ? -3.254  -27.921 39.094 1.00 88.47  ? 98  LYS A CA  1 
ATOM   787  C  C   . LYS A 1 98  ? -2.607  -26.945 40.071 1.00 84.85  ? 98  LYS A C   1 
ATOM   788  O  O   . LYS A 1 98  ? -1.592  -27.284 40.692 1.00 81.87  ? 98  LYS A O   1 
ATOM   789  C  CB  . LYS A 1 98  ? -2.179  -28.721 38.353 1.00 85.20  ? 98  LYS A CB  1 
ATOM   790  C  CG  . LYS A 1 98  ? -2.729  -29.598 37.235 1.00 84.47  ? 98  LYS A CG  1 
ATOM   791  C  CD  . LYS A 1 98  ? -1.888  -30.847 37.038 1.00 90.23  ? 98  LYS A CD  1 
ATOM   792  C  CE  . LYS A 1 98  ? -0.572  -30.524 36.353 1.00 97.42  ? 98  LYS A CE  1 
ATOM   793  N  NZ  . LYS A 1 98  ? -0.773  -30.155 34.924 1.00 101.14 ? 98  LYS A NZ  1 
ATOM   794  N  N   . GLY A 1 99  ? -3.164  -25.748 40.217 1.00 84.92  ? 99  GLY A N   1 
ATOM   795  C  CA  . GLY A 1 99  ? -2.644  -24.767 41.144 1.00 85.44  ? 99  GLY A CA  1 
ATOM   796  C  C   . GLY A 1 99  ? -1.748  -23.701 40.550 1.00 80.91  ? 99  GLY A C   1 
ATOM   797  O  O   . GLY A 1 99  ? -1.139  -22.943 41.313 1.00 79.71  ? 99  GLY A O   1 
ATOM   798  N  N   . GLY A 1 100 ? -1.643  -23.619 39.225 1.00 78.52  ? 100 GLY A N   1 
ATOM   799  C  CA  . GLY A 1 100 ? -0.833  -22.591 38.597 1.00 80.53  ? 100 GLY A CA  1 
ATOM   800  C  C   . GLY A 1 100 ? -1.337  -21.199 38.913 1.00 87.02  ? 100 GLY A C   1 
ATOM   801  O  O   . GLY A 1 100 ? -2.531  -20.924 38.768 1.00 93.68  ? 100 GLY A O   1 
ATOM   802  N  N   . LEU A 1 101 ? -0.442  -20.309 39.336 1.00 83.70  ? 101 LEU A N   1 
ATOM   803  C  CA  . LEU A 1 101 ? -0.868  -19.010 39.834 1.00 85.71  ? 101 LEU A CA  1 
ATOM   804  C  C   . LEU A 1 101 ? 0.313   -18.048 39.848 1.00 79.01  ? 101 LEU A C   1 
ATOM   805  O  O   . LEU A 1 101 ? 1.417   -18.418 40.252 1.00 77.71  ? 101 LEU A O   1 
ATOM   806  C  CB  . LEU A 1 101 ? -1.477  -19.151 41.236 1.00 85.86  ? 101 LEU A CB  1 
ATOM   807  C  CG  . LEU A 1 101 ? -1.749  -17.892 42.053 1.00 90.28  ? 101 LEU A CG  1 
ATOM   808  C  CD1 . LEU A 1 101 ? -3.031  -17.259 41.587 1.00 101.50 ? 101 LEU A CD1 1 
ATOM   809  C  CD2 . LEU A 1 101 ? -1.860  -18.244 43.527 1.00 85.82  ? 101 LEU A CD2 1 
ATOM   810  N  N   . SER A 1 102 ? 0.066   -16.816 39.417 1.00 73.79  ? 102 SER A N   1 
ATOM   811  C  CA  . SER A 1 102 ? 1.088   -15.781 39.386 1.00 74.00  ? 102 SER A CA  1 
ATOM   812  C  C   . SER A 1 102 ? 0.874   -14.776 40.512 1.00 75.42  ? 102 SER A C   1 
ATOM   813  O  O   . SER A 1 102 ? -0.201  -14.693 41.113 1.00 79.33  ? 102 SER A O   1 
ATOM   814  C  CB  . SER A 1 102 ? 1.092   -15.059 38.036 1.00 77.82  ? 102 SER A CB  1 
ATOM   815  O  OG  . SER A 1 102 ? -0.121  -14.357 37.820 1.00 77.02  ? 102 SER A OG  1 
ATOM   816  N  N   . LEU A 1 103 ? 1.923   -14.006 40.789 1.00 70.75  ? 103 LEU A N   1 
ATOM   817  C  CA  . LEU A 1 103 ? 1.917   -12.996 41.839 1.00 73.04  ? 103 LEU A CA  1 
ATOM   818  C  C   . LEU A 1 103 ? 2.225   -11.647 41.210 1.00 75.15  ? 103 LEU A C   1 
ATOM   819  O  O   . LEU A 1 103 ? 3.280   -11.476 40.591 1.00 78.83  ? 103 LEU A O   1 
ATOM   820  C  CB  . LEU A 1 103 ? 2.937   -13.330 42.929 1.00 74.54  ? 103 LEU A CB  1 
ATOM   821  C  CG  . LEU A 1 103 ? 2.978   -12.412 44.152 1.00 75.61  ? 103 LEU A CG  1 
ATOM   822  C  CD1 . LEU A 1 103 ? 3.124   -13.236 45.420 1.00 74.01  ? 103 LEU A CD1 1 
ATOM   823  C  CD2 . LEU A 1 103 ? 4.105   -11.395 44.043 1.00 73.39  ? 103 LEU A CD2 1 
ATOM   824  N  N   . ASP A 1 104 ? 1.310   -10.694 41.372 1.00 74.96  ? 104 ASP A N   1 
ATOM   825  C  CA  . ASP A 1 104 ? 1.425   -9.368  40.771 1.00 73.71  ? 104 ASP A CA  1 
ATOM   826  C  C   . ASP A 1 104 ? 1.465   -8.335  41.889 1.00 80.77  ? 104 ASP A C   1 
ATOM   827  O  O   . ASP A 1 104 ? 0.458   -8.108  42.569 1.00 83.42  ? 104 ASP A O   1 
ATOM   828  C  CB  . ASP A 1 104 ? 0.263   -9.106  39.813 1.00 72.31  ? 104 ASP A CB  1 
ATOM   829  C  CG  . ASP A 1 104 ? 0.462   -7.861  38.970 1.00 78.01  ? 104 ASP A CG  1 
ATOM   830  O  OD1 . ASP A 1 104 ? 0.787   -6.794  39.531 1.00 82.61  ? 104 ASP A OD1 1 
ATOM   831  O  OD2 . ASP A 1 104 ? 0.282   -7.949  37.737 1.00 80.58  ? 104 ASP A OD2 1 
ATOM   832  N  N   . TYR A 1 105 ? 2.622   -7.704  42.068 1.00 78.45  ? 105 TYR A N   1 
ATOM   833  C  CA  . TYR A 1 105 ? 2.832   -6.707  43.110 1.00 81.75  ? 105 TYR A CA  1 
ATOM   834  C  C   . TYR A 1 105 ? 3.294   -5.416  42.454 1.00 87.00  ? 105 TYR A C   1 
ATOM   835  O  O   . TYR A 1 105 ? 4.359   -5.382  41.828 1.00 97.54  ? 105 TYR A O   1 
ATOM   836  C  CB  . TYR A 1 105 ? 3.859   -7.194  44.134 1.00 85.98  ? 105 TYR A CB  1 
ATOM   837  C  CG  . TYR A 1 105 ? 4.244   -6.167  45.178 1.00 88.03  ? 105 TYR A CG  1 
ATOM   838  C  CD1 . TYR A 1 105 ? 3.415   -5.904  46.261 1.00 91.21  ? 105 TYR A CD1 1 
ATOM   839  C  CD2 . TYR A 1 105 ? 5.443   -5.470  45.086 1.00 84.01  ? 105 TYR A CD2 1 
ATOM   840  C  CE1 . TYR A 1 105 ? 3.766   -4.971  47.220 1.00 90.94  ? 105 TYR A CE1 1 
ATOM   841  C  CE2 . TYR A 1 105 ? 5.802   -4.536  46.039 1.00 87.05  ? 105 TYR A CE2 1 
ATOM   842  C  CZ  . TYR A 1 105 ? 4.960   -4.291  47.104 1.00 91.72  ? 105 TYR A CZ  1 
ATOM   843  O  OH  . TYR A 1 105 ? 5.313   -3.363  48.056 1.00 98.20  ? 105 TYR A OH  1 
ATOM   844  N  N   . GLU A 1 106 ? 2.496   -4.362  42.593 1.00 87.55  ? 106 GLU A N   1 
ATOM   845  C  CA  . GLU A 1 106 ? 2.814   -3.072  42.002 1.00 89.00  ? 106 GLU A CA  1 
ATOM   846  C  C   . GLU A 1 106 ? 2.568   -1.976  43.026 1.00 93.91  ? 106 GLU A C   1 
ATOM   847  O  O   . GLU A 1 106 ? 1.570   -2.006  43.751 1.00 96.45  ? 106 GLU A O   1 
ATOM   848  C  CB  . GLU A 1 106 ? 1.981   -2.814  40.741 1.00 75.80  ? 106 GLU A CB  1 
ATOM   849  C  CG  . GLU A 1 106 ? 2.357   -1.550  39.992 1.00 77.22  ? 106 GLU A CG  1 
ATOM   850  C  CD  . GLU A 1 106 ? 1.389   -1.243  38.869 1.00 86.71  ? 106 GLU A CD  1 
ATOM   851  O  OE1 . GLU A 1 106 ? 0.457   -2.048  38.664 1.00 87.86  ? 106 GLU A OE1 1 
ATOM   852  O  OE2 . GLU A 1 106 ? 1.553   -0.198  38.201 1.00 84.56  ? 106 GLU A OE2 1 
ATOM   853  N  N   . ALA A 1 107 ? 3.489   -1.011  43.082 1.00 90.77  ? 107 ALA A N   1 
ATOM   854  C  CA  . ALA A 1 107 ? 3.405   0.111   44.011 1.00 91.87  ? 107 ALA A CA  1 
ATOM   855  C  C   . ALA A 1 107 ? 3.576   1.408   43.218 1.00 95.91  ? 107 ALA A C   1 
ATOM   856  O  O   . ALA A 1 107 ? 4.592   2.098   43.323 1.00 102.08 ? 107 ALA A O   1 
ATOM   857  C  CB  . ALA A 1 107 ? 4.446   -0.012  45.124 1.00 88.32  ? 107 ALA A CB  1 
ATOM   858  N  N   . SER A 1 108 ? 2.571   1.733   42.411 1.00 95.85  ? 108 SER A N   1 
ATOM   859  C  CA  . SER A 1 108 ? 2.574   2.995   41.694 1.00 101.35 ? 108 SER A CA  1 
ATOM   860  C  C   . SER A 1 108 ? 2.029   4.107   42.587 1.00 109.22 ? 108 SER A C   1 
ATOM   861  O  O   . SER A 1 108 ? 1.509   3.868   43.681 1.00 119.22 ? 108 SER A O   1 
ATOM   862  C  CB  . SER A 1 108 ? 1.752   2.887   40.412 1.00 100.78 ? 108 SER A CB  1 
ATOM   863  O  OG  . SER A 1 108 ? 0.405   3.253   40.648 1.00 103.64 ? 108 SER A OG  1 
ATOM   864  N  N   . GLY A 1 109 ? 2.151   5.345   42.105 1.00 104.57 ? 109 GLY A N   1 
ATOM   865  C  CA  . GLY A 1 109 ? 1.686   6.484   42.877 1.00 113.44 ? 109 GLY A CA  1 
ATOM   866  C  C   . GLY A 1 109 ? 0.185   6.534   43.071 1.00 114.94 ? 109 GLY A C   1 
ATOM   867  O  O   . GLY A 1 109 ? -0.289  7.248   43.961 1.00 119.17 ? 109 GLY A O   1 
ATOM   868  N  N   . ARG A 1 110 ? -0.571  5.795   42.265 1.00 108.29 ? 110 ARG A N   1 
ATOM   869  C  CA  . ARG A 1 110 ? -2.024  5.804   42.323 1.00 104.28 ? 110 ARG A CA  1 
ATOM   870  C  C   . ARG A 1 110 ? -2.535  4.621   43.138 1.00 102.87 ? 110 ARG A C   1 
ATOM   871  O  O   . ARG A 1 110 ? -1.932  3.545   43.155 1.00 102.47 ? 110 ARG A O   1 
ATOM   872  C  CB  . ARG A 1 110 ? -2.623  5.768   40.914 1.00 109.72 ? 110 ARG A CB  1 
ATOM   873  C  CG  . ARG A 1 110 ? -2.268  6.979   40.059 1.00 115.09 ? 110 ARG A CG  1 
ATOM   874  C  CD  . ARG A 1 110 ? -2.125  6.604   38.591 1.00 119.17 ? 110 ARG A CD  1 
ATOM   875  N  NE  . ARG A 1 110 ? -0.997  5.704   38.366 1.00 126.44 ? 110 ARG A NE  1 
ATOM   876  C  CZ  . ARG A 1 110 ? -0.610  5.272   37.169 1.00 126.12 ? 110 ARG A CZ  1 
ATOM   877  N  NH1 . ARG A 1 110 ? -1.259  5.659   36.079 1.00 132.29 ? 110 ARG A NH1 1 
ATOM   878  N  NH2 . ARG A 1 110 ? 0.428   4.453   37.062 1.00 114.13 ? 110 ARG A NH2 1 
ATOM   879  N  N   . ALA A 1 111 ? -3.665  4.836   43.818 1.00 106.36 ? 111 ALA A N   1 
ATOM   880  C  CA  . ALA A 1 111 ? -4.249  3.788   44.647 1.00 107.00 ? 111 ALA A CA  1 
ATOM   881  C  C   . ALA A 1 111 ? -4.820  2.642   43.823 1.00 109.19 ? 111 ALA A C   1 
ATOM   882  O  O   . ALA A 1 111 ? -4.968  1.533   44.346 1.00 111.37 ? 111 ALA A O   1 
ATOM   883  C  CB  . ALA A 1 111 ? -5.340  4.373   45.545 1.00 111.96 ? 111 ALA A CB  1 
ATOM   884  N  N   . VAL A 1 112 ? -5.144  2.882   42.551 1.00 111.57 ? 112 VAL A N   1 
ATOM   885  C  CA  . VAL A 1 112 ? -5.691  1.818   41.718 1.00 112.58 ? 112 VAL A CA  1 
ATOM   886  C  C   . VAL A 1 112 ? -4.611  0.805   41.355 1.00 115.23 ? 112 VAL A C   1 
ATOM   887  O  O   . VAL A 1 112 ? -4.909  -0.373  41.121 1.00 110.35 ? 112 VAL A O   1 
ATOM   888  C  CB  . VAL A 1 112 ? -6.353  2.415   40.461 1.00 110.78 ? 112 VAL A CB  1 
ATOM   889  C  CG1 . VAL A 1 112 ? -7.272  1.397   39.803 1.00 107.00 ? 112 VAL A CG1 1 
ATOM   890  C  CG2 . VAL A 1 112 ? -7.118  3.683   40.816 1.00 117.12 ? 112 VAL A CG2 1 
ATOM   891  N  N   . SER A 1 113 ? -3.347  1.233   41.310 1.00 120.35 ? 113 SER A N   1 
ATOM   892  C  CA  . SER A 1 113 ? -2.244  0.367   40.910 1.00 122.03 ? 113 SER A CA  1 
ATOM   893  C  C   . SER A 1 113 ? -1.256  0.118   42.044 1.00 123.51 ? 113 SER A C   1 
ATOM   894  O  O   . SER A 1 113 ? -0.117  -0.286  41.791 1.00 127.64 ? 113 SER A O   1 
ATOM   895  C  CB  . SER A 1 113 ? -1.519  0.952   39.697 1.00 126.48 ? 113 SER A CB  1 
ATOM   896  O  OG  . SER A 1 113 ? -2.394  1.059   38.591 1.00 132.90 ? 113 SER A OG  1 
ATOM   897  N  N   . SER A 1 114 ? -1.660  0.358   43.286 1.00 117.45 ? 114 SER A N   1 
ATOM   898  C  CA  . SER A 1 114 ? -0.870  0.006   44.464 1.00 107.75 ? 114 SER A CA  1 
ATOM   899  C  C   . SER A 1 114 ? -1.554  -1.207  45.088 1.00 105.58 ? 114 SER A C   1 
ATOM   900  O  O   . SER A 1 114 ? -2.391  -1.075  45.983 1.00 107.89 ? 114 SER A O   1 
ATOM   901  C  CB  . SER A 1 114 ? -0.771  1.175   45.442 1.00 106.47 ? 114 SER A CB  1 
ATOM   902  O  OG  . SER A 1 114 ? -0.002  2.233   44.896 1.00 102.04 ? 114 SER A OG  1 
ATOM   903  N  N   . ARG A 1 115 ? -1.197  -2.395  44.602 1.00 99.99  ? 115 ARG A N   1 
ATOM   904  C  CA  . ARG A 1 115 ? -1.943  -3.596  44.944 1.00 96.05  ? 115 ARG A CA  1 
ATOM   905  C  C   . ARG A 1 115 ? -1.043  -4.821  44.872 1.00 97.54  ? 115 ARG A C   1 
ATOM   906  O  O   . ARG A 1 115 ? 0.018   -4.808  44.242 1.00 100.03 ? 115 ARG A O   1 
ATOM   907  C  CB  . ARG A 1 115 ? -3.140  -3.790  44.007 1.00 94.61  ? 115 ARG A CB  1 
ATOM   908  C  CG  . ARG A 1 115 ? -2.748  -4.348  42.646 1.00 102.12 ? 115 ARG A CG  1 
ATOM   909  C  CD  . ARG A 1 115 ? -3.620  -3.801  41.531 1.00 113.78 ? 115 ARG A CD  1 
ATOM   910  N  NE  . ARG A 1 115 ? -5.018  -4.193  41.682 1.00 120.03 ? 115 ARG A NE  1 
ATOM   911  C  CZ  . ARG A 1 115 ? -5.919  -4.133  40.705 1.00 125.01 ? 115 ARG A CZ  1 
ATOM   912  N  NH1 . ARG A 1 115 ? -5.570  -3.696  39.503 1.00 121.89 ? 115 ARG A NH1 1 
ATOM   913  N  NH2 . ARG A 1 115 ? -7.169  -4.510  40.931 1.00 130.06 ? 115 ARG A NH2 1 
ATOM   914  N  N   . LEU A 1 116 ? -1.496  -5.883  45.536 1.00 95.05  ? 116 LEU A N   1 
ATOM   915  C  CA  . LEU A 1 116 ? -0.963  -7.230  45.389 1.00 87.72  ? 116 LEU A CA  1 
ATOM   916  C  C   . LEU A 1 116 ? -2.115  -8.130  44.969 1.00 91.87  ? 116 LEU A C   1 
ATOM   917  O  O   . LEU A 1 116 ? -3.153  -8.157  45.637 1.00 100.47 ? 116 LEU A O   1 
ATOM   918  C  CB  . LEU A 1 116 ? -0.344  -7.731  46.701 1.00 84.01  ? 116 LEU A CB  1 
ATOM   919  C  CG  . LEU A 1 116 ? 0.704   -8.855  46.720 1.00 82.22  ? 116 LEU A CG  1 
ATOM   920  C  CD1 . LEU A 1 116 ? 1.079   -9.185  48.159 1.00 82.30  ? 116 LEU A CD1 1 
ATOM   921  C  CD2 . LEU A 1 116 ? 0.253   -10.120 45.996 1.00 79.91  ? 116 LEU A CD2 1 
ATOM   922  N  N   . GLN A 1 117 ? -1.939  -8.863  43.872 1.00 89.01  ? 117 GLN A N   1 
ATOM   923  C  CA  . GLN A 1 117 ? -2.992  -9.740  43.385 1.00 91.61  ? 117 GLN A CA  1 
ATOM   924  C  C   . GLN A 1 117 ? -2.418  -11.098 43.008 1.00 89.12  ? 117 GLN A C   1 
ATOM   925  O  O   . GLN A 1 117 ? -1.301  -11.192 42.491 1.00 94.80  ? 117 GLN A O   1 
ATOM   926  C  CB  . GLN A 1 117 ? -3.726  -9.128  42.185 1.00 96.49  ? 117 GLN A CB  1 
ATOM   927  C  CG  . GLN A 1 117 ? -2.849  -8.295  41.273 1.00 102.83 ? 117 GLN A CG  1 
ATOM   928  C  CD  . GLN A 1 117 ? -3.625  -7.665  40.133 1.00 105.92 ? 117 GLN A CD  1 
ATOM   929  O  OE1 . GLN A 1 117 ? -4.636  -8.204  39.684 1.00 109.54 ? 117 GLN A OE1 1 
ATOM   930  N  NE2 . GLN A 1 117 ? -3.151  -6.522  39.655 1.00 106.80 ? 117 GLN A NE2 1 
ATOM   931  N  N   . LEU A 1 118 ? -3.194  -12.147 43.283 1.00 82.82  ? 118 LEU A N   1 
ATOM   932  C  CA  . LEU A 1 118 ? -2.866  -13.515 42.891 1.00 74.74  ? 118 LEU A CA  1 
ATOM   933  C  C   . LEU A 1 118 ? -3.806  -13.917 41.762 1.00 76.41  ? 118 LEU A C   1 
ATOM   934  O  O   . LEU A 1 118 ? -5.025  -13.983 41.954 1.00 78.30  ? 118 LEU A O   1 
ATOM   935  C  CB  . LEU A 1 118 ? -2.976  -14.476 44.071 1.00 71.73  ? 118 LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 118 ? -2.054  -14.184 45.253 1.00 72.81  ? 118 LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 118 ? -2.185  -15.260 46.320 1.00 69.91  ? 118 LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 118 ? -0.614  -14.060 44.782 1.00 74.91  ? 118 LEU A CD2 1 
ATOM   939  N  N   . GLU A 1 119 ? -3.235  -14.192 40.594 1.00 78.43  ? 119 GLU A N   1 
ATOM   940  C  CA  . GLU A 1 119 ? -3.976  -14.378 39.352 1.00 81.80  ? 119 GLU A CA  1 
ATOM   941  C  C   . GLU A 1 119 ? -3.656  -15.758 38.790 1.00 81.38  ? 119 GLU A C   1 
ATOM   942  O  O   . GLU A 1 119 ? -2.496  -16.044 38.473 1.00 84.67  ? 119 GLU A O   1 
ATOM   943  C  CB  . GLU A 1 119 ? -3.601  -13.262 38.369 1.00 81.58  ? 119 GLU A CB  1 
ATOM   944  C  CG  . GLU A 1 119 ? -4.072  -13.414 36.938 1.00 84.33  ? 119 GLU A CG  1 
ATOM   945  C  CD  . GLU A 1 119 ? -5.563  -13.238 36.794 1.00 99.32  ? 119 GLU A CD  1 
ATOM   946  O  OE1 . GLU A 1 119 ? -6.323  -13.738 37.646 1.00 106.41 ? 119 GLU A OE1 1 
ATOM   947  O  OE2 . GLU A 1 119 ? -5.975  -12.557 35.839 1.00 102.01 ? 119 GLU A OE2 1 
ATOM   948  N  N   . ASP A 1 120 ? -4.662  -16.633 38.709 1.00 95.56  ? 120 ASP A N   1 
ATOM   949  C  CA  . ASP A 1 120 ? -6.037  -16.385 39.167 1.00 94.42  ? 120 ASP A CA  1 
ATOM   950  C  C   . ASP A 1 120 ? -6.306  -17.146 40.464 1.00 94.46  ? 120 ASP A C   1 
ATOM   951  O  O   . ASP A 1 120 ? -5.921  -18.305 40.596 1.00 97.48  ? 120 ASP A O   1 
ATOM   952  C  CB  . ASP A 1 120 ? -7.041  -16.808 38.088 1.00 96.77  ? 120 ASP A CB  1 
ATOM   953  C  CG  . ASP A 1 120 ? -8.483  -16.500 38.460 1.00 100.86 ? 120 ASP A CG  1 
ATOM   954  O  OD1 . ASP A 1 120 ? -8.977  -17.057 39.463 1.00 99.81  ? 120 ASP A OD1 1 
ATOM   955  O  OD2 . ASP A 1 120 ? -9.136  -15.720 37.732 1.00 105.09 ? 120 ASP A OD2 1 
ATOM   956  N  N   . ALA A 1 121 ? -7.008  -16.505 41.401 1.00 95.51  ? 121 ALA A N   1 
ATOM   957  C  CA  . ALA A 1 121 ? -7.240  -17.102 42.712 1.00 93.65  ? 121 ALA A CA  1 
ATOM   958  C  C   . ALA A 1 121 ? -8.087  -18.368 42.656 1.00 99.31  ? 121 ALA A C   1 
ATOM   959  O  O   . ALA A 1 121 ? -8.119  -19.109 43.644 1.00 98.16  ? 121 ALA A O   1 
ATOM   960  C  CB  . ALA A 1 121 ? -7.898  -16.085 43.644 1.00 93.31  ? 121 ALA A CB  1 
ATOM   961  N  N   . GLY A 1 122 ? -8.775  -18.632 41.542 1.00 102.58 ? 122 GLY A N   1 
ATOM   962  C  CA  . GLY A 1 122 ? -9.532  -19.865 41.418 1.00 101.96 ? 122 GLY A CA  1 
ATOM   963  C  C   . GLY A 1 122 ? -8.673  -21.112 41.371 1.00 95.37  ? 122 GLY A C   1 
ATOM   964  O  O   . GLY A 1 122 ? -9.180  -22.213 41.612 1.00 101.06 ? 122 GLY A O   1 
ATOM   965  N  N   . SER A 1 123 ? -7.383  -20.964 41.062 1.00 86.62  ? 123 SER A N   1 
ATOM   966  C  CA  . SER A 1 123 ? -6.485  -22.112 41.069 1.00 84.38  ? 123 SER A CA  1 
ATOM   967  C  C   . SER A 1 123 ? -6.270  -22.633 42.483 1.00 86.90  ? 123 SER A C   1 
ATOM   968  O  O   . SER A 1 123 ? -6.172  -23.847 42.694 1.00 93.60  ? 123 SER A O   1 
ATOM   969  C  CB  . SER A 1 123 ? -5.152  -21.736 40.428 1.00 84.76  ? 123 SER A CB  1 
ATOM   970  O  OG  . SER A 1 123 ? -5.325  -21.423 39.057 1.00 91.16  ? 123 SER A OG  1 
ATOM   971  N  N   . LEU A 1 124 ? -6.198  -21.731 43.466 1.00 81.59  ? 124 LEU A N   1 
ATOM   972  C  CA  . LEU A 1 124 ? -6.047  -22.147 44.854 1.00 84.67  ? 124 LEU A CA  1 
ATOM   973  C  C   . LEU A 1 124 ? -7.273  -22.887 45.374 1.00 93.75  ? 124 LEU A C   1 
ATOM   974  O  O   . LEU A 1 124 ? -7.155  -23.671 46.323 1.00 94.19  ? 124 LEU A O   1 
ATOM   975  C  CB  . LEU A 1 124 ? -5.757  -20.937 45.740 1.00 85.07  ? 124 LEU A CB  1 
ATOM   976  C  CG  . LEU A 1 124 ? -4.438  -20.208 45.479 1.00 84.34  ? 124 LEU A CG  1 
ATOM   977  C  CD1 . LEU A 1 124 ? -4.387  -18.913 46.271 1.00 86.00  ? 124 LEU A CD1 1 
ATOM   978  C  CD2 . LEU A 1 124 ? -3.250  -21.093 45.816 1.00 73.73  ? 124 LEU A CD2 1 
ATOM   979  N  N   . LEU A 1 125 ? -8.445  -22.652 44.781 1.00 97.85  ? 125 LEU A N   1 
ATOM   980  C  CA  . LEU A 1 125 ? -9.639  -23.382 45.191 1.00 98.67  ? 125 LEU A CA  1 
ATOM   981  C  C   . LEU A 1 125 ? -9.577  -24.842 44.766 1.00 102.23 ? 125 LEU A C   1 
ATOM   982  O  O   . LEU A 1 125 ? -10.127 -25.711 45.451 1.00 106.64 ? 125 LEU A O   1 
ATOM   983  C  CB  . LEU A 1 125 ? -10.883 -22.716 44.610 1.00 91.19  ? 125 LEU A CB  1 
ATOM   984  C  CG  . LEU A 1 125 ? -11.412 -21.504 45.373 1.00 89.34  ? 125 LEU A CG  1 
ATOM   985  C  CD1 . LEU A 1 125 ? -12.878 -21.300 45.056 1.00 95.86  ? 125 LEU A CD1 1 
ATOM   986  C  CD2 . LEU A 1 125 ? -11.211 -21.680 46.868 1.00 83.83  ? 125 LEU A CD2 1 
ATOM   987  N  N   . GLN A 1 126 ? -8.914  -25.129 43.654 1.00 101.56 ? 126 GLN A N   1 
ATOM   988  C  CA  . GLN A 1 126 ? -8.769  -26.492 43.167 1.00 100.80 ? 126 GLN A CA  1 
ATOM   989  C  C   . GLN A 1 126 ? -7.715  -27.296 43.913 1.00 102.95 ? 126 GLN A C   1 
ATOM   990  O  O   . GLN A 1 126 ? -7.349  -28.386 43.445 1.00 106.17 ? 126 GLN A O   1 
ATOM   991  C  CB  . GLN A 1 126 ? -8.420  -26.479 41.678 1.00 99.37  ? 126 GLN A CB  1 
ATOM   992  C  CG  . GLN A 1 126 ? -9.564  -26.104 40.761 1.00 104.18 ? 126 GLN A CG  1 
ATOM   993  C  CD  . GLN A 1 126 ? -9.809  -27.160 39.697 1.00 108.37 ? 126 GLN A CD  1 
ATOM   994  O  OE1 . GLN A 1 126 ? -8.910  -27.926 39.353 1.00 108.84 ? 126 GLN A OE1 1 
ATOM   995  N  NE2 . GLN A 1 126 ? -11.036 -27.226 39.193 1.00 113.95 ? 126 GLN A NE2 1 
ATOM   996  N  N   . VAL A 1 127 ? -7.219  -26.816 45.053 1.00 100.88 ? 127 VAL A N   1 
ATOM   997  C  CA  . VAL A 1 127 ? -6.063  -27.476 45.649 1.00 101.33 ? 127 VAL A CA  1 
ATOM   998  C  C   . VAL A 1 127 ? -6.062  -27.366 47.177 1.00 106.72 ? 127 VAL A C   1 
ATOM   999  O  O   . VAL A 1 127 ? -5.587  -28.268 47.884 1.00 112.87 ? 127 VAL A O   1 
ATOM   1000 C  CB  . VAL A 1 127 ? -4.779  -26.882 45.040 1.00 98.47  ? 127 VAL A CB  1 
ATOM   1001 C  CG1 . VAL A 1 127 ? -4.807  -25.376 45.109 1.00 98.08  ? 127 VAL A CG1 1 
ATOM   1002 C  CG2 . VAL A 1 127 ? -3.558  -27.378 45.736 1.00 102.98 ? 127 VAL A CG2 1 
ATOM   1003 N  N   . PHE A 1 128 ? -6.604  -26.273 47.708 1.00 106.45 ? 128 PHE A N   1 
ATOM   1004 C  CA  . PHE A 1 128 ? -6.709  -26.142 49.156 1.00 111.62 ? 128 PHE A CA  1 
ATOM   1005 C  C   . PHE A 1 128 ? -7.712  -27.147 49.712 1.00 117.93 ? 128 PHE A C   1 
ATOM   1006 O  O   . PHE A 1 128 ? -8.825  -27.278 49.196 1.00 114.24 ? 128 PHE A O   1 
ATOM   1007 C  CB  . PHE A 1 128 ? -7.121  -24.723 49.531 1.00 109.23 ? 128 PHE A CB  1 
ATOM   1008 C  CG  . PHE A 1 128 ? -5.969  -23.749 49.586 1.00 104.92 ? 128 PHE A CG  1 
ATOM   1009 C  CD1 . PHE A 1 128 ? -4.677  -24.184 49.841 1.00 103.64 ? 128 PHE A CD1 1 
ATOM   1010 C  CD2 . PHE A 1 128 ? -6.183  -22.392 49.392 1.00 104.10 ? 128 PHE A CD2 1 
ATOM   1011 C  CE1 . PHE A 1 128 ? -3.622  -23.285 49.887 1.00 100.94 ? 128 PHE A CE1 1 
ATOM   1012 C  CE2 . PHE A 1 128 ? -5.142  -21.495 49.439 1.00 104.20 ? 128 PHE A CE2 1 
ATOM   1013 C  CZ  . PHE A 1 128 ? -3.856  -21.939 49.687 1.00 102.47 ? 128 PHE A CZ  1 
ATOM   1014 N  N   . ASP A 1 129 ? -7.323  -27.851 50.779 1.00 124.60 ? 129 ASP A N   1 
ATOM   1015 C  CA  . ASP A 1 129 ? -8.261  -28.736 51.468 1.00 133.43 ? 129 ASP A CA  1 
ATOM   1016 C  C   . ASP A 1 129 ? -9.342  -27.931 52.179 1.00 135.55 ? 129 ASP A C   1 
ATOM   1017 O  O   . ASP A 1 129 ? -10.530 -28.033 51.851 1.00 138.18 ? 129 ASP A O   1 
ATOM   1018 C  CB  . ASP A 1 129 ? -7.524  -29.639 52.467 1.00 140.70 ? 129 ASP A CB  1 
ATOM   1019 C  CG  . ASP A 1 129 ? -6.570  -30.601 51.789 1.00 147.57 ? 129 ASP A CG  1 
ATOM   1020 O  OD1 . ASP A 1 129 ? -6.882  -31.047 50.663 1.00 149.84 ? 129 ASP A OD1 1 
ATOM   1021 O  OD2 . ASP A 1 129 ? -5.511  -30.908 52.376 1.00 150.15 ? 129 ASP A OD2 1 
ATOM   1022 N  N   . ALA A 1 130 ? -8.943  -27.133 53.171 1.00 135.00 ? 130 ALA A N   1 
ATOM   1023 C  CA  . ALA A 1 130 ? -9.829  -26.181 53.823 1.00 132.88 ? 130 ALA A CA  1 
ATOM   1024 C  C   . ALA A 1 130 ? -9.534  -24.800 53.257 1.00 125.55 ? 130 ALA A C   1 
ATOM   1025 O  O   . ALA A 1 130 ? -8.566  -24.154 53.685 1.00 126.22 ? 130 ALA A O   1 
ATOM   1026 C  CB  . ALA A 1 130 ? -9.628  -26.198 55.341 1.00 135.97 ? 130 ALA A CB  1 
ATOM   1027 N  N   . PRO A 1 131 ? -10.312 -24.310 52.287 1.00 119.33 ? 131 PRO A N   1 
ATOM   1028 C  CA  . PRO A 1 131 ? -9.968  -23.022 51.658 1.00 112.88 ? 131 PRO A CA  1 
ATOM   1029 C  C   . PRO A 1 131 ? -10.031 -21.843 52.612 1.00 112.98 ? 131 PRO A C   1 
ATOM   1030 O  O   . PRO A 1 131 ? -9.190  -20.941 52.524 1.00 114.39 ? 131 PRO A O   1 
ATOM   1031 C  CB  . PRO A 1 131 ? -11.005 -22.899 50.530 1.00 110.10 ? 131 PRO A CB  1 
ATOM   1032 C  CG  . PRO A 1 131 ? -11.520 -24.292 50.316 1.00 109.62 ? 131 PRO A CG  1 
ATOM   1033 C  CD  . PRO A 1 131 ? -11.486 -24.936 51.662 1.00 117.67 ? 131 PRO A CD  1 
ATOM   1034 N  N   . ALA A 1 132 ? -11.003 -21.823 53.526 1.00 113.34 ? 132 ALA A N   1 
ATOM   1035 C  CA  . ALA A 1 132 ? -11.147 -20.686 54.430 1.00 112.55 ? 132 ALA A CA  1 
ATOM   1036 C  C   . ALA A 1 132 ? -9.935  -20.549 55.345 1.00 117.70 ? 132 ALA A C   1 
ATOM   1037 O  O   . ALA A 1 132 ? -9.399  -19.450 55.523 1.00 122.08 ? 132 ALA A O   1 
ATOM   1038 C  CB  . ALA A 1 132 ? -12.430 -20.826 55.249 1.00 109.19 ? 132 ALA A CB  1 
ATOM   1039 N  N   . SER A 1 133 ? -9.484  -21.661 55.931 1.00 117.98 ? 133 SER A N   1 
ATOM   1040 C  CA  . SER A 1 133 ? -8.349  -21.603 56.847 1.00 123.13 ? 133 SER A CA  1 
ATOM   1041 C  C   . SER A 1 133 ? -7.072  -21.191 56.124 1.00 118.38 ? 133 SER A C   1 
ATOM   1042 O  O   . SER A 1 133 ? -6.267  -20.423 56.665 1.00 119.35 ? 133 SER A O   1 
ATOM   1043 C  CB  . SER A 1 133 ? -8.161  -22.954 57.536 1.00 133.81 ? 133 SER A CB  1 
ATOM   1044 O  OG  . SER A 1 133 ? -7.608  -23.907 56.645 1.00 135.93 ? 133 SER A OG  1 
ATOM   1045 N  N   . SER A 1 134 ? -6.870  -21.687 54.902 1.00 115.36 ? 134 SER A N   1 
ATOM   1046 C  CA  . SER A 1 134 ? -5.673  -21.337 54.147 1.00 108.94 ? 134 SER A CA  1 
ATOM   1047 C  C   . SER A 1 134 ? -5.747  -19.929 53.568 1.00 110.65 ? 134 SER A C   1 
ATOM   1048 O  O   . SER A 1 134 ? -4.720  -19.250 53.471 1.00 110.01 ? 134 SER A O   1 
ATOM   1049 C  CB  . SER A 1 134 ? -5.443  -22.349 53.023 1.00 102.98 ? 134 SER A CB  1 
ATOM   1050 O  OG  . SER A 1 134 ? -5.312  -23.664 53.532 1.00 104.93 ? 134 SER A OG  1 
ATOM   1051 N  N   . PHE A 1 135 ? -6.940  -19.474 53.180 1.00 109.26 ? 135 PHE A N   1 
ATOM   1052 C  CA  . PHE A 1 135 ? -7.050  -18.153 52.572 1.00 106.07 ? 135 PHE A CA  1 
ATOM   1053 C  C   . PHE A 1 135 ? -6.864  -17.042 53.597 1.00 100.96 ? 135 PHE A C   1 
ATOM   1054 O  O   . PHE A 1 135 ? -6.252  -16.014 53.285 1.00 98.01  ? 135 PHE A O   1 
ATOM   1055 C  CB  . PHE A 1 135 ? -8.394  -18.009 51.859 1.00 109.89 ? 135 PHE A CB  1 
ATOM   1056 C  CG  . PHE A 1 135 ? -8.321  -18.277 50.387 1.00 106.83 ? 135 PHE A CG  1 
ATOM   1057 C  CD1 . PHE A 1 135 ? -7.275  -17.772 49.634 1.00 104.25 ? 135 PHE A CD1 1 
ATOM   1058 C  CD2 . PHE A 1 135 ? -9.292  -19.036 49.755 1.00 104.39 ? 135 PHE A CD2 1 
ATOM   1059 C  CE1 . PHE A 1 135 ? -7.200  -18.013 48.276 1.00 99.97  ? 135 PHE A CE1 1 
ATOM   1060 C  CE2 . PHE A 1 135 ? -9.224  -19.282 48.396 1.00 101.17 ? 135 PHE A CE2 1 
ATOM   1061 C  CZ  . PHE A 1 135 ? -8.176  -18.771 47.655 1.00 98.99  ? 135 PHE A CZ  1 
ATOM   1062 N  N   . VAL A 1 136 ? -7.371  -17.227 54.820 1.00 95.25  ? 136 VAL A N   1 
ATOM   1063 C  CA  . VAL A 1 136 ? -7.160  -16.216 55.851 1.00 95.19  ? 136 VAL A CA  1 
ATOM   1064 C  C   . VAL A 1 136 ? -5.710  -16.215 56.311 1.00 93.28  ? 136 VAL A C   1 
ATOM   1065 O  O   . VAL A 1 136 ? -5.204  -15.190 56.785 1.00 98.04  ? 136 VAL A O   1 
ATOM   1066 C  CB  . VAL A 1 136 ? -8.117  -16.428 57.041 1.00 96.90  ? 136 VAL A CB  1 
ATOM   1067 C  CG1 . VAL A 1 136 ? -9.567  -16.356 56.588 1.00 97.19  ? 136 VAL A CG1 1 
ATOM   1068 C  CG2 . VAL A 1 136 ? -7.822  -17.747 57.742 1.00 97.57  ? 136 VAL A CG2 1 
ATOM   1069 N  N   . ALA A 1 137 ? -5.019  -17.350 56.185 1.00 88.41  ? 137 ALA A N   1 
ATOM   1070 C  CA  . ALA A 1 137 ? -3.630  -17.417 56.625 1.00 88.20  ? 137 ALA A CA  1 
ATOM   1071 C  C   . ALA A 1 137 ? -2.746  -16.487 55.808 1.00 97.95  ? 137 ALA A C   1 
ATOM   1072 O  O   . ALA A 1 137 ? -1.811  -15.878 56.345 1.00 103.76 ? 137 ALA A O   1 
ATOM   1073 C  CB  . ALA A 1 137 ? -3.117  -18.853 56.540 1.00 80.49  ? 137 ALA A CB  1 
ATOM   1074 N  N   . ILE A 1 138 ? -3.028  -16.365 54.508 1.00 97.22  ? 138 ILE A N   1 
ATOM   1075 C  CA  . ILE A 1 138 ? -2.227  -15.488 53.662 1.00 101.53 ? 138 ILE A CA  1 
ATOM   1076 C  C   . ILE A 1 138 ? -2.745  -14.055 53.745 1.00 101.14 ? 138 ILE A C   1 
ATOM   1077 O  O   . ILE A 1 138 ? -2.034  -13.099 53.397 1.00 104.51 ? 138 ILE A O   1 
ATOM   1078 C  CB  . ILE A 1 138 ? -2.199  -16.021 52.217 1.00 109.79 ? 138 ILE A CB  1 
ATOM   1079 C  CG1 . ILE A 1 138 ? -3.566  -15.961 51.552 1.00 111.42 ? 138 ILE A CG1 1 
ATOM   1080 C  CG2 . ILE A 1 138 ? -1.762  -17.468 52.207 1.00 113.50 ? 138 ILE A CG2 1 
ATOM   1081 C  CD1 . ILE A 1 138 ? -3.652  -16.786 50.271 1.00 111.36 ? 138 ILE A CD1 1 
ATOM   1082 N  N   . PHE A 1 139 ? -3.978  -13.877 54.214 1.00 98.38  ? 139 PHE A N   1 
ATOM   1083 C  CA  . PHE A 1 139 ? -4.451  -12.561 54.611 1.00 100.63 ? 139 PHE A CA  1 
ATOM   1084 C  C   . PHE A 1 139 ? -3.629  -12.052 55.789 1.00 105.24 ? 139 PHE A C   1 
ATOM   1085 O  O   . PHE A 1 139 ? -2.878  -11.080 55.650 1.00 108.21 ? 139 PHE A O   1 
ATOM   1086 C  CB  . PHE A 1 139 ? -5.932  -12.609 54.972 1.00 99.82  ? 139 PHE A CB  1 
ATOM   1087 C  CG  . PHE A 1 139 ? -6.848  -12.291 53.823 1.00 104.99 ? 139 PHE A CG  1 
ATOM   1088 C  CD1 . PHE A 1 139 ? -7.012  -10.983 53.411 1.00 104.74 ? 139 PHE A CD1 1 
ATOM   1089 C  CD2 . PHE A 1 139 ? -7.559  -13.287 53.168 1.00 107.58 ? 139 PHE A CD2 1 
ATOM   1090 C  CE1 . PHE A 1 139 ? -7.848  -10.668 52.363 1.00 101.64 ? 139 PHE A CE1 1 
ATOM   1091 C  CE2 . PHE A 1 139 ? -8.404  -12.976 52.112 1.00 104.26 ? 139 PHE A CE2 1 
ATOM   1092 C  CZ  . PHE A 1 139 ? -8.546  -11.663 51.712 1.00 98.77  ? 139 PHE A CZ  1 
ATOM   1093 N  N   . LEU A 1 140 ? -3.765  -12.707 56.953 1.00 105.45 ? 140 LEU A N   1 
ATOM   1094 C  CA  . LEU A 1 140 ? -3.033  -12.297 58.152 1.00 108.63 ? 140 LEU A CA  1 
ATOM   1095 C  C   . LEU A 1 140 ? -1.539  -12.180 57.893 1.00 102.89 ? 140 LEU A C   1 
ATOM   1096 O  O   . LEU A 1 140 ? -0.863  -11.385 58.558 1.00 102.00 ? 140 LEU A O   1 
ATOM   1097 C  CB  . LEU A 1 140 ? -3.289  -13.279 59.305 1.00 109.10 ? 140 LEU A CB  1 
ATOM   1098 C  CG  . LEU A 1 140 ? -2.467  -13.112 60.593 1.00 110.77 ? 140 LEU A CG  1 
ATOM   1099 C  CD1 . LEU A 1 140 ? -3.327  -13.329 61.827 1.00 112.18 ? 140 LEU A CD1 1 
ATOM   1100 C  CD2 . LEU A 1 140 ? -1.243  -14.036 60.640 1.00 106.80 ? 140 LEU A CD2 1 
ATOM   1101 N  N   . ALA A 1 141 ? -1.007  -12.955 56.946 1.00 99.92  ? 141 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 141 ? 0.341   -12.700 56.456 1.00 101.73 ? 141 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 141 ? 0.432   -11.270 55.938 1.00 109.06 ? 141 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 141 ? 0.937   -10.397 56.656 1.00 119.94 ? 141 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 141 ? 0.747   -13.705 55.373 1.00 98.20  ? 141 ALA A CB  1 
ATOM   1106 N  N   . VAL A 1 142 ? -0.089  -11.032 54.722 1.00 107.24 ? 142 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 142 ? 0.001   -9.740  54.037 1.00 113.09 ? 142 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 142 ? -0.053  -8.582  55.013 1.00 117.12 ? 142 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 142 ? 0.767   -7.658  54.950 1.00 122.33 ? 142 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 142 ? -1.113  -9.624  52.969 1.00 111.19 ? 142 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 142 ? -1.310  -8.174  52.552 1.00 111.09 ? 142 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 142 ? -0.785  -10.478 51.750 1.00 108.92 ? 142 VAL A CG2 1 
ATOM   1113 N  N   . LEU A 1 143 ? -0.979  -8.635  55.955 1.00 112.28 ? 143 LEU A N   1 
ATOM   1114 C  CA  . LEU A 1 143 ? -1.180  -7.536  56.885 1.00 116.66 ? 143 LEU A CA  1 
ATOM   1115 C  C   . LEU A 1 143 ? -0.096  -7.437  57.957 1.00 123.95 ? 143 LEU A C   1 
ATOM   1116 O  O   . LEU A 1 143 ? 0.117   -6.351  58.513 1.00 139.38 ? 143 LEU A O   1 
ATOM   1117 C  CB  . LEU A 1 143 ? -2.551  -7.685  57.537 1.00 120.36 ? 143 LEU A CB  1 
ATOM   1118 C  CG  . LEU A 1 143 ? -3.295  -6.408  57.932 1.00 134.84 ? 143 LEU A CG  1 
ATOM   1119 C  CD1 . LEU A 1 143 ? -4.759  -6.758  58.009 1.00 139.04 ? 143 LEU A CD1 1 
ATOM   1120 C  CD2 . LEU A 1 143 ? -2.804  -5.834  59.253 1.00 143.03 ? 143 LEU A CD2 1 
ATOM   1121 N  N   . GLU A 1 144 ? 0.605   -8.529  58.252 1.00 123.85 ? 144 GLU A N   1 
ATOM   1122 C  CA  . GLU A 1 144 ? 1.726   -8.449  59.179 1.00 126.48 ? 144 GLU A CA  1 
ATOM   1123 C  C   . GLU A 1 144 ? 2.943   -7.814  58.522 1.00 130.11 ? 144 GLU A C   1 
ATOM   1124 O  O   . GLU A 1 144 ? 3.626   -6.995  59.145 1.00 131.63 ? 144 GLU A O   1 
ATOM   1125 C  CB  . GLU A 1 144 ? 2.072   -9.839  59.708 1.00 122.93 ? 144 GLU A CB  1 
ATOM   1126 C  CG  . GLU A 1 144 ? 3.446   -9.928  60.348 1.00 127.35 ? 144 GLU A CG  1 
ATOM   1127 C  CD  . GLU A 1 144 ? 3.664   -11.231 61.081 1.00 134.33 ? 144 GLU A CD  1 
ATOM   1128 O  OE1 . GLU A 1 144 ? 4.830   -11.528 61.411 1.00 138.04 ? 144 GLU A OE1 1 
ATOM   1129 O  OE2 . GLU A 1 144 ? 2.675   -11.957 61.320 1.00 135.90 ? 144 GLU A OE2 1 
ATOM   1130 N  N   . ILE A 1 145 ? 3.228   -8.170  57.265 1.00 128.99 ? 145 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 145 ? 4.414   -7.627  56.610 1.00 128.58 ? 145 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 145 ? 4.154   -6.224  56.051 1.00 127.54 ? 145 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 145 ? 5.043   -5.364  56.091 1.00 135.38 ? 145 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 145 ? 4.939   -8.579  55.515 1.00 131.29 ? 145 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 145 ? 4.967   -10.047 55.989 1.00 129.26 ? 145 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 145 ? 6.325   -8.140  55.074 1.00 140.04 ? 145 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 145 ? 3.907   -10.954 55.403 1.00 124.22 ? 145 ILE A CD1 1 
ATOM   1138 N  N   . TRP A 1 146 ? 2.949   -5.954  55.542 1.00 125.64 ? 146 TRP A N   1 
ATOM   1139 C  CA  . TRP A 1 146 ? 2.621   -4.640  54.988 1.00 113.83 ? 146 TRP A CA  1 
ATOM   1140 C  C   . TRP A 1 146 ? 1.659   -3.905  55.915 1.00 114.18 ? 146 TRP A C   1 
ATOM   1141 O  O   . TRP A 1 146 ? 0.440   -4.129  55.846 1.00 107.97 ? 146 TRP A O   1 
ATOM   1142 C  CB  . TRP A 1 146 ? 2.011   -4.778  53.587 1.00 104.68 ? 146 TRP A CB  1 
ATOM   1143 C  CG  . TRP A 1 146 ? 3.016   -4.984  52.485 1.00 102.10 ? 146 TRP A CG  1 
ATOM   1144 C  CD1 . TRP A 1 146 ? 3.853   -4.046  51.954 1.00 102.21 ? 146 TRP A CD1 1 
ATOM   1145 C  CD2 . TRP A 1 146 ? 3.288   -6.204  51.784 1.00 103.20 ? 146 TRP A CD2 1 
ATOM   1146 N  NE1 . TRP A 1 146 ? 4.629   -4.605  50.968 1.00 109.40 ? 146 TRP A NE1 1 
ATOM   1147 C  CE2 . TRP A 1 146 ? 4.302   -5.929  50.844 1.00 106.73 ? 146 TRP A CE2 1 
ATOM   1148 C  CE3 . TRP A 1 146 ? 2.774   -7.503  51.860 1.00 100.51 ? 146 TRP A CE3 1 
ATOM   1149 C  CZ2 . TRP A 1 146 ? 4.810   -6.902  49.990 1.00 104.43 ? 146 TRP A CZ2 1 
ATOM   1150 C  CZ3 . TRP A 1 146 ? 3.280   -8.466  51.012 1.00 102.15 ? 146 TRP A CZ3 1 
ATOM   1151 C  CH2 . TRP A 1 146 ? 4.288   -8.161  50.090 1.00 104.64 ? 146 TRP A CH2 1 
ATOM   1152 N  N   . PRO A 1 147 ? 2.139   -3.018  56.793 1.00 111.95 ? 147 PRO A N   1 
ATOM   1153 C  CA  . PRO A 1 147 ? 1.205   -2.240  57.623 1.00 118.40 ? 147 PRO A CA  1 
ATOM   1154 C  C   . PRO A 1 147 ? 0.390   -1.232  56.832 1.00 123.12 ? 147 PRO A C   1 
ATOM   1155 O  O   . PRO A 1 147 ? -0.630  -0.752  57.342 1.00 113.07 ? 147 PRO A O   1 
ATOM   1156 C  CB  . PRO A 1 147 ? 2.126   -1.541  58.631 1.00 120.54 ? 147 PRO A CB  1 
ATOM   1157 C  CG  . PRO A 1 147 ? 3.446   -1.475  57.942 1.00 117.09 ? 147 PRO A CG  1 
ATOM   1158 C  CD  . PRO A 1 147 ? 3.544   -2.724  57.121 1.00 114.26 ? 147 PRO A CD  1 
ATOM   1159 N  N   . GLU A 1 148 ? 0.799   -0.904  55.606 1.00 122.20 ? 148 GLU A N   1 
ATOM   1160 C  CA  . GLU A 1 148 ? 0.110   0.086   54.786 1.00 125.46 ? 148 GLU A CA  1 
ATOM   1161 C  C   . GLU A 1 148 ? -1.125  -0.468  54.087 1.00 124.23 ? 148 GLU A C   1 
ATOM   1162 O  O   . GLU A 1 148 ? -1.675  0.212   53.216 1.00 131.29 ? 148 GLU A O   1 
ATOM   1163 C  CB  . GLU A 1 148 ? 1.065   0.667   53.738 1.00 126.02 ? 148 GLU A CB  1 
ATOM   1164 C  CG  . GLU A 1 148 ? 2.368   1.205   54.300 1.00 130.05 ? 148 GLU A CG  1 
ATOM   1165 C  CD  . GLU A 1 148 ? 3.457   0.157   54.329 1.00 133.27 ? 148 GLU A CD  1 
ATOM   1166 O  OE1 . GLU A 1 148 ? 3.122   -1.045  54.383 1.00 133.55 ? 148 GLU A OE1 1 
ATOM   1167 O  OE2 . GLU A 1 148 ? 4.650   0.527   54.294 1.00 137.20 ? 148 GLU A OE2 1 
ATOM   1168 N  N   . THR A 1 149 ? -1.571  -1.670  54.442 1.00 122.07 ? 149 THR A N   1 
ATOM   1169 C  CA  . THR A 1 149 ? -2.719  -2.278  53.782 1.00 115.17 ? 149 THR A CA  1 
ATOM   1170 C  C   . THR A 1 149 ? -3.984  -1.486  54.093 1.00 110.40 ? 149 THR A C   1 
ATOM   1171 O  O   . THR A 1 149 ? -4.375  -1.364  55.259 1.00 112.81 ? 149 THR A O   1 
ATOM   1172 C  CB  . THR A 1 149 ? -2.874  -3.730  54.227 1.00 116.27 ? 149 THR A CB  1 
ATOM   1173 O  OG1 . THR A 1 149 ? -1.635  -4.425  54.035 1.00 114.84 ? 149 THR A OG1 1 
ATOM   1174 C  CG2 . THR A 1 149 ? -3.966  -4.421  53.425 1.00 101.75 ? 149 THR A CG2 1 
ATOM   1175 N  N   . THR A 1 150 ? -4.623  -0.947  53.052 1.00 111.06 ? 150 THR A N   1 
ATOM   1176 C  CA  . THR A 1 150 ? -5.856  -0.184  53.221 1.00 115.11 ? 150 THR A CA  1 
ATOM   1177 C  C   . THR A 1 150 ? -7.104  -1.030  53.032 1.00 114.28 ? 150 THR A C   1 
ATOM   1178 O  O   . THR A 1 150 ? -8.141  -0.730  53.634 1.00 114.51 ? 150 THR A O   1 
ATOM   1179 C  CB  . THR A 1 150 ? -5.913  0.988   52.235 1.00 117.77 ? 150 THR A CB  1 
ATOM   1180 O  OG1 . THR A 1 150 ? -6.055  0.488   50.898 1.00 122.42 ? 150 THR A OG1 1 
ATOM   1181 C  CG2 . THR A 1 150 ? -4.657  1.830   52.328 1.00 118.14 ? 150 THR A CG2 1 
ATOM   1182 N  N   . TRP A 1 151 ? -7.035  -2.074  52.210 1.00 114.32 ? 151 TRP A N   1 
ATOM   1183 C  CA  . TRP A 1 151 ? -8.224  -2.841  51.875 1.00 113.09 ? 151 TRP A CA  1 
ATOM   1184 C  C   . TRP A 1 151 ? -7.815  -4.197  51.321 1.00 112.97 ? 151 TRP A C   1 
ATOM   1185 O  O   . TRP A 1 151 ? -6.727  -4.356  50.760 1.00 115.10 ? 151 TRP A O   1 
ATOM   1186 C  CB  . TRP A 1 151 ? -9.098  -2.096  50.858 1.00 111.22 ? 151 TRP A CB  1 
ATOM   1187 C  CG  . TRP A 1 151 ? -10.394 -2.784  50.550 1.00 109.56 ? 151 TRP A CG  1 
ATOM   1188 C  CD1 . TRP A 1 151 ? -10.622 -3.692  49.559 1.00 109.21 ? 151 TRP A CD1 1 
ATOM   1189 C  CD2 . TRP A 1 151 ? -11.641 -2.617  51.234 1.00 109.97 ? 151 TRP A CD2 1 
ATOM   1190 N  NE1 . TRP A 1 151 ? -11.930 -4.101  49.584 1.00 108.88 ? 151 TRP A NE1 1 
ATOM   1191 C  CE2 . TRP A 1 151 ? -12.577 -3.456  50.603 1.00 109.44 ? 151 TRP A CE2 1 
ATOM   1192 C  CE3 . TRP A 1 151 ? -12.054 -1.843  52.322 1.00 116.27 ? 151 TRP A CE3 1 
ATOM   1193 C  CZ2 . TRP A 1 151 ? -13.900 -3.541  51.019 1.00 112.29 ? 151 TRP A CZ2 1 
ATOM   1194 C  CZ3 . TRP A 1 151 ? -13.367 -1.936  52.740 1.00 116.63 ? 151 TRP A CZ3 1 
ATOM   1195 C  CH2 . TRP A 1 151 ? -14.276 -2.772  52.086 1.00 114.41 ? 151 TRP A CH2 1 
ATOM   1196 N  N   . GLY A 1 152 ? -8.706  -5.168  51.483 1.00 111.70 ? 152 GLY A N   1 
ATOM   1197 C  CA  . GLY A 1 152 ? -8.510  -6.478  50.896 1.00 107.25 ? 152 GLY A CA  1 
ATOM   1198 C  C   . GLY A 1 152 ? -9.843  -7.129  50.615 1.00 110.66 ? 152 GLY A C   1 
ATOM   1199 O  O   . GLY A 1 152 ? -10.867 -6.775  51.209 1.00 114.69 ? 152 GLY A O   1 
HETATM 1200 N  N   . MSE A 1 153 ? -9.821  -8.086  49.695 1.00 108.88 ? 153 MSE A N   1 
HETATM 1201 C  CA  . MSE A 1 153 ? -11.035 -8.792  49.319 1.00 113.45 ? 153 MSE A CA  1 
HETATM 1202 C  C   . MSE A 1 153 ? -10.744 -10.040 48.486 1.00 107.45 ? 153 MSE A C   1 
HETATM 1203 O  O   . MSE A 1 153 ? -9.801  -10.076 47.693 1.00 101.55 ? 153 MSE A O   1 
HETATM 1204 C  CB  . MSE A 1 153 ? -11.976 -7.858  48.549 1.00 118.92 ? 153 MSE A CB  1 
HETATM 1205 C  CG  . MSE A 1 153 ? -12.911 -8.578  47.601 1.00 125.54 ? 153 MSE A CG  1 
HETATM 1206 SE SE  . MSE A 1 153 ? -13.516 -7.500  46.111 0.60 133.02 ? 153 MSE A SE  1 
HETATM 1207 C  CE  . MSE A 1 153 ? -13.927 -8.966  44.904 1.00 129.30 ? 153 MSE A CE  1 
ATOM   1208 N  N   . LEU A 1 154 ? -11.569 -11.065 48.686 1.00 109.83 ? 154 LEU A N   1 
ATOM   1209 C  CA  . LEU A 1 154 ? -11.533 -12.287 47.896 1.00 105.71 ? 154 LEU A CA  1 
ATOM   1210 C  C   . LEU A 1 154 ? -12.956 -12.582 47.447 1.00 104.16 ? 154 LEU A C   1 
ATOM   1211 O  O   . LEU A 1 154 ? -13.848 -12.740 48.287 1.00 110.45 ? 154 LEU A O   1 
ATOM   1212 C  CB  . LEU A 1 154 ? -10.956 -13.437 48.727 1.00 111.75 ? 154 LEU A CB  1 
ATOM   1213 C  CG  . LEU A 1 154 ? -10.456 -14.746 48.117 1.00 114.20 ? 154 LEU A CG  1 
ATOM   1214 C  CD1 . LEU A 1 154 ? -9.955  -15.628 49.235 1.00 121.08 ? 154 LEU A CD1 1 
ATOM   1215 C  CD2 . LEU A 1 154 ? -11.521 -15.476 47.336 1.00 114.71 ? 154 LEU A CD2 1 
ATOM   1216 N  N   . ALA A 1 155 ? -13.179 -12.644 46.136 1.00 100.71 ? 155 ALA A N   1 
ATOM   1217 C  CA  . ALA A 1 155 ? -14.512 -12.869 45.604 1.00 104.80 ? 155 ALA A CA  1 
ATOM   1218 C  C   . ALA A 1 155 ? -14.398 -13.411 44.194 1.00 103.98 ? 155 ALA A C   1 
ATOM   1219 O  O   . ALA A 1 155 ? -13.326 -13.301 43.571 1.00 100.04 ? 155 ALA A O   1 
ATOM   1220 C  CB  . ALA A 1 155 ? -15.347 -11.577 45.623 1.00 103.93 ? 155 ALA A CB  1 
ATOM   1221 N  N   . PRO A 1 156 ? -15.451 -14.014 43.650 1.00 108.17 ? 156 PRO A N   1 
ATOM   1222 C  CA  . PRO A 1 156 ? -15.397 -14.543 42.288 1.00 109.91 ? 156 PRO A CA  1 
ATOM   1223 C  C   . PRO A 1 156 ? -15.344 -13.434 41.248 1.00 111.94 ? 156 PRO A C   1 
ATOM   1224 O  O   . PRO A 1 156 ? -15.694 -12.280 41.506 1.00 113.16 ? 156 PRO A O   1 
ATOM   1225 C  CB  . PRO A 1 156 ? -16.690 -15.352 42.153 1.00 113.71 ? 156 PRO A CB  1 
ATOM   1226 C  CG  . PRO A 1 156 ? -17.162 -15.578 43.552 1.00 113.68 ? 156 PRO A CG  1 
ATOM   1227 C  CD  . PRO A 1 156 ? -16.713 -14.390 44.329 1.00 110.65 ? 156 PRO A CD  1 
ATOM   1228 N  N   . HIS A 1 157 ? -14.924 -13.817 40.039 1.00 113.72 ? 157 HIS A N   1 
ATOM   1229 C  CA  . HIS A 1 157 ? -14.772 -12.838 38.968 1.00 111.78 ? 157 HIS A CA  1 
ATOM   1230 C  C   . HIS A 1 157 ? -16.123 -12.383 38.436 1.00 111.90 ? 157 HIS A C   1 
ATOM   1231 O  O   . HIS A 1 157 ? -16.342 -11.185 38.225 1.00 111.38 ? 157 HIS A O   1 
ATOM   1232 C  CB  . HIS A 1 157 ? -13.920 -13.416 37.839 1.00 114.30 ? 157 HIS A CB  1 
ATOM   1233 C  CG  . HIS A 1 157 ? -13.351 -12.378 36.923 1.00 118.86 ? 157 HIS A CG  1 
ATOM   1234 N  ND1 . HIS A 1 157 ? -14.134 -11.601 36.095 1.00 122.16 ? 157 HIS A ND1 1 
ATOM   1235 C  CD2 . HIS A 1 157 ? -12.075 -11.975 36.718 1.00 117.80 ? 157 HIS A CD2 1 
ATOM   1236 C  CE1 . HIS A 1 157 ? -13.363 -10.774 35.412 1.00 122.76 ? 157 HIS A CE1 1 
ATOM   1237 N  NE2 . HIS A 1 157 ? -12.109 -10.980 35.772 1.00 119.96 ? 157 HIS A NE2 1 
ATOM   1238 N  N   . ALA A 1 158 ? -17.043 -13.323 38.215 1.00 115.04 ? 158 ALA A N   1 
ATOM   1239 C  CA  . ALA A 1 158 ? -18.351 -12.955 37.686 1.00 117.09 ? 158 ALA A CA  1 
ATOM   1240 C  C   . ALA A 1 158 ? -19.129 -12.073 38.655 1.00 116.10 ? 158 ALA A C   1 
ATOM   1241 O  O   . ALA A 1 158 ? -19.981 -11.289 38.225 1.00 119.69 ? 158 ALA A O   1 
ATOM   1242 C  CB  . ALA A 1 158 ? -19.150 -14.213 37.355 1.00 122.60 ? 158 ALA A CB  1 
ATOM   1243 N  N   . TYR A 1 159 ? -18.854 -12.179 39.956 1.00 112.88 ? 159 TYR A N   1 
ATOM   1244 C  CA  . TYR A 1 159 ? -19.648 -11.440 40.931 1.00 117.08 ? 159 TYR A CA  1 
ATOM   1245 C  C   . TYR A 1 159 ? -19.256 -9.969  40.981 1.00 119.67 ? 159 TYR A C   1 
ATOM   1246 O  O   . TYR A 1 159 ? -20.116 -9.089  40.872 1.00 128.69 ? 159 TYR A O   1 
ATOM   1247 C  CB  . TYR A 1 159 ? -19.516 -12.072 42.318 1.00 118.62 ? 159 TYR A CB  1 
ATOM   1248 C  CG  . TYR A 1 159 ? -20.263 -11.309 43.392 1.00 119.14 ? 159 TYR A CG  1 
ATOM   1249 C  CD1 . TYR A 1 159 ? -21.652 -11.334 43.450 1.00 119.43 ? 159 TYR A CD1 1 
ATOM   1250 C  CD2 . TYR A 1 159 ? -19.582 -10.556 44.339 1.00 118.53 ? 159 TYR A CD2 1 
ATOM   1251 C  CE1 . TYR A 1 159 ? -22.339 -10.635 44.424 1.00 119.69 ? 159 TYR A CE1 1 
ATOM   1252 C  CE2 . TYR A 1 159 ? -20.262 -9.853  45.317 1.00 120.65 ? 159 TYR A CE2 1 
ATOM   1253 C  CZ  . TYR A 1 159 ? -21.639 -9.896  45.355 1.00 120.86 ? 159 TYR A CZ  1 
ATOM   1254 O  OH  . TYR A 1 159 ? -22.315 -9.197  46.329 1.00 125.24 ? 159 TYR A OH  1 
ATOM   1255 N  N   . PHE A 1 160 ? -17.965 -9.682  41.161 1.00 117.61 ? 160 PHE A N   1 
ATOM   1256 C  CA  . PHE A 1 160 ? -17.522 -8.294  41.244 1.00 117.07 ? 160 PHE A CA  1 
ATOM   1257 C  C   . PHE A 1 160 ? -17.757 -7.567  39.927 1.00 121.29 ? 160 PHE A C   1 
ATOM   1258 O  O   . PHE A 1 160 ? -18.337 -6.478  39.903 1.00 122.40 ? 160 PHE A O   1 
ATOM   1259 C  CB  . PHE A 1 160 ? -16.044 -8.240  41.640 1.00 109.14 ? 160 PHE A CB  1 
ATOM   1260 C  CG  . PHE A 1 160 ? -15.519 -6.846  41.894 1.00 114.35 ? 160 PHE A CG  1 
ATOM   1261 C  CD1 . PHE A 1 160 ? -15.270 -6.422  43.187 1.00 119.64 ? 160 PHE A CD1 1 
ATOM   1262 C  CD2 . PHE A 1 160 ? -15.229 -5.981  40.850 1.00 121.48 ? 160 PHE A CD2 1 
ATOM   1263 C  CE1 . PHE A 1 160 ? -14.771 -5.157  43.441 1.00 124.97 ? 160 PHE A CE1 1 
ATOM   1264 C  CE2 . PHE A 1 160 ? -14.734 -4.711  41.100 1.00 126.11 ? 160 PHE A CE2 1 
ATOM   1265 C  CZ  . PHE A 1 160 ? -14.503 -4.302  42.399 1.00 125.15 ? 160 PHE A CZ  1 
ATOM   1266 N  N   . VAL A 1 161 ? -17.312 -8.159  38.819 1.00 120.48 ? 161 VAL A N   1 
ATOM   1267 C  CA  . VAL A 1 161 ? -17.359 -7.479  37.533 1.00 121.16 ? 161 VAL A CA  1 
ATOM   1268 C  C   . VAL A 1 161 ? -18.791 -7.152  37.124 1.00 125.07 ? 161 VAL A C   1 
ATOM   1269 O  O   . VAL A 1 161 ? -19.038 -6.078  36.562 1.00 132.57 ? 161 VAL A O   1 
ATOM   1270 C  CB  . VAL A 1 161 ? -16.619 -8.337  36.487 1.00 120.80 ? 161 VAL A CB  1 
ATOM   1271 C  CG1 . VAL A 1 161 ? -17.159 -8.087  35.090 1.00 124.47 ? 161 VAL A CG1 1 
ATOM   1272 C  CG2 . VAL A 1 161 ? -15.114 -8.054  36.563 1.00 120.39 ? 161 VAL A CG2 1 
ATOM   1273 N  N   . HIS A 1 162 ? -19.751 -8.029  37.418 1.00 118.71 ? 162 HIS A N   1 
ATOM   1274 C  CA  . HIS A 1 162 ? -21.097 -7.910  36.862 1.00 118.50 ? 162 HIS A CA  1 
ATOM   1275 C  C   . HIS A 1 162 ? -22.216 -7.757  37.886 1.00 125.75 ? 162 HIS A C   1 
ATOM   1276 O  O   . HIS A 1 162 ? -23.222 -7.104  37.583 1.00 133.92 ? 162 HIS A O   1 
ATOM   1277 C  CB  . HIS A 1 162 ? -21.409 -9.130  35.985 1.00 119.74 ? 162 HIS A CB  1 
ATOM   1278 C  CG  . HIS A 1 162 ? -20.581 -9.197  34.745 1.00 121.97 ? 162 HIS A CG  1 
ATOM   1279 N  ND1 . HIS A 1 162 ? -19.854 -10.314 34.394 1.00 121.10 ? 162 HIS A ND1 1 
ATOM   1280 C  CD2 . HIS A 1 162 ? -20.376 -8.289  33.763 1.00 121.88 ? 162 HIS A CD2 1 
ATOM   1281 C  CE1 . HIS A 1 162 ? -19.233 -10.088 33.250 1.00 119.06 ? 162 HIS A CE1 1 
ATOM   1282 N  NE2 . HIS A 1 162 ? -19.533 -8.866  32.846 1.00 119.17 ? 162 HIS A NE2 1 
ATOM   1283 N  N   . GLN A 1 163 ? -22.084 -8.346  39.076 1.00 122.66 ? 163 GLN A N   1 
ATOM   1284 C  CA  . GLN A 1 163 ? -23.165 -8.382  40.055 1.00 123.70 ? 163 GLN A CA  1 
ATOM   1285 C  C   . GLN A 1 163 ? -22.786 -7.718  41.372 1.00 122.46 ? 163 GLN A C   1 
ATOM   1286 O  O   . GLN A 1 163 ? -23.396 -8.012  42.407 1.00 120.75 ? 163 GLN A O   1 
ATOM   1287 C  CB  . GLN A 1 163 ? -23.605 -9.825  40.311 1.00 127.82 ? 163 GLN A CB  1 
ATOM   1288 C  CG  . GLN A 1 163 ? -24.032 -10.570 39.059 1.00 134.87 ? 163 GLN A CG  1 
ATOM   1289 C  CD  . GLN A 1 163 ? -23.740 -12.058 39.128 1.00 136.74 ? 163 GLN A CD  1 
ATOM   1290 O  OE1 . GLN A 1 163 ? -22.993 -12.520 39.991 1.00 133.65 ? 163 GLN A OE1 1 
ATOM   1291 N  NE2 . GLN A 1 163 ? -24.332 -12.817 38.213 1.00 141.36 ? 163 GLN A NE2 1 
ATOM   1292 N  N   . ARG A 1 164 ? -21.795 -6.830  41.359 1.00 122.52 ? 164 ARG A N   1 
ATOM   1293 C  CA  . ARG A 1 164 ? -21.423 -6.123  42.573 1.00 128.36 ? 164 ARG A CA  1 
ATOM   1294 C  C   . ARG A 1 164 ? -22.583 -5.260  43.047 1.00 130.71 ? 164 ARG A C   1 
ATOM   1295 O  O   . ARG A 1 164 ? -23.341 -4.705  42.247 1.00 134.57 ? 164 ARG A O   1 
ATOM   1296 C  CB  . ARG A 1 164 ? -20.184 -5.262  42.336 1.00 133.51 ? 164 ARG A CB  1 
ATOM   1297 C  CG  . ARG A 1 164 ? -19.622 -4.630  43.599 1.00 136.64 ? 164 ARG A CG  1 
ATOM   1298 C  CD  . ARG A 1 164 ? -18.331 -3.890  43.307 1.00 135.73 ? 164 ARG A CD  1 
ATOM   1299 N  NE  . ARG A 1 164 ? -18.197 -3.593  41.885 1.00 139.88 ? 164 ARG A NE  1 
ATOM   1300 C  CZ  . ARG A 1 164 ? -17.400 -2.655  41.385 1.00 140.05 ? 164 ARG A CZ  1 
ATOM   1301 N  NH1 . ARG A 1 164 ? -16.656 -1.912  42.192 1.00 140.41 ? 164 ARG A NH1 1 
ATOM   1302 N  NH2 . ARG A 1 164 ? -17.347 -2.459  40.075 1.00 135.60 ? 164 ARG A NH2 1 
ATOM   1303 N  N   . THR A 1 165 ? -22.727 -5.166  44.370 1.00 131.14 ? 165 THR A N   1 
ATOM   1304 C  CA  . THR A 1 165 ? -23.873 -4.463  44.936 1.00 141.14 ? 165 THR A CA  1 
ATOM   1305 C  C   . THR A 1 165 ? -23.869 -3.006  44.504 1.00 142.83 ? 165 THR A C   1 
ATOM   1306 O  O   . THR A 1 165 ? -24.859 -2.504  43.962 1.00 146.34 ? 165 THR A O   1 
ATOM   1307 C  CB  . THR A 1 165 ? -23.859 -4.572  46.460 1.00 143.78 ? 165 THR A CB  1 
ATOM   1308 O  OG1 . THR A 1 165 ? -23.346 -5.853  46.836 1.00 144.39 ? 165 THR A OG1 1 
ATOM   1309 C  CG2 . THR A 1 165 ? -25.266 -4.441  47.020 1.00 145.14 ? 165 THR A CG2 1 
ATOM   1310 N  N   . PHE A 1 166 ? -22.754 -2.317  44.720 1.00 141.01 ? 166 PHE A N   1 
ATOM   1311 C  CA  . PHE A 1 166 ? -22.615 -0.910  44.338 1.00 142.33 ? 166 PHE A CA  1 
ATOM   1312 C  C   . PHE A 1 166 ? -21.527 -0.769  43.280 1.00 136.27 ? 166 PHE A C   1 
ATOM   1313 O  O   . PHE A 1 166 ? -20.329 -0.925  43.609 1.00 133.65 ? 166 PHE A O   1 
ATOM   1314 C  CB  . PHE A 1 166 ? -22.297 -0.039  45.557 1.00 150.24 ? 166 PHE A CB  1 
ATOM   1315 C  CG  . PHE A 1 166 ? -23.223 -0.253  46.747 1.00 165.03 ? 166 PHE A CG  1 
ATOM   1316 C  CD1 . PHE A 1 166 ? -24.534 -0.679  46.584 1.00 172.88 ? 166 PHE A CD1 1 
ATOM   1317 C  CD2 . PHE A 1 166 ? -22.762 -0.047  48.031 1.00 170.13 ? 166 PHE A CD2 1 
ATOM   1318 C  CE1 . PHE A 1 166 ? -25.360 -0.873  47.679 1.00 181.35 ? 166 PHE A CE1 1 
ATOM   1319 C  CE2 . PHE A 1 166 ? -23.581 -0.242  49.110 1.00 174.91 ? 166 PHE A CE2 1 
ATOM   1320 C  CZ  . PHE A 1 166 ? -24.883 -0.653  48.934 1.00 181.50 ? 166 PHE A CZ  1 
ATOM   1321 N  N   . PRO A 1 167 ? -21.848 -0.448  42.024 1.00 133.73 ? 167 PRO A N   1 
ATOM   1322 C  CA  . PRO A 1 167 ? -20.824 -0.495  40.964 1.00 128.63 ? 167 PRO A CA  1 
ATOM   1323 C  C   . PRO A 1 167 ? -19.787 0.615   41.039 1.00 128.63 ? 167 PRO A C   1 
ATOM   1324 O  O   . PRO A 1 167 ? -18.737 0.498   40.394 1.00 129.15 ? 167 PRO A O   1 
ATOM   1325 C  CB  . PRO A 1 167 ? -21.646 -0.389  39.674 1.00 126.97 ? 167 PRO A CB  1 
ATOM   1326 C  CG  . PRO A 1 167 ? -22.847 0.392   40.074 1.00 129.92 ? 167 PRO A CG  1 
ATOM   1327 C  CD  . PRO A 1 167 ? -23.157 -0.014  41.499 1.00 134.68 ? 167 PRO A CD  1 
ATOM   1328 N  N   . ASP A 1 168 ? -20.042 1.684   41.793 1.00 130.74 ? 168 ASP A N   1 
ATOM   1329 C  CA  . ASP A 1 168 ? -19.126 2.816   41.836 1.00 140.12 ? 168 ASP A CA  1 
ATOM   1330 C  C   . ASP A 1 168 ? -17.950 2.605   42.781 1.00 138.66 ? 168 ASP A C   1 
ATOM   1331 O  O   . ASP A 1 168 ? -17.034 3.434   42.793 1.00 141.66 ? 168 ASP A O   1 
ATOM   1332 C  CB  . ASP A 1 168 ? -19.881 4.086   42.239 1.00 154.36 ? 168 ASP A CB  1 
ATOM   1333 C  CG  . ASP A 1 168 ? -20.855 3.849   43.379 1.00 167.38 ? 168 ASP A CG  1 
ATOM   1334 O  OD1 . ASP A 1 168 ? -20.924 4.699   44.292 1.00 170.41 ? 168 ASP A OD1 1 
ATOM   1335 O  OD2 . ASP A 1 168 ? -21.555 2.813   43.363 1.00 171.76 ? 168 ASP A OD2 1 
ATOM   1336 N  N   . ARG A 1 169 ? -17.945 1.530   43.566 1.00 133.71 ? 169 ARG A N   1 
ATOM   1337 C  CA  . ARG A 1 169 ? -16.888 1.310   44.542 1.00 131.85 ? 169 ARG A CA  1 
ATOM   1338 C  C   . ARG A 1 169 ? -16.707 -0.188  44.761 1.00 131.44 ? 169 ARG A C   1 
ATOM   1339 O  O   . ARG A 1 169 ? -17.451 -1.010  44.219 1.00 132.40 ? 169 ARG A O   1 
ATOM   1340 C  CB  . ARG A 1 169 ? -17.194 2.051   45.846 1.00 134.22 ? 169 ARG A CB  1 
ATOM   1341 C  CG  . ARG A 1 169 ? -18.667 2.112   46.208 1.00 137.64 ? 169 ARG A CG  1 
ATOM   1342 C  CD  . ARG A 1 169 ? -19.001 3.447   46.851 1.00 143.54 ? 169 ARG A CD  1 
ATOM   1343 N  NE  . ARG A 1 169 ? -17.963 3.872   47.786 1.00 148.77 ? 169 ARG A NE  1 
ATOM   1344 C  CZ  . ARG A 1 169 ? -17.740 5.136   48.134 1.00 153.17 ? 169 ARG A CZ  1 
ATOM   1345 N  NH1 . ARG A 1 169 ? -18.485 6.109   47.626 1.00 153.09 ? 169 ARG A NH1 1 
ATOM   1346 N  NH2 . ARG A 1 169 ? -16.773 5.426   48.994 1.00 153.49 ? 169 ARG A NH2 1 
ATOM   1347 N  N   . ARG A 1 170 ? -15.707 -0.535  45.575 1.00 128.50 ? 170 ARG A N   1 
ATOM   1348 C  CA  . ARG A 1 170 ? -15.244 -1.910  45.745 1.00 123.93 ? 170 ARG A CA  1 
ATOM   1349 C  C   . ARG A 1 170 ? -16.229 -2.794  46.505 1.00 125.64 ? 170 ARG A C   1 
ATOM   1350 O  O   . ARG A 1 170 ? -17.427 -2.499  46.564 1.00 132.22 ? 170 ARG A O   1 
ATOM   1351 C  CB  . ARG A 1 170 ? -13.888 -1.911  46.457 1.00 122.74 ? 170 ARG A CB  1 
ATOM   1352 C  CG  . ARG A 1 170 ? -12.784 -1.229  45.661 1.00 123.77 ? 170 ARG A CG  1 
ATOM   1353 C  CD  . ARG A 1 170 ? -11.571 -0.903  46.521 1.00 123.70 ? 170 ARG A CD  1 
ATOM   1354 N  NE  . ARG A 1 170 ? -10.548 -0.193  45.755 1.00 123.80 ? 170 ARG A NE  1 
ATOM   1355 C  CZ  . ARG A 1 170 ? -9.506  0.433   46.294 1.00 122.57 ? 170 ARG A CZ  1 
ATOM   1356 N  NH1 . ARG A 1 170 ? -9.341  0.441   47.610 1.00 126.15 ? 170 ARG A NH1 1 
ATOM   1357 N  NH2 . ARG A 1 170 ? -8.629  1.052   45.515 1.00 117.47 ? 170 ARG A NH2 1 
ATOM   1358 N  N   . SER A 1 171 ? -15.732 -3.885  47.086 1.00 124.54 ? 171 SER A N   1 
ATOM   1359 C  CA  . SER A 1 171 ? -16.585 -4.844  47.776 1.00 129.56 ? 171 SER A CA  1 
ATOM   1360 C  C   . SER A 1 171 ? -15.749 -5.619  48.786 1.00 127.08 ? 171 SER A C   1 
ATOM   1361 O  O   . SER A 1 171 ? -14.516 -5.583  48.761 1.00 122.65 ? 171 SER A O   1 
ATOM   1362 C  CB  . SER A 1 171 ? -17.262 -5.800  46.789 1.00 127.61 ? 171 SER A CB  1 
ATOM   1363 O  OG  . SER A 1 171 ? -17.756 -6.951  47.451 1.00 125.05 ? 171 SER A OG  1 
ATOM   1364 N  N   . ILE A 1 172 ? -16.444 -6.330  49.676 1.00 127.01 ? 172 ILE A N   1 
ATOM   1365 C  CA  . ILE A 1 172 ? -15.768 -7.152  50.675 1.00 122.67 ? 172 ILE A CA  1 
ATOM   1366 C  C   . ILE A 1 172 ? -15.596 -8.600  50.226 1.00 123.38 ? 172 ILE A C   1 
ATOM   1367 O  O   . ILE A 1 172 ? -14.694 -9.289  50.724 1.00 125.11 ? 172 ILE A O   1 
ATOM   1368 C  CB  . ILE A 1 172 ? -16.514 -7.104  52.021 1.00 122.41 ? 172 ILE A CB  1 
ATOM   1369 C  CG1 . ILE A 1 172 ? -15.556 -7.435  53.165 1.00 120.08 ? 172 ILE A CG1 1 
ATOM   1370 C  CG2 . ILE A 1 172 ? -17.710 -8.049  52.022 1.00 124.60 ? 172 ILE A CG2 1 
ATOM   1371 C  CD1 . ILE A 1 172 ? -14.437 -6.440  53.316 1.00 115.51 ? 172 ILE A CD1 1 
ATOM   1372 N  N   . GLY A 1 173 ? -16.425 -9.077  49.299 1.00 122.13 ? 173 GLY A N   1 
ATOM   1373 C  CA  . GLY A 1 173 ? -16.266 -10.414 48.767 1.00 116.27 ? 173 GLY A CA  1 
ATOM   1374 C  C   . GLY A 1 173 ? -16.502 -11.503 49.799 1.00 117.27 ? 173 GLY A C   1 
ATOM   1375 O  O   . GLY A 1 173 ? -17.248 -11.340 50.771 1.00 121.57 ? 173 GLY A O   1 
ATOM   1376 N  N   . TRP A 1 174 ? -15.849 -12.646 49.569 1.00 118.00 ? 174 TRP A N   1 
ATOM   1377 C  CA  . TRP A 1 174 ? -15.925 -13.749 50.522 1.00 119.06 ? 174 TRP A CA  1 
ATOM   1378 C  C   . TRP A 1 174 ? -15.167 -13.412 51.801 1.00 117.32 ? 174 TRP A C   1 
ATOM   1379 O  O   . TRP A 1 174 ? -15.704 -13.519 52.908 1.00 117.04 ? 174 TRP A O   1 
ATOM   1380 C  CB  . TRP A 1 174 ? -15.381 -15.030 49.882 1.00 115.32 ? 174 TRP A CB  1 
ATOM   1381 C  CG  . TRP A 1 174 ? -15.507 -16.249 50.740 1.00 118.71 ? 174 TRP A CG  1 
ATOM   1382 C  CD1 . TRP A 1 174 ? -16.384 -16.450 51.768 1.00 120.27 ? 174 TRP A CD1 1 
ATOM   1383 C  CD2 . TRP A 1 174 ? -14.718 -17.439 50.648 1.00 122.74 ? 174 TRP A CD2 1 
ATOM   1384 N  NE1 . TRP A 1 174 ? -16.190 -17.695 52.317 1.00 123.17 ? 174 TRP A NE1 1 
ATOM   1385 C  CE2 . TRP A 1 174 ? -15.171 -18.321 51.647 1.00 126.31 ? 174 TRP A CE2 1 
ATOM   1386 C  CE3 . TRP A 1 174 ? -13.671 -17.844 49.815 1.00 118.06 ? 174 TRP A CE3 1 
ATOM   1387 C  CZ2 . TRP A 1 174 ? -14.611 -19.584 51.838 1.00 130.58 ? 174 TRP A CZ2 1 
ATOM   1388 C  CZ3 . TRP A 1 174 ? -13.117 -19.099 50.005 1.00 115.99 ? 174 TRP A CZ3 1 
ATOM   1389 C  CH2 . TRP A 1 174 ? -13.589 -19.953 51.007 1.00 124.18 ? 174 TRP A CH2 1 
ATOM   1390 N  N   . ILE A 1 175 ? -13.911 -13.010 51.672 1.00 115.44 ? 175 ILE A N   1 
ATOM   1391 C  CA  . ILE A 1 175 ? -13.097 -12.604 52.809 1.00 115.43 ? 175 ILE A CA  1 
ATOM   1392 C  C   . ILE A 1 175 ? -12.443 -11.292 52.432 1.00 115.15 ? 175 ILE A C   1 
ATOM   1393 O  O   . ILE A 1 175 ? -11.725 -11.227 51.428 1.00 115.30 ? 175 ILE A O   1 
ATOM   1394 C  CB  . ILE A 1 175 ? -12.021 -13.639 53.172 1.00 115.75 ? 175 ILE A CB  1 
ATOM   1395 C  CG1 . ILE A 1 175 ? -12.629 -15.037 53.246 1.00 120.51 ? 175 ILE A CG1 1 
ATOM   1396 C  CG2 . ILE A 1 175 ? -11.400 -13.299 54.513 1.00 116.77 ? 175 ILE A CG2 1 
ATOM   1397 C  CD1 . ILE A 1 175 ? -12.366 -15.887 52.034 1.00 122.71 ? 175 ILE A CD1 1 
ATOM   1398 N  N   . GLY A 1 176 ? -12.680 -10.255 53.229 1.00 114.52 ? 176 GLY A N   1 
ATOM   1399 C  CA  . GLY A 1 176 ? -12.039 -8.977  53.009 1.00 112.39 ? 176 GLY A CA  1 
ATOM   1400 C  C   . GLY A 1 176 ? -11.589 -8.368  54.322 1.00 116.48 ? 176 GLY A C   1 
ATOM   1401 O  O   . GLY A 1 176 ? -12.038 -8.764  55.399 1.00 119.02 ? 176 GLY A O   1 
ATOM   1402 N  N   . PHE A 1 177 ? -10.671 -7.407  54.217 1.00 115.73 ? 177 PHE A N   1 
ATOM   1403 C  CA  . PHE A 1 177 ? -10.126 -6.707  55.374 1.00 126.29 ? 177 PHE A CA  1 
ATOM   1404 C  C   . PHE A 1 177 ? -10.462 -5.227  55.256 1.00 132.57 ? 177 PHE A C   1 
ATOM   1405 O  O   . PHE A 1 177 ? -10.126 -4.591  54.251 1.00 133.72 ? 177 PHE A O   1 
ATOM   1406 C  CB  . PHE A 1 177 ? -8.614  -6.911  55.478 1.00 124.88 ? 177 PHE A CB  1 
ATOM   1407 C  CG  . PHE A 1 177 ? -7.901  -5.783  56.156 1.00 122.89 ? 177 PHE A CG  1 
ATOM   1408 C  CD1 . PHE A 1 177 ? -7.069  -4.941  55.438 1.00 119.91 ? 177 PHE A CD1 1 
ATOM   1409 C  CD2 . PHE A 1 177 ? -8.071  -5.557  57.511 1.00 126.22 ? 177 PHE A CD2 1 
ATOM   1410 C  CE1 . PHE A 1 177 ? -6.418  -3.900  56.059 1.00 123.44 ? 177 PHE A CE1 1 
ATOM   1411 C  CE2 . PHE A 1 177 ? -7.427  -4.519  58.136 1.00 129.58 ? 177 PHE A CE2 1 
ATOM   1412 C  CZ  . PHE A 1 177 ? -6.596  -3.689  57.410 1.00 128.74 ? 177 PHE A CZ  1 
ATOM   1413 N  N   . CYS A 1 178 ? -11.135 -4.685  56.284 1.00 134.90 ? 178 CYS A N   1 
ATOM   1414 C  CA  . CYS A 1 178 ? -11.451 -3.272  56.424 1.00 142.23 ? 178 CYS A CA  1 
ATOM   1415 C  C   . CYS A 1 178 ? -10.582 -2.666  57.518 1.00 148.01 ? 178 CYS A C   1 
ATOM   1416 O  O   . CYS A 1 178 ? -10.460 -3.254  58.599 1.00 148.89 ? 178 CYS A O   1 
ATOM   1417 C  CB  . CYS A 1 178 ? -12.929 -3.063  56.780 1.00 152.01 ? 178 CYS A CB  1 
ATOM   1418 S  SG  . CYS A 1 178 ? -14.085 -3.769  55.590 1.00 154.81 ? 178 CYS A SG  1 
ATOM   1419 N  N   . PRO A 1 179 ? -9.972  -1.503  57.281 1.00 147.14 ? 179 PRO A N   1 
ATOM   1420 C  CA  . PRO A 1 179 ? -8.946  -1.011  58.212 1.00 152.05 ? 179 PRO A CA  1 
ATOM   1421 C  C   . PRO A 1 179 ? -9.488  -0.395  59.494 1.00 156.17 ? 179 PRO A C   1 
ATOM   1422 O  O   . PRO A 1 179 ? -8.894  0.551   60.019 1.00 160.12 ? 179 PRO A O   1 
ATOM   1423 C  CB  . PRO A 1 179 ? -8.195  0.034   57.378 1.00 151.09 ? 179 PRO A CB  1 
ATOM   1424 C  CG  . PRO A 1 179 ? -9.220  0.539   56.421 1.00 151.05 ? 179 PRO A CG  1 
ATOM   1425 C  CD  . PRO A 1 179 ? -10.148 -0.611  56.122 1.00 147.94 ? 179 PRO A CD  1 
ATOM   1426 N  N   . HIS A 1 180 ? -10.605 -0.895  60.023 1.00 155.03 ? 180 HIS A N   1 
ATOM   1427 C  CA  . HIS A 1 180 ? -11.174 -0.365  61.227 1.00 156.00 ? 180 HIS A CA  1 
ATOM   1428 C  C   . HIS A 1 180 ? -11.814 -1.493  62.028 1.00 154.04 ? 180 HIS A C   1 
ATOM   1429 O  O   . HIS A 1 180 ? -11.972 -2.609  61.486 1.00 153.79 ? 180 HIS A O   1 
ATOM   1430 C  CB  . HIS A 1 180 ? -12.218 0.730   60.941 1.00 160.36 ? 180 HIS A CB  1 
ATOM   1431 C  CG  . HIS A 1 180 ? -11.710 1.823   60.053 1.00 156.23 ? 180 HIS A CG  1 
ATOM   1432 N  ND1 . HIS A 1 180 ? -11.376 3.072   60.531 1.00 158.26 ? 180 HIS A ND1 1 
ATOM   1433 C  CD2 . HIS A 1 180 ? -11.504 1.864   58.716 1.00 151.06 ? 180 HIS A CD2 1 
ATOM   1434 C  CE1 . HIS A 1 180 ? -10.971 3.830   59.527 1.00 155.91 ? 180 HIS A CE1 1 
ATOM   1435 N  NE2 . HIS A 1 180 ? -11.038 3.121   58.415 1.00 152.00 ? 180 HIS A NE2 1 
ATOM   1436 N  N   . PRO A 1 181 ? -12.162 -1.278  63.280 1.00 157.20 ? 181 PRO A N   1 
ATOM   1437 C  CA  . PRO A 1 181 ? -12.928 -2.280  64.025 1.00 163.27 ? 181 PRO A CA  1 
ATOM   1438 C  C   . PRO A 1 181 ? -14.423 -2.182  63.749 1.00 168.62 ? 181 PRO A C   1 
ATOM   1439 O  O   . PRO A 1 181 ? -14.956 -1.113  63.446 1.00 171.67 ? 181 PRO A O   1 
ATOM   1440 C  CB  . PRO A 1 181 ? -12.608 -1.960  65.489 1.00 168.21 ? 181 PRO A CB  1 
ATOM   1441 C  CG  . PRO A 1 181 ? -12.304 -0.514  65.490 1.00 167.60 ? 181 PRO A CG  1 
ATOM   1442 C  CD  . PRO A 1 181 ? -11.619 -0.234  64.180 1.00 159.85 ? 181 PRO A CD  1 
ATOM   1443 N  N   . LEU A 1 182 ? -15.101 -3.325  63.863 1.00 169.07 ? 182 LEU A N   1 
ATOM   1444 C  CA  . LEU A 1 182 ? -16.510 -3.442  63.507 1.00 168.79 ? 182 LEU A CA  1 
ATOM   1445 C  C   . LEU A 1 182 ? -17.311 -4.095  64.627 1.00 176.66 ? 182 LEU A C   1 
ATOM   1446 O  O   . LEU A 1 182 ? -16.785 -4.863  65.436 1.00 177.74 ? 182 LEU A O   1 
ATOM   1447 C  CB  . LEU A 1 182 ? -16.715 -4.264  62.224 1.00 158.44 ? 182 LEU A CB  1 
ATOM   1448 C  CG  . LEU A 1 182 ? -16.157 -3.791  60.882 1.00 150.33 ? 182 LEU A CG  1 
ATOM   1449 C  CD1 . LEU A 1 182 ? -16.566 -2.360  60.654 1.00 152.09 ? 182 LEU A CD1 1 
ATOM   1450 C  CD2 . LEU A 1 182 ? -14.656 -3.976  60.714 1.00 144.88 ? 182 LEU A CD2 1 
ATOM   1451 N  N   . ARG A 1 183 ? -18.606 -3.787  64.646 1.00 182.67 ? 183 ARG A N   1 
ATOM   1452 C  CA  . ARG A 1 183 ? -19.556 -4.430  65.542 1.00 179.75 ? 183 ARG A CA  1 
ATOM   1453 C  C   . ARG A 1 183 ? -20.118 -5.689  64.889 1.00 175.02 ? 183 ARG A C   1 
ATOM   1454 O  O   . ARG A 1 183 ? -20.315 -5.749  63.672 1.00 169.52 ? 183 ARG A O   1 
ATOM   1455 C  CB  . ARG A 1 183 ? -20.693 -3.471  65.908 1.00 185.72 ? 183 ARG A CB  1 
ATOM   1456 C  CG  . ARG A 1 183 ? -21.556 -3.930  67.076 1.00 189.27 ? 183 ARG A CG  1 
ATOM   1457 C  CD  . ARG A 1 183 ? -22.565 -2.864  67.480 1.00 191.07 ? 183 ARG A CD  1 
ATOM   1458 N  NE  . ARG A 1 183 ? -23.565 -2.633  66.442 1.00 190.22 ? 183 ARG A NE  1 
ATOM   1459 C  CZ  . ARG A 1 183 ? -24.756 -2.087  66.661 1.00 195.94 ? 183 ARG A CZ  1 
ATOM   1460 N  NH1 . ARG A 1 183 ? -25.101 -1.716  67.886 1.00 201.18 ? 183 ARG A NH1 1 
ATOM   1461 N  NH2 . ARG A 1 183 ? -25.604 -1.915  65.656 1.00 196.06 ? 183 ARG A NH2 1 
ATOM   1462 N  N   . ALA A 1 184 ? -20.382 -6.702  65.718 1.00 179.50 ? 184 ALA A N   1 
ATOM   1463 C  CA  . ALA A 1 184 ? -20.807 -7.995  65.189 1.00 169.56 ? 184 ALA A CA  1 
ATOM   1464 C  C   . ALA A 1 184 ? -22.242 -7.951  64.676 1.00 171.79 ? 184 ALA A C   1 
ATOM   1465 O  O   . ALA A 1 184 ? -22.542 -8.506  63.613 1.00 159.30 ? 184 ALA A O   1 
ATOM   1466 C  CB  . ALA A 1 184 ? -20.653 -9.077  66.258 1.00 164.93 ? 184 ALA A CB  1 
ATOM   1467 N  N   . THR A 1 185 ? -23.143 -7.300  65.415 1.00 176.36 ? 185 THR A N   1 
ATOM   1468 C  CA  . THR A 1 185 ? -24.549 -7.269  65.032 1.00 182.18 ? 185 THR A CA  1 
ATOM   1469 C  C   . THR A 1 185 ? -24.838 -6.303  63.890 1.00 182.27 ? 185 THR A C   1 
ATOM   1470 O  O   . THR A 1 185 ? -25.957 -6.309  63.367 1.00 184.58 ? 185 THR A O   1 
ATOM   1471 C  CB  . THR A 1 185 ? -25.422 -6.910  66.237 1.00 190.74 ? 185 THR A CB  1 
ATOM   1472 O  OG1 . THR A 1 185 ? -26.797 -6.863  65.835 1.00 196.23 ? 185 THR A OG1 1 
ATOM   1473 C  CG2 . THR A 1 185 ? -25.020 -5.563  66.807 1.00 190.30 ? 185 THR A CG2 1 
ATOM   1474 N  N   . ASP A 1 186 ? -23.867 -5.477  63.492 1.00 178.99 ? 186 ASP A N   1 
ATOM   1475 C  CA  . ASP A 1 186 ? -24.032 -4.641  62.309 1.00 174.93 ? 186 ASP A CA  1 
ATOM   1476 C  C   . ASP A 1 186 ? -23.947 -5.441  61.018 1.00 170.23 ? 186 ASP A C   1 
ATOM   1477 O  O   . ASP A 1 186 ? -24.191 -4.880  59.944 1.00 165.97 ? 186 ASP A O   1 
ATOM   1478 C  CB  . ASP A 1 186 ? -22.977 -3.532  62.293 1.00 171.36 ? 186 ASP A CB  1 
ATOM   1479 C  CG  . ASP A 1 186 ? -23.387 -2.324  63.111 1.00 177.72 ? 186 ASP A CG  1 
ATOM   1480 O  OD1 . ASP A 1 186 ? -24.605 -2.096  63.269 1.00 183.45 ? 186 ASP A OD1 1 
ATOM   1481 O  OD2 . ASP A 1 186 ? -22.490 -1.600  63.593 1.00 176.50 ? 186 ASP A OD2 1 
ATOM   1482 N  N   . PHE A 1 187 ? -23.617 -6.727  61.099 1.00 176.23 ? 187 PHE A N   1 
ATOM   1483 C  CA  . PHE A 1 187 ? -23.405 -7.577  59.935 1.00 177.40 ? 187 PHE A CA  1 
ATOM   1484 C  C   . PHE A 1 187 ? -24.377 -8.752  59.971 1.00 182.29 ? 187 PHE A C   1 
ATOM   1485 O  O   . PHE A 1 187 ? -25.004 -9.000  61.009 1.00 182.93 ? 187 PHE A O   1 
ATOM   1486 C  CB  . PHE A 1 187 ? -21.954 -8.063  59.900 1.00 171.37 ? 187 PHE A CB  1 
ATOM   1487 C  CG  . PHE A 1 187 ? -20.963 -6.990  59.546 1.00 167.23 ? 187 PHE A CG  1 
ATOM   1488 C  CD1 . PHE A 1 187 ? -20.499 -6.859  58.249 1.00 163.02 ? 187 PHE A CD1 1 
ATOM   1489 C  CD2 . PHE A 1 187 ? -20.495 -6.113  60.511 1.00 171.59 ? 187 PHE A CD2 1 
ATOM   1490 C  CE1 . PHE A 1 187 ? -19.588 -5.875  57.922 1.00 160.48 ? 187 PHE A CE1 1 
ATOM   1491 C  CE2 . PHE A 1 187 ? -19.584 -5.125  60.188 1.00 167.80 ? 187 PHE A CE2 1 
ATOM   1492 C  CZ  . PHE A 1 187 ? -19.130 -5.006  58.891 1.00 162.40 ? 187 PHE A CZ  1 
ATOM   1493 N  N   . PRO A 1 188 ? -24.545 -9.492  58.860 1.00 183.74 ? 188 PRO A N   1 
ATOM   1494 C  CA  . PRO A 1 188 ? -25.442 -10.658 58.881 1.00 187.79 ? 188 PRO A CA  1 
ATOM   1495 C  C   . PRO A 1 188 ? -25.014 -11.737 59.867 1.00 188.01 ? 188 PRO A C   1 
ATOM   1496 O  O   . PRO A 1 188 ? -24.010 -11.593 60.572 1.00 186.23 ? 188 PRO A O   1 
ATOM   1497 C  CB  . PRO A 1 188 ? -25.386 -11.167 57.434 1.00 184.87 ? 188 PRO A CB  1 
ATOM   1498 C  CG  . PRO A 1 188 ? -25.046 -9.963  56.631 1.00 183.47 ? 188 PRO A CG  1 
ATOM   1499 C  CD  . PRO A 1 188 ? -24.114 -9.158  57.489 1.00 180.34 ? 188 PRO A CD  1 
ATOM   1500 N  N   . ALA A 1 189 ? -25.775 -12.832 59.906 1.00 194.41 ? 189 ALA A N   1 
ATOM   1501 C  CA  . ALA A 1 189 ? -25.619 -13.825 60.965 1.00 192.29 ? 189 ALA A CA  1 
ATOM   1502 C  C   . ALA A 1 189 ? -24.268 -14.528 60.886 1.00 181.72 ? 189 ALA A C   1 
ATOM   1503 O  O   . ALA A 1 189 ? -23.437 -14.407 61.793 1.00 176.34 ? 189 ALA A O   1 
ATOM   1504 C  CB  . ALA A 1 189 ? -26.761 -14.842 60.897 1.00 195.79 ? 189 ALA A CB  1 
ATOM   1505 N  N   . ALA A 1 190 ? -24.035 -15.275 59.808 1.00 180.89 ? 190 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 190 ? -22.850 -16.118 59.666 1.00 176.52 ? 190 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 190 ? -21.715 -15.410 58.939 1.00 165.74 ? 190 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 190 ? -21.023 -16.016 58.117 1.00 152.69 ? 190 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 190 ? -23.209 -17.419 58.956 1.00 175.63 ? 190 ALA A CB  1 
ATOM   1510 N  N   . THR A 1 191 ? -21.511 -14.124 59.210 1.00 171.96 ? 191 THR A N   1 
ATOM   1511 C  CA  . THR A 1 191 ? -20.318 -13.410 58.772 1.00 174.60 ? 191 THR A CA  1 
ATOM   1512 C  C   . THR A 1 191 ? -19.414 -13.224 59.984 1.00 173.47 ? 191 THR A C   1 
ATOM   1513 O  O   . THR A 1 191 ? -19.788 -12.539 60.943 1.00 184.87 ? 191 THR A O   1 
ATOM   1514 C  CB  . THR A 1 191 ? -20.665 -12.062 58.139 1.00 182.85 ? 191 THR A CB  1 
ATOM   1515 O  OG1 . THR A 1 191 ? -20.799 -11.067 59.162 1.00 193.53 ? 191 THR A OG1 1 
ATOM   1516 C  CG2 . THR A 1 191 ? -21.957 -12.159 57.350 1.00 186.87 ? 191 THR A CG2 1 
ATOM   1517 N  N   . GLU A 1 192 ? -18.237 -13.839 59.944 1.00 161.52 ? 192 GLU A N   1 
ATOM   1518 C  CA  . GLU A 1 192 ? -17.366 -13.915 61.108 1.00 157.84 ? 192 GLU A CA  1 
ATOM   1519 C  C   . GLU A 1 192 ? -16.368 -12.763 61.108 1.00 153.32 ? 192 GLU A C   1 
ATOM   1520 O  O   . GLU A 1 192 ? -15.710 -12.499 60.096 1.00 146.97 ? 192 GLU A O   1 
ATOM   1521 C  CB  . GLU A 1 192 ? -16.630 -15.255 61.136 1.00 152.07 ? 192 GLU A CB  1 
ATOM   1522 C  CG  . GLU A 1 192 ? -15.620 -15.387 62.259 1.00 148.01 ? 192 GLU A CG  1 
ATOM   1523 C  CD  . GLU A 1 192 ? -14.938 -16.739 62.264 1.00 145.05 ? 192 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A 1 192 ? -15.477 -17.680 61.643 1.00 143.62 ? 192 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A 1 192 ? -13.863 -16.862 62.889 1.00 145.02 ? 192 GLU A OE2 1 
ATOM   1526 N  N   . LEU A 1 193 ? -16.264 -12.085 62.247 1.00 156.42 ? 193 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 193 ? -15.308 -11.005 62.448 1.00 158.24 ? 193 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 193 ? -14.126 -11.523 63.255 1.00 160.03 ? 193 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 193 ? -14.310 -12.099 64.333 1.00 172.39 ? 193 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 193 ? -15.952 -9.827  63.184 1.00 163.26 ? 193 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 193 ? -16.766 -8.775  62.429 1.00 162.55 ? 193 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 193 ? -18.001 -9.381  61.785 1.00 164.98 ? 193 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 193 ? -17.155 -7.648  63.375 1.00 166.38 ? 193 LEU A CD2 1 
ATOM   1534 N  N   . VAL A 1 194 ? -12.919 -11.320 62.738 1.00 151.36 ? 194 VAL A N   1 
ATOM   1535 C  CA  . VAL A 1 194 ? -11.695 -11.586 63.486 1.00 145.31 ? 194 VAL A CA  1 
ATOM   1536 C  C   . VAL A 1 194 ? -10.970 -10.251 63.626 1.00 146.85 ? 194 VAL A C   1 
ATOM   1537 O  O   . VAL A 1 194 ? -10.261 -9.802  62.716 1.00 141.26 ? 194 VAL A O   1 
ATOM   1538 C  CB  . VAL A 1 194 ? -10.821 -12.663 62.828 1.00 133.58 ? 194 VAL A CB  1 
ATOM   1539 C  CG1 . VAL A 1 194 ? -10.675 -12.428 61.339 1.00 121.20 ? 194 VAL A CG1 1 
ATOM   1540 C  CG2 . VAL A 1 194 ? -9.458  -12.762 63.514 1.00 134.36 ? 194 VAL A CG2 1 
ATOM   1541 N  N   . ASP A 1 195 ? -11.180 -9.593  64.763 1.00 159.30 ? 195 ASP A N   1 
ATOM   1542 C  CA  . ASP A 1 195 ? -10.565 -8.302  65.048 1.00 171.62 ? 195 ASP A CA  1 
ATOM   1543 C  C   . ASP A 1 195 ? -9.068  -8.481  65.265 1.00 174.02 ? 195 ASP A C   1 
ATOM   1544 O  O   . ASP A 1 195 ? -8.643  -9.063  66.268 1.00 177.33 ? 195 ASP A O   1 
ATOM   1545 C  CB  . ASP A 1 195 ? -11.216 -7.682  66.280 1.00 183.09 ? 195 ASP A CB  1 
ATOM   1546 C  CG  . ASP A 1 195 ? -11.014 -6.183  66.358 1.00 188.33 ? 195 ASP A CG  1 
ATOM   1547 O  OD1 . ASP A 1 195 ? -9.951  -5.743  66.843 1.00 190.52 ? 195 ASP A OD1 1 
ATOM   1548 O  OD2 . ASP A 1 195 ? -11.927 -5.435  65.959 1.00 192.01 ? 195 ASP A OD2 1 
ATOM   1549 N  N   . ILE A 1 196 ? -8.265  -7.980  64.332 1.00 170.37 ? 196 ILE A N   1 
ATOM   1550 C  CA  . ILE A 1 196 ? -6.821  -7.927  64.529 1.00 168.47 ? 196 ILE A CA  1 
ATOM   1551 C  C   . ILE A 1 196 ? -6.503  -6.613  65.243 1.00 177.39 ? 196 ILE A C   1 
ATOM   1552 O  O   . ILE A 1 196 ? -7.166  -5.597  64.983 1.00 179.62 ? 196 ILE A O   1 
ATOM   1553 C  CB  . ILE A 1 196 ? -6.061  -8.083  63.200 1.00 159.96 ? 196 ILE A CB  1 
ATOM   1554 C  CG1 . ILE A 1 196 ? -6.379  -6.945  62.227 1.00 159.83 ? 196 ILE A CG1 1 
ATOM   1555 C  CG2 . ILE A 1 196 ? -6.386  -9.416  62.553 1.00 156.59 ? 196 ILE A CG2 1 
ATOM   1556 C  CD1 . ILE A 1 196 ? -5.390  -5.814  62.271 1.00 160.29 ? 196 ILE A CD1 1 
ATOM   1557 N  N   . PRO A 1 197 ? -5.542  -6.587  66.159 1.00 181.27 ? 197 PRO A N   1 
ATOM   1558 C  CA  . PRO A 1 197 ? -5.276  -5.351  66.919 1.00 182.51 ? 197 PRO A CA  1 
ATOM   1559 C  C   . PRO A 1 197 ? -4.401  -4.391  66.134 1.00 176.25 ? 197 PRO A C   1 
ATOM   1560 O  O   . PRO A 1 197 ? -3.280  -4.730  65.735 1.00 171.39 ? 197 PRO A O   1 
ATOM   1561 C  CB  . PRO A 1 197 ? -4.570  -5.856  68.185 1.00 187.73 ? 197 PRO A CB  1 
ATOM   1562 C  CG  . PRO A 1 197 ? -4.700  -7.361  68.162 1.00 188.97 ? 197 PRO A CG  1 
ATOM   1563 C  CD  . PRO A 1 197 ? -4.805  -7.731  66.719 1.00 183.96 ? 197 PRO A CD  1 
ATOM   1564 N  N   . GLY A 1 198 ? -4.909  -3.183  65.904 1.00 178.41 ? 198 GLY A N   1 
ATOM   1565 C  CA  . GLY A 1 198 ? -4.097  -2.123  65.346 1.00 174.91 ? 198 GLY A CA  1 
ATOM   1566 C  C   . GLY A 1 198 ? -4.493  -1.633  63.970 1.00 168.75 ? 198 GLY A C   1 
ATOM   1567 O  O   . GLY A 1 198 ? -4.452  -0.428  63.708 1.00 168.12 ? 198 GLY A O   1 
ATOM   1568 N  N   . ARG A 1 199 ? -4.870  -2.545  63.075 1.00 161.67 ? 199 ARG A N   1 
ATOM   1569 C  CA  . ARG A 1 199 ? -5.114  -2.182  61.688 1.00 157.34 ? 199 ARG A CA  1 
ATOM   1570 C  C   . ARG A 1 199 ? -6.544  -2.421  61.229 1.00 157.04 ? 199 ARG A C   1 
ATOM   1571 O  O   . ARG A 1 199 ? -6.849  -2.151  60.065 1.00 154.74 ? 199 ARG A O   1 
ATOM   1572 C  CB  . ARG A 1 199 ? -4.162  -2.943  60.755 1.00 152.04 ? 199 ARG A CB  1 
ATOM   1573 C  CG  . ARG A 1 199 ? -2.681  -2.640  60.938 1.00 149.86 ? 199 ARG A CG  1 
ATOM   1574 C  CD  . ARG A 1 199 ? -2.058  -3.495  62.036 1.00 150.00 ? 199 ARG A CD  1 
ATOM   1575 N  NE  . ARG A 1 199 ? -0.654  -3.162  62.248 1.00 148.92 ? 199 ARG A NE  1 
ATOM   1576 C  CZ  . ARG A 1 199 ? 0.361   -3.816  61.694 1.00 144.05 ? 199 ARG A CZ  1 
ATOM   1577 N  NH1 . ARG A 1 199 ? 0.130   -4.854  60.900 1.00 138.93 ? 199 ARG A NH1 1 
ATOM   1578 N  NH2 . ARG A 1 199 ? 1.607   -3.439  61.941 1.00 143.75 ? 199 ARG A NH2 1 
ATOM   1579 N  N   . GLY A 1 200 ? -7.425  -2.922  62.090 1.00 157.88 ? 200 GLY A N   1 
ATOM   1580 C  CA  . GLY A 1 200 ? -8.801  -3.148  61.692 1.00 154.67 ? 200 GLY A CA  1 
ATOM   1581 C  C   . GLY A 1 200 ? -9.282  -4.554  61.976 1.00 151.30 ? 200 GLY A C   1 
ATOM   1582 O  O   . GLY A 1 200 ? -8.857  -5.173  62.954 1.00 155.70 ? 200 GLY A O   1 
ATOM   1583 N  N   . THR A 1 201 ? -10.192 -5.067  61.149 1.00 146.31 ? 201 THR A N   1 
ATOM   1584 C  CA  . THR A 1 201 ? -10.632 -6.450  61.269 1.00 143.45 ? 201 THR A CA  1 
ATOM   1585 C  C   . THR A 1 201 ? -10.696 -7.080  59.889 1.00 143.10 ? 201 THR A C   1 
ATOM   1586 O  O   . THR A 1 201 ? -10.683 -6.397  58.862 1.00 142.60 ? 201 THR A O   1 
ATOM   1587 C  CB  . THR A 1 201 ? -12.017 -6.605  61.918 1.00 140.56 ? 201 THR A CB  1 
ATOM   1588 O  OG1 . THR A 1 201 ? -13.024 -6.540  60.900 1.00 133.69 ? 201 THR A OG1 1 
ATOM   1589 C  CG2 . THR A 1 201 ? -12.288 -5.537  62.952 1.00 142.56 ? 201 THR A CG2 1 
ATOM   1590 N  N   . LEU A 1 202 ? -10.801 -8.404  59.885 1.00 140.39 ? 202 LEU A N   1 
ATOM   1591 C  CA  . LEU A 1 202 ? -11.006 -9.189  58.678 1.00 136.09 ? 202 LEU A CA  1 
ATOM   1592 C  C   . LEU A 1 202 ? -12.386 -9.828  58.739 1.00 135.58 ? 202 LEU A C   1 
ATOM   1593 O  O   . LEU A 1 202 ? -12.747 -10.435 59.753 1.00 136.66 ? 202 LEU A O   1 
ATOM   1594 C  CB  . LEU A 1 202 ? -9.920  -10.256 58.542 1.00 134.92 ? 202 LEU A CB  1 
ATOM   1595 C  CG  . LEU A 1 202 ? -10.022 -11.245 57.385 1.00 132.45 ? 202 LEU A CG  1 
ATOM   1596 C  CD1 . LEU A 1 202 ? -8.643  -11.480 56.829 1.00 131.30 ? 202 LEU A CD1 1 
ATOM   1597 C  CD2 . LEU A 1 202 ? -10.633 -12.557 57.843 1.00 134.07 ? 202 LEU A CD2 1 
ATOM   1598 N  N   . LEU A 1 203 ? -13.150 -9.700  57.657 1.00 132.09 ? 203 LEU A N   1 
ATOM   1599 C  CA  . LEU A 1 203 ? -14.520 -10.195 57.604 1.00 127.85 ? 203 LEU A CA  1 
ATOM   1600 C  C   . LEU A 1 203 ? -14.587 -11.411 56.685 1.00 119.40 ? 203 LEU A C   1 
ATOM   1601 O  O   . LEU A 1 203 ? -14.224 -11.331 55.507 1.00 117.11 ? 203 LEU A O   1 
ATOM   1602 C  CB  . LEU A 1 203 ? -15.478 -9.095  57.137 1.00 126.81 ? 203 LEU A CB  1 
ATOM   1603 C  CG  . LEU A 1 203 ? -16.803 -9.526  56.508 1.00 127.13 ? 203 LEU A CG  1 
ATOM   1604 C  CD1 . LEU A 1 203 ? -17.637 -10.260 57.540 1.00 135.85 ? 203 LEU A CD1 1 
ATOM   1605 C  CD2 . LEU A 1 203 ? -17.568 -8.335  55.957 1.00 122.44 ? 203 LEU A CD2 1 
ATOM   1606 N  N   . LEU A 1 204 ? -15.045 -12.532 57.234 1.00 126.68 ? 204 LEU A N   1 
ATOM   1607 C  CA  . LEU A 1 204 ? -15.302 -13.763 56.495 1.00 130.87 ? 204 LEU A CA  1 
ATOM   1608 C  C   . LEU A 1 204 ? -16.808 -13.951 56.333 1.00 136.36 ? 204 LEU A C   1 
ATOM   1609 O  O   . LEU A 1 204 ? -17.569 -13.770 57.291 1.00 138.48 ? 204 LEU A O   1 
ATOM   1610 C  CB  . LEU A 1 204 ? -14.661 -14.950 57.231 1.00 131.50 ? 204 LEU A CB  1 
ATOM   1611 C  CG  . LEU A 1 204 ? -14.662 -16.459 56.868 1.00 134.95 ? 204 LEU A CG  1 
ATOM   1612 C  CD1 . LEU A 1 204 ? -16.010 -17.149 56.916 1.00 141.77 ? 204 LEU A CD1 1 
ATOM   1613 C  CD2 . LEU A 1 204 ? -13.957 -16.751 55.485 1.00 130.65 ? 204 LEU A CD2 1 
ATOM   1614 N  N   . ASN A 1 205 ? -17.238 -14.296 55.121 1.00 132.16 ? 205 ASN A N   1 
ATOM   1615 C  CA  . ASN A 1 205 ? -18.654 -14.485 54.806 1.00 143.43 ? 205 ASN A CA  1 
ATOM   1616 C  C   . ASN A 1 205 ? -18.899 -15.973 54.571 1.00 159.71 ? 205 ASN A C   1 
ATOM   1617 O  O   . ASN A 1 205 ? -18.969 -16.439 53.433 1.00 153.51 ? 205 ASN A O   1 
ATOM   1618 C  CB  . ASN A 1 205 ? -19.067 -13.653 53.584 1.00 136.59 ? 205 ASN A CB  1 
ATOM   1619 C  CG  . ASN A 1 205 ? -19.224 -12.182 53.905 1.00 131.19 ? 205 ASN A CG  1 
ATOM   1620 O  OD1 . ASN A 1 205 ? -18.647 -11.680 54.867 1.00 127.86 ? 205 ASN A OD1 1 
ATOM   1621 N  ND2 . ASN A 1 205 ? -20.003 -11.480 53.092 1.00 129.85 ? 205 ASN A ND2 1 
ATOM   1622 N  N   . GLY A 1 206 ? -19.061 -16.717 55.662 1.00 184.83 ? 206 GLY A N   1 
ATOM   1623 C  CA  . GLY A 1 206 ? -19.309 -18.144 55.573 1.00 194.89 ? 206 GLY A CA  1 
ATOM   1624 C  C   . GLY A 1 206 ? -18.090 -18.942 55.156 1.00 193.54 ? 206 GLY A C   1 
ATOM   1625 O  O   . GLY A 1 206 ? -17.513 -18.692 54.094 1.00 201.20 ? 206 GLY A O   1 
ATOM   1626 N  N   . ARG A 1 207 ? -17.694 -19.918 55.979 1.00 183.21 ? 207 ARG A N   1 
ATOM   1627 C  CA  . ARG A 1 207 ? -16.465 -20.665 55.731 1.00 166.92 ? 207 ARG A CA  1 
ATOM   1628 C  C   . ARG A 1 207 ? -16.506 -21.477 54.441 1.00 157.41 ? 207 ARG A C   1 
ATOM   1629 O  O   . ARG A 1 207 ? -15.453 -21.945 53.994 1.00 156.13 ? 207 ARG A O   1 
ATOM   1630 C  CB  . ARG A 1 207 ? -16.160 -21.586 56.917 1.00 166.36 ? 207 ARG A CB  1 
ATOM   1631 C  CG  . ARG A 1 207 ? -15.811 -20.848 58.205 1.00 167.52 ? 207 ARG A CG  1 
ATOM   1632 C  CD  . ARG A 1 207 ? -14.358 -21.072 58.614 1.00 165.35 ? 207 ARG A CD  1 
ATOM   1633 N  NE  . ARG A 1 207 ? -13.860 -20.001 59.475 1.00 164.34 ? 207 ARG A NE  1 
ATOM   1634 C  CZ  . ARG A 1 207 ? -12.625 -19.943 59.964 1.00 156.74 ? 207 ARG A CZ  1 
ATOM   1635 N  NH1 . ARG A 1 207 ? -11.750 -20.899 59.680 1.00 151.01 ? 207 ARG A NH1 1 
ATOM   1636 N  NH2 . ARG A 1 207 ? -12.263 -18.928 60.738 1.00 153.47 ? 207 ARG A NH2 1 
ATOM   1637 N  N   . GLU A 1 208 ? -17.690 -21.659 53.831 1.00 152.30 ? 208 GLU A N   1 
ATOM   1638 C  CA  . GLU A 1 208 ? -17.704 -22.335 52.543 1.00 144.78 ? 208 GLU A CA  1 
ATOM   1639 C  C   . GLU A 1 208 ? -17.485 -21.332 51.413 1.00 140.51 ? 208 GLU A C   1 
ATOM   1640 O  O   . GLU A 1 208 ? -17.896 -20.171 51.517 1.00 152.89 ? 208 GLU A O   1 
ATOM   1641 C  CB  . GLU A 1 208 ? -19.030 -23.064 52.338 1.00 149.12 ? 208 GLU A CB  1 
ATOM   1642 C  CG  . GLU A 1 208 ? -20.255 -22.175 52.448 1.00 155.56 ? 208 GLU A CG  1 
ATOM   1643 C  CD  . GLU A 1 208 ? -21.537 -22.910 52.115 1.00 160.17 ? 208 GLU A CD  1 
ATOM   1644 O  OE1 . GLU A 1 208 ? -22.467 -22.896 52.949 1.00 163.80 ? 208 GLU A OE1 1 
ATOM   1645 O  OE2 . GLU A 1 208 ? -21.615 -23.503 51.018 1.00 157.74 ? 208 GLU A OE2 1 
ATOM   1646 N  N   . PRO A 1 209 ? -16.825 -21.751 50.332 1.00 126.20 ? 209 PRO A N   1 
ATOM   1647 C  CA  . PRO A 1 209 ? -16.538 -20.819 49.231 1.00 114.77 ? 209 PRO A CA  1 
ATOM   1648 C  C   . PRO A 1 209 ? -17.809 -20.250 48.616 1.00 117.62 ? 209 PRO A C   1 
ATOM   1649 O  O   . PRO A 1 209 ? -18.800 -20.958 48.429 1.00 127.95 ? 209 PRO A O   1 
ATOM   1650 C  CB  . PRO A 1 209 ? -15.766 -21.685 48.229 1.00 108.87 ? 209 PRO A CB  1 
ATOM   1651 C  CG  . PRO A 1 209 ? -15.187 -22.791 49.050 1.00 109.62 ? 209 PRO A CG  1 
ATOM   1652 C  CD  . PRO A 1 209 ? -16.196 -23.067 50.123 1.00 119.92 ? 209 PRO A CD  1 
HETATM 1653 N  N   . MSE A 1 210 ? -17.770 -18.956 48.305 1.00 115.35 ? 210 MSE A N   1 
HETATM 1654 C  CA  . MSE A 1 210 ? -18.913 -18.288 47.696 1.00 123.25 ? 210 MSE A CA  1 
HETATM 1655 C  C   . MSE A 1 210 ? -19.342 -18.954 46.403 1.00 133.68 ? 210 MSE A C   1 
HETATM 1656 O  O   . MSE A 1 210 ? -18.510 -19.441 45.640 1.00 133.61 ? 210 MSE A O   1 
HETATM 1657 C  CB  . MSE A 1 210 ? -18.608 -16.812 47.416 1.00 117.76 ? 210 MSE A CB  1 
HETATM 1658 C  CG  . MSE A 1 210 ? -19.741 -16.102 46.676 1.00 122.78 ? 210 MSE A CG  1 
HETATM 1659 SE SE  . MSE A 1 210 ? -19.644 -14.173 46.658 0.48 128.81 ? 210 MSE A SE  1 
HETATM 1660 C  CE  . MSE A 1 210 ? -18.433 -13.970 48.145 1.00 128.08 ? 210 MSE A CE  1 
ATOM   1661 N  N   . ASP A 1 211 ? -20.651 -18.974 46.169 1.00 144.16 ? 211 ASP A N   1 
ATOM   1662 C  CA  . ASP A 1 211 ? -21.221 -19.378 44.893 1.00 144.55 ? 211 ASP A CA  1 
ATOM   1663 C  C   . ASP A 1 211 ? -22.161 -18.277 44.427 1.00 149.27 ? 211 ASP A C   1 
ATOM   1664 O  O   . ASP A 1 211 ? -23.157 -17.985 45.098 1.00 154.46 ? 211 ASP A O   1 
ATOM   1665 C  CB  . ASP A 1 211 ? -21.960 -20.708 45.021 1.00 144.01 ? 211 ASP A CB  1 
ATOM   1666 C  CG  . ASP A 1 211 ? -22.242 -21.344 43.683 1.00 141.83 ? 211 ASP A CG  1 
ATOM   1667 O  OD1 . ASP A 1 211 ? -21.824 -20.769 42.654 1.00 138.22 ? 211 ASP A OD1 1 
ATOM   1668 O  OD2 . ASP A 1 211 ? -22.885 -22.413 43.656 1.00 145.13 ? 211 ASP A OD2 1 
ATOM   1669 N  N   . GLU A 1 212 ? -21.838 -17.659 43.288 1.00 149.11 ? 212 GLU A N   1 
ATOM   1670 C  CA  . GLU A 1 212 ? -22.670 -16.590 42.749 1.00 154.26 ? 212 GLU A CA  1 
ATOM   1671 C  C   . GLU A 1 212 ? -24.049 -17.073 42.317 1.00 158.16 ? 212 GLU A C   1 
ATOM   1672 O  O   . GLU A 1 212 ? -24.929 -16.240 42.080 1.00 166.65 ? 212 GLU A O   1 
ATOM   1673 C  CB  . GLU A 1 212 ? -21.967 -15.916 41.567 1.00 152.74 ? 212 GLU A CB  1 
ATOM   1674 C  CG  . GLU A 1 212 ? -21.396 -16.883 40.541 1.00 152.42 ? 212 GLU A CG  1 
ATOM   1675 C  CD  . GLU A 1 212 ? -19.889 -17.012 40.638 1.00 151.06 ? 212 GLU A CD  1 
ATOM   1676 O  OE1 . GLU A 1 212 ? -19.371 -17.085 41.771 1.00 153.41 ? 212 GLU A OE1 1 
ATOM   1677 O  OE2 . GLU A 1 212 ? -19.222 -17.040 39.582 1.00 148.83 ? 212 GLU A OE2 1 
ATOM   1678 N  N   . THR A 1 213 ? -24.258 -18.385 42.211 1.00 148.69 ? 213 THR A N   1 
ATOM   1679 C  CA  . THR A 1 213 ? -25.554 -18.932 41.832 1.00 145.33 ? 213 THR A CA  1 
ATOM   1680 C  C   . THR A 1 213 ? -26.468 -19.189 43.024 1.00 146.16 ? 213 THR A C   1 
ATOM   1681 O  O   . THR A 1 213 ? -27.668 -19.410 42.825 1.00 145.64 ? 213 THR A O   1 
ATOM   1682 C  CB  . THR A 1 213 ? -25.373 -20.236 41.043 1.00 139.30 ? 213 THR A CB  1 
ATOM   1683 O  OG1 . THR A 1 213 ? -24.299 -20.998 41.607 1.00 134.18 ? 213 THR A OG1 1 
ATOM   1684 C  CG2 . THR A 1 213 ? -25.059 -19.938 39.585 1.00 132.21 ? 213 THR A CG2 1 
ATOM   1685 N  N   . ARG A 1 214 ? -25.942 -19.169 44.246 1.00 146.30 ? 214 ARG A N   1 
ATOM   1686 C  CA  . ARG A 1 214 ? -26.749 -19.397 45.439 1.00 155.48 ? 214 ARG A CA  1 
ATOM   1687 C  C   . ARG A 1 214 ? -27.231 -18.054 45.978 1.00 160.94 ? 214 ARG A C   1 
ATOM   1688 O  O   . ARG A 1 214 ? -26.418 -17.169 46.268 1.00 158.28 ? 214 ARG A O   1 
ATOM   1689 C  CB  . ARG A 1 214 ? -25.954 -20.153 46.504 1.00 155.56 ? 214 ARG A CB  1 
ATOM   1690 C  CG  . ARG A 1 214 ? -25.280 -21.433 46.020 1.00 158.70 ? 214 ARG A CG  1 
ATOM   1691 C  CD  . ARG A 1 214 ? -26.172 -22.254 45.097 1.00 167.32 ? 214 ARG A CD  1 
ATOM   1692 N  NE  . ARG A 1 214 ? -25.413 -23.287 44.395 1.00 164.48 ? 214 ARG A NE  1 
ATOM   1693 C  CZ  . ARG A 1 214 ? -25.748 -23.790 43.211 1.00 166.04 ? 214 ARG A CZ  1 
ATOM   1694 N  NH1 . ARG A 1 214 ? -26.833 -23.354 42.585 1.00 172.27 ? 214 ARG A NH1 1 
ATOM   1695 N  NH2 . ARG A 1 214 ? -24.996 -24.727 42.650 1.00 161.48 ? 214 ARG A NH2 1 
ATOM   1696 N  N   . ARG A 1 215 ? -28.553 -17.909 46.113 1.00 176.08 ? 215 ARG A N   1 
ATOM   1697 C  CA  . ARG A 1 215 ? -29.125 -16.642 46.562 1.00 176.22 ? 215 ARG A CA  1 
ATOM   1698 C  C   . ARG A 1 215 ? -28.691 -16.300 47.980 1.00 173.08 ? 215 ARG A C   1 
ATOM   1699 O  O   . ARG A 1 215 ? -28.602 -15.118 48.335 1.00 174.86 ? 215 ARG A O   1 
ATOM   1700 C  CB  . ARG A 1 215 ? -30.650 -16.694 46.476 1.00 182.89 ? 215 ARG A CB  1 
ATOM   1701 C  CG  . ARG A 1 215 ? -31.178 -17.239 45.161 1.00 185.15 ? 215 ARG A CG  1 
ATOM   1702 C  CD  . ARG A 1 215 ? -30.604 -16.473 43.981 1.00 182.42 ? 215 ARG A CD  1 
ATOM   1703 N  NE  . ARG A 1 215 ? -31.264 -16.827 42.728 1.00 180.88 ? 215 ARG A NE  1 
ATOM   1704 C  CZ  . ARG A 1 215 ? -30.860 -16.419 41.530 1.00 175.01 ? 215 ARG A CZ  1 
ATOM   1705 N  NH1 . ARG A 1 215 ? -29.794 -15.639 41.417 1.00 168.30 ? 215 ARG A NH1 1 
ATOM   1706 N  NH2 . ARG A 1 215 ? -31.523 -16.792 40.444 1.00 177.25 ? 215 ARG A NH2 1 
ATOM   1707 N  N   . GLU A 1 216 ? -28.432 -17.313 48.803 1.00 169.86 ? 216 GLU A N   1 
ATOM   1708 C  CA  . GLU A 1 216 ? -27.915 -17.114 50.151 1.00 166.15 ? 216 GLU A CA  1 
ATOM   1709 C  C   . GLU A 1 216 ? -26.569 -16.407 50.106 1.00 154.46 ? 216 GLU A C   1 
ATOM   1710 O  O   . GLU A 1 216 ? -26.430 -15.291 50.618 1.00 151.02 ? 216 GLU A O   1 
ATOM   1711 C  CB  . GLU A 1 216 ? -27.785 -18.453 50.883 1.00 169.95 ? 216 GLU A CB  1 
ATOM   1712 C  CG  . GLU A 1 216 ? -28.944 -19.426 50.658 1.00 172.05 ? 216 GLU A CG  1 
ATOM   1713 C  CD  . GLU A 1 216 ? -28.837 -20.210 49.357 1.00 170.09 ? 216 GLU A CD  1 
ATOM   1714 O  OE1 . GLU A 1 216 ? -28.638 -19.586 48.293 1.00 167.22 ? 216 GLU A OE1 1 
ATOM   1715 O  OE2 . GLU A 1 216 ? -28.962 -21.453 49.399 1.00 170.24 ? 216 GLU A OE2 1 
ATOM   1716 N  N   . HIS A 1 217 ? -25.576 -17.047 49.480 1.00 152.31 ? 217 HIS A N   1 
ATOM   1717 C  CA  . HIS A 1 217 ? -24.250 -16.445 49.379 1.00 150.48 ? 217 HIS A CA  1 
ATOM   1718 C  C   . HIS A 1 217 ? -24.301 -15.095 48.676 1.00 148.98 ? 217 HIS A C   1 
ATOM   1719 O  O   . HIS A 1 217 ? -23.433 -14.243 48.898 1.00 139.40 ? 217 HIS A O   1 
ATOM   1720 C  CB  . HIS A 1 217 ? -23.291 -17.390 48.647 1.00 139.81 ? 217 HIS A CB  1 
ATOM   1721 C  CG  . HIS A 1 217 ? -23.084 -18.704 49.339 1.00 146.24 ? 217 HIS A CG  1 
ATOM   1722 N  ND1 . HIS A 1 217 ? -22.200 -19.657 48.877 1.00 143.44 ? 217 HIS A ND1 1 
ATOM   1723 C  CD2 . HIS A 1 217 ? -23.656 -19.231 50.448 1.00 148.13 ? 217 HIS A CD2 1 
ATOM   1724 C  CE1 . HIS A 1 217 ? -22.228 -20.707 49.679 1.00 140.57 ? 217 HIS A CE1 1 
ATOM   1725 N  NE2 . HIS A 1 217 ? -23.106 -20.475 50.638 1.00 143.31 ? 217 HIS A NE2 1 
ATOM   1726 N  N   . PHE A 1 218 ? -25.302 -14.886 47.819 1.00 151.80 ? 218 PHE A N   1 
ATOM   1727 C  CA  . PHE A 1 218 ? -25.514 -13.575 47.215 1.00 152.51 ? 218 PHE A CA  1 
ATOM   1728 C  C   . PHE A 1 218 ? -25.869 -12.536 48.274 1.00 156.27 ? 218 PHE A C   1 
ATOM   1729 O  O   . PHE A 1 218 ? -25.250 -11.468 48.342 1.00 158.60 ? 218 PHE A O   1 
ATOM   1730 C  CB  . PHE A 1 218 ? -26.619 -13.675 46.158 1.00 159.37 ? 218 PHE A CB  1 
ATOM   1731 C  CG  . PHE A 1 218 ? -26.707 -12.490 45.231 1.00 163.57 ? 218 PHE A CG  1 
ATOM   1732 C  CD1 . PHE A 1 218 ? -25.818 -11.429 45.327 1.00 163.71 ? 218 PHE A CD1 1 
ATOM   1733 C  CD2 . PHE A 1 218 ? -27.692 -12.443 44.257 1.00 165.45 ? 218 PHE A CD2 1 
ATOM   1734 C  CE1 . PHE A 1 218 ? -25.913 -10.347 44.473 1.00 162.73 ? 218 PHE A CE1 1 
ATOM   1735 C  CE2 . PHE A 1 218 ? -27.789 -11.365 43.401 1.00 165.62 ? 218 PHE A CE2 1 
ATOM   1736 C  CZ  . PHE A 1 218 ? -26.898 -10.317 43.509 1.00 163.82 ? 218 PHE A CZ  1 
ATOM   1737 N  N   . GLU A 1 219 ? -26.863 -12.836 49.114 1.00 157.07 ? 219 GLU A N   1 
ATOM   1738 C  CA  . GLU A 1 219 ? -27.377 -11.834 50.043 1.00 157.18 ? 219 GLU A CA  1 
ATOM   1739 C  C   . GLU A 1 219 ? -26.396 -11.538 51.171 1.00 156.87 ? 219 GLU A C   1 
ATOM   1740 O  O   . GLU A 1 219 ? -26.360 -10.407 51.671 1.00 156.89 ? 219 GLU A O   1 
ATOM   1741 C  CB  . GLU A 1 219 ? -28.718 -12.293 50.615 1.00 164.17 ? 219 GLU A CB  1 
ATOM   1742 C  CG  . GLU A 1 219 ? -29.854 -12.256 49.607 1.00 168.24 ? 219 GLU A CG  1 
ATOM   1743 C  CD  . GLU A 1 219 ? -31.093 -12.982 50.092 1.00 174.06 ? 219 GLU A CD  1 
ATOM   1744 O  OE1 . GLU A 1 219 ? -31.947 -13.323 49.247 1.00 175.92 ? 219 GLU A OE1 1 
ATOM   1745 O  OE2 . GLU A 1 219 ? -31.214 -13.210 51.314 1.00 175.73 ? 219 GLU A OE2 1 
ATOM   1746 N  N   . ARG A 1 220 ? -25.607 -12.533 51.590 1.00 160.45 ? 220 ARG A N   1 
ATOM   1747 C  CA  . ARG A 1 220 ? -24.654 -12.322 52.677 1.00 161.36 ? 220 ARG A CA  1 
ATOM   1748 C  C   . ARG A 1 220 ? -23.681 -11.201 52.338 1.00 156.68 ? 220 ARG A C   1 
ATOM   1749 O  O   . ARG A 1 220 ? -23.508 -10.255 53.117 1.00 159.69 ? 220 ARG A O   1 
ATOM   1750 C  CB  . ARG A 1 220 ? -23.889 -13.614 52.983 1.00 166.27 ? 220 ARG A CB  1 
ATOM   1751 C  CG  . ARG A 1 220 ? -24.747 -14.843 53.286 1.00 175.09 ? 220 ARG A CG  1 
ATOM   1752 C  CD  . ARG A 1 220 ? -23.900 -15.936 53.912 1.00 175.99 ? 220 ARG A CD  1 
ATOM   1753 N  NE  . ARG A 1 220 ? -23.269 -16.816 52.931 1.00 179.87 ? 220 ARG A NE  1 
ATOM   1754 C  CZ  . ARG A 1 220 ? -21.974 -16.790 52.626 1.00 185.10 ? 220 ARG A CZ  1 
ATOM   1755 N  NH1 . ARG A 1 220 ? -21.177 -15.893 53.192 1.00 187.77 ? 220 ARG A NH1 1 
ATOM   1756 N  NH2 . ARG A 1 220 ? -21.474 -17.638 51.733 1.00 183.30 ? 220 ARG A NH2 1 
ATOM   1757 N  N   . VAL A 1 221 ? -23.042 -11.290 51.169 1.00 153.16 ? 221 VAL A N   1 
ATOM   1758 C  CA  . VAL A 1 221 ? -22.093 -10.264 50.751 1.00 147.66 ? 221 VAL A CA  1 
ATOM   1759 C  C   . VAL A 1 221 ? -22.820 -8.999  50.321 1.00 146.51 ? 221 VAL A C   1 
ATOM   1760 O  O   . VAL A 1 221 ? -22.296 -7.889  50.479 1.00 142.65 ? 221 VAL A O   1 
ATOM   1761 C  CB  . VAL A 1 221 ? -21.195 -10.809 49.629 1.00 140.47 ? 221 VAL A CB  1 
ATOM   1762 C  CG1 . VAL A 1 221 ? -19.945 -9.952  49.479 1.00 135.24 ? 221 VAL A CG1 1 
ATOM   1763 C  CG2 . VAL A 1 221 ? -20.833 -12.249 49.914 1.00 137.85 ? 221 VAL A CG2 1 
ATOM   1764 N  N   . GLY A 1 222 ? -24.022 -9.134  49.769 1.00 151.75 ? 222 GLY A N   1 
ATOM   1765 C  CA  . GLY A 1 222 ? -24.840 -7.977  49.472 1.00 158.74 ? 222 GLY A CA  1 
ATOM   1766 C  C   . GLY A 1 222 ? -25.167 -7.190  50.725 1.00 164.31 ? 222 GLY A C   1 
ATOM   1767 O  O   . GLY A 1 222 ? -24.704 -6.056  50.883 1.00 165.27 ? 222 GLY A O   1 
ATOM   1768 N  N   . GLU A 1 223 ? -25.945 -7.794  51.634 1.00 167.01 ? 223 GLU A N   1 
ATOM   1769 C  CA  . GLU A 1 223 ? -26.293 -7.127  52.887 1.00 168.31 ? 223 GLU A CA  1 
ATOM   1770 C  C   . GLU A 1 223 ? -25.055 -6.658  53.640 1.00 162.00 ? 223 GLU A C   1 
ATOM   1771 O  O   . GLU A 1 223 ? -25.121 -5.677  54.392 1.00 164.30 ? 223 GLU A O   1 
ATOM   1772 C  CB  . GLU A 1 223 ? -27.122 -8.053  53.778 1.00 169.76 ? 223 GLU A CB  1 
ATOM   1773 C  CG  . GLU A 1 223 ? -28.445 -8.484  53.180 1.00 169.85 ? 223 GLU A CG  1 
ATOM   1774 C  CD  . GLU A 1 223 ? -29.082 -9.617  53.955 1.00 173.40 ? 223 GLU A CD  1 
ATOM   1775 O  OE1 . GLU A 1 223 ? -28.468 -10.081 54.938 1.00 173.66 ? 223 GLU A OE1 1 
ATOM   1776 O  OE2 . GLU A 1 223 ? -30.195 -10.043 53.585 1.00 177.46 ? 223 GLU A OE2 1 
ATOM   1777 N  N   . ALA A 1 224 ? -23.922 -7.339  53.452 1.00 153.59 ? 224 ALA A N   1 
ATOM   1778 C  CA  . ALA A 1 224 ? -22.656 -6.869  53.997 1.00 151.25 ? 224 ALA A CA  1 
ATOM   1779 C  C   . ALA A 1 224 ? -22.335 -5.487  53.449 1.00 157.22 ? 224 ALA A C   1 
ATOM   1780 O  O   . ALA A 1 224 ? -22.480 -4.488  54.158 1.00 169.79 ? 224 ALA A O   1 
ATOM   1781 C  CB  . ALA A 1 224 ? -21.521 -7.842  53.674 1.00 147.43 ? 224 ALA A CB  1 
ATOM   1782 N  N   . ASP A 1 225 ? -21.913 -5.424  52.181 1.00 149.70 ? 225 ASP A N   1 
ATOM   1783 C  CA  . ASP A 1 225 ? -21.458 -4.173  51.582 1.00 149.64 ? 225 ASP A CA  1 
ATOM   1784 C  C   . ASP A 1 225 ? -22.436 -3.022  51.787 1.00 154.17 ? 225 ASP A C   1 
ATOM   1785 O  O   . ASP A 1 225 ? -22.019 -1.858  51.753 1.00 156.33 ? 225 ASP A O   1 
ATOM   1786 C  CB  . ASP A 1 225 ? -21.202 -4.374  50.085 1.00 150.24 ? 225 ASP A CB  1 
ATOM   1787 C  CG  . ASP A 1 225 ? -19.975 -5.228  49.811 1.00 147.74 ? 225 ASP A CG  1 
ATOM   1788 O  OD1 . ASP A 1 225 ? -19.081 -5.287  50.682 1.00 149.37 ? 225 ASP A OD1 1 
ATOM   1789 O  OD2 . ASP A 1 225 ? -19.906 -5.839  48.723 1.00 142.25 ? 225 ASP A OD2 1 
ATOM   1790 N  N   . ILE A 1 226 ? -23.724 -3.312  51.992 1.00 155.48 ? 226 ILE A N   1 
ATOM   1791 C  CA  . ILE A 1 226 ? -24.654 -2.260  52.392 1.00 158.96 ? 226 ILE A CA  1 
ATOM   1792 C  C   . ILE A 1 226 ? -24.264 -1.697  53.755 1.00 162.14 ? 226 ILE A C   1 
ATOM   1793 O  O   . ILE A 1 226 ? -24.207 -0.473  53.941 1.00 165.93 ? 226 ILE A O   1 
ATOM   1794 C  CB  . ILE A 1 226 ? -26.111 -2.768  52.376 1.00 157.82 ? 226 ILE A CB  1 
ATOM   1795 C  CG1 . ILE A 1 226 ? -26.560 -3.118  50.955 1.00 156.41 ? 226 ILE A CG1 1 
ATOM   1796 C  CG2 . ILE A 1 226 ? -27.042 -1.719  52.965 1.00 162.95 ? 226 ILE A CG2 1 
ATOM   1797 C  CD1 . ILE A 1 226 ? -27.445 -4.341  50.868 1.00 157.49 ? 226 ILE A CD1 1 
ATOM   1798 N  N   . LYS A 1 227 ? -23.981 -2.571  54.726 1.00 156.16 ? 227 LYS A N   1 
ATOM   1799 C  CA  . LYS A 1 227 ? -23.460 -2.103  56.005 1.00 157.73 ? 227 LYS A CA  1 
ATOM   1800 C  C   . LYS A 1 227 ? -22.122 -1.399  55.814 1.00 164.92 ? 227 LYS A C   1 
ATOM   1801 O  O   . LYS A 1 227 ? -21.969 -0.229  56.179 1.00 169.72 ? 227 LYS A O   1 
ATOM   1802 C  CB  . LYS A 1 227 ? -23.335 -3.272  56.984 1.00 157.58 ? 227 LYS A CB  1 
ATOM   1803 N  N   . LEU A 1 228 ? -21.150 -2.091  55.200 1.00 157.11 ? 228 LEU A N   1 
ATOM   1804 C  CA  . LEU A 1 228 ? -19.810 -1.534  55.015 1.00 155.10 ? 228 LEU A CA  1 
ATOM   1805 C  C   . LEU A 1 228 ? -19.836 -0.105  54.486 1.00 158.04 ? 228 LEU A C   1 
ATOM   1806 O  O   . LEU A 1 228 ? -18.946 0.691   54.806 1.00 163.66 ? 228 LEU A O   1 
ATOM   1807 C  CB  . LEU A 1 228 ? -18.989 -2.408  54.061 1.00 151.73 ? 228 LEU A CB  1 
ATOM   1808 C  CG  . LEU A 1 228 ? -18.382 -3.738  54.519 1.00 153.52 ? 228 LEU A CG  1 
ATOM   1809 C  CD1 . LEU A 1 228 ? -17.594 -3.553  55.810 1.00 154.97 ? 228 LEU A CD1 1 
ATOM   1810 C  CD2 . LEU A 1 228 ? -19.404 -4.844  54.655 1.00 157.01 ? 228 LEU A CD2 1 
HETATM 1811 N  N   . MSE A 1 229 ? -20.841 0.243   53.690 1.00 155.92 ? 229 MSE A N   1 
HETATM 1812 C  CA  . MSE A 1 229 ? -20.956 1.604   53.186 1.00 155.42 ? 229 MSE A CA  1 
HETATM 1813 C  C   . MSE A 1 229 ? -21.734 2.500   54.150 1.00 161.91 ? 229 MSE A C   1 
HETATM 1814 O  O   . MSE A 1 229 ? -21.560 3.719   54.153 1.00 164.88 ? 229 MSE A O   1 
HETATM 1815 C  CB  . MSE A 1 229 ? -21.614 1.614   51.804 1.00 155.93 ? 229 MSE A CB  1 
HETATM 1816 C  CG  . MSE A 1 229 ? -21.570 2.969   51.106 1.00 161.91 ? 229 MSE A CG  1 
HETATM 1817 SE SE  . MSE A 1 229 ? -19.799 3.418   50.415 0.55 170.84 ? 229 MSE A SE  1 
HETATM 1818 C  CE  . MSE A 1 229 ? -18.972 4.187   52.005 1.00 173.26 ? 229 MSE A CE  1 
ATOM   1819 N  N   . GLU A 1 230 ? -22.586 1.891   54.977 1.00 163.95 ? 230 GLU A N   1 
ATOM   1820 C  CA  . GLU A 1 230 ? -23.336 2.668   55.960 1.00 167.90 ? 230 GLU A CA  1 
ATOM   1821 C  C   . GLU A 1 230 ? -22.402 3.341   56.958 1.00 173.42 ? 230 GLU A C   1 
ATOM   1822 O  O   . GLU A 1 230 ? -22.662 4.465   57.405 1.00 177.12 ? 230 GLU A O   1 
ATOM   1823 C  CB  . GLU A 1 230 ? -24.340 1.773   56.684 1.00 169.39 ? 230 GLU A CB  1 
ATOM   1824 C  CG  . GLU A 1 230 ? -25.762 1.869   56.162 1.00 171.05 ? 230 GLU A CG  1 
ATOM   1825 C  CD  . GLU A 1 230 ? -26.732 1.039   56.980 1.00 173.99 ? 230 GLU A CD  1 
ATOM   1826 O  OE1 . GLU A 1 230 ? -27.227 0.014   56.463 1.00 172.62 ? 230 GLU A OE1 1 
ATOM   1827 O  OE2 . GLU A 1 230 ? -27.000 1.412   58.143 1.00 177.86 ? 230 GLU A OE2 1 
ATOM   1828 N  N   . LEU A 1 231 ? -21.307 2.674   57.315 1.00 180.27 ? 231 LEU A N   1 
ATOM   1829 C  CA  . LEU A 1 231 ? -20.325 3.234   58.233 1.00 188.81 ? 231 LEU A CA  1 
ATOM   1830 C  C   . LEU A 1 231 ? -19.241 4.039   57.527 1.00 194.68 ? 231 LEU A C   1 
ATOM   1831 O  O   . LEU A 1 231 ? -18.348 4.564   58.199 1.00 206.03 ? 231 LEU A O   1 
ATOM   1832 C  CB  . LEU A 1 231 ? -19.667 2.126   59.069 1.00 188.50 ? 231 LEU A CB  1 
ATOM   1833 C  CG  . LEU A 1 231 ? -20.495 1.072   59.814 1.00 191.84 ? 231 LEU A CG  1 
ATOM   1834 C  CD1 . LEU A 1 231 ? -20.833 -0.119  58.935 1.00 188.16 ? 231 LEU A CD1 1 
ATOM   1835 C  CD2 . LEU A 1 231 ? -19.766 0.608   61.071 1.00 193.53 ? 231 LEU A CD2 1 
ATOM   1836 N  N   . GLY A 1 232 ? -19.294 4.151   56.202 1.00 183.15 ? 232 GLY A N   1 
ATOM   1837 C  CA  . GLY A 1 232 ? -18.273 4.879   55.476 1.00 178.38 ? 232 GLY A CA  1 
ATOM   1838 C  C   . GLY A 1 232 ? -16.972 4.132   55.304 1.00 164.80 ? 232 GLY A C   1 
ATOM   1839 O  O   . GLY A 1 232 ? -15.909 4.758   55.249 1.00 160.06 ? 232 GLY A O   1 
ATOM   1840 N  N   . TYR A 1 233 ? -17.022 2.804   55.208 1.00 161.48 ? 233 TYR A N   1 
ATOM   1841 C  CA  . TYR A 1 233 ? -15.823 1.978   55.141 1.00 163.74 ? 233 TYR A CA  1 
ATOM   1842 C  C   . TYR A 1 233 ? -15.480 1.526   53.731 1.00 159.06 ? 233 TYR A C   1 
ATOM   1843 O  O   . TYR A 1 233 ? -14.298 1.382   53.405 1.00 158.79 ? 233 TYR A O   1 
ATOM   1844 C  CB  . TYR A 1 233 ? -15.983 0.749   56.037 1.00 169.87 ? 233 TYR A CB  1 
ATOM   1845 C  CG  . TYR A 1 233 ? -15.841 1.077   57.496 1.00 174.77 ? 233 TYR A CG  1 
ATOM   1846 C  CD1 . TYR A 1 233 ? -16.673 0.505   58.441 1.00 177.78 ? 233 TYR A CD1 1 
ATOM   1847 C  CD2 . TYR A 1 233 ? -14.880 1.976   57.927 1.00 174.20 ? 233 TYR A CD2 1 
ATOM   1848 C  CE1 . TYR A 1 233 ? -16.545 0.817   59.776 1.00 181.47 ? 233 TYR A CE1 1 
ATOM   1849 C  CE2 . TYR A 1 233 ? -14.751 2.292   59.258 1.00 176.23 ? 233 TYR A CE2 1 
ATOM   1850 C  CZ  . TYR A 1 233 ? -15.581 1.704   60.180 1.00 179.37 ? 233 TYR A CZ  1 
ATOM   1851 O  OH  . TYR A 1 233 ? -15.453 2.012   61.514 1.00 180.37 ? 233 TYR A OH  1 
ATOM   1852 N  N   . LEU A 1 234 ? -16.479 1.293   52.896 1.00 156.29 ? 234 LEU A N   1 
ATOM   1853 C  CA  . LEU A 1 234 ? -16.233 0.842   51.533 1.00 151.54 ? 234 LEU A CA  1 
ATOM   1854 C  C   . LEU A 1 234 ? -15.529 1.942   50.745 1.00 148.41 ? 234 LEU A C   1 
ATOM   1855 O  O   . LEU A 1 234 ? -16.110 3.017   50.543 1.00 149.71 ? 234 LEU A O   1 
ATOM   1856 C  CB  . LEU A 1 234 ? -17.550 0.449   50.870 1.00 149.51 ? 234 LEU A CB  1 
ATOM   1857 C  CG  . LEU A 1 234 ? -17.491 -0.675  49.836 1.00 141.09 ? 234 LEU A CG  1 
ATOM   1858 C  CD1 . LEU A 1 234 ? -18.879 -1.226  49.556 1.00 138.65 ? 234 LEU A CD1 1 
ATOM   1859 C  CD2 . LEU A 1 234 ? -16.861 -0.159  48.568 1.00 139.08 ? 234 LEU A CD2 1 
ATOM   1860 N  N   . PRO A 1 235 ? -14.300 1.725   50.286 1.00 143.53 ? 235 PRO A N   1 
ATOM   1861 C  CA  . PRO A 1 235 ? -13.572 2.775   49.580 1.00 144.33 ? 235 PRO A CA  1 
ATOM   1862 C  C   . PRO A 1 235 ? -13.995 2.839   48.125 1.00 142.03 ? 235 PRO A C   1 
ATOM   1863 O  O   . PRO A 1 235 ? -14.532 1.862   47.582 1.00 139.78 ? 235 PRO A O   1 
ATOM   1864 C  CB  . PRO A 1 235 ? -12.110 2.330   49.718 1.00 142.60 ? 235 PRO A CB  1 
ATOM   1865 C  CG  . PRO A 1 235 ? -12.197 0.841   49.727 1.00 140.78 ? 235 PRO A CG  1 
ATOM   1866 C  CD  . PRO A 1 235 ? -13.515 0.483   50.381 1.00 140.30 ? 235 PRO A CD  1 
ATOM   1867 N  N   . PRO A 1 236 ? -13.774 3.970   47.461 1.00 143.17 ? 236 PRO A N   1 
ATOM   1868 C  CA  . PRO A 1 236 ? -14.172 4.092   46.055 1.00 142.26 ? 236 PRO A CA  1 
ATOM   1869 C  C   . PRO A 1 236 ? -13.385 3.149   45.157 1.00 134.44 ? 236 PRO A C   1 
ATOM   1870 O  O   . PRO A 1 236 ? -12.298 2.675   45.494 1.00 123.77 ? 236 PRO A O   1 
ATOM   1871 C  CB  . PRO A 1 236 ? -13.866 5.557   45.721 1.00 143.46 ? 236 PRO A CB  1 
ATOM   1872 C  CG  . PRO A 1 236 ? -13.799 6.249   47.048 1.00 148.07 ? 236 PRO A CG  1 
ATOM   1873 C  CD  . PRO A 1 236 ? -13.250 5.236   47.998 1.00 145.41 ? 236 PRO A CD  1 
ATOM   1874 N  N   . LEU A 1 237 ? -13.964 2.881   43.985 1.00 127.72 ? 237 LEU A N   1 
ATOM   1875 C  CA  . LEU A 1 237 ? -13.305 2.013   43.015 1.00 124.53 ? 237 LEU A CA  1 
ATOM   1876 C  C   . LEU A 1 237 ? -12.090 2.697   42.401 1.00 130.57 ? 237 LEU A C   1 
ATOM   1877 O  O   . LEU A 1 237 ? -11.046 2.063   42.209 1.00 133.39 ? 237 LEU A O   1 
ATOM   1878 C  CB  . LEU A 1 237 ? -14.298 1.597   41.930 1.00 123.48 ? 237 LEU A CB  1 
ATOM   1879 C  CG  . LEU A 1 237 ? -13.790 0.664   40.831 1.00 117.57 ? 237 LEU A CG  1 
ATOM   1880 C  CD1 . LEU A 1 237 ? -13.280 -0.638  41.424 1.00 116.03 ? 237 LEU A CD1 1 
ATOM   1881 C  CD2 . LEU A 1 237 ? -14.889 0.400   39.812 1.00 118.06 ? 237 LEU A CD2 1 
ATOM   1882 N  N   . ARG A 1 238 ? -12.205 3.989   42.090 1.00 141.71 ? 238 ARG A N   1 
ATOM   1883 C  CA  . ARG A 1 238 ? -11.103 4.763   41.520 1.00 145.04 ? 238 ARG A CA  1 
ATOM   1884 C  C   . ARG A 1 238 ? -10.404 5.507   42.654 1.00 158.44 ? 238 ARG A C   1 
ATOM   1885 O  O   . ARG A 1 238 ? -10.640 6.689   42.906 1.00 160.99 ? 238 ARG A O   1 
ATOM   1886 C  CB  . ARG A 1 238 ? -11.614 5.716   40.444 1.00 140.65 ? 238 ARG A CB  1 
ATOM   1887 C  CG  . ARG A 1 238 ? -12.022 5.031   39.154 1.00 132.79 ? 238 ARG A CG  1 
ATOM   1888 C  CD  . ARG A 1 238 ? -10.834 4.353   38.495 1.00 126.67 ? 238 ARG A CD  1 
ATOM   1889 N  NE  . ARG A 1 238 ? -9.995  5.295   37.760 1.00 122.25 ? 238 ARG A NE  1 
ATOM   1890 C  CZ  . ARG A 1 238 ? -8.843  4.973   37.182 1.00 121.56 ? 238 ARG A CZ  1 
ATOM   1891 N  NH1 . ARG A 1 238 ? -8.143  5.892   36.531 1.00 124.54 ? 238 ARG A NH1 1 
ATOM   1892 N  NH2 . ARG A 1 238 ? -8.388  3.730   37.254 1.00 122.97 ? 238 ARG A NH2 1 
ATOM   1893 N  N   . GLY A 1 239 ? -9.525  4.790   43.347 1.00 162.79 ? 239 GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 239 ? -8.785  5.356   44.459 1.00 167.06 ? 239 GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 239 ? -9.526  5.271   45.779 1.00 171.03 ? 239 GLY A C   1 
ATOM   1896 O  O   . GLY A 1 239 ? -10.312 6.154   46.122 1.00 174.76 ? 239 GLY A O   1 
ATOM   1897 O  OXT . GLY A 1 239 ? -9.356  4.319   46.540 1.00 169.49 ? 239 GLY A OXT 1 
ATOM   1898 N  N   . GLN B 2 1   ? -17.735 21.739  36.012 1.00 146.14 ? 84  GLN B N   1 
ATOM   1899 C  CA  . GLN B 2 1   ? -19.050 22.297  35.719 1.00 149.86 ? 84  GLN B CA  1 
ATOM   1900 C  C   . GLN B 2 1   ? -18.933 23.743  35.244 1.00 155.54 ? 84  GLN B C   1 
ATOM   1901 O  O   . GLN B 2 1   ? -18.157 24.524  35.791 1.00 158.75 ? 84  GLN B O   1 
ATOM   1902 C  CB  . GLN B 2 1   ? -19.954 22.214  36.951 1.00 150.76 ? 84  GLN B CB  1 
ATOM   1903 C  CG  . GLN B 2 1   ? -21.434 22.399  36.652 1.00 149.63 ? 84  GLN B CG  1 
ATOM   1904 C  CD  . GLN B 2 1   ? -22.077 23.472  37.512 1.00 147.07 ? 84  GLN B CD  1 
ATOM   1905 O  OE1 . GLN B 2 1   ? -21.732 24.650  37.419 1.00 143.87 ? 84  GLN B OE1 1 
ATOM   1906 N  NE2 . GLN B 2 1   ? -23.017 23.067  38.358 1.00 147.18 ? 84  GLN B NE2 1 
ATOM   1907 N  N   . GLY B 2 2   ? -19.717 24.093  34.228 1.00 159.01 ? 85  GLY B N   1 
ATOM   1908 C  CA  . GLY B 2 2   ? -19.650 25.412  33.626 1.00 161.44 ? 85  GLY B CA  1 
ATOM   1909 C  C   . GLY B 2 2   ? -19.607 25.323  32.116 1.00 161.47 ? 85  GLY B C   1 
ATOM   1910 O  O   . GLY B 2 2   ? -20.603 25.605  31.442 1.00 162.36 ? 85  GLY B O   1 
ATOM   1911 N  N   . ARG B 2 3   ? -18.446 24.935  31.583 1.00 160.32 ? 86  ARG B N   1 
ATOM   1912 C  CA  . ARG B 2 3   ? -18.282 24.561  30.181 1.00 155.01 ? 86  ARG B CA  1 
ATOM   1913 C  C   . ARG B 2 3   ? -18.761 25.646  29.223 1.00 157.03 ? 86  ARG B C   1 
ATOM   1914 O  O   . ARG B 2 3   ? -19.902 25.595  28.750 1.00 156.97 ? 86  ARG B O   1 
ATOM   1915 C  CB  . ARG B 2 3   ? -19.023 23.247  29.903 1.00 148.34 ? 86  ARG B CB  1 
ATOM   1916 C  CG  . ARG B 2 3   ? -18.818 22.179  30.973 1.00 143.49 ? 86  ARG B CG  1 
ATOM   1917 C  CD  . ARG B 2 3   ? -20.063 21.319  31.159 1.00 140.10 ? 86  ARG B CD  1 
ATOM   1918 N  NE  . ARG B 2 3   ? -20.088 20.664  32.465 1.00 138.32 ? 86  ARG B NE  1 
ATOM   1919 C  CZ  . ARG B 2 3   ? -21.053 19.846  32.877 1.00 136.13 ? 86  ARG B CZ  1 
ATOM   1920 N  NH1 . ARG B 2 3   ? -22.081 19.575  32.084 1.00 133.61 ? 86  ARG B NH1 1 
ATOM   1921 N  NH2 . ARG B 2 3   ? -20.990 19.297  34.083 1.00 136.07 ? 86  ARG B NH2 1 
ATOM   1922 N  N   . ASP B 2 4   ? -17.906 26.621  28.920 1.00 161.02 ? 87  ASP B N   1 
ATOM   1923 C  CA  . ASP B 2 4   ? -18.279 27.654  27.963 1.00 167.78 ? 87  ASP B CA  1 
ATOM   1924 C  C   . ASP B 2 4   ? -17.024 28.230  27.321 1.00 168.48 ? 87  ASP B C   1 
ATOM   1925 O  O   . ASP B 2 4   ? -15.914 28.072  27.834 1.00 167.88 ? 87  ASP B O   1 
ATOM   1926 C  CB  . ASP B 2 4   ? -19.116 28.749  28.622 1.00 175.58 ? 87  ASP B CB  1 
ATOM   1927 C  CG  . ASP B 2 4   ? -20.589 28.634  28.267 1.00 176.74 ? 87  ASP B CG  1 
ATOM   1928 O  OD1 . ASP B 2 4   ? -20.913 27.918  27.293 1.00 175.08 ? 87  ASP B OD1 1 
ATOM   1929 O  OD2 . ASP B 2 4   ? -21.428 29.267  28.937 1.00 177.59 ? 87  ASP B OD2 1 
ATOM   1930 N  N   . LYS B 2 5   ? -17.235 28.948  26.210 1.00 167.74 ? 88  LYS B N   1 
ATOM   1931 C  CA  . LYS B 2 5   ? -16.189 29.322  25.260 1.00 169.12 ? 88  LYS B CA  1 
ATOM   1932 C  C   . LYS B 2 5   ? -15.171 28.198  25.117 1.00 183.69 ? 88  LYS B C   1 
ATOM   1933 O  O   . LYS B 2 5   ? -14.077 28.271  25.683 1.00 178.49 ? 88  LYS B O   1 
ATOM   1934 C  CB  . LYS B 2 5   ? -15.471 30.615  25.664 1.00 154.42 ? 88  LYS B CB  1 
ATOM   1935 C  CG  . LYS B 2 5   ? -14.721 31.260  24.489 1.00 137.82 ? 88  LYS B CG  1 
ATOM   1936 C  CD  . LYS B 2 5   ? -13.636 32.227  24.939 1.00 126.74 ? 88  LYS B CD  1 
ATOM   1937 C  CE  . LYS B 2 5   ? -12.780 32.694  23.761 1.00 123.14 ? 88  LYS B CE  1 
ATOM   1938 N  NZ  . LYS B 2 5   ? -11.522 31.903  23.603 1.00 118.22 ? 88  LYS B NZ  1 
ATOM   1939 N  N   . ASP B 2 6   ? -15.519 27.148  24.379 1.00 205.12 ? 89  ASP B N   1 
ATOM   1940 C  CA  . ASP B 2 6   ? -14.625 26.010  24.198 1.00 205.55 ? 89  ASP B CA  1 
ATOM   1941 C  C   . ASP B 2 6   ? -13.675 26.318  23.044 1.00 208.90 ? 89  ASP B C   1 
ATOM   1942 O  O   . ASP B 2 6   ? -14.089 26.401  21.881 1.00 213.99 ? 89  ASP B O   1 
ATOM   1943 C  CB  . ASP B 2 6   ? -15.415 24.717  23.982 1.00 205.46 ? 89  ASP B CB  1 
ATOM   1944 C  CG  . ASP B 2 6   ? -16.048 24.626  22.607 1.00 207.64 ? 89  ASP B CG  1 
ATOM   1945 O  OD1 . ASP B 2 6   ? -15.415 24.040  21.710 1.00 205.42 ? 89  ASP B OD1 1 
ATOM   1946 O  OD2 . ASP B 2 6   ? -17.162 25.150  22.416 1.00 209.22 ? 89  ASP B OD2 1 
ATOM   1947 N  N   . CYS B 2 7   ? -12.398 26.516  23.379 1.00 192.28 ? 90  CYS B N   1 
ATOM   1948 C  CA  . CYS B 2 7   ? -11.418 26.919  22.378 1.00 169.21 ? 90  CYS B CA  1 
ATOM   1949 C  C   . CYS B 2 7   ? -10.877 25.729  21.599 1.00 154.82 ? 90  CYS B C   1 
ATOM   1950 O  O   . CYS B 2 7   ? -10.701 25.819  20.379 1.00 149.51 ? 90  CYS B O   1 
ATOM   1951 C  CB  . CYS B 2 7   ? -10.262 27.670  23.039 1.00 156.32 ? 90  CYS B CB  1 
ATOM   1952 S  SG  . CYS B 2 7   ? -10.479 29.455  23.165 1.00 149.16 ? 90  CYS B SG  1 
ATOM   1953 N  N   . VAL B 2 8   ? -10.590 24.619  22.280 1.00 146.33 ? 91  VAL B N   1 
ATOM   1954 C  CA  . VAL B 2 8   ? -9.941  23.463  21.670 1.00 137.72 ? 91  VAL B CA  1 
ATOM   1955 C  C   . VAL B 2 8   ? -10.779 22.227  21.966 1.00 124.92 ? 91  VAL B C   1 
ATOM   1956 O  O   . VAL B 2 8   ? -10.698 21.656  23.057 1.00 127.83 ? 91  VAL B O   1 
ATOM   1957 C  CB  . VAL B 2 8   ? -8.502  23.275  22.155 1.00 141.75 ? 91  VAL B CB  1 
ATOM   1958 C  CG1 . VAL B 2 8   ? -7.926  22.016  21.535 1.00 138.47 ? 91  VAL B CG1 1 
ATOM   1959 C  CG2 . VAL B 2 8   ? -7.668  24.483  21.770 1.00 148.18 ? 91  VAL B CG2 1 
ATOM   1960 N  N   . GLU B 2 9   ? -11.577 21.806  21.004 1.00 112.07 ? 92  GLU B N   1 
ATOM   1961 C  CA  . GLU B 2 9   ? -12.149 20.478  21.013 1.00 103.43 ? 92  GLU B CA  1 
ATOM   1962 C  C   . GLU B 2 9   ? -11.048 19.493  20.643 1.00 107.55 ? 92  GLU B C   1 
ATOM   1963 O  O   . GLU B 2 9   ? -10.167 19.801  19.825 1.00 117.07 ? 92  GLU B O   1 
ATOM   1964 C  CB  . GLU B 2 9   ? -13.274 20.404  19.996 1.00 101.17 ? 92  GLU B CB  1 
ATOM   1965 C  CG  . GLU B 2 9   ? -12.989 21.328  18.824 1.00 106.94 ? 92  GLU B CG  1 
ATOM   1966 C  CD  . GLU B 2 9   ? -13.996 21.195  17.723 1.00 112.90 ? 92  GLU B CD  1 
ATOM   1967 O  OE1 . GLU B 2 9   ? -14.051 20.099  17.124 1.00 114.14 ? 92  GLU B OE1 1 
ATOM   1968 O  OE2 . GLU B 2 9   ? -14.685 22.201  17.439 1.00 113.95 ? 92  GLU B OE2 1 
ATOM   1969 N  N   . CYS B 2 10  ? -11.093 18.318  21.263 1.00 96.39  ? 93  CYS B N   1 
ATOM   1970 C  CA  . CYS B 2 10  ? -10.175 17.215  20.984 1.00 81.16  ? 93  CYS B CA  1 
ATOM   1971 C  C   . CYS B 2 10  ? -8.710  17.632  21.114 1.00 70.73  ? 93  CYS B C   1 
ATOM   1972 O  O   . CYS B 2 10  ? -8.051  17.933  20.109 1.00 67.89  ? 93  CYS B O   1 
ATOM   1973 C  CB  . CYS B 2 10  ? -10.428 16.645  19.587 1.00 79.72  ? 93  CYS B CB  1 
ATOM   1974 S  SG  . CYS B 2 10  ? -10.187 14.884  19.489 1.00 87.65  ? 93  CYS B SG  1 
ATOM   1975 N  N   . PRO B 2 11  ? -8.170  17.678  22.330 1.00 71.11  ? 94  PRO B N   1 
ATOM   1976 C  CA  . PRO B 2 11  ? -6.742  17.975  22.505 1.00 72.35  ? 94  PRO B CA  1 
ATOM   1977 C  C   . PRO B 2 11  ? -5.847  16.999  21.755 1.00 73.17  ? 94  PRO B C   1 
ATOM   1978 O  O   . PRO B 2 11  ? -4.835  17.429  21.181 1.00 72.64  ? 94  PRO B O   1 
ATOM   1979 C  CB  . PRO B 2 11  ? -6.544  17.877  24.027 1.00 59.23  ? 94  PRO B CB  1 
ATOM   1980 C  CG  . PRO B 2 11  ? -7.873  18.240  24.578 1.00 62.18  ? 94  PRO B CG  1 
ATOM   1981 C  CD  . PRO B 2 11  ? -8.889  17.694  23.615 1.00 63.77  ? 94  PRO B CD  1 
ATOM   1982 N  N   . PRO B 2 12  ? -6.156  15.691  21.717 1.00 70.49  ? 95  PRO B N   1 
ATOM   1983 C  CA  . PRO B 2 12  ? -5.288  14.772  20.954 1.00 69.13  ? 95  PRO B CA  1 
ATOM   1984 C  C   . PRO B 2 12  ? -5.174  15.089  19.470 1.00 71.69  ? 95  PRO B C   1 
ATOM   1985 O  O   . PRO B 2 12  ? -4.340  14.472  18.795 1.00 75.45  ? 95  PRO B O   1 
ATOM   1986 C  CB  . PRO B 2 12  ? -5.936  13.396  21.176 1.00 67.95  ? 95  PRO B CB  1 
ATOM   1987 C  CG  . PRO B 2 12  ? -7.287  13.675  21.713 1.00 68.98  ? 95  PRO B CG  1 
ATOM   1988 C  CD  . PRO B 2 12  ? -7.119  14.913  22.518 1.00 69.62  ? 95  PRO B CD  1 
ATOM   1989 N  N   . SER B 2 13  ? -5.971  16.018  18.938 1.00 66.94  ? 96  SER B N   1 
ATOM   1990 C  CA  . SER B 2 13  ? -5.765  16.450  17.561 1.00 60.61  ? 96  SER B CA  1 
ATOM   1991 C  C   . SER B 2 13  ? -4.437  17.174  17.384 1.00 58.61  ? 96  SER B C   1 
ATOM   1992 O  O   . SER B 2 13  ? -3.966  17.313  16.251 1.00 68.98  ? 96  SER B O   1 
ATOM   1993 C  CB  . SER B 2 13  ? -6.916  17.349  17.112 1.00 59.30  ? 96  SER B CB  1 
ATOM   1994 O  OG  . SER B 2 13  ? -6.889  18.587  17.799 1.00 72.94  ? 96  SER B OG  1 
ATOM   1995 N  N   . ARG B 2 14  ? -3.824  17.629  18.474 1.00 58.91  ? 97  ARG B N   1 
ATOM   1996 C  CA  . ARG B 2 14  ? -2.533  18.300  18.434 1.00 61.95  ? 97  ARG B CA  1 
ATOM   1997 C  C   . ARG B 2 14  ? -1.363  17.328  18.499 1.00 63.23  ? 97  ARG B C   1 
ATOM   1998 O  O   . ARG B 2 14  ? -0.223  17.760  18.701 1.00 63.78  ? 97  ARG B O   1 
ATOM   1999 C  CB  . ARG B 2 14  ? -2.430  19.313  19.577 1.00 67.49  ? 97  ARG B CB  1 
ATOM   2000 C  CG  . ARG B 2 14  ? -3.668  20.174  19.756 1.00 74.21  ? 97  ARG B CG  1 
ATOM   2001 C  CD  . ARG B 2 14  ? -3.483  21.547  19.132 1.00 85.00  ? 97  ARG B CD  1 
ATOM   2002 N  NE  . ARG B 2 14  ? -2.551  22.377  19.889 1.00 91.67  ? 97  ARG B NE  1 
ATOM   2003 C  CZ  . ARG B 2 14  ? -2.847  22.976  21.039 1.00 92.62  ? 97  ARG B CZ  1 
ATOM   2004 N  NH1 . ARG B 2 14  ? -4.053  22.836  21.575 1.00 89.60  ? 97  ARG B NH1 1 
ATOM   2005 N  NH2 . ARG B 2 14  ? -1.934  23.714  21.656 1.00 94.14  ? 97  ARG B NH2 1 
ATOM   2006 N  N   . GLY B 2 15  ? -1.616  16.032  18.343 1.00 67.93  ? 98  GLY B N   1 
ATOM   2007 C  CA  . GLY B 2 15  ? -0.558  15.046  18.280 1.00 65.90  ? 98  GLY B CA  1 
ATOM   2008 C  C   . GLY B 2 15  ? 0.105   15.035  16.918 1.00 64.75  ? 98  GLY B C   1 
ATOM   2009 O  O   . GLY B 2 15  ? 0.061   16.011  16.164 1.00 72.42  ? 98  GLY B O   1 
ATOM   2010 N  N   . GLU B 2 16  ? 0.724   13.902  16.596 1.00 63.24  ? 99  GLU B N   1 
ATOM   2011 C  CA  . GLU B 2 16  ? 1.449   13.776  15.339 1.00 65.06  ? 99  GLU B CA  1 
ATOM   2012 C  C   . GLU B 2 16  ? 1.652   12.304  15.020 1.00 67.77  ? 99  GLU B C   1 
ATOM   2013 O  O   . GLU B 2 16  ? 1.647   11.449  15.909 1.00 67.91  ? 99  GLU B O   1 
ATOM   2014 C  CB  . GLU B 2 16  ? 2.800   14.498  15.397 1.00 69.28  ? 99  GLU B CB  1 
ATOM   2015 C  CG  . GLU B 2 16  ? 3.730   13.986  16.486 1.00 77.76  ? 99  GLU B CG  1 
ATOM   2016 C  CD  . GLU B 2 16  ? 5.150   14.497  16.333 1.00 96.42  ? 99  GLU B CD  1 
ATOM   2017 O  OE1 . GLU B 2 16  ? 5.626   14.607  15.183 1.00 103.96 ? 99  GLU B OE1 1 
ATOM   2018 O  OE2 . GLU B 2 16  ? 5.791   14.791  17.365 1.00 105.91 ? 99  GLU B OE2 1 
HETATM 2019 N  N   . MSE B 2 17  ? 1.831   12.024  13.732 1.00 56.69  ? 100 MSE B N   1 
HETATM 2020 C  CA  . MSE B 2 17  ? 2.197   10.689  13.272 1.00 61.19  ? 100 MSE B CA  1 
HETATM 2021 C  C   . MSE B 2 17  ? 3.710   10.517  13.283 1.00 59.14  ? 100 MSE B C   1 
HETATM 2022 O  O   . MSE B 2 17  ? 4.450   11.447  12.956 1.00 58.54  ? 100 MSE B O   1 
HETATM 2023 C  CB  . MSE B 2 17  ? 1.665   10.429  11.865 1.00 67.79  ? 100 MSE B CB  1 
HETATM 2024 C  CG  . MSE B 2 17  ? 0.163   10.486  11.738 1.00 84.06  ? 100 MSE B CG  1 
HETATM 2025 SE SE  . MSE B 2 17  ? -0.399  10.070  9.919  0.60 98.17  ? 100 MSE B SE  1 
HETATM 2026 C  CE  . MSE B 2 17  ? 0.349   8.292   9.757  1.00 84.60  ? 100 MSE B CE  1 
ATOM   2027 N  N   . ALA B 2 18  ? 4.165   9.319   13.643 1.00 56.03  ? 101 ALA B N   1 
ATOM   2028 C  CA  . ALA B 2 18  ? 5.591   9.039   13.708 1.00 58.78  ? 101 ALA B CA  1 
ATOM   2029 C  C   . ALA B 2 18  ? 5.807   7.535   13.637 1.00 63.24  ? 101 ALA B C   1 
ATOM   2030 O  O   . ALA B 2 18  ? 4.888   6.744   13.866 1.00 58.71  ? 101 ALA B O   1 
ATOM   2031 C  CB  . ALA B 2 18  ? 6.214   9.615   14.984 1.00 57.98  ? 101 ALA B CB  1 
ATOM   2032 N  N   . ILE B 2 19  ? 7.042   7.151   13.312 1.00 65.45  ? 102 ILE B N   1 
ATOM   2033 C  CA  . ILE B 2 19  ? 7.430   5.748   13.354 1.00 62.59  ? 102 ILE B CA  1 
ATOM   2034 C  C   . ILE B 2 19  ? 7.532   5.297   14.805 1.00 58.08  ? 102 ILE B C   1 
ATOM   2035 O  O   . ILE B 2 19  ? 8.067   6.015   15.662 1.00 76.03  ? 102 ILE B O   1 
ATOM   2036 C  CB  . ILE B 2 19  ? 8.755   5.537   12.602 1.00 66.10  ? 102 ILE B CB  1 
ATOM   2037 C  CG1 . ILE B 2 19  ? 8.657   6.108   11.185 1.00 59.74  ? 102 ILE B CG1 1 
ATOM   2038 C  CG2 . ILE B 2 19  ? 9.124   4.061   12.561 1.00 64.94  ? 102 ILE B CG2 1 
ATOM   2039 C  CD1 . ILE B 2 19  ? 9.969   6.122   10.440 1.00 61.71  ? 102 ILE B CD1 1 
ATOM   2040 N  N   . ALA B 2 20  ? 7.015   4.102   15.090 1.00 86.41  ? 103 ALA B N   1 
ATOM   2041 C  CA  . ALA B 2 20  ? 6.935   3.602   16.458 1.00 87.89  ? 103 ALA B CA  1 
ATOM   2042 C  C   . ALA B 2 20  ? 8.315   3.369   17.065 1.00 129.59 ? 103 ALA B C   1 
ATOM   2043 O  O   . ALA B 2 20  ? 8.723   4.091   17.981 1.00 128.32 ? 103 ALA B O   1 
ATOM   2044 C  CB  . ALA B 2 20  ? 6.112   2.316   16.500 1.00 87.96  ? 103 ALA B CB  1 
ATOM   2045 N  N   . ASN B 2 21  ? 9.029   2.355   16.568 1.00 123.92 ? 104 ASN B N   1 
ATOM   2046 C  CA  . ASN B 2 21  ? 10.384  2.027   17.028 1.00 124.96 ? 104 ASN B CA  1 
ATOM   2047 C  C   . ASN B 2 21  ? 10.407  1.646   18.507 1.00 129.17 ? 104 ASN B C   1 
ATOM   2048 O  O   . ASN B 2 21  ? 11.374  1.921   19.222 1.00 133.36 ? 104 ASN B O   1 
ATOM   2049 C  CB  . ASN B 2 21  ? 11.360  3.173   16.753 1.00 120.48 ? 104 ASN B CB  1 
ATOM   2050 C  CG  . ASN B 2 21  ? 11.640  3.360   15.280 1.00 113.44 ? 104 ASN B CG  1 
ATOM   2051 O  OD1 . ASN B 2 21  ? 11.767  4.485   14.800 1.00 115.55 ? 104 ASN B OD1 1 
ATOM   2052 N  ND2 . ASN B 2 21  ? 11.737  2.254   14.551 1.00 106.81 ? 104 ASN B ND2 1 
ATOM   2053 N  N   . ASN B 2 22  ? 9.336   1.000   18.973 1.00 135.25 ? 105 ASN B N   1 
ATOM   2054 C  CA  . ASN B 2 22  ? 9.256   0.535   20.352 1.00 155.39 ? 105 ASN B CA  1 
ATOM   2055 C  C   . ASN B 2 22  ? 9.920   -0.822  20.548 1.00 169.06 ? 105 ASN B C   1 
ATOM   2056 O  O   . ASN B 2 22  ? 9.476   -1.607  21.397 1.00 168.17 ? 105 ASN B O   1 
ATOM   2057 C  CB  . ASN B 2 22  ? 7.798   0.487   20.810 1.00 157.42 ? 105 ASN B CB  1 
ATOM   2058 C  CG  . ASN B 2 22  ? 7.242   1.862   21.130 1.00 154.41 ? 105 ASN B CG  1 
ATOM   2059 O  OD1 . ASN B 2 22  ? 6.959   2.655   20.230 1.00 148.17 ? 105 ASN B OD1 1 
ATOM   2060 N  ND2 . ASN B 2 22  ? 7.074   2.148   22.417 1.00 156.06 ? 105 ASN B ND2 1 
ATOM   2061 N  N   . GLY B 2 23  ? 10.975  -1.111  19.783 1.00 181.36 ? 106 GLY B N   1 
ATOM   2062 C  CA  . GLY B 2 23  ? 11.613  -2.428  19.772 1.00 193.60 ? 106 GLY B CA  1 
ATOM   2063 C  C   . GLY B 2 23  ? 10.583  -3.523  19.510 1.00 196.69 ? 106 GLY B C   1 
ATOM   2064 O  O   . GLY B 2 23  ? 10.633  -4.610  20.087 1.00 209.10 ? 106 GLY B O   1 
ATOM   2065 N  N   . LYS B 2 24  ? 9.632   -3.222  18.626 1.00 180.64 ? 107 LYS B N   1 
ATOM   2066 C  CA  . LYS B 2 24  ? 8.522   -4.120  18.339 1.00 168.71 ? 107 LYS B CA  1 
ATOM   2067 C  C   . LYS B 2 24  ? 8.912   -5.165  17.302 1.00 172.14 ? 107 LYS B C   1 
ATOM   2068 O  O   . LYS B 2 24  ? 10.006  -5.737  17.359 1.00 178.53 ? 107 LYS B O   1 
ATOM   2069 C  CB  . LYS B 2 24  ? 7.310   -3.321  17.850 1.00 150.59 ? 107 LYS B CB  1 
ATOM   2070 C  CG  . LYS B 2 24  ? 7.633   -2.289  16.769 1.00 136.37 ? 107 LYS B CG  1 
ATOM   2071 C  CD  . LYS B 2 24  ? 6.411   -1.978  15.913 1.00 124.64 ? 107 LYS B CD  1 
ATOM   2072 C  CE  . LYS B 2 24  ? 6.710   -0.905  14.872 1.00 111.00 ? 107 LYS B CE  1 
ATOM   2073 N  NZ  . LYS B 2 24  ? 5.473   -0.409  14.200 1.00 94.82  ? 107 LYS B NZ  1 
ATOM   2074 N  N   . GLY B 2 25  ? 8.012   -5.427  16.366 1.00 164.16 ? 108 GLY B N   1 
ATOM   2075 C  CA  . GLY B 2 25  ? 8.308   -6.262  15.215 1.00 159.30 ? 108 GLY B CA  1 
ATOM   2076 C  C   . GLY B 2 25  ? 8.114   -5.453  13.936 1.00 147.90 ? 108 GLY B C   1 
ATOM   2077 O  O   . GLY B 2 25  ? 7.155   -4.693  13.824 1.00 139.20 ? 108 GLY B O   1 
ATOM   2078 N  N   . HIS B 2 26  ? 9.039   -5.626  13.001 1.00 147.10 ? 109 HIS B N   1 
ATOM   2079 C  CA  . HIS B 2 26  ? 8.998   -4.893  11.740 1.00 132.93 ? 109 HIS B CA  1 
ATOM   2080 C  C   . HIS B 2 26  ? 8.176   -5.671  10.722 1.00 126.08 ? 109 HIS B C   1 
ATOM   2081 O  O   . HIS B 2 26  ? 7.293   -6.441  11.111 1.00 132.20 ? 109 HIS B O   1 
ATOM   2082 C  CB  . HIS B 2 26  ? 10.422  -4.639  11.251 1.00 131.86 ? 109 HIS B CB  1 
ATOM   2083 C  CG  . HIS B 2 26  ? 11.430  -4.629  12.357 1.00 135.40 ? 109 HIS B CG  1 
ATOM   2084 N  ND1 . HIS B 2 26  ? 11.336  -3.773  13.434 1.00 134.09 ? 109 HIS B ND1 1 
ATOM   2085 C  CD2 . HIS B 2 26  ? 12.530  -5.388  12.574 1.00 141.16 ? 109 HIS B CD2 1 
ATOM   2086 C  CE1 . HIS B 2 26  ? 12.340  -3.998  14.261 1.00 138.93 ? 109 HIS B CE1 1 
ATOM   2087 N  NE2 . HIS B 2 26  ? 13.082  -4.970  13.761 1.00 144.21 ? 109 HIS B NE2 1 
ATOM   2088 N  N   . SER B 2 27  ? 8.448   -5.470  9.430  1.00 117.22 ? 110 SER B N   1 
ATOM   2089 C  CA  . SER B 2 27  ? 7.752   -6.154  8.340  1.00 110.64 ? 110 SER B CA  1 
ATOM   2090 C  C   . SER B 2 27  ? 6.281   -5.753  8.244  1.00 97.46  ? 110 SER B C   1 
ATOM   2091 O  O   . SER B 2 27  ? 5.560   -5.729  9.247  1.00 93.77  ? 110 SER B O   1 
ATOM   2092 C  CB  . SER B 2 27  ? 7.873   -7.675  8.483  1.00 117.23 ? 110 SER B CB  1 
ATOM   2093 O  OG  . SER B 2 27  ? 6.997   -8.342  7.591  1.00 103.56 ? 110 SER B OG  1 
HETATM 2094 N  N   . MSE B 2 28  ? 5.826   -5.463  7.030  1.00 97.72  ? 111 MSE B N   1 
HETATM 2095 C  CA  . MSE B 2 28  ? 4.482   -4.939  6.800  1.00 92.41  ? 111 MSE B CA  1 
HETATM 2096 C  C   . MSE B 2 28  ? 3.404   -6.017  6.713  1.00 96.19  ? 111 MSE B C   1 
HETATM 2097 O  O   . MSE B 2 28  ? 2.219   -5.703  6.626  1.00 93.79  ? 111 MSE B O   1 
HETATM 2098 C  CB  . MSE B 2 28  ? 4.463   -4.120  5.509  1.00 87.35  ? 111 MSE B CB  1 
HETATM 2099 C  CG  . MSE B 2 28  ? 5.049   -4.868  4.323  1.00 97.95  ? 111 MSE B CG  1 
HETATM 2100 SE SE  . MSE B 2 28  ? 5.421   -3.723  2.796  0.41 110.06 ? 111 MSE B SE  1 
HETATM 2101 C  CE  . MSE B 2 28  ? 3.936   -2.491  2.987  1.00 81.78  ? 111 MSE B CE  1 
ATOM   2102 N  N   . SER B 2 29  ? 3.812   -7.286  6.732  1.00 108.37 ? 112 SER B N   1 
ATOM   2103 C  CA  . SER B 2 29  ? 2.913   -8.379  6.391  1.00 115.30 ? 112 SER B CA  1 
ATOM   2104 C  C   . SER B 2 29  ? 2.471   -9.227  7.576  1.00 116.53 ? 112 SER B C   1 
ATOM   2105 O  O   . SER B 2 29  ? 1.599   -10.085 7.401  1.00 121.72 ? 112 SER B O   1 
ATOM   2106 C  CB  . SER B 2 29  ? 3.569   -9.292  5.344  1.00 129.21 ? 112 SER B CB  1 
ATOM   2107 O  OG  . SER B 2 29  ? 3.825   -8.585  4.143  1.00 136.20 ? 112 SER B OG  1 
ATOM   2108 N  N   . ASP B 2 30  ? 3.038   -9.024  8.762  1.00 114.32 ? 113 ASP B N   1 
ATOM   2109 C  CA  . ASP B 2 30  ? 2.643   -9.835  9.905  1.00 108.76 ? 113 ASP B CA  1 
ATOM   2110 C  C   . ASP B 2 30  ? 1.206   -9.533  10.307 1.00 96.42  ? 113 ASP B C   1 
ATOM   2111 O  O   . ASP B 2 30  ? 0.687   -8.440  10.073 1.00 88.79  ? 113 ASP B O   1 
ATOM   2112 C  CB  . ASP B 2 30  ? 3.574   -9.596  11.093 1.00 116.54 ? 113 ASP B CB  1 
ATOM   2113 C  CG  . ASP B 2 30  ? 5.019   -9.440  10.681 1.00 129.08 ? 113 ASP B CG  1 
ATOM   2114 O  OD1 . ASP B 2 30  ? 5.477   -10.189 9.791  1.00 133.79 ? 113 ASP B OD1 1 
ATOM   2115 O  OD2 . ASP B 2 30  ? 5.700   -8.574  11.262 1.00 133.99 ? 113 ASP B OD2 1 
ATOM   2116 N  N   . LEU B 2 31  ? 0.560   -10.531 10.917 1.00 77.49  ? 114 LEU B N   1 
ATOM   2117 C  CA  . LEU B 2 31  ? -0.805  -10.353 11.398 1.00 76.74  ? 114 LEU B CA  1 
ATOM   2118 C  C   . LEU B 2 31  ? -0.911  -9.167  12.348 1.00 75.80  ? 114 LEU B C   1 
ATOM   2119 O  O   . LEU B 2 31  ? -1.924  -8.458  12.343 1.00 76.34  ? 114 LEU B O   1 
ATOM   2120 C  CB  . LEU B 2 31  ? -1.284  -11.632 12.086 1.00 77.51  ? 114 LEU B CB  1 
ATOM   2121 C  CG  . LEU B 2 31  ? -2.756  -11.699 12.492 1.00 74.80  ? 114 LEU B CG  1 
ATOM   2122 C  CD1 . LEU B 2 31  ? -3.640  -11.678 11.258 1.00 76.26  ? 114 LEU B CD1 1 
ATOM   2123 C  CD2 . LEU B 2 31  ? -3.015  -12.945 13.324 1.00 80.45  ? 114 LEU B CD2 1 
ATOM   2124 N  N   . SER B 2 32  ? 0.121   -8.933  13.162 1.00 74.72  ? 115 SER B N   1 
ATOM   2125 C  CA  . SER B 2 32  ? 0.110   -7.781  14.058 1.00 66.63  ? 115 SER B CA  1 
ATOM   2126 C  C   . SER B 2 32  ? 0.001   -6.477  13.280 1.00 65.37  ? 115 SER B C   1 
ATOM   2127 O  O   . SER B 2 32  ? -0.788  -5.594  13.640 1.00 60.24  ? 115 SER B O   1 
ATOM   2128 C  CB  . SER B 2 32  ? 1.364   -7.783  14.932 1.00 75.61  ? 115 SER B CB  1 
ATOM   2129 O  OG  . SER B 2 32  ? 1.107   -7.169  16.183 1.00 86.09  ? 115 SER B OG  1 
ATOM   2130 N  N   . ALA B 2 33  ? 0.780   -6.341  12.204 1.00 70.64  ? 116 ALA B N   1 
ATOM   2131 C  CA  . ALA B 2 33  ? 0.794   -5.092  11.451 1.00 62.00  ? 116 ALA B CA  1 
ATOM   2132 C  C   . ALA B 2 33  ? -0.461  -4.937  10.600 1.00 65.31  ? 116 ALA B C   1 
ATOM   2133 O  O   . ALA B 2 33  ? -1.056  -3.853  10.554 1.00 65.98  ? 116 ALA B O   1 
ATOM   2134 C  CB  . ALA B 2 33  ? 2.044   -5.019  10.577 1.00 62.10  ? 116 ALA B CB  1 
ATOM   2135 N  N   . ARG B 2 34  ? -0.875  -6.005  9.913  1.00 67.30  ? 117 ARG B N   1 
ATOM   2136 C  CA  . ARG B 2 34  ? -2.051  -5.916  9.051  1.00 65.55  ? 117 ARG B CA  1 
ATOM   2137 C  C   . ARG B 2 34  ? -3.311  -5.624  9.858  1.00 65.88  ? 117 ARG B C   1 
ATOM   2138 O  O   . ARG B 2 34  ? -4.174  -4.855  9.418  1.00 66.60  ? 117 ARG B O   1 
ATOM   2139 C  CB  . ARG B 2 34  ? -2.213  -7.205  8.246  1.00 68.81  ? 117 ARG B CB  1 
ATOM   2140 C  CG  . ARG B 2 34  ? -0.953  -7.634  7.503  1.00 79.17  ? 117 ARG B CG  1 
ATOM   2141 C  CD  . ARG B 2 34  ? -1.252  -8.662  6.419  1.00 82.14  ? 117 ARG B CD  1 
ATOM   2142 N  NE  . ARG B 2 34  ? -2.420  -9.477  6.741  1.00 86.31  ? 117 ARG B NE  1 
ATOM   2143 C  CZ  . ARG B 2 34  ? -2.377  -10.601 7.448  1.00 90.52  ? 117 ARG B CZ  1 
ATOM   2144 N  NH1 . ARG B 2 34  ? -1.221  -11.053 7.913  1.00 89.48  ? 117 ARG B NH1 1 
ATOM   2145 N  NH2 . ARG B 2 34  ? -3.494  -11.275 7.691  1.00 100.03 ? 117 ARG B NH2 1 
ATOM   2146 N  N   . TYR B 2 35  ? -3.434  -6.222  11.045 1.00 64.12  ? 118 TYR B N   1 
ATOM   2147 C  CA  . TYR B 2 35  ? -4.599  -5.944  11.880 1.00 61.46  ? 118 TYR B CA  1 
ATOM   2148 C  C   . TYR B 2 35  ? -4.577  -4.513  12.401 1.00 65.02  ? 118 TYR B C   1 
ATOM   2149 O  O   . TYR B 2 35  ? -5.625  -3.861  12.486 1.00 66.29  ? 118 TYR B O   1 
ATOM   2150 C  CB  . TYR B 2 35  ? -4.669  -6.930  13.045 1.00 63.80  ? 118 TYR B CB  1 
ATOM   2151 C  CG  . TYR B 2 35  ? -5.879  -6.720  13.922 1.00 62.82  ? 118 TYR B CG  1 
ATOM   2152 C  CD1 . TYR B 2 35  ? -5.766  -6.113  15.166 1.00 59.07  ? 118 TYR B CD1 1 
ATOM   2153 C  CD2 . TYR B 2 35  ? -7.140  -7.117  13.499 1.00 64.68  ? 118 TYR B CD2 1 
ATOM   2154 C  CE1 . TYR B 2 35  ? -6.875  -5.912  15.964 1.00 62.35  ? 118 TYR B CE1 1 
ATOM   2155 C  CE2 . TYR B 2 35  ? -8.252  -6.922  14.288 1.00 63.45  ? 118 TYR B CE2 1 
ATOM   2156 C  CZ  . TYR B 2 35  ? -8.118  -6.319  15.520 1.00 64.78  ? 118 TYR B CZ  1 
ATOM   2157 O  OH  . TYR B 2 35  ? -9.229  -6.124  16.311 1.00 62.36  ? 118 TYR B OH  1 
ATOM   2158 N  N   . GLN B 2 36  ? -3.395  -4.010  12.762 1.00 63.85  ? 119 GLN B N   1 
ATOM   2159 C  CA  . GLN B 2 36  ? -3.297  -2.640  13.252 1.00 62.59  ? 119 GLN B CA  1 
ATOM   2160 C  C   . GLN B 2 36  ? -3.674  -1.640  12.168 1.00 64.94  ? 119 GLN B C   1 
ATOM   2161 O  O   . GLN B 2 36  ? -4.380  -0.660  12.437 1.00 63.34  ? 119 GLN B O   1 
ATOM   2162 C  CB  . GLN B 2 36  ? -1.884  -2.368  13.766 1.00 64.93  ? 119 GLN B CB  1 
ATOM   2163 C  CG  . GLN B 2 36  ? -1.760  -1.134  14.639 1.00 59.19  ? 119 GLN B CG  1 
ATOM   2164 C  CD  . GLN B 2 36  ? -0.668  -1.275  15.677 1.00 62.58  ? 119 GLN B CD  1 
ATOM   2165 O  OE1 . GLN B 2 36  ? -0.684  -2.202  16.490 1.00 68.82  ? 119 GLN B OE1 1 
ATOM   2166 N  NE2 . GLN B 2 36  ? 0.288   -0.354  15.659 1.00 66.96  ? 119 GLN B NE2 1 
ATOM   2167 N  N   . GLN B 2 37  ? -3.223  -1.874  10.935 1.00 67.43  ? 120 GLN B N   1 
ATOM   2168 C  CA  . GLN B 2 37  ? -3.513  -0.935  9.857  1.00 60.79  ? 120 GLN B CA  1 
ATOM   2169 C  C   . GLN B 2 37  ? -4.996  -0.918  9.513  1.00 62.42  ? 120 GLN B C   1 
ATOM   2170 O  O   . GLN B 2 37  ? -5.531  0.131   9.138  1.00 69.40  ? 120 GLN B O   1 
ATOM   2171 C  CB  . GLN B 2 37  ? -2.679  -1.281  8.625  1.00 55.59  ? 120 GLN B CB  1 
ATOM   2172 C  CG  . GLN B 2 37  ? -2.832  -0.303  7.475  1.00 56.95  ? 120 GLN B CG  1 
ATOM   2173 C  CD  . GLN B 2 37  ? -1.660  -0.349  6.514  1.00 67.28  ? 120 GLN B CD  1 
ATOM   2174 O  OE1 . GLN B 2 37  ? -0.524  -0.611  6.911  1.00 72.52  ? 120 GLN B OE1 1 
ATOM   2175 N  NE2 . GLN B 2 37  ? -1.933  -0.101  5.239  1.00 71.96  ? 120 GLN B NE2 1 
ATOM   2176 N  N   . TRP B 2 38  ? -5.677  -2.057  9.649  1.00 64.60  ? 121 TRP B N   1 
ATOM   2177 C  CA  . TRP B 2 38  ? -7.098  -2.129  9.319  1.00 67.74  ? 121 TRP B CA  1 
ATOM   2178 C  C   . TRP B 2 38  ? -7.961  -1.446  10.373 1.00 62.78  ? 121 TRP B C   1 
ATOM   2179 O  O   . TRP B 2 38  ? -8.998  -0.861  10.040 1.00 66.81  ? 121 TRP B O   1 
ATOM   2180 C  CB  . TRP B 2 38  ? -7.509  -3.592  9.151  1.00 70.66  ? 121 TRP B CB  1 
ATOM   2181 C  CG  . TRP B 2 38  ? -8.973  -3.833  8.926  1.00 75.36  ? 121 TRP B CG  1 
ATOM   2182 C  CD1 . TRP B 2 38  ? -9.647  -3.757  7.741  1.00 83.05  ? 121 TRP B CD1 1 
ATOM   2183 C  CD2 . TRP B 2 38  ? -9.941  -4.207  9.913  1.00 75.09  ? 121 TRP B CD2 1 
ATOM   2184 N  NE1 . TRP B 2 38  ? -10.976 -4.056  7.931  1.00 80.35  ? 121 TRP B NE1 1 
ATOM   2185 C  CE2 . TRP B 2 38  ? -11.181 -4.336  9.256  1.00 73.62  ? 121 TRP B CE2 1 
ATOM   2186 C  CE3 . TRP B 2 38  ? -9.878  -4.446  11.289 1.00 74.11  ? 121 TRP B CE3 1 
ATOM   2187 C  CZ2 . TRP B 2 38  ? -12.348 -4.689  9.930  1.00 67.42  ? 121 TRP B CZ2 1 
ATOM   2188 C  CZ3 . TRP B 2 38  ? -11.039 -4.796  11.956 1.00 68.22  ? 121 TRP B CZ3 1 
ATOM   2189 C  CH2 . TRP B 2 38  ? -12.257 -4.913  11.276 1.00 65.12  ? 121 TRP B CH2 1 
ATOM   2190 N  N   . VAL B 2 39  ? -7.555  -1.510  11.641 1.00 58.86  ? 122 VAL B N   1 
ATOM   2191 C  CA  . VAL B 2 39  ? -8.309  -0.847  12.698 1.00 63.63  ? 122 VAL B CA  1 
ATOM   2192 C  C   . VAL B 2 39  ? -8.052  0.655   12.686 1.00 70.87  ? 122 VAL B C   1 
ATOM   2193 O  O   . VAL B 2 39  ? -8.982  1.456   12.838 1.00 67.56  ? 122 VAL B O   1 
ATOM   2194 C  CB  . VAL B 2 39  ? -7.959  -1.470  14.061 1.00 65.58  ? 122 VAL B CB  1 
ATOM   2195 C  CG1 . VAL B 2 39  ? -8.542  -0.642  15.194 1.00 55.20  ? 122 VAL B CG1 1 
ATOM   2196 C  CG2 . VAL B 2 39  ? -8.456  -2.906  14.131 1.00 75.45  ? 122 VAL B CG2 1 
ATOM   2197 N  N   . THR B 2 40  ? -6.797  1.062   12.490 1.00 77.16  ? 123 THR B N   1 
ATOM   2198 C  CA  . THR B 2 40  ? -6.408  2.459   12.634 1.00 72.59  ? 123 THR B CA  1 
ATOM   2199 C  C   . THR B 2 40  ? -6.406  3.235   11.325 1.00 72.92  ? 123 THR B C   1 
ATOM   2200 O  O   . THR B 2 40  ? -6.496  4.467   11.359 1.00 71.82  ? 123 THR B O   1 
ATOM   2201 C  CB  . THR B 2 40  ? -5.013  2.558   13.256 1.00 67.06  ? 123 THR B CB  1 
ATOM   2202 O  OG1 . THR B 2 40  ? -4.046  2.034   12.337 1.00 75.49  ? 123 THR B OG1 1 
ATOM   2203 C  CG2 . THR B 2 40  ? -4.953  1.768   14.551 1.00 69.97  ? 123 THR B CG2 1 
ATOM   2204 N  N   . ASN B 2 41  ? -6.297  2.551   10.184 1.00 72.71  ? 124 ASN B N   1 
ATOM   2205 C  CA  . ASN B 2 41  ? -6.090  3.198   8.885  1.00 73.68  ? 124 ASN B CA  1 
ATOM   2206 C  C   . ASN B 2 41  ? -4.824  4.052   8.876  1.00 70.59  ? 124 ASN B C   1 
ATOM   2207 O  O   . ASN B 2 41  ? -4.716  5.018   8.118  1.00 64.74  ? 124 ASN B O   1 
ATOM   2208 C  CB  . ASN B 2 41  ? -7.305  4.030   8.467  1.00 76.36  ? 124 ASN B CB  1 
ATOM   2209 C  CG  . ASN B 2 41  ? -8.180  3.309   7.470  1.00 91.71  ? 124 ASN B CG  1 
ATOM   2210 O  OD1 . ASN B 2 41  ? -7.828  3.182   6.297  1.00 99.22  ? 124 ASN B OD1 1 
ATOM   2211 N  ND2 . ASN B 2 41  ? -9.327  2.821   7.932  1.00 101.81 ? 124 ASN B ND2 1 
ATOM   2212 N  N   . PHE B 2 42  ? -3.860  3.700   9.727  1.00 65.48  ? 125 PHE B N   1 
ATOM   2213 C  CA  . PHE B 2 42  ? -2.543  4.318   9.740  1.00 61.72  ? 125 PHE B CA  1 
ATOM   2214 C  C   . PHE B 2 42  ? -1.592  3.480   8.907  1.00 62.67  ? 125 PHE B C   1 
ATOM   2215 O  O   . PHE B 2 42  ? -1.561  2.251   9.070  1.00 67.10  ? 125 PHE B O   1 
ATOM   2216 C  CB  . PHE B 2 42  ? -2.010  4.431   11.166 1.00 66.40  ? 125 PHE B CB  1 
ATOM   2217 C  CG  . PHE B 2 42  ? -2.366  5.719   11.853 1.00 66.81  ? 125 PHE B CG  1 
ATOM   2218 C  CD1 . PHE B 2 42  ? -3.648  6.237   11.772 1.00 64.63  ? 125 PHE B CD1 1 
ATOM   2219 C  CD2 . PHE B 2 42  ? -1.417  6.407   12.593 1.00 61.96  ? 125 PHE B CD2 1 
ATOM   2220 C  CE1 . PHE B 2 42  ? -3.974  7.421   12.409 1.00 55.86  ? 125 PHE B CE1 1 
ATOM   2221 C  CE2 . PHE B 2 42  ? -1.738  7.590   13.232 1.00 56.54  ? 125 PHE B CE2 1 
ATOM   2222 C  CZ  . PHE B 2 42  ? -3.017  8.097   13.139 1.00 52.79  ? 125 PHE B CZ  1 
ATOM   2223 N  N   . PRO B 2 43  ? -0.819  4.079   8.003  1.00 60.42  ? 126 PRO B N   1 
ATOM   2224 C  CA  . PRO B 2 43  ? 0.169   3.293   7.253  1.00 61.11  ? 126 PRO B CA  1 
ATOM   2225 C  C   . PRO B 2 43  ? 1.262   2.774   8.179  1.00 59.23  ? 126 PRO B C   1 
ATOM   2226 O  O   . PRO B 2 43  ? 1.784   3.508   9.021  1.00 60.02  ? 126 PRO B O   1 
ATOM   2227 C  CB  . PRO B 2 43  ? 0.717   4.292   6.226  1.00 58.80  ? 126 PRO B CB  1 
ATOM   2228 C  CG  . PRO B 2 43  ? 0.424   5.640   6.808  1.00 59.60  ? 126 PRO B CG  1 
ATOM   2229 C  CD  . PRO B 2 43  ? -0.858  5.486   7.569  1.00 55.57  ? 126 PRO B CD  1 
ATOM   2230 N  N   . PHE B 2 44  ? 1.584   1.494   8.031  1.00 60.61  ? 127 PHE B N   1 
ATOM   2231 C  CA  . PHE B 2 44  ? 2.678   0.906   8.788  1.00 55.38  ? 127 PHE B CA  1 
ATOM   2232 C  C   . PHE B 2 44  ? 3.992   1.593   8.418  1.00 69.27  ? 127 PHE B C   1 
ATOM   2233 O  O   . PHE B 2 44  ? 4.221   1.900   7.241  1.00 72.39  ? 127 PHE B O   1 
ATOM   2234 C  CB  . PHE B 2 44  ? 2.759   -0.596  8.500  1.00 57.59  ? 127 PHE B CB  1 
ATOM   2235 C  CG  . PHE B 2 44  ? 3.825   -1.313  9.278  1.00 57.83  ? 127 PHE B CG  1 
ATOM   2236 C  CD1 . PHE B 2 44  ? 5.074   -1.539  8.726  1.00 60.52  ? 127 PHE B CD1 1 
ATOM   2237 C  CD2 . PHE B 2 44  ? 3.572   -1.772  10.558 1.00 62.32  ? 127 PHE B CD2 1 
ATOM   2238 C  CE1 . PHE B 2 44  ? 6.055   -2.199  9.443  1.00 61.12  ? 127 PHE B CE1 1 
ATOM   2239 C  CE2 . PHE B 2 44  ? 4.546   -2.434  11.279 1.00 62.97  ? 127 PHE B CE2 1 
ATOM   2240 C  CZ  . PHE B 2 44  ? 5.787   -2.647  10.722 1.00 68.64  ? 127 PHE B CZ  1 
ATOM   2241 N  N   . PRO B 2 45  ? 4.880   1.856   9.391  1.00 65.12  ? 128 PRO B N   1 
ATOM   2242 C  CA  . PRO B 2 45  ? 4.736   1.572   10.819 1.00 67.69  ? 128 PRO B CA  1 
ATOM   2243 C  C   . PRO B 2 45  ? 4.401   2.810   11.641 1.00 64.08  ? 128 PRO B C   1 
ATOM   2244 O  O   . PRO B 2 45  ? 4.929   2.977   12.740 1.00 65.67  ? 128 PRO B O   1 
ATOM   2245 C  CB  . PRO B 2 45  ? 6.119   1.057   11.191 1.00 76.30  ? 128 PRO B CB  1 
ATOM   2246 C  CG  . PRO B 2 45  ? 7.030   1.917   10.345 1.00 73.65  ? 128 PRO B CG  1 
ATOM   2247 C  CD  . PRO B 2 45  ? 6.254   2.289   9.082  1.00 68.47  ? 128 PRO B CD  1 
ATOM   2248 N  N   . HIS B 2 46  ? 3.539   3.670   11.113 1.00 59.26  ? 129 HIS B N   1 
ATOM   2249 C  CA  . HIS B 2 46  ? 3.229   4.921   11.786 1.00 54.22  ? 129 HIS B CA  1 
ATOM   2250 C  C   . HIS B 2 46  ? 2.186   4.710   12.872 1.00 57.75  ? 129 HIS B C   1 
ATOM   2251 O  O   . HIS B 2 46  ? 1.269   3.895   12.730 1.00 63.51  ? 129 HIS B O   1 
ATOM   2252 C  CB  . HIS B 2 46  ? 2.735   5.959   10.783 1.00 51.45  ? 129 HIS B CB  1 
ATOM   2253 C  CG  . HIS B 2 46  ? 3.717   6.263   9.697  1.00 56.96  ? 129 HIS B CG  1 
ATOM   2254 N  ND1 . HIS B 2 46  ? 4.636   7.285   9.790  1.00 61.28  ? 129 HIS B ND1 1 
ATOM   2255 C  CD2 . HIS B 2 46  ? 3.928   5.676   8.496  1.00 63.89  ? 129 HIS B CD2 1 
ATOM   2256 C  CE1 . HIS B 2 46  ? 5.370   7.316   8.692  1.00 68.09  ? 129 HIS B CE1 1 
ATOM   2257 N  NE2 . HIS B 2 46  ? 4.960   6.350   7.890  1.00 67.76  ? 129 HIS B NE2 1 
ATOM   2258 N  N   . GLU B 2 47  ? 2.342   5.449   13.969 1.00 61.40  ? 130 GLU B N   1 
ATOM   2259 C  CA  . GLU B 2 47  ? 1.352   5.473   15.037 1.00 59.92  ? 130 GLU B CA  1 
ATOM   2260 C  C   . GLU B 2 47  ? 1.096   6.920   15.441 1.00 59.07  ? 130 GLU B C   1 
ATOM   2261 O  O   . GLU B 2 47  ? 1.571   7.842   14.771 1.00 57.47  ? 130 GLU B O   1 
ATOM   2262 C  CB  . GLU B 2 47  ? 1.816   4.628   16.227 1.00 52.34  ? 130 GLU B CB  1 
ATOM   2263 C  CG  . GLU B 2 47  ? 1.904   3.136   15.916 1.00 49.44  ? 130 GLU B CG  1 
ATOM   2264 C  CD  . GLU B 2 47  ? 2.475   2.318   17.061 1.00 51.93  ? 130 GLU B CD  1 
ATOM   2265 O  OE1 . GLU B 2 47  ? 2.642   2.868   18.169 1.00 53.92  ? 130 GLU B OE1 1 
ATOM   2266 O  OE2 . GLU B 2 47  ? 2.759   1.119   16.852 1.00 55.68  ? 130 GLU B OE2 1 
ATOM   2267 N  N   . TRP B 2 48  ? 0.351   7.134   16.521 1.00 57.77  ? 131 TRP B N   1 
ATOM   2268 C  CA  . TRP B 2 48  ? -0.034  8.470   16.960 1.00 53.28  ? 131 TRP B CA  1 
ATOM   2269 C  C   . TRP B 2 48  ? 0.635   8.773   18.292 1.00 56.71  ? 131 TRP B C   1 
ATOM   2270 O  O   . TRP B 2 48  ? 0.482   8.013   19.255 1.00 62.22  ? 131 TRP B O   1 
ATOM   2271 C  CB  . TRP B 2 48  ? -1.553  8.588   17.083 1.00 53.26  ? 131 TRP B CB  1 
ATOM   2272 C  CG  . TRP B 2 48  ? -2.043  9.992   17.277 1.00 60.42  ? 131 TRP B CG  1 
ATOM   2273 C  CD1 . TRP B 2 48  ? -2.594  10.523  18.411 1.00 56.34  ? 131 TRP B CD1 1 
ATOM   2274 C  CD2 . TRP B 2 48  ? -2.035  11.045  16.305 1.00 62.06  ? 131 TRP B CD2 1 
ATOM   2275 N  NE1 . TRP B 2 48  ? -2.927  11.839  18.203 1.00 49.77  ? 131 TRP B NE1 1 
ATOM   2276 C  CE2 . TRP B 2 48  ? -2.596  12.184  16.919 1.00 58.33  ? 131 TRP B CE2 1 
ATOM   2277 C  CE3 . TRP B 2 48  ? -1.610  11.135  14.976 1.00 64.94  ? 131 TRP B CE3 1 
ATOM   2278 C  CZ2 . TRP B 2 48  ? -2.742  13.396  16.248 1.00 60.04  ? 131 TRP B CZ2 1 
ATOM   2279 C  CZ3 . TRP B 2 48  ? -1.753  12.342  14.313 1.00 59.29  ? 131 TRP B CZ3 1 
ATOM   2280 C  CH2 . TRP B 2 48  ? -2.309  13.457  14.953 1.00 53.91  ? 131 TRP B CH2 1 
ATOM   2281 N  N   . PHE B 2 49  ? 1.364   9.884   18.347 1.00 56.70  ? 132 PHE B N   1 
ATOM   2282 C  CA  . PHE B 2 49  ? 2.055   10.325  19.553 1.00 56.97  ? 132 PHE B CA  1 
ATOM   2283 C  C   . PHE B 2 49  ? 1.365   11.580  20.072 1.00 64.24  ? 132 PHE B C   1 
ATOM   2284 O  O   . PHE B 2 49  ? 1.401   12.630  19.420 1.00 72.65  ? 132 PHE B O   1 
ATOM   2285 C  CB  . PHE B 2 49  ? 3.533   10.583  19.266 1.00 52.36  ? 132 PHE B CB  1 
ATOM   2286 C  CG  . PHE B 2 49  ? 4.374   10.739  20.499 1.00 52.05  ? 132 PHE B CG  1 
ATOM   2287 C  CD1 . PHE B 2 49  ? 4.711   9.639   21.268 1.00 60.24  ? 132 PHE B CD1 1 
ATOM   2288 C  CD2 . PHE B 2 49  ? 4.831   11.984  20.887 1.00 57.72  ? 132 PHE B CD2 1 
ATOM   2289 C  CE1 . PHE B 2 49  ? 5.488   9.781   22.404 1.00 57.76  ? 132 PHE B CE1 1 
ATOM   2290 C  CE2 . PHE B 2 49  ? 5.607   12.130  22.021 1.00 72.47  ? 132 PHE B CE2 1 
ATOM   2291 C  CZ  . PHE B 2 49  ? 5.935   11.027  22.779 1.00 60.62  ? 132 PHE B CZ  1 
ATOM   2292 N  N   . TRP B 2 50  ? 0.730   11.468  21.238 1.00 60.42  ? 133 TRP B N   1 
ATOM   2293 C  CA  . TRP B 2 50  ? 0.098   12.610  21.882 1.00 56.02  ? 133 TRP B CA  1 
ATOM   2294 C  C   . TRP B 2 50  ? 0.157   12.423  23.390 1.00 58.28  ? 133 TRP B C   1 
ATOM   2295 O  O   . TRP B 2 50  ? 0.045   11.300  23.887 1.00 59.10  ? 133 TRP B O   1 
ATOM   2296 C  CB  . TRP B 2 50  ? -1.357  12.794  21.433 1.00 52.94  ? 133 TRP B CB  1 
ATOM   2297 C  CG  . TRP B 2 50  ? -2.081  13.823  22.246 1.00 60.35  ? 133 TRP B CG  1 
ATOM   2298 C  CD1 . TRP B 2 50  ? -1.967  15.178  22.139 1.00 68.54  ? 133 TRP B CD1 1 
ATOM   2299 C  CD2 . TRP B 2 50  ? -3.010  13.581  23.310 1.00 61.07  ? 133 TRP B CD2 1 
ATOM   2300 N  NE1 . TRP B 2 50  ? -2.775  15.795  23.064 1.00 72.10  ? 133 TRP B NE1 1 
ATOM   2301 C  CE2 . TRP B 2 50  ? -3.425  14.836  23.796 1.00 64.00  ? 133 TRP B CE2 1 
ATOM   2302 C  CE3 . TRP B 2 50  ? -3.534  12.425  23.894 1.00 63.12  ? 133 TRP B CE3 1 
ATOM   2303 C  CZ2 . TRP B 2 50  ? -4.340  14.967  24.835 1.00 66.17  ? 133 TRP B CZ2 1 
ATOM   2304 C  CZ3 . TRP B 2 50  ? -4.442  12.559  24.927 1.00 62.31  ? 133 TRP B CZ3 1 
ATOM   2305 C  CH2 . TRP B 2 50  ? -4.835  13.820  25.387 1.00 65.13  ? 133 TRP B CH2 1 
ATOM   2306 N  N   . SER B 2 51  ? 0.331   13.535  24.108 1.00 60.35  ? 134 SER B N   1 
ATOM   2307 C  CA  . SER B 2 51  ? 0.406   13.543  25.570 1.00 58.40  ? 134 SER B CA  1 
ATOM   2308 C  C   . SER B 2 51  ? 1.517   12.632  26.084 1.00 60.38  ? 134 SER B C   1 
ATOM   2309 O  O   . SER B 2 51  ? 1.413   12.059  27.170 1.00 68.73  ? 134 SER B O   1 
ATOM   2310 C  CB  . SER B 2 51  ? -0.937  13.163  26.202 1.00 58.27  ? 134 SER B CB  1 
ATOM   2311 O  OG  . SER B 2 51  ? -0.968  13.484  27.585 1.00 57.58  ? 134 SER B OG  1 
ATOM   2312 N  N   . GLY B 2 52  ? 2.587   12.493  25.302 1.00 59.59  ? 135 GLY B N   1 
ATOM   2313 C  CA  . GLY B 2 52  ? 3.746   11.727  25.705 1.00 57.90  ? 135 GLY B CA  1 
ATOM   2314 C  C   . GLY B 2 52  ? 3.610   10.225  25.594 1.00 60.85  ? 135 GLY B C   1 
ATOM   2315 O  O   . GLY B 2 52  ? 4.549   9.508   25.963 1.00 65.65  ? 135 GLY B O   1 
ATOM   2316 N  N   . THR B 2 53  ? 2.485   9.717   25.105 1.00 53.82  ? 136 THR B N   1 
ATOM   2317 C  CA  . THR B 2 53  ? 2.281   8.284   24.977 1.00 65.55  ? 136 THR B CA  1 
ATOM   2318 C  C   . THR B 2 53  ? 1.984   7.922   23.528 1.00 68.11  ? 136 THR B C   1 
ATOM   2319 O  O   . THR B 2 53  ? 1.687   8.777   22.690 1.00 66.44  ? 136 THR B O   1 
ATOM   2320 C  CB  . THR B 2 53  ? 1.146   7.796   25.887 1.00 74.41  ? 136 THR B CB  1 
ATOM   2321 O  OG1 . THR B 2 53  ? -0.086  8.408   25.489 1.00 84.31  ? 136 THR B OG1 1 
ATOM   2322 C  CG2 . THR B 2 53  ? 1.442   8.145   27.337 1.00 78.33  ? 136 THR B CG2 1 
ATOM   2323 N  N   . TRP B 2 54  ? 2.067   6.625   23.245 1.00 67.12  ? 137 TRP B N   1 
ATOM   2324 C  CA  . TRP B 2 54  ? 1.842   6.094   21.910 1.00 53.54  ? 137 TRP B CA  1 
ATOM   2325 C  C   . TRP B 2 54  ? 0.426   5.550   21.788 1.00 46.89  ? 137 TRP B C   1 
ATOM   2326 O  O   . TRP B 2 54  ? -0.061  4.847   22.677 1.00 56.30  ? 137 TRP B O   1 
ATOM   2327 C  CB  . TRP B 2 54  ? 2.850   4.991   21.588 1.00 51.75  ? 137 TRP B CB  1 
ATOM   2328 C  CG  . TRP B 2 54  ? 4.211   5.506   21.265 1.00 49.10  ? 137 TRP B CG  1 
ATOM   2329 C  CD1 . TRP B 2 54  ? 5.296   5.529   22.090 1.00 50.39  ? 137 TRP B CD1 1 
ATOM   2330 C  CD2 . TRP B 2 54  ? 4.638   6.075   20.023 1.00 45.68  ? 137 TRP B CD2 1 
ATOM   2331 N  NE1 . TRP B 2 54  ? 6.374   6.080   21.440 1.00 50.40  ? 137 TRP B NE1 1 
ATOM   2332 C  CE2 . TRP B 2 54  ? 5.996   6.423   20.168 1.00 45.80  ? 137 TRP B CE2 1 
ATOM   2333 C  CE3 . TRP B 2 54  ? 4.004   6.324   18.803 1.00 47.35  ? 137 TRP B CE3 1 
ATOM   2334 C  CZ2 . TRP B 2 54  ? 6.731   7.009   19.140 1.00 46.49  ? 137 TRP B CZ2 1 
ATOM   2335 C  CZ3 . TRP B 2 54  ? 4.736   6.907   17.782 1.00 57.01  ? 137 TRP B CZ3 1 
ATOM   2336 C  CH2 . TRP B 2 54  ? 6.086   7.242   17.957 1.00 52.49  ? 137 TRP B CH2 1 
ATOM   2337 N  N   . TRP B 2 55  ? -0.230  5.886   20.682 1.00 47.95  ? 138 TRP B N   1 
ATOM   2338 C  CA  . TRP B 2 55  ? -1.556  5.383   20.358 1.00 51.69  ? 138 TRP B CA  1 
ATOM   2339 C  C   . TRP B 2 55  ? -1.527  4.816   18.947 1.00 58.66  ? 138 TRP B C   1 
ATOM   2340 O  O   . TRP B 2 55  ? -0.895  5.388   18.054 1.00 65.52  ? 138 TRP B O   1 
ATOM   2341 C  CB  . TRP B 2 55  ? -2.624  6.483   20.464 1.00 53.26  ? 138 TRP B CB  1 
ATOM   2342 C  CG  . TRP B 2 55  ? -2.442  7.410   21.634 1.00 54.05  ? 138 TRP B CG  1 
ATOM   2343 C  CD1 . TRP B 2 55  ? -1.531  8.424   21.748 1.00 53.03  ? 138 TRP B CD1 1 
ATOM   2344 C  CD2 . TRP B 2 55  ? -3.197  7.413   22.851 1.00 53.47  ? 138 TRP B CD2 1 
ATOM   2345 N  NE1 . TRP B 2 55  ? -1.669  9.051   22.963 1.00 46.60  ? 138 TRP B NE1 1 
ATOM   2346 C  CE2 . TRP B 2 55  ? -2.685  8.450   23.659 1.00 50.51  ? 138 TRP B CE2 1 
ATOM   2347 C  CE3 . TRP B 2 55  ? -4.254  6.638   23.340 1.00 54.37  ? 138 TRP B CE3 1 
ATOM   2348 C  CZ2 . TRP B 2 55  ? -3.196  8.732   24.925 1.00 52.97  ? 138 TRP B CZ2 1 
ATOM   2349 C  CZ3 . TRP B 2 55  ? -4.760  6.921   24.597 1.00 53.06  ? 138 TRP B CZ3 1 
ATOM   2350 C  CH2 . TRP B 2 55  ? -4.230  7.957   25.375 1.00 53.58  ? 138 TRP B CH2 1 
ATOM   2351 N  N   . ASP B 2 56  ? -2.205  3.685   18.748 1.00 54.43  ? 139 ASP B N   1 
ATOM   2352 C  CA  . ASP B 2 56  ? -2.157  3.036   17.444 1.00 55.51  ? 139 ASP B CA  1 
ATOM   2353 C  C   . ASP B 2 56  ? -2.890  3.846   16.383 1.00 59.17  ? 139 ASP B C   1 
ATOM   2354 O  O   . ASP B 2 56  ? -2.478  3.851   15.217 1.00 65.05  ? 139 ASP B O   1 
ATOM   2355 C  CB  . ASP B 2 56  ? -2.733  1.623   17.536 1.00 57.67  ? 139 ASP B CB  1 
ATOM   2356 C  CG  . ASP B 2 56  ? -1.763  0.639   18.166 1.00 61.37  ? 139 ASP B CG  1 
ATOM   2357 O  OD1 . ASP B 2 56  ? -0.610  1.033   18.444 1.00 65.78  ? 139 ASP B OD1 1 
ATOM   2358 O  OD2 . ASP B 2 56  ? -2.149  -0.530  18.378 1.00 60.54  ? 139 ASP B OD2 1 
ATOM   2359 N  N   . GLY B 2 57  ? -3.962  4.537   16.762 1.00 58.66  ? 140 GLY B N   1 
ATOM   2360 C  CA  . GLY B 2 57  ? -4.736  5.316   15.819 1.00 63.03  ? 140 GLY B CA  1 
ATOM   2361 C  C   . GLY B 2 57  ? -5.431  6.467   16.514 1.00 62.99  ? 140 GLY B C   1 
ATOM   2362 O  O   . GLY B 2 57  ? -5.313  6.650   17.727 1.00 59.05  ? 140 GLY B O   1 
ATOM   2363 N  N   . PHE B 2 58  ? -6.167  7.249   15.725 1.00 69.03  ? 141 PHE B N   1 
ATOM   2364 C  CA  . PHE B 2 58  ? -6.863  8.421   16.256 1.00 67.10  ? 141 PHE B CA  1 
ATOM   2365 C  C   . PHE B 2 58  ? -7.990  8.787   15.300 1.00 65.66  ? 141 PHE B C   1 
ATOM   2366 O  O   . PHE B 2 58  ? -7.733  9.335   14.223 1.00 62.44  ? 141 PHE B O   1 
ATOM   2367 C  CB  . PHE B 2 58  ? -5.899  9.586   16.438 1.00 64.19  ? 141 PHE B CB  1 
ATOM   2368 C  CG  . PHE B 2 58  ? -6.579  10.892  16.732 1.00 66.85  ? 141 PHE B CG  1 
ATOM   2369 C  CD1 . PHE B 2 58  ? -7.551  10.978  17.715 1.00 66.00  ? 141 PHE B CD1 1 
ATOM   2370 C  CD2 . PHE B 2 58  ? -6.243  12.036  16.029 1.00 72.58  ? 141 PHE B CD2 1 
ATOM   2371 C  CE1 . PHE B 2 58  ? -8.177  12.178  17.986 1.00 66.07  ? 141 PHE B CE1 1 
ATOM   2372 C  CE2 . PHE B 2 58  ? -6.865  13.239  16.297 1.00 74.15  ? 141 PHE B CE2 1 
ATOM   2373 C  CZ  . PHE B 2 58  ? -7.832  13.310  17.276 1.00 70.70  ? 141 PHE B CZ  1 
ATOM   2374 N  N   . ASP B 2 59  ? -9.228  8.491   15.695 1.00 67.35  ? 142 ASP B N   1 
ATOM   2375 C  CA  . ASP B 2 59  ? -10.410 8.850   14.911 1.00 69.16  ? 142 ASP B CA  1 
ATOM   2376 C  C   . ASP B 2 59  ? -10.793 10.277  15.281 1.00 73.33  ? 142 ASP B C   1 
ATOM   2377 O  O   . ASP B 2 59  ? -11.575 10.518  16.202 1.00 72.52  ? 142 ASP B O   1 
ATOM   2378 C  CB  . ASP B 2 59  ? -11.546 7.869   15.171 1.00 72.71  ? 142 ASP B CB  1 
ATOM   2379 C  CG  . ASP B 2 59  ? -12.609 7.905   14.091 1.00 85.71  ? 142 ASP B CG  1 
ATOM   2380 O  OD1 . ASP B 2 59  ? -12.882 8.999   13.552 1.00 92.40  ? 142 ASP B OD1 1 
ATOM   2381 O  OD2 . ASP B 2 59  ? -13.177 6.836   13.782 1.00 91.89  ? 142 ASP B OD2 1 
ATOM   2382 N  N   . GLU B 2 60  ? -10.231 11.237  14.547 1.00 75.03  ? 143 GLU B N   1 
ATOM   2383 C  CA  . GLU B 2 60  ? -10.438 12.644  14.882 1.00 72.40  ? 143 GLU B CA  1 
ATOM   2384 C  C   . GLU B 2 60  ? -11.898 13.083  14.819 1.00 74.13  ? 143 GLU B C   1 
ATOM   2385 O  O   . GLU B 2 60  ? -12.334 13.790  15.744 1.00 68.89  ? 143 GLU B O   1 
ATOM   2386 C  CB  . GLU B 2 60  ? -9.563  13.522  13.978 1.00 71.93  ? 143 GLU B CB  1 
ATOM   2387 C  CG  . GLU B 2 60  ? -9.882  15.003  14.044 1.00 75.05  ? 143 GLU B CG  1 
ATOM   2388 C  CD  . GLU B 2 60  ? -8.676  15.870  13.744 1.00 88.37  ? 143 GLU B CD  1 
ATOM   2389 O  OE1 . GLU B 2 60  ? -8.508  16.909  14.415 1.00 95.08  ? 143 GLU B OE1 1 
ATOM   2390 O  OE2 . GLU B 2 60  ? -7.893  15.512  12.839 1.00 93.49  ? 143 GLU B OE2 1 
ATOM   2391 N  N   . PRO B 2 61  ? -12.694 12.731  13.797 1.00 75.03  ? 144 PRO B N   1 
ATOM   2392 C  CA  . PRO B 2 61  ? -14.108 13.147  13.820 1.00 77.88  ? 144 PRO B CA  1 
ATOM   2393 C  C   . PRO B 2 61  ? -14.864 12.662  15.047 1.00 81.57  ? 144 PRO B C   1 
ATOM   2394 O  O   . PRO B 2 61  ? -15.748 13.371  15.543 1.00 88.32  ? 144 PRO B O   1 
ATOM   2395 C  CB  . PRO B 2 61  ? -14.666 12.544  12.524 1.00 75.17  ? 144 PRO B CB  1 
ATOM   2396 C  CG  . PRO B 2 61  ? -13.491 12.458  11.626 1.00 72.28  ? 144 PRO B CG  1 
ATOM   2397 C  CD  . PRO B 2 61  ? -12.343 12.091  12.515 1.00 71.23  ? 144 PRO B CD  1 
ATOM   2398 N  N   . ARG B 2 62  ? -14.542 11.471  15.552 1.00 74.81  ? 145 ARG B N   1 
ATOM   2399 C  CA  . ARG B 2 62  ? -15.138 10.963  16.780 1.00 69.12  ? 145 ARG B CA  1 
ATOM   2400 C  C   . ARG B 2 62  ? -14.339 11.325  18.024 1.00 65.94  ? 145 ARG B C   1 
ATOM   2401 O  O   . ARG B 2 62  ? -14.804 11.052  19.136 1.00 59.76  ? 145 ARG B O   1 
ATOM   2402 C  CB  . ARG B 2 62  ? -15.282 9.438   16.715 1.00 70.90  ? 145 ARG B CB  1 
ATOM   2403 C  CG  . ARG B 2 62  ? -16.237 8.929   15.655 1.00 72.69  ? 145 ARG B CG  1 
ATOM   2404 C  CD  . ARG B 2 62  ? -15.954 7.471   15.332 1.00 67.43  ? 145 ARG B CD  1 
ATOM   2405 N  NE  . ARG B 2 62  ? -15.909 6.641   16.533 1.00 67.57  ? 145 ARG B NE  1 
ATOM   2406 C  CZ  . ARG B 2 62  ? -14.993 5.704   16.763 1.00 68.96  ? 145 ARG B CZ  1 
ATOM   2407 N  NH1 . ARG B 2 62  ? -14.034 5.476   15.875 1.00 72.24  ? 145 ARG B NH1 1 
ATOM   2408 N  NH2 . ARG B 2 62  ? -15.031 4.996   17.883 1.00 62.00  ? 145 ARG B NH2 1 
ATOM   2409 N  N   . CYS B 2 63  ? -13.157 11.920  17.862 1.00 66.00  ? 146 CYS B N   1 
ATOM   2410 C  CA  . CYS B 2 63  ? -12.261 12.218  18.980 1.00 68.22  ? 146 CYS B CA  1 
ATOM   2411 C  C   . CYS B 2 63  ? -12.032 10.985  19.849 1.00 70.47  ? 146 CYS B C   1 
ATOM   2412 O  O   . CYS B 2 63  ? -12.053 11.049  21.080 1.00 71.39  ? 146 CYS B O   1 
ATOM   2413 C  CB  . CYS B 2 63  ? -12.782 13.381  19.821 1.00 70.26  ? 146 CYS B CB  1 
ATOM   2414 S  SG  . CYS B 2 63  ? -11.477 14.129  20.833 1.00 76.19  ? 146 CYS B SG  1 
ATOM   2415 N  N   . THR B 2 64  ? -11.818 9.846   19.200 1.00 71.89  ? 147 THR B N   1 
ATOM   2416 C  CA  . THR B 2 64  ? -11.556 8.589   19.883 1.00 65.69  ? 147 THR B CA  1 
ATOM   2417 C  C   . THR B 2 64  ? -10.167 8.103   19.499 1.00 64.75  ? 147 THR B C   1 
ATOM   2418 O  O   . THR B 2 64  ? -9.833  8.043   18.311 1.00 67.01  ? 147 THR B O   1 
ATOM   2419 C  CB  . THR B 2 64  ? -12.605 7.531   19.526 1.00 66.36  ? 147 THR B CB  1 
ATOM   2420 O  OG1 . THR B 2 64  ? -13.901 7.978   19.940 1.00 76.63  ? 147 THR B OG1 1 
ATOM   2421 C  CG2 . THR B 2 64  ? -12.289 6.218   20.214 1.00 67.60  ? 147 THR B CG2 1 
ATOM   2422 N  N   . LEU B 2 65  ? -9.359  7.770   20.499 1.00 58.26  ? 148 LEU B N   1 
ATOM   2423 C  CA  . LEU B 2 65  ? -8.040  7.208   20.253 1.00 62.43  ? 148 LEU B CA  1 
ATOM   2424 C  C   . LEU B 2 65  ? -8.133  5.691   20.187 1.00 63.58  ? 148 LEU B C   1 
ATOM   2425 O  O   . LEU B 2 65  ? -8.815  5.062   20.999 1.00 64.39  ? 148 LEU B O   1 
ATOM   2426 C  CB  . LEU B 2 65  ? -7.052  7.636   21.338 1.00 62.98  ? 148 LEU B CB  1 
ATOM   2427 C  CG  . LEU B 2 65  ? -6.862  9.148   21.457 1.00 62.13  ? 148 LEU B CG  1 
ATOM   2428 C  CD1 . LEU B 2 65  ? -6.873  9.588   22.912 1.00 67.12  ? 148 LEU B CD1 1 
ATOM   2429 C  CD2 . LEU B 2 65  ? -5.581  9.580   20.761 1.00 59.59  ? 148 LEU B CD2 1 
ATOM   2430 N  N   . LEU B 2 66  ? -7.444  5.109   19.213 1.00 64.15  ? 149 LEU B N   1 
ATOM   2431 C  CA  . LEU B 2 66  ? -7.572  3.695   18.906 1.00 61.43  ? 149 LEU B CA  1 
ATOM   2432 C  C   . LEU B 2 66  ? -6.315  2.932   19.303 1.00 61.33  ? 149 LEU B C   1 
ATOM   2433 O  O   . LEU B 2 66  ? -5.204  3.469   19.275 1.00 67.95  ? 149 LEU B O   1 
ATOM   2434 C  CB  . LEU B 2 66  ? -7.851  3.486   17.415 1.00 64.24  ? 149 LEU B CB  1 
ATOM   2435 C  CG  . LEU B 2 66  ? -8.972  4.343   16.826 1.00 70.61  ? 149 LEU B CG  1 
ATOM   2436 C  CD1 . LEU B 2 66  ? -9.063  4.147   15.322 1.00 77.66  ? 149 LEU B CD1 1 
ATOM   2437 C  CD2 . LEU B 2 66  ? -10.297 4.019   17.498 1.00 73.15  ? 149 LEU B CD2 1 
ATOM   2438 N  N   . GLU B 2 67  ? -6.510  1.668   19.674 1.00 58.12  ? 150 GLU B N   1 
ATOM   2439 C  CA  . GLU B 2 67  ? -5.415  0.741   19.929 1.00 58.74  ? 150 GLU B CA  1 
ATOM   2440 C  C   . GLU B 2 67  ? -5.861  -0.649  19.501 1.00 58.96  ? 150 GLU B C   1 
ATOM   2441 O  O   . GLU B 2 67  ? -6.953  -1.089  19.869 1.00 67.03  ? 150 GLU B O   1 
ATOM   2442 C  CB  . GLU B 2 67  ? -5.012  0.744   21.407 1.00 64.27  ? 150 GLU B CB  1 
ATOM   2443 C  CG  . GLU B 2 67  ? -3.873  -0.206  21.747 1.00 67.71  ? 150 GLU B CG  1 
ATOM   2444 C  CD  . GLU B 2 67  ? -2.503  0.414   21.532 1.00 70.96  ? 150 GLU B CD  1 
ATOM   2445 O  OE1 . GLU B 2 67  ? -1.491  -0.255  21.836 1.00 72.87  ? 150 GLU B OE1 1 
ATOM   2446 O  OE2 . GLU B 2 67  ? -2.438  1.570   21.061 1.00 72.97  ? 150 GLU B OE2 1 
ATOM   2447 N  N   . ALA B 2 68  ? -5.021  -1.330  18.726 1.00 54.60  ? 151 ALA B N   1 
ATOM   2448 C  CA  . ALA B 2 68  ? -5.330  -2.651  18.199 1.00 53.45  ? 151 ALA B CA  1 
ATOM   2449 C  C   . ALA B 2 68  ? -4.370  -3.685  18.773 1.00 62.16  ? 151 ALA B C   1 
ATOM   2450 O  O   . ALA B 2 68  ? -3.170  -3.423  18.912 1.00 68.84  ? 151 ALA B O   1 
ATOM   2451 C  CB  . ALA B 2 68  ? -5.255  -2.662  16.670 1.00 53.45  ? 151 ALA B CB  1 
ATOM   2452 N  N   . LYS B 2 69  ? -4.906  -4.862  19.097 1.00 62.05  ? 152 LYS B N   1 
ATOM   2453 C  CA  . LYS B 2 69  ? -4.133  -5.967  19.658 1.00 55.18  ? 152 LYS B CA  1 
ATOM   2454 C  C   . LYS B 2 69  ? -4.479  -7.238  18.898 1.00 60.02  ? 152 LYS B C   1 
ATOM   2455 O  O   . LYS B 2 69  ? -5.642  -7.656  18.877 1.00 58.32  ? 152 LYS B O   1 
ATOM   2456 C  CB  . LYS B 2 69  ? -4.417  -6.138  21.154 1.00 51.67  ? 152 LYS B CB  1 
ATOM   2457 C  CG  . LYS B 2 69  ? -3.970  -4.959  22.010 1.00 56.54  ? 152 LYS B CG  1 
ATOM   2458 C  CD  . LYS B 2 69  ? -2.455  -4.834  22.019 1.00 64.82  ? 152 LYS B CD  1 
ATOM   2459 C  CE  . LYS B 2 69  ? -2.008  -3.501  22.588 1.00 67.05  ? 152 LYS B CE  1 
ATOM   2460 N  NZ  . LYS B 2 69  ? -0.523  -3.392  22.633 1.00 75.29  ? 152 LYS B NZ  1 
ATOM   2461 N  N   . ALA B 2 70  ? -3.471  -7.858  18.286 1.00 67.44  ? 153 ALA B N   1 
ATOM   2462 C  CA  . ALA B 2 70  ? -3.707  -9.002  17.415 1.00 70.68  ? 153 ALA B CA  1 
ATOM   2463 C  C   . ALA B 2 70  ? -3.472  -10.331 18.124 1.00 78.46  ? 153 ALA B C   1 
ATOM   2464 O  O   . ALA B 2 70  ? -4.418  -10.943 18.631 1.00 89.90  ? 153 ALA B O   1 
ATOM   2465 C  CB  . ALA B 2 70  ? -2.821  -8.911  16.171 1.00 76.04  ? 153 ALA B CB  1 
ATOM   2466 N  N   . ASN B 2 71  ? -2.221  -10.785 18.164 1.00 76.61  ? 154 ASN B N   1 
ATOM   2467 C  CA  . ASN B 2 71  ? -1.888  -12.136 18.617 1.00 77.47  ? 154 ASN B CA  1 
ATOM   2468 C  C   . ASN B 2 71  ? -1.545  -12.104 20.103 1.00 76.82  ? 154 ASN B C   1 
ATOM   2469 O  O   . ASN B 2 71  ? -0.447  -11.700 20.492 1.00 78.34  ? 154 ASN B O   1 
ATOM   2470 C  CB  . ASN B 2 71  ? -0.738  -12.704 17.792 1.00 74.89  ? 154 ASN B CB  1 
ATOM   2471 C  CG  . ASN B 2 71  ? -0.492  -14.174 18.066 1.00 86.08  ? 154 ASN B CG  1 
ATOM   2472 O  OD1 . ASN B 2 71  ? -1.399  -14.905 18.468 1.00 87.15  ? 154 ASN B OD1 1 
ATOM   2473 N  ND2 . ASN B 2 71  ? 0.741   -14.618 17.845 1.00 95.24  ? 154 ASN B ND2 1 
ATOM   2474 N  N   . TYR B 2 72  ? -2.486  -12.549 20.940 1.00 73.55  ? 155 TYR B N   1 
ATOM   2475 C  CA  . TYR B 2 72  ? -2.248  -12.635 22.373 1.00 69.05  ? 155 TYR B CA  1 
ATOM   2476 C  C   . TYR B 2 72  ? -2.903  -13.840 23.033 1.00 77.49  ? 155 TYR B C   1 
ATOM   2477 O  O   . TYR B 2 72  ? -2.701  -14.042 24.234 1.00 83.63  ? 155 TYR B O   1 
ATOM   2478 C  CB  . TYR B 2 72  ? -2.731  -11.357 23.076 1.00 65.35  ? 155 TYR B CB  1 
ATOM   2479 C  CG  . TYR B 2 72  ? -1.784  -10.188 22.941 1.00 67.77  ? 155 TYR B CG  1 
ATOM   2480 C  CD1 . TYR B 2 72  ? -0.697  -10.047 23.793 1.00 67.31  ? 155 TYR B CD1 1 
ATOM   2481 C  CD2 . TYR B 2 72  ? -1.976  -9.225  21.961 1.00 66.29  ? 155 TYR B CD2 1 
ATOM   2482 C  CE1 . TYR B 2 72  ? 0.171   -8.978  23.671 1.00 63.36  ? 155 TYR B CE1 1 
ATOM   2483 C  CE2 . TYR B 2 72  ? -1.115  -8.153  21.832 1.00 64.10  ? 155 TYR B CE2 1 
ATOM   2484 C  CZ  . TYR B 2 72  ? -0.042  -8.034  22.689 1.00 66.23  ? 155 TYR B CZ  1 
ATOM   2485 O  OH  . TYR B 2 72  ? 0.818   -6.966  22.558 1.00 69.86  ? 155 TYR B OH  1 
ATOM   2486 N  N   . ALA B 2 73  ? -3.673  -14.647 22.298 1.00 78.18  ? 156 ALA B N   1 
ATOM   2487 C  CA  . ALA B 2 73  ? -4.371  -15.772 22.907 1.00 72.24  ? 156 ALA B CA  1 
ATOM   2488 C  C   . ALA B 2 73  ? -3.419  -16.845 23.413 1.00 72.17  ? 156 ALA B C   1 
ATOM   2489 O  O   . ALA B 2 73  ? -3.787  -17.601 24.319 1.00 83.11  ? 156 ALA B O   1 
ATOM   2490 C  CB  . ALA B 2 73  ? -5.356  -16.385 21.910 1.00 73.52  ? 156 ALA B CB  1 
ATOM   2491 N  N   . PHE B 2 74  ? -2.208  -16.925 22.860 1.00 69.83  ? 157 PHE B N   1 
ATOM   2492 C  CA  . PHE B 2 74  ? -1.268  -17.969 23.252 1.00 73.91  ? 157 PHE B CA  1 
ATOM   2493 C  C   . PHE B 2 74  ? -0.751  -17.800 24.674 1.00 76.85  ? 157 PHE B C   1 
ATOM   2494 O  O   . PHE B 2 74  ? -0.089  -18.711 25.184 1.00 87.79  ? 157 PHE B O   1 
ATOM   2495 C  CB  . PHE B 2 74  ? -0.096  -18.021 22.266 1.00 69.77  ? 157 PHE B CB  1 
ATOM   2496 C  CG  . PHE B 2 74  ? 0.785   -16.803 22.294 1.00 69.49  ? 157 PHE B CG  1 
ATOM   2497 C  CD1 . PHE B 2 74  ? 0.324   -15.579 21.834 1.00 71.54  ? 157 PHE B CD1 1 
ATOM   2498 C  CD2 . PHE B 2 74  ? 2.083   -16.886 22.764 1.00 66.08  ? 157 PHE B CD2 1 
ATOM   2499 C  CE1 . PHE B 2 74  ? 1.137   -14.459 21.858 1.00 66.13  ? 157 PHE B CE1 1 
ATOM   2500 C  CE2 . PHE B 2 74  ? 2.900   -15.774 22.785 1.00 64.16  ? 157 PHE B CE2 1 
ATOM   2501 C  CZ  . PHE B 2 74  ? 2.426   -14.559 22.334 1.00 61.21  ? 157 PHE B CZ  1 
ATOM   2502 N  N   . LEU B 2 75  ? -1.039  -16.675 25.326 1.00 68.05  ? 158 LEU B N   1 
ATOM   2503 C  CA  . LEU B 2 75  ? -0.685  -16.469 26.723 1.00 68.01  ? 158 LEU B CA  1 
ATOM   2504 C  C   . LEU B 2 75  ? -1.839  -16.751 27.675 1.00 73.64  ? 158 LEU B C   1 
ATOM   2505 O  O   . LEU B 2 75  ? -1.667  -16.632 28.894 1.00 69.63  ? 158 LEU B O   1 
ATOM   2506 C  CB  . LEU B 2 75  ? -0.172  -15.041 26.928 1.00 60.63  ? 158 LEU B CB  1 
ATOM   2507 C  CG  . LEU B 2 75  ? 0.889   -14.601 25.919 1.00 66.95  ? 158 LEU B CG  1 
ATOM   2508 C  CD1 . LEU B 2 75  ? 1.116   -13.100 25.997 1.00 60.51  ? 158 LEU B CD1 1 
ATOM   2509 C  CD2 . LEU B 2 75  ? 2.193   -15.364 26.139 1.00 70.84  ? 158 LEU B CD2 1 
ATOM   2510 N  N   . PHE B 2 76  ? -3.003  -17.123 27.153 1.00 75.27  ? 159 PHE B N   1 
ATOM   2511 C  CA  . PHE B 2 76  ? -4.146  -17.518 27.958 1.00 72.56  ? 159 PHE B CA  1 
ATOM   2512 C  C   . PHE B 2 76  ? -4.448  -18.991 27.727 1.00 80.28  ? 159 PHE B C   1 
ATOM   2513 O  O   . PHE B 2 76  ? -4.126  -19.551 26.675 1.00 85.18  ? 159 PHE B O   1 
ATOM   2514 C  CB  . PHE B 2 76  ? -5.384  -16.683 27.614 1.00 70.21  ? 159 PHE B CB  1 
ATOM   2515 C  CG  . PHE B 2 76  ? -5.164  -15.201 27.702 1.00 70.22  ? 159 PHE B CG  1 
ATOM   2516 C  CD1 . PHE B 2 76  ? -5.464  -14.514 28.865 1.00 63.62  ? 159 PHE B CD1 1 
ATOM   2517 C  CD2 . PHE B 2 76  ? -4.671  -14.492 26.619 1.00 73.71  ? 159 PHE B CD2 1 
ATOM   2518 C  CE1 . PHE B 2 76  ? -5.267  -13.155 28.949 1.00 66.16  ? 159 PHE B CE1 1 
ATOM   2519 C  CE2 . PHE B 2 76  ? -4.471  -13.129 26.697 1.00 66.99  ? 159 PHE B CE2 1 
ATOM   2520 C  CZ  . PHE B 2 76  ? -4.769  -12.459 27.863 1.00 66.97  ? 159 PHE B CZ  1 
ATOM   2521 N  N   . VAL B 2 77  ? -5.063  -19.621 28.720 1.00 84.68  ? 160 VAL B N   1 
ATOM   2522 C  CA  . VAL B 2 77  ? -5.618  -20.954 28.511 1.00 95.82  ? 160 VAL B CA  1 
ATOM   2523 C  C   . VAL B 2 77  ? -7.027  -20.750 27.964 1.00 98.09  ? 160 VAL B C   1 
ATOM   2524 O  O   . VAL B 2 77  ? -7.774  -19.897 28.464 1.00 93.90  ? 160 VAL B O   1 
ATOM   2525 C  CB  . VAL B 2 77  ? -5.565  -21.801 29.796 1.00 99.21  ? 160 VAL B CB  1 
ATOM   2526 C  CG1 . VAL B 2 77  ? -4.198  -21.665 30.450 1.00 99.10  ? 160 VAL B CG1 1 
ATOM   2527 C  CG2 . VAL B 2 77  ? -6.634  -21.390 30.773 1.00 100.87 ? 160 VAL B CG2 1 
ATOM   2528 N  N   . PRO B 2 78  ? -7.410  -21.458 26.906 1.00 105.41 ? 161 PRO B N   1 
ATOM   2529 C  CA  . PRO B 2 78  ? -8.649  -21.110 26.197 1.00 110.74 ? 161 PRO B CA  1 
ATOM   2530 C  C   . PRO B 2 78  ? -9.912  -21.362 27.005 1.00 115.44 ? 161 PRO B C   1 
ATOM   2531 O  O   . PRO B 2 78  ? -10.726 -20.453 27.193 1.00 118.87 ? 161 PRO B O   1 
ATOM   2532 C  CB  . PRO B 2 78  ? -8.602  -22.006 24.950 1.00 121.36 ? 161 PRO B CB  1 
ATOM   2533 C  CG  . PRO B 2 78  ? -7.165  -22.424 24.821 1.00 120.97 ? 161 PRO B CG  1 
ATOM   2534 C  CD  . PRO B 2 78  ? -6.663  -22.525 26.223 1.00 115.32 ? 161 PRO B CD  1 
ATOM   2535 N  N   . LEU B 2 79  ? -10.085 -22.593 27.491 1.00 113.41 ? 162 LEU B N   1 
ATOM   2536 C  CA  . LEU B 2 79  ? -11.353 -22.983 28.096 1.00 111.87 ? 162 LEU B CA  1 
ATOM   2537 C  C   . LEU B 2 79  ? -11.622 -22.289 29.425 1.00 103.80 ? 162 LEU B C   1 
ATOM   2538 O  O   . LEU B 2 79  ? -12.787 -22.158 29.814 1.00 108.91 ? 162 LEU B O   1 
ATOM   2539 C  CB  . LEU B 2 79  ? -11.390 -24.500 28.288 1.00 120.26 ? 162 LEU B CB  1 
ATOM   2540 C  CG  . LEU B 2 79  ? -11.098 -25.332 27.038 1.00 125.15 ? 162 LEU B CG  1 
ATOM   2541 C  CD1 . LEU B 2 79  ? -10.693 -26.750 27.413 1.00 123.08 ? 162 LEU B CD1 1 
ATOM   2542 C  CD2 . LEU B 2 79  ? -12.300 -25.342 26.104 1.00 126.85 ? 162 LEU B CD2 1 
ATOM   2543 N  N   . LEU B 2 80  ? -10.586 -21.834 30.126 1.00 96.55  ? 163 LEU B N   1 
ATOM   2544 C  CA  . LEU B 2 80  ? -10.746 -21.328 31.483 1.00 96.72  ? 163 LEU B CA  1 
ATOM   2545 C  C   . LEU B 2 80  ? -10.829 -19.808 31.549 1.00 96.47  ? 163 LEU B C   1 
ATOM   2546 O  O   . LEU B 2 80  ? -11.223 -19.270 32.589 1.00 98.50  ? 163 LEU B O   1 
ATOM   2547 C  CB  . LEU B 2 80  ? -9.591  -21.812 32.374 1.00 95.52  ? 163 LEU B CB  1 
ATOM   2548 C  CG  . LEU B 2 80  ? -9.347  -23.294 32.696 1.00 100.27 ? 163 LEU B CG  1 
ATOM   2549 C  CD1 . LEU B 2 80  ? -9.103  -24.162 31.466 1.00 104.72 ? 163 LEU B CD1 1 
ATOM   2550 C  CD2 . LEU B 2 80  ? -8.162  -23.411 33.645 1.00 101.70 ? 163 LEU B CD2 1 
ATOM   2551 N  N   . GLY B 2 81  ? -10.468 -19.107 30.475 1.00 93.31  ? 164 GLY B N   1 
ATOM   2552 C  CA  . GLY B 2 81  ? -10.546 -17.660 30.453 1.00 81.94  ? 164 GLY B CA  1 
ATOM   2553 C  C   . GLY B 2 81  ? -9.540  -16.944 31.320 1.00 77.41  ? 164 GLY B C   1 
ATOM   2554 O  O   . GLY B 2 81  ? -9.711  -15.750 31.583 1.00 79.32  ? 164 GLY B O   1 
ATOM   2555 N  N   . VAL B 2 82  ? -8.498  -17.630 31.777 1.00 77.80  ? 165 VAL B N   1 
ATOM   2556 C  CA  . VAL B 2 82  ? -7.462  -17.006 32.596 1.00 77.16  ? 165 VAL B CA  1 
ATOM   2557 C  C   . VAL B 2 82  ? -6.141  -17.067 31.839 1.00 72.40  ? 165 VAL B C   1 
ATOM   2558 O  O   . VAL B 2 82  ? -5.950  -17.953 30.992 1.00 75.30  ? 165 VAL B O   1 
ATOM   2559 C  CB  . VAL B 2 82  ? -7.350  -17.682 33.974 1.00 82.26  ? 165 VAL B CB  1 
ATOM   2560 C  CG1 . VAL B 2 82  ? -8.692  -17.652 34.694 1.00 82.38  ? 165 VAL B CG1 1 
ATOM   2561 C  CG2 . VAL B 2 82  ? -6.841  -19.113 33.836 1.00 79.51  ? 165 VAL B CG2 1 
ATOM   2562 N  N   . PRO B 2 83  ? -5.216  -16.146 32.094 1.00 67.73  ? 166 PRO B N   1 
ATOM   2563 C  CA  . PRO B 2 83  ? -3.895  -16.231 31.466 1.00 68.41  ? 166 PRO B CA  1 
ATOM   2564 C  C   . PRO B 2 83  ? -3.076  -17.376 32.037 1.00 71.49  ? 166 PRO B C   1 
ATOM   2565 O  O   . PRO B 2 83  ? -3.310  -17.860 33.147 1.00 70.62  ? 166 PRO B O   1 
ATOM   2566 C  CB  . PRO B 2 83  ? -3.249  -14.880 31.799 1.00 65.96  ? 166 PRO B CB  1 
ATOM   2567 C  CG  . PRO B 2 83  ? -4.381  -13.990 32.203 1.00 62.76  ? 166 PRO B CG  1 
ATOM   2568 C  CD  . PRO B 2 83  ? -5.394  -14.887 32.832 1.00 66.29  ? 166 PRO B CD  1 
ATOM   2569 N  N   . ARG B 2 84  ? -2.104  -17.808 31.248 1.00 74.62  ? 167 ARG B N   1 
ATOM   2570 C  CA  . ARG B 2 84  ? -1.120  -18.752 31.751 1.00 79.52  ? 167 ARG B CA  1 
ATOM   2571 C  C   . ARG B 2 84  ? -0.274  -18.053 32.807 1.00 81.53  ? 167 ARG B C   1 
ATOM   2572 O  O   . ARG B 2 84  ? 0.181   -16.927 32.579 1.00 75.33  ? 167 ARG B O   1 
ATOM   2573 C  CB  . ARG B 2 84  ? -0.247  -19.277 30.615 1.00 76.51  ? 167 ARG B CB  1 
ATOM   2574 C  CG  . ARG B 2 84  ? -1.047  -19.810 29.435 1.00 79.97  ? 167 ARG B CG  1 
ATOM   2575 C  CD  . ARG B 2 84  ? -0.154  -20.508 28.426 1.00 88.70  ? 167 ARG B CD  1 
ATOM   2576 N  NE  . ARG B 2 84  ? -0.838  -20.756 27.159 1.00 90.43  ? 167 ARG B NE  1 
ATOM   2577 C  CZ  . ARG B 2 84  ? -1.570  -21.835 26.903 1.00 92.25  ? 167 ARG B CZ  1 
ATOM   2578 N  NH1 . ARG B 2 84  ? -1.719  -22.772 27.828 1.00 88.53  ? 167 ARG B NH1 1 
ATOM   2579 N  NH2 . ARG B 2 84  ? -2.155  -21.977 25.721 1.00 100.29 ? 167 ARG B NH2 1 
ATOM   2580 N  N   . PRO B 2 85  ? -0.061  -18.668 33.973 1.00 69.09  ? 168 PRO B N   1 
ATOM   2581 C  CA  . PRO B 2 85  ? 0.634   -17.959 35.062 1.00 72.29  ? 168 PRO B CA  1 
ATOM   2582 C  C   . PRO B 2 85  ? 2.017   -17.462 34.680 1.00 72.88  ? 168 PRO B C   1 
ATOM   2583 O  O   . PRO B 2 85  ? 2.477   -16.455 35.233 1.00 72.54  ? 168 PRO B O   1 
ATOM   2584 C  CB  . PRO B 2 85  ? 0.699   -19.012 36.178 1.00 75.54  ? 168 PRO B CB  1 
ATOM   2585 C  CG  . PRO B 2 85  ? -0.410  -19.969 35.865 1.00 71.96  ? 168 PRO B CG  1 
ATOM   2586 C  CD  . PRO B 2 85  ? -0.489  -20.019 34.371 1.00 66.67  ? 168 PRO B CD  1 
ATOM   2587 N  N   . TRP B 2 86  ? 2.688   -18.126 33.738 1.00 71.45  ? 169 TRP B N   1 
ATOM   2588 C  CA  . TRP B 2 86  ? 4.022   -17.709 33.331 1.00 65.47  ? 169 TRP B CA  1 
ATOM   2589 C  C   . TRP B 2 86  ? 4.015   -16.478 32.437 1.00 65.38  ? 169 TRP B C   1 
ATOM   2590 O  O   . TRP B 2 86  ? 5.089   -15.935 32.153 1.00 66.80  ? 169 TRP B O   1 
ATOM   2591 C  CB  . TRP B 2 86  ? 4.741   -18.860 32.619 1.00 58.91  ? 169 TRP B CB  1 
ATOM   2592 C  CG  . TRP B 2 86  ? 4.051   -19.384 31.392 1.00 61.65  ? 169 TRP B CG  1 
ATOM   2593 C  CD1 . TRP B 2 86  ? 3.259   -20.492 31.310 1.00 61.38  ? 169 TRP B CD1 1 
ATOM   2594 C  CD2 . TRP B 2 86  ? 4.113   -18.839 30.067 1.00 65.20  ? 169 TRP B CD2 1 
ATOM   2595 N  NE1 . TRP B 2 86  ? 2.816   -20.665 30.022 1.00 58.55  ? 169 TRP B NE1 1 
ATOM   2596 C  CE2 . TRP B 2 86  ? 3.326   -19.663 29.238 1.00 59.28  ? 169 TRP B CE2 1 
ATOM   2597 C  CE3 . TRP B 2 86  ? 4.755   -17.731 29.501 1.00 65.51  ? 169 TRP B CE3 1 
ATOM   2598 C  CZ2 . TRP B 2 86  ? 3.163   -19.416 27.877 1.00 58.45  ? 169 TRP B CZ2 1 
ATOM   2599 C  CZ3 . TRP B 2 86  ? 4.588   -17.487 28.150 1.00 61.71  ? 169 TRP B CZ3 1 
ATOM   2600 C  CH2 . TRP B 2 86  ? 3.802   -18.327 27.353 1.00 60.49  ? 169 TRP B CH2 1 
ATOM   2601 N  N   . ALA B 2 87  ? 2.843   -16.024 31.992 1.00 67.00  ? 170 ALA B N   1 
ATOM   2602 C  CA  . ALA B 2 87  ? 2.736   -14.888 31.087 1.00 68.35  ? 170 ALA B CA  1 
ATOM   2603 C  C   . ALA B 2 87  ? 2.100   -13.673 31.752 1.00 66.38  ? 170 ALA B C   1 
ATOM   2604 O  O   . ALA B 2 87  ? 1.679   -12.742 31.058 1.00 69.65  ? 170 ALA B O   1 
ATOM   2605 C  CB  . ALA B 2 87  ? 1.946   -15.281 29.839 1.00 64.45  ? 170 ALA B CB  1 
ATOM   2606 N  N   . ARG B 2 88  ? 2.029   -13.662 33.085 1.00 59.91  ? 171 ARG B N   1 
ATOM   2607 C  CA  . ARG B 2 88  ? 1.391   -12.552 33.785 1.00 62.88  ? 171 ARG B CA  1 
ATOM   2608 C  C   . ARG B 2 88  ? 2.116   -11.236 33.524 1.00 68.75  ? 171 ARG B C   1 
ATOM   2609 O  O   . ARG B 2 88  ? 1.477   -10.195 33.334 1.00 69.80  ? 171 ARG B O   1 
ATOM   2610 C  CB  . ARG B 2 88  ? 1.333   -12.845 35.283 1.00 63.02  ? 171 ARG B CB  1 
ATOM   2611 C  CG  . ARG B 2 88  ? 0.774   -11.707 36.122 1.00 64.30  ? 171 ARG B CG  1 
ATOM   2612 C  CD  . ARG B 2 88  ? -0.694  -11.463 35.812 1.00 67.00  ? 171 ARG B CD  1 
ATOM   2613 N  NE  . ARG B 2 88  ? -1.083  -10.082 36.076 1.00 71.29  ? 171 ARG B NE  1 
ATOM   2614 C  CZ  . ARG B 2 88  ? -2.313  -9.607  35.912 1.00 71.97  ? 171 ARG B CZ  1 
ATOM   2615 N  NH1 . ARG B 2 88  ? -3.282  -10.405 35.485 1.00 78.81  ? 171 ARG B NH1 1 
ATOM   2616 N  NH2 . ARG B 2 88  ? -2.574  -8.335  36.177 1.00 68.21  ? 171 ARG B NH2 1 
ATOM   2617 N  N   . ALA B 2 89  ? 3.451   -11.263 33.506 1.00 70.53  ? 172 ALA B N   1 
ATOM   2618 C  CA  . ALA B 2 89  ? 4.211   -10.034 33.299 1.00 65.45  ? 172 ALA B CA  1 
ATOM   2619 C  C   . ALA B 2 89  ? 3.974   -9.459  31.907 1.00 62.98  ? 172 ALA B C   1 
ATOM   2620 O  O   . ALA B 2 89  ? 3.851   -8.238  31.750 1.00 65.66  ? 172 ALA B O   1 
ATOM   2621 C  CB  . ALA B 2 89  ? 5.700   -10.290 33.527 1.00 64.32  ? 172 ALA B CB  1 
ATOM   2622 N  N   . LYS B 2 90  ? 3.907   -10.318 30.887 1.00 62.55  ? 173 LYS B N   1 
ATOM   2623 C  CA  . LYS B 2 90  ? 3.657   -9.836  29.531 1.00 54.10  ? 173 LYS B CA  1 
ATOM   2624 C  C   . LYS B 2 90  ? 2.223   -9.346  29.377 1.00 59.07  ? 173 LYS B C   1 
ATOM   2625 O  O   . LYS B 2 90  ? 1.970   -8.359  28.676 1.00 61.38  ? 173 LYS B O   1 
ATOM   2626 C  CB  . LYS B 2 90  ? 3.963   -10.936 28.514 1.00 48.60  ? 173 LYS B CB  1 
ATOM   2627 C  CG  . LYS B 2 90  ? 3.654   -10.562 27.074 1.00 50.00  ? 173 LYS B CG  1 
ATOM   2628 C  CD  . LYS B 2 90  ? 4.732   -11.049 26.123 1.00 53.30  ? 173 LYS B CD  1 
ATOM   2629 C  CE  . LYS B 2 90  ? 4.537   -10.461 24.732 1.00 66.66  ? 173 LYS B CE  1 
ATOM   2630 N  NZ  . LYS B 2 90  ? 5.821   -10.387 23.972 1.00 79.01  ? 173 LYS B NZ  1 
ATOM   2631 N  N   . VAL B 2 91  ? 1.272   -10.021 30.026 1.00 58.34  ? 174 VAL B N   1 
ATOM   2632 C  CA  . VAL B 2 91  ? -0.117  -9.574  29.981 1.00 58.82  ? 174 VAL B CA  1 
ATOM   2633 C  C   . VAL B 2 91  ? -0.271  -8.245  30.709 1.00 59.15  ? 174 VAL B C   1 
ATOM   2634 O  O   . VAL B 2 91  ? -1.009  -7.357  30.262 1.00 67.45  ? 174 VAL B O   1 
ATOM   2635 C  CB  . VAL B 2 91  ? -1.044  -10.656 30.568 1.00 62.15  ? 174 VAL B CB  1 
ATOM   2636 C  CG1 . VAL B 2 91  ? -2.440  -10.096 30.812 1.00 64.51  ? 174 VAL B CG1 1 
ATOM   2637 C  CG2 . VAL B 2 91  ? -1.106  -11.863 29.645 1.00 60.12  ? 174 VAL B CG2 1 
ATOM   2638 N  N   . LYS B 2 92  ? 0.432   -8.080  31.831 1.00 57.68  ? 175 LYS B N   1 
ATOM   2639 C  CA  . LYS B 2 92  ? 0.314   -6.853  32.612 1.00 59.85  ? 175 LYS B CA  1 
ATOM   2640 C  C   . LYS B 2 92  ? 0.795   -5.644  31.819 1.00 64.51  ? 175 LYS B C   1 
ATOM   2641 O  O   . LYS B 2 92  ? 0.110   -4.618  31.750 1.00 71.00  ? 175 LYS B O   1 
ATOM   2642 C  CB  . LYS B 2 92  ? 1.102   -6.991  33.916 1.00 60.73  ? 175 LYS B CB  1 
ATOM   2643 C  CG  . LYS B 2 92  ? 1.053   -5.768  34.819 1.00 67.78  ? 175 LYS B CG  1 
ATOM   2644 C  CD  . LYS B 2 92  ? 2.030   -5.908  35.979 1.00 72.86  ? 175 LYS B CD  1 
ATOM   2645 C  CE  . LYS B 2 92  ? 1.894   -4.765  36.975 1.00 72.50  ? 175 LYS B CE  1 
ATOM   2646 N  NZ  . LYS B 2 92  ? 0.580   -4.777  37.671 1.00 70.77  ? 175 LYS B NZ  1 
ATOM   2647 N  N   . SER B 2 93  ? 1.971   -5.752  31.199 1.00 63.88  ? 176 SER B N   1 
ATOM   2648 C  CA  . SER B 2 93  ? 2.561   -4.600  30.529 1.00 65.54  ? 176 SER B CA  1 
ATOM   2649 C  C   . SER B 2 93  ? 1.899   -4.328  29.182 1.00 65.84  ? 176 SER B C   1 
ATOM   2650 O  O   . SER B 2 93  ? 1.590   -3.177  28.857 1.00 68.39  ? 176 SER B O   1 
ATOM   2651 C  CB  . SER B 2 93  ? 4.065   -4.811  30.353 1.00 60.02  ? 176 SER B CB  1 
ATOM   2652 O  OG  . SER B 2 93  ? 4.321   -5.850  29.428 1.00 62.66  ? 176 SER B OG  1 
ATOM   2653 N  N   . ASP B 2 94  ? 1.671   -5.373  28.387 1.00 65.31  ? 177 ASP B N   1 
ATOM   2654 C  CA  . ASP B 2 94  ? 1.195   -5.175  27.022 1.00 65.90  ? 177 ASP B CA  1 
ATOM   2655 C  C   . ASP B 2 94  ? -0.307  -4.924  26.950 1.00 66.27  ? 177 ASP B C   1 
ATOM   2656 O  O   . ASP B 2 94  ? -0.767  -4.229  26.037 1.00 67.07  ? 177 ASP B O   1 
ATOM   2657 C  CB  . ASP B 2 94  ? 1.556   -6.386  26.158 1.00 67.81  ? 177 ASP B CB  1 
ATOM   2658 C  CG  . ASP B 2 94  ? 3.043   -6.479  25.873 1.00 69.86  ? 177 ASP B CG  1 
ATOM   2659 O  OD1 . ASP B 2 94  ? 3.460   -7.436  25.187 1.00 71.50  ? 177 ASP B OD1 1 
ATOM   2660 O  OD2 . ASP B 2 94  ? 3.796   -5.593  26.330 1.00 72.90  ? 177 ASP B OD2 1 
ATOM   2661 N  N   . LEU B 2 95  ? -1.082  -5.466  27.884 1.00 64.47  ? 178 LEU B N   1 
ATOM   2662 C  CA  . LEU B 2 95  ? -2.536  -5.434  27.773 1.00 61.36  ? 178 LEU B CA  1 
ATOM   2663 C  C   . LEU B 2 95  ? -3.227  -4.642  28.873 1.00 67.66  ? 178 LEU B C   1 
ATOM   2664 O  O   . LEU B 2 95  ? -4.220  -3.963  28.601 1.00 72.40  ? 178 LEU B O   1 
ATOM   2665 C  CB  . LEU B 2 95  ? -3.092  -6.865  27.762 1.00 59.02  ? 178 LEU B CB  1 
ATOM   2666 C  CG  . LEU B 2 95  ? -2.691  -7.764  26.591 1.00 57.98  ? 178 LEU B CG  1 
ATOM   2667 C  CD1 . LEU B 2 95  ? -3.279  -9.159  26.757 1.00 59.90  ? 178 LEU B CD1 1 
ATOM   2668 C  CD2 . LEU B 2 95  ? -3.129  -7.153  25.273 1.00 55.19  ? 178 LEU B CD2 1 
ATOM   2669 N  N   . LEU B 2 96  ? -2.741  -4.708  30.113 1.00 61.86  ? 179 LEU B N   1 
ATOM   2670 C  CA  . LEU B 2 96  ? -3.463  -4.140  31.247 1.00 58.05  ? 179 LEU B CA  1 
ATOM   2671 C  C   . LEU B 2 96  ? -2.986  -2.735  31.607 1.00 57.26  ? 179 LEU B C   1 
ATOM   2672 O  O   . LEU B 2 96  ? -3.749  -1.772  31.496 1.00 66.94  ? 179 LEU B O   1 
ATOM   2673 C  CB  . LEU B 2 96  ? -3.354  -5.076  32.459 1.00 65.99  ? 179 LEU B CB  1 
ATOM   2674 C  CG  . LEU B 2 96  ? -4.137  -6.390  32.344 1.00 68.00  ? 179 LEU B CG  1 
ATOM   2675 C  CD1 . LEU B 2 96  ? -4.328  -7.036  33.706 1.00 72.10  ? 179 LEU B CD1 1 
ATOM   2676 C  CD2 . LEU B 2 96  ? -5.480  -6.174  31.659 1.00 61.00  ? 179 LEU B CD2 1 
ATOM   2677 N  N   . GLN B 2 97  ? -1.733  -2.594  32.044 1.00 50.06  ? 180 GLN B N   1 
ATOM   2678 C  CA  . GLN B 2 97  ? -1.283  -1.291  32.520 1.00 56.59  ? 180 GLN B CA  1 
ATOM   2679 C  C   . GLN B 2 97  ? -1.032  -0.310  31.382 1.00 62.61  ? 180 GLN B C   1 
ATOM   2680 O  O   . GLN B 2 97  ? -1.006  0.902   31.619 1.00 71.40  ? 180 GLN B O   1 
ATOM   2681 C  CB  . GLN B 2 97  ? -0.031  -1.445  33.383 1.00 62.24  ? 180 GLN B CB  1 
ATOM   2682 C  CG  . GLN B 2 97  ? 1.257   -1.653  32.619 1.00 68.59  ? 180 GLN B CG  1 
ATOM   2683 C  CD  . GLN B 2 97  ? 2.465   -1.681  33.537 1.00 81.01  ? 180 GLN B CD  1 
ATOM   2684 O  OE1 . GLN B 2 97  ? 2.367   -1.357  34.723 1.00 77.54  ? 180 GLN B OE1 1 
ATOM   2685 N  NE2 . GLN B 2 97  ? 3.611   -2.078  32.996 1.00 89.91  ? 180 GLN B NE2 1 
ATOM   2686 N  N   . LYS B 2 98  ? -0.851  -0.800  30.156 1.00 60.32  ? 181 LYS B N   1 
ATOM   2687 C  CA  . LYS B 2 98  ? -0.815  0.101   29.011 1.00 59.20  ? 181 LYS B CA  1 
ATOM   2688 C  C   . LYS B 2 98  ? -2.187  0.705   28.743 1.00 66.68  ? 181 LYS B C   1 
ATOM   2689 O  O   . LYS B 2 98  ? -2.283  1.862   28.319 1.00 77.25  ? 181 LYS B O   1 
ATOM   2690 C  CB  . LYS B 2 98  ? -0.301  -0.642  27.778 1.00 65.63  ? 181 LYS B CB  1 
ATOM   2691 C  CG  . LYS B 2 98  ? 0.024   0.250   26.595 1.00 67.44  ? 181 LYS B CG  1 
ATOM   2692 C  CD  . LYS B 2 98  ? 0.952   -0.457  25.615 1.00 75.35  ? 181 LYS B CD  1 
ATOM   2693 C  CE  . LYS B 2 98  ? 2.272   -0.842  26.275 1.00 73.39  ? 181 LYS B CE  1 
ATOM   2694 N  NZ  . LYS B 2 98  ? 3.231   -1.445  25.307 1.00 68.00  ? 181 LYS B NZ  1 
ATOM   2695 N  N   . ALA B 2 99  ? -3.258  -0.057  28.987 1.00 62.39  ? 182 ALA B N   1 
ATOM   2696 C  CA  . ALA B 2 99  ? -4.601  0.495   28.859 1.00 60.52  ? 182 ALA B CA  1 
ATOM   2697 C  C   . ALA B 2 99  ? -4.938  1.418   30.020 1.00 60.82  ? 182 ALA B C   1 
ATOM   2698 O  O   . ALA B 2 99  ? -5.716  2.364   29.853 1.00 61.63  ? 182 ALA B O   1 
ATOM   2699 C  CB  . ALA B 2 99  ? -5.628  -0.631  28.762 1.00 59.64  ? 182 ALA B CB  1 
ATOM   2700 N  N   . GLU B 2 100 ? -4.371  1.158   31.199 1.00 60.23  ? 183 GLU B N   1 
ATOM   2701 C  CA  . GLU B 2 100 ? -4.563  2.066   32.324 1.00 63.57  ? 183 GLU B CA  1 
ATOM   2702 C  C   . GLU B 2 100 ? -3.930  3.423   32.046 1.00 64.37  ? 183 GLU B C   1 
ATOM   2703 O  O   . GLU B 2 100 ? -4.494  4.464   32.403 1.00 61.61  ? 183 GLU B O   1 
ATOM   2704 C  CB  . GLU B 2 100 ? -3.985  1.450   33.597 1.00 65.16  ? 183 GLU B CB  1 
ATOM   2705 C  CG  . GLU B 2 100 ? -4.153  2.316   34.828 1.00 79.40  ? 183 GLU B CG  1 
ATOM   2706 C  CD  . GLU B 2 100 ? -3.091  2.050   35.872 1.00 90.50  ? 183 GLU B CD  1 
ATOM   2707 O  OE1 . GLU B 2 100 ? -2.119  1.328   35.562 1.00 96.06  ? 183 GLU B OE1 1 
ATOM   2708 O  OE2 . GLU B 2 100 ? -3.225  2.564   37.002 1.00 95.00  ? 183 GLU B OE2 1 
ATOM   2709 N  N   . VAL B 2 101 ? -2.758  3.429   31.406 1.00 64.65  ? 184 VAL B N   1 
ATOM   2710 C  CA  . VAL B 2 101 ? -2.121  4.687   31.030 1.00 61.64  ? 184 VAL B CA  1 
ATOM   2711 C  C   . VAL B 2 101 ? -2.937  5.396   29.957 1.00 60.25  ? 184 VAL B C   1 
ATOM   2712 O  O   . VAL B 2 101 ? -3.126  6.618   30.006 1.00 54.30  ? 184 VAL B O   1 
ATOM   2713 C  CB  . VAL B 2 101 ? -0.672  4.430   30.574 1.00 49.89  ? 184 VAL B CB  1 
ATOM   2714 C  CG1 . VAL B 2 101 ? -0.104  5.650   29.869 1.00 44.35  ? 184 VAL B CG1 1 
ATOM   2715 C  CG2 . VAL B 2 101 ? 0.193   4.049   31.762 1.00 48.58  ? 184 VAL B CG2 1 
ATOM   2716 N  N   . HIS B 2 102 ? -3.439  4.640   28.976 1.00 55.95  ? 185 HIS B N   1 
ATOM   2717 C  CA  . HIS B 2 102 ? -4.284  5.223   27.939 1.00 56.61  ? 185 HIS B CA  1 
ATOM   2718 C  C   . HIS B 2 102 ? -5.503  5.911   28.541 1.00 61.24  ? 185 HIS B C   1 
ATOM   2719 O  O   . HIS B 2 102 ? -5.883  7.006   28.110 1.00 63.25  ? 185 HIS B O   1 
ATOM   2720 C  CB  . HIS B 2 102 ? -4.719  4.140   26.953 1.00 61.08  ? 185 HIS B CB  1 
ATOM   2721 C  CG  . HIS B 2 102 ? -3.792  3.973   25.790 1.00 62.62  ? 185 HIS B CG  1 
ATOM   2722 N  ND1 . HIS B 2 102 ? -4.110  3.209   24.688 1.00 58.04  ? 185 HIS B ND1 1 
ATOM   2723 C  CD2 . HIS B 2 102 ? -2.556  4.475   25.556 1.00 55.51  ? 185 HIS B CD2 1 
ATOM   2724 C  CE1 . HIS B 2 102 ? -3.111  3.247   23.825 1.00 52.73  ? 185 HIS B CE1 1 
ATOM   2725 N  NE2 . HIS B 2 102 ? -2.156  4.009   24.328 1.00 50.96  ? 185 HIS B NE2 1 
ATOM   2726 N  N   . SER B 2 103 ? -6.123  5.286   29.544 1.00 60.58  ? 186 SER B N   1 
ATOM   2727 C  CA  . SER B 2 103 ? -7.303  5.875   30.167 1.00 59.58  ? 186 SER B CA  1 
ATOM   2728 C  C   . SER B 2 103 ? -6.952  7.138   30.944 1.00 61.49  ? 186 SER B C   1 
ATOM   2729 O  O   . SER B 2 103 ? -7.722  8.106   30.943 1.00 64.89  ? 186 SER B O   1 
ATOM   2730 C  CB  . SER B 2 103 ? -7.976  4.852   31.081 1.00 61.21  ? 186 SER B CB  1 
ATOM   2731 O  OG  . SER B 2 103 ? -9.023  5.446   31.829 1.00 67.81  ? 186 SER B OG  1 
ATOM   2732 N  N   . ASP B 2 104 ? -5.795  7.149   31.614 1.00 59.84  ? 187 ASP B N   1 
ATOM   2733 C  CA  . ASP B 2 104 ? -5.425  8.303   32.429 1.00 66.47  ? 187 ASP B CA  1 
ATOM   2734 C  C   . ASP B 2 104 ? -5.086  9.515   31.576 1.00 69.84  ? 187 ASP B C   1 
ATOM   2735 O  O   . ASP B 2 104 ? -5.335  10.652  31.992 1.00 74.96  ? 187 ASP B O   1 
ATOM   2736 C  CB  . ASP B 2 104 ? -4.240  7.961   33.332 1.00 71.77  ? 187 ASP B CB  1 
ATOM   2737 C  CG  . ASP B 2 104 ? -4.608  6.999   34.436 1.00 86.87  ? 187 ASP B CG  1 
ATOM   2738 O  OD1 . ASP B 2 104 ? -3.706  6.286   34.921 1.00 91.90  ? 187 ASP B OD1 1 
ATOM   2739 O  OD2 . ASP B 2 104 ? -5.798  6.956   34.818 1.00 96.10  ? 187 ASP B OD2 1 
ATOM   2740 N  N   . LYS B 2 105 ? -4.520  9.296   30.391 1.00 69.93  ? 188 LYS B N   1 
ATOM   2741 C  CA  . LYS B 2 105 ? -4.088  10.390  29.533 1.00 67.51  ? 188 LYS B CA  1 
ATOM   2742 C  C   . LYS B 2 105 ? -5.170  10.864  28.572 1.00 64.82  ? 188 LYS B C   1 
ATOM   2743 O  O   . LYS B 2 105 ? -5.074  11.987  28.063 1.00 69.25  ? 188 LYS B O   1 
ATOM   2744 C  CB  . LYS B 2 105 ? -2.844  9.973   28.742 1.00 64.13  ? 188 LYS B CB  1 
ATOM   2745 C  CG  . LYS B 2 105 ? -1.644  9.638   29.618 1.00 62.22  ? 188 LYS B CG  1 
ATOM   2746 C  CD  . LYS B 2 105 ? -0.462  10.543  29.305 1.00 61.03  ? 188 LYS B CD  1 
ATOM   2747 C  CE  . LYS B 2 105 ? 0.735   10.239  30.198 1.00 68.35  ? 188 LYS B CE  1 
ATOM   2748 N  NZ  . LYS B 2 105 ? 0.733   11.042  31.455 1.00 78.26  ? 188 LYS B NZ  1 
ATOM   2749 N  N   . ALA B 2 106 ? -6.193  10.047  28.316 1.00 65.49  ? 189 ALA B N   1 
ATOM   2750 C  CA  . ALA B 2 106 ? -7.285  10.424  27.418 1.00 65.08  ? 189 ALA B CA  1 
ATOM   2751 C  C   . ALA B 2 106 ? -8.296  11.255  28.202 1.00 68.18  ? 189 ALA B C   1 
ATOM   2752 O  O   . ALA B 2 106 ? -9.332  10.771  28.666 1.00 73.75  ? 189 ALA B O   1 
ATOM   2753 C  CB  . ALA B 2 106 ? -7.929  9.189   26.801 1.00 64.59  ? 189 ALA B CB  1 
ATOM   2754 N  N   . ARG B 2 107 ? -7.982  12.539  28.346 1.00 64.22  ? 190 ARG B N   1 
ATOM   2755 C  CA  . ARG B 2 107 ? -8.802  13.480  29.090 1.00 63.33  ? 190 ARG B CA  1 
ATOM   2756 C  C   . ARG B 2 107 ? -8.793  14.823  28.368 1.00 69.54  ? 190 ARG B C   1 
ATOM   2757 O  O   . ARG B 2 107 ? -7.819  15.148  27.681 1.00 73.04  ? 190 ARG B O   1 
ATOM   2758 C  CB  . ARG B 2 107 ? -8.291  13.651  30.531 1.00 62.68  ? 190 ARG B CB  1 
ATOM   2759 C  CG  . ARG B 2 107 ? -6.853  14.123  30.639 1.00 52.45  ? 190 ARG B CG  1 
ATOM   2760 C  CD  . ARG B 2 107 ? -6.410  14.201  32.093 1.00 58.98  ? 190 ARG B CD  1 
ATOM   2761 N  NE  . ARG B 2 107 ? -5.230  15.045  32.259 1.00 64.95  ? 190 ARG B NE  1 
ATOM   2762 C  CZ  . ARG B 2 107 ? -4.676  15.334  33.431 1.00 70.68  ? 190 ARG B CZ  1 
ATOM   2763 N  NH1 . ARG B 2 107 ? -3.605  16.115  33.487 1.00 68.65  ? 190 ARG B NH1 1 
ATOM   2764 N  NH2 . ARG B 2 107 ? -5.193  14.843  34.549 1.00 81.71  ? 190 ARG B NH2 1 
ATOM   2765 N  N   . PRO B 2 108 ? -9.869  15.619  28.502 1.00 65.68  ? 191 PRO B N   1 
ATOM   2766 C  CA  . PRO B 2 108 ? -11.078 15.384  29.299 1.00 61.63  ? 191 PRO B CA  1 
ATOM   2767 C  C   . PRO B 2 108 ? -12.062 14.451  28.607 1.00 64.18  ? 191 PRO B C   1 
ATOM   2768 O  O   . PRO B 2 108 ? -11.998 14.286  27.391 1.00 70.32  ? 191 PRO B O   1 
ATOM   2769 C  CB  . PRO B 2 108 ? -11.687 16.788  29.449 1.00 61.68  ? 191 PRO B CB  1 
ATOM   2770 C  CG  . PRO B 2 108 ? -10.830 17.718  28.623 1.00 59.34  ? 191 PRO B CG  1 
ATOM   2771 C  CD  . PRO B 2 108 ? -9.971  16.873  27.742 1.00 63.90  ? 191 PRO B CD  1 
ATOM   2772 N  N   . THR B 2 109 ? -12.968 13.856  29.374 1.00 62.82  ? 192 THR B N   1 
ATOM   2773 C  CA  . THR B 2 109 ? -13.945 12.909  28.841 1.00 62.55  ? 192 THR B CA  1 
ATOM   2774 C  C   . THR B 2 109 ? -15.335 13.306  29.312 1.00 65.75  ? 192 THR B C   1 
ATOM   2775 O  O   . THR B 2 109 ? -15.647 13.143  30.510 1.00 70.45  ? 192 THR B O   1 
ATOM   2776 C  CB  . THR B 2 109 ? -13.618 11.483  29.274 1.00 64.11  ? 192 THR B CB  1 
ATOM   2777 O  OG1 . THR B 2 109 ? -12.274 11.164  28.889 1.00 65.47  ? 192 THR B OG1 1 
ATOM   2778 C  CG2 . THR B 2 109 ? -14.577 10.503  28.619 1.00 56.08  ? 192 THR B CG2 1 
ATOM   2779 N  N   . PRO B 2 110 ? -16.204 13.825  28.428 1.00 68.79  ? 193 PRO B N   1 
ATOM   2780 C  CA  . PRO B 2 110 ? -16.002 14.082  26.994 1.00 69.16  ? 193 PRO B CA  1 
ATOM   2781 C  C   . PRO B 2 110 ? -15.004 15.214  26.726 1.00 71.26  ? 193 PRO B C   1 
ATOM   2782 O  O   . PRO B 2 110 ? -14.694 15.962  27.651 1.00 75.44  ? 193 PRO B O   1 
ATOM   2783 C  CB  . PRO B 2 110 ? -17.409 14.464  26.513 1.00 70.16  ? 193 PRO B CB  1 
ATOM   2784 C  CG  . PRO B 2 110 ? -18.080 15.004  27.714 1.00 62.84  ? 193 PRO B CG  1 
ATOM   2785 C  CD  . PRO B 2 110 ? -17.563 14.192  28.861 1.00 62.20  ? 193 PRO B CD  1 
ATOM   2786 N  N   . PRO B 2 111 ? -14.507 15.341  25.482 1.00 70.52  ? 194 PRO B N   1 
ATOM   2787 C  CA  . PRO B 2 111 ? -14.816 14.540  24.294 1.00 68.32  ? 194 PRO B CA  1 
ATOM   2788 C  C   . PRO B 2 111 ? -13.823 13.420  23.999 1.00 65.95  ? 194 PRO B C   1 
ATOM   2789 O  O   . PRO B 2 111 ? -14.056 12.645  23.072 1.00 75.88  ? 194 PRO B O   1 
ATOM   2790 C  CB  . PRO B 2 111 ? -14.772 15.578  23.179 1.00 72.36  ? 194 PRO B CB  1 
ATOM   2791 C  CG  . PRO B 2 111 ? -13.672 16.500  23.614 1.00 66.22  ? 194 PRO B CG  1 
ATOM   2792 C  CD  . PRO B 2 111 ? -13.675 16.507  25.133 1.00 66.20  ? 194 PRO B CD  1 
ATOM   2793 N  N   . VAL B 2 112 ? -12.735 13.337  24.758 1.00 63.65  ? 195 VAL B N   1 
ATOM   2794 C  CA  . VAL B 2 112 ? -11.670 12.386  24.454 1.00 62.53  ? 195 VAL B CA  1 
ATOM   2795 C  C   . VAL B 2 112 ? -12.056 11.007  24.975 1.00 61.17  ? 195 VAL B C   1 
ATOM   2796 O  O   . VAL B 2 112 ? -12.261 10.819  26.179 1.00 62.16  ? 195 VAL B O   1 
ATOM   2797 C  CB  . VAL B 2 112 ? -10.329 12.844  25.044 1.00 60.20  ? 195 VAL B CB  1 
ATOM   2798 C  CG1 . VAL B 2 112 ? -9.187  12.071  24.409 1.00 54.98  ? 195 VAL B CG1 1 
ATOM   2799 C  CG2 . VAL B 2 112 ? -10.142 14.340  24.833 1.00 58.06  ? 195 VAL B CG2 1 
ATOM   2800 N  N   . PHE B 2 113 ? -12.158 10.043  24.066 1.00 59.89  ? 196 PHE B N   1 
ATOM   2801 C  CA  . PHE B 2 113 ? -12.402 8.647   24.392 1.00 60.78  ? 196 PHE B CA  1 
ATOM   2802 C  C   . PHE B 2 113 ? -11.277 7.793   23.824 1.00 62.46  ? 196 PHE B C   1 
ATOM   2803 O  O   . PHE B 2 113 ? -10.481 8.240   22.995 1.00 69.00  ? 196 PHE B O   1 
ATOM   2804 C  CB  . PHE B 2 113 ? -13.750 8.171   23.839 1.00 59.74  ? 196 PHE B CB  1 
ATOM   2805 C  CG  . PHE B 2 113 ? -14.935 8.838   24.465 1.00 49.36  ? 196 PHE B CG  1 
ATOM   2806 C  CD1 . PHE B 2 113 ? -15.494 8.340   25.630 1.00 50.71  ? 196 PHE B CD1 1 
ATOM   2807 C  CD2 . PHE B 2 113 ? -15.502 9.958   23.883 1.00 57.70  ? 196 PHE B CD2 1 
ATOM   2808 C  CE1 . PHE B 2 113 ? -16.595 8.951   26.204 1.00 53.46  ? 196 PHE B CE1 1 
ATOM   2809 C  CE2 . PHE B 2 113 ? -16.603 10.574  24.453 1.00 54.69  ? 196 PHE B CE2 1 
ATOM   2810 C  CZ  . PHE B 2 113 ? -17.148 10.070  25.614 1.00 54.85  ? 196 PHE B CZ  1 
ATOM   2811 N  N   . VAL B 2 114 ? -11.217 6.545   24.276 1.00 60.49  ? 197 VAL B N   1 
ATOM   2812 C  CA  . VAL B 2 114 ? -10.206 5.603   23.812 1.00 65.95  ? 197 VAL B CA  1 
ATOM   2813 C  C   . VAL B 2 114 ? -10.852 4.231   23.670 1.00 72.25  ? 197 VAL B C   1 
ATOM   2814 O  O   . VAL B 2 114 ? -11.667 3.826   24.506 1.00 74.07  ? 197 VAL B O   1 
ATOM   2815 C  CB  . VAL B 2 114 ? -8.987  5.568   24.761 1.00 65.99  ? 197 VAL B CB  1 
ATOM   2816 C  CG1 . VAL B 2 114 ? -9.428  5.389   26.204 1.00 72.04  ? 197 VAL B CG1 1 
ATOM   2817 C  CG2 . VAL B 2 114 ? -8.006  4.479   24.349 1.00 63.36  ? 197 VAL B CG2 1 
ATOM   2818 N  N   . GLU B 2 115 ? -10.508 3.527   22.591 1.00 68.27  ? 198 GLU B N   1 
ATOM   2819 C  CA  . GLU B 2 115 ? -11.048 2.204   22.314 1.00 62.41  ? 198 GLU B CA  1 
ATOM   2820 C  C   . GLU B 2 115 ? -9.917  1.221   22.060 1.00 64.59  ? 198 GLU B C   1 
ATOM   2821 O  O   . GLU B 2 115 ? -8.897  1.574   21.462 1.00 70.83  ? 198 GLU B O   1 
ATOM   2822 C  CB  . GLU B 2 115 ? -11.987 2.228   21.111 1.00 61.70  ? 198 GLU B CB  1 
ATOM   2823 C  CG  . GLU B 2 115 ? -13.255 3.018   21.340 1.00 67.66  ? 198 GLU B CG  1 
ATOM   2824 C  CD  . GLU B 2 115 ? -14.118 3.082   20.099 1.00 74.88  ? 198 GLU B CD  1 
ATOM   2825 O  OE1 . GLU B 2 115 ? -13.683 2.561   19.051 1.00 74.48  ? 198 GLU B OE1 1 
ATOM   2826 O  OE2 . GLU B 2 115 ? -15.223 3.663   20.166 1.00 79.17  ? 198 GLU B OE2 1 
ATOM   2827 N  N   . TRP B 2 116 ? -10.107 -0.014  22.520 1.00 61.89  ? 199 TRP B N   1 
ATOM   2828 C  CA  . TRP B 2 116 ? -9.156  -1.099  22.316 1.00 58.76  ? 199 TRP B CA  1 
ATOM   2829 C  C   . TRP B 2 116 ? -9.854  -2.203  21.537 1.00 66.77  ? 199 TRP B C   1 
ATOM   2830 O  O   . TRP B 2 116 ? -10.837 -2.779  22.017 1.00 75.54  ? 199 TRP B O   1 
ATOM   2831 C  CB  . TRP B 2 116 ? -8.626  -1.628  23.652 1.00 58.13  ? 199 TRP B CB  1 
ATOM   2832 C  CG  . TRP B 2 116 ? -7.473  -0.840  24.196 1.00 57.29  ? 199 TRP B CG  1 
ATOM   2833 C  CD1 . TRP B 2 116 ? -7.419  0.511   24.385 1.00 54.79  ? 199 TRP B CD1 1 
ATOM   2834 C  CD2 . TRP B 2 116 ? -6.204  -1.355  24.620 1.00 59.56  ? 199 TRP B CD2 1 
ATOM   2835 N  NE1 . TRP B 2 116 ? -6.195  0.869   24.899 1.00 47.43  ? 199 TRP B NE1 1 
ATOM   2836 C  CE2 . TRP B 2 116 ? -5.431  -0.258  25.052 1.00 57.08  ? 199 TRP B CE2 1 
ATOM   2837 C  CE3 . TRP B 2 116 ? -5.647  -2.637  24.674 1.00 58.44  ? 199 TRP B CE3 1 
ATOM   2838 C  CZ2 . TRP B 2 116 ? -4.130  -0.403  25.530 1.00 62.45  ? 199 TRP B CZ2 1 
ATOM   2839 C  CZ3 . TRP B 2 116 ? -4.354  -2.779  25.151 1.00 59.15  ? 199 TRP B CZ3 1 
ATOM   2840 C  CH2 . TRP B 2 116 ? -3.611  -1.669  25.573 1.00 61.44  ? 199 TRP B CH2 1 
ATOM   2841 N  N   . HIS B 2 117 ? -9.354  -2.491  20.339 1.00 62.50  ? 200 HIS B N   1 
ATOM   2842 C  CA  . HIS B 2 117 ? -9.953  -3.479  19.451 1.00 64.87  ? 200 HIS B CA  1 
ATOM   2843 C  C   . HIS B 2 117 ? -9.102  -4.741  19.439 1.00 66.76  ? 200 HIS B C   1 
ATOM   2844 O  O   . HIS B 2 117 ? -7.903  -4.686  19.147 1.00 66.04  ? 200 HIS B O   1 
ATOM   2845 C  CB  . HIS B 2 117 ? -10.104 -2.920  18.036 1.00 61.24  ? 200 HIS B CB  1 
ATOM   2846 C  CG  . HIS B 2 117 ? -11.113 -1.821  17.932 1.00 58.53  ? 200 HIS B CG  1 
ATOM   2847 N  ND1 . HIS B 2 117 ? -10.829 -0.517  18.279 1.00 58.17  ? 200 HIS B ND1 1 
ATOM   2848 C  CD2 . HIS B 2 117 ? -12.407 -1.831  17.534 1.00 63.05  ? 200 HIS B CD2 1 
ATOM   2849 C  CE1 . HIS B 2 117 ? -11.903 0.229   18.093 1.00 63.38  ? 200 HIS B CE1 1 
ATOM   2850 N  NE2 . HIS B 2 117 ? -12.874 -0.544  17.642 1.00 66.55  ? 200 HIS B NE2 1 
ATOM   2851 N  N   . PHE B 2 118 ? -9.728  -5.872  19.748 1.00 68.09  ? 201 PHE B N   1 
ATOM   2852 C  CA  . PHE B 2 118 ? -9.047  -7.154  19.853 1.00 63.16  ? 201 PHE B CA  1 
ATOM   2853 C  C   . PHE B 2 118 ? -9.447  -8.048  18.689 1.00 64.70  ? 201 PHE B C   1 
ATOM   2854 O  O   . PHE B 2 118 ? -10.637 -8.195  18.391 1.00 68.39  ? 201 PHE B O   1 
ATOM   2855 C  CB  . PHE B 2 118 ? -9.376  -7.837  21.181 1.00 60.99  ? 201 PHE B CB  1 
ATOM   2856 C  CG  . PHE B 2 118 ? -8.872  -7.094  22.383 1.00 60.68  ? 201 PHE B CG  1 
ATOM   2857 C  CD1 . PHE B 2 118 ? -7.590  -7.314  22.861 1.00 56.08  ? 201 PHE B CD1 1 
ATOM   2858 C  CD2 . PHE B 2 118 ? -9.679  -6.176  23.034 1.00 59.45  ? 201 PHE B CD2 1 
ATOM   2859 C  CE1 . PHE B 2 118 ? -7.122  -6.634  23.970 1.00 56.23  ? 201 PHE B CE1 1 
ATOM   2860 C  CE2 . PHE B 2 118 ? -9.217  -5.489  24.144 1.00 54.57  ? 201 PHE B CE2 1 
ATOM   2861 C  CZ  . PHE B 2 118 ? -7.938  -5.718  24.612 1.00 55.21  ? 201 PHE B CZ  1 
ATOM   2862 N  N   . LEU B 2 119 ? -8.449  -8.645  18.036 1.00 61.34  ? 202 LEU B N   1 
ATOM   2863 C  CA  . LEU B 2 119 ? -8.732  -9.590  16.963 1.00 60.39  ? 202 LEU B CA  1 
ATOM   2864 C  C   . LEU B 2 119 ? -9.327  -10.886 17.500 1.00 63.67  ? 202 LEU B C   1 
ATOM   2865 O  O   . LEU B 2 119 ? -10.150 -11.515 16.825 1.00 71.05  ? 202 LEU B O   1 
ATOM   2866 C  CB  . LEU B 2 119 ? -7.452  -9.874  16.173 1.00 58.40  ? 202 LEU B CB  1 
ATOM   2867 C  CG  . LEU B 2 119 ? -7.426  -11.096 15.251 1.00 63.74  ? 202 LEU B CG  1 
ATOM   2868 C  CD1 . LEU B 2 119 ? -8.424  -10.947 14.106 1.00 66.78  ? 202 LEU B CD1 1 
ATOM   2869 C  CD2 . LEU B 2 119 ? -6.023  -11.329 14.719 1.00 62.03  ? 202 LEU B CD2 1 
ATOM   2870 N  N   . GLN B 2 120 ? -8.939  -11.290 18.706 1.00 63.09  ? 203 GLN B N   1 
ATOM   2871 C  CA  . GLN B 2 120 ? -9.333  -12.568 19.282 1.00 69.37  ? 203 GLN B CA  1 
ATOM   2872 C  C   . GLN B 2 120 ? -10.372 -12.351 20.372 1.00 74.66  ? 203 GLN B C   1 
ATOM   2873 O  O   . GLN B 2 120 ? -10.213 -11.466 21.220 1.00 73.18  ? 203 GLN B O   1 
ATOM   2874 C  CB  . GLN B 2 120 ? -8.116  -13.303 19.846 1.00 69.16  ? 203 GLN B CB  1 
ATOM   2875 C  CG  . GLN B 2 120 ? -7.158  -13.812 18.779 1.00 69.73  ? 203 GLN B CG  1 
ATOM   2876 C  CD  . GLN B 2 120 ? -5.702  -13.603 19.146 1.00 66.87  ? 203 GLN B CD  1 
ATOM   2877 O  OE1 . GLN B 2 120 ? -5.351  -13.512 20.321 1.00 64.37  ? 203 GLN B OE1 1 
ATOM   2878 N  NE2 . GLN B 2 120 ? -4.845  -13.527 18.137 1.00 67.76  ? 203 GLN B NE2 1 
ATOM   2879 N  N   . ARG B 2 121 ? -11.432 -13.165 20.347 1.00 80.11  ? 204 ARG B N   1 
ATOM   2880 C  CA  . ARG B 2 121 ? -12.486 -13.041 21.351 1.00 84.07  ? 204 ARG B CA  1 
ATOM   2881 C  C   . ARG B 2 121 ? -11.969 -13.377 22.743 1.00 80.68  ? 204 ARG B C   1 
ATOM   2882 O  O   . ARG B 2 121 ? -12.295 -12.689 23.717 1.00 78.72  ? 204 ARG B O   1 
ATOM   2883 C  CB  . ARG B 2 121 ? -13.664 -13.946 20.992 1.00 96.07  ? 204 ARG B CB  1 
ATOM   2884 C  CG  . ARG B 2 121 ? -14.982 -13.516 21.616 1.00 108.68 ? 204 ARG B CG  1 
ATOM   2885 C  CD  . ARG B 2 121 ? -15.800 -14.703 22.105 1.00 118.96 ? 204 ARG B CD  1 
ATOM   2886 N  NE  . ARG B 2 121 ? -15.120 -15.445 23.164 1.00 124.58 ? 204 ARG B NE  1 
ATOM   2887 C  CZ  . ARG B 2 121 ? -15.284 -16.745 23.391 1.00 128.74 ? 204 ARG B CZ  1 
ATOM   2888 N  NH1 . ARG B 2 121 ? -16.110 -17.450 22.632 1.00 131.57 ? 204 ARG B NH1 1 
ATOM   2889 N  NH2 . ARG B 2 121 ? -14.625 -17.339 24.377 1.00 128.98 ? 204 ARG B NH2 1 
ATOM   2890 N  N   . ILE B 2 122 ? -11.165 -14.437 22.854 1.00 82.41  ? 205 ILE B N   1 
ATOM   2891 C  CA  . ILE B 2 122 ? -10.675 -14.878 24.157 1.00 80.32  ? 205 ILE B CA  1 
ATOM   2892 C  C   . ILE B 2 122 ? -9.871  -13.771 24.828 1.00 71.95  ? 205 ILE B C   1 
ATOM   2893 O  O   . ILE B 2 122 ? -9.984  -13.549 26.040 1.00 67.77  ? 205 ILE B O   1 
ATOM   2894 C  CB  . ILE B 2 122 ? -9.855  -16.174 24.004 1.00 86.89  ? 205 ILE B CB  1 
ATOM   2895 C  CG1 . ILE B 2 122 ? -9.048  -16.461 25.270 1.00 89.11  ? 205 ILE B CG1 1 
ATOM   2896 C  CG2 . ILE B 2 122 ? -8.950  -16.094 22.785 1.00 90.71  ? 205 ILE B CG2 1 
ATOM   2897 C  CD1 . ILE B 2 122 ? -9.902  -16.847 26.460 1.00 101.16 ? 205 ILE B CD1 1 
ATOM   2898 N  N   . VAL B 2 123 ? -9.063  -13.048 24.051 1.00 73.53  ? 206 VAL B N   1 
ATOM   2899 C  CA  . VAL B 2 123 ? -8.298  -11.938 24.613 1.00 65.58  ? 206 VAL B CA  1 
ATOM   2900 C  C   . VAL B 2 123 ? -9.223  -10.784 24.976 1.00 70.66  ? 206 VAL B C   1 
ATOM   2901 O  O   . VAL B 2 123 ? -9.012  -10.093 25.980 1.00 72.51  ? 206 VAL B O   1 
ATOM   2902 C  CB  . VAL B 2 123 ? -7.198  -11.495 23.631 1.00 56.33  ? 206 VAL B CB  1 
ATOM   2903 C  CG1 . VAL B 2 123 ? -6.351  -10.394 24.244 1.00 53.72  ? 206 VAL B CG1 1 
ATOM   2904 C  CG2 . VAL B 2 123 ? -6.330  -12.677 23.243 1.00 56.40  ? 206 VAL B CG2 1 
ATOM   2905 N  N   . TYR B 2 124 ? -10.266 -10.561 24.172 1.00 74.91  ? 207 TYR B N   1 
ATOM   2906 C  CA  . TYR B 2 124 ? -11.186 -9.463  24.447 1.00 72.56  ? 207 TYR B CA  1 
ATOM   2907 C  C   . TYR B 2 124 ? -11.943 -9.683  25.749 1.00 73.14  ? 207 TYR B C   1 
ATOM   2908 O  O   . TYR B 2 124 ? -12.102 -8.751  26.544 1.00 77.21  ? 207 TYR B O   1 
ATOM   2909 C  CB  . TYR B 2 124 ? -12.170 -9.293  23.291 1.00 75.66  ? 207 TYR B CB  1 
ATOM   2910 C  CG  . TYR B 2 124 ? -13.499 -8.707  23.716 1.00 82.93  ? 207 TYR B CG  1 
ATOM   2911 C  CD1 . TYR B 2 124 ? -13.621 -7.355  24.010 1.00 84.22  ? 207 TYR B CD1 1 
ATOM   2912 C  CD2 . TYR B 2 124 ? -14.631 -9.507  23.829 1.00 87.36  ? 207 TYR B CD2 1 
ATOM   2913 C  CE1 . TYR B 2 124 ? -14.831 -6.815  24.402 1.00 87.15  ? 207 TYR B CE1 1 
ATOM   2914 C  CE2 . TYR B 2 124 ? -15.846 -8.975  24.221 1.00 88.27  ? 207 TYR B CE2 1 
ATOM   2915 C  CZ  . TYR B 2 124 ? -15.940 -7.629  24.506 1.00 87.16  ? 207 TYR B CZ  1 
ATOM   2916 O  OH  . TYR B 2 124 ? -17.145 -7.091  24.895 1.00 85.63  ? 207 TYR B OH  1 
ATOM   2917 N  N   . GLU B 2 125 ? -12.419 -10.907 25.984 1.00 72.52  ? 208 GLU B N   1 
ATOM   2918 C  CA  . GLU B 2 125 ? -13.256 -11.151 27.153 1.00 75.54  ? 208 GLU B CA  1 
ATOM   2919 C  C   . GLU B 2 125 ? -12.473 -10.972 28.447 1.00 70.93  ? 208 GLU B C   1 
ATOM   2920 O  O   . GLU B 2 125 ? -13.013 -10.473 29.441 1.00 71.57  ? 208 GLU B O   1 
ATOM   2921 C  CB  . GLU B 2 125 ? -13.870 -12.547 27.077 1.00 80.08  ? 208 GLU B CB  1 
ATOM   2922 C  CG  . GLU B 2 125 ? -15.317 -12.545 26.626 1.00 92.39  ? 208 GLU B CG  1 
ATOM   2923 C  CD  . GLU B 2 125 ? -15.675 -13.771 25.818 1.00 107.64 ? 208 GLU B CD  1 
ATOM   2924 O  OE1 . GLU B 2 125 ? -14.955 -14.786 25.929 1.00 111.77 ? 208 GLU B OE1 1 
ATOM   2925 O  OE2 . GLU B 2 125 ? -16.675 -13.720 25.072 1.00 115.67 ? 208 GLU B OE2 1 
ATOM   2926 N  N   . TYR B 2 126 ? -11.198 -11.363 28.455 1.00 66.44  ? 209 TYR B N   1 
ATOM   2927 C  CA  . TYR B 2 126 ? -10.388 -11.174 29.654 1.00 66.51  ? 209 TYR B CA  1 
ATOM   2928 C  C   . TYR B 2 126 ? -10.116 -9.697  29.904 1.00 70.45  ? 209 TYR B C   1 
ATOM   2929 O  O   . TYR B 2 126 ? -10.371 -9.186  31.000 1.00 76.76  ? 209 TYR B O   1 
ATOM   2930 C  CB  . TYR B 2 126 ? -9.072  -11.944 29.538 1.00 63.96  ? 209 TYR B CB  1 
ATOM   2931 C  CG  . TYR B 2 126 ? -8.094  -11.606 30.641 1.00 65.21  ? 209 TYR B CG  1 
ATOM   2932 C  CD1 . TYR B 2 126 ? -7.041  -10.728 30.418 1.00 64.17  ? 209 TYR B CD1 1 
ATOM   2933 C  CD2 . TYR B 2 126 ? -8.235  -12.150 31.910 1.00 66.07  ? 209 TYR B CD2 1 
ATOM   2934 C  CE1 . TYR B 2 126 ? -6.150  -10.411 31.424 1.00 64.50  ? 209 TYR B CE1 1 
ATOM   2935 C  CE2 . TYR B 2 126 ? -7.349  -11.838 32.924 1.00 66.66  ? 209 TYR B CE2 1 
ATOM   2936 C  CZ  . TYR B 2 126 ? -6.308  -10.968 32.675 1.00 67.56  ? 209 TYR B CZ  1 
ATOM   2937 O  OH  . TYR B 2 126 ? -5.423  -10.656 33.682 1.00 71.45  ? 209 TYR B OH  1 
ATOM   2938 N  N   . CYS B 2 127 ? -9.603  -8.993  28.892 1.00 69.65  ? 210 CYS B N   1 
ATOM   2939 C  CA  . CYS B 2 127 ? -9.190  -7.606  29.086 1.00 68.28  ? 210 CYS B CA  1 
ATOM   2940 C  C   . CYS B 2 127 ? -10.376 -6.700  29.399 1.00 67.50  ? 210 CYS B C   1 
ATOM   2941 O  O   . CYS B 2 127 ? -10.289 -5.847  30.290 1.00 65.41  ? 210 CYS B O   1 
ATOM   2942 C  CB  . CYS B 2 127 ? -8.443  -7.107  27.850 1.00 66.60  ? 210 CYS B CB  1 
ATOM   2943 S  SG  . CYS B 2 127 ? -6.836  -7.894  27.581 1.00 65.92  ? 210 CYS B SG  1 
ATOM   2944 N  N   . ALA B 2 128 ? -11.491 -6.868  28.681 1.00 63.84  ? 211 ALA B N   1 
ATOM   2945 C  CA  . ALA B 2 128 ? -12.640 -5.991  28.884 1.00 58.91  ? 211 ALA B CA  1 
ATOM   2946 C  C   . ALA B 2 128 ? -13.160 -6.079  30.313 1.00 68.30  ? 211 ALA B C   1 
ATOM   2947 O  O   . ALA B 2 128 ? -13.575 -5.070  30.895 1.00 76.67  ? 211 ALA B O   1 
ATOM   2948 C  CB  . ALA B 2 128 ? -13.748 -6.332  27.888 1.00 54.96  ? 211 ALA B CB  1 
ATOM   2949 N  N   . ALA B 2 129 ? -13.145 -7.278  30.897 1.00 70.75  ? 212 ALA B N   1 
ATOM   2950 C  CA  . ALA B 2 129 ? -13.552 -7.414  32.290 1.00 70.14  ? 212 ALA B CA  1 
ATOM   2951 C  C   . ALA B 2 129 ? -12.519 -6.812  33.233 1.00 73.23  ? 212 ALA B C   1 
ATOM   2952 O  O   . ALA B 2 129 ? -12.882 -6.290  34.294 1.00 74.74  ? 212 ALA B O   1 
ATOM   2953 C  CB  . ALA B 2 129 ? -13.794 -8.885  32.625 1.00 66.71  ? 212 ALA B CB  1 
ATOM   2954 N  N   . GLU B 2 130 ? -11.235 -6.870  32.866 1.00 68.93  ? 213 GLU B N   1 
ATOM   2955 C  CA  . GLU B 2 130 ? -10.201 -6.245  33.685 1.00 68.37  ? 213 GLU B CA  1 
ATOM   2956 C  C   . GLU B 2 130 ? -10.351 -4.730  33.702 1.00 69.84  ? 213 GLU B C   1 
ATOM   2957 O  O   . GLU B 2 130 ? -10.161 -4.093  34.744 1.00 71.77  ? 213 GLU B O   1 
ATOM   2958 C  CB  . GLU B 2 130 ? -8.815  -6.632  33.172 1.00 71.46  ? 213 GLU B CB  1 
ATOM   2959 C  CG  . GLU B 2 130 ? -8.491  -8.105  33.308 1.00 79.13  ? 213 GLU B CG  1 
ATOM   2960 C  CD  . GLU B 2 130 ? -8.546  -8.576  34.743 1.00 84.27  ? 213 GLU B CD  1 
ATOM   2961 O  OE1 . GLU B 2 130 ? -7.961  -7.895  35.613 1.00 81.46  ? 213 GLU B OE1 1 
ATOM   2962 O  OE2 . GLU B 2 130 ? -9.179  -9.622  35.003 1.00 84.64  ? 213 GLU B OE2 1 
ATOM   2963 N  N   . TYR B 2 131 ? -10.685 -4.136  32.553 1.00 68.73  ? 214 TYR B N   1 
ATOM   2964 C  CA  . TYR B 2 131 ? -10.864 -2.690  32.490 1.00 61.78  ? 214 TYR B CA  1 
ATOM   2965 C  C   . TYR B 2 131 ? -12.073 -2.251  33.304 1.00 66.59  ? 214 TYR B C   1 
ATOM   2966 O  O   . TYR B 2 131 ? -12.054 -1.183  33.928 1.00 67.19  ? 214 TYR B O   1 
ATOM   2967 C  CB  . TYR B 2 131 ? -11.005 -2.243  31.036 1.00 55.13  ? 214 TYR B CB  1 
ATOM   2968 C  CG  . TYR B 2 131 ? -9.885  -2.711  30.137 1.00 53.16  ? 214 TYR B CG  1 
ATOM   2969 C  CD1 . TYR B 2 131 ? -8.602  -2.903  30.632 1.00 53.40  ? 214 TYR B CD1 1 
ATOM   2970 C  CD2 . TYR B 2 131 ? -10.109 -2.954  28.789 1.00 56.12  ? 214 TYR B CD2 1 
ATOM   2971 C  CE1 . TYR B 2 131 ? -7.576  -3.330  29.811 1.00 52.52  ? 214 TYR B CE1 1 
ATOM   2972 C  CE2 . TYR B 2 131 ? -9.089  -3.380  27.960 1.00 52.96  ? 214 TYR B CE2 1 
ATOM   2973 C  CZ  . TYR B 2 131 ? -7.824  -3.565  28.476 1.00 52.92  ? 214 TYR B CZ  1 
ATOM   2974 O  OH  . TYR B 2 131 ? -6.805  -3.988  27.653 1.00 56.58  ? 214 TYR B OH  1 
ATOM   2975 N  N   . LEU B 2 132 ? -13.136 -3.060  33.305 1.00 69.70  ? 215 LEU B N   1 
ATOM   2976 C  CA  . LEU B 2 132 ? -14.288 -2.768  34.150 1.00 76.18  ? 215 LEU B CA  1 
ATOM   2977 C  C   . LEU B 2 132 ? -13.912 -2.835  35.622 1.00 81.94  ? 215 LEU B C   1 
ATOM   2978 O  O   . LEU B 2 132 ? -14.404 -2.044  36.436 1.00 74.28  ? 215 LEU B O   1 
ATOM   2979 C  CB  . LEU B 2 132 ? -15.422 -3.746  33.845 1.00 81.21  ? 215 LEU B CB  1 
ATOM   2980 C  CG  . LEU B 2 132 ? -16.394 -3.353  32.734 1.00 84.69  ? 215 LEU B CG  1 
ATOM   2981 C  CD1 . LEU B 2 132 ? -17.106 -4.583  32.194 1.00 84.86  ? 215 LEU B CD1 1 
ATOM   2982 C  CD2 . LEU B 2 132 ? -17.394 -2.331  33.249 1.00 93.59  ? 215 LEU B CD2 1 
ATOM   2983 N  N   . ARG B 2 133 ? -13.035 -3.775  35.982 1.00 88.81  ? 216 ARG B N   1 
ATOM   2984 C  CA  . ARG B 2 133 ? -12.589 -3.886  37.365 1.00 88.41  ? 216 ARG B CA  1 
ATOM   2985 C  C   . ARG B 2 133 ? -11.744 -2.686  37.778 1.00 84.76  ? 216 ARG B C   1 
ATOM   2986 O  O   . ARG B 2 133 ? -11.791 -2.265  38.940 1.00 87.82  ? 216 ARG B O   1 
ATOM   2987 C  CB  . ARG B 2 133 ? -11.809 -5.187  37.553 1.00 88.27  ? 216 ARG B CB  1 
ATOM   2988 C  CG  . ARG B 2 133 ? -11.422 -5.485  38.988 1.00 94.07  ? 216 ARG B CG  1 
ATOM   2989 C  CD  . ARG B 2 133 ? -11.171 -6.968  39.183 1.00 101.44 ? 216 ARG B CD  1 
ATOM   2990 N  NE  . ARG B 2 133 ? -9.807  -7.238  39.625 1.00 107.10 ? 216 ARG B NE  1 
ATOM   2991 C  CZ  . ARG B 2 133 ? -8.891  -7.857  38.889 1.00 106.84 ? 216 ARG B CZ  1 
ATOM   2992 N  NH1 . ARG B 2 133 ? -9.193  -8.277  37.670 1.00 105.31 ? 216 ARG B NH1 1 
ATOM   2993 N  NH2 . ARG B 2 133 ? -7.674  -8.057  39.376 1.00 111.31 ? 216 ARG B NH2 1 
HETATM 2994 N  N   . MSE B 2 134 ? -10.980 -2.123  36.849 1.00 76.25  ? 217 MSE B N   1 
HETATM 2995 C  CA  . MSE B 2 134 ? -10.151 -0.962  37.139 1.00 76.59  ? 217 MSE B CA  1 
HETATM 2996 C  C   . MSE B 2 134 ? -10.939 0.333   36.974 1.00 77.79  ? 217 MSE B C   1 
HETATM 2997 O  O   . MSE B 2 134 ? -10.442 1.413   37.286 1.00 71.63  ? 217 MSE B O   1 
HETATM 2998 C  CB  . MSE B 2 134 ? -8.921  -0.945  36.234 1.00 74.86  ? 217 MSE B CB  1 
HETATM 2999 C  CG  . MSE B 2 134 ? -7.698  -1.595  36.847 1.00 81.39  ? 217 MSE B CG  1 
HETATM 3000 SE SE  . MSE B 2 134 ? -6.131  -1.457  35.701 0.50 85.09  ? 217 MSE B SE  1 
HETATM 3001 C  CE  . MSE B 2 134 ? -6.917  -2.088  34.041 1.00 72.02  ? 217 MSE B CE  1 
ATOM   3002 N  N   . GLY B 2 135 ? -12.164 0.216   36.474 1.00 78.59  ? 218 GLY B N   1 
ATOM   3003 C  CA  . GLY B 2 135 ? -13.029 1.373   36.320 1.00 76.65  ? 218 GLY B CA  1 
ATOM   3004 C  C   . GLY B 2 135 ? -12.592 2.358   35.257 1.00 73.17  ? 218 GLY B C   1 
ATOM   3005 O  O   . GLY B 2 135 ? -12.709 3.574   35.460 1.00 74.46  ? 218 GLY B O   1 
ATOM   3006 N  N   . LEU B 2 136 ? -12.086 1.866   34.125 1.00 66.51  ? 219 LEU B N   1 
ATOM   3007 C  CA  . LEU B 2 136 ? -11.685 2.728   33.013 1.00 65.77  ? 219 LEU B CA  1 
ATOM   3008 C  C   . LEU B 2 136 ? -12.934 3.081   32.210 1.00 74.10  ? 219 LEU B C   1 
ATOM   3009 O  O   . LEU B 2 136 ? -13.261 2.464   31.193 1.00 82.51  ? 219 LEU B O   1 
ATOM   3010 C  CB  . LEU B 2 136 ? -10.631 2.044   32.152 1.00 64.45  ? 219 LEU B CB  1 
ATOM   3011 C  CG  . LEU B 2 136 ? -9.477  1.371   32.899 1.00 63.54  ? 219 LEU B CG  1 
ATOM   3012 C  CD1 . LEU B 2 136 ? -8.521  0.706   31.920 1.00 59.29  ? 219 LEU B CD1 1 
ATOM   3013 C  CD2 . LEU B 2 136 ? -8.741  2.373   33.777 1.00 59.16  ? 219 LEU B CD2 1 
ATOM   3014 N  N   . ALA B 2 137 ? -13.644 4.108   32.687 1.00 74.04  ? 220 ALA B N   1 
ATOM   3015 C  CA  . ALA B 2 137 ? -14.925 4.471   32.089 1.00 68.03  ? 220 ALA B CA  1 
ATOM   3016 C  C   . ALA B 2 137 ? -14.766 5.033   30.683 1.00 72.17  ? 220 ALA B C   1 
ATOM   3017 O  O   . ALA B 2 137 ? -15.640 4.826   29.834 1.00 81.28  ? 220 ALA B O   1 
ATOM   3018 C  CB  . ALA B 2 137 ? -15.652 5.478   32.978 1.00 63.31  ? 220 ALA B CB  1 
ATOM   3019 N  N   . ASN B 2 138 ? -13.673 5.741   30.414 1.00 70.54  ? 221 ASN B N   1 
ATOM   3020 C  CA  . ASN B 2 138 ? -13.450 6.351   29.110 1.00 64.77  ? 221 ASN B CA  1 
ATOM   3021 C  C   . ASN B 2 138 ? -12.814 5.394   28.110 1.00 63.90  ? 221 ASN B C   1 
ATOM   3022 O  O   . ASN B 2 138 ? -12.465 5.819   27.003 1.00 64.70  ? 221 ASN B O   1 
ATOM   3023 C  CB  . ASN B 2 138 ? -12.584 7.607   29.254 1.00 64.10  ? 221 ASN B CB  1 
ATOM   3024 C  CG  . ASN B 2 138 ? -11.171 7.298   29.708 1.00 63.52  ? 221 ASN B CG  1 
ATOM   3025 O  OD1 . ASN B 2 138 ? -10.900 6.234   30.267 1.00 61.27  ? 221 ASN B OD1 1 
ATOM   3026 N  ND2 . ASN B 2 138 ? -10.260 8.236   29.473 1.00 61.90  ? 221 ASN B ND2 1 
ATOM   3027 N  N   . LEU B 2 139 ? -12.663 4.120   28.467 1.00 67.67  ? 222 LEU B N   1 
ATOM   3028 C  CA  . LEU B 2 139 ? -12.044 3.121   27.606 1.00 60.56  ? 222 LEU B CA  1 
ATOM   3029 C  C   . LEU B 2 139 ? -13.048 2.015   27.312 1.00 64.06  ? 222 LEU B C   1 
ATOM   3030 O  O   . LEU B 2 139 ? -13.609 1.420   28.238 1.00 75.08  ? 222 LEU B O   1 
ATOM   3031 C  CB  . LEU B 2 139 ? -10.784 2.541   28.258 1.00 55.48  ? 222 LEU B CB  1 
ATOM   3032 C  CG  . LEU B 2 139 ? -9.837  1.746   27.357 1.00 54.78  ? 222 LEU B CG  1 
ATOM   3033 C  CD1 . LEU B 2 139 ? -8.387  1.993   27.747 1.00 51.35  ? 222 LEU B CD1 1 
ATOM   3034 C  CD2 . LEU B 2 139 ? -10.157 0.259   27.412 1.00 54.10  ? 222 LEU B CD2 1 
ATOM   3035 N  N   . LYS B 2 140 ? -13.268 1.743   26.029 1.00 64.18  ? 223 LYS B N   1 
ATOM   3036 C  CA  . LYS B 2 140 ? -14.171 0.690   25.587 1.00 66.03  ? 223 LYS B CA  1 
ATOM   3037 C  C   . LYS B 2 140 ? -13.385 -0.372  24.832 1.00 67.97  ? 223 LYS B C   1 
ATOM   3038 O  O   . LYS B 2 140 ? -12.527 -0.049  24.006 1.00 74.95  ? 223 LYS B O   1 
ATOM   3039 C  CB  . LYS B 2 140 ? -15.281 1.248   24.692 1.00 66.70  ? 223 LYS B CB  1 
ATOM   3040 C  CG  . LYS B 2 140 ? -16.563 1.596   25.427 1.00 76.46  ? 223 LYS B CG  1 
ATOM   3041 C  CD  . LYS B 2 140 ? -17.572 2.239   24.488 1.00 83.13  ? 223 LYS B CD  1 
ATOM   3042 C  CE  . LYS B 2 140 ? -18.898 2.493   25.182 1.00 86.33  ? 223 LYS B CE  1 
ATOM   3043 N  NZ  . LYS B 2 140 ? -19.810 3.298   24.326 1.00 91.67  ? 223 LYS B NZ  1 
ATOM   3044 N  N   . ALA B 2 141 ? -13.681 -1.637  25.115 1.00 65.41  ? 224 ALA B N   1 
ATOM   3045 C  CA  . ALA B 2 141 ? -13.040 -2.760  24.447 1.00 62.93  ? 224 ALA B CA  1 
ATOM   3046 C  C   . ALA B 2 141 ? -14.017 -3.417  23.482 1.00 69.88  ? 224 ALA B C   1 
ATOM   3047 O  O   . ALA B 2 141 ? -15.220 -3.494  23.756 1.00 72.52  ? 224 ALA B O   1 
ATOM   3048 C  CB  . ALA B 2 141 ? -12.530 -3.787  25.461 1.00 60.02  ? 224 ALA B CB  1 
ATOM   3049 N  N   . PHE B 2 142 ? -13.495 -3.888  22.349 1.00 71.88  ? 225 PHE B N   1 
ATOM   3050 C  CA  . PHE B 2 142 ? -14.307 -4.529  21.325 1.00 73.31  ? 225 PHE B CA  1 
ATOM   3051 C  C   . PHE B 2 142 ? -13.599 -5.770  20.803 1.00 73.57  ? 225 PHE B C   1 
ATOM   3052 O  O   . PHE B 2 142 ? -12.368 -5.816  20.728 1.00 74.10  ? 225 PHE B O   1 
ATOM   3053 C  CB  . PHE B 2 142 ? -14.590 -3.592  20.141 1.00 71.31  ? 225 PHE B CB  1 
ATOM   3054 C  CG  . PHE B 2 142 ? -15.349 -2.354  20.508 1.00 76.96  ? 225 PHE B CG  1 
ATOM   3055 C  CD1 . PHE B 2 142 ? -16.730 -2.318  20.415 1.00 79.50  ? 225 PHE B CD1 1 
ATOM   3056 C  CD2 . PHE B 2 142 ? -14.680 -1.217  20.930 1.00 82.92  ? 225 PHE B CD2 1 
ATOM   3057 C  CE1 . PHE B 2 142 ? -17.432 -1.174  20.745 1.00 88.36  ? 225 PHE B CE1 1 
ATOM   3058 C  CE2 . PHE B 2 142 ? -15.375 -0.069  21.263 1.00 88.21  ? 225 PHE B CE2 1 
ATOM   3059 C  CZ  . PHE B 2 142 ? -16.753 -0.047  21.170 1.00 90.42  ? 225 PHE B CZ  1 
ATOM   3060 N  N   . TRP B 2 143 ? -14.394 -6.775  20.441 1.00 72.72  ? 226 TRP B N   1 
ATOM   3061 C  CA  . TRP B 2 143 ? -13.915 -7.900  19.641 1.00 68.62  ? 226 TRP B CA  1 
ATOM   3062 C  C   . TRP B 2 143 ? -14.197 -7.561  18.184 1.00 73.49  ? 226 TRP B C   1 
ATOM   3063 O  O   . TRP B 2 143 ? -15.317 -7.741  17.698 1.00 83.41  ? 226 TRP B O   1 
ATOM   3064 C  CB  . TRP B 2 143 ? -14.593 -9.202  20.047 1.00 65.26  ? 226 TRP B CB  1 
ATOM   3065 C  CG  . TRP B 2 143 ? -14.169 -10.367 19.202 1.00 63.71  ? 226 TRP B CG  1 
ATOM   3066 C  CD1 . TRP B 2 143 ? -12.937 -10.571 18.652 1.00 68.42  ? 226 TRP B CD1 1 
ATOM   3067 C  CD2 . TRP B 2 143 ? -14.975 -11.481 18.800 1.00 70.54  ? 226 TRP B CD2 1 
ATOM   3068 N  NE1 . TRP B 2 143 ? -12.923 -11.745 17.939 1.00 69.56  ? 226 TRP B NE1 1 
ATOM   3069 C  CE2 . TRP B 2 143 ? -14.162 -12.323 18.013 1.00 72.37  ? 226 TRP B CE2 1 
ATOM   3070 C  CE3 . TRP B 2 143 ? -16.305 -11.849 19.029 1.00 76.42  ? 226 TRP B CE3 1 
ATOM   3071 C  CZ2 . TRP B 2 143 ? -14.632 -13.511 17.460 1.00 71.79  ? 226 TRP B CZ2 1 
ATOM   3072 C  CZ3 . TRP B 2 143 ? -16.769 -13.032 18.481 1.00 77.11  ? 226 TRP B CZ3 1 
ATOM   3073 C  CH2 . TRP B 2 143 ? -15.935 -13.847 17.705 1.00 75.72  ? 226 TRP B CH2 1 
ATOM   3074 N  N   . ASN B 2 144 ? -13.181 -7.060  17.482 1.00 68.13  ? 227 ASN B N   1 
ATOM   3075 C  CA  . ASN B 2 144 ? -13.318 -6.575  16.111 1.00 70.87  ? 227 ASN B CA  1 
ATOM   3076 C  C   . ASN B 2 144 ? -12.385 -7.385  15.218 1.00 70.77  ? 227 ASN B C   1 
ATOM   3077 O  O   . ASN B 2 144 ? -11.257 -6.958  14.930 1.00 78.20  ? 227 ASN B O   1 
ATOM   3078 C  CB  . ASN B 2 144 ? -13.014 -5.079  16.027 1.00 71.43  ? 227 ASN B CB  1 
ATOM   3079 C  CG  . ASN B 2 144 ? -13.581 -4.439  14.780 1.00 76.56  ? 227 ASN B CG  1 
ATOM   3080 O  OD1 . ASN B 2 144 ? -14.592 -4.888  14.242 1.00 82.28  ? 227 ASN B OD1 1 
ATOM   3081 N  ND2 . ASN B 2 144 ? -12.932 -3.379  14.313 1.00 81.85  ? 227 ASN B ND2 1 
ATOM   3082 N  N   . PRO B 2 145 ? -12.818 -8.556  14.762 1.00 65.65  ? 228 PRO B N   1 
ATOM   3083 C  CA  . PRO B 2 145 ? -11.947 -9.391  13.932 1.00 67.95  ? 228 PRO B CA  1 
ATOM   3084 C  C   . PRO B 2 145 ? -11.899 -8.913  12.489 1.00 72.59  ? 228 PRO B C   1 
ATOM   3085 O  O   . PRO B 2 145 ? -12.871 -8.387  11.944 1.00 76.21  ? 228 PRO B O   1 
ATOM   3086 C  CB  . PRO B 2 145 ? -12.595 -10.775 14.034 1.00 67.99  ? 228 PRO B CB  1 
ATOM   3087 C  CG  . PRO B 2 145 ? -14.037 -10.478 14.221 1.00 69.94  ? 228 PRO B CG  1 
ATOM   3088 C  CD  . PRO B 2 145 ? -14.115 -9.202  15.026 1.00 69.00  ? 228 PRO B CD  1 
HETATM 3089 N  N   . MSE B 2 146 ? -10.739 -9.116  11.872 1.00 75.32  ? 229 MSE B N   1 
HETATM 3090 C  CA  . MSE B 2 146 ? -10.482 -8.676  10.503 1.00 80.83  ? 229 MSE B CA  1 
HETATM 3091 C  C   . MSE B 2 146 ? -10.958 -9.679  9.461  1.00 86.54  ? 229 MSE B C   1 
HETATM 3092 O  O   . MSE B 2 146 ? -10.795 -10.884 9.642  1.00 87.85  ? 229 MSE B O   1 
HETATM 3093 C  CB  . MSE B 2 146 ? -8.988  -8.426  10.304 1.00 84.05  ? 229 MSE B CB  1 
HETATM 3094 C  CG  . MSE B 2 146 ? -8.671  -7.288  9.368  1.00 90.19  ? 229 MSE B CG  1 
HETATM 3095 SE SE  . MSE B 2 146 ? -6.767  -6.934  9.256  0.58 97.22  ? 229 MSE B SE  1 
HETATM 3096 C  CE  . MSE B 2 146 ? -6.101  -8.733  8.980  1.00 93.97  ? 229 MSE B CE  1 
ATOM   3097 N  N   . PRO B 2 147 ? -11.525 -9.183  8.363  1.00 91.17  ? 230 PRO B N   1 
ATOM   3098 C  CA  . PRO B 2 147 ? -11.895 -10.079 7.260  1.00 95.25  ? 230 PRO B CA  1 
ATOM   3099 C  C   . PRO B 2 147 ? -10.686 -10.848 6.746  1.00 103.36 ? 230 PRO B C   1 
ATOM   3100 O  O   . PRO B 2 147 ? -9.631  -10.272 6.465  1.00 116.20 ? 230 PRO B O   1 
ATOM   3101 C  CB  . PRO B 2 147 ? -12.455 -9.123  6.200  1.00 95.43  ? 230 PRO B CB  1 
ATOM   3102 C  CG  . PRO B 2 147 ? -12.897 -7.928  6.966  1.00 93.39  ? 230 PRO B CG  1 
ATOM   3103 C  CD  . PRO B 2 147 ? -11.940 -7.793  8.111  1.00 91.76  ? 230 PRO B CD  1 
ATOM   3104 N  N   . GLY B 2 148 ? -10.848 -12.164 6.630  1.00 101.41 ? 231 GLY B N   1 
ATOM   3105 C  CA  . GLY B 2 148 ? -9.795  -13.056 6.201  1.00 98.13  ? 231 GLY B CA  1 
ATOM   3106 C  C   . GLY B 2 148 ? -9.243  -13.936 7.301  1.00 93.33  ? 231 GLY B C   1 
ATOM   3107 O  O   . GLY B 2 148 ? -8.674  -14.995 7.003  1.00 97.48  ? 231 GLY B O   1 
ATOM   3108 N  N   . THR B 2 149 ? -9.389  -13.530 8.558  1.00 87.13  ? 232 THR B N   1 
ATOM   3109 C  CA  . THR B 2 149 ? -8.927  -14.337 9.674  1.00 85.98  ? 232 THR B CA  1 
ATOM   3110 C  C   . THR B 2 149 ? -9.933  -15.440 9.986  1.00 82.62  ? 232 THR B C   1 
ATOM   3111 O  O   . THR B 2 149 ? -11.106 -15.376 9.608  1.00 89.23  ? 232 THR B O   1 
ATOM   3112 C  CB  . THR B 2 149 ? -8.712  -13.471 10.916 1.00 85.55  ? 232 THR B CB  1 
ATOM   3113 O  OG1 . THR B 2 149 ? -9.980  -13.136 11.493 1.00 90.84  ? 232 THR B OG1 1 
ATOM   3114 C  CG2 . THR B 2 149 ? -7.973  -12.192 10.553 1.00 74.88  ? 232 THR B CG2 1 
ATOM   3115 N  N   . ASP B 2 150 ? -9.456  -16.469 10.687 1.00 101.13 ? 233 ASP B N   1 
ATOM   3116 C  CA  . ASP B 2 150 ? -10.367 -17.480 11.203 1.00 105.59 ? 233 ASP B CA  1 
ATOM   3117 C  C   . ASP B 2 150 ? -11.157 -16.974 12.401 1.00 106.34 ? 233 ASP B C   1 
ATOM   3118 O  O   . ASP B 2 150 ? -12.206 -17.542 12.722 1.00 117.81 ? 233 ASP B O   1 
ATOM   3119 C  CB  . ASP B 2 150 ? -9.599  -18.753 11.570 1.00 114.06 ? 233 ASP B CB  1 
ATOM   3120 C  CG  . ASP B 2 150 ? -8.473  -18.494 12.545 1.00 121.75 ? 233 ASP B CG  1 
ATOM   3121 O  OD1 . ASP B 2 150 ? -8.411  -19.191 13.581 1.00 125.92 ? 233 ASP B OD1 1 
ATOM   3122 O  OD2 . ASP B 2 150 ? -7.651  -17.592 12.277 1.00 125.12 ? 233 ASP B OD2 1 
ATOM   3123 N  N   . GLU B 2 151 ? -10.679 -15.916 13.062 1.00 100.42 ? 234 GLU B N   1 
ATOM   3124 C  CA  . GLU B 2 151 ? -11.464 -15.280 14.113 1.00 93.94  ? 234 GLU B CA  1 
ATOM   3125 C  C   . GLU B 2 151 ? -12.682 -14.568 13.542 1.00 95.53  ? 234 GLU B C   1 
ATOM   3126 O  O   . GLU B 2 151 ? -13.732 -14.519 14.192 1.00 99.84  ? 234 GLU B O   1 
ATOM   3127 C  CB  . GLU B 2 151 ? -10.595 -14.298 14.898 1.00 85.09  ? 234 GLU B CB  1 
ATOM   3128 C  CG  . GLU B 2 151 ? -9.696  -14.947 15.938 1.00 85.82  ? 234 GLU B CG  1 
ATOM   3129 C  CD  . GLU B 2 151 ? -10.401 -15.171 17.261 1.00 86.65  ? 234 GLU B CD  1 
ATOM   3130 O  OE1 . GLU B 2 151 ? -9.805  -15.805 18.157 1.00 84.58  ? 234 GLU B OE1 1 
ATOM   3131 O  OE2 . GLU B 2 151 ? -11.551 -14.706 17.407 1.00 90.85  ? 234 GLU B OE2 1 
ATOM   3132 N  N   . HIS B 2 152 ? -12.563 -14.010 12.334 1.00 95.12  ? 235 HIS B N   1 
ATOM   3133 C  CA  . HIS B 2 152 ? -13.710 -13.373 11.696 1.00 100.27 ? 235 HIS B CA  1 
ATOM   3134 C  C   . HIS B 2 152 ? -14.759 -14.395 11.282 1.00 111.26 ? 235 HIS B C   1 
ATOM   3135 O  O   . HIS B 2 152 ? -15.959 -14.100 11.321 1.00 116.59 ? 235 HIS B O   1 
ATOM   3136 C  CB  . HIS B 2 152 ? -13.256 -12.565 10.481 1.00 98.30  ? 235 HIS B CB  1 
ATOM   3137 C  CG  . HIS B 2 152 ? -14.336 -11.721 9.878  1.00 105.48 ? 235 HIS B CG  1 
ATOM   3138 N  ND1 . HIS B 2 152 ? -15.158 -10.912 10.633 1.00 109.93 ? 235 HIS B ND1 1 
ATOM   3139 C  CD2 . HIS B 2 152 ? -14.731 -11.564 8.593  1.00 110.99 ? 235 HIS B CD2 1 
ATOM   3140 C  CE1 . HIS B 2 152 ? -16.013 -10.292 9.838  1.00 114.95 ? 235 HIS B CE1 1 
ATOM   3141 N  NE2 . HIS B 2 152 ? -15.775 -10.670 8.595  1.00 114.50 ? 235 HIS B NE2 1 
ATOM   3142 N  N   . ASP B 2 153 ? -14.331 -15.595 10.880 1.00 113.69 ? 236 ASP B N   1 
ATOM   3143 C  CA  . ASP B 2 153 ? -15.287 -16.635 10.521 1.00 123.77 ? 236 ASP B CA  1 
ATOM   3144 C  C   . ASP B 2 153 ? -16.110 -17.077 11.726 1.00 131.74 ? 236 ASP B C   1 
ATOM   3145 O  O   . ASP B 2 153 ? -17.282 -17.439 11.573 1.00 138.29 ? 236 ASP B O   1 
ATOM   3146 C  CB  . ASP B 2 153 ? -14.558 -17.828 9.899  1.00 122.37 ? 236 ASP B CB  1 
ATOM   3147 C  CG  . ASP B 2 153 ? -13.661 -17.426 8.739  1.00 117.62 ? 236 ASP B CG  1 
ATOM   3148 O  OD1 . ASP B 2 153 ? -12.487 -17.854 8.712  1.00 108.76 ? 236 ASP B OD1 1 
ATOM   3149 O  OD2 . ASP B 2 153 ? -14.130 -16.680 7.853  1.00 119.75 ? 236 ASP B OD2 1 
ATOM   3150 N  N   . ASP B 2 154 ? -15.522 -17.047 12.925 1.00 129.68 ? 237 ASP B N   1 
ATOM   3151 C  CA  . ASP B 2 154 ? -16.278 -17.379 14.128 1.00 133.82 ? 237 ASP B CA  1 
ATOM   3152 C  C   . ASP B 2 154 ? -17.215 -16.249 14.532 1.00 136.43 ? 237 ASP B C   1 
ATOM   3153 O  O   . ASP B 2 154 ? -18.283 -16.504 15.101 1.00 141.02 ? 237 ASP B O   1 
ATOM   3154 C  CB  . ASP B 2 154 ? -15.328 -17.704 15.282 1.00 129.77 ? 237 ASP B CB  1 
ATOM   3155 C  CG  . ASP B 2 154 ? -14.223 -18.661 14.881 1.00 128.02 ? 237 ASP B CG  1 
ATOM   3156 O  OD1 . ASP B 2 154 ? -14.313 -19.252 13.785 1.00 133.86 ? 237 ASP B OD1 1 
ATOM   3157 O  OD2 . ASP B 2 154 ? -13.264 -18.824 15.664 1.00 122.34 ? 237 ASP B OD2 1 
ATOM   3158 N  N   . TYR B 2 155 ? -16.836 -15.000 14.251 1.00 137.39 ? 238 TYR B N   1 
ATOM   3159 C  CA  . TYR B 2 155 ? -17.658 -13.863 14.655 1.00 144.14 ? 238 TYR B CA  1 
ATOM   3160 C  C   . TYR B 2 155 ? -18.958 -13.815 13.867 1.00 151.70 ? 238 TYR B C   1 
ATOM   3161 O  O   . TYR B 2 155 ? -20.046 -13.738 14.449 1.00 157.31 ? 238 TYR B O   1 
ATOM   3162 C  CB  . TYR B 2 155 ? -16.875 -12.563 14.480 1.00 142.69 ? 238 TYR B CB  1 
ATOM   3163 C  CG  . TYR B 2 155 ? -17.710 -11.311 14.648 1.00 147.08 ? 238 TYR B CG  1 
ATOM   3164 C  CD1 . TYR B 2 155 ? -18.161 -10.600 13.542 1.00 151.65 ? 238 TYR B CD1 1 
ATOM   3165 C  CD2 . TYR B 2 155 ? -18.043 -10.839 15.911 1.00 148.64 ? 238 TYR B CD2 1 
ATOM   3166 C  CE1 . TYR B 2 155 ? -18.921 -9.456  13.691 1.00 154.43 ? 238 TYR B CE1 1 
ATOM   3167 C  CE2 . TYR B 2 155 ? -18.803 -9.696  16.069 1.00 151.11 ? 238 TYR B CE2 1 
ATOM   3168 C  CZ  . TYR B 2 155 ? -19.239 -9.008  14.956 1.00 154.77 ? 238 TYR B CZ  1 
ATOM   3169 O  OH  . TYR B 2 155 ? -19.997 -7.870  15.109 1.00 160.33 ? 238 TYR B OH  1 
ATOM   3170 N  N   . GLN B 2 156 ? -18.868 -13.853 12.535 1.00 151.64 ? 239 GLN B N   1 
ATOM   3171 C  CA  . GLN B 2 156 ? -20.074 -13.823 11.720 1.00 161.52 ? 239 GLN B CA  1 
ATOM   3172 C  C   . GLN B 2 156 ? -20.913 -15.081 11.887 1.00 171.48 ? 239 GLN B C   1 
ATOM   3173 O  O   . GLN B 2 156 ? -22.081 -15.086 11.488 1.00 179.26 ? 239 GLN B O   1 
ATOM   3174 C  CB  . GLN B 2 156 ? -19.722 -13.623 10.245 1.00 161.50 ? 239 GLN B CB  1 
ATOM   3175 C  CG  . GLN B 2 156 ? -18.726 -14.622 9.693  1.00 162.79 ? 239 GLN B CG  1 
ATOM   3176 C  CD  . GLN B 2 156 ? -18.095 -14.145 8.401  1.00 165.24 ? 239 GLN B CD  1 
ATOM   3177 O  OE1 . GLN B 2 156 ? -18.148 -12.960 8.074  1.00 167.06 ? 239 GLN B OE1 1 
ATOM   3178 N  NE2 . GLN B 2 156 ? -17.492 -15.067 7.659  1.00 163.84 ? 239 GLN B NE2 1 
ATOM   3179 N  N   . GLU B 2 157 ? -20.351 -16.144 12.465 1.00 168.65 ? 240 GLU B N   1 
ATOM   3180 C  CA  . GLU B 2 157 ? -21.157 -17.319 12.777 1.00 170.12 ? 240 GLU B CA  1 
ATOM   3181 C  C   . GLU B 2 157 ? -22.183 -17.004 13.858 1.00 173.74 ? 240 GLU B C   1 
ATOM   3182 O  O   . GLU B 2 157 ? -23.360 -17.357 13.732 1.00 178.77 ? 240 GLU B O   1 
ATOM   3183 C  CB  . GLU B 2 157 ? -20.260 -18.477 13.211 1.00 162.48 ? 240 GLU B CB  1 
ATOM   3184 C  CG  . GLU B 2 157 ? -19.777 -19.349 12.068 1.00 159.49 ? 240 GLU B CG  1 
ATOM   3185 C  CD  . GLU B 2 157 ? -19.178 -20.654 12.550 1.00 155.95 ? 240 GLU B CD  1 
ATOM   3186 O  OE1 . GLU B 2 157 ? -19.411 -21.019 13.722 1.00 154.93 ? 240 GLU B OE1 1 
ATOM   3187 O  OE2 . GLU B 2 157 ? -18.468 -21.310 11.759 1.00 154.16 ? 240 GLU B OE2 1 
ATOM   3188 N  N   . THR B 2 158 ? -21.758 -16.331 14.925 1.00 173.69 ? 241 THR B N   1 
ATOM   3189 C  CA  . THR B 2 158 ? -22.658 -16.045 16.034 1.00 179.57 ? 241 THR B CA  1 
ATOM   3190 C  C   . THR B 2 158 ? -23.507 -14.800 15.806 1.00 199.52 ? 241 THR B C   1 
ATOM   3191 O  O   . THR B 2 158 ? -24.635 -14.741 16.300 1.00 206.88 ? 241 THR B O   1 
ATOM   3192 C  CB  . THR B 2 158 ? -21.866 -15.907 17.338 1.00 163.06 ? 241 THR B CB  1 
ATOM   3193 O  OG1 . THR B 2 158 ? -21.112 -14.688 17.325 1.00 153.70 ? 241 THR B OG1 1 
ATOM   3194 C  CG2 . THR B 2 158 ? -20.916 -17.087 17.508 1.00 153.98 ? 241 THR B CG2 1 
ATOM   3195 N  N   . ARG B 2 159 ? -23.012 -13.807 15.065 1.00 211.07 ? 242 ARG B N   1 
ATOM   3196 C  CA  . ARG B 2 159 ? -23.842 -12.650 14.746 1.00 214.33 ? 242 ARG B CA  1 
ATOM   3197 C  C   . ARG B 2 159 ? -24.834 -12.930 13.622 1.00 225.93 ? 242 ARG B C   1 
ATOM   3198 O  O   . ARG B 2 159 ? -25.760 -12.138 13.422 1.00 234.48 ? 242 ARG B O   1 
ATOM   3199 C  CB  . ARG B 2 159 ? -22.968 -11.441 14.387 1.00 204.04 ? 242 ARG B CB  1 
ATOM   3200 C  CG  . ARG B 2 159 ? -23.684 -10.089 14.478 1.00 202.07 ? 242 ARG B CG  1 
ATOM   3201 C  CD  . ARG B 2 159 ? -24.564 -9.982  15.723 1.00 200.62 ? 242 ARG B CD  1 
ATOM   3202 N  NE  . ARG B 2 159 ? -25.067 -8.625  15.938 1.00 197.74 ? 242 ARG B NE  1 
ATOM   3203 C  CZ  . ARG B 2 159 ? -26.302 -8.224  15.647 1.00 200.80 ? 242 ARG B CZ  1 
ATOM   3204 N  NH1 . ARG B 2 159 ? -27.174 -9.075  15.124 1.00 205.93 ? 242 ARG B NH1 1 
ATOM   3205 N  NH2 . ARG B 2 159 ? -26.665 -6.970  15.880 1.00 200.61 ? 242 ARG B NH2 1 
ATOM   3206 N  N   . ALA B 2 160 ? -24.667 -14.032 12.888 1.00 228.75 ? 243 ALA B N   1 
ATOM   3207 C  CA  . ALA B 2 160 ? -25.683 -14.499 11.955 1.00 227.00 ? 243 ALA B CA  1 
ATOM   3208 C  C   . ALA B 2 160 ? -26.566 -15.589 12.543 1.00 225.03 ? 243 ALA B C   1 
ATOM   3209 O  O   . ALA B 2 160 ? -27.613 -15.895 11.965 1.00 234.52 ? 243 ALA B O   1 
ATOM   3210 C  CB  . ALA B 2 160 ? -25.039 -15.013 10.661 1.00 226.62 ? 243 ALA B CB  1 
ATOM   3211 N  N   . LYS B 2 161 ? -26.170 -16.184 13.669 1.00 200.16 ? 244 LYS B N   1 
ATOM   3212 C  CA  . LYS B 2 161 ? -27.001 -17.148 14.376 1.00 187.74 ? 244 LYS B CA  1 
ATOM   3213 C  C   . LYS B 2 161 ? -27.483 -16.622 15.722 1.00 212.41 ? 244 LYS B C   1 
ATOM   3214 O  O   . LYS B 2 161 ? -28.043 -17.390 16.512 1.00 217.85 ? 244 LYS B O   1 
ATOM   3215 C  CB  . LYS B 2 161 ? -26.253 -18.472 14.557 1.00 185.99 ? 244 LYS B CB  1 
ATOM   3216 C  CG  . LYS B 2 161 ? -25.862 -19.145 13.246 1.00 169.73 ? 244 LYS B CG  1 
ATOM   3217 C  CD  . LYS B 2 161 ? -26.999 -19.107 12.235 1.00 154.83 ? 244 LYS B CD  1 
ATOM   3218 C  CE  . LYS B 2 161 ? -26.494 -19.371 10.826 1.00 140.97 ? 244 LYS B CE  1 
ATOM   3219 N  NZ  . LYS B 2 161 ? -25.366 -18.470 10.465 1.00 139.99 ? 244 LYS B NZ  1 
ATOM   3220 N  N   . GLU B 2 162 ? -27.265 -15.337 16.012 1.00 234.18 ? 245 GLU B N   1 
ATOM   3221 C  CA  . GLU B 2 162 ? -27.974 -14.677 17.101 1.00 245.46 ? 245 GLU B CA  1 
ATOM   3222 C  C   . GLU B 2 162 ? -29.300 -14.087 16.647 1.00 254.05 ? 245 GLU B C   1 
ATOM   3223 O  O   . GLU B 2 162 ? -30.198 -13.901 17.477 1.00 259.53 ? 245 GLU B O   1 
ATOM   3224 C  CB  . GLU B 2 162 ? -27.118 -13.568 17.725 1.00 246.31 ? 245 GLU B CB  1 
ATOM   3225 C  CG  . GLU B 2 162 ? -26.207 -14.021 18.864 1.00 246.65 ? 245 GLU B CG  1 
ATOM   3226 C  CD  . GLU B 2 162 ? -26.710 -15.264 19.573 1.00 246.16 ? 245 GLU B CD  1 
ATOM   3227 O  OE1 . GLU B 2 162 ? -26.250 -16.374 19.230 1.00 243.42 ? 245 GLU B OE1 1 
ATOM   3228 O  OE2 . GLU B 2 162 ? -27.559 -15.131 20.480 1.00 249.27 ? 245 GLU B OE2 1 
ATOM   3229 N  N   . GLN B 2 163 ? -29.439 -13.785 15.356 1.00 250.94 ? 246 GLN B N   1 
ATOM   3230 C  CA  . GLN B 2 163 ? -30.720 -13.390 14.785 1.00 245.30 ? 246 GLN B CA  1 
ATOM   3231 C  C   . GLN B 2 163 ? -31.654 -14.574 14.578 1.00 243.47 ? 246 GLN B C   1 
ATOM   3232 O  O   . GLN B 2 163 ? -32.805 -14.375 14.175 1.00 243.34 ? 246 GLN B O   1 
ATOM   3233 C  CB  . GLN B 2 163 ? -30.504 -12.653 13.459 1.00 238.94 ? 246 GLN B CB  1 
ATOM   3234 C  CG  . GLN B 2 163 ? -29.545 -13.344 12.505 1.00 231.21 ? 246 GLN B CG  1 
ATOM   3235 C  CD  . GLN B 2 163 ? -30.258 -14.235 11.507 1.00 224.19 ? 246 GLN B CD  1 
ATOM   3236 O  OE1 . GLN B 2 163 ? -31.131 -13.781 10.767 1.00 221.48 ? 246 GLN B OE1 1 
ATOM   3237 N  NE2 . GLN B 2 163 ? -29.887 -15.510 11.480 1.00 222.29 ? 246 GLN B NE2 1 
ATOM   3238 N  N   . GLU B 2 164 ? -31.181 -15.796 14.830 1.00 244.37 ? 247 GLU B N   1 
ATOM   3239 C  CA  . GLU B 2 164 ? -32.041 -16.968 14.901 1.00 236.30 ? 247 GLU B CA  1 
ATOM   3240 C  C   . GLU B 2 164 ? -32.405 -17.339 16.332 1.00 245.30 ? 247 GLU B C   1 
ATOM   3241 O  O   . GLU B 2 164 ? -33.350 -18.109 16.537 1.00 244.24 ? 247 GLU B O   1 
ATOM   3242 C  CB  . GLU B 2 164 ? -31.368 -18.166 14.219 1.00 220.38 ? 247 GLU B CB  1 
ATOM   3243 C  CG  . GLU B 2 164 ? -32.338 -19.123 13.546 1.00 207.89 ? 247 GLU B CG  1 
ATOM   3244 C  CD  . GLU B 2 164 ? -32.573 -20.381 14.358 1.00 204.71 ? 247 GLU B CD  1 
ATOM   3245 O  OE1 . GLU B 2 164 ? -33.277 -21.286 13.863 1.00 200.17 ? 247 GLU B OE1 1 
ATOM   3246 O  OE2 . GLU B 2 164 ? -32.053 -20.468 15.491 1.00 207.20 ? 247 GLU B OE2 1 
ATOM   3247 N  N   . GLU B 2 165 ? -31.675 -16.814 17.316 1.00 255.61 ? 248 GLU B N   1 
ATOM   3248 C  CA  . GLU B 2 165 ? -32.005 -16.981 18.726 1.00 258.18 ? 248 GLU B CA  1 
ATOM   3249 C  C   . GLU B 2 165 ? -32.728 -15.776 19.311 1.00 262.77 ? 248 GLU B C   1 
ATOM   3250 O  O   . GLU B 2 165 ? -33.517 -15.935 20.248 1.00 267.40 ? 248 GLU B O   1 
ATOM   3251 C  CB  . GLU B 2 165 ? -30.733 -17.252 19.539 1.00 259.40 ? 248 GLU B CB  1 
ATOM   3252 C  CG  . GLU B 2 165 ? -30.980 -17.841 20.920 1.00 261.90 ? 248 GLU B CG  1 
ATOM   3253 C  CD  . GLU B 2 165 ? -31.059 -19.356 20.910 1.00 257.66 ? 248 GLU B CD  1 
ATOM   3254 O  OE1 . GLU B 2 165 ? -31.585 -19.922 19.929 1.00 252.49 ? 248 GLU B OE1 1 
ATOM   3255 O  OE2 . GLU B 2 165 ? -30.593 -19.982 21.886 1.00 260.42 ? 248 GLU B OE2 1 
HETATM 3256 N  N   . MSE B 2 166 ? -32.475 -14.581 18.783 1.00 254.69 ? 249 MSE B N   1 
HETATM 3257 C  CA  . MSE B 2 166 ? -33.199 -13.382 19.191 1.00 246.84 ? 249 MSE B CA  1 
HETATM 3258 C  C   . MSE B 2 166 ? -34.263 -13.046 18.145 1.00 239.61 ? 249 MSE B C   1 
HETATM 3259 O  O   . MSE B 2 166 ? -34.235 -11.983 17.524 1.00 237.58 ? 249 MSE B O   1 
HETATM 3260 C  CB  . MSE B 2 166 ? -32.237 -12.205 19.391 1.00 237.18 ? 249 MSE B CB  1 
HETATM 3261 C  CG  . MSE B 2 166 ? -32.854 -10.978 20.061 1.00 229.37 ? 249 MSE B CG  1 
HETATM 3262 SE SE  . MSE B 2 166 ? -32.446 -10.814 21.962 0.51 230.89 ? 249 MSE B SE  1 
HETATM 3263 C  CE  . MSE B 2 166 ? -33.043 -8.977  22.236 1.00 231.77 ? 249 MSE B CE  1 
ATOM   3264 N  N   . LYS B 2 167 ? -35.193 -13.980 17.944 1.00 233.28 ? 250 LYS B N   1 
ATOM   3265 C  CA  . LYS B 2 167 ? -36.295 -13.787 17.009 1.00 221.21 ? 250 LYS B CA  1 
ATOM   3266 C  C   . LYS B 2 167 ? -37.445 -14.724 17.356 1.00 217.74 ? 250 LYS B C   1 
ATOM   3267 O  O   . LYS B 2 167 ? -38.600 -14.294 17.447 1.00 219.79 ? 250 LYS B O   1 
ATOM   3268 C  CB  . LYS B 2 167 ? -35.832 -14.014 15.568 1.00 212.67 ? 250 LYS B CB  1 
ATOM   3269 C  CG  . LYS B 2 167 ? -36.866 -13.632 14.521 1.00 205.63 ? 250 LYS B CG  1 
ATOM   3270 C  CD  . LYS B 2 167 ? -37.171 -12.143 14.565 1.00 201.52 ? 250 LYS B CD  1 
ATOM   3271 C  CE  . LYS B 2 167 ? -38.232 -11.761 13.545 1.00 192.61 ? 250 LYS B CE  1 
ATOM   3272 N  NZ  . LYS B 2 167 ? -39.608 -12.055 14.037 1.00 192.25 ? 250 LYS B NZ  1 
ATOM   3273 N  N   . ARG B 2 168 ? -37.138 -16.008 17.553 1.00 216.95 ? 251 ARG B N   1 
ATOM   3274 C  CA  . ARG B 2 168 ? -38.147 -16.968 17.980 1.00 206.41 ? 251 ARG B CA  1 
ATOM   3275 C  C   . ARG B 2 168 ? -38.439 -16.881 19.472 1.00 215.58 ? 251 ARG B C   1 
ATOM   3276 O  O   . ARG B 2 168 ? -39.480 -17.378 19.916 1.00 211.91 ? 251 ARG B O   1 
ATOM   3277 C  CB  . ARG B 2 168 ? -37.705 -18.391 17.628 1.00 189.21 ? 251 ARG B CB  1 
ATOM   3278 C  CG  . ARG B 2 168 ? -37.089 -18.524 16.246 1.00 175.95 ? 251 ARG B CG  1 
ATOM   3279 C  CD  . ARG B 2 168 ? -37.504 -19.822 15.574 1.00 168.77 ? 251 ARG B CD  1 
ATOM   3280 N  NE  . ARG B 2 168 ? -36.996 -19.912 14.208 1.00 161.13 ? 251 ARG B NE  1 
ATOM   3281 C  CZ  . ARG B 2 168 ? -37.587 -19.359 13.153 1.00 154.51 ? 251 ARG B CZ  1 
ATOM   3282 N  NH1 . ARG B 2 168 ? -38.712 -18.674 13.304 1.00 154.51 ? 251 ARG B NH1 1 
ATOM   3283 N  NH2 . ARG B 2 168 ? -37.053 -19.491 11.946 1.00 147.04 ? 251 ARG B NH2 1 
ATOM   3284 N  N   . PHE B 2 169 ? -37.553 -16.263 20.247 1.00 224.20 ? 252 PHE B N   1 
ATOM   3285 C  CA  . PHE B 2 169 ? -37.738 -16.136 21.689 1.00 230.79 ? 252 PHE B CA  1 
ATOM   3286 C  C   . PHE B 2 169 ? -38.867 -15.163 22.016 1.00 235.92 ? 252 PHE B C   1 
ATOM   3287 O  O   . PHE B 2 169 ? -39.262 -14.353 21.179 1.00 235.40 ? 252 PHE B O   1 
ATOM   3288 C  CB  . PHE B 2 169 ? -36.435 -15.682 22.357 1.00 230.76 ? 252 PHE B CB  1 
ATOM   3289 C  CG  . PHE B 2 169 ? -36.266 -14.187 22.417 1.00 229.34 ? 252 PHE B CG  1 
ATOM   3290 C  CD1 . PHE B 2 169 ? -36.214 -13.531 23.636 1.00 232.73 ? 252 PHE B CD1 1 
ATOM   3291 C  CD2 . PHE B 2 169 ? -36.151 -13.440 21.255 1.00 223.57 ? 252 PHE B CD2 1 
ATOM   3292 C  CE1 . PHE B 2 169 ? -36.056 -12.157 23.696 1.00 232.19 ? 252 PHE B CE1 1 
ATOM   3293 C  CE2 . PHE B 2 169 ? -35.995 -12.067 21.308 1.00 223.61 ? 252 PHE B CE2 1 
ATOM   3294 C  CZ  . PHE B 2 169 ? -35.946 -11.425 22.531 1.00 227.89 ? 252 PHE B CZ  1 
HETATM 3295 C  C1  . CIT C 3 .   ? -16.953 -1.143  16.189 1.00 163.55 ? 301 CIT B C1  1 
HETATM 3296 O  O1  . CIT C 3 .   ? -17.632 -0.215  15.698 1.00 163.72 ? 301 CIT B O1  1 
HETATM 3297 O  O2  . CIT C 3 .   ? -16.580 -1.048  17.378 1.00 161.77 ? 301 CIT B O2  1 
HETATM 3298 C  C2  . CIT C 3 .   ? -16.570 -2.346  15.357 1.00 166.55 ? 301 CIT B C2  1 
HETATM 3299 C  C3  . CIT C 3 .   ? -17.648 -3.426  15.420 1.00 169.25 ? 301 CIT B C3  1 
HETATM 3300 O  O7  . CIT C 3 .   ? -17.383 -4.392  14.372 1.00 168.39 ? 301 CIT B O7  1 
HETATM 3301 C  C4  . CIT C 3 .   ? -17.663 -4.122  16.778 1.00 168.49 ? 301 CIT B C4  1 
HETATM 3302 C  C5  . CIT C 3 .   ? -17.825 -5.617  16.613 1.00 168.46 ? 301 CIT B C5  1 
HETATM 3303 O  O3  . CIT C 3 .   ? -17.724 -6.160  15.492 1.00 168.35 ? 301 CIT B O3  1 
HETATM 3304 O  O4  . CIT C 3 .   ? -18.073 -6.336  17.606 1.00 167.88 ? 301 CIT B O4  1 
HETATM 3305 C  C6  . CIT C 3 .   ? -19.011 -2.798  15.182 1.00 173.03 ? 301 CIT B C6  1 
HETATM 3306 O  O5  . CIT C 3 .   ? -19.213 -2.058  14.194 1.00 173.97 ? 301 CIT B O5  1 
HETATM 3307 O  O6  . CIT C 3 .   ? -19.946 -3.013  15.984 1.00 174.04 ? 301 CIT B O6  1 
HETATM 3308 MG MG  . MG  D 4 .   ? 1.070   -5.241  19.092 1.00 87.53  ? 302 MG  B MG  1 
HETATM 3309 O  O   . HOH E 5 .   ? -0.105  -7.770  18.467 1.00 55.26  ? 401 HOH B O   1 
HETATM 3310 O  O   . HOH E 5 .   ? 2.869   -4.068  19.287 1.00 89.34  ? 402 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . LYS A 5   ? 1.8901 1.5457 2.5135 -0.2754 0.0401  0.1842  5   LYS A N   
2    C  CA  . LYS A 5   ? 1.8271 1.5091 2.4825 -0.2632 0.0638  0.2491  5   LYS A CA  
3    C  C   . LYS A 5   ? 1.7320 1.4879 2.3978 -0.2632 0.0846  0.2853  5   LYS A C   
4    O  O   . LYS A 5   ? 1.6716 1.4543 2.3089 -0.2646 0.0849  0.2571  5   LYS A O   
5    C  CB  . LYS A 5   ? 1.8118 1.4673 2.4351 -0.2179 0.0872  0.2446  5   LYS A CB  
6    C  CG  . LYS A 5   ? 1.8224 1.4070 2.4501 -0.2133 0.0706  0.2364  5   LYS A CG  
7    C  CD  . LYS A 5   ? 1.8279 1.4007 2.5073 -0.2382 0.0657  0.2967  5   LYS A CD  
8    C  CE  . LYS A 5   ? 1.7830 1.3982 2.4731 -0.2181 0.1023  0.3612  5   LYS A CE  
9    N  NZ  . LYS A 5   ? 1.7997 1.4131 2.5496 -0.2453 0.1032  0.4249  5   LYS A NZ  
10   N  N   . ALA A 6   ? 1.6322 1.4188 2.3371 -0.2592 0.1046  0.3495  6   ALA A N   
11   C  CA  . ALA A 6   ? 1.4695 1.3267 2.1927 -0.2556 0.1264  0.3916  6   ALA A CA  
12   C  C   . ALA A 6   ? 1.4009 1.2662 2.0897 -0.2082 0.1692  0.4141  6   ALA A C   
13   O  O   . ALA A 6   ? 1.3491 1.2278 2.0638 -0.1960 0.1929  0.4698  6   ALA A O   
14   C  CB  . ALA A 6   ? 1.3689 1.2635 2.1725 -0.2898 0.1162  0.4497  6   ALA A CB  
15   N  N   . PHE A 7   ? 1.3539 1.2089 1.9822 -0.1816 0.1795  0.3699  7   PHE A N   
16   C  CA  . PHE A 7   ? 1.3219 1.1821 1.9087 -0.1382 0.2147  0.3827  7   PHE A CA  
17   C  C   . PHE A 7   ? 1.2357 1.1482 1.8135 -0.1322 0.2336  0.3967  7   PHE A C   
18   O  O   . PHE A 7   ? 1.1649 1.1097 1.7659 -0.1600 0.2179  0.3945  7   PHE A O   
19   C  CB  . PHE A 7   ? 1.3503 1.1656 1.8831 -0.1132 0.2120  0.3271  7   PHE A CB  
20   C  CG  . PHE A 7   ? 1.2882 1.1162 1.7871 -0.1134 0.2116  0.2775  7   PHE A CG  
21   C  CD1 . PHE A 7   ? 1.2838 1.1055 1.7362 -0.0815 0.2302  0.2561  7   PHE A CD1 
22   C  CD2 . PHE A 7   ? 1.2579 1.0998 1.7683 -0.1461 0.1921  0.2523  7   PHE A CD2 
23   C  CE1 . PHE A 7   ? 1.1583 0.9905 1.5843 -0.0848 0.2328  0.2136  7   PHE A CE1 
24   C  CE2 . PHE A 7   ? 1.2237 1.0743 1.6990 -0.1457 0.1967  0.2109  7   PHE A CE2 
25   C  CZ  . PHE A 7   ? 1.1285 0.9754 1.5653 -0.1163 0.2187  0.1927  7   PHE A CZ  
26   N  N   . ARG A 8   ? 1.2409 1.1565 1.7794 -0.0937 0.2658  0.4108  8   ARG A N   
27   C  CA  . ARG A 8   ? 1.2608 1.2162 1.7841 -0.0809 0.2878  0.4268  8   ARG A CA  
28   C  C   . ARG A 8   ? 1.2094 1.1381 1.6643 -0.0524 0.3011  0.3856  8   ARG A C   
29   O  O   . ARG A 8   ? 1.3041 1.1935 1.7256 -0.0286 0.3048  0.3685  8   ARG A O   
30   C  CB  . ARG A 8   ? 1.4242 1.4128 1.9720 -0.0604 0.3192  0.4954  8   ARG A CB  
31   C  CG  . ARG A 8   ? 1.6347 1.5907 2.1757 -0.0379 0.3347  0.5222  8   ARG A CG  
32   C  CD  . ARG A 8   ? 1.7912 1.7782 2.3417 -0.0092 0.3756  0.5877  8   ARG A CD  
33   N  NE  . ARG A 8   ? 1.8864 1.9425 2.4863 -0.0228 0.3704  0.6089  8   ARG A NE  
34   C  CZ  . ARG A 8   ? 1.9753 2.0721 2.6474 -0.0494 0.3537  0.6368  8   ARG A CZ  
35   N  NH1 . ARG A 8   ? 2.0420 2.1138 2.7428 -0.0672 0.3426  0.6467  8   ARG A NH1 
36   N  NH2 . ARG A 8   ? 2.0490 2.2087 2.7659 -0.0580 0.3471  0.6559  8   ARG A NH2 
37   N  N   . ARG A 9   ? 1.0652 1.0141 1.5005 -0.0559 0.3060  0.3703  9   ARG A N   
38   C  CA  . ARG A 9   ? 1.0253 0.9500 1.4016 -0.0337 0.3197  0.3341  9   ARG A CA  
39   C  C   . ARG A 9   ? 1.0530 0.9673 1.3946 0.0079  0.3502  0.3654  9   ARG A C   
40   O  O   . ARG A 9   ? 1.0465 0.9887 1.4059 0.0202  0.3700  0.4183  9   ARG A O   
41   C  CB  . ARG A 9   ? 0.8849 0.8293 1.2471 -0.0483 0.3207  0.3174  9   ARG A CB  
42   C  CG  . ARG A 9   ? 0.9322 0.8837 1.3152 -0.0865 0.2925  0.2871  9   ARG A CG  
43   C  CD  . ARG A 9   ? 0.9383 0.9026 1.2934 -0.0960 0.2974  0.2729  9   ARG A CD  
44   N  NE  . ARG A 9   ? 0.9774 0.9155 1.2837 -0.0785 0.3173  0.2410  9   ARG A NE  
45   C  CZ  . ARG A 9   ? 0.9830 0.9222 1.2557 -0.0800 0.3304  0.2325  9   ARG A CZ  
46   N  NH1 . ARG A 9   ? 1.0309 0.9964 1.3081 -0.0946 0.3246  0.2536  9   ARG A NH1 
47   N  NH2 . ARG A 9   ? 1.0002 0.9124 1.2354 -0.0677 0.3473  0.2036  9   ARG A NH2 
48   N  N   . TYR A 10  ? 1.0832 0.9575 1.3752 0.0307  0.3536  0.3318  10  TYR A N   
49   C  CA  . TYR A 10  ? 1.1850 1.0359 1.4289 0.0726  0.3782  0.3531  10  TYR A CA  
50   C  C   . TYR A 10  ? 1.2205 1.0418 1.4096 0.0856  0.3812  0.3097  10  TYR A C   
51   O  O   . TYR A 10  ? 1.2542 1.0671 1.4464 0.0659  0.3623  0.2596  10  TYR A O   
52   C  CB  . TYR A 10  ? 1.2770 1.0975 1.5129 0.0919  0.3736  0.3639  10  TYR A CB  
53   C  CG  . TYR A 10  ? 1.3223 1.1598 1.5788 0.1058  0.3962  0.4299  10  TYR A CG  
54   C  CD1 . TYR A 10  ? 1.2829 1.1495 1.6074 0.0765  0.3864  0.4589  10  TYR A CD1 
55   C  CD2 . TYR A 10  ? 1.3578 1.1809 1.5657 0.1481  0.4285  0.4633  10  TYR A CD2 
56   C  CE1 . TYR A 10  ? 1.2915 1.1788 1.6447 0.0865  0.4102  0.5223  10  TYR A CE1 
57   C  CE2 . TYR A 10  ? 1.3469 1.1891 1.5756 0.1630  0.4557  0.5261  10  TYR A CE2 
58   C  CZ  . TYR A 10  ? 1.3307 1.2085 1.6371 0.1307  0.4474  0.5570  10  TYR A CZ  
59   O  OH  . TYR A 10  ? 1.3761 1.2865 1.7106 0.1433  0.4633  0.6019  10  TYR A OH  
60   N  N   . ILE A 11  ? 1.2760 1.0804 1.4163 0.1189  0.4065  0.3296  11  ILE A N   
61   C  CA  . ILE A 11  ? 1.2825 1.0521 1.3680 0.1316  0.4103  0.2932  11  ILE A CA  
62   C  C   . ILE A 11  ? 1.3383 1.0591 1.3690 0.1671  0.4081  0.2832  11  ILE A C   
63   O  O   . ILE A 11  ? 1.3674 1.0779 1.3765 0.1975  0.4239  0.3232  11  ILE A O   
64   C  CB  . ILE A 11  ? 1.2390 1.0142 1.2997 0.1440  0.4378  0.3180  11  ILE A CB  
65   C  CG1 . ILE A 11  ? 1.1896 0.9978 1.2843 0.1079  0.4324  0.3075  11  ILE A CG1 
66   C  CG2 . ILE A 11  ? 1.1716 0.8930 1.1607 0.1701  0.4464  0.2924  11  ILE A CG2 
67   C  CD1 . ILE A 11  ? 1.1927 1.0515 1.3492 0.0846  0.4245  0.3375  11  ILE A CD1 
68   N  N   . PHE A 12  ? 1.3627 1.0542 1.3710 0.1635  0.3882  0.2303  12  PHE A N   
69   C  CA  . PHE A 12  ? 1.4746 1.1162 1.4246 0.1964  0.3784  0.2131  12  PHE A CA  
70   C  C   . PHE A 12  ? 1.5412 1.1557 1.4604 0.1914  0.3710  0.1666  12  PHE A C   
71   O  O   . PHE A 12  ? 1.5369 1.1536 1.4816 0.1708  0.3452  0.1192  12  PHE A O   
72   C  CB  . PHE A 12  ? 1.4679 1.1053 1.4405 0.1949  0.3489  0.1953  12  PHE A CB  
73   C  CG  . PHE A 12  ? 1.5546 1.1409 1.4642 0.2316  0.3338  0.1814  12  PHE A CG  
74   C  CD1 . PHE A 12  ? 1.6522 1.1974 1.4840 0.2689  0.3526  0.1996  12  PHE A CD1 
75   C  CD2 . PHE A 12  ? 1.5981 1.1745 1.5222 0.2314  0.2991  0.1484  12  PHE A CD2 
76   C  CE1 . PHE A 12  ? 1.7410 1.2334 1.5047 0.3037  0.3347  0.1845  12  PHE A CE1 
77   C  CE2 . PHE A 12  ? 1.6893 1.2182 1.5522 0.2665  0.2794  0.1350  12  PHE A CE2 
78   C  CZ  . PHE A 12  ? 1.7446 1.2297 1.5238 0.3019  0.2961  0.1525  12  PHE A CZ  
79   N  N   . GLU A 13  ? 1.5586 1.1474 1.4268 0.2102  0.3947  0.1813  13  GLU A N   
80   C  CA  . GLU A 13  ? 1.5854 1.1361 1.4161 0.2074  0.3893  0.1416  13  GLU A CA  
81   C  C   . GLU A 13  ? 1.6937 1.1807 1.4367 0.2523  0.3921  0.1445  13  GLU A C   
82   O  O   . GLU A 13  ? 1.7889 1.2644 1.4927 0.2876  0.4170  0.1892  13  GLU A O   
83   C  CB  . GLU A 13  ? 1.6143 1.1751 1.4503 0.1898  0.4133  0.1506  13  GLU A CB  
84   C  CG  . GLU A 13  ? 1.6293 1.2498 1.5300 0.1596  0.4215  0.1718  13  GLU A CG  
85   C  CD  . GLU A 13  ? 1.6970 1.3224 1.5832 0.1639  0.4507  0.2053  13  GLU A CD  
86   O  OE1 . GLU A 13  ? 1.6900 1.3484 1.6135 0.1328  0.4528  0.2046  13  GLU A OE1 
87   O  OE2 . GLU A 13  ? 1.6944 1.2882 1.5280 0.2013  0.4717  0.2323  13  GLU A OE2 
88   N  N   . LEU A 14  ? 1.6899 1.1354 1.4023 0.2508  0.3670  0.0965  14  LEU A N   
89   C  CA  . LEU A 14  ? 1.7624 1.1360 1.3808 0.2903  0.3647  0.0897  14  LEU A CA  
90   C  C   . LEU A 14  ? 1.8137 1.1504 1.4115 0.2728  0.3611  0.0532  14  LEU A C   
91   O  O   . LEU A 14  ? 1.9231 1.2772 1.5721 0.2346  0.3374  0.0107  14  LEU A O   
92   C  CB  . LEU A 14  ? 1.7915 1.1383 1.3815 0.3103  0.3273  0.0656  14  LEU A CB  
93   C  CG  . LEU A 14  ? 1.8232 1.1533 1.3597 0.3564  0.3460  0.1141  14  LEU A CG  
94   C  CD1 . LEU A 14  ? 1.7388 1.1336 1.3513 0.3405  0.3574  0.1503  14  LEU A CD1 
95   C  CD2 . LEU A 14  ? 1.8813 1.1537 1.3413 0.3933  0.3152  0.0958  14  LEU A CD2 
96   N  N   . TYR A 15  ? 1.8501 1.1350 1.3753 0.3012  0.3868  0.0712  15  TYR A N   
97   C  CA  . TYR A 15  ? 1.8267 1.0640 1.3238 0.2867  0.3867  0.0415  15  TYR A CA  
98   C  C   . TYR A 15  ? 1.9164 1.0747 1.3345 0.3091  0.3563  0.0029  15  TYR A C   
99   O  O   . TYR A 15  ? 1.9870 1.1066 1.3321 0.3551  0.3547  0.0165  15  TYR A O   
100  C  CB  . TYR A 15  ? 1.8138 1.0332 1.2756 0.3060  0.4308  0.0816  15  TYR A CB  
101  C  CG  . TYR A 15  ? 1.7110 1.0059 1.2486 0.2819  0.4551  0.1174  15  TYR A CG  
102  C  CD1 . TYR A 15  ? 1.6469 0.9923 1.2099 0.3004  0.4734  0.1657  15  TYR A CD1 
103  C  CD2 . TYR A 15  ? 1.7154 1.0290 1.2976 0.2397  0.4587  0.1034  15  TYR A CD2 
104  C  CE1 . TYR A 15  ? 1.6234 1.0363 1.2555 0.2768  0.4889  0.1960  15  TYR A CE1 
105  C  CE2 . TYR A 15  ? 1.6888 1.0663 1.3303 0.2194  0.4764  0.1344  15  TYR A CE2 
106  C  CZ  . TYR A 15  ? 1.6746 1.1018 1.3414 0.2377  0.4886  0.1791  15  TYR A CZ  
107  O  OH  . TYR A 15  ? 1.6573 1.1468 1.3831 0.2160  0.4999  0.2077  15  TYR A OH  
108  N  N   . PHE A 16  ? 1.9050 1.0386 1.3372 0.2756  0.3317  -0.0451 16  PHE A N   
109  C  CA  . PHE A 16  ? 1.9675 1.0253 1.3324 0.2884  0.2952  -0.0883 16  PHE A CA  
110  C  C   . PHE A 16  ? 1.9871 0.9762 1.3078 0.2786  0.3065  -0.1041 16  PHE A C   
111  O  O   . PHE A 16  ? 1.9108 0.9215 1.2722 0.2512  0.3360  -0.0897 16  PHE A O   
112  C  CB  . PHE A 16  ? 1.9559 1.0466 1.3881 0.2545  0.2442  -0.1377 16  PHE A CB  
113  C  CG  . PHE A 16  ? 1.9151 1.0870 1.4221 0.2485  0.2374  -0.1242 16  PHE A CG  
114  C  CD1 . PHE A 16  ? 1.8296 1.0786 1.4347 0.2089  0.2555  -0.1153 16  PHE A CD1 
115  C  CD2 . PHE A 16  ? 1.9282 1.0919 1.4002 0.2841  0.2125  -0.1206 16  PHE A CD2 
116  C  CE1 . PHE A 16  ? 1.7930 1.1071 1.4616 0.2041  0.2478  -0.1057 16  PHE A CE1 
117  C  CE2 . PHE A 16  ? 1.8655 1.0950 1.4037 0.2790  0.2058  -0.1079 16  PHE A CE2 
118  C  CZ  . PHE A 16  ? 1.8164 1.1199 1.4539 0.2387  0.2230  -0.1016 16  PHE A CZ  
119  N  N   . ASP A 17  ? 2.0767 0.9763 1.3072 0.3025  0.2810  -0.1340 17  ASP A N   
120  C  CA  . ASP A 17  ? 2.1759 0.9905 1.3498 0.2970  0.2858  -0.1537 17  ASP A CA  
121  C  C   . ASP A 17  ? 2.1684 1.0117 1.4346 0.2300  0.2730  -0.1866 17  ASP A C   
122  O  O   . ASP A 17  ? 2.2268 1.0848 1.5409 0.1988  0.2276  -0.2316 17  ASP A O   
123  C  CB  . ASP A 17  ? 2.3413 1.0545 1.4047 0.3305  0.2487  -0.1891 17  ASP A CB  
124  C  CG  . ASP A 17  ? 2.4576 1.0653 1.4407 0.3359  0.2583  -0.2040 17  ASP A CG  
125  O  OD1 . ASP A 17  ? 2.4636 1.0647 1.4997 0.2846  0.2504  -0.2301 17  ASP A OD1 
126  O  OD2 . ASP A 17  ? 2.5742 1.1019 1.4390 0.3927  0.2759  -0.1889 17  ASP A OD2 
127  N  N   . PRO A 18  ? 2.1099 0.9625 1.4038 0.2077  0.3126  -0.1640 18  PRO A N   
128  C  CA  . PRO A 18  ? 2.0520 0.9353 1.4343 0.1434  0.3073  -0.1902 18  PRO A CA  
129  C  C   . PRO A 18  ? 2.1616 0.9635 1.5174 0.1188  0.2759  -0.2389 18  PRO A C   
130  O  O   . PRO A 18  ? 2.1237 0.9589 1.5643 0.0641  0.2576  -0.2711 18  PRO A O   
131  C  CB  . PRO A 18  ? 1.9748 0.8731 1.3671 0.1373  0.3598  -0.1465 18  PRO A CB  
132  C  CG  . PRO A 18  ? 2.0480 0.8803 1.3349 0.1975  0.3852  -0.1125 18  PRO A CG  
133  C  CD  . PRO A 18  ? 2.0911 0.9260 1.3364 0.2416  0.3640  -0.1124 18  PRO A CD  
134  N  N   . ALA A 19  ? 2.3127 1.0080 1.5543 0.1574  0.2694  -0.2458 19  ALA A N   
135  C  CA  . ALA A 19  ? 2.4928 1.0984 1.7030 0.1320  0.2381  -0.2926 19  ALA A CA  
136  C  C   . ALA A 19  ? 2.5480 1.1763 1.8075 0.1055  0.1749  -0.3453 19  ALA A C   
137  O  O   . ALA A 19  ? 2.5869 1.2222 1.9190 0.0489  0.1521  -0.3812 19  ALA A O   
138  C  CB  . ALA A 19  ? 2.6101 1.0896 1.6750 0.1862  0.2438  -0.2899 19  ALA A CB  
139  N  N   . ARG A 20  ? 2.5481 1.1903 1.7725 0.1459  0.1461  -0.3487 20  ARG A N   
140  C  CA  . ARG A 20  ? 2.5545 1.2109 1.8125 0.1305  0.0802  -0.3978 20  ARG A CA  
141  C  C   . ARG A 20  ? 2.3981 1.1790 1.7703 0.1142  0.0700  -0.3936 20  ARG A C   
142  O  O   . ARG A 20  ? 2.4296 1.2346 1.8391 0.1058  0.0147  -0.4309 20  ARG A O   
143  C  CB  . ARG A 20  ? 2.7396 1.3071 1.8636 0.1893  0.0450  -0.4120 20  ARG A CB  
144  C  CG  . ARG A 20  ? 2.7406 1.3164 1.7911 0.2545  0.0784  -0.3632 20  ARG A CG  
145  C  CD  . ARG A 20  ? 2.8823 1.3801 1.8094 0.3085  0.0367  -0.3827 20  ARG A CD  
146  N  NE  . ARG A 20  ? 2.8890 1.4020 1.7545 0.3688  0.0689  -0.3344 20  ARG A NE  
147  C  CZ  . ARG A 20  ? 2.9321 1.4256 1.7292 0.4116  0.0361  -0.3396 20  ARG A CZ  
148  N  NH1 . ARG A 20  ? 3.0121 1.4715 1.7924 0.4026  -0.0350 -0.3931 20  ARG A NH1 
149  N  NH2 . ARG A 20  ? 2.8858 1.3945 1.6330 0.4628  0.0734  -0.2900 20  ARG A NH2 
150  N  N   . LEU A 21  ? 2.2415 1.0991 1.6686 0.1109  0.1189  -0.3504 21  LEU A N   
151  C  CA  . LEU A 21  ? 2.0653 1.0356 1.6084 0.0875  0.1108  -0.3516 21  LEU A CA  
152  C  C   . LEU A 21  ? 1.9760 0.9962 1.6373 0.0210  0.1024  -0.3842 21  LEU A C   
153  O  O   . LEU A 21  ? 1.9169 1.0148 1.6740 -0.0001 0.0751  -0.4067 21  LEU A O   
154  C  CB  . LEU A 21  ? 1.8018 0.8322 1.3625 0.1033  0.1622  -0.2977 21  LEU A CB  
155  C  CG  . LEU A 21  ? 1.7720 0.8963 1.4098 0.1043  0.1516  -0.2912 21  LEU A CG  
156  C  CD1 . LEU A 21  ? 1.7966 0.8967 1.3756 0.1504  0.1111  -0.2983 21  LEU A CD1 
157  C  CD2 . LEU A 21  ? 1.6252 0.8014 1.2830 0.1109  0.2019  -0.2402 21  LEU A CD2 
158  N  N   . LEU A 22  ? 1.9969 0.9728 1.6538 -0.0109 0.1276  -0.3856 22  LEU A N   
159  C  CA  . LEU A 22  ? 2.0322 1.0462 1.7964 -0.0757 0.1233  -0.4151 22  LEU A CA  
160  C  C   . LEU A 22  ? 2.1533 1.1440 1.9432 -0.0965 0.0590  -0.4706 22  LEU A C   
161  O  O   . LEU A 22  ? 2.2384 1.2919 2.1454 -0.1470 0.0449  -0.4985 22  LEU A O   
162  C  CB  . LEU A 22  ? 2.0643 1.0251 1.8061 -0.1025 0.1688  -0.3976 22  LEU A CB  
163  C  CG  . LEU A 22  ? 1.9860 1.0083 1.7732 -0.1184 0.2282  -0.3564 22  LEU A CG  
164  C  CD1 . LEU A 22  ? 1.9712 0.9858 1.6799 -0.0641 0.2588  -0.3077 22  LEU A CD1 
165  C  CD2 . LEU A 22  ? 1.9878 0.9657 1.7820 -0.1613 0.2611  -0.3527 22  LEU A CD2 
166  N  N   . GLU A 23  ? 2.2163 1.1189 1.8996 -0.0580 0.0194  -0.4873 23  GLU A N   
167  C  CA  . GLU A 23  ? 2.3047 1.1767 2.0024 -0.0763 -0.0496 -0.5421 23  GLU A CA  
168  C  C   . GLU A 23  ? 2.2058 1.1783 2.0063 -0.0829 -0.0943 -0.5660 23  GLU A C   
169  O  O   . GLU A 23  ? 2.2540 1.2414 2.1245 -0.1175 -0.1469 -0.6117 23  GLU A O   
170  C  CB  . GLU A 23  ? 2.4879 1.2385 2.0307 -0.0250 -0.0820 -0.5531 23  GLU A CB  
171  C  CG  . GLU A 23  ? 2.5877 1.2303 2.0240 -0.0127 -0.0397 -0.5324 23  GLU A CG  
172  C  CD  . GLU A 23  ? 2.7654 1.2785 2.0486 0.0343  -0.0751 -0.5527 23  GLU A CD  
173  O  OE1 . GLU A 23  ? 2.8425 1.3351 2.1161 0.0347  -0.1441 -0.5977 23  GLU A OE1 
174  O  OE2 . GLU A 23  ? 2.8319 1.2630 2.0024 0.0732  -0.0344 -0.5240 23  GLU A OE2 
175  N  N   . LEU A 24  ? 2.1688 1.2100 1.9839 -0.0511 -0.0758 -0.5361 24  LEU A N   
176  C  CA  . LEU A 24  ? 1.9077 1.0448 1.8233 -0.0546 -0.1130 -0.5555 24  LEU A CA  
177  C  C   . LEU A 24  ? 1.9137 1.1473 1.9854 -0.1156 -0.0931 -0.5675 24  LEU A C   
178  O  O   . LEU A 24  ? 1.8835 1.1449 1.9832 -0.1361 -0.0315 -0.5374 24  LEU A O   
179  C  CB  . LEU A 24  ? 1.8441 1.0182 1.7282 -0.0051 -0.0935 -0.5170 24  LEU A CB  
180  C  CG  . LEU A 24  ? 1.9184 1.0044 1.6475 0.0579  -0.0928 -0.4913 24  LEU A CG  
181  C  CD1 . LEU A 24  ? 1.8395 0.9601 1.5503 0.0869  -0.0382 -0.4364 24  LEU A CD1 
182  C  CD2 . LEU A 24  ? 1.9925 1.0529 1.6745 0.0943  -0.1618 -0.5187 24  LEU A CD2 
183  N  N   . ASP A 25  ? 1.8676 1.1534 2.0407 -0.1434 -0.1449 -0.6107 25  ASP A N   
184  C  CA  . ASP A 25  ? 1.8155 1.2027 2.1450 -0.1974 -0.1242 -0.6222 25  ASP A CA  
185  C  C   . ASP A 25  ? 1.7357 1.2210 2.1298 -0.1771 -0.1048 -0.6036 25  ASP A C   
186  O  O   . ASP A 25  ? 1.6312 1.1030 1.9510 -0.1260 -0.1056 -0.5793 25  ASP A O   
187  C  CB  . ASP A 25  ? 1.8589 1.2713 2.2854 -0.2368 -0.1851 -0.6743 25  ASP A CB  
188  C  CG  . ASP A 25  ? 1.8666 1.2934 2.2897 -0.1992 -0.2630 -0.7027 25  ASP A CG  
189  O  OD1 . ASP A 25  ? 1.8154 1.2684 2.2070 -0.1508 -0.2633 -0.6825 25  ASP A OD1 
190  O  OD2 . ASP A 25  ? 1.9253 1.3346 2.3773 -0.2193 -0.3268 -0.7453 25  ASP A OD2 
191  N  N   . ASP A 26  ? 1.9064 0.7968 1.8384 -0.1268 -0.1618 -0.1009 26  ASP A N   
192  C  CA  . ASP A 26  ? 1.8497 0.8341 1.7692 -0.1196 -0.1512 -0.0640 26  ASP A CA  
193  C  C   . ASP A 26  ? 1.9029 0.9930 1.8216 -0.0976 -0.1661 -0.1065 26  ASP A C   
194  O  O   . ASP A 26  ? 1.9923 1.1495 1.8907 -0.0753 -0.1609 -0.0804 26  ASP A O   
195  C  CB  . ASP A 26  ? 1.8529 0.8501 1.7998 -0.1805 -0.1320 -0.0280 26  ASP A CB  
196  C  CG  . ASP A 26  ? 2.0494 1.0292 2.0447 -0.2444 -0.1320 -0.0684 26  ASP A CG  
197  O  OD1 . ASP A 26  ? 2.1932 1.1612 2.2056 -0.2393 -0.1502 -0.1307 26  ASP A OD1 
198  O  OD2 . ASP A 26  ? 2.1249 1.1094 2.1430 -0.3015 -0.1124 -0.0408 26  ASP A OD2 
199  N  N   . ASP A 27  ? 1.9084 1.0125 1.8465 -0.1002 -0.1852 -0.1725 27  ASP A N   
200  C  CA  . ASP A 27  ? 1.8008 1.0023 1.7273 -0.0698 -0.2025 -0.2128 27  ASP A CA  
201  C  C   . ASP A 27  ? 1.7048 0.9110 1.5750 -0.0025 -0.2072 -0.2074 27  ASP A C   
202  O  O   . ASP A 27  ? 1.6277 0.8883 1.4645 0.0258  -0.2024 -0.1812 27  ASP A O   
203  C  CB  . ASP A 27  ? 1.9137 1.1397 1.8795 -0.0903 -0.2230 -0.2910 27  ASP A CB  
204  C  CG  . ASP A 27  ? 1.9861 1.3253 1.9438 -0.0648 -0.2424 -0.3318 27  ASP A CG  
205  O  OD1 . ASP A 27  ? 2.0440 1.4389 2.0486 -0.0998 -0.2532 -0.3828 27  ASP A OD1 
206  O  OD2 . ASP A 27  ? 1.9995 1.3717 1.9026 -0.0096 -0.2465 -0.3140 27  ASP A OD2 
207  N  N   . GLN A 28  ? 1.7765 0.9260 1.6361 0.0225  -0.2156 -0.2343 28  GLN A N   
208  C  CA  . GLN A 28  ? 1.7254 0.8900 1.5326 0.0836  -0.2176 -0.2349 28  GLN A CA  
209  C  C   . GLN A 28  ? 1.7029 0.8511 1.4816 0.1005  -0.1948 -0.1704 28  GLN A C   
210  O  O   . GLN A 28  ? 1.6840 0.8704 1.4198 0.1406  -0.1879 -0.1590 28  GLN A O   
211  C  CB  . GLN A 28  ? 1.6946 0.8104 1.5034 0.1069  -0.2334 -0.2855 28  GLN A CB  
212  C  CG  . GLN A 28  ? 1.7619 0.7715 1.6044 0.0773  -0.2311 -0.2792 28  GLN A CG  
213  C  CD  . GLN A 28  ? 1.8406 0.8105 1.7180 0.0685  -0.2531 -0.3513 28  GLN A CD  
214  O  OE1 . GLN A 28  ? 1.8250 0.8178 1.7449 0.0277  -0.2613 -0.3906 28  GLN A OE1 
215  N  NE2 . GLN A 28  ? 1.8673 0.7836 1.7314 0.1073  -0.2635 -0.3753 28  GLN A NE2 
216  N  N   . HIS A 29  ? 1.6792 0.7742 1.4798 0.0700  -0.1814 -0.1290 29  HIS A N   
217  C  CA  . HIS A 29  ? 1.6070 0.7021 1.3867 0.0859  -0.1613 -0.0730 29  HIS A CA  
218  C  C   . HIS A 29  ? 1.6060 0.7821 1.3738 0.0873  -0.1509 -0.0484 29  HIS A C   
219  O  O   . HIS A 29  ? 1.6098 0.8143 1.3468 0.1191  -0.1388 -0.0297 29  HIS A O   
220  C  CB  . HIS A 29  ? 1.6259 0.6572 1.4276 0.0538  -0.1513 -0.0334 29  HIS A CB  
221  C  CG  . HIS A 29  ? 1.6889 0.6345 1.4779 0.0797  -0.1541 -0.0300 29  HIS A CG  
222  N  ND1 . HIS A 29  ? 1.6515 0.6072 1.4107 0.1299  -0.1496 -0.0225 29  HIS A ND1 
223  C  CD2 . HIS A 29  ? 1.7544 0.6008 1.5565 0.0635  -0.1613 -0.0351 29  HIS A CD2 
224  C  CE1 . HIS A 29  ? 1.7006 0.5730 1.4545 0.1497  -0.1577 -0.0262 29  HIS A CE1 
225  N  NE2 . HIS A 29  ? 1.7938 0.5905 1.5708 0.1110  -0.1653 -0.0312 29  HIS A NE2 
226  N  N   . LEU A 30  ? 1.5602 0.7745 1.3542 0.0519  -0.1552 -0.0516 30  LEU A N   
227  C  CA  . LEU A 30  ? 1.4436 0.7287 1.2285 0.0557  -0.1497 -0.0323 30  LEU A CA  
228  C  C   . LEU A 30  ? 1.4927 0.8149 1.2337 0.0977  -0.1572 -0.0540 30  LEU A C   
229  O  O   . LEU A 30  ? 1.4930 0.8465 1.2083 0.1158  -0.1459 -0.0274 30  LEU A O   
230  C  CB  . LEU A 30  ? 1.3767 0.7031 1.2010 0.0131  -0.1571 -0.0426 30  LEU A CB  
231  C  CG  . LEU A 30  ? 1.3811 0.6904 1.2413 -0.0321 -0.1429 -0.0080 30  LEU A CG  
232  C  CD1 . LEU A 30  ? 1.4024 0.7512 1.3060 -0.0802 -0.1507 -0.0355 30  LEU A CD1 
233  C  CD2 . LEU A 30  ? 1.2758 0.6192 1.1293 -0.0232 -0.1265 0.0396  30  LEU A CD2 
234  N  N   . GLN A 31  ? 1.5529 0.8706 1.2830 0.1140  -0.1754 -0.1022 31  GLN A N   
235  C  CA  . GLN A 31  ? 1.5560 0.9118 1.2347 0.1572  -0.1829 -0.1211 31  GLN A CA  
236  C  C   . GLN A 31  ? 1.5404 0.8825 1.1738 0.1915  -0.1625 -0.0951 31  GLN A C   
237  O  O   . GLN A 31  ? 1.5796 0.9504 1.1649 0.2184  -0.1546 -0.0813 31  GLN A O   
238  C  CB  . GLN A 31  ? 1.6517 1.0169 1.3318 0.1692  -0.2086 -0.1849 31  GLN A CB  
239  C  CG  . GLN A 31  ? 1.7079 1.1278 1.3342 0.2126  -0.2224 -0.2078 31  GLN A CG  
240  C  CD  . GLN A 31  ? 1.8400 1.2594 1.4310 0.2522  -0.2313 -0.2470 31  GLN A CD  
241  O  OE1 . GLN A 31  ? 1.8590 1.2436 1.4384 0.2637  -0.2166 -0.2350 31  GLN A OE1 
242  N  NE2 . GLN A 31  ? 1.8855 1.3534 1.4596 0.2772  -0.2572 -0.2990 31  GLN A NE2 
243  N  N   . ARG A 32  ? 1.5363 0.8347 1.1824 0.1913  -0.1529 -0.0888 32  ARG A N   
244  C  CA  . ARG A 32  ? 1.5639 0.8641 1.1740 0.2224  -0.1326 -0.0721 32  ARG A CA  
245  C  C   . ARG A 32  ? 1.5529 0.8707 1.1624 0.2129  -0.1067 -0.0217 32  ARG A C   
246  O  O   . ARG A 32  ? 1.5669 0.9092 1.1390 0.2320  -0.0870 -0.0063 32  ARG A O   
247  C  CB  . ARG A 32  ? 1.6462 0.9006 1.2720 0.2321  -0.1349 -0.0881 32  ARG A CB  
248  C  CG  . ARG A 32  ? 1.7449 0.9696 1.3856 0.2347  -0.1620 -0.1419 32  ARG A CG  
249  C  CD  . ARG A 32  ? 1.7568 0.9941 1.3640 0.2790  -0.1668 -0.1805 32  ARG A CD  
250  N  NE  . ARG A 32  ? 1.7284 0.9271 1.3437 0.2966  -0.1623 -0.1816 32  ARG A NE  
251  C  CZ  . ARG A 32  ? 1.7710 0.9302 1.3988 0.3148  -0.1825 -0.2278 32  ARG A CZ  
252  N  NH1 . ARG A 32  ? 1.7663 0.9235 1.4047 0.3127  -0.2064 -0.2779 32  ARG A NH1 
253  N  NH2 . ARG A 32  ? 1.8330 0.9577 1.4647 0.3379  -0.1810 -0.2291 32  ARG A NH2 
254  N  N   . ILE A 33  ? 1.5265 0.8339 1.1784 0.1815  -0.1046 0.0031  33  ILE A N   
255  C  CA  . ILE A 33  ? 1.4573 0.7914 1.1169 0.1715  -0.0839 0.0433  33  ILE A CA  
256  C  C   . ILE A 33  ? 1.5026 0.8708 1.1383 0.1744  -0.0846 0.0488  33  ILE A C   
257  O  O   . ILE A 33  ? 1.4747 0.8595 1.0915 0.1819  -0.0640 0.0726  33  ILE A O   
258  C  CB  . ILE A 33  ? 1.3748 0.6997 1.0819 0.1396  -0.0849 0.0649  33  ILE A CB  
259  C  CG1 . ILE A 33  ? 1.3320 0.6143 1.0496 0.1467  -0.0816 0.0692  33  ILE A CG1 
260  C  CG2 . ILE A 33  ? 1.3190 0.6857 1.0396 0.1294  -0.0689 0.0969  33  ILE A CG2 
261  C  CD1 . ILE A 33  ? 1.2674 0.5694 0.9742 0.1717  -0.0604 0.0833  33  ILE A CD1 
262  N  N   . GLU A 34  ? 1.5502 0.9280 1.1864 0.1697  -0.1087 0.0239  34  GLU A N   
263  C  CA  . GLU A 34  ? 1.5533 0.9602 1.1597 0.1824  -0.1157 0.0252  34  GLU A CA  
264  C  C   . GLU A 34  ? 1.5796 0.9821 1.1184 0.2192  -0.1041 0.0286  34  GLU A C   
265  O  O   . GLU A 34  ? 1.5623 0.9680 1.0690 0.2290  -0.0907 0.0551  34  GLU A O   
266  C  CB  . GLU A 34  ? 1.6238 1.0529 1.2449 0.1762  -0.1470 -0.0133 34  GLU A CB  
267  C  CG  . GLU A 34  ? 1.7170 1.1803 1.3101 0.1950  -0.1612 -0.0163 34  GLU A CG  
268  C  CD  . GLU A 34  ? 1.7750 1.2784 1.3965 0.1858  -0.1928 -0.0617 34  GLU A CD  
269  O  OE1 . GLU A 34  ? 1.7567 1.2571 1.4256 0.1551  -0.1990 -0.0869 34  GLU A OE1 
270  O  OE2 . GLU A 34  ? 1.7903 1.3276 1.3869 0.2096  -0.2114 -0.0740 34  GLU A OE2 
271  N  N   . ARG A 35  ? 1.6509 1.0441 1.1659 0.2392  -0.1078 0.0021  35  ARG A N   
272  C  CA  . ARG A 35  ? 1.6585 1.0552 1.1052 0.2729  -0.0930 0.0059  35  ARG A CA  
273  C  C   . ARG A 35  ? 1.6322 1.0232 1.0722 0.2681  -0.0549 0.0397  35  ARG A C   
274  O  O   . ARG A 35  ? 1.6716 1.0660 1.0546 0.2855  -0.0331 0.0561  35  ARG A O   
275  C  CB  . ARG A 35  ? 1.6651 1.0661 1.0942 0.2969  -0.1085 -0.0389 35  ARG A CB  
276  C  CG  . ARG A 35  ? 1.6988 1.1185 1.1264 0.3079  -0.1448 -0.0821 35  ARG A CG  
277  C  CD  . ARG A 35  ? 1.8131 1.2359 1.2437 0.3252  -0.1613 -0.1341 35  ARG A CD  
278  N  NE  . ARG A 35  ? 1.9368 1.3704 1.3101 0.3588  -0.1426 -0.1322 35  ARG A NE  
279  C  CZ  . ARG A 35  ? 2.0200 1.4548 1.3986 0.3749  -0.1473 -0.1695 35  ARG A CZ  
280  N  NH1 . ARG A 35  ? 2.0114 1.4225 1.4492 0.3599  -0.1705 -0.2093 35  ARG A NH1 
281  N  NH2 . ARG A 35  ? 2.1111 1.5698 1.4361 0.4049  -0.1277 -0.1681 35  ARG A NH2 
282  N  N   . PHE A 36  ? 1.5750 0.9606 1.0703 0.2449  -0.0454 0.0495  36  PHE A N   
283  C  CA  . PHE A 36  ? 1.5394 0.9341 1.0380 0.2404  -0.0106 0.0727  36  PHE A CA  
284  C  C   . PHE A 36  ? 1.5268 0.9268 1.0310 0.2227  0.0075  0.1076  36  PHE A C   
285  O  O   . PHE A 36  ? 1.5854 0.9906 1.0627 0.2232  0.0391  0.1259  36  PHE A O   
286  C  CB  . PHE A 36  ? 1.4686 0.8600 1.0197 0.2318  -0.0111 0.0658  36  PHE A CB  
287  C  CG  . PHE A 36  ? 1.4400 0.8563 1.0025 0.2308  0.0213  0.0792  36  PHE A CG  
288  C  CD1 . PHE A 36  ? 1.4860 0.9244 1.0105 0.2467  0.0464  0.0717  36  PHE A CD1 
289  C  CD2 . PHE A 36  ? 1.3780 0.8058 0.9903 0.2137  0.0278  0.0955  36  PHE A CD2 
290  C  CE1 . PHE A 36  ? 1.4369 0.9104 0.9793 0.2419  0.0782  0.0764  36  PHE A CE1 
291  C  CE2 . PHE A 36  ? 1.3246 0.7880 0.9535 0.2144  0.0563  0.0990  36  PHE A CE2 
292  C  CZ  . PHE A 36  ? 1.3798 0.8673 0.9770 0.2267  0.0819  0.0874  36  PHE A CZ  
293  N  N   . LEU A 37  ? 1.4657 0.8661 1.0067 0.2051  -0.0107 0.1143  37  LEU A N   
294  C  CA  . LEU A 37  ? 1.3679 0.7737 0.9169 0.1923  0.0012  0.1406  37  LEU A CA  
295  C  C   . LEU A 37  ? 1.4390 0.8247 0.9219 0.2118  0.0022  0.1508  37  LEU A C   
296  O  O   . LEU A 37  ? 1.4721 0.8448 0.9387 0.2071  0.0261  0.1760  37  LEU A O   
297  C  CB  . LEU A 37  ? 1.2332 0.6551 0.8357 0.1726  -0.0214 0.1395  37  LEU A CB  
298  C  CG  . LEU A 37  ? 1.2364 0.6706 0.8946 0.1544  -0.0228 0.1371  37  LEU A CG  
299  C  CD1 . LEU A 37  ? 1.2079 0.6594 0.9062 0.1338  -0.0462 0.1333  37  LEU A CD1 
300  C  CD2 . LEU A 37  ? 1.2368 0.6915 0.9225 0.1471  0.0055  0.1542  37  LEU A CD2 
301  N  N   . ASP A 38  ? 1.5407 0.9213 0.9836 0.2352  -0.0238 0.1303  38  ASP A N   
302  C  CA  . ASP A 38  ? 1.6586 1.0186 1.0226 0.2643  -0.0236 0.1411  38  ASP A CA  
303  C  C   . ASP A 38  ? 1.6568 1.0017 0.9680 0.2707  0.0160  0.1617  38  ASP A C   
304  O  O   . ASP A 38  ? 1.6584 0.9723 0.9096 0.2809  0.0340  0.1909  38  ASP A O   
305  C  CB  . ASP A 38  ? 1.7901 1.1628 1.1233 0.2930  -0.0599 0.1063  38  ASP A CB  
306  C  CG  . ASP A 38  ? 1.8668 1.2608 1.2412 0.2875  -0.0967 0.0851  38  ASP A CG  
307  O  OD1 . ASP A 38  ? 1.8581 1.2562 1.2787 0.2642  -0.0943 0.1007  38  ASP A OD1 
308  O  OD2 . ASP A 38  ? 1.9049 1.3207 1.2685 0.3064  -0.1277 0.0480  38  ASP A OD2 
309  N  N   . ALA A 39  ? 1.6596 1.0250 0.9906 0.2649  0.0309  0.1464  39  ALA A N   
310  C  CA  . ALA A 39  ? 1.6868 1.0551 0.9772 0.2663  0.0718  0.1597  39  ALA A CA  
311  C  C   . ALA A 39  ? 1.6719 1.0383 0.9959 0.2343  0.1099  0.1865  39  ALA A C   
312  O  O   . ALA A 39  ? 1.7137 1.0695 0.9940 0.2281  0.1488  0.2087  39  ALA A O   
313  C  CB  . ALA A 39  ? 1.5862 0.9867 0.8920 0.2757  0.0711  0.1257  39  ALA A CB  
314  N  N   . LEU A 40  ? 1.5662 0.9458 0.9670 0.2123  0.1010  0.1833  40  LEU A N   
315  C  CA  . LEU A 40  ? 1.5087 0.9004 0.9541 0.1833  0.1335  0.1982  40  LEU A CA  
316  C  C   . LEU A 40  ? 1.6552 1.0074 1.0788 0.1731  0.1456  0.2281  40  LEU A C   
317  O  O   . LEU A 40  ? 1.7069 1.0561 1.1397 0.1499  0.1847  0.2425  40  LEU A O   
318  C  CB  . LEU A 40  ? 1.3609 0.7842 0.8892 0.1697  0.1161  0.1845  40  LEU A CB  
319  C  CG  . LEU A 40  ? 1.2550 0.7141 0.8173 0.1741  0.1186  0.1611  40  LEU A CG  
320  C  CD1 . LEU A 40  ? 1.1420 0.6230 0.7733 0.1638  0.1016  0.1570  40  LEU A CD1 
321  C  CD2 . LEU A 40  ? 1.2210 0.7110 0.7808 0.1665  0.1624  0.1579  40  LEU A CD2 
322  N  N   . ALA A 41  ? 1.6624 0.9849 1.0601 0.1905  0.1123  0.2336  41  ALA A N   
323  C  CA  . ALA A 41  ? 1.6239 0.9039 1.0064 0.1871  0.1154  0.2582  41  ALA A CA  
324  C  C   . ALA A 41  ? 1.7522 0.9789 1.0629 0.1849  0.1563  0.2907  41  ALA A C   
325  O  O   . ALA A 41  ? 1.8395 1.0382 1.1699 0.1614  0.1811  0.3084  41  ALA A O   
326  C  CB  . ALA A 41  ? 1.5907 0.8570 0.9502 0.2157  0.0678  0.2510  41  ALA A CB  
327  N  N   . PRO A 42  ? 1.8222 1.0319 1.0495 0.2064  0.1671  0.2999  42  PRO A N   
328  C  CA  . PRO A 42  ? 1.8527 1.0033 1.0016 0.2016  0.2096  0.3390  42  PRO A CA  
329  C  C   . PRO A 42  ? 1.7655 0.9362 0.9458 0.1580  0.2676  0.3438  42  PRO A C   
330  O  O   . PRO A 42  ? 1.8719 0.9993 0.9876 0.1457  0.3114  0.3755  42  PRO A O   
331  C  CB  . PRO A 42  ? 1.9565 1.1021 1.0080 0.2416  0.2002  0.3420  42  PRO A CB  
332  C  CG  . PRO A 42  ? 1.9638 1.1521 1.0452 0.2701  0.1441  0.3030  42  PRO A CG  
333  C  CD  . PRO A 42  ? 1.8576 1.0951 1.0507 0.2388  0.1385  0.2761  42  PRO A CD  
334  N  N   . LEU A 43  ? 1.6664 0.9043 0.9424 0.1346  0.2700  0.3125  43  LEU A N   
335  C  CA  . LEU A 43  ? 1.6670 0.9432 0.9836 0.0958  0.3219  0.3057  43  LEU A CA  
336  C  C   . LEU A 43  ? 1.6289 0.8906 1.0087 0.0586  0.3433  0.3113  43  LEU A C   
337  O  O   . LEU A 43  ? 1.6353 0.8910 1.0173 0.0223  0.3959  0.3203  43  LEU A O   
338  C  CB  . LEU A 43  ? 1.6661 1.0297 1.0468 0.0987  0.3127  0.2636  43  LEU A CB  
339  C  CG  . LEU A 43  ? 1.7717 1.1610 1.0964 0.1246  0.3126  0.2508  43  LEU A CG  
340  C  CD1 . LEU A 43  ? 1.7534 1.1379 1.0677 0.1629  0.2557  0.2353  43  LEU A CD1 
341  C  CD2 . LEU A 43  ? 1.7711 1.2406 1.1460 0.1122  0.3383  0.2166  43  LEU A CD2 
342  N  N   . HIS A 44  ? 1.5842 0.8471 1.0198 0.0645  0.3053  0.3018  44  HIS A N   
343  C  CA  . HIS A 44  ? 1.5548 0.8021 1.0482 0.0350  0.3197  0.3034  44  HIS A CA  
344  C  C   . HIS A 44  ? 1.5735 0.8058 1.0908 0.0568  0.2680  0.3004  44  HIS A C   
345  O  O   . HIS A 44  ? 1.6452 0.9161 1.1756 0.0811  0.2266  0.2841  44  HIS A O   
346  C  CB  . HIS A 44  ? 1.3993 0.7331 0.9905 0.0035  0.3445  0.2688  44  HIS A CB  
347  C  CG  . HIS A 44  ? 1.4243 0.7474 1.0764 -0.0298 0.3653  0.2642  44  HIS A CG  
348  N  ND1 . HIS A 44  ? 1.5354 0.8098 1.1703 -0.0670 0.4181  0.2800  44  HIS A ND1 
349  C  CD2 . HIS A 44  ? 1.3715 0.7217 1.0988 -0.0316 0.3400  0.2451  44  HIS A CD2 
350  C  CE1 . HIS A 44  ? 1.5668 0.8362 1.2699 -0.0908 0.4233  0.2669  44  HIS A CE1 
351  N  NE2 . HIS A 44  ? 1.4543 0.7744 1.2141 -0.0674 0.3750  0.2443  44  HIS A NE2 
352  N  N   . PRO A 45  ? 1.5053 0.6832 1.0307 0.0475  0.2700  0.3130  45  PRO A N   
353  C  CA  . PRO A 45  ? 1.4500 0.6269 1.0030 0.0700  0.2199  0.3036  45  PRO A CA  
354  C  C   . PRO A 45  ? 1.4066 0.6813 1.0525 0.0663  0.1941  0.2684  45  PRO A C   
355  O  O   . PRO A 45  ? 1.4432 0.7368 1.0997 0.0885  0.1494  0.2588  45  PRO A O   
356  C  CB  . PRO A 45  ? 1.4716 0.5824 1.0353 0.0534  0.2368  0.3150  45  PRO A CB  
357  C  CG  . PRO A 45  ? 1.5584 0.6217 1.0642 0.0345  0.2783  0.3389  45  PRO A CG  
358  C  CD  . PRO A 45  ? 1.5594 0.6645 1.0571 0.0192  0.3162  0.3375  45  PRO A CD  
359  N  N   . VAL A 46  ? 1.2750 0.6159 0.9860 0.0401  0.2212  0.2483  46  VAL A N   
360  C  CA  . VAL A 46  ? 1.2142 0.6434 1.0032 0.0412  0.1973  0.2203  46  VAL A CA  
361  C  C   . VAL A 46  ? 1.3319 0.7851 1.0970 0.0640  0.1690  0.2179  46  VAL A C   
362  O  O   . VAL A 46  ? 1.2853 0.7906 1.0955 0.0696  0.1413  0.2039  46  VAL A O   
363  C  CB  . VAL A 46  ? 1.1343 0.6319 0.9955 0.0145  0.2316  0.1960  46  VAL A CB  
364  C  CG1 . VAL A 46  ? 1.1583 0.6897 1.0029 0.0171  0.2503  0.1896  46  VAL A CG1 
365  C  CG2 . VAL A 46  ? 1.0547 0.6320 0.9988 0.0161  0.2075  0.1704  46  VAL A CG2 
366  N  N   . LEU A 47  ? 1.3786 0.7938 1.0728 0.0765  0.1761  0.2307  47  LEU A N   
367  C  CA  . LEU A 47  ? 1.3279 0.7565 0.9987 0.0979  0.1489  0.2238  47  LEU A CA  
368  C  C   . LEU A 47  ? 1.3989 0.7891 1.0224 0.1215  0.1110  0.2306  47  LEU A C   
369  O  O   . LEU A 47  ? 1.4475 0.8395 1.0438 0.1384  0.0900  0.2223  47  LEU A O   
370  C  CB  . LEU A 47  ? 1.3197 0.7449 0.9467 0.1022  0.1751  0.2233  47  LEU A CB  
371  C  CG  . LEU A 47  ? 1.2506 0.7187 0.9158 0.0798  0.2181  0.2120  47  LEU A CG  
372  C  CD1 . LEU A 47  ? 1.2181 0.6861 0.8310 0.0860  0.2439  0.2100  47  LEU A CD1 
373  C  CD2 . LEU A 47  ? 1.1577 0.6959 0.8997 0.0789  0.2061  0.1876  47  LEU A CD2 
374  N  N   . GLU A 48  ? 1.3752 0.7339 0.9914 0.1250  0.1001  0.2399  48  GLU A N   
375  C  CA  . GLU A 48  ? 1.4079 0.7368 0.9754 0.1535  0.0630  0.2412  48  GLU A CA  
376  C  C   . GLU A 48  ? 1.4598 0.8431 1.0796 0.1549  0.0234  0.2179  48  GLU A C   
377  O  O   . GLU A 48  ? 1.5994 0.9862 1.1924 0.1733  -0.0065 0.2060  48  GLU A O   
378  C  CB  . GLU A 48  ? 1.4105 0.6775 0.9414 0.1640  0.0647  0.2595  48  GLU A CB  
379  C  CG  . GLU A 48  ? 1.5357 0.7311 0.9889 0.1659  0.1021  0.2900  48  GLU A CG  
380  C  CD  . GLU A 48  ? 1.6582 0.7908 1.0789 0.1752  0.0999  0.3071  48  GLU A CD  
381  O  OE1 . GLU A 48  ? 1.7691 0.8573 1.1469 0.1642  0.1335  0.3294  48  GLU A OE1 
382  O  OE2 . GLU A 48  ? 1.6560 0.7930 1.1001 0.1920  0.0633  0.2943  48  GLU A OE2 
383  N  N   . ASN A 49  ? 1.3674 0.7995 1.0621 0.1345  0.0240  0.2088  49  ASN A N   
384  C  CA  . ASN A 49  ? 1.2496 0.7385 0.9936 0.1307  -0.0081 0.1902  49  ASN A CA  
385  C  C   . ASN A 49  ? 1.1725 0.7118 0.9681 0.1109  0.0012  0.1856  49  ASN A C   
386  O  O   . ASN A 49  ? 1.2638 0.8186 1.0879 0.0994  0.0285  0.1894  49  ASN A O   
387  C  CB  . ASN A 49  ? 1.2078 0.7179 0.9903 0.1305  -0.0211 0.1824  49  ASN A CB  
388  C  CG  . ASN A 49  ? 1.2294 0.6757 0.9558 0.1561  -0.0307 0.1897  49  ASN A CG  
389  O  OD1 . ASN A 49  ? 1.2828 0.6728 0.9848 0.1548  -0.0040 0.2075  49  ASN A OD1 
390  N  ND2 . ASN A 49  ? 1.1773 0.6307 0.8806 0.1800  -0.0684 0.1751  49  ASN A ND2 
391  N  N   . TRP A 50  ? 1.0978 0.6618 0.9044 0.1077  -0.0214 0.1759  50  TRP A N   
392  C  CA  . TRP A 50  ? 1.0529 0.6497 0.8964 0.0931  -0.0163 0.1767  50  TRP A CA  
393  C  C   . TRP A 50  ? 0.9964 0.6435 0.8804 0.0785  -0.0389 0.1689  50  TRP A C   
394  O  O   . TRP A 50  ? 0.9499 0.6034 0.8262 0.0799  -0.0626 0.1556  50  TRP A O   
395  C  CB  . TRP A 50  ? 1.0572 0.6167 0.8654 0.0999  -0.0142 0.1761  50  TRP A CB  
396  C  CG  . TRP A 50  ? 1.0579 0.5869 0.8324 0.1115  0.0125  0.1818  50  TRP A CG  
397  C  CD1 . TRP A 50  ? 1.1478 0.6365 0.8671 0.1257  0.0192  0.1850  50  TRP A CD1 
398  C  CD2 . TRP A 50  ? 1.0332 0.5774 0.8254 0.1104  0.0376  0.1835  50  TRP A CD2 
399  N  NE1 . TRP A 50  ? 1.2068 0.6861 0.9096 0.1275  0.0507  0.1899  50  TRP A NE1 
400  C  CE2 . TRP A 50  ? 1.1445 0.6618 0.8954 0.1187  0.0614  0.1851  50  TRP A CE2 
401  C  CE3 . TRP A 50  ? 1.0029 0.5854 0.8386 0.1062  0.0419  0.1827  50  TRP A CE3 
402  C  CZ2 . TRP A 50  ? 1.1945 0.7309 0.9546 0.1193  0.0898  0.1801  50  TRP A CZ2 
403  C  CZ3 . TRP A 50  ? 1.0543 0.6527 0.8962 0.1137  0.0659  0.1771  50  TRP A CZ3 
404  C  CH2 . TRP A 50  ? 1.1470 0.7268 0.9555 0.1183  0.0899  0.1730  50  TRP A CH2 
405  N  N   . TYR A 51  ? 0.9609 0.6503 0.8863 0.0659  -0.0308 0.1756  51  TYR A N   
406  C  CA  . TYR A 51  ? 0.8925 0.6397 0.8564 0.0486  -0.0452 0.1728  51  TYR A CA  
407  C  C   . TYR A 51  ? 0.9480 0.6915 0.9155 0.0369  -0.0407 0.1874  51  TYR A C   
408  O  O   . TYR A 51  ? 1.0097 0.7172 0.9596 0.0478  -0.0273 0.1970  51  TYR A O   
409  C  CB  . TYR A 51  ? 0.7515 0.5651 0.7625 0.0476  -0.0408 0.1684  51  TYR A CB  
410  C  CG  . TYR A 51  ? 0.7738 0.5832 0.7856 0.0594  -0.0466 0.1540  51  TYR A CG  
411  C  CD1 . TYR A 51  ? 0.8307 0.5870 0.8176 0.0712  -0.0286 0.1582  51  TYR A CD1 
412  C  CD2 . TYR A 51  ? 0.7823 0.6397 0.8187 0.0588  -0.0693 0.1358  51  TYR A CD2 
413  C  CE1 . TYR A 51  ? 0.8985 0.6330 0.8793 0.0819  -0.0325 0.1504  51  TYR A CE1 
414  C  CE2 . TYR A 51  ? 0.8351 0.6772 0.8683 0.0756  -0.0781 0.1224  51  TYR A CE2 
415  C  CZ  . TYR A 51  ? 0.8992 0.6718 0.9021 0.0869  -0.0593 0.1326  51  TYR A CZ  
416  O  OH  . TYR A 51  ? 0.9438 0.6837 0.9368 0.1034  -0.0667 0.1245  51  TYR A OH  
417  N  N   . LEU A 52  ? 0.9272 0.7076 0.9156 0.0151  -0.0516 0.1887  52  LEU A N   
418  C  CA  . LEU A 52  ? 0.9393 0.7154 0.9303 0.0023  -0.0446 0.2103  52  LEU A CA  
419  C  C   . LEU A 52  ? 0.9277 0.7561 0.9426 0.0136  -0.0315 0.2236  52  LEU A C   
420  O  O   . LEU A 52  ? 1.0066 0.9007 1.0538 0.0171  -0.0318 0.2119  52  LEU A O   
421  C  CB  . LEU A 52  ? 0.9489 0.7535 0.9548 -0.0311 -0.0544 0.2099  52  LEU A CB  
422  C  CG  . LEU A 52  ? 0.9736 0.7474 0.9679 -0.0477 -0.0692 0.1880  52  LEU A CG  
423  C  CD1 . LEU A 52  ? 0.8752 0.6834 0.8914 -0.0893 -0.0705 0.1896  52  LEU A CD1 
424  C  CD2 . LEU A 52  ? 1.0630 0.7469 1.0204 -0.0360 -0.0679 0.1884  52  LEU A CD2 
425  N  N   . CYS A 53  ? 0.9210 0.7213 0.9200 0.0234  -0.0222 0.2442  53  CYS A N   
426  C  CA  . CYS A 53  ? 0.8707 0.7301 0.8896 0.0389  -0.0128 0.2546  53  CYS A CA  
427  C  C   . CYS A 53  ? 0.8205 0.7437 0.8577 0.0185  -0.0161 0.2690  53  CYS A C   
428  O  O   . CYS A 53  ? 0.7591 0.6761 0.7943 -0.0116 -0.0231 0.2718  53  CYS A O   
429  C  CB  . CYS A 53  ? 0.9492 0.7611 0.9396 0.0640  -0.0057 0.2704  53  CYS A CB  
430  S  SG  . CYS A 53  ? 0.9872 0.7736 0.9706 0.0929  0.0050  0.2465  53  CYS A SG  
431  N  N   . GLY A 54  ? 0.7027 0.6981 0.7596 0.0350  -0.0100 0.2746  54  GLY A N   
432  C  CA  . GLY A 54  ? 0.6931 0.7633 0.7644 0.0193  -0.0109 0.2887  54  GLY A CA  
433  C  C   . GLY A 54  ? 0.6853 0.8184 0.7610 0.0490  -0.0041 0.3002  54  GLY A C   
434  O  O   . GLY A 54  ? 0.7181 0.8594 0.8024 0.0809  -0.0001 0.2851  54  GLY A O   
435  N  N   . ASP A 55  ? 0.7689 0.9539 0.8378 0.0382  -0.0019 0.3253  55  ASP A N   
436  C  CA  . ASP A 55  ? 0.7714 1.0313 0.8397 0.0709  0.0022  0.3366  55  ASP A CA  
437  C  C   . ASP A 55  ? 0.7785 1.1568 0.9081 0.0880  -0.0015 0.2925  55  ASP A C   
438  O  O   . ASP A 55  ? 0.8368 1.2847 0.9761 0.1231  0.0002  0.2865  55  ASP A O   
439  C  CB  . ASP A 55  ? 0.8674 1.1550 0.9061 0.0526  0.0080  0.3784  55  ASP A CB  
440  C  CG  . ASP A 55  ? 1.0269 1.1895 0.9996 0.0449  0.0145  0.4273  55  ASP A CG  
441  O  OD1 . ASP A 55  ? 1.1347 1.2988 1.0642 0.0572  0.0216  0.4702  55  ASP A OD1 
442  O  OD2 . ASP A 55  ? 1.0878 1.1478 1.0495 0.0290  0.0119  0.4224  55  ASP A OD2 
443  N  N   . SER A 56  ? 0.7511 1.1527 0.9221 0.0668  -0.0081 0.2586  56  SER A N   
444  C  CA  . SER A 56  ? 0.6168 1.1109 0.8491 0.0804  -0.0124 0.2127  56  SER A CA  
445  C  C   . SER A 56  ? 0.6861 1.1175 0.9352 0.0711  -0.0153 0.1845  56  SER A C   
446  O  O   . SER A 56  ? 0.7362 1.0808 0.9543 0.0518  -0.0183 0.1969  56  SER A O   
447  C  CB  . SER A 56  ? 0.4874 1.0975 0.7545 0.0685  -0.0208 0.1990  56  SER A CB  
448  O  OG  . SER A 56  ? 0.4859 1.0705 0.7497 0.0344  -0.0287 0.1987  56  SER A OG  
449  N  N   . LEU A 57  ? 1.0522 0.8791 0.9304 0.2072  0.1204  0.0940  57  LEU A N   
450  C  CA  . LEU A 57  ? 0.9424 0.7569 0.8359 0.1909  0.1004  0.0941  57  LEU A CA  
451  C  C   . LEU A 57  ? 0.8657 0.6909 0.7966 0.1862  0.0898  0.1024  57  LEU A C   
452  O  O   . LEU A 57  ? 0.8702 0.6778 0.8043 0.1702  0.0730  0.1099  57  LEU A O   
453  C  CB  . LEU A 57  ? 0.9379 0.7568 0.8379 0.2009  0.0960  0.0760  57  LEU A CB  
454  C  CG  . LEU A 57  ? 0.8986 0.6989 0.8135 0.1881  0.0786  0.0777  57  LEU A CG  
455  C  CD1 . LEU A 57  ? 0.9667 0.7321 0.8518 0.1640  0.0716  0.0898  57  LEU A CD1 
456  C  CD2 . LEU A 57  ? 0.8741 0.6787 0.8019 0.1976  0.0796  0.0572  57  LEU A CD2 
457  N  N   . ARG A 58  ? 0.8448 0.7006 0.8030 0.2022  0.0987  0.0988  58  ARG A N   
458  C  CA  . ARG A 58  ? 0.8865 0.7601 0.8863 0.1990  0.0898  0.1014  58  ARG A CA  
459  C  C   . ARG A 58  ? 0.8607 0.7256 0.8643 0.1791  0.0907  0.1126  58  ARG A C   
460  O  O   . ARG A 58  ? 0.7718 0.6381 0.8019 0.1702  0.0717  0.1121  58  ARG A O   
461  C  CB  . ARG A 58  ? 0.8574 0.7696 0.8834 0.2192  0.1051  0.0939  58  ARG A CB  
462  C  CG  . ARG A 58  ? 0.8226 0.7616 0.8959 0.2148  0.1027  0.0933  58  ARG A CG  
463  C  CD  . ARG A 58  ? 0.9860 0.9661 1.0832 0.2360  0.1194  0.0838  58  ARG A CD  
464  N  NE  . ARG A 58  ? 1.0883 1.1007 1.2383 0.2320  0.1167  0.0774  58  ARG A NE  
465  C  CZ  . ARG A 58  ? 1.1129 1.1675 1.2948 0.2489  0.1265  0.0655  58  ARG A CZ  
466  N  NH1 . ARG A 58  ? 1.1613 1.2293 1.3242 0.2730  0.1384  0.0597  58  ARG A NH1 
467  N  NH2 . ARG A 58  ? 0.9966 1.0837 1.2312 0.2434  0.1235  0.0558  58  ARG A NH2 
468  N  N   . ASP A 59  ? 0.9287 0.7832 0.9063 0.1738  0.1109  0.1203  59  ASP A N   
469  C  CA  . ASP A 59  ? 1.0048 0.8503 0.9908 0.1540  0.1136  0.1283  59  ASP A CA  
470  C  C   . ASP A 59  ? 0.9644 0.7817 0.9305 0.1384  0.0913  0.1302  59  ASP A C   
471  O  O   . ASP A 59  ? 1.0270 0.8440 1.0149 0.1249  0.0784  0.1300  59  ASP A O   
472  C  CB  . ASP A 59  ? 1.2303 1.0661 1.1917 0.1546  0.1433  0.1370  59  ASP A CB  
473  C  CG  . ASP A 59  ? 1.4225 1.2702 1.4201 0.1417  0.1611  0.1416  59  ASP A CG  
474  O  OD1 . ASP A 59  ? 1.5408 1.3873 1.5668 0.1226  0.1475  0.1388  59  ASP A OD1 
475  O  OD2 . ASP A 59  ? 1.4724 1.3312 1.4706 0.1512  0.1898  0.1464  59  ASP A OD2 
476  N  N   . ALA A 60  ? 0.9251 0.7215 0.8514 0.1410  0.0868  0.1293  60  ALA A N   
477  C  CA  . ALA A 60  ? 0.9422 0.7116 0.8419 0.1264  0.0705  0.1316  60  ALA A CA  
478  C  C   . ALA A 60  ? 0.9223 0.6828 0.8288 0.1241  0.0447  0.1312  60  ALA A C   
479  O  O   . ALA A 60  ? 0.9164 0.6531 0.7967 0.1135  0.0308  0.1345  60  ALA A O   
480  C  CB  . ALA A 60  ? 0.8038 0.5569 0.6606 0.1289  0.0787  0.1275  60  ALA A CB  
481  N  N   . LEU A 61  ? 0.8954 0.6719 0.8322 0.1357  0.0376  0.1273  61  LEU A N   
482  C  CA  . LEU A 61  ? 0.9438 0.7062 0.8849 0.1376  0.0112  0.1277  61  LEU A CA  
483  C  C   . LEU A 61  ? 0.9659 0.7492 0.9493 0.1402  -0.0052 0.1228  61  LEU A C   
484  O  O   . LEU A 61  ? 1.0456 0.8202 1.0360 0.1482  -0.0303 0.1205  61  LEU A O   
485  C  CB  . LEU A 61  ? 0.9662 0.7269 0.9122 0.1507  0.0100  0.1231  61  LEU A CB  
486  C  CG  . LEU A 61  ? 0.8996 0.6356 0.8097 0.1468  0.0199  0.1227  61  LEU A CG  
487  C  CD1 . LEU A 61  ? 0.8295 0.5695 0.7590 0.1602  0.0196  0.1135  61  LEU A CD1 
488  C  CD2 . LEU A 61  ? 0.9146 0.6091 0.7834 0.1326  0.0081  0.1326  61  LEU A CD2 
489  N  N   . SER A 62  ? 0.9626 0.7718 0.9751 0.1340  0.0088  0.1194  62  SER A N   
490  C  CA  . SER A 62  ? 0.9479 0.7865 1.0134 0.1350  -0.0021 0.1082  62  SER A CA  
491  C  C   . SER A 62  ? 0.8723 0.7014 0.9394 0.1259  -0.0249 0.1038  62  SER A C   
492  O  O   . SER A 62  ? 0.8773 0.7281 0.9866 0.1310  -0.0449 0.0892  62  SER A O   
493  C  CB  . SER A 62  ? 1.0095 0.8810 1.1111 0.1306  0.0292  0.1050  62  SER A CB  
494  O  OG  . SER A 62  ? 1.1089 0.9946 1.2099 0.1445  0.0474  0.1061  62  SER A OG  
495  N  N   . HIS A 63  ? 0.8490 0.6498 0.8735 0.1148  -0.0242 0.1121  63  HIS A N   
496  C  CA  . HIS A 63  ? 0.9288 0.7236 0.9540 0.1074  -0.0449 0.1053  63  HIS A CA  
497  C  C   . HIS A 63  ? 0.9333 0.6876 0.8955 0.1094  -0.0639 0.1149  63  HIS A C   
498  O  O   . HIS A 63  ? 0.9859 0.7207 0.9088 0.0991  -0.0520 0.1225  63  HIS A O   
499  C  CB  . HIS A 63  ? 1.0946 0.8971 1.1343 0.0903  -0.0234 0.1035  63  HIS A CB  
500  C  CG  . HIS A 63  ? 1.2191 1.0545 1.3147 0.0853  0.0023  0.0971  63  HIS A CG  
501  N  ND1 . HIS A 63  ? 1.2506 1.1109 1.4033 0.0745  0.0025  0.0809  63  HIS A ND1 
502  C  CD2 . HIS A 63  ? 1.2437 1.0910 1.3462 0.0895  0.0309  0.1038  63  HIS A CD2 
503  C  CE1 . HIS A 63  ? 1.2605 1.1445 1.4521 0.0695  0.0337  0.0800  63  HIS A CE1 
504  N  NE2 . HIS A 63  ? 1.2353 1.1115 1.3936 0.0802  0.0505  0.0948  63  HIS A NE2 
505  N  N   . ASN A 64  ? 0.9353 0.6754 0.8855 0.1237  -0.0928 0.1139  64  ASN A N   
506  C  CA  . ASN A 64  ? 1.0185 0.7170 0.9060 0.1263  -0.1113 0.1234  64  ASN A CA  
507  C  C   . ASN A 64  ? 1.1373 0.8420 1.0273 0.1240  -0.1311 0.1119  64  ASN A C   
508  O  O   . ASN A 64  ? 1.2260 0.9523 1.1548 0.1351  -0.1558 0.0947  64  ASN A O   
509  C  CB  . ASN A 64  ? 1.0542 0.7268 0.9216 0.1452  -0.1353 0.1282  64  ASN A CB  
510  C  CG  . ASN A 64  ? 1.1586 0.7787 0.9500 0.1478  -0.1480 0.1430  64  ASN A CG  
511  O  OD1 . ASN A 64  ? 1.1942 0.8056 0.9543 0.1394  -0.1488 0.1441  64  ASN A OD1 
512  N  ND2 . ASN A 64  ? 1.3062 0.8887 1.0665 0.1597  -0.1566 0.1545  64  ASN A ND2 
513  N  N   . VAL A 65  ? 1.1663 0.8560 1.0191 0.1113  -0.1218 0.1170  65  VAL A N   
514  C  CA  . VAL A 65  ? 1.1792 0.8764 1.0350 0.1094  -0.1404 0.1036  65  VAL A CA  
515  C  C   . VAL A 65  ? 1.2307 0.8951 1.0248 0.1233  -0.1700 0.1074  65  VAL A C   
516  O  O   . VAL A 65  ? 1.2150 0.8893 1.0148 0.1302  -0.1953 0.0914  65  VAL A O   
517  C  CB  . VAL A 65  ? 1.1713 0.8726 1.0245 0.0901  -0.1169 0.1032  65  VAL A CB  
518  C  CG1 . VAL A 65  ? 1.2099 0.9313 1.1052 0.0799  -0.0843 0.1051  65  VAL A CG1 
519  C  CG2 . VAL A 65  ? 1.2581 0.9260 1.0399 0.0852  -0.1086 0.1173  65  VAL A CG2 
520  N  N   . THR A 66  ? 1.2168 0.8412 0.9515 0.1280  -0.1665 0.1273  66  THR A N   
521  C  CA  . THR A 66  ? 1.1457 0.7315 0.8158 0.1446  -0.1933 0.1344  66  THR A CA  
522  C  C   . THR A 66  ? 1.2635 0.8524 0.9544 0.1711  -0.2287 0.1242  66  THR A C   
523  O  O   . THR A 66  ? 1.2403 0.8228 0.9090 0.1904  -0.2623 0.1139  66  THR A O   
524  C  CB  . THR A 66  ? 1.2042 0.7413 0.8068 0.1391  -0.1740 0.1593  66  THR A CB  
525  O  OG1 . THR A 66  ? 1.2488 0.7842 0.8243 0.1184  -0.1486 0.1625  66  THR A OG1 
526  C  CG2 . THR A 66  ? 1.2582 0.7454 0.7899 0.1597  -0.1996 0.1715  66  THR A CG2 
527  N  N   . GLU A 67  ? 1.2514 0.8528 0.9856 0.1752  -0.2237 0.1236  67  GLU A N   
528  C  CA  . GLU A 67  ? 1.2246 0.8366 0.9890 0.2013  -0.2581 0.1084  67  GLU A CA  
529  C  C   . GLU A 67  ? 1.1962 0.8648 1.0343 0.2032  -0.2744 0.0756  67  GLU A C   
530  O  O   . GLU A 67  ? 1.2043 0.8806 1.0512 0.2280  -0.3134 0.0554  67  GLU A O   
531  C  CB  . GLU A 67  ? 1.2221 0.8387 1.0194 0.2040  -0.2465 0.1131  67  GLU A CB  
532  C  CG  . GLU A 67  ? 1.3454 0.9428 1.1362 0.2353  -0.2827 0.1082  67  GLU A CG  
533  C  CD  . GLU A 67  ? 1.3880 1.0077 1.2330 0.2386  -0.2741 0.1032  67  GLU A CD  
534  O  OE1 . GLU A 67  ? 1.3786 1.0356 1.2709 0.2180  -0.2410 0.1009  67  GLU A OE1 
535  O  OE2 . GLU A 67  ? 1.4417 1.0401 1.2788 0.2643  -0.3015 0.1010  67  GLU A OE2 
536  N  N   . HIS A 68  ? 1.2745 0.9810 1.1662 0.1783  -0.2448 0.0683  68  HIS A N   
537  C  CA  . HIS A 68  ? 1.3576 1.1164 1.3275 0.1730  -0.2510 0.0372  68  HIS A CA  
538  C  C   . HIS A 68  ? 1.5538 1.3145 1.5165 0.1511  -0.2332 0.0376  68  HIS A C   
539  O  O   . HIS A 68  ? 1.6997 1.4697 1.6834 0.1284  -0.1968 0.0456  68  HIS A O   
540  C  CB  . HIS A 68  ? 1.2257 1.0267 1.2745 0.1640  -0.2288 0.0272  68  HIS A CB  
541  C  CG  . HIS A 68  ? 1.2024 1.0037 1.2604 0.1855  -0.2453 0.0255  68  HIS A CG  
542  N  ND1 . HIS A 68  ? 1.2421 1.0586 1.3246 0.2120  -0.2869 0.0000  68  HIS A ND1 
543  C  CD2 . HIS A 68  ? 1.1746 0.9637 1.2225 0.1869  -0.2281 0.0430  68  HIS A CD2 
544  C  CE1 . HIS A 68  ? 1.2339 1.0448 1.3190 0.2284  -0.2945 0.0035  68  HIS A CE1 
545  N  NE2 . HIS A 68  ? 1.2090 1.0037 1.2749 0.2127  -0.2587 0.0295  68  HIS A NE2 
546  N  N   . ARG A 69  ? 1.5611 1.3116 1.4912 0.1612  -0.2608 0.0276  69  ARG A N   
547  C  CA  . ARG A 69  ? 1.4873 1.2396 1.4096 0.1438  -0.2498 0.0241  69  ARG A CA  
548  C  C   . ARG A 69  ? 1.4190 1.2172 1.4317 0.1274  -0.2404 -0.0033 69  ARG A C   
549  O  O   . ARG A 69  ? 1.3370 1.1351 1.3526 0.1092  -0.2241 -0.0045 69  ARG A O   
550  C  CB  . ARG A 69  ? 1.5144 1.2456 1.3755 0.1630  -0.2844 0.0185  69  ARG A CB  
551  C  CG  . ARG A 69  ? 1.6170 1.2963 1.3858 0.1799  -0.2925 0.0462  69  ARG A CG  
552  C  CD  . ARG A 69  ? 1.7521 1.4132 1.4674 0.2108  -0.3358 0.0363  69  ARG A CD  
553  N  NE  . ARG A 69  ? 1.8524 1.4860 1.4930 0.2064  -0.3310 0.0483  69  ARG A NE  
554  C  CZ  . ARG A 69  ? 1.9595 1.5446 1.5181 0.2009  -0.3107 0.0804  69  ARG A CZ  
555  N  NH1 . ARG A 69  ? 1.9536 1.5098 1.4957 0.1993  -0.2945 0.1040  69  ARG A NH1 
556  N  NH2 . ARG A 69  ? 2.0266 1.5943 1.5236 0.1963  -0.3056 0.0865  69  ARG A NH2 
557  N  N   . GLN A 70  ? 1.4849 1.3209 1.5728 0.1327  -0.2488 -0.0265 70  GLN A N   
558  C  CA  . GLN A 70  ? 1.4718 1.3500 1.6517 0.1128  -0.2324 -0.0524 70  GLN A CA  
559  C  C   . GLN A 70  ? 1.3675 1.2394 1.5590 0.0849  -0.1814 -0.0305 70  GLN A C   
560  O  O   . GLN A 70  ? 1.2962 1.1850 1.5418 0.0638  -0.1606 -0.0433 70  GLN A O   
561  C  CB  . GLN A 70  ? 1.5454 1.4688 1.8053 0.1238  -0.2487 -0.0836 70  GLN A CB  
562  C  CG  . GLN A 70  ? 1.6755 1.5937 1.9216 0.1379  -0.2473 -0.0680 70  GLN A CG  
563  C  CD  . GLN A 70  ? 1.8560 1.7423 2.0312 0.1716  -0.2892 -0.0610 70  GLN A CD  
564  O  OE1 . GLN A 70  ? 1.9368 1.7808 2.0309 0.1775  -0.2983 -0.0412 70  GLN A OE1 
565  N  NE2 . GLN A 70  ? 1.9129 1.8172 2.1163 0.1945  -0.3136 -0.0773 70  GLN A NE2 
566  N  N   . ASP A 71  ? 1.3359 1.1822 1.4777 0.0858  -0.1613 0.0007  71  ASP A N   
567  C  CA  . ASP A 71  ? 1.3061 1.1444 1.4484 0.0665  -0.1163 0.0209  71  ASP A CA  
568  C  C   . ASP A 71  ? 1.2877 1.0899 1.3637 0.0584  -0.1037 0.0404  71  ASP A C   
569  O  O   . ASP A 71  ? 1.3926 1.1820 1.4528 0.0488  -0.0706 0.0583  71  ASP A O   
570  C  CB  . ASP A 71  ? 1.3480 1.1869 1.4834 0.0747  -0.1020 0.0370  71  ASP A CB  
571  C  CG  . ASP A 71  ? 1.3901 1.2702 1.5977 0.0815  -0.1096 0.0155  71  ASP A CG  
572  O  OD1 . ASP A 71  ? 1.4284 1.3323 1.6775 0.0878  -0.1386 -0.0129 71  ASP A OD1 
573  O  OD2 . ASP A 71  ? 1.3940 1.2862 1.6186 0.0822  -0.0879 0.0234  71  ASP A OD2 
574  N  N   . LEU A 72  ? 1.1871 0.9741 1.2220 0.0648  -0.1302 0.0354  72  LEU A N   
575  C  CA  . LEU A 72  ? 1.1250 0.8847 1.1052 0.0562  -0.1188 0.0476  72  LEU A CA  
576  C  C   . LEU A 72  ? 1.1397 0.9055 1.1594 0.0374  -0.0988 0.0383  72  LEU A C   
577  O  O   . LEU A 72  ? 1.1697 0.9141 1.1558 0.0291  -0.0772 0.0513  72  LEU A O   
578  C  CB  . LEU A 72  ? 1.1148 0.8596 1.0411 0.0684  -0.1511 0.0429  72  LEU A CB  
579  C  CG  . LEU A 72  ? 1.0854 0.8041 0.9481 0.0615  -0.1407 0.0542  72  LEU A CG  
580  C  CD1 . LEU A 72  ? 1.0779 0.7759 0.8995 0.0585  -0.1139 0.0784  72  LEU A CD1 
581  C  CD2 . LEU A 72  ? 1.0638 0.7705 0.8726 0.0746  -0.1713 0.0487  72  LEU A CD2 
582  N  N   . ALA A 73  ? 1.1047 0.8981 1.1971 0.0313  -0.1057 0.0138  73  ALA A N   
583  C  CA  . ALA A 73  ? 1.0748 0.8684 1.2107 0.0110  -0.0828 0.0055  73  ALA A CA  
584  C  C   . ALA A 73  ? 1.0636 0.8453 1.2047 -0.0003 -0.0386 0.0270  73  ALA A C   
585  O  O   . ALA A 73  ? 1.2056 0.9671 1.3480 -0.0139 -0.0141 0.0323  73  ALA A O   
586  C  CB  . ALA A 73  ? 0.9471 0.7761 1.1702 0.0049  -0.0966 -0.0290 73  ALA A CB  
587  N  N   . LYS A 74  ? 0.9839 0.7750 1.1242 0.0078  -0.0288 0.0393  74  LYS A N   
588  C  CA  . LYS A 74  ? 1.0446 0.8266 1.1837 0.0021  0.0117  0.0588  74  LYS A CA  
589  C  C   . LYS A 74  ? 1.0917 0.8389 1.1559 0.0077  0.0251  0.0812  74  LYS A C   
590  O  O   . LYS A 74  ? 1.1514 0.8842 1.2054 0.0054  0.0578  0.0959  74  LYS A O   
591  C  CB  . LYS A 74  ? 0.9834 0.7909 1.1457 0.0120  0.0146  0.0610  74  LYS A CB  
592  C  CG  . LYS A 74  ? 0.9485 0.7965 1.1949 0.0064  0.0071  0.0347  74  LYS A CG  
593  C  CD  . LYS A 74  ? 0.9331 0.8082 1.2009 0.0189  0.0066  0.0341  74  LYS A CD  
594  C  CE  . LYS A 74  ? 0.9370 0.8583 1.2955 0.0131  0.0005  0.0025  74  LYS A CE  
595  N  NZ  . LYS A 74  ? 0.9318 0.8829 1.3130 0.0283  -0.0055 -0.0027 74  LYS A NZ  
596  N  N   . ALA A 75  ? 1.0614 0.7957 1.0723 0.0161  0.0013  0.0823  75  ALA A N   
597  C  CA  . ALA A 75  ? 1.0703 0.7776 1.0173 0.0206  0.0129  0.0964  75  ALA A CA  
598  C  C   . ALA A 75  ? 1.1176 0.8039 1.0550 0.0115  0.0212  0.0926  75  ALA A C   
599  O  O   . ALA A 75  ? 1.1388 0.8033 1.0397 0.0152  0.0407  0.1030  75  ALA A O   
600  C  CB  . ALA A 75  ? 1.0463 0.7479 0.9422 0.0301  -0.0107 0.0976  75  ALA A CB  
601  N  N   . LEU A 76  ? 1.1451 0.8375 1.1156 0.0021  0.0046  0.0752  76  LEU A N   
602  C  CA  . LEU A 76  ? 1.1762 0.8478 1.1385 -0.0057 0.0065  0.0681  76  LEU A CA  
603  C  C   . LEU A 76  ? 1.1635 0.8207 1.1671 -0.0185 0.0375  0.0719  76  LEU A C   
604  O  O   . LEU A 76  ? 1.1215 0.7967 1.1913 -0.0304 0.0415  0.0609  76  LEU A O   
605  C  CB  . LEU A 76  ? 1.1654 0.8510 1.1452 -0.0082 -0.0271 0.0446  76  LEU A CB  
606  C  CG  . LEU A 76  ? 1.2008 0.8678 1.1757 -0.0151 -0.0301 0.0326  76  LEU A CG  
607  C  CD1 . LEU A 76  ? 1.2561 0.9171 1.1651 -0.0049 -0.0495 0.0300  76  LEU A CD1 
608  C  CD2 . LEU A 76  ? 1.1403 0.8254 1.1829 -0.0251 -0.0467 0.0059  76  LEU A CD2 
609  N  N   . SER A 77  ? 1.2169 0.8404 1.1805 -0.0152 0.0603  0.0862  77  SER A N   
610  C  CA  . SER A 77  ? 1.3103 0.9052 1.2960 -0.0257 0.0921  0.0938  77  SER A CA  
611  C  C   . SER A 77  ? 1.3183 0.8851 1.2975 -0.0318 0.0838  0.0825  77  SER A C   
612  O  O   . SER A 77  ? 1.3162 0.8732 1.2437 -0.0205 0.0663  0.0787  77  SER A O   
613  C  CB  . SER A 77  ? 1.3923 0.9624 1.3312 -0.0121 0.1227  0.1181  77  SER A CB  
614  O  OG  . SER A 77  ? 1.5351 1.0585 1.4574 -0.0144 0.1466  0.1273  77  SER A OG  
615  N  N   . ARG A 78  ? 1.3101 0.8654 1.3458 -0.0507 0.0969  0.0744  78  ARG A N   
616  C  CA  . ARG A 78  ? 1.3248 0.8551 1.3681 -0.0583 0.0868  0.0593  78  ARG A CA  
617  C  C   . ARG A 78  ? 1.3680 0.8476 1.4233 -0.0702 0.1254  0.0730  78  ARG A C   
618  O  O   . ARG A 78  ? 1.3344 0.8154 1.4399 -0.0861 0.1550  0.0790  78  ARG A O   
619  C  CB  . ARG A 78  ? 1.2380 0.8054 1.3481 -0.0706 0.0572  0.0270  78  ARG A CB  
620  C  CG  . ARG A 78  ? 1.1979 0.7420 1.3572 -0.0882 0.0611  0.0089  78  ARG A CG  
621  C  CD  . ARG A 78  ? 1.2589 0.8366 1.4489 -0.0875 0.0178  -0.0269 78  ARG A CD  
622  N  NE  . ARG A 78  ? 1.3653 0.9261 1.4937 -0.0735 -0.0046 -0.0312 78  ARG A NE  
623  C  CZ  . ARG A 78  ? 1.4098 0.9997 1.5348 -0.0651 -0.0442 -0.0574 78  ARG A CZ  
624  N  NH1 . ARG A 78  ? 1.4139 1.0483 1.5896 -0.0663 -0.0685 -0.0813 78  ARG A NH1 
625  N  NH2 . ARG A 78  ? 1.4252 1.0011 1.4940 -0.0532 -0.0602 -0.0616 78  ARG A NH2 
626  N  N   . ASP A 79  ? 1.4160 0.8490 1.4235 -0.0618 0.1261  0.0774  79  ASP A N   
627  C  CA  . ASP A 79  ? 1.5278 0.9003 1.5399 -0.0718 0.1591  0.0896  79  ASP A CA  
628  C  C   . ASP A 79  ? 1.4893 0.8598 1.5701 -0.0938 0.1467  0.0619  79  ASP A C   
629  O  O   . ASP A 79  ? 1.3741 0.7609 1.4513 -0.0880 0.1092  0.0380  79  ASP A O   
630  C  CB  . ASP A 79  ? 1.6114 0.9313 1.5358 -0.0472 0.1620  0.1053  79  ASP A CB  
631  C  CG  . ASP A 79  ? 1.8081 1.0527 1.7188 -0.0517 0.2005  0.1260  79  ASP A CG  
632  O  OD1 . ASP A 79  ? 1.9035 1.1039 1.7369 -0.0267 0.2132  0.1469  79  ASP A OD1 
633  O  OD2 . ASP A 79  ? 1.9074 1.1344 1.8829 -0.0788 0.2184  0.1204  79  ASP A OD2 
634  N  N   . ARG A 80  ? 1.5550 0.9079 1.7013 -0.1195 0.1797  0.0630  80  ARG A N   
635  C  CA  . ARG A 80  ? 1.6200 0.9740 1.8450 -0.1425 0.1701  0.0319  80  ARG A CA  
636  C  C   . ARG A 80  ? 1.6969 0.9858 1.8896 -0.1392 0.1692  0.0324  80  ARG A C   
637  O  O   . ARG A 80  ? 1.6999 0.9978 1.9353 -0.1466 0.1415  0.0004  80  ARG A O   
638  C  CB  . ARG A 80  ? 1.6453 1.0016 1.9580 -0.1740 0.2097  0.0293  80  ARG A CB  
639  C  CG  . ARG A 80  ? 1.5798 0.9948 1.9223 -0.1757 0.2163  0.0309  80  ARG A CG  
640  C  CD  . ARG A 80  ? 1.6271 1.0800 2.0885 -0.2067 0.2283  0.0001  80  ARG A CD  
641  N  NE  . ARG A 80  ? 1.7480 1.1513 2.2601 -0.2337 0.2560  -0.0082 80  ARG A NE  
642  C  CZ  . ARG A 80  ? 1.8163 1.1786 2.3580 -0.2588 0.3141  0.0097  80  ARG A CZ  
643  N  NH1 . ARG A 80  ? 1.8262 1.1962 2.3510 -0.2585 0.3494  0.0357  80  ARG A NH1 
644  N  NH2 . ARG A 80  ? 1.8324 1.1441 2.4202 -0.2844 0.3386  0.0014  80  ARG A NH2 
645  N  N   . ARG A 81  ? 1.7751 0.9982 1.8914 -0.1249 0.1965  0.0660  81  ARG A N   
646  C  CA  . ARG A 81  ? 1.7854 0.9372 1.8690 -0.1197 0.1977  0.0678  81  ARG A CA  
647  C  C   . ARG A 81  ? 1.6578 0.8270 1.6933 -0.0946 0.1481  0.0472  81  ARG A C   
648  O  O   . ARG A 81  ? 1.5732 0.7344 1.6373 -0.0998 0.1244  0.0201  81  ARG A O   
649  C  CB  . ARG A 81  ? 1.8677 0.9407 1.8763 -0.1066 0.2406  0.1100  81  ARG A CB  
650  C  CG  . ARG A 81  ? 1.8590 0.8459 1.8248 -0.0974 0.2440  0.1157  81  ARG A CG  
651  C  CD  . ARG A 81  ? 1.9227 0.8388 1.7863 -0.0690 0.2734  0.1561  81  ARG A CD  
652  N  NE  . ARG A 81  ? 1.9231 0.8768 1.7133 -0.0327 0.2455  0.1572  81  ARG A NE  
653  C  CZ  . ARG A 81  ? 1.9321 0.8506 1.6397 0.0028  0.2251  0.1577  81  ARG A CZ  
654  N  NH1 . ARG A 81  ? 1.9834 0.8236 1.6645 0.0095  0.2271  0.1595  81  ARG A NH1 
655  N  NH2 . ARG A 81  ? 1.8795 0.8408 1.5338 0.0319  0.2023  0.1537  81  ARG A NH2 
656  N  N   . THR A 82  ? 1.6035 0.7985 1.5692 -0.0679 0.1331  0.0570  82  THR A N   
657  C  CA  . THR A 82  ? 1.5953 0.8101 1.5138 -0.0453 0.0913  0.0369  82  THR A CA  
658  C  C   . THR A 82  ? 1.5344 0.8282 1.4884 -0.0497 0.0542  0.0085  82  THR A C   
659  O  O   . THR A 82  ? 1.4607 0.7750 1.3859 -0.0358 0.0202  -0.0128 82  THR A O   
660  C  CB  . THR A 82  ? 1.6628 0.8645 1.4894 -0.0139 0.0946  0.0569  82  THR A CB  
661  O  OG1 . THR A 82  ? 1.6929 0.9323 1.4855 0.0036  0.0557  0.0330  82  THR A OG1 
662  C  CG2 . THR A 82  ? 1.6534 0.8864 1.4756 -0.0135 0.1153  0.0788  82  THR A CG2 
663  N  N   . ARG A 83  ? 1.5535 0.8907 1.5656 -0.0668 0.0601  0.0069  83  ARG A N   
664  C  CA  . ARG A 83  ? 1.4999 0.9065 1.5418 -0.0679 0.0251  -0.0181 83  ARG A CA  
665  C  C   . ARG A 83  ? 1.4059 0.8423 1.3774 -0.0457 0.0070  -0.0117 83  ARG A C   
666  O  O   . ARG A 83  ? 1.3227 0.8017 1.2904 -0.0401 -0.0258 -0.0322 83  ARG A O   
667  C  CB  . ARG A 83  ? 1.5453 0.9651 1.6294 -0.0736 -0.0075 -0.0557 83  ARG A CB  
668  C  CG  . ARG A 83  ? 1.6893 1.1174 1.8731 -0.0993 -0.0003 -0.0754 83  ARG A CG  
669  C  CD  . ARG A 83  ? 1.8298 1.3284 2.0594 -0.0991 -0.0346 -0.1052 83  ARG A CD  
670  N  NE  . ARG A 83  ? 1.9826 1.5071 2.1711 -0.0801 -0.0770 -0.1267 83  ARG A NE  
671  C  CZ  . ARG A 83  ? 2.0611 1.6365 2.2825 -0.0753 -0.1141 -0.1602 83  ARG A CZ  
672  N  NH1 . ARG A 83  ? 2.0781 1.6869 2.3787 -0.0868 -0.1176 -0.1794 83  ARG A NH1 
673  N  NH2 . ARG A 83  ? 2.1319 1.7265 2.3059 -0.0572 -0.1478 -0.1766 83  ARG A NH2 
674  N  N   . ALA A 84  ? 1.4331 0.8465 1.3485 -0.0325 0.0297  0.0157  84  ALA A N   
675  C  CA  . ALA A 84  ? 1.3695 0.8106 1.2268 -0.0142 0.0183  0.0208  84  ALA A CA  
676  C  C   . ALA A 84  ? 1.3691 0.8466 1.2461 -0.0185 0.0261  0.0334  84  ALA A C   
677  O  O   . ALA A 84  ? 1.3673 0.8374 1.2817 -0.0294 0.0515  0.0475  84  ALA A O   
678  C  CB  . ALA A 84  ? 1.3421 0.7444 1.1313 0.0065  0.0343  0.0369  84  ALA A CB  
679  N  N   . VAL A 85  ? 1.3489 0.8642 1.1998 -0.0101 0.0051  0.0275  85  VAL A N   
680  C  CA  . VAL A 85  ? 1.3072 0.8545 1.1702 -0.0109 0.0074  0.0379  85  VAL A CA  
681  C  C   . VAL A 85  ? 1.2457 0.7988 1.0479 0.0052  0.0100  0.0488  85  VAL A C   
682  O  O   . VAL A 85  ? 1.2643 0.8121 1.0206 0.0152  0.0006  0.0400  85  VAL A O   
683  C  CB  . VAL A 85  ? 1.2796 0.8662 1.1777 -0.0168 -0.0224 0.0187  85  VAL A CB  
684  C  CG1 . VAL A 85  ? 1.3146 0.9040 1.2879 -0.0329 -0.0233 0.0034  85  VAL A CG1 
685  C  CG2 . VAL A 85  ? 1.2349 0.8324 1.0926 -0.0087 -0.0510 0.0010  85  VAL A CG2 
686  N  N   . GLU A 86  ? 1.2149 0.7815 1.0222 0.0074  0.0230  0.0646  86  GLU A N   
687  C  CA  . GLU A 86  ? 1.1752 0.7527 0.9374 0.0205  0.0245  0.0717  86  GLU A CA  
688  C  C   . GLU A 86  ? 1.1352 0.7392 0.9219 0.0179  0.0224  0.0796  86  GLU A C   
689  O  O   . GLU A 86  ? 1.1460 0.7568 0.9814 0.0099  0.0297  0.0839  86  GLU A O   
690  C  CB  . GLU A 86  ? 1.1437 0.6970 0.8716 0.0351  0.0486  0.0836  86  GLU A CB  
691  C  CG  . GLU A 86  ? 1.1780 0.7194 0.9307 0.0345  0.0760  0.1026  86  GLU A CG  
692  C  CD  . GLU A 86  ? 1.3481 0.8576 1.0576 0.0535  0.0977  0.1131  86  GLU A CD  
693  O  OE1 . GLU A 86  ? 1.4081 0.9268 1.1000 0.0676  0.1099  0.1221  86  GLU A OE1 
694  O  OE2 . GLU A 86  ? 1.4358 0.9096 1.1271 0.0570  0.1009  0.1110  86  GLU A OE2 
695  N  N   . LEU A 87  ? 1.0848 0.7030 0.8391 0.0245  0.0129  0.0798  87  LEU A N   
696  C  CA  . LEU A 87  ? 1.0688 0.7066 0.8385 0.0249  0.0068  0.0868  87  LEU A CA  
697  C  C   . LEU A 87  ? 1.1063 0.7454 0.8352 0.0342  0.0135  0.0928  87  LEU A C   
698  O  O   . LEU A 87  ? 1.0914 0.7277 0.7810 0.0353  0.0075  0.0846  87  LEU A O   
699  C  CB  . LEU A 87  ? 1.0622 0.7136 0.8421 0.0204  -0.0220 0.0756  87  LEU A CB  
700  C  CG  . LEU A 87  ? 1.0643 0.7299 0.8516 0.0249  -0.0348 0.0810  87  LEU A CG  
701  C  CD1 . LEU A 87  ? 1.0734 0.7553 0.9068 0.0225  -0.0571 0.0678  87  LEU A CD1 
702  C  CD2 . LEU A 87  ? 1.0358 0.6953 0.7668 0.0299  -0.0450 0.0836  87  LEU A CD2 
703  N  N   . VAL A 88  ? 1.1891 0.8346 0.9310 0.0402  0.0267  0.1041  88  VAL A N   
704  C  CA  . VAL A 88  ? 1.1697 0.8176 0.8831 0.0492  0.0350  0.1068  88  VAL A CA  
705  C  C   . VAL A 88  ? 1.2030 0.8622 0.9344 0.0503  0.0283  0.1147  88  VAL A C   
706  O  O   . VAL A 88  ? 1.3299 0.9991 1.0999 0.0517  0.0318  0.1205  88  VAL A O   
707  C  CB  . VAL A 88  ? 1.1101 0.7532 0.8164 0.0620  0.0578  0.1094  88  VAL A CB  
708  C  CG1 . VAL A 88  ? 1.1194 0.7704 0.8037 0.0722  0.0638  0.1051  88  VAL A CG1 
709  C  CG2 . VAL A 88  ? 1.0604 0.6855 0.7455 0.0647  0.0620  0.1020  88  VAL A CG2 
710  N  N   . LEU A 89  ? 1.1391 0.7949 0.8423 0.0496  0.0198  0.1141  89  LEU A N   
711  C  CA  . LEU A 89  ? 1.0704 0.7279 0.7810 0.0531  0.0132  0.1221  89  LEU A CA  
712  C  C   . LEU A 89  ? 1.0830 0.7355 0.7684 0.0561  0.0261  0.1211  89  LEU A C   
713  O  O   . LEU A 89  ? 1.1196 0.7715 0.7830 0.0555  0.0379  0.1112  89  LEU A O   
714  C  CB  . LEU A 89  ? 1.0633 0.7127 0.7621 0.0497  -0.0115 0.1236  89  LEU A CB  
715  C  CG  . LEU A 89  ? 1.1109 0.7707 0.8425 0.0480  -0.0288 0.1176  89  LEU A CG  
716  C  CD1 . LEU A 89  ? 0.9619 0.6126 0.6670 0.0497  -0.0554 0.1148  89  LEU A CD1 
717  C  CD2 . LEU A 89  ? 0.9146 0.5920 0.7001 0.0528  -0.0284 0.1192  89  LEU A CD2 
718  N  N   . TRP A 90  ? 1.1179 0.7671 0.8100 0.0600  0.0230  0.1282  90  TRP A N   
719  C  CA  . TRP A 90  ? 1.1688 0.8121 0.8450 0.0607  0.0360  0.1248  90  TRP A CA  
720  C  C   . TRP A 90  ? 1.2918 0.9156 0.9604 0.0601  0.0256  0.1355  90  TRP A C   
721  O  O   . TRP A 90  ? 1.2637 0.8821 0.9405 0.0639  0.0063  0.1442  90  TRP A O   
722  C  CB  . TRP A 90  ? 1.0877 0.7502 0.7891 0.0731  0.0523  0.1179  90  TRP A CB  
723  C  CG  . TRP A 90  ? 1.0275 0.7007 0.7647 0.0834  0.0491  0.1249  90  TRP A CG  
724  C  CD1 . TRP A 90  ? 1.0104 0.6943 0.7776 0.0864  0.0410  0.1317  90  TRP A CD1 
725  C  CD2 . TRP A 90  ? 1.0847 0.7626 0.8368 0.0922  0.0545  0.1216  90  TRP A CD2 
726  N  NE1 . TRP A 90  ? 0.9853 0.6822 0.7830 0.0972  0.0407  0.1331  90  TRP A NE1 
727  C  CE2 . TRP A 90  ? 1.0803 0.7726 0.8684 0.1019  0.0477  0.1275  90  TRP A CE2 
728  C  CE3 . TRP A 90  ? 1.1307 0.8043 0.8744 0.0923  0.0648  0.1110  90  TRP A CE3 
729  C  CZ2 . TRP A 90  ? 1.1304 0.8319 0.9425 0.1135  0.0486  0.1243  90  TRP A CZ2 
730  C  CZ3 . TRP A 90  ? 1.1057 0.7865 0.8760 0.1028  0.0662  0.1076  90  TRP A CZ3 
731  C  CH2 . TRP A 90  ? 1.1413 0.8356 0.9436 0.1143  0.0570  0.1147  90  TRP A CH2 
732  N  N   . ASN A 91  ? 1.3609 0.8903 1.1895 -0.0491 0.1399  0.2262  91  ASN A N   
733  C  CA  . ASN A 91  ? 1.2650 0.7999 1.1015 -0.0632 0.1422  0.2306  91  ASN A CA  
734  C  C   . ASN A 91  ? 1.2140 0.7528 1.0722 -0.0792 0.1266  0.2320  91  ASN A C   
735  O  O   . ASN A 91  ? 1.1721 0.7019 1.0286 -0.0921 0.1216  0.2372  91  ASN A O   
736  C  CB  . ASN A 91  ? 1.2223 0.7962 1.0924 -0.0597 0.1561  0.2318  91  ASN A CB  
737  C  CG  . ASN A 91  ? 1.3911 0.9579 1.2401 -0.0581 0.1732  0.2365  91  ASN A CG  
738  O  OD1 . ASN A 91  ? 1.6576 1.1905 1.4653 -0.0631 0.1729  0.2388  91  ASN A OD1 
739  N  ND2 . ASN A 91  ? 1.3892 0.9902 1.2661 -0.0519 0.1884  0.2386  91  ASN A ND2 
740  N  N   . GLY A 92  ? 1.1812 0.7374 1.0616 -0.0782 0.1180  0.2268  92  GLY A N   
741  C  CA  . GLY A 92  ? 1.1241 0.6952 1.0360 -0.0907 0.1083  0.2242  92  GLY A CA  
742  C  C   . GLY A 92  ? 1.0913 0.6997 1.0452 -0.0938 0.1129  0.2194  92  GLY A C   
743  O  O   . GLY A 92  ? 1.0104 0.6336 0.9940 -0.1025 0.1057  0.2128  92  GLY A O   
744  N  N   . GLU A 93  ? 1.0595 0.6835 1.0188 -0.0872 0.1248  0.2219  93  GLU A N   
745  C  CA  . GLU A 93  ? 1.0383 0.7000 1.0399 -0.0904 0.1283  0.2182  93  GLU A CA  
746  C  C   . GLU A 93  ? 1.0932 0.7835 1.1052 -0.0793 0.1274  0.2119  93  GLU A C   
747  O  O   . GLU A 93  ? 1.1551 0.8425 1.1485 -0.0649 0.1340  0.2158  93  GLU A O   
748  C  CB  . GLU A 93  ? 1.0316 0.6990 1.0382 -0.0911 0.1421  0.2276  93  GLU A CB  
749  C  CG  . GLU A 93  ? 1.0914 0.7808 1.1428 -0.1051 0.1411  0.2287  93  GLU A CG  
750  C  CD  . GLU A 93  ? 1.1059 0.8303 1.1969 -0.1066 0.1340  0.2163  93  GLU A CD  
751  O  OE1 . GLU A 93  ? 1.0892 0.8173 1.2083 -0.1188 0.1244  0.2084  93  GLU A OE1 
752  O  OE2 . GLU A 93  ? 1.1298 0.8778 1.2240 -0.0955 0.1374  0.2138  93  GLU A OE2 
753  N  N   . GLU A 94  ? 1.1283 0.8460 1.1704 -0.0859 0.1187  0.2019  94  GLU A N   
754  C  CA  . GLU A 94  ? 1.1427 0.8895 1.1917 -0.0779 0.1140  0.1971  94  GLU A CA  
755  C  C   . GLU A 94  ? 1.1089 0.8881 1.1832 -0.0715 0.1209  0.2009  94  GLU A C   
756  O  O   . GLU A 94  ? 1.1182 0.9119 1.1888 -0.0584 0.1211  0.2050  94  GLU A O   
757  C  CB  . GLU A 94  ? 1.2263 0.9921 1.2936 -0.0886 0.1025  0.1829  94  GLU A CB  
758  C  CG  . GLU A 94  ? 1.3905 1.1914 1.4637 -0.0838 0.0952  0.1781  94  GLU A CG  
759  C  CD  . GLU A 94  ? 1.4625 1.2864 1.5548 -0.0964 0.0859  0.1601  94  GLU A CD  
760  O  OE1 . GLU A 94  ? 1.4537 1.2625 1.5561 -0.1068 0.0859  0.1510  94  GLU A OE1 
761  O  OE2 . GLU A 94  ? 1.4918 1.3486 1.5890 -0.0958 0.0782  0.1548  94  GLU A OE2 
762  N  N   . ASP A 95  ? 1.0950 0.8868 1.1987 -0.0807 0.1260  0.2016  95  ASP A N   
763  C  CA  . ASP A 95  ? 1.0203 0.8494 1.1575 -0.0777 0.1314  0.2053  95  ASP A CA  
764  C  C   . ASP A 95  ? 1.0562 0.8776 1.1807 -0.0645 0.1493  0.2185  95  ASP A C   
765  O  O   . ASP A 95  ? 1.1172 0.9145 1.2268 -0.0687 0.1593  0.2246  95  ASP A O   
766  C  CB  . ASP A 95  ? 0.9810 0.8276 1.1596 -0.0951 0.1288  0.2011  95  ASP A CB  
767  C  CG  . ASP A 95  ? 1.0581 0.9492 1.2784 -0.0952 0.1300  0.2038  95  ASP A CG  
768  O  OD1 . ASP A 95  ? 1.1172 1.0293 1.3366 -0.0813 0.1308  0.2079  95  ASP A OD1 
769  O  OD2 . ASP A 95  ? 1.1491 1.0546 1.4069 -0.1096 0.1293  0.2031  95  ASP A OD2 
770  N  N   . PRO A 96  ? 0.9853 0.8269 1.1151 -0.0483 0.1543  0.2232  96  PRO A N   
771  C  CA  . PRO A 96  ? 1.0183 0.8572 1.1425 -0.0346 0.1749  0.2331  96  PRO A CA  
772  C  C   . PRO A 96  ? 1.0597 0.9212 1.2161 -0.0439 0.1873  0.2399  96  PRO A C   
773  O  O   . PRO A 96  ? 1.1539 1.0043 1.2952 -0.0382 0.2067  0.2474  96  PRO A O   
774  C  CB  . PRO A 96  ? 0.9850 0.8493 1.1238 -0.0159 0.1744  0.2365  96  PRO A CB  
775  C  CG  . PRO A 96  ? 0.9363 0.7984 1.0644 -0.0184 0.1535  0.2304  96  PRO A CG  
776  C  CD  . PRO A 96  ? 0.8646 0.7292 1.0016 -0.0404 0.1415  0.2207  96  PRO A CD  
777  N  N   . LEU A 97  ? 1.0331 0.9261 1.2329 -0.0591 0.1768  0.2373  97  LEU A N   
778  C  CA  . LEU A 97  ? 1.0280 0.9433 1.2638 -0.0703 0.1873  0.2461  97  LEU A CA  
779  C  C   . LEU A 97  ? 1.0877 0.9695 1.3023 -0.0831 0.1931  0.2511  97  LEU A C   
780  O  O   . LEU A 97  ? 1.1389 1.0283 1.3629 -0.0870 0.2094  0.2640  97  LEU A O   
781  C  CB  . LEU A 97  ? 0.9755 0.9281 1.2635 -0.0855 0.1713  0.2403  97  LEU A CB  
782  C  CG  . LEU A 97  ? 0.9327 0.9275 1.2492 -0.0762 0.1632  0.2389  97  LEU A CG  
783  C  CD1 . LEU A 97  ? 0.9026 0.9273 1.2612 -0.0949 0.1430  0.2287  97  LEU A CD1 
784  C  CD2 . LEU A 97  ? 0.9378 0.9619 1.2786 -0.0627 0.1829  0.2541  97  LEU A CD2 
785  N  N   . LYS A 98  ? 1.1328 0.9799 1.3202 -0.0901 0.1801  0.2431  98  LYS A N   
786  C  CA  . LYS A 98  ? 1.1254 0.9406 1.2953 -0.1028 0.1814  0.2495  98  LYS A CA  
787  C  C   . LYS A 98  ? 1.1116 0.8889 1.2234 -0.0928 0.1909  0.2542  98  LYS A C   
788  O  O   . LYS A 98  ? 1.0923 0.8379 1.1808 -0.1026 0.1860  0.2581  98  LYS A O   
789  C  CB  . LYS A 98  ? 1.0850 0.8861 1.2661 -0.1166 0.1617  0.2384  98  LYS A CB  
790  C  CG  . LYS A 98  ? 1.0474 0.8820 1.2800 -0.1262 0.1501  0.2276  98  LYS A CG  
791  C  CD  . LYS A 98  ? 1.1176 0.9374 1.3734 -0.1438 0.1376  0.2206  98  LYS A CD  
792  C  CE  . LYS A 98  ? 1.2253 1.0208 1.4554 -0.1414 0.1261  0.2064  98  LYS A CE  
793  N  NZ  . LYS A 98  ? 1.2629 1.0823 1.4977 -0.1366 0.1165  0.1886  98  LYS A NZ  
794  N  N   . GLY A 99  ? 1.1192 0.8984 1.2091 -0.0739 0.2030  0.2536  99  GLY A N   
795  C  CA  . GLY A 99  ? 1.1567 0.8985 1.1911 -0.0642 0.2123  0.2547  99  GLY A CA  
796  C  C   . GLY A 99  ? 1.1199 0.8327 1.1216 -0.0549 0.2002  0.2447  99  GLY A C   
797  O  O   . GLY A 99  ? 1.1328 0.8087 1.0872 -0.0501 0.2040  0.2442  99  GLY A O   
798  N  N   . GLY A 100 ? 1.0769 0.8054 1.1010 -0.0534 0.1854  0.2372  100 GLY A N   
799  C  CA  . GLY A 100 ? 1.1195 0.8244 1.1157 -0.0454 0.1744  0.2308  100 GLY A CA  
800  C  C   . GLY A 100 ? 1.2139 0.9065 1.1859 -0.0246 0.1859  0.2313  100 GLY A C   
801  O  O   . GLY A 100 ? 1.2803 1.0022 1.2770 -0.0120 0.1965  0.2337  100 GLY A O   
802  N  N   . LEU A 101 ? 1.2010 0.8505 1.1286 -0.0207 0.1833  0.2290  101 LEU A N   
803  C  CA  . LEU A 101 ? 1.2417 0.8710 1.1437 -0.0012 0.1957  0.2272  101 LEU A CA  
804  C  C   . LEU A 101 ? 1.1862 0.7688 1.0471 -0.0005 0.1842  0.2234  101 LEU A C   
805  O  O   . LEU A 101 ? 1.1861 0.7431 1.0235 -0.0156 0.1747  0.2234  101 LEU A O   
806  C  CB  . LEU A 101 ? 1.2512 0.8750 1.1362 0.0017  0.2180  0.2283  101 LEU A CB  
807  C  CG  . LEU A 101 ? 1.3296 0.9228 1.1777 0.0201  0.2340  0.2219  101 LEU A CG  
808  C  CD1 . LEU A 101 ? 1.4504 1.0732 1.3328 0.0423  0.2467  0.2220  101 LEU A CD1 
809  C  CD2 . LEU A 101 ? 1.2884 0.8686 1.1038 0.0147  0.2521  0.2220  101 LEU A CD2 
810  N  N   . SER A 102 ? 1.1252 0.6972 0.9812 0.0167  0.1841  0.2219  102 SER A N   
811  C  CA  . SER A 102 ? 1.1543 0.6817 0.9757 0.0180  0.1730  0.2195  102 SER A CA  
812  C  C   . SER A 102 ? 1.1977 0.6855 0.9823 0.0314  0.1872  0.2122  102 SER A C   
813  O  O   . SER A 102 ? 1.2413 0.7412 1.0316 0.0446  0.2077  0.2090  102 SER A O   
814  C  CB  . SER A 102 ? 1.1921 0.7311 1.0336 0.0260  0.1601  0.2246  102 SER A CB  
815  O  OG  . SER A 102 ? 1.1691 0.7250 1.0321 0.0472  0.1706  0.2266  102 SER A OG  
816  N  N   . LEU A 103 ? 1.1669 0.6073 0.9141 0.0274  0.1765  0.2086  103 LEU A N   
817  C  CA  . LEU A 103 ? 1.2251 0.6194 0.9308 0.0376  0.1865  0.1979  103 LEU A CA  
818  C  C   . LEU A 103 ? 1.2626 0.6271 0.9657 0.0489  0.1760  0.1975  103 LEU A C   
819  O  O   . LEU A 103 ? 1.3149 0.6658 1.0147 0.0368  0.1556  0.2038  103 LEU A O   
820  C  CB  . LEU A 103 ? 1.2711 0.6306 0.9302 0.0190  0.1809  0.1938  103 LEU A CB  
821  C  CG  . LEU A 103 ? 1.3184 0.6289 0.9254 0.0257  0.1908  0.1794  103 LEU A CG  
822  C  CD1 . LEU A 103 ? 1.3111 0.6178 0.8831 0.0114  0.1986  0.1775  103 LEU A CD1 
823  C  CD2 . LEU A 103 ? 1.3162 0.5764 0.8959 0.0206  0.1709  0.1757  103 LEU A CD2 
824  N  N   . ASP A 104 ? 1.2619 0.6168 0.9696 0.0721  0.1905  0.1913  104 ASP A N   
825  C  CA  . ASP A 104 ? 1.2537 0.5806 0.9664 0.0856  0.1817  0.1930  104 ASP A CA  
826  C  C   . ASP A 104 ? 1.3759 0.6456 1.0476 0.0964  0.1921  0.1753  104 ASP A C   
827  O  O   . ASP A 104 ? 1.4090 0.6803 1.0804 0.1147  0.2158  0.1640  104 ASP A O   
828  C  CB  . ASP A 104 ? 1.2053 0.5727 0.9693 0.1056  0.1870  0.2028  104 ASP A CB  
829  C  CG  . ASP A 104 ? 1.2809 0.6258 1.0574 0.1166  0.1731  0.2115  104 ASP A CG  
830  O  OD1 . ASP A 104 ? 1.3658 0.6564 1.1164 0.1243  0.1737  0.2020  104 ASP A OD1 
831  O  OD2 . ASP A 104 ? 1.2894 0.6707 1.1013 0.1167  0.1608  0.2282  104 ASP A OD2 
832  N  N   . TYR A 105 ? 1.3741 0.5942 1.0127 0.0848  0.1749  0.1719  105 TYR A N   
833  C  CA  . TYR A 105 ? 1.4508 0.6100 1.0453 0.0911  0.1803  0.1525  105 TYR A CA  
834  C  C   . TYR A 105 ? 1.5277 0.6477 1.1304 0.0974  0.1639  0.1565  105 TYR A C   
835  O  O   . TYR A 105 ? 1.6633 0.7757 1.2672 0.0796  0.1403  0.1695  105 TYR A O   
836  C  CB  . TYR A 105 ? 1.5311 0.6625 1.0731 0.0670  0.1724  0.1442  105 TYR A CB  
837  C  CG  . TYR A 105 ? 1.5966 0.6616 1.0864 0.0687  0.1729  0.1227  105 TYR A CG  
838  C  CD1 . TYR A 105 ? 1.6519 0.7015 1.1122 0.0838  0.1988  0.1009  105 TYR A CD1 
839  C  CD2 . TYR A 105 ? 1.5679 0.5864 1.0378 0.0542  0.1477  0.1232  105 TYR A CD2 
840  C  CE1 . TYR A 105 ? 1.6865 0.6736 1.0950 0.0848  0.1994  0.0773  105 TYR A CE1 
841  C  CE2 . TYR A 105 ? 1.6435 0.5990 1.0651 0.0538  0.1460  0.1015  105 TYR A CE2 
842  C  CZ  . TYR A 105 ? 1.7191 0.6579 1.1081 0.0692  0.1717  0.0771  105 TYR A CZ  
843  O  OH  . TYR A 105 ? 1.8400 0.7143 1.1769 0.0685  0.1701  0.0518  105 TYR A OH  
844  N  N   . GLU A 106 ? 1.5396 0.6356 1.1513 0.1227  0.1769  0.1465  106 GLU A N   
845  C  CA  . GLU A 106 ? 1.5670 0.6229 1.1916 0.1309  0.1622  0.1515  106 GLU A CA  
846  C  C   . GLU A 106 ? 1.6601 0.6536 1.2545 0.1471  0.1749  0.1249  106 GLU A C   
847  O  O   . GLU A 106 ? 1.6917 0.6910 1.2820 0.1661  0.2020  0.1075  106 GLU A O   
848  C  CB  . GLU A 106 ? 1.3663 0.4623 1.0514 0.1491  0.1615  0.1727  106 GLU A CB  
849  C  CG  . GLU A 106 ? 1.3903 0.4501 1.0937 0.1550  0.1433  0.1852  106 GLU A CG  
850  C  CD  . GLU A 106 ? 1.4779 0.5772 1.2395 0.1754  0.1437  0.2066  106 GLU A CD  
851  O  OE1 . GLU A 106 ? 1.4648 0.6211 1.2524 0.1835  0.1571  0.2104  106 GLU A OE1 
852  O  OE2 . GLU A 106 ? 1.4521 0.5261 1.2349 0.1824  0.1294  0.2210  106 GLU A OE2 
853  N  N   . ALA A 107 ? 1.6469 0.5809 1.2211 0.1389  0.1558  0.1210  107 ALA A N   
854  C  CA  . ALA A 107 ? 1.6939 0.5595 1.2371 0.1517  0.1638  0.0930  107 ALA A CA  
855  C  C   . ALA A 107 ? 1.7441 0.5773 1.3227 0.1611  0.1467  0.1032  107 ALA A C   
856  O  O   . ALA A 107 ? 1.8338 0.6413 1.4034 0.1424  0.1219  0.0987  107 ALA A O   
857  C  CB  . ALA A 107 ? 1.6860 0.5073 1.1624 0.1270  0.1545  0.0732  107 ALA A CB  
858  N  N   . SER A 108 ? 1.7163 0.5761 1.3492 0.1866  0.1558  0.1177  108 SER A N   
859  C  CA  . SER A 108 ? 1.7732 0.6245 1.4529 0.1949  0.1375  0.1273  108 SER A CA  
860  C  C   . SER A 108 ? 1.8961 0.6872 1.5664 0.2191  0.1537  0.0962  108 SER A C   
861  O  O   . SER A 108 ? 2.0458 0.8086 1.6755 0.2328  0.1831  0.0676  108 SER A O   
862  C  CB  . SER A 108 ? 1.7266 0.6335 1.4690 0.2103  0.1365  0.1585  108 SER A CB  
863  O  OG  . SER A 108 ? 1.7560 0.6575 1.5245 0.2467  0.1639  0.1498  108 SER A OG  
864  N  N   . GLY A 109 ? 1.8305 0.6025 1.5402 0.2242  0.1348  0.1016  109 GLY A N   
865  C  CA  . GLY A 109 ? 1.9621 0.6775 1.6707 0.2465  0.1469  0.0713  109 GLY A CA  
866  C  C   . GLY A 109 ? 1.9689 0.6942 1.7041 0.2859  0.1818  0.0613  109 GLY A C   
867  O  O   . GLY A 109 ? 2.0410 0.7225 1.7646 0.3062  0.2010  0.0278  109 GLY A O   
868  N  N   . ARG A 110 ? 1.8516 0.6375 1.6254 0.2970  0.1906  0.0887  110 ARG A N   
869  C  CA  . ARG A 110 ? 1.7797 0.5890 1.5935 0.3343  0.2222  0.0852  110 ARG A CA  
870  C  C   . ARG A 110 ? 1.7666 0.5981 1.5439 0.3391  0.2570  0.0696  110 ARG A C   
871  O  O   . ARG A 110 ? 1.7614 0.6259 1.5060 0.3103  0.2482  0.0771  110 ARG A O   
872  C  CB  . ARG A 110 ? 1.8043 0.6737 1.6907 0.3434  0.2083  0.1266  110 ARG A CB  
873  C  CG  . ARG A 110 ? 1.8637 0.7180 1.7912 0.3402  0.1740  0.1449  110 ARG A CG  
874  C  CD  . ARG A 110 ? 1.8839 0.7962 1.8479 0.3262  0.1472  0.1900  110 ARG A CD  
875  N  NE  . ARG A 110 ? 1.9844 0.9129 1.9067 0.2904  0.1315  0.1997  110 ARG A NE  
876  C  CZ  . ARG A 110 ? 1.9589 0.9353 1.8979 0.2715  0.1079  0.2336  110 ARG A CZ  
877  N  NH1 . ARG A 110 ? 2.0081 1.0192 1.9991 0.2838  0.0960  0.2626  110 ARG A NH1 
878  N  NH2 . ARG A 110 ? 1.8142 0.8055 1.7169 0.2400  0.0962  0.2377  110 ARG A NH2 
879  N  N   . ALA A 111 ? 1.8046 0.6401 1.5967 0.3700  0.2916  0.0467  111 ALA A N   
880  C  CA  . ALA A 111 ? 1.8059 0.6870 1.5726 0.3695  0.3215  0.0306  111 ALA A CA  
881  C  C   . ALA A 111 ? 1.7888 0.7605 1.5994 0.3641  0.3199  0.0632  111 ALA A C   
882  O  O   . ALA A 111 ? 1.8113 0.8242 1.5961 0.3511  0.3344  0.0582  111 ALA A O   
883  C  CB  . ALA A 111 ? 1.8712 0.7358 1.6469 0.4056  0.3614  -0.0016 111 ALA A CB  
884  N  N   . VAL A 112 ? 1.7869 0.7898 1.6625 0.3725  0.3017  0.0967  112 VAL A N   
885  C  CA  . VAL A 112 ? 1.7578 0.8456 1.6743 0.3660  0.2976  0.1261  112 VAL A CA  
886  C  C   . VAL A 112 ? 1.7973 0.9045 1.6764 0.3268  0.2732  0.1398  112 VAL A C   
887  O  O   . VAL A 112 ? 1.7113 0.8816 1.5999 0.3148  0.2760  0.1512  112 VAL A O   
888  C  CB  . VAL A 112 ? 1.7000 0.8152 1.6937 0.3858  0.2832  0.1582  112 VAL A CB  
889  C  CG1 . VAL A 112 ? 1.6063 0.8113 1.6480 0.3867  0.2867  0.1813  112 VAL A CG1 
890  C  CG2 . VAL A 112 ? 1.7821 0.8566 1.8113 0.4242  0.3015  0.1440  112 VAL A CG2 
891  N  N   . SER A 113 ? 1.8931 0.9469 1.7326 0.3064  0.2494  0.1385  113 SER A N   
892  C  CA  . SER A 113 ? 1.9190 0.9890 1.7287 0.2707  0.2256  0.1524  113 SER A CA  
893  C  C   . SER A 113 ? 1.9768 1.0016 1.7144 0.2488  0.2266  0.1271  113 SER A C   
894  O  O   . SER A 113 ? 2.0397 1.0589 1.7512 0.2201  0.2036  0.1365  113 SER A O   
895  C  CB  . SER A 113 ? 1.9717 1.0309 1.8032 0.2609  0.1931  0.1805  113 SER A CB  
896  O  OG  . SER A 113 ? 2.0156 1.1236 1.9102 0.2772  0.1888  0.2077  113 SER A OG  
897  N  N   . SER A 114 ? 1.9210 0.9152 1.6262 0.2617  0.2525  0.0955  114 SER A N   
898  C  CA  . SER A 114 ? 1.8338 0.7933 1.4670 0.2409  0.2554  0.0713  114 SER A CA  
899  C  C   . SER A 114 ? 1.7914 0.8052 1.4150 0.2390  0.2805  0.0664  114 SER A C   
900  O  O   . SER A 114 ? 1.8253 0.8364 1.4377 0.2581  0.3116  0.0441  114 SER A O   
901  C  CB  . SER A 114 ? 1.8558 0.7384 1.4512 0.2540  0.2655  0.0377  114 SER A CB  
902  O  OG  . SER A 114 ? 1.8151 0.6441 1.4178 0.2504  0.2388  0.0439  114 SER A OG  
903  N  N   . ARG A 115 ? 1.7019 0.7654 1.3319 0.2160  0.2675  0.0876  115 ARG A N   
904  C  CA  . ARG A 115 ? 1.6297 0.7526 1.2672 0.2142  0.2883  0.0903  115 ARG A CA  
905  C  C   . ARG A 115 ? 1.6480 0.7944 1.2635 0.1808  0.2704  0.1033  115 ARG A C   
906  O  O   . ARG A 115 ? 1.6858 0.8181 1.2969 0.1618  0.2417  0.1156  115 ARG A O   
907  C  CB  . ARG A 115 ? 1.5667 0.7510 1.2772 0.2343  0.2970  0.1094  115 ARG A CB  
908  C  CG  . ARG A 115 ? 1.6363 0.8605 1.3834 0.2183  0.2688  0.1391  115 ARG A CG  
909  C  CD  . ARG A 115 ? 1.7517 1.0060 1.5653 0.2407  0.2654  0.1575  115 ARG A CD  
910  N  NE  . ARG A 115 ? 1.7996 1.1058 1.6550 0.2606  0.2913  0.1581  115 ARG A NE  
911  C  CZ  . ARG A 115 ? 1.8255 1.1794 1.7451 0.2756  0.2881  0.1782  115 ARG A CZ  
912  N  NH1 . ARG A 115 ? 1.7769 1.1328 1.7218 0.2730  0.2605  0.1996  115 ARG A NH1 
913  N  NH2 . ARG A 115 ? 1.8602 1.2622 1.8192 0.2924  0.3121  0.1785  115 ARG A NH2 
914  N  N   . LEU A 116 ? 1.6077 0.7911 1.2125 0.1743  0.2888  0.1012  116 LEU A N   
915  C  CA  . LEU A 116 ? 1.5039 0.7235 1.1056 0.1471  0.2763  0.1167  116 LEU A CA  
916  C  C   . LEU A 116 ? 1.5157 0.8053 1.1698 0.1548  0.2920  0.1301  116 LEU A C   
917  O  O   . LEU A 116 ? 1.6169 0.9241 1.2763 0.1712  0.3214  0.1211  116 LEU A O   
918  C  CB  . LEU A 116 ? 1.4867 0.6819 1.0236 0.1278  0.2809  0.1038  116 LEU A CB  
919  C  CG  . LEU A 116 ? 1.4661 0.6723 0.9857 0.0957  0.2595  0.1174  116 LEU A CG  
920  C  CD1 . LEU A 116 ? 1.4969 0.6785 0.9515 0.0814  0.2676  0.1047  116 LEU A CD1 
921  C  CD2 . LEU A 116 ? 1.3982 0.6700 0.9680 0.0888  0.2593  0.1381  116 LEU A CD2 
922  N  N   . GLN A 117 ? 1.4530 0.7830 1.1461 0.1426  0.2731  0.1507  117 GLN A N   
923  C  CA  . GLN A 117 ? 1.4465 0.8425 1.1917 0.1470  0.2835  0.1636  117 GLN A CA  
924  C  C   . GLN A 117 ? 1.4024 0.8299 1.1538 0.1196  0.2675  0.1766  117 GLN A C   
925  O  O   . GLN A 117 ? 1.4843 0.8946 1.2232 0.1026  0.2428  0.1819  117 GLN A O   
926  C  CB  . GLN A 117 ? 1.4804 0.9024 1.2833 0.1667  0.2779  0.1753  117 GLN A CB  
927  C  CG  . GLN A 117 ? 1.5719 0.9623 1.3729 0.1642  0.2508  0.1822  117 GLN A CG  
928  C  CD  . GLN A 117 ? 1.5837 1.0009 1.4400 0.1837  0.2448  0.1969  117 GLN A CD  
929  O  OE1 . GLN A 117 ? 1.5956 1.0684 1.4981 0.1908  0.2517  0.2068  117 GLN A OE1 
930  N  NE2 . GLN A 117 ? 1.6085 0.9869 1.4623 0.1913  0.2302  0.2003  117 GLN A NE2 
931  N  N   . LEU A 118 ? 1.2997 0.7734 1.0735 0.1158  0.2825  0.1818  118 LEU A N   
932  C  CA  . LEU A 118 ? 1.1801 0.6883 0.9712 0.0922  0.2696  0.1938  118 LEU A CA  
933  C  C   . LEU A 118 ? 1.1608 0.7260 1.0162 0.0986  0.2668  0.2058  118 LEU A C   
934  O  O   . LEU A 118 ? 1.1627 0.7622 1.0502 0.1128  0.2870  0.2076  118 LEU A O   
935  C  CB  . LEU A 118 ? 1.1471 0.6628 0.9157 0.0792  0.2856  0.1929  118 LEU A CB  
936  C  CG  . LEU A 118 ? 1.2010 0.6639 0.9016 0.0697  0.2865  0.1822  118 LEU A CG  
937  C  CD1 . LEU A 118 ? 1.1656 0.6434 0.8473 0.0543  0.2999  0.1869  118 LEU A CD1 
938  C  CD2 . LEU A 118 ? 1.2459 0.6747 0.9257 0.0533  0.2562  0.1839  118 LEU A CD2 
939  N  N   . GLU A 119 ? 1.1763 0.7535 1.0503 0.0873  0.2419  0.2139  119 GLU A N   
940  C  CA  . GLU A 119 ? 1.1847 0.8105 1.1126 0.0923  0.2331  0.2243  119 GLU A CA  
941  C  C   . GLU A 119 ? 1.1625 0.8206 1.1091 0.0687  0.2193  0.2292  119 GLU A C   
942  O  O   . GLU A 119 ? 1.2176 0.8562 1.1433 0.0523  0.2021  0.2281  119 GLU A O   
943  C  CB  . GLU A 119 ? 1.1873 0.7958 1.1167 0.1022  0.2158  0.2285  119 GLU A CB  
944  C  CG  . GLU A 119 ? 1.1915 0.8463 1.1661 0.1028  0.1996  0.2409  119 GLU A CG  
945  C  CD  . GLU A 119 ? 1.3515 1.0482 1.3742 0.1222  0.2122  0.2473  119 GLU A CD  
946  O  OE1 . GLU A 119 ? 1.4317 1.1455 1.4659 0.1257  0.2333  0.2435  119 GLU A OE1 
947  O  OE2 . GLU A 119 ? 1.3707 1.0841 1.4210 0.1342  0.2008  0.2581  119 GLU A OE2 
948  N  N   . ASP A 120 ? 1.3257 1.2689 1.0363 -0.0004 0.3252  0.3251  120 ASP A N   
949  C  CA  . ASP A 120 ? 1.3094 1.2400 1.0381 0.0514  0.3165  0.3674  120 ASP A CA  
950  C  C   . ASP A 120 ? 1.2761 1.2391 1.0740 0.0768  0.3181  0.3591  120 ASP A C   
951  O  O   . ASP A 120 ? 1.2792 1.2961 1.1285 0.0619  0.3088  0.3316  120 ASP A O   
952  C  CB  . ASP A 120 ? 1.3163 1.2968 1.0637 0.0617  0.2909  0.3903  120 ASP A CB  
953  C  CG  . ASP A 120 ? 1.3589 1.3425 1.1308 0.1156  0.2807  0.4280  120 ASP A CG  
954  O  OD1 . ASP A 120 ? 1.3121 1.3328 1.1475 0.1383  0.2844  0.4266  120 ASP A OD1 
955  O  OD2 . ASP A 120 ? 1.4382 1.3903 1.1643 0.1353  0.2676  0.4572  120 ASP A OD2 
956  N  N   . ALA A 121 ? 1.3026 1.2297 1.0968 0.1161  0.3282  0.3828  121 ALA A N   
957  C  CA  . ALA A 121 ? 1.2554 1.2042 1.0985 0.1359  0.3348  0.3772  121 ALA A CA  
958  C  C   . ALA A 121 ? 1.2764 1.3049 1.1920 0.1406  0.3178  0.3838  121 ALA A C   
959  O  O   . ALA A 121 ? 1.2449 1.2900 1.1948 0.1435  0.3208  0.3765  121 ALA A O   
960  C  CB  . ALA A 121 ? 1.2744 1.1757 1.0954 0.1777  0.3513  0.3991  121 ALA A CB  
961  N  N   . GLY A 122 ? 1.2967 1.3701 1.2307 0.1388  0.2990  0.3978  122 GLY A N   
962  C  CA  . GLY A 122 ? 1.2408 1.3897 1.2436 0.1352  0.2818  0.4001  122 GLY A CA  
963  C  C   . GLY A 122 ? 1.1421 1.3112 1.1705 0.1014  0.2690  0.3668  122 GLY A C   
964  O  O   . GLY A 122 ? 1.1833 1.3940 1.2626 0.0957  0.2565  0.3668  122 GLY A O   
965  N  N   . SER A 123 ? 1.0523 1.1929 1.0458 0.0783  0.2709  0.3357  123 SER A N   
966  C  CA  . SER A 123 ? 1.0088 1.1692 1.0281 0.0548  0.2552  0.2956  123 SER A CA  
967  C  C   . SER A 123 ? 1.0444 1.1794 1.0780 0.0655  0.2578  0.2887  123 SER A C   
968  O  O   . SER A 123 ? 1.1133 1.2633 1.1800 0.0578  0.2366  0.2728  123 SER A O   
969  C  CB  . SER A 123 ? 1.0291 1.1795 1.0118 0.0284  0.2597  0.2575  123 SER A CB  
970  O  OG  . SER A 123 ? 1.1095 1.2833 1.0710 0.0119  0.2552  0.2633  123 SER A OG  
971  N  N   . LEU A 124 ? 1.0032 1.0919 1.0050 0.0836  0.2813  0.3005  124 LEU A N   
972  C  CA  . LEU A 124 ? 1.0507 1.1117 1.0547 0.0948  0.2846  0.2973  124 LEU A CA  
973  C  C   . LEU A 124 ? 1.1461 1.2313 1.1847 0.1026  0.2816  0.3282  124 LEU A C   
974  O  O   . LEU A 124 ? 1.1576 1.2230 1.1981 0.1008  0.2751  0.3247  124 LEU A O   
975  C  CB  . LEU A 124 ? 1.0881 1.0970 1.0473 0.1124  0.3114  0.3017  124 LEU A CB  
976  C  CG  . LEU A 124 ? 1.1013 1.0805 1.0227 0.0969  0.3180  0.2671  124 LEU A CG  
977  C  CD1 . LEU A 124 ? 1.1568 1.0790 1.0318 0.1139  0.3444  0.2772  124 LEU A CD1 
978  C  CD2 . LEU A 124 ? 0.9608 0.9459 0.8948 0.0840  0.2990  0.2204  124 LEU A CD2 
979  N  N   . LEU A 125 ? 1.1758 1.3036 1.2385 0.1094  0.2853  0.3574  125 LEU A N   
980  C  CA  . LEU A 125 ? 1.1592 1.3271 1.2627 0.1087  0.2848  0.3820  125 LEU A CA  
981  C  C   . LEU A 125 ? 1.1864 1.3750 1.3230 0.0796  0.2551  0.3688  125 LEU A C   
982  O  O   . LEU A 125 ? 1.2354 1.4272 1.3891 0.0672  0.2526  0.3810  125 LEU A O   
983  C  CB  . LEU A 125 ? 1.0388 1.2592 1.1669 0.1271  0.2928  0.4089  125 LEU A CB  
984  C  CG  . LEU A 125 ? 1.0266 1.2331 1.1346 0.1631  0.3213  0.4270  125 LEU A CG  
985  C  CD1 . LEU A 125 ? 1.0695 1.3495 1.2233 0.1828  0.3234  0.4494  125 LEU A CD1 
986  C  CD2 . LEU A 125 ? 0.9736 1.1475 1.0642 0.1649  0.3412  0.4262  125 LEU A CD2 
987  N  N   . GLN A 126 ? 1.1731 1.3721 1.3137 0.0660  0.2329  0.3429  126 GLN A N   
988  C  CA  . GLN A 126 ? 1.1490 1.3622 1.3187 0.0421  0.2006  0.3230  126 GLN A CA  
989  C  C   . GLN A 126 ? 1.2010 1.3584 1.3521 0.0377  0.1831  0.2938  126 GLN A C   
990  O  O   . GLN A 126 ? 1.2364 1.3930 1.4045 0.0233  0.1505  0.2675  126 GLN A O   
991  C  CB  . GLN A 126 ? 1.1157 1.3660 1.2939 0.0318  0.1835  0.3001  126 GLN A CB  
992  C  CG  . GLN A 126 ? 1.1497 1.4579 1.3508 0.0336  0.1845  0.3264  126 GLN A CG  
993  C  CD  . GLN A 126 ? 1.1755 1.5292 1.4130 0.0113  0.1529  0.3096  126 GLN A CD  
994  O  OE1 . GLN A 126 ? 1.1856 1.5273 1.4225 -0.0029 0.1316  0.2718  126 GLN A OE1 
995  N  NE2 . GLN A 126 ? 1.2156 1.6257 1.4882 0.0102  0.1476  0.3332  126 GLN A NE2 
996  N  N   . VAL A 127 ? 1.2030 1.3119 1.3181 0.0529  0.1992  0.2948  127 VAL A N   
997  C  CA  . VAL A 127 ? 1.2330 1.2905 1.3267 0.0553  0.1761  0.2600  127 VAL A CA  
998  C  C   . VAL A 127 ? 1.3327 1.3340 1.3882 0.0676  0.1889  0.2774  127 VAL A C   
999  O  O   . VAL A 127 ? 1.4349 1.3839 1.4699 0.0678  0.1631  0.2651  127 VAL A O   
1000 C  CB  . VAL A 127 ? 1.1968 1.2639 1.2808 0.0598  0.1742  0.2150  127 VAL A CB  
1001 C  CG1 . VAL A 127 ? 1.1999 1.2686 1.2581 0.0686  0.2117  0.2305  127 VAL A CG1 
1002 C  CG2 . VAL A 127 ? 1.2734 1.2994 1.3400 0.0701  0.1512  0.1733  127 VAL A CG2 
1003 N  N   . PHE A 128 ? 1.3327 1.3391 1.3727 0.0802  0.2261  0.3053  128 PHE A N   
1004 C  CA  . PHE A 128 ? 1.4266 1.3868 1.4275 0.0907  0.2417  0.3222  128 PHE A CA  
1005 C  C   . PHE A 128 ? 1.5072 1.4617 1.5119 0.0715  0.2385  0.3542  128 PHE A C   
1006 O  O   . PHE A 128 ? 1.4294 1.4382 1.4729 0.0572  0.2486  0.3783  128 PHE A O   
1007 C  CB  . PHE A 128 ? 1.3976 1.3688 1.3838 0.1107  0.2820  0.3403  128 PHE A CB  
1008 C  CG  . PHE A 128 ? 1.3625 1.3052 1.3187 0.1252  0.2880  0.3100  128 PHE A CG  
1009 C  CD1 . PHE A 128 ? 1.3635 1.2724 1.3018 0.1244  0.2632  0.2702  128 PHE A CD1 
1010 C  CD2 . PHE A 128 ? 1.3541 1.3024 1.2989 0.1396  0.3164  0.3188  128 PHE A CD2 
1011 C  CE1 . PHE A 128 ? 1.3418 1.2357 1.2579 0.1313  0.2707  0.2381  128 PHE A CE1 
1012 C  CE2 . PHE A 128 ? 1.3764 1.2932 1.2896 0.1444  0.3233  0.2913  128 PHE A CE2 
1013 C  CZ  . PHE A 128 ? 1.3653 1.2608 1.2671 0.1371  0.3026  0.2501  128 PHE A CZ  
1014 N  N   . ASP A 129 ? 1.6288 1.5164 1.5889 0.0688  0.2238  0.3541  129 ASP A N   
1015 C  CA  . ASP A 129 ? 1.7519 1.6204 1.6974 0.0426  0.2263  0.3888  129 ASP A CA  
1016 C  C   . ASP A 129 ? 1.7660 1.6751 1.7092 0.0438  0.2757  0.4229  129 ASP A C   
1017 O  O   . ASP A 129 ? 1.7641 1.7374 1.7488 0.0247  0.2941  0.4465  129 ASP A O   
1018 C  CB  . ASP A 129 ? 1.8983 1.6688 1.7789 0.0408  0.1950  0.3825  129 ASP A CB  
1019 C  CG  . ASP A 129 ? 1.9957 1.7279 1.8833 0.0431  0.1403  0.3451  129 ASP A CG  
1020 O  OD1 . ASP A 129 ? 1.9935 1.7678 1.9320 0.0276  0.1266  0.3379  129 ASP A OD1 
1021 O  OD2 . ASP A 129 ? 2.0659 1.7299 1.9092 0.0634  0.1089  0.3191  129 ASP A OD2 
1022 N  N   . ALA A 130 ? 1.7845 1.6628 1.6820 0.0675  0.2964  0.4209  130 ALA A N   
1023 C  CA  . ALA A 130 ? 1.7445 1.6644 1.6401 0.0790  0.3436  0.4426  130 ALA A CA  
1024 C  C   . ALA A 130 ? 1.6353 1.5840 1.5510 0.1135  0.3585  0.4252  130 ALA A C   
1025 O  O   . ALA A 130 ? 1.6722 1.5744 1.5494 0.1350  0.3577  0.4037  130 ALA A O   
1026 C  CB  . ALA A 130 ? 1.8276 1.6884 1.6502 0.0815  0.3571  0.4513  130 ALA A CB  
1027 N  N   . PRO A 131 ? 1.5152 1.5336 1.4851 0.1187  0.3691  0.4330  131 PRO A N   
1028 C  CA  . PRO A 131 ? 1.4299 1.4547 1.4042 0.1486  0.3771  0.4190  131 PRO A CA  
1029 C  C   . PRO A 131 ? 1.4498 1.4546 1.3884 0.1797  0.4090  0.4197  131 PRO A C   
1030 O  O   . PRO A 131 ? 1.4909 1.4544 1.4011 0.1976  0.4093  0.4002  131 PRO A O   
1031 C  CB  . PRO A 131 ? 1.3497 1.4507 1.3828 0.1484  0.3776  0.4333  131 PRO A CB  
1032 C  CG  . PRO A 131 ? 1.3229 1.4536 1.3886 0.1116  0.3603  0.4436  131 PRO A CG  
1033 C  CD  . PRO A 131 ? 1.4521 1.5413 1.4776 0.0958  0.3694  0.4529  131 PRO A CD  
1034 N  N   . ALA A 132 ? 1.4444 1.4795 1.3824 0.1837  0.4372  0.4388  132 ALA A N   
1035 C  CA  . ALA A 132 ? 1.4493 1.4715 1.3554 0.2172  0.4682  0.4354  132 ALA A CA  
1036 C  C   . ALA A 132 ? 1.5641 1.5039 1.4039 0.2208  0.4632  0.4159  132 ALA A C   
1037 O  O   . ALA A 132 ? 1.6412 1.5444 1.4530 0.2470  0.4716  0.3985  132 ALA A O   
1038 C  CB  . ALA A 132 ? 1.3807 1.4659 1.3020 0.2164  0.5012  0.4543  132 ALA A CB  
1039 N  N   . SER A 133 ? 1.5890 1.4940 1.3997 0.1949  0.4461  0.4174  133 SER A N   
1040 C  CA  . SER A 133 ? 1.7001 1.5309 1.4473 0.2018  0.4355  0.3967  133 SER A CA  
1041 C  C   . SER A 133 ? 1.6503 1.4485 1.3990 0.2090  0.4102  0.3628  133 SER A C   
1042 O  O   . SER A 133 ? 1.6889 1.4460 1.3996 0.2259  0.4138  0.3390  133 SER A O   
1043 C  CB  . SER A 133 ? 1.8609 1.6524 1.5710 0.1752  0.4140  0.4070  133 SER A CB  
1044 O  OG  . SER A 133 ? 1.8835 1.6626 1.6185 0.1567  0.3730  0.3974  133 SER A OG  
1045 N  N   . SER A 134 ? 1.5900 1.4111 1.3820 0.1930  0.3861  0.3572  134 SER A N   
1046 C  CA  . SER A 134 ? 1.5131 1.3173 1.3088 0.1926  0.3662  0.3218  134 SER A CA  
1047 C  C   . SER A 134 ? 1.5313 1.3425 1.3305 0.2066  0.3890  0.3187  134 SER A C   
1048 O  O   . SER A 134 ? 1.5408 1.3212 1.3181 0.2071  0.3865  0.2887  134 SER A O   
1049 C  CB  . SER A 134 ? 1.4153 1.2452 1.2523 0.1704  0.3341  0.3135  134 SER A CB  
1050 O  OG  . SER A 134 ? 1.4520 1.2572 1.2778 0.1588  0.3067  0.3148  134 SER A OG  
1051 N  N   . PHE A 135 ? 1.4928 1.3418 1.3168 0.2173  0.4091  0.3474  135 PHE A N   
1052 C  CA  . PHE A 135 ? 1.4576 1.2972 1.2752 0.2342  0.4236  0.3472  135 PHE A CA  
1053 C  C   . PHE A 135 ? 1.4252 1.2155 1.1952 0.2596  0.4466  0.3379  135 PHE A C   
1054 O  O   . PHE A 135 ? 1.4121 1.1582 1.1535 0.2632  0.4502  0.3221  135 PHE A O   
1055 C  CB  . PHE A 135 ? 1.4741 1.3689 1.3325 0.2464  0.4308  0.3769  135 PHE A CB  
1056 C  CG  . PHE A 135 ? 1.4170 1.3379 1.3042 0.2280  0.4095  0.3782  135 PHE A CG  
1057 C  CD1 . PHE A 135 ? 1.4055 1.2889 1.2666 0.2138  0.4002  0.3572  135 PHE A CD1 
1058 C  CD2 . PHE A 135 ? 1.3470 1.3340 1.2854 0.2207  0.4000  0.3980  135 PHE A CD2 
1059 C  CE1 . PHE A 135 ? 1.3363 1.2459 1.2161 0.1945  0.3828  0.3573  135 PHE A CE1 
1060 C  CE2 . PHE A 135 ? 1.2906 1.3024 1.2511 0.2045  0.3790  0.3972  135 PHE A CE2 
1061 C  CZ  . PHE A 135 ? 1.2868 1.2591 1.2153 0.1921  0.3708  0.3774  135 PHE A CZ  
1062 N  N   . VAL A 136 ? 1.3565 1.1505 1.1120 0.2737  0.4628  0.3463  136 VAL A N   
1063 C  CA  . VAL A 136 ? 1.3872 1.1350 1.0946 0.2988  0.4835  0.3327  136 VAL A CA  
1064 C  C   . VAL A 136 ? 1.3945 1.0876 1.0619 0.2853  0.4687  0.2986  136 VAL A C   
1065 O  O   . VAL A 136 ? 1.4841 1.1289 1.1121 0.2985  0.4794  0.2780  136 VAL A O   
1066 C  CB  . VAL A 136 ? 1.4023 1.1780 1.1016 0.3153  0.5078  0.3483  136 VAL A CB  
1067 C  CG1 . VAL A 136 ? 1.3655 1.2128 1.1146 0.3301  0.5237  0.3739  136 VAL A CG1 
1068 C  CG2 . VAL A 136 ? 1.4157 1.1911 1.1002 0.2892  0.4949  0.3522  136 VAL A CG2 
1069 N  N   . ALA A 137 ? 1.3270 1.0273 1.0047 0.2608  0.4413  0.2881  137 ALA A N   
1070 C  CA  . ALA A 137 ? 1.3473 1.0088 0.9950 0.2526  0.4221  0.2491  137 ALA A CA  
1071 C  C   . ALA A 137 ? 1.4767 1.1210 1.1242 0.2407  0.4216  0.2202  137 ALA A C   
1072 O  O   . ALA A 137 ? 1.5731 1.1813 1.1880 0.2402  0.4218  0.1868  137 ALA A O   
1073 C  CB  . ALA A 137 ? 1.2405 0.9141 0.9036 0.2354  0.3866  0.2406  137 ALA A CB  
1074 N  N   . ILE A 138 ? 1.4484 1.1179 1.1277 0.2270  0.4212  0.2321  138 ILE A N   
1075 C  CA  . ILE A 138 ? 1.5135 1.1624 1.1818 0.2066  0.4238  0.2088  138 ILE A CA  
1076 C  C   . ILE A 138 ? 1.5377 1.1362 1.1689 0.2245  0.4496  0.2236  138 ILE A C   
1077 O  O   . ILE A 138 ? 1.6057 1.1600 1.2051 0.2070  0.4561  0.2038  138 ILE A O   
1078 C  CB  . ILE A 138 ? 1.5909 1.2833 1.2974 0.1809  0.4096  0.2126  138 ILE A CB  
1079 C  CG1 . ILE A 138 ? 1.5975 1.3118 1.3242 0.1950  0.4171  0.2576  138 ILE A CG1 
1080 C  CG2 . ILE A 138 ? 1.6117 1.3467 1.3540 0.1705  0.3806  0.1956  138 ILE A CG2 
1081 C  CD1 . ILE A 138 ? 1.5657 1.3321 1.3334 0.1723  0.3982  0.2620  138 ILE A CD1 
1082 N  N   . PHE A 139 ? 1.5006 1.1037 1.1335 0.2585  0.4641  0.2554  139 PHE A N   
1083 C  CA  . PHE A 139 ? 1.5596 1.1098 1.1541 0.2877  0.4850  0.2614  139 PHE A CA  
1084 C  C   . PHE A 139 ? 1.6495 1.1501 1.1991 0.2911  0.4924  0.2287  139 PHE A C   
1085 O  O   . PHE A 139 ? 1.7197 1.1606 1.2313 0.2778  0.4960  0.2063  139 PHE A O   
1086 C  CB  . PHE A 139 ? 1.5298 1.1168 1.1461 0.3267  0.4985  0.2928  139 PHE A CB  
1087 C  CG  . PHE A 139 ? 1.5808 1.1868 1.2215 0.3390  0.4950  0.3203  139 PHE A CG  
1088 C  CD1 . PHE A 139 ? 1.6118 1.1530 1.2147 0.3596  0.4987  0.3232  139 PHE A CD1 
1089 C  CD2 . PHE A 139 ? 1.5699 1.2517 1.2659 0.3314  0.4846  0.3427  139 PHE A CD2 
1090 C  CE1 . PHE A 139 ? 1.5647 1.1157 1.1815 0.3762  0.4894  0.3486  139 PHE A CE1 
1091 C  CE2 . PHE A 139 ? 1.5139 1.2164 1.2311 0.3458  0.4775  0.3654  139 PHE A CE2 
1092 C  CZ  . PHE A 139 ? 1.4799 1.1168 1.1560 0.3705  0.4785  0.3688  139 PHE A CZ  
1093 N  N   . LEU A 140 ? 1.6457 1.1675 1.1935 0.3053  0.4940  0.2258  140 LEU A N   
1094 C  CA  . LEU A 140 ? 1.7154 1.1946 1.2173 0.3119  0.4980  0.1943  140 LEU A CA  
1095 C  C   . LEU A 140 ? 1.6539 1.1104 1.1452 0.2778  0.4811  0.1526  140 LEU A C   
1096 O  O   . LEU A 140 ? 1.6717 1.0808 1.1229 0.2781  0.4863  0.1215  140 LEU A O   
1097 C  CB  . LEU A 140 ? 1.7140 1.2215 1.2098 0.3237  0.4955  0.1999  140 LEU A CB  
1098 C  CG  . LEU A 140 ? 1.7647 1.2346 1.2094 0.3301  0.4919  0.1667  140 LEU A CG  
1099 C  CD1 . LEU A 140 ? 1.7898 1.2680 1.2043 0.3566  0.5101  0.1840  140 LEU A CD1 
1100 C  CD2 . LEU A 140 ? 1.7106 1.1878 1.1594 0.3066  0.4572  0.1382  140 LEU A CD2 
1101 N  N   . ALA A 141 ? 1.5904 1.0864 1.1195 0.2477  0.4613  0.1466  141 ALA A N   
1102 C  CA  . ALA A 141 ? 1.6158 1.1058 1.1436 0.2111  0.4506  0.1034  141 ALA A CA  
1103 C  C   . ALA A 141 ? 1.7405 1.1708 1.2327 0.1968  0.4710  0.1013  141 ALA A C   
1104 O  O   . ALA A 141 ? 1.9092 1.2877 1.3602 0.1969  0.4800  0.0752  141 ALA A O   
1105 C  CB  . ALA A 141 ? 1.5347 1.0847 1.1117 0.1835  0.4294  0.0970  141 ALA A CB  
1106 N  N   . VAL A 142 ? 1.7149 1.1442 1.2157 0.1853  0.4760  0.1298  142 VAL A N   
1107 C  CA  . VAL A 142 ? 1.8275 1.1863 1.2830 0.1663  0.4902  0.1337  142 VAL A CA  
1108 C  C   . VAL A 142 ? 1.9239 1.2012 1.3248 0.1882  0.5049  0.1240  142 VAL A C   
1109 O  O   . VAL A 142 ? 2.0247 1.2410 1.3825 0.1563  0.5119  0.0974  142 VAL A O   
1110 C  CB  . VAL A 142 ? 1.8023 1.1590 1.2634 0.1794  0.4910  0.1814  142 VAL A CB  
1111 C  CG1 . VAL A 142 ? 1.8565 1.1122 1.2521 0.1786  0.5021  0.1946  142 VAL A CG1 
1112 C  CG2 . VAL A 142 ? 1.7396 1.1600 1.2389 0.1428  0.4780  0.1822  142 VAL A CG2 
1113 N  N   . LEU A 143 ? 1.8622 1.1403 1.2636 0.2389  0.5105  0.1412  143 LEU A N   
1114 C  CA  . LEU A 143 ? 1.9596 1.1631 1.3098 0.2679  0.5244  0.1312  143 LEU A CA  
1115 C  C   . LEU A 143 ? 2.0638 1.2539 1.3917 0.2540  0.5231  0.0836  143 LEU A C   
1116 O  O   . LEU A 143 ? 2.3016 1.4154 1.5788 0.2599  0.5328  0.0636  143 LEU A O   
1117 C  CB  . LEU A 143 ? 1.9941 1.2218 1.3572 0.3262  0.5336  0.1598  143 LEU A CB  
1118 C  CG  . LEU A 143 ? 2.2173 1.3699 1.5362 0.3700  0.5472  0.1640  143 LEU A CG  
1119 C  CD1 . LEU A 143 ? 2.2385 1.4498 1.5947 0.4195  0.5539  0.1965  143 LEU A CD1 
1120 C  CD2 . LEU A 143 ? 2.3508 1.4579 1.6257 0.3823  0.5564  0.1269  143 LEU A CD2 
1121 N  N   . GLU A 144 ? 2.0287 1.2864 1.3906 0.2378  0.5075  0.0624  144 GLU A N   
1122 C  CA  . GLU A 144 ? 2.0708 1.3214 1.4135 0.2247  0.4997  0.0125  144 GLU A CA  
1123 C  C   . GLU A 144 ? 2.1274 1.3557 1.4605 0.1691  0.4989  -0.0266 144 GLU A C   
1124 O  O   . GLU A 144 ? 2.1750 1.3557 1.4706 0.1566  0.5035  -0.0640 144 GLU A O   
1125 C  CB  . GLU A 144 ? 1.9901 1.3136 1.3671 0.2314  0.4763  0.0015  144 GLU A CB  
1126 C  CG  . GLU A 144 ? 2.0448 1.3788 1.4151 0.2124  0.4575  -0.0571 144 GLU A CG  
1127 C  CD  . GLU A 144 ? 2.1117 1.4949 1.4975 0.2329  0.4286  -0.0647 144 GLU A CD  
1128 O  OE1 . GLU A 144 ? 2.1479 1.5559 1.5412 0.2204  0.4036  -0.1148 144 GLU A OE1 
1129 O  OE2 . GLU A 144 ? 2.1265 1.5221 1.5150 0.2605  0.4293  -0.0219 144 GLU A OE2 
1130 N  N   . ILE A 145 ? 2.0905 1.3555 1.4550 0.1315  0.4950  -0.0209 145 ILE A N   
1131 C  CA  . ILE A 145 ? 2.0906 1.3484 1.4466 0.0696  0.4987  -0.0610 145 ILE A CA  
1132 C  C   . ILE A 145 ? 2.1332 1.2861 1.4264 0.0476  0.5201  -0.0425 145 ILE A C   
1133 O  O   . ILE A 145 ? 2.2601 1.3665 1.5172 0.0027  0.5291  -0.0788 145 ILE A O   
1134 C  CB  . ILE A 145 ? 2.0771 1.4230 1.4882 0.0340  0.4870  -0.0709 145 ILE A CB  
1135 C  CG1 . ILE A 145 ? 2.0043 1.4356 1.4714 0.0659  0.4597  -0.0791 145 ILE A CG1 
1136 C  CG2 . ILE A 145 ? 2.1821 1.5465 1.5924 -0.0326 0.4923  -0.1272 145 ILE A CG2 
1137 C  CD1 . ILE A 145 ? 1.9188 1.3833 1.4178 0.0914  0.4529  -0.0288 145 ILE A CD1 
1138 N  N   . TRP A 146 ? 1.8886 1.3522 1.5332 0.3914  0.4728  -0.2154 146 TRP A N   
1139 C  CA  . TRP A 146 ? 1.7270 1.1876 1.4103 0.3694  0.5073  -0.2285 146 TRP A CA  
1140 C  C   . TRP A 146 ? 1.7571 1.1873 1.3937 0.3744  0.5398  -0.2196 146 TRP A C   
1141 O  O   . TRP A 146 ? 1.6875 1.0978 1.3170 0.3781  0.5657  -0.1778 146 TRP A O   
1142 C  CB  . TRP A 146 ? 1.5929 1.0516 1.3330 0.3552  0.5253  -0.1987 146 TRP A CB  
1143 C  CG  . TRP A 146 ? 1.5324 1.0191 1.3278 0.3436  0.5053  -0.2185 146 TRP A CG  
1144 C  CD1 . TRP A 146 ? 1.5144 1.0190 1.3502 0.3253  0.5096  -0.2574 146 TRP A CD1 
1145 C  CD2 . TRP A 146 ? 1.5369 1.0337 1.3507 0.3490  0.4810  -0.2007 146 TRP A CD2 
1146 N  NE1 . TRP A 146 ? 1.5819 1.1124 1.4625 0.3197  0.4901  -0.2646 146 TRP A NE1 
1147 C  CE2 . TRP A 146 ? 1.5543 1.0795 1.4213 0.3356  0.4717  -0.2306 146 TRP A CE2 
1148 C  CE3 . TRP A 146 ? 1.5169 0.9973 1.3049 0.3627  0.4683  -0.1631 146 TRP A CE3 
1149 C  CZ2 . TRP A 146 ? 1.5115 1.0508 1.4057 0.3387  0.4499  -0.2244 146 TRP A CZ2 
1150 C  CZ3 . TRP A 146 ? 1.5266 1.0154 1.3392 0.3645  0.4459  -0.1576 146 TRP A CZ3 
1151 C  CH2 . TRP A 146 ? 1.5306 1.0496 1.3956 0.3543  0.4367  -0.1882 146 TRP A CH2 
1152 N  N   . PRO A 147 ? 1.7406 1.1679 1.3451 0.3743  0.5408  -0.2588 147 PRO A N   
1153 C  CA  . PRO A 147 ? 1.8487 1.2425 1.4076 0.3800  0.5761  -0.2520 147 PRO A CA  
1154 C  C   . PRO A 147 ? 1.9016 1.2771 1.4994 0.3667  0.6199  -0.2410 147 PRO A C   
1155 O  O   . PRO A 147 ? 1.7932 1.1422 1.3608 0.3759  0.6539  -0.2231 147 PRO A O   
1156 C  CB  . PRO A 147 ? 1.8885 1.2849 1.4065 0.3798  0.5610  -0.3046 147 PRO A CB  
1157 C  CG  . PRO A 147 ? 1.8144 1.2496 1.3851 0.3629  0.5314  -0.3431 147 PRO A CG  
1158 C  CD  . PRO A 147 ? 1.7595 1.2163 1.3657 0.3693  0.5090  -0.3121 147 PRO A CD  
1159 N  N   . GLU A 148 ? 1.8647 1.2528 1.5257 0.3481  0.6212  -0.2500 148 GLU A N   
1160 C  CA  . GLU A 148 ? 1.8970 1.2739 1.5961 0.3330  0.6509  -0.2361 148 GLU A CA  
1161 C  C   . GLU A 148 ? 1.8713 1.2529 1.5960 0.3378  0.6637  -0.1807 148 GLU A C   
1162 O  O   . GLU A 148 ? 1.9468 1.3316 1.7101 0.3238  0.6750  -0.1627 148 GLU A O   
1163 C  CB  . GLU A 148 ? 1.8806 1.2735 1.6340 0.3064  0.6400  -0.2638 148 GLU A CB  
1164 C  CG  . GLU A 148 ? 1.9350 1.3313 1.6749 0.2960  0.6282  -0.3236 148 GLU A CG  
1165 C  CD  . GLU A 148 ? 1.9607 1.3931 1.7098 0.3014  0.5910  -0.3440 148 GLU A CD  
1166 O  OE1 . GLU A 148 ? 1.9632 1.4079 1.7034 0.3193  0.5715  -0.3102 148 GLU A OE1 
1167 O  OE2 . GLU A 148 ? 1.9955 1.4526 1.7647 0.2843  0.5738  -0.3904 148 GLU A OE2 
1168 N  N   . THR A 149 ? 1.8523 1.2327 1.5531 0.3574  0.6627  -0.1538 149 THR A N   
1169 C  CA  . THR A 149 ? 1.7535 1.1415 1.4810 0.3595  0.6763  -0.1048 149 THR A CA  
1170 C  C   . THR A 149 ? 1.6961 1.0802 1.4184 0.3612  0.7053  -0.0799 149 THR A C   
1171 O  O   . THR A 149 ? 1.7486 1.1176 1.4202 0.3752  0.7196  -0.0794 149 THR A O   
1172 C  CB  . THR A 149 ? 1.7736 1.1688 1.4753 0.3665  0.6526  -0.0786 149 THR A CB  
1173 O  OG1 . THR A 149 ? 1.7506 1.1570 1.4559 0.3633  0.6120  -0.1008 149 THR A OG1 
1174 C  CG2 . THR A 149 ? 1.5743 0.9812 1.3105 0.3613  0.6633  -0.0322 149 THR A CG2 
1175 N  N   . THR A 150 ? 1.6837 1.0811 1.4549 0.3492  0.7134  -0.0591 150 THR A N   
1176 C  CA  . THR A 150 ? 1.7345 1.1321 1.5069 0.3545  0.7390  -0.0339 150 THR A CA  
1177 C  C   . THR A 150 ? 1.7113 1.1303 1.5004 0.3636  0.7546  0.0116  150 THR A C   
1178 O  O   . THR A 150 ? 1.7174 1.1400 1.4935 0.3745  0.7774  0.0319  150 THR A O   
1179 C  CB  . THR A 150 ? 1.7566 1.1530 1.5652 0.3413  0.7408  -0.0362 150 THR A CB  
1180 O  OG1 . THR A 150 ? 1.7923 1.2096 1.6495 0.3328  0.7316  -0.0156 150 THR A OG1 
1181 C  CG2 . THR A 150 ? 1.7716 1.1479 1.5692 0.3272  0.7291  -0.0815 150 THR A CG2 
1182 N  N   . TRP A 151 ? 1.6965 1.1313 1.5157 0.3586  0.7440  0.0268  151 TRP A N   
1183 C  CA  . TRP A 151 ? 1.6642 1.1244 1.5084 0.3622  0.7603  0.0684  151 TRP A CA  
1184 C  C   . TRP A 151 ? 1.6565 1.1226 1.5131 0.3524  0.7378  0.0765  151 TRP A C   
1185 O  O   . TRP A 151 ? 1.6835 1.1411 1.5486 0.3438  0.7110  0.0533  151 TRP A O   
1186 C  CB  . TRP A 151 ? 1.6154 1.1007 1.5096 0.3576  0.7670  0.0890  151 TRP A CB  
1187 C  CG  . TRP A 151 ? 1.5711 1.0942 1.4973 0.3603  0.7836  0.1294  151 TRP A CG  
1188 C  CD1 . TRP A 151 ? 1.5451 1.0931 1.5112 0.3513  0.7784  0.1482  151 TRP A CD1 
1189 C  CD2 . TRP A 151 ? 1.5695 1.1149 1.4938 0.3705  0.8082  0.1543  151 TRP A CD2 
1190 N  NE1 . TRP A 151 ? 1.5189 1.1078 1.5103 0.3520  0.7978  0.1830  151 TRP A NE1 
1191 C  CE2 . TRP A 151 ? 1.5333 1.1232 1.5016 0.3641  0.8155  0.1875  151 TRP A CE2 
1192 C  CE3 . TRP A 151 ? 1.6644 1.1985 1.5549 0.3835  0.8248  0.1507  151 TRP A CE3 
1193 C  CZ2 . TRP A 151 ? 1.5510 1.1801 1.5354 0.3683  0.8367  0.2164  151 TRP A CZ2 
1194 C  CZ3 . TRP A 151 ? 1.6535 1.2213 1.5565 0.3913  0.8472  0.1800  151 TRP A CZ3 
1195 C  CH2 . TRP A 151 ? 1.5924 1.2101 1.5445 0.3831  0.8522  0.2121  151 TRP A CH2 
1196 N  N   . GLY A 152 ? 1.6340 1.1177 1.4923 0.3467  0.7400  0.1108  152 GLY A N   
1197 C  CA  . GLY A 152 ? 1.5723 1.0602 1.4424 0.3290  0.7109  0.1246  152 GLY A CA  
1198 C  C   . GLY A 152 ? 1.5959 1.1147 1.4939 0.3174  0.7245  0.1649  152 GLY A C   
1199 O  O   . GLY A 152 ? 1.6410 1.1782 1.5384 0.3250  0.7556  0.1832  152 GLY A O   
1200 N  N   . MSE A 153 ? 1.5623 1.0887 1.4861 0.2980  0.7017  0.1769  153 MSE A N   
1201 C  CA  . MSE A 153 ? 1.5990 1.1578 1.5538 0.2803  0.7104  0.2120  153 MSE A CA  
1202 C  C   . MSE A 153 ? 1.5232 1.0722 1.4870 0.2569  0.6798  0.2186  153 MSE A C   
1203 O  O   . MSE A 153 ? 1.4510 0.9852 1.4223 0.2559  0.6551  0.1986  153 MSE A O   
1204 C  CB  . MSE A 153 ? 1.6331 1.2402 1.6450 0.2851  0.7314  0.2238  153 MSE A CB  
1205 C  CG  . MSE A 153 ? 1.6867 1.3362 1.7472 0.2624  0.7255  0.2508  153 MSE A CG  
1206 SE SE  . MSE A 153 ? 1.7410 1.4424 1.8709 0.2716  0.7305  0.2559  153 MSE A SE  
1207 C  CE  . MSE A 153 ? 1.6736 1.4009 1.8384 0.2328  0.6991  0.2745  153 MSE A CE  
1208 N  N   . LEU A 154 ? 1.5523 1.1074 1.5134 0.2369  0.6842  0.2462  154 LEU A N   
1209 C  CA  . LEU A 154 ? 1.5012 1.0450 1.4702 0.2108  0.6602  0.2559  154 LEU A CA  
1210 C  C   . LEU A 154 ? 1.4490 1.0433 1.4652 0.1866  0.6757  0.2854  154 LEU A C   
1211 O  O   . LEU A 154 ? 1.5258 1.1357 1.5352 0.1810  0.7016  0.3059  154 LEU A O   
1212 C  CB  . LEU A 154 ? 1.6187 1.1044 1.5230 0.2077  0.6475  0.2574  154 LEU A CB  
1213 C  CG  . LEU A 154 ? 1.6685 1.1144 1.5563 0.1896  0.6185  0.2586  154 LEU A CG  
1214 C  CD1 . LEU A 154 ? 1.8004 1.1862 1.6139 0.1976  0.6136  0.2621  154 LEU A CD1 
1215 C  CD2 . LEU A 154 ? 1.6549 1.1241 1.5796 0.1544  0.6216  0.2827  154 LEU A CD2 
1216 N  N   . ALA A 155 ? 1.3797 1.0032 1.4437 0.1721  0.6606  0.2867  155 ALA A N   
1217 C  CA  . ALA A 155 ? 1.3944 1.0773 1.5103 0.1488  0.6708  0.3114  155 ALA A CA  
1218 C  C   . ALA A 155 ? 1.3725 1.0617 1.5166 0.1275  0.6418  0.3080  155 ALA A C   
1219 O  O   . ALA A 155 ? 1.3385 0.9937 1.4691 0.1375  0.6195  0.2863  155 ALA A O   
1220 C  CB  . ALA A 155 ? 1.3476 1.0935 1.5078 0.1701  0.6975  0.3184  155 ALA A CB  
1221 N  N   . PRO A 156 ? 1.3982 1.1311 1.5807 0.0968  0.6412  0.3272  156 PRO A N   
1222 C  CA  . PRO A 156 ? 1.4105 1.1496 1.6161 0.0751  0.6126  0.3228  156 PRO A CA  
1223 C  C   . PRO A 156 ? 1.4098 1.1889 1.6544 0.0967  0.6059  0.3140  156 PRO A C   
1224 O  O   . PRO A 156 ? 1.4057 1.2218 1.6721 0.1240  0.6265  0.3172  156 PRO A O   
1225 C  CB  . PRO A 156 ? 1.4316 1.2177 1.6712 0.0354  0.6181  0.3455  156 PRO A CB  
1226 C  CG  . PRO A 156 ? 1.4406 1.2205 1.6584 0.0321  0.6482  0.3611  156 PRO A CG  
1227 C  CD  . PRO A 156 ? 1.4091 1.1842 1.6108 0.0759  0.6666  0.3527  156 PRO A CD  
1228 N  N   . HIS A 157 ? 1.4352 1.2018 1.6838 0.0848  0.5781  0.3036  157 HIS A N   
1229 C  CA  . HIS A 157 ? 1.3929 1.1860 1.6684 0.1050  0.5707  0.2955  157 HIS A CA  
1230 C  C   . HIS A 157 ? 1.3466 1.2254 1.6797 0.1024  0.5772  0.3155  157 HIS A C   
1231 O  O   . HIS A 157 ? 1.3218 1.2333 1.6770 0.1332  0.5898  0.3178  157 HIS A O   
1232 C  CB  . HIS A 157 ? 1.4439 1.1970 1.7018 0.0937  0.5406  0.2786  157 HIS A CB  
1233 C  CG  . HIS A 157 ? 1.4987 1.2533 1.7641 0.1192  0.5365  0.2655  157 HIS A CG  
1234 N  ND1 . HIS A 157 ? 1.5087 1.3201 1.8127 0.1290  0.5385  0.2767  157 HIS A ND1 
1235 C  CD2 . HIS A 157 ? 1.5108 1.2165 1.7487 0.1373  0.5324  0.2425  157 HIS A CD2 
1236 C  CE1 . HIS A 157 ? 1.5271 1.3161 1.8212 0.1515  0.5372  0.2626  157 HIS A CE1 
1237 N  NE2 . HIS A 157 ? 1.5246 1.2517 1.7816 0.1547  0.5345  0.2410  157 HIS A NE2 
1238 N  N   . ALA A 158 ? 1.3657 1.2820 1.7235 0.0662  0.5690  0.3296  158 ALA A N   
1239 C  CA  . ALA A 158 ? 1.3399 1.3502 1.7587 0.0626  0.5717  0.3473  158 ALA A CA  
1240 C  C   . ALA A 158 ? 1.3012 1.3628 1.7471 0.0877  0.6063  0.3627  158 ALA A C   
1241 O  O   . ALA A 158 ? 1.3058 1.4423 1.7995 0.1063  0.6123  0.3745  158 ALA A O   
1242 C  CB  . ALA A 158 ? 1.3924 1.4332 1.8327 0.0123  0.5568  0.3560  158 ALA A CB  
1243 N  N   . TYR A 159 ? 1.2845 1.3067 1.6976 0.0916  0.6292  0.3630  159 TYR A N   
1244 C  CA  . TYR A 159 ? 1.3148 1.3840 1.7498 0.1131  0.6647  0.3776  159 TYR A CA  
1245 C  C   . TYR A 159 ? 1.3523 1.4135 1.7812 0.1632  0.6795  0.3697  159 TYR A C   
1246 O  O   . TYR A 159 ? 1.4309 1.5574 1.9014 0.1880  0.6963  0.3824  159 TYR A O   
1247 C  CB  . TYR A 159 ? 1.3621 1.3883 1.7565 0.1001  0.6853  0.3811  159 TYR A CB  
1248 C  CG  . TYR A 159 ? 1.3504 1.4175 1.7589 0.1238  0.7250  0.3944  159 TYR A CG  
1249 C  CD1 . TYR A 159 ? 1.3032 1.4629 1.7718 0.1124  0.7431  0.4160  159 TYR A CD1 
1250 C  CD2 . TYR A 159 ? 1.3750 1.3913 1.7375 0.1576  0.7446  0.3837  159 TYR A CD2 
1251 C  CE1 . TYR A 159 ? 1.2891 1.4877 1.7708 0.1368  0.7820  0.4279  159 TYR A CE1 
1252 C  CE2 . TYR A 159 ? 1.3885 1.4373 1.7584 0.1806  0.7822  0.3944  159 TYR A CE2 
1253 C  CZ  . TYR A 159 ? 1.3414 1.4803 1.7704 0.1715  0.8020  0.4171  159 TYR A CZ  
1254 O  OH  . TYR A 159 ? 1.3834 1.5557 1.8196 0.1970  0.8421  0.4275  159 TYR A OH  
1255 N  N   . PHE A 160 ? 1.3699 1.3516 1.7472 0.1788  0.6745  0.3483  160 PHE A N   
1256 C  CA  . PHE A 160 ? 1.3727 1.3364 1.7389 0.2211  0.6907  0.3378  160 PHE A CA  
1257 C  C   . PHE A 160 ? 1.4043 1.4014 1.8028 0.2380  0.6796  0.3406  160 PHE A C   
1258 O  O   . PHE A 160 ? 1.3997 1.4313 1.8197 0.2712  0.7001  0.3496  160 PHE A O   
1259 C  CB  . PHE A 160 ? 1.3203 1.1976 1.6288 0.2272  0.6843  0.3112  160 PHE A CB  
1260 C  CG  . PHE A 160 ? 1.4014 1.2510 1.6924 0.2644  0.7041  0.2967  160 PHE A CG  
1261 C  CD1 . PHE A 160 ? 1.4893 1.3097 1.7468 0.2797  0.7277  0.2885  160 PHE A CD1 
1262 C  CD2 . PHE A 160 ? 1.4897 1.3350 1.7912 0.2823  0.6995  0.2899  160 PHE A CD2 
1263 C  CE1 . PHE A 160 ? 1.5738 1.3628 1.8116 0.3099  0.7464  0.2722  160 PHE A CE1 
1264 C  CE2 . PHE A 160 ? 1.5666 1.3772 1.8477 0.3127  0.7206  0.2757  160 PHE A CE2 
1265 C  CZ  . PHE A 160 ? 1.5741 1.3566 1.8244 0.3252  0.7438  0.2657  160 PHE A CZ  
1266 N  N   . VAL A 161 ? 1.3990 1.3824 1.7962 0.2181  0.6480  0.3333  161 VAL A N   
1267 C  CA  . VAL A 161 ? 1.3958 1.3974 1.8102 0.2355  0.6360  0.3341  161 VAL A CA  
1268 C  C   . VAL A 161 ? 1.3954 1.4909 1.8659 0.2458  0.6403  0.3587  161 VAL A C   
1269 O  O   . VAL A 161 ? 1.4804 1.5945 1.9622 0.2812  0.6477  0.3648  161 VAL A O   
1270 C  CB  . VAL A 161 ? 1.4082 1.3759 1.8057 0.2086  0.6015  0.3209  161 VAL A CB  
1271 C  CG1 . VAL A 161 ? 1.4304 1.4436 1.8555 0.2137  0.5831  0.3301  161 VAL A CG1 
1272 C  CG2 . VAL A 161 ? 1.4472 1.3309 1.7963 0.2180  0.6011  0.2948  161 VAL A CG2 
1273 N  N   . HIS A 162 ? 1.2829 1.4389 1.7887 0.2169  0.6373  0.3733  162 HIS A N   
1274 C  CA  . HIS A 162 ? 1.2254 1.4841 1.7929 0.2196  0.6336  0.3941  162 HIS A CA  
1275 C  C   . HIS A 162 ? 1.2807 1.6091 1.8882 0.2257  0.6641  0.4124  162 HIS A C   
1276 O  O   . HIS A 162 ? 1.3402 1.7516 1.9967 0.2513  0.6715  0.4287  162 HIS A O   
1277 C  CB  . HIS A 162 ? 1.2239 1.5140 1.8117 0.1731  0.5983  0.3944  162 HIS A CB  
1278 C  CG  . HIS A 162 ? 1.2773 1.5211 1.8359 0.1716  0.5678  0.3800  162 HIS A CG  
1279 N  ND1 . HIS A 162 ? 1.2954 1.4839 1.8222 0.1334  0.5435  0.3647  162 HIS A ND1 
1280 C  CD2 . HIS A 162 ? 1.2785 1.5207 1.8317 0.2049  0.5599  0.3794  162 HIS A CD2 
1281 C  CE1 . HIS A 162 ? 1.2865 1.4452 1.7919 0.1427  0.5223  0.3542  162 HIS A CE1 
1282 N  NE2 . HIS A 162 ? 1.2730 1.4624 1.7927 0.1849  0.5319  0.3633  162 HIS A NE2 
1283 N  N   . GLN A 163 ? 1.2583 1.5571 1.8452 0.2051  0.6824  0.4108  163 GLN A N   
1284 C  CA  . GLN A 163 ? 1.2372 1.6023 1.8605 0.2034  0.7129  0.4284  163 GLN A CA  
1285 C  C   . GLN A 163 ? 1.2518 1.5665 1.8348 0.2322  0.7499  0.4244  163 GLN A C   
1286 O  O   . GLN A 163 ? 1.2185 1.5595 1.8101 0.2225  0.7768  0.4352  163 GLN A O   
1287 C  CB  . GLN A 163 ? 1.2779 1.6635 1.9152 0.1458  0.7049  0.4341  163 GLN A CB  
1288 C  CG  . GLN A 163 ? 1.3376 1.7735 2.0132 0.1108  0.6682  0.4353  163 GLN A CG  
1289 C  CD  . GLN A 163 ? 1.3848 1.7753 2.0355 0.0525  0.6516  0.4290  163 GLN A CD  
1290 O  OE1 . GLN A 163 ? 1.3920 1.6991 1.9870 0.0433  0.6625  0.4224  163 GLN A OE1 
1291 N  NE2 . GLN A 163 ? 1.4132 1.8564 2.1017 0.0138  0.6247  0.4306  163 GLN A NE2 
1292 N  N   . ARG A 164 ? 1.2919 1.5341 1.8293 0.2654  0.7528  0.4083  164 ARG A N   
1293 C  CA  . ARG A 164 ? 1.3956 1.5894 1.8921 0.2929  0.7862  0.4011  164 ARG A CA  
1294 C  C   . ARG A 164 ? 1.3935 1.6513 1.9217 0.3239  0.8098  0.4151  164 ARG A C   
1295 O  O   . ARG A 164 ? 1.4058 1.7280 1.9792 0.3445  0.8037  0.4266  164 ARG A O   
1296 C  CB  . ARG A 164 ? 1.5053 1.6150 1.9524 0.3191  0.7818  0.3782  164 ARG A CB  
1297 C  CG  . ARG A 164 ? 1.5850 1.6299 1.9767 0.3378  0.8021  0.3621  164 ARG A CG  
1298 C  CD  . ARG A 164 ? 1.6161 1.5794 1.9616 0.3525  0.7920  0.3358  164 ARG A CD  
1299 N  NE  . ARG A 164 ? 1.6570 1.6313 2.0266 0.3598  0.7770  0.3376  164 ARG A NE  
1300 C  CZ  . ARG A 164 ? 1.6881 1.6057 2.0273 0.3763  0.7690  0.3202  164 ARG A CZ  
1301 N  NH1 . ARG A 164 ? 1.7322 1.5826 2.0201 0.3836  0.7731  0.2984  164 ARG A NH1 
1302 N  NH2 . ARG A 164 ? 1.6217 1.5503 1.9802 0.3829  0.7573  0.3248  164 ARG A NH2 
1303 N  N   . THR A 165 ? 1.4172 1.6520 1.9135 0.3265  0.8284  0.4114  165 THR A N   
1304 C  CA  . THR A 165 ? 1.5179 1.8079 2.0369 0.3501  0.8444  0.4213  165 THR A CA  
1305 C  C   . THR A 165 ? 1.5482 1.8214 2.0571 0.3965  0.8414  0.4155  165 THR A C   
1306 O  O   . THR A 165 ? 1.5528 1.8987 2.1086 0.4177  0.8408  0.4300  165 THR A O   
1307 C  CB  . THR A 165 ? 1.5786 1.8315 2.0530 0.3465  0.8663  0.4158  165 THR A CB  
1308 O  OG1 . THR A 165 ? 1.6030 1.8266 2.0566 0.3063  0.8664  0.4161  165 THR A OG1 
1309 C  CG2 . THR A 165 ? 1.5546 1.8900 2.0701 0.3521  0.8853  0.4317  165 THR A CG2 
1310 N  N   . PHE A 166 ? 1.5780 1.7551 2.0245 0.4112  0.8392  0.3945  166 PHE A N   
1311 C  CA  . PHE A 166 ? 1.6141 1.7555 2.0383 0.4490  0.8377  0.3880  166 PHE A CA  
1312 C  C   . PHE A 166 ? 1.5620 1.6490 1.9668 0.4464  0.8184  0.3757  166 PHE A C   
1313 O  O   . PHE A 166 ? 1.5697 1.5806 1.9277 0.4317  0.8143  0.3541  166 PHE A O   
1314 C  CB  . PHE A 166 ? 1.7564 1.8303 2.1217 0.4658  0.8545  0.3724  166 PHE A CB  
1315 C  CG  . PHE A 166 ? 1.9270 2.0424 2.3009 0.4663  0.8765  0.3814  166 PHE A CG  
1316 C  CD1 . PHE A 166 ? 1.9712 2.1884 2.4091 0.4649  0.8827  0.4040  166 PHE A CD1 
1317 C  CD2 . PHE A 166 ? 2.0305 2.0854 2.3482 0.4667  0.8913  0.3661  166 PHE A CD2 
1318 C  CE1 . PHE A 166 ? 2.0637 2.3181 2.5086 0.4632  0.9050  0.4111  166 PHE A CE1 
1319 C  CE2 . PHE A 166 ? 2.0787 2.1675 2.3996 0.4676  0.9132  0.3743  166 PHE A CE2 
1320 C  CZ  . PHE A 166 ? 2.1080 2.2955 2.4925 0.4654  0.9210  0.3969  166 PHE A CZ  
1321 N  N   . PRO A 167 ? 1.5078 1.6296 1.9439 0.4615  0.8066  0.3873  167 PRO A N   
1322 C  CA  . PRO A 167 ? 1.4643 1.5388 1.8841 0.4546  0.7895  0.3765  167 PRO A CA  
1323 C  C   . PRO A 167 ? 1.5190 1.4936 1.8747 0.4676  0.7903  0.3549  167 PRO A C   
1324 O  O   . PRO A 167 ? 1.5493 1.4738 1.8838 0.4548  0.7782  0.3402  167 PRO A O   
1325 C  CB  . PRO A 167 ? 1.4018 1.5501 1.8724 0.4722  0.7793  0.3984  167 PRO A CB  
1326 C  CG  . PRO A 167 ? 1.4157 1.6153 1.9055 0.5036  0.7919  0.4141  167 PRO A CG  
1327 C  CD  . PRO A 167 ? 1.4743 1.6823 1.9608 0.4881  0.8084  0.4106  167 PRO A CD  
1328 N  N   . ASP A 168 ? 1.5656 1.5111 1.8909 0.4897  0.8052  0.3519  168 ASP A N   
1329 C  CA  . ASP A 168 ? 1.7339 1.5889 2.0010 0.4974  0.8080  0.3325  168 ASP A CA  
1330 C  C   . ASP A 168 ? 1.7525 1.5409 1.9751 0.4723  0.8080  0.3039  168 ASP A C   
1331 O  O   . ASP A 168 ? 1.8290 1.5462 2.0073 0.4699  0.8082  0.2840  168 ASP A O   
1332 C  CB  . ASP A 168 ? 1.9220 1.7704 2.1725 0.5312  0.8260  0.3411  168 ASP A CB  
1333 C  CG  . ASP A 168 ? 2.0639 1.9624 2.3332 0.5384  0.8414  0.3502  168 ASP A CG  
1334 O  OD1 . ASP A 168 ? 2.1274 1.9871 2.3603 0.5525  0.8585  0.3424  168 ASP A OD1 
1335 O  OD2 . ASP A 168 ? 2.0765 2.0532 2.3964 0.5282  0.8380  0.3648  168 ASP A OD2 
1336 N  N   . ARG A 169 ? 1.6789 1.4902 1.9115 0.4531  0.8085  0.3016  169 ARG A N   
1337 C  CA  . ARG A 169 ? 1.6890 1.4431 1.8777 0.4345  0.8087  0.2756  169 ARG A CA  
1338 C  C   . ARG A 169 ? 1.6691 1.4497 1.8755 0.4103  0.8027  0.2775  169 ARG A C   
1339 O  O   . ARG A 169 ? 1.6446 1.4880 1.8981 0.4043  0.8006  0.2989  169 ARG A O   
1340 C  CB  . ARG A 169 ? 1.7372 1.4700 1.8924 0.4485  0.8278  0.2697  169 ARG A CB  
1341 C  CG  . ARG A 169 ? 1.7485 1.5457 1.9355 0.4686  0.8441  0.2953  169 ARG A CG  
1342 C  CD  . ARG A 169 ? 1.8445 1.6102 1.9990 0.4944  0.8620  0.2913  169 ARG A CD  
1343 N  NE  . ARG A 169 ? 1.9550 1.6467 2.0509 0.4849  0.8657  0.2624  169 ARG A NE  
1344 C  CZ  . ARG A 169 ? 2.0418 1.6802 2.0977 0.4987  0.8769  0.2493  169 ARG A CZ  
1345 N  NH1 . ARG A 169 ? 2.0361 1.6807 2.0999 0.5253  0.8869  0.2644  169 ARG A NH1 
1346 N  NH2 . ARG A 169 ? 2.0818 1.6614 2.0886 0.4864  0.8787  0.2209  169 ARG A NH2 
1347 N  N   . ARG A 170 ? 1.6610 1.3938 1.8276 0.3959  0.8010  0.2549  170 ARG A N   
1348 C  CA  . ARG A 170 ? 1.6008 1.3382 1.7699 0.3740  0.7955  0.2530  170 ARG A CA  
1349 C  C   . ARG A 170 ? 1.6008 1.3865 1.7865 0.3682  0.8112  0.2755  170 ARG A C   
1350 O  O   . ARG A 170 ? 1.6570 1.4940 1.8728 0.3793  0.8224  0.2962  170 ARG A O   
1351 C  CB  . ARG A 170 ? 1.6242 1.2977 1.7416 0.3660  0.7892  0.2214  170 ARG A CB  
1352 C  CG  . ARG A 170 ? 1.6554 1.2864 1.7608 0.3615  0.7718  0.1972  170 ARG A CG  
1353 C  CD  . ARG A 170 ? 1.6880 1.2667 1.7454 0.3554  0.7666  0.1634  170 ARG A CD  
1354 N  NE  . ARG A 170 ? 1.7023 1.2482 1.7534 0.3460  0.7518  0.1403  170 ARG A NE  
1355 C  CZ  . ARG A 170 ? 1.7108 1.2179 1.7284 0.3388  0.7469  0.1086  170 ARG A CZ  
1356 N  NH1 . ARG A 170 ? 1.7722 1.2655 1.7554 0.3430  0.7540  0.0951  170 ARG A NH1 
1357 N  NH2 . ARG A 170 ? 1.6537 1.1377 1.6717 0.3267  0.7364  0.0898  170 ARG A NH2 
1358 N  N   . SER A 171 ? 1.5992 1.3688 1.7640 0.3505  0.8131  0.2721  171 SER A N   
1359 C  CA  . SER A 171 ? 1.6470 1.4546 1.8209 0.3371  0.8290  0.2953  171 SER A CA  
1360 C  C   . SER A 171 ? 1.6516 1.4082 1.7687 0.3269  0.8318  0.2838  171 SER A C   
1361 O  O   . SER A 171 ? 1.6250 1.3281 1.7069 0.3264  0.8111  0.2574  171 SER A O   
1362 C  CB  . SER A 171 ? 1.5845 1.4502 1.8139 0.3131  0.8207  0.3193  171 SER A CB  
1363 O  OG  . SER A 171 ? 1.5492 1.4292 1.7730 0.2859  0.8233  0.3357  171 SER A OG  
1364 N  N   . ILE A 172 ? 1.6490 1.4219 1.7548 0.3158  0.8477  0.3028  172 ILE A N   
1365 C  CA  . ILE A 172 ? 1.6326 1.3530 1.6754 0.3046  0.8396  0.2954  172 ILE A CA  
1366 C  C   . ILE A 172 ? 1.6441 1.3558 1.6880 0.2698  0.8104  0.3057  172 ILE A C   
1367 O  O   . ILE A 172 ? 1.7024 1.3588 1.6924 0.2639  0.7920  0.2943  172 ILE A O   
1368 C  CB  . ILE A 172 ? 1.6370 1.3639 1.6499 0.3140  0.8770  0.3093  172 ILE A CB  
1369 C  CG1 . ILE A 172 ? 1.6577 1.3164 1.5883 0.3185  0.8704  0.2921  172 ILE A CG1 
1370 C  CG2 . ILE A 172 ? 1.6362 1.4144 1.6838 0.2874  0.8902  0.3430  172 ILE A CG2 
1371 C  CD1 . ILE A 172 ? 1.6251 1.2408 1.5229 0.3423  0.8610  0.2560  172 ILE A CD1 
1372 N  N   . GLY A 173 ? 1.5918 1.3553 1.6933 0.2479  0.8050  0.3259  173 GLY A N   
1373 C  CA  . GLY A 173 ? 1.5221 1.2717 1.6238 0.2131  0.7775  0.3332  173 GLY A CA  
1374 C  C   . GLY A 173 ? 1.5591 1.2803 1.6164 0.1934  0.7880  0.3489  173 GLY A C   
1375 O  O   . GLY A 173 ? 1.6109 1.3500 1.6582 0.1985  0.8218  0.3636  173 GLY A O   
1376 N  N   . TRP A 174 ? 1.5951 1.2669 1.6214 0.1717  0.7602  0.3462  174 TRP A N   
1377 C  CA  . TRP A 174 ? 1.6419 1.2688 1.6129 0.1545  0.7681  0.3610  174 TRP A CA  
1378 C  C   . TRP A 174 ? 1.6620 1.2362 1.5595 0.1847  0.7762  0.3485  174 TRP A C   
1379 O  O   . TRP A 174 ? 1.6719 1.2399 1.5351 0.1867  0.8058  0.3637  174 TRP A O   
1380 C  CB  . TRP A 174 ? 1.6165 1.1963 1.5690 0.1278  0.7358  0.3604  174 TRP A CB  
1381 C  CG  . TRP A 174 ? 1.6976 1.2225 1.5904 0.1080  0.7444  0.3786  174 TRP A CG  
1382 C  CD1 . TRP A 174 ? 1.7214 1.2532 1.5950 0.0989  0.7807  0.4017  174 TRP A CD1 
1383 C  CD2 . TRP A 174 ? 1.7918 1.2406 1.6312 0.0969  0.7185  0.3762  174 TRP A CD2 
1384 N  NE1 . TRP A 174 ? 1.8037 1.2640 1.6120 0.0809  0.7794  0.4149  174 TRP A NE1 
1385 C  CE2 . TRP A 174 ? 1.8690 1.2758 1.6544 0.0810  0.7408  0.3997  174 TRP A CE2 
1386 C  CE3 . TRP A 174 ? 1.7486 1.1587 1.5785 0.1005  0.6805  0.3568  174 TRP A CE3 
1387 C  CZ2 . TRP A 174 ? 1.9736 1.2955 1.6924 0.0704  0.7255  0.4053  174 TRP A CZ2 
1388 C  CZ3 . TRP A 174 ? 1.7691 1.1006 1.5372 0.0916  0.6649  0.3611  174 TRP A CZ3 
1389 C  CH2 . TRP A 174 ? 1.9071 1.1925 1.6186 0.0775  0.6869  0.3856  174 TRP A CH2 
1390 N  N   . ILE A 175 ? 1.6588 1.1968 1.5306 0.2074  0.7502  0.3197  175 ILE A N   
1391 C  CA  . ILE A 175 ? 1.6952 1.1899 1.5006 0.2366  0.7521  0.3020  175 ILE A CA  
1392 C  C   . ILE A 175 ? 1.6791 1.1889 1.5073 0.2611  0.7455  0.2718  175 ILE A C   
1393 O  O   . ILE A 175 ? 1.6725 1.1810 1.5274 0.2588  0.7181  0.2546  175 ILE A O   
1394 C  CB  . ILE A 175 ? 1.7444 1.1704 1.4831 0.2383  0.7224  0.2941  175 ILE A CB  
1395 C  CG1 . ILE A 175 ? 1.8197 1.2203 1.5389 0.2086  0.7264  0.3243  175 ILE A CG1 
1396 C  CG2 . ILE A 175 ? 1.7941 1.1830 1.4596 0.2674  0.7271  0.2806  175 ILE A CG2 
1397 C  CD1 . ILE A 175 ? 1.8415 1.2319 1.5890 0.1851  0.6973  0.3242  175 ILE A CD1 
1398 N  N   . GLY A 176 ? 1.6724 1.1919 1.4868 0.2836  0.7725  0.2649  176 GLY A N   
1399 C  CA  . GLY A 176 ? 1.6409 1.1629 1.4665 0.3055  0.7704  0.2347  176 GLY A CA  
1400 C  C   . GLY A 176 ? 1.7245 1.2147 1.4864 0.3296  0.7829  0.2159  176 GLY A C   
1401 O  O   . GLY A 176 ? 1.7769 1.2532 1.4920 0.3328  0.8015  0.2310  176 GLY A O   
1402 N  N   . PHE A 177 ? 1.7209 1.1978 1.4786 0.3448  0.7729  0.1813  177 PHE A N   
1403 C  CA  . PHE A 177 ? 1.8843 1.3313 1.5828 0.3660  0.7809  0.1558  177 PHE A CA  
1404 C  C   . PHE A 177 ? 1.9515 1.4116 1.6737 0.3807  0.8096  0.1421  177 PHE A C   
1405 O  O   . PHE A 177 ? 1.9483 1.4175 1.7149 0.3783  0.8024  0.1280  177 PHE A O   
1406 C  CB  . PHE A 177 ? 1.8878 1.3036 1.5533 0.3692  0.7417  0.1215  177 PHE A CB  
1407 C  CG  . PHE A 177 ? 1.8797 1.2776 1.5120 0.3860  0.7455  0.0832  177 PHE A CG  
1408 C  CD1 . PHE A 177 ? 1.8305 1.2307 1.4947 0.3837  0.7337  0.0504  177 PHE A CD1 
1409 C  CD2 . PHE A 177 ? 1.9509 1.3275 1.5174 0.4019  0.7625  0.0792  177 PHE A CD2 
1410 C  CE1 . PHE A 177 ? 1.8917 1.2733 1.5253 0.3940  0.7382  0.0128  177 PHE A CE1 
1411 C  CE2 . PHE A 177 ? 2.0108 1.3690 1.5438 0.4147  0.7652  0.0412  177 PHE A CE2 
1412 C  CZ  . PHE A 177 ? 1.9875 1.3484 1.5556 0.4093  0.7528  0.0071  177 PHE A CZ  
1413 N  N   . CYS A 178 ? 1.9938 1.4498 1.6818 0.3971  0.8444  0.1470  178 CYS A N   
1414 C  CA  . CYS A 178 ? 2.0827 1.5413 1.7801 0.4078  0.8581  0.1338  178 CYS A CA  
1415 C  C   . CYS A 178 ? 2.1929 1.6089 1.8220 0.4191  0.8524  0.0977  178 CYS A C   
1416 O  O   . CYS A 178 ? 2.2330 1.6265 1.7976 0.4291  0.8609  0.0980  178 CYS A O   
1417 C  CB  . CYS A 178 ? 2.1895 1.6809 1.9052 0.4119  0.8857  0.1655  178 CYS A CB  
1418 S  SG  . CYS A 178 ? 2.1764 1.7305 1.9752 0.3965  0.8911  0.2066  178 CYS A SG  
1419 N  N   . PRO A 179 ? 2.4241 1.4018 1.7647 0.5221  0.5406  -0.0159 179 PRO A N   
1420 C  CA  . PRO A 179 ? 2.5030 1.4712 1.8029 0.5214  0.5191  -0.0574 179 PRO A CA  
1421 C  C   . PRO A 179 ? 2.5505 1.5443 1.8390 0.5534  0.5416  -0.0862 179 PRO A C   
1422 O  O   . PRO A 179 ? 2.6002 1.5907 1.8930 0.5577  0.5207  -0.1257 179 PRO A O   
1423 C  CB  . PRO A 179 ? 2.4815 1.4301 1.8290 0.5020  0.4809  -0.0745 179 PRO A CB  
1424 C  CG  . PRO A 179 ? 2.4576 1.4111 1.8705 0.5099  0.4891  -0.0504 179 PRO A CG  
1425 C  CD  . PRO A 179 ? 2.4119 1.3847 1.8245 0.5152  0.5186  -0.0096 179 PRO A CD  
1426 N  N   . HIS A 180 ? 2.5294 1.5537 1.8071 0.5748  0.5853  -0.0698 180 HIS A N   
1427 C  CA  . HIS A 180 ? 2.5341 1.5918 1.8016 0.6040  0.6082  -0.0964 180 HIS A CA  
1428 C  C   . HIS A 180 ? 2.5194 1.6030 1.7306 0.6106  0.6526  -0.0754 180 HIS A C   
1429 O  O   . HIS A 180 ? 2.5254 1.5994 1.7186 0.5933  0.6687  -0.0380 180 HIS A O   
1430 C  CB  . HIS A 180 ? 2.5539 1.6402 1.8988 0.6289  0.6193  -0.1058 180 HIS A CB  
1431 C  CG  . HIS A 180 ? 2.4956 1.5483 1.8921 0.6204  0.5790  -0.1195 180 HIS A CG  
1432 N  ND1 . HIS A 180 ? 2.5195 1.5625 1.9312 0.6327  0.5590  -0.1621 180 HIS A ND1 
1433 C  CD2 . HIS A 180 ? 2.4264 1.4522 1.8611 0.5995  0.5567  -0.0957 180 HIS A CD2 
1434 C  CE1 . HIS A 180 ? 2.4878 1.4947 1.9414 0.6181  0.5284  -0.1625 180 HIS A CE1 
1435 N  NE2 . HIS A 180 ? 2.4370 1.4347 1.9036 0.5977  0.5257  -0.1219 180 HIS A NE2 
1436 N  N   . PRO A 181 ? 2.5594 1.6739 1.7394 0.6317  0.6734  -0.0973 181 PRO A N   
1437 C  CA  . PRO A 181 ? 2.6422 1.7879 1.7734 0.6340  0.7216  -0.0743 181 PRO A CA  
1438 C  C   . PRO A 181 ? 2.6662 1.8751 1.8656 0.6452  0.7681  -0.0590 181 PRO A C   
1439 O  O   . PRO A 181 ? 2.6709 1.9069 1.9449 0.6663  0.7631  -0.0792 181 PRO A O   
1440 C  CB  . PRO A 181 ? 2.7206 1.8767 1.7939 0.6520  0.7192  -0.1085 181 PRO A CB  
1441 C  CG  . PRO A 181 ? 2.6943 1.8522 1.8217 0.6689  0.6877  -0.1527 181 PRO A CG  
1442 C  CD  . PRO A 181 ? 2.5949 1.7112 1.7677 0.6484  0.6494  -0.1460 181 PRO A CD  
1443 N  N   . LEU A 182 ? 2.6710 1.9070 1.8460 0.6286  0.8124  -0.0237 182 LEU A N   
1444 C  CA  . LEU A 182 ? 2.6176 1.9291 1.8667 0.6295  0.8587  -0.0058 182 LEU A CA  
1445 C  C   . LEU A 182 ? 2.7119 2.0793 1.9212 0.6212  0.9099  0.0031  182 LEU A C   
1446 O  O   . LEU A 182 ? 2.7691 2.1017 1.8824 0.6058  0.9127  0.0132  182 LEU A O   
1447 C  CB  . LEU A 182 ? 2.4725 1.7828 1.7647 0.5982  0.8599  0.0362  182 LEU A CB  
1448 C  CG  . LEU A 182 ? 2.3632 1.6345 1.7144 0.5928  0.8059  0.0397  182 LEU A CG  
1449 C  CD1 . LEU A 182 ? 2.3565 1.6437 1.7785 0.6362  0.7994  0.0064  182 LEU A CD1 
1450 C  CD2 . LEU A 182 ? 2.3476 1.5291 1.6281 0.5822  0.7630  0.0347  182 LEU A CD2 
1451 N  N   . ARG A 183 ? 2.7323 2.1893 2.0191 0.6307  0.9480  -0.0009 183 ARG A N   
1452 C  CA  . ARG A 183 ? 2.6775 2.2046 1.9474 0.6140  1.0018  0.0100  183 ARG A CA  
1453 C  C   . ARG A 183 ? 2.6027 2.1550 1.8922 0.5654  1.0337  0.0588  183 ARG A C   
1454 O  O   . ARG A 183 ? 2.5047 2.0674 1.8689 0.5569  1.0247  0.0752  183 ARG A O   
1455 C  CB  . ARG A 183 ? 2.6937 2.3179 2.0448 0.6457  1.0259  -0.0242 183 ARG A CB  
1456 C  CG  . ARG A 183 ? 2.7232 2.4210 2.0474 0.6324  1.0785  -0.0251 183 ARG A CG  
1457 C  CD  . ARG A 183 ? 2.6881 2.4818 2.0899 0.6702  1.0959  -0.0685 183 ARG A CD  
1458 N  NE  . ARG A 183 ? 2.6097 2.4816 2.1361 0.6745  1.1061  -0.0666 183 ARG A NE  
1459 C  CZ  . ARG A 183 ? 2.6175 2.6007 2.2267 0.6954  1.1330  -0.0954 183 ARG A CZ  
1460 N  NH1 . ARG A 183 ? 2.6792 2.7072 2.2576 0.7116  1.1560  -0.1279 183 ARG A NH1 
1461 N  NH2 . ARG A 183 ? 2.5570 2.6111 2.2814 0.7018  1.1353  -0.0943 183 ARG A NH2 
1462 N  N   . ALA A 184 ? 2.6784 2.2398 1.9019 0.5303  1.0670  0.0820  184 ALA A N   
1463 C  CA  . ALA A 184 ? 2.5465 2.1181 1.7777 0.4735  1.0902  0.1296  184 ALA A CA  
1464 C  C   . ALA A 184 ? 2.4932 2.1847 1.8494 0.4588  1.1306  0.1324  184 ALA A C   
1465 O  O   . ALA A 184 ? 2.3079 2.0174 1.7274 0.4272  1.1303  0.1602  184 ALA A O   
1466 C  CB  . ALA A 184 ? 2.5363 2.0722 1.6580 0.4385  1.1075  0.1528  184 ALA A CB  
1467 N  N   . THR A 185 ? 2.5074 2.2882 1.9053 0.4809  1.1620  0.1010  185 THR A N   
1468 C  CA  . THR A 185 ? 2.4974 2.4068 2.0177 0.4681  1.2002  0.0968  185 THR A CA  
1469 C  C   . THR A 185 ? 2.4454 2.3955 2.0846 0.5094  1.1754  0.0761  185 THR A C   
1470 O  O   . THR A 185 ? 2.4005 2.4592 2.1535 0.5016  1.1983  0.0726  185 THR A O   
1471 C  CB  . THR A 185 ? 2.5753 2.5733 2.0986 0.4788  1.2415  0.0661  185 THR A CB  
1472 O  OG1 . THR A 185 ? 2.5570 2.6913 2.2078 0.4672  1.2762  0.0559  185 THR A OG1 
1473 C  CG2 . THR A 185 ? 2.5809 2.5622 2.0874 0.5455  1.2159  0.0179  185 THR A CG2 
1474 N  N   . ASP A 186 ? 2.4388 2.3056 2.0565 0.5524  1.1263  0.0607  186 ASP A N   
1475 C  CA  . ASP A 186 ? 2.3464 2.2303 2.0698 0.5795  1.0775  0.0476  186 ASP A CA  
1476 C  C   . ASP A 186 ? 2.2749 2.1468 2.0461 0.5326  1.0418  0.0867  186 ASP A C   
1477 O  O   . ASP A 186 ? 2.1845 2.0771 2.0447 0.5506  1.0030  0.0813  186 ASP A O   
1478 C  CB  . ASP A 186 ? 2.3469 2.1360 2.0280 0.6292  1.0307  0.0201  186 ASP A CB  
1479 C  CG  . ASP A 186 ? 2.4096 2.2371 2.1057 0.6831  1.0383  -0.0297 186 ASP A CG  
1480 O  OD1 . ASP A 186 ? 2.4186 2.3577 2.1939 0.6946  1.0682  -0.0468 186 ASP A OD1 
1481 O  OD2 . ASP A 186 ? 2.4400 2.1917 2.0746 0.7070  1.0041  -0.0543 186 ASP A OD2 
1482 N  N   . PHE A 187 ? 2.3836 2.2190 2.0933 0.4758  1.0530  0.1250  187 PHE A N   
1483 C  CA  . PHE A 187 ? 2.3962 2.2080 2.1361 0.4300  1.0172  0.1614  187 PHE A CA  
1484 C  C   . PHE A 187 ? 2.4211 2.3084 2.1965 0.3717  1.0626  0.1873  187 PHE A C   
1485 O  O   . PHE A 187 ? 2.4206 2.3583 2.1715 0.3619  1.1239  0.1819  187 PHE A O   
1486 C  CB  . PHE A 187 ? 2.4002 2.0822 2.0287 0.4156  0.9796  0.1816  187 PHE A CB  
1487 C  CG  . PHE A 187 ? 2.3766 1.9872 1.9900 0.4604  0.9277  0.1583  187 PHE A CG  
1488 C  CD1 . PHE A 187 ? 2.3197 1.8966 1.9776 0.4553  0.8723  0.1696  187 PHE A CD1 
1489 C  CD2 . PHE A 187 ? 2.4633 2.0398 2.0167 0.5055  0.9357  0.1239  187 PHE A CD2 
1490 C  CE1 . PHE A 187 ? 2.3156 1.8241 1.9578 0.4903  0.8295  0.1490  187 PHE A CE1 
1491 C  CE2 . PHE A 187 ? 2.4415 1.9502 1.9838 0.5410  0.8904  0.1004  187 PHE A CE2 
1492 C  CZ  . PHE A 187 ? 2.3701 1.8436 1.9566 0.5313  0.8389  0.1140  187 PHE A CZ  
1493 N  N   . PRO A 188 ? 2.4163 2.3149 2.2500 0.3302  1.0364  0.2141  188 PRO A N   
1494 C  CA  . PRO A 188 ? 2.4340 2.3990 2.3023 0.2681  1.0796  0.2372  188 PRO A CA  
1495 C  C   . PRO A 188 ? 2.5032 2.3964 2.2437 0.2255  1.1186  0.2659  188 PRO A C   
1496 O  O   . PRO A 188 ? 2.5523 2.3487 2.1749 0.2482  1.1104  0.2660  188 PRO A O   
1497 C  CB  . PRO A 188 ? 2.3751 2.3372 2.3119 0.2392  1.0287  0.2581  188 PRO A CB  
1498 C  CG  . PRO A 188 ? 2.3440 2.2967 2.3303 0.2965  0.9730  0.2357  188 PRO A CG  
1499 C  CD  . PRO A 188 ? 2.3644 2.2346 2.2532 0.3418  0.9694  0.2183  188 PRO A CD  
1500 N  N   . ALA A 189 ? 2.5622 2.5002 2.3242 0.1632  1.1602  0.2895  189 ALA A N   
1501 C  CA  . ALA A 189 ? 2.5945 2.4743 2.2374 0.1216  1.2053  0.3155  189 ALA A CA  
1502 C  C   . ALA A 189 ? 2.5517 2.2820 2.0710 0.1107  1.1558  0.3437  189 ALA A C   
1503 O  O   . ALA A 189 ? 2.5494 2.1985 1.9521 0.1360  1.1439  0.3387  189 ALA A O   
1504 C  CB  . ALA A 189 ? 2.5904 2.5506 2.2980 0.0500  1.2395  0.3290  189 ALA A CB  
1505 N  N   . ALA A 190 ? 2.5429 2.2404 2.0895 0.0751  1.1227  0.3698  190 ALA A N   
1506 C  CA  . ALA A 190 ? 2.5662 2.1334 2.0073 0.0590  1.0697  0.3935  190 ALA A CA  
1507 C  C   . ALA A 190 ? 2.4552 1.9598 1.8822 0.1057  1.0136  0.3856  190 ALA A C   
1508 O  O   . ALA A 190 ? 2.3165 1.7577 1.7275 0.0878  0.9652  0.4037  190 ALA A O   
1509 C  CB  . ALA A 190 ? 2.5446 2.1094 2.0192 -0.0081 1.0551  0.4206  190 ALA A CB  
1510 N  N   . THR A 191 ? 2.5217 2.0480 1.9640 0.1639  1.0044  0.3512  191 THR A N   
1511 C  CA  . THR A 191 ? 2.5868 2.0453 2.0018 0.2065  0.9430  0.3351  191 THR A CA  
1512 C  C   . THR A 191 ? 2.6441 2.0227 1.9244 0.2374  0.9516  0.3238  191 THR A C   
1513 O  O   . THR A 191 ? 2.7815 2.1955 2.0473 0.2676  0.9903  0.3006  191 THR A O   
1514 C  CB  . THR A 191 ? 2.6319 2.1585 2.1572 0.2497  0.9212  0.3032  191 THR A CB  
1515 O  OG1 . THR A 191 ? 2.7675 2.3150 2.2708 0.2958  0.9509  0.2710  191 THR A OG1 
1516 C  CG2 . THR A 191 ? 2.6009 2.2385 2.2607 0.2269  0.9344  0.3067  191 THR A CG2 
1517 N  N   . GLU A 192 ? 2.5597 1.8351 1.7422 0.2326  0.9144  0.3371  192 GLU A N   
1518 C  CA  . GLU A 192 ? 2.5832 1.7816 1.6324 0.2572  0.9147  0.3269  192 GLU A CA  
1519 C  C   . GLU A 192 ? 2.5422 1.7089 1.5744 0.3114  0.8782  0.2897  192 GLU A C   
1520 O  O   . GLU A 192 ? 2.4542 1.6010 1.5288 0.3152  0.8251  0.2838  192 GLU A O   
1521 C  CB  . GLU A 192 ? 2.5618 1.6803 1.5360 0.2244  0.8716  0.3473  192 GLU A CB  
1522 C  CG  . GLU A 192 ? 2.5762 1.6197 1.4279 0.2531  0.8510  0.3303  192 GLU A CG  
1523 C  CD  . GLU A 192 ? 2.5843 1.5563 1.3707 0.2263  0.8084  0.3464  192 GLU A CD  
1524 O  OE1 . GLU A 192 ? 2.5465 1.5333 1.3772 0.1784  0.8054  0.3719  192 GLU A OE1 
1525 O  OE2 . GLU A 192 ? 2.6370 1.5417 1.3313 0.2551  0.7767  0.3301  192 GLU A OE2 
1526 N  N   . LEU A 193 ? 2.6012 1.7661 1.5761 0.3506  0.9036  0.2616  193 LEU A N   
1527 C  CA  . LEU A 193 ? 2.6419 1.7751 1.5955 0.4001  0.8691  0.2195  193 LEU A CA  
1528 C  C   . LEU A 193 ? 2.7374 1.7834 1.5597 0.4118  0.8424  0.2131  193 LEU A C   
1529 O  O   . LEU A 193 ? 2.9175 1.9557 1.6768 0.4048  0.8574  0.2197  193 LEU A O   
1530 C  CB  . LEU A 193 ? 2.6739 1.8675 1.6617 0.4401  0.9043  0.1839  193 LEU A CB  
1531 C  CG  . LEU A 193 ? 2.5923 1.8649 1.7188 0.4539  0.9031  0.1667  193 LEU A CG  
1532 C  CD1 . LEU A 193 ? 2.5672 1.9168 1.7845 0.4135  0.9297  0.1982  193 LEU A CD1 
1533 C  CD2 . LEU A 193 ? 2.6271 1.9383 1.7562 0.5023  0.9335  0.1252  193 LEU A CD2 
1534 N  N   . VAL A 194 ? 2.6557 1.6444 1.4508 0.4276  0.7936  0.1967  194 VAL A N   
1535 C  CA  . VAL A 194 ? 2.6336 1.5565 1.3312 0.4463  0.7519  0.1767  194 VAL A CA  
1536 C  C   . VAL A 194 ? 2.6465 1.5708 1.3621 0.4881  0.7264  0.1252  194 VAL A C   
1537 O  O   . VAL A 194 ? 2.5704 1.4763 1.3205 0.4925  0.6924  0.1086  194 VAL A O   
1538 C  CB  . VAL A 194 ? 2.5190 1.3804 1.1761 0.4229  0.7063  0.1971  194 VAL A CB  
1539 C  CG1 . VAL A 194 ? 2.3333 1.2037 1.0681 0.4071  0.6842  0.2044  194 VAL A CG1 
1540 C  CG2 . VAL A 194 ? 2.5766 1.3807 1.1478 0.4514  0.6584  0.1668  194 VAL A CG2 
1541 N  N   . ASP A 195 ? 2.7998 1.7509 1.5019 0.5142  0.7398  0.0988  195 ASP A N   
1542 C  CA  . ASP A 195 ? 2.9426 1.9045 1.6736 0.5460  0.7099  0.0493  195 ASP A CA  
1543 C  C   . ASP A 195 ? 3.0085 1.9214 1.6822 0.5526  0.6504  0.0275  195 ASP A C   
1544 O  O   . ASP A 195 ? 3.0854 1.9758 1.6767 0.5613  0.6406  0.0268  195 ASP A O   
1545 C  CB  . ASP A 195 ? 3.0745 2.0821 1.8000 0.5689  0.7391  0.0289  195 ASP A CB  
1546 C  CG  . ASP A 195 ? 3.1095 2.1466 1.8996 0.5947  0.7183  -0.0186 195 ASP A CG  
1547 O  OD1 . ASP A 195 ? 3.1519 2.1707 1.9162 0.6073  0.6748  -0.0526 195 ASP A OD1 
1548 O  OD2 . ASP A 195 ? 3.1140 2.1964 1.9850 0.6014  0.7437  -0.0233 195 ASP A OD2 
1549 N  N   . ILE A 196 ? 2.9493 1.8518 1.6721 0.5475  0.6094  0.0092  196 ILE A N   
1550 C  CA  . ILE A 196 ? 2.9413 1.8236 1.6361 0.5510  0.5506  -0.0204 196 ILE A CA  
1551 C  C   . ILE A 196 ? 3.0290 1.9498 1.7611 0.5698  0.5347  -0.0687 196 ILE A C   
1552 O  O   . ILE A 196 ? 3.0233 1.9745 1.8270 0.5740  0.5534  -0.0806 196 ILE A O   
1553 C  CB  . ILE A 196 ? 2.8272 1.6904 1.5602 0.5285  0.5138  -0.0175 196 ILE A CB  
1554 C  CG1 . ILE A 196 ? 2.7820 1.6718 1.6189 0.5204  0.5159  -0.0288 196 ILE A CG1 
1555 C  CG2 . ILE A 196 ? 2.8119 1.6352 1.5027 0.5109  0.5291  0.0274  196 ILE A CG2 
1556 C  CD1 . ILE A 196 ? 2.7640 1.6771 1.6493 0.5191  0.4731  -0.0752 196 ILE A CD1 
1557 N  N   . PRO A 197 ? 3.0922 2.0145 1.7808 0.5825  0.5008  -0.0985 197 PRO A N   
1558 C  CA  . PRO A 197 ? 3.0833 2.0443 1.8068 0.5989  0.4891  -0.1474 197 PRO A CA  
1559 C  C   . PRO A 197 ? 2.9712 1.9487 1.7769 0.5819  0.4501  -0.1823 197 PRO A C   
1560 O  O   . PRO A 197 ? 2.9116 1.8833 1.7171 0.5666  0.4096  -0.1920 197 PRO A O   
1561 C  CB  . PRO A 197 ? 3.1785 2.1344 1.8200 0.6181  0.4692  -0.1628 197 PRO A CB  
1562 C  CG  . PRO A 197 ? 3.2377 2.1465 1.7959 0.6147  0.4783  -0.1159 197 PRO A CG  
1563 C  CD  . PRO A 197 ? 3.1671 2.0561 1.7664 0.5874  0.4774  -0.0880 197 PRO A CD  
1564 N  N   . GLY A 198 ? 2.9670 1.9663 1.8454 0.5838  0.4627  -0.2020 198 GLY A N   
1565 C  CA  . GLY A 198 ? 2.8936 1.9052 1.8470 0.5677  0.4298  -0.2399 198 GLY A CA  
1566 C  C   . GLY A 198 ? 2.7952 1.7951 1.8212 0.5485  0.4347  -0.2225 198 GLY A C   
1567 O  O   . GLY A 198 ? 2.7631 1.7703 1.8542 0.5457  0.4280  -0.2502 198 GLY A O   
1568 N  N   . ARG A 199 ? 2.7167 1.6946 1.7313 0.5356  0.4458  -0.1770 199 ARG A N   
1569 C  CA  . ARG A 199 ? 2.6437 1.6098 1.7248 0.5156  0.4447  -0.1588 199 ARG A CA  
1570 C  C   . ARG A 199 ? 2.6353 1.5985 1.7331 0.5250  0.4874  -0.1181 199 ARG A C   
1571 O  O   . ARG A 199 ? 2.5898 1.5452 1.7446 0.5116  0.4864  -0.0997 199 ARG A O   
1572 C  CB  . ARG A 199 ? 2.5838 1.5340 1.6589 0.4867  0.4138  -0.1459 199 ARG A CB  
1573 C  CG  . ARG A 199 ? 2.5485 1.5140 1.6314 0.4726  0.3706  -0.1890 199 ARG A CG  
1574 C  CD  . ARG A 199 ? 2.5720 1.5459 1.5813 0.4863  0.3564  -0.2006 199 ARG A CD  
1575 N  NE  . ARG A 199 ? 2.5421 1.5437 1.5724 0.4747  0.3167  -0.2470 199 ARG A NE  
1576 C  CZ  . ARG A 199 ? 2.4785 1.4871 1.5075 0.4557  0.2853  -0.2495 199 ARG A CZ  
1577 N  NH1 . ARG A 199 ? 2.4313 1.4148 1.4328 0.4468  0.2861  -0.2073 199 ARG A NH1 
1578 N  NH2 . ARG A 199 ? 2.4530 1.4973 1.5118 0.4456  0.2547  -0.2969 199 ARG A NH2 
1579 N  N   . GLY A 200 ? 2.6568 1.6312 1.7108 0.5467  0.5254  -0.1042 200 GLY A N   
1580 C  CA  . GLY A 200 ? 2.6027 1.5896 1.6845 0.5550  0.5706  -0.0704 200 GLY A CA  
1581 C  C   . GLY A 200 ? 2.5847 1.5636 1.6003 0.5526  0.6045  -0.0337 200 GLY A C   
1582 O  O   . GLY A 200 ? 2.6704 1.6390 1.6065 0.5570  0.6023  -0.0378 200 GLY A O   
1583 N  N   . THR A 201 ? 2.5084 1.4935 1.5572 0.5451  0.6366  0.0023  201 THR A N   
1584 C  CA  . THR A 201 ? 2.4945 1.4714 1.4845 0.5329  0.6714  0.0396  201 THR A CA  
1585 C  C   . THR A 201 ? 2.4697 1.4496 1.5178 0.4940  0.6472  0.0778  201 THR A C   
1586 O  O   . THR A 201 ? 2.4347 1.4210 1.5623 0.4899  0.6248  0.0753  201 THR A O   
1587 C  CB  . THR A 201 ? 2.4345 1.4692 1.4371 0.5375  0.7282  0.0566  201 THR A CB  
1588 O  OG1 . THR A 201 ? 2.2934 1.3820 1.4043 0.5170  0.7349  0.0837  201 THR A OG1 
1589 C  CG2 . THR A 201 ? 2.4455 1.5134 1.4576 0.5686  0.7365  0.0195  201 THR A CG2 
1590 N  N   . LEU A 202 ? 2.4525 1.4249 1.4567 0.4651  0.6521  0.1143  202 LEU A N   
1591 C  CA  . LEU A 202 ? 2.3784 1.3594 1.4331 0.4257  0.6328  0.1530  202 LEU A CA  
1592 C  C   . LEU A 202 ? 2.3419 1.3772 1.4324 0.4028  0.6755  0.1890  202 LEU A C   
1593 O  O   . LEU A 202 ? 2.3787 1.4121 1.4017 0.4010  0.7122  0.1988  202 LEU A O   
1594 C  CB  . LEU A 202 ? 2.4094 1.3318 1.3851 0.4089  0.5981  0.1625  202 LEU A CB  
1595 C  CG  . LEU A 202 ? 2.3664 1.2892 1.3770 0.3686  0.5757  0.2008  202 LEU A CG  
1596 C  CD1 . LEU A 202 ? 2.3792 1.2538 1.3557 0.3667  0.5234  0.1862  202 LEU A CD1 
1597 C  CD2 . LEU A 202 ? 2.4069 1.3222 1.3651 0.3433  0.6033  0.2382  202 LEU A CD2 
1598 N  N   . LEU A 203 ? 2.2465 1.3310 1.4412 0.3847  0.6714  0.2075  203 LEU A N   
1599 C  CA  . LEU A 203 ? 2.1518 1.3036 1.4023 0.3618  0.7105  0.2348  203 LEU A CA  
1600 C  C   . LEU A 203 ? 2.0415 1.1876 1.3074 0.3158  0.6918  0.2728  203 LEU A C   
1601 O  O   . LEU A 203 ? 1.9981 1.1382 1.3135 0.3070  0.6502  0.2777  203 LEU A O   
1602 C  CB  . LEU A 203 ? 2.0775 1.3009 1.4399 0.3822  0.7207  0.2213  203 LEU A CB  
1603 C  CG  . LEU A 203 ? 2.0226 1.3282 1.4797 0.3559  0.7412  0.2461  203 LEU A CG  
1604 C  CD1 . LEU A 203 ? 2.1305 1.4742 1.5568 0.3373  0.7985  0.2580  203 LEU A CD1 
1605 C  CD2 . LEU A 203 ? 1.9078 1.2748 1.4697 0.3870  0.7388  0.2273  203 LEU A CD2 
1606 N  N   . LEU A 204 ? 2.1501 1.2941 1.3693 0.2860  0.7236  0.2990  204 LEU A N   
1607 C  CA  . LEU A 204 ? 2.1992 1.3398 1.4333 0.2387  0.7143  0.3350  204 LEU A CA  
1608 C  C   . LEU A 204 ? 2.2082 1.4389 1.5338 0.2124  0.7565  0.3504  204 LEU A C   
1609 O  O   . LEU A 204 ? 2.2239 1.4949 1.5428 0.2175  0.8086  0.3450  204 LEU A O   
1610 C  CB  . LEU A 204 ? 2.2773 1.3361 1.3829 0.2219  0.7179  0.3533  204 LEU A CB  
1611 C  CG  . LEU A 204 ? 2.3288 1.3706 1.4280 0.1742  0.6893  0.3737  204 LEU A CG  
1612 C  CD1 . LEU A 204 ? 2.3786 1.4776 1.5304 0.1303  0.7309  0.3977  204 LEU A CD1 
1613 C  CD2 . LEU A 204 ? 2.2621 1.2944 1.4077 0.1625  0.6236  0.3719  204 LEU A CD2 
1614 N  N   . ASN A 205 ? 2.1134 1.3818 1.5265 0.1853  0.7338  0.3660  205 ASN A N   
1615 C  CA  . ASN A 205 ? 2.1899 1.5546 1.7051 0.1592  0.7665  0.3754  205 ASN A CA  
1616 C  C   . ASN A 205 ? 2.4087 1.7544 1.9052 0.1017  0.7734  0.4087  205 ASN A C   
1617 O  O   . ASN A 205 ? 2.3069 1.6647 1.8611 0.0779  0.7395  0.4206  205 ASN A O   
1618 C  CB  . ASN A 205 ? 2.0412 1.4711 1.6776 0.1770  0.7342  0.3632  205 ASN A CB  
1619 C  CG  . ASN A 205 ? 1.9510 1.4132 1.6206 0.2304  0.7409  0.3310  205 ASN A CG  
1620 O  OD1 . ASN A 205 ? 1.9483 1.3664 1.5434 0.2585  0.7533  0.3139  205 ASN A OD1 
1621 N  ND2 . ASN A 205 ? 1.8726 1.4092 1.6519 0.2474  0.7302  0.3208  205 ASN A ND2 
1622 N  N   . GLY A 206 ? 2.7657 2.0790 2.1781 0.0793  0.8188  0.4236  206 GLY A N   
1623 C  CA  . GLY A 206 ? 2.9054 2.1992 2.3005 0.0235  0.8141  0.4456  206 GLY A CA  
1624 C  C   . GLY A 206 ? 2.9376 2.1470 2.2691 0.0187  0.7414  0.4449  206 GLY A C   
1625 O  O   . GLY A 206 ? 3.0262 2.2264 2.3923 0.0308  0.6946  0.4411  206 GLY A O   
1626 N  N   . ARG A 207 ? 2.8553 2.0087 2.0971 0.0026  0.7311  0.4467  207 ARG A N   
1627 C  CA  . ARG A 207 ? 2.6936 1.7755 1.8730 0.0064  0.6647  0.4396  207 ARG A CA  
1628 C  C   . ARG A 207 ? 2.5481 1.6437 1.7891 -0.0279 0.6209  0.4490  207 ARG A C   
1629 O  O   . ARG A 207 ? 2.5555 1.6104 1.7661 -0.0196 0.5620  0.4382  207 ARG A O   
1630 C  CB  . ARG A 207 ? 2.7414 1.7636 1.8160 -0.0015 0.6695  0.4430  207 ARG A CB  
1631 C  CG  . ARG A 207 ? 2.7923 1.7864 1.7864 0.0403  0.6982  0.4286  207 ARG A CG  
1632 C  CD  . ARG A 207 ? 2.8230 1.7384 1.7214 0.0749  0.6495  0.4089  207 ARG A CD  
1633 N  NE  . ARG A 207 ? 2.8346 1.7316 1.6778 0.1250  0.6657  0.3873  207 ARG A NE  
1634 C  CZ  . ARG A 207 ? 2.7864 1.6222 1.5467 0.1626  0.6316  0.3645  207 ARG A CZ  
1635 N  NH1 . ARG A 207 ? 2.7409 1.5312 1.4656 0.1576  0.5808  0.3595  207 ARG A NH1 
1636 N  NH2 . ARG A 207 ? 2.7643 1.5881 1.4788 0.2070  0.6485  0.3439  207 ARG A NH2 
1637 N  N   . GLU A 208 ? 2.4328 1.5911 1.7629 -0.0653 0.6491  0.4659  208 GLU A N   
1638 C  CA  . GLU A 208 ? 2.3135 1.4848 1.7028 -0.0933 0.6054  0.4725  208 GLU A CA  
1639 C  C   . GLU A 208 ? 2.2243 1.4288 1.6856 -0.0649 0.5809  0.4640  208 GLU A C   
1640 O  O   . GLU A 208 ? 2.3556 1.5970 1.8565 -0.0377 0.6180  0.4624  208 GLU A O   
1641 C  CB  . GLU A 208 ? 2.3298 1.5519 1.7842 -0.1489 0.6432  0.4920  208 GLU A CB  
1642 C  CG  . GLU A 208 ? 2.3532 1.6633 1.8940 -0.1512 0.7106  0.4947  208 GLU A CG  
1643 C  CD  . GLU A 208 ? 2.3617 1.7385 1.9855 -0.2102 0.7448  0.5069  208 GLU A CD  
1644 O  OE1 . GLU A 208 ? 2.3863 1.8124 2.0251 -0.2316 0.8060  0.5084  208 GLU A OE1 
1645 O  OE2 . GLU A 208 ? 2.3106 1.6954 1.9873 -0.2361 0.7102  0.5120  208 GLU A OE2 
1646 N  N   . PRO A 209 ? 2.0416 1.2338 1.5195 -0.0684 0.5190  0.4589  209 PRO A N   
1647 C  CA  . PRO A 209 ? 1.8678 1.0864 1.4066 -0.0411 0.4907  0.4510  209 PRO A CA  
1648 C  C   . PRO A 209 ? 1.8447 1.1336 1.4908 -0.0490 0.5327  0.4685  209 PRO A C   
1649 O  O   . PRO A 209 ? 1.9452 1.2730 1.6433 -0.0906 0.5587  0.4837  209 PRO A O   
1650 C  CB  . PRO A 209 ? 1.7992 1.0013 1.3362 -0.0553 0.4213  0.4440  209 PRO A CB  
1651 C  CG  . PRO A 209 ? 1.8537 1.0044 1.3069 -0.0686 0.4075  0.4411  209 PRO A CG  
1652 C  CD  . PRO A 209 ? 1.9903 1.1412 1.4249 -0.0917 0.4704  0.4584  209 PRO A CD  
1653 N  N   . MSE A 210 ? 1.7964 1.1049 1.4814 -0.0081 0.5403  0.4659  210 MSE A N   
1654 C  CA  . MSE A 210 ? 1.8185 1.2352 1.6291 -0.0018 0.5488  0.4564  210 MSE A CA  
1655 C  C   . MSE A 210 ? 1.9113 1.3689 1.7988 -0.0304 0.5156  0.4638  210 MSE A C   
1656 O  O   . MSE A 210 ? 1.9392 1.3434 1.7940 -0.0357 0.4697  0.4705  210 MSE A O   
1657 C  CB  . MSE A 210 ? 1.7337 1.1684 1.5722 0.0525  0.5297  0.4359  210 MSE A CB  
1658 C  CG  . MSE A 210 ? 1.7206 1.2608 1.6837 0.0676  0.5288  0.4248  210 MSE A CG  
1659 SE SE  . MSE A 210 ? 1.7819 1.3391 1.7732 0.1381  0.5211  0.3993  210 MSE A SE  
1660 C  CE  . MSE A 210 ? 1.8528 1.3071 1.7065 0.1519  0.5441  0.3929  210 MSE A CE  
1661 N  N   . ASP A 211 ? 1.9758 1.5341 1.9676 -0.0474 0.5386  0.4589  211 ASP A N   
1662 C  CA  . ASP A 211 ? 1.9292 1.5490 2.0139 -0.0659 0.5058  0.4581  211 ASP A CA  
1663 C  C   . ASP A 211 ? 1.9157 1.6441 2.1117 -0.0306 0.5059  0.4376  211 ASP A C   
1664 O  O   . ASP A 211 ? 1.9390 1.7426 2.1874 -0.0319 0.5519  0.4262  211 ASP A O   
1665 C  CB  . ASP A 211 ? 1.9086 1.5476 2.0157 -0.1290 0.5314  0.4692  211 ASP A CB  
1666 C  CG  . ASP A 211 ? 1.8446 1.5206 2.0237 -0.1516 0.4877  0.4682  211 ASP A CG  
1667 O  OD1 . ASP A 211 ? 1.7882 1.4720 1.9917 -0.1164 0.4372  0.4613  211 ASP A OD1 
1668 O  OD2 . ASP A 211 ? 1.8697 1.5656 2.0791 -0.2055 0.5045  0.4736  211 ASP A OD2 
1669 N  N   . GLU A 212 ? 1.9010 1.6362 2.1283 0.0031  0.4547  0.4323  212 GLU A N   
1670 C  CA  . GLU A 212 ? 1.9041 1.7299 2.2270 0.0442  0.4467  0.4139  212 GLU A CA  
1671 C  C   . GLU A 212 ? 1.8749 1.8195 2.3149 0.0193  0.4565  0.4025  212 GLU A C   
1672 O  O   . GLU A 212 ? 1.9239 1.9588 2.4492 0.0541  0.4582  0.3826  212 GLU A O   
1673 C  CB  . GLU A 212 ? 1.8979 1.6910 2.2146 0.0824  0.3887  0.4152  212 GLU A CB  
1674 C  CG  . GLU A 212 ? 1.9112 1.6694 2.2107 0.0536  0.3441  0.4285  212 GLU A CG  
1675 C  CD  . GLU A 212 ? 1.9696 1.6128 2.1574 0.0542  0.3239  0.4403  212 GLU A CD  
1676 O  OE1 . GLU A 212 ? 2.0432 1.6289 2.1569 0.0482  0.3545  0.4427  212 GLU A OE1 
1677 O  OE2 . GLU A 212 ? 1.9555 1.5700 2.1294 0.0619  0.2773  0.4449  212 GLU A OE2 
1678 N  N   . THR A 213 ? 1.7519 1.6986 2.1990 -0.0387 0.4618  0.4119  213 THR A N   
1679 C  CA  . THR A 213 ? 1.6326 1.6947 2.1947 -0.0707 0.4733  0.3974  213 THR A CA  
1680 C  C   . THR A 213 ? 1.6146 1.7343 2.2045 -0.1037 0.5434  0.3899  213 THR A C   
1681 O  O   . THR A 213 ? 1.5320 1.7693 2.2324 -0.1249 0.5608  0.3702  213 THR A O   
1682 C  CB  . THR A 213 ? 1.5643 1.6012 2.1273 -0.1209 0.4429  0.4081  213 THR A CB  
1683 O  OG1 . THR A 213 ? 1.5823 1.4924 2.0236 -0.1487 0.4481  0.4325  213 THR A OG1 
1684 C  CG2 . THR A 213 ? 1.4617 1.5073 2.0545 -0.0881 0.3747  0.4039  213 THR A CG2 
1685 N  N   . ARG A 214 ? 1.6734 1.7184 2.1668 -0.1086 0.5844  0.4030  214 ARG A N   
1686 C  CA  . ARG A 214 ? 1.7699 1.8624 2.2751 -0.1396 0.6555  0.3983  214 ARG A CA  
1687 C  C   . ARG A 214 ? 1.8033 1.9646 2.3468 -0.0835 0.6793  0.3746  214 ARG A C   
1688 O  O   . ARG A 214 ? 1.8151 1.9094 2.2892 -0.0340 0.6660  0.3765  214 ARG A O   
1689 C  CB  . ARG A 214 ? 1.8562 1.8276 2.2270 -0.1733 0.6876  0.4255  214 ARG A CB  
1690 C  CG  . ARG A 214 ? 1.9468 1.8252 2.2577 -0.2191 0.6580  0.4494  214 ARG A CG  
1691 C  CD  . ARG A 214 ? 1.9940 1.9514 2.4119 -0.2661 0.6461  0.4415  214 ARG A CD  
1692 N  NE  . ARG A 214 ? 2.0057 1.8727 2.3712 -0.2948 0.6018  0.4594  214 ARG A NE  
1693 C  CZ  . ARG A 214 ? 1.9840 1.8968 2.4281 -0.3137 0.5609  0.4504  214 ARG A CZ  
1694 N  NH1 . ARG A 214 ? 1.9720 2.0220 2.5514 -0.3059 0.5571  0.4234  214 ARG A NH1 
1695 N  NH2 . ARG A 214 ? 1.9750 1.7986 2.3619 -0.3368 0.5216  0.4653  214 ARG A NH2 
1696 N  N   . ARG A 215 ? 1.8393 2.1891 2.6620 0.1826  0.9976  0.6129  215 ARG A N   
1697 C  CA  . ARG A 215 ? 1.8278 2.1946 2.6730 0.2194  1.0060  0.6303  215 ARG A CA  
1698 C  C   . ARG A 215 ? 1.8273 2.1279 2.6211 0.2683  1.0308  0.6299  215 ARG A C   
1699 O  O   . ARG A 215 ? 1.8559 2.1440 2.6439 0.3038  1.0348  0.6357  215 ARG A O   
1700 C  CB  . ARG A 215 ? 1.8707 2.3049 2.7735 0.2066  1.0153  0.6559  215 ARG A CB  
1701 C  CG  . ARG A 215 ? 1.8628 2.3621 2.8099 0.1510  0.9919  0.6569  215 ARG A CG  
1702 C  CD  . ARG A 215 ? 1.8157 2.3368 2.7788 0.1386  0.9595  0.6461  215 ARG A CD  
1703 N  NE  . ARG A 215 ? 1.7584 2.3482 2.7660 0.0863  0.9364  0.6495  215 ARG A NE  
1704 C  CZ  . ARG A 215 ? 1.6695 2.2872 2.6927 0.0621  0.9048  0.6390  215 ARG A CZ  
1705 N  NH1 . ARG A 215 ? 1.6027 2.1883 2.6035 0.0854  0.8927  0.6258  215 ARG A NH1 
1706 N  NH2 . ARG A 215 ? 1.6659 2.3443 2.7244 0.0123  0.8848  0.6417  215 ARG A NH2 
1707 N  N   . GLU A 216 ? 1.8148 2.0707 2.5683 0.2698  1.0482  0.6240  216 GLU A N   
1708 C  CA  . GLU A 216 ? 1.8089 1.9984 2.5057 0.3113  1.0691  0.6212  216 GLU A CA  
1709 C  C   . GLU A 216 ? 1.6920 1.8345 2.3423 0.3299  1.0539  0.6032  216 GLU A C   
1710 O  O   . GLU A 216 ? 1.6613 1.7831 2.2939 0.3639  1.0595  0.6071  216 GLU A O   
1711 C  CB  . GLU A 216 ? 1.8803 2.0331 2.5437 0.3032  1.0861  0.6174  216 GLU A CB  
1712 C  CG  . GLU A 216 ? 1.8764 2.0780 2.5828 0.2696  1.0955  0.6322  216 GLU A CG  
1713 C  CD  . GLU A 216 ? 1.8341 2.0654 2.5633 0.2194  1.0742  0.6232  216 GLU A CD  
1714 O  OE1 . GLU A 216 ? 1.7785 2.0421 2.5331 0.2060  1.0494  0.6171  216 GLU A OE1 
1715 O  OE2 . GLU A 216 ? 1.8425 2.0635 2.5623 0.1923  1.0826  0.6227  216 GLU A OE2 
1716 N  N   . HIS A 217 ? 1.6773 1.8037 2.3059 0.3071  1.0354  0.5843  217 HIS A N   
1717 C  CA  . HIS A 217 ? 1.6810 1.7709 2.2656 0.3209  1.0189  0.5682  217 HIS A CA  
1718 C  C   . HIS A 217 ? 1.6412 1.7646 2.2550 0.3263  1.0020  0.5725  217 HIS A C   
1719 O  O   . HIS A 217 ? 1.5429 1.6347 2.1191 0.3479  0.9953  0.5659  217 HIS A O   
1720 C  CB  . HIS A 217 ? 1.5552 1.6359 2.1211 0.2930  1.0015  0.5499  217 HIS A CB  
1721 C  CG  . HIS A 217 ? 1.6625 1.7007 2.1934 0.2911  1.0191  0.5460  217 HIS A CG  
1722 N  ND1 . HIS A 217 ? 1.6425 1.6599 2.1478 0.2732  1.0107  0.5312  217 HIS A ND1 
1723 C  CD2 . HIS A 217 ? 1.6991 1.7122 2.2169 0.3053  1.0458  0.5563  217 HIS A CD2 
1724 C  CE1 . HIS A 217 ? 1.6287 1.6062 2.1061 0.2775  1.0320  0.5332  217 HIS A CE1 
1725 N  NE2 . HIS A 217 ? 1.6614 1.6373 2.1465 0.2954  1.0525  0.5482  217 HIS A NE2 
1726 N  N   . PHE A 218 ? 1.6334 1.8216 2.3129 0.3057  0.9945  0.5848  218 PHE A N   
1727 C  CA  . PHE A 218 ? 1.6197 1.8419 2.3329 0.3139  0.9816  0.5937  218 PHE A CA  
1728 C  C   . PHE A 218 ? 1.6832 1.8752 2.3791 0.3601  1.0055  0.6078  218 PHE A C   
1729 O  O   . PHE A 218 ? 1.7291 1.8964 2.4007 0.3822  1.0009  0.6057  218 PHE A O   
1730 C  CB  . PHE A 218 ? 1.6558 1.9562 2.4432 0.2816  0.9697  0.6067  218 PHE A CB  
1731 C  CG  . PHE A 218 ? 1.6816 2.0244 2.5089 0.2801  0.9486  0.6141  218 PHE A CG  
1732 C  CD1 . PHE A 218 ? 1.7040 2.0148 2.5015 0.3049  0.9420  0.6092  218 PHE A CD1 
1733 C  CD2 . PHE A 218 ? 1.6588 2.0751 2.5525 0.2520  0.9348  0.6275  218 PHE A CD2 
1734 C  CE1 . PHE A 218 ? 1.6658 2.0155 2.5018 0.3031  0.9234  0.6184  218 PHE A CE1 
1735 C  CE2 . PHE A 218 ? 1.6348 2.0911 2.5668 0.2505  0.9144  0.6363  218 PHE A CE2 
1736 C  CZ  . PHE A 218 ? 1.6326 2.0548 2.5371 0.2767  0.9092  0.6321  218 PHE A CZ  
1737 N  N   . GLU A 219 ? 1.6898 1.8831 2.3950 0.3746  1.0325  0.6226  219 GLU A N   
1738 C  CA  . GLU A 219 ? 1.7021 1.8741 2.3960 0.4181  1.0572  0.6381  219 GLU A CA  
1739 C  C   . GLU A 219 ? 1.7524 1.8431 2.3650 0.4495  1.0694  0.6257  219 GLU A C   
1740 O  O   . GLU A 219 ? 1.7705 1.8319 2.3587 0.4834  1.0813  0.6316  219 GLU A O   
1741 C  CB  . GLU A 219 ? 1.7695 1.9723 2.4961 0.4234  1.0822  0.6581  219 GLU A CB  
1742 C  CG  . GLU A 219 ? 1.7656 2.0537 2.5730 0.3995  1.0727  0.6766  219 GLU A CG  
1743 C  CD  . GLU A 219 ? 1.8163 2.1425 2.6546 0.3947  1.0941  0.6953  219 GLU A CD  
1744 O  OE1 . GLU A 219 ? 1.7960 2.1938 2.6945 0.3633  1.0835  0.7078  219 GLU A OE1 
1745 O  OE2 . GLU A 219 ? 1.8628 2.1500 2.6640 0.4205  1.1207  0.6981  219 GLU A OE2 
1746 N  N   . ARG A 220 ? 1.8254 1.8780 2.3928 0.4388  1.0674  0.6096  220 ARG A N   
1747 C  CA  . ARG A 220 ? 1.8879 1.8670 2.3761 0.4653  1.0765  0.5987  220 ARG A CA  
1748 C  C   . ARG A 220 ? 1.8464 1.8028 2.3037 0.4759  1.0604  0.5902  220 ARG A C   
1749 O  O   . ARG A 220 ? 1.9141 1.8266 2.3269 0.5081  1.0745  0.5926  220 ARG A O   
1750 C  CB  . ARG A 220 ? 1.9721 1.9220 2.4233 0.4489  1.0723  0.5841  220 ARG A CB  
1751 C  CG  . ARG A 220 ? 2.0690 2.0374 2.5463 0.4346  1.0883  0.5919  220 ARG A CG  
1752 C  CD  . ARG A 220 ? 2.1136 2.0343 2.5388 0.4307  1.0907  0.5796  220 ARG A CD  
1753 N  NE  . ARG A 220 ? 2.1554 2.0890 2.5898 0.3982  1.0701  0.5667  220 ARG A NE  
1754 C  CZ  . ARG A 220 ? 2.2433 2.1513 2.6386 0.3960  1.0506  0.5507  220 ARG A CZ  
1755 N  NH1 . ARG A 220 ? 2.3060 2.1769 2.6514 0.4213  1.0470  0.5460  220 ARG A NH1 
1756 N  NH2 . ARG A 220 ? 2.2131 2.1342 2.6174 0.3679  1.0350  0.5400  220 ARG A NH2 
1757 N  N   . VAL A 221 ? 1.7850 1.7714 2.2629 0.4481  1.0314  0.5803  221 VAL A N   
1758 C  CA  . VAL A 221 ? 1.7281 1.7015 2.1806 0.4541  1.0143  0.5735  221 VAL A CA  
1759 C  C   . VAL A 221 ? 1.6909 1.6914 2.1846 0.4686  1.0182  0.5898  221 VAL A C   
1760 O  O   . VAL A 221 ? 1.6636 1.6334 2.1229 0.4899  1.0193  0.5899  221 VAL A O   
1761 C  CB  . VAL A 221 ? 1.6237 1.6267 2.0867 0.4189  0.9821  0.5589  221 VAL A CB  
1762 C  CG1 . VAL A 221 ? 1.5806 1.5606 1.9973 0.4261  0.9658  0.5502  221 VAL A CG1 
1763 C  CG2 . VAL A 221 ? 1.6032 1.5904 2.0442 0.4034  0.9826  0.5474  221 VAL A CG2 
1764 N  N   . GLY A 222 ? 1.7140 1.7721 2.2799 0.4578  1.0209  0.6049  222 GLY A N   
1765 C  CA  . GLY A 222 ? 1.7797 1.8644 2.3873 0.4765  1.0283  0.6244  222 GLY A CA  
1766 C  C   . GLY A 222 ? 1.8838 1.9131 2.4460 0.5228  1.0615  0.6332  222 GLY A C   
1767 O  O   . GLY A 222 ? 1.9200 1.9124 2.4473 0.5474  1.0657  0.6335  222 GLY A O   
1768 N  N   . GLU A 223 ? 1.9220 1.9434 2.4802 0.5345  1.0858  0.6401  223 GLU A N   
1769 C  CA  . GLU A 223 ? 1.9718 1.9408 2.4826 0.5778  1.1182  0.6474  223 GLU A CA  
1770 C  C   . GLU A 223 ? 1.9496 1.8379 2.3680 0.5953  1.1199  0.6298  223 GLU A C   
1771 O  O   . GLU A 223 ? 2.0106 1.8497 2.3824 0.6311  1.1411  0.6333  223 GLU A O   
1772 C  CB  . GLU A 223 ? 1.9872 1.9613 2.5016 0.5816  1.1406  0.6546  223 GLU A CB  
1773 C  CG  . GLU A 223 ? 1.9331 1.9875 2.5330 0.5666  1.1429  0.6748  223 GLU A CG  
1774 C  CD  . GLU A 223 ? 1.9743 2.0376 2.5764 0.5614  1.1607  0.6795  223 GLU A CD  
1775 O  OE1 . GLU A 223 ? 2.0176 2.0240 2.5568 0.5693  1.1702  0.6667  223 GLU A OE1 
1776 O  OE2 . GLU A 223 ? 1.9822 2.1117 2.6488 0.5483  1.1648  0.6971  223 GLU A OE2 
1777 N  N   . ALA A 224 ? 1.8581 1.7317 2.2457 0.5708  1.0982  0.6111  224 ALA A N   
1778 C  CA  . ALA A 224 ? 1.8786 1.6862 2.1818 0.5827  1.0944  0.5957  224 ALA A CA  
1779 C  C   . ALA A 224 ? 1.9597 1.7583 2.2558 0.5964  1.0893  0.5986  224 ALA A C   
1780 O  O   . ALA A 224 ? 2.1509 1.8991 2.4011 0.6309  1.1113  0.6024  224 ALA A O   
1781 C  CB  . ALA A 224 ? 1.8362 1.6455 2.1198 0.5523  1.0684  0.5782  224 ALA A CB  
1782 N  N   . ASP A 225 ? 1.8339 1.6803 2.1737 0.5697  1.0610  0.5967  225 ASP A N   
1783 C  CA  . ASP A 225 ? 1.8370 1.6782 2.1706 0.5789  1.0533  0.5996  225 ASP A CA  
1784 C  C   . ASP A 225 ? 1.8932 1.7227 2.2418 0.6149  1.0786  0.6171  225 ASP A C   
1785 O  O   . ASP A 225 ? 1.9450 1.7374 2.2576 0.6363  1.0832  0.6177  225 ASP A O   
1786 C  CB  . ASP A 225 ? 1.7973 1.7121 2.1989 0.5412  1.0194  0.6003  225 ASP A CB  
1787 C  CG  . ASP A 225 ? 1.7747 1.6926 2.1460 0.5106  0.9929  0.5814  225 ASP A CG  
1788 O  OD1 . ASP A 225 ? 1.8417 1.7012 2.1323 0.5223  0.9981  0.5696  225 ASP A OD1 
1789 O  OD2 . ASP A 225 ? 1.6665 1.6458 2.0924 0.4750  0.9664  0.5787  225 ASP A OD2 
1790 N  N   . ILE A 226 ? 1.8830 1.7430 2.2815 0.6233  1.0958  0.6321  226 ILE A N   
1791 C  CA  . ILE A 226 ? 1.9321 1.7743 2.3334 0.6633  1.1235  0.6486  226 ILE A CA  
1792 C  C   . ILE A 226 ? 2.0387 1.7855 2.3363 0.6996  1.1496  0.6380  226 ILE A C   
1793 O  O   . ILE A 226 ? 2.1161 1.8148 2.3738 0.7315  1.1628  0.6394  226 ILE A O   
1794 C  CB  . ILE A 226 ? 1.8735 1.7753 2.3477 0.6639  1.1366  0.6685  226 ILE A CB  
1795 C  CG1 . ILE A 226 ? 1.7916 1.7863 2.3650 0.6287  1.1099  0.6803  226 ILE A CG1 
1796 C  CG2 . ILE A 226 ? 1.9489 1.8275 2.4150 0.7102  1.1684  0.6852  226 ILE A CG2 
1797 C  CD1 . ILE A 226 ? 1.7674 1.8208 2.3959 0.6044  1.1089  0.6875  226 ILE A CD1 
1798 N  N   . LYS A 227 ? 1.9898 1.7048 2.2388 0.6951  1.1564  0.6265  227 LYS A N   
1799 C  CA  . LYS A 227 ? 2.0746 1.6992 2.2190 0.7232  1.1761  0.6144  227 LYS A CA  
1800 C  C   . LYS A 227 ? 2.2058 1.7790 2.2816 0.7222  1.1614  0.5989  227 LYS A C   
1801 O  O   . LYS A 227 ? 2.3083 1.8178 2.3226 0.7527  1.1758  0.5957  227 LYS A O   
1802 C  CB  . LYS A 227 ? 2.0878 1.6979 2.2018 0.7135  1.1815  0.6066  227 LYS A CB  
1803 N  N   . LEU A 228 ? 2.0951 1.6956 2.1787 0.6874  1.1321  0.5890  228 LEU A N   
1804 C  CA  . LEU A 228 ? 2.1050 1.6658 2.1222 0.6830  1.1167  0.5757  228 LEU A CA  
1805 C  C   . LEU A 228 ? 2.1521 1.6913 2.1616 0.7055  1.1219  0.5811  228 LEU A C   
1806 O  O   . LEU A 228 ? 2.2755 1.7462 2.1965 0.7192  1.1239  0.5700  228 LEU A O   
1807 C  CB  . LEU A 228 ? 2.0297 1.6504 2.0851 0.6407  1.0816  0.5698  228 LEU A CB  
1808 C  CG  . LEU A 228 ? 2.0581 1.6821 2.0928 0.6179  1.0688  0.5580  228 LEU A CG  
1809 C  CD1 . LEU A 228 ? 2.1400 1.6827 2.0655 0.6358  1.0801  0.5466  228 LEU A CD1 
1810 C  CD2 . LEU A 228 ? 2.0682 1.7319 2.1656 0.6090  1.0761  0.5643  228 LEU A CD2 
1811 N  N   . MSE A 229 ? 2.0778 1.6716 2.1751 0.7103  1.1239  0.5981  229 MSE A N   
1812 C  CA  . MSE A 229 ? 2.0782 1.6512 2.1760 0.7361  1.1284  0.6046  229 MSE A CA  
1813 C  C   . MSE A 229 ? 2.2013 1.7021 2.2484 0.7832  1.1605  0.6063  229 MSE A C   
1814 O  O   . MSE A 229 ? 2.2761 1.7134 2.2753 0.8131  1.1654  0.6022  229 MSE A O   
1815 C  CB  . MSE A 229 ? 2.0118 1.6821 2.2309 0.7179  1.1110  0.6241  229 MSE A CB  
1816 C  CG  . MSE A 229 ? 2.0879 1.7450 2.3190 0.7412  1.1075  0.6318  229 MSE A CG  
1817 SE SE  . MSE A 229 ? 2.2331 1.8607 2.3972 0.6999  1.0470  0.6140  229 MSE A SE  
1818 C  CE  . MSE A 229 ? 2.3777 1.8438 2.3616 0.7308  1.0576  0.5881  229 MSE A CE  
1819 N  N   . GLU A 230 ? 2.2227 1.7297 2.2770 0.7903  1.1806  0.6114  230 GLU A N   
1820 C  CA  . GLU A 230 ? 2.3105 1.7549 2.3139 0.8335  1.2121  0.6130  230 GLU A CA  
1821 C  C   . GLU A 230 ? 2.4645 1.7924 2.3321 0.8538  1.2210  0.5904  230 GLU A C   
1822 O  O   . GLU A 230 ? 2.5555 1.8105 2.3637 0.8906  1.2375  0.5860  230 GLU A O   
1823 C  CB  . GLU A 230 ? 2.3067 1.7864 2.3429 0.8346  1.2313  0.6233  230 GLU A CB  
1824 C  CG  . GLU A 230 ? 2.2705 1.8238 2.4048 0.8456  1.2416  0.6487  230 GLU A CG  
1825 C  CD  . GLU A 230 ? 2.2914 1.8726 2.4469 0.8504  1.2629  0.6587  230 GLU A CD  
1826 O  OE1 . GLU A 230 ? 2.2197 1.8818 2.4572 0.8219  1.2519  0.6705  230 GLU A OE1 
1827 O  OE2 . GLU A 230 ? 2.3832 1.9041 2.4704 0.8825  1.2901  0.6543  230 GLU A OE2 
1828 N  N   . LEU A 231 ? 2.5768 1.8831 2.3897 0.8298  1.2087  0.5756  231 LEU A N   
1829 C  CA  . LEU A 231 ? 2.7654 1.9638 2.4447 0.8433  1.2141  0.5548  231 LEU A CA  
1830 C  C   . LEU A 231 ? 2.8690 2.0267 2.5012 0.8405  1.1939  0.5438  231 LEU A C   
1831 O  O   . LEU A 231 ? 3.0852 2.1465 2.5966 0.8495  1.1954  0.5256  231 LEU A O   
1832 C  CB  . LEU A 231 ? 2.7769 1.9707 2.4146 0.8206  1.2105  0.5461  231 LEU A CB  
1833 C  CG  . LEU A 231 ? 2.7927 2.0248 2.4714 0.8175  1.2245  0.5544  231 LEU A CG  
1834 C  CD1 . LEU A 231 ? 2.6727 2.0101 2.4662 0.7841  1.2056  0.5663  231 LEU A CD1 
1835 C  CD2 . LEU A 231 ? 2.8645 2.0378 2.4510 0.8149  1.2289  0.5408  231 LEU A CD2 
1836 N  N   . GLY A 232 ? 2.6703 1.8970 2.3915 0.8279  1.1744  0.5548  232 GLY A N   
1837 C  CA  . GLY A 232 ? 2.6333 1.8298 2.3144 0.8059  1.1290  0.5467  232 GLY A CA  
1838 C  C   . GLY A 232 ? 2.4636 1.6864 2.1115 0.7537  1.0900  0.5387  232 GLY A C   
1839 O  O   . GLY A 232 ? 2.4506 1.6185 2.0126 0.7261  1.0432  0.5279  232 GLY A O   
1840 N  N   . TYR A 233 ? 2.3722 1.6784 2.0850 0.7391  1.1078  0.5452  233 TYR A N   
1841 C  CA  . TYR A 233 ? 2.4026 1.7347 2.0839 0.6970  1.0787  0.5388  233 TYR A CA  
1842 C  C   . TYR A 233 ? 2.2813 1.7116 2.0508 0.6524  1.0346  0.5470  233 TYR A C   
1843 O  O   . TYR A 233 ? 2.2882 1.7275 2.0175 0.6146  0.9904  0.5413  233 TYR A O   
1844 C  CB  . TYR A 233 ? 2.4752 1.8201 2.1590 0.7000  1.1045  0.5366  233 TYR A CB  
1845 C  CG  . TYR A 233 ? 2.6074 1.8532 2.1798 0.7256  1.1265  0.5248  233 TYR A CG  
1846 C  CD1 . TYR A 233 ? 2.6435 1.8811 2.2304 0.7396  1.1458  0.5261  233 TYR A CD1 
1847 C  CD2 . TYR A 233 ? 2.6714 1.8313 2.1162 0.7310  1.1266  0.5141  233 TYR A CD2 
1848 C  CE1 . TYR A 233 ? 2.7527 1.9035 2.2389 0.7608  1.1653  0.5162  233 TYR A CE1 
1849 C  CE2 . TYR A 233 ? 2.7639 1.8299 2.1021 0.7517  1.1450  0.5019  233 TYR A CE2 
1850 C  CZ  . TYR A 233 ? 2.7957 1.8600 2.1596 0.7673  1.1643  0.5029  233 TYR A CZ  
1851 O  OH  . TYR A 233 ? 2.8726 1.8482 2.1325 0.7854  1.1819  0.4919  233 TYR A OH  
1852 N  N   . LEU A 234 ? 2.1813 1.6886 2.0685 0.6553  1.0458  0.5614  234 LEU A N   
1853 C  CA  . LEU A 234 ? 2.0610 1.6633 2.0337 0.6122  1.0064  0.5687  234 LEU A CA  
1854 C  C   . LEU A 234 ? 2.0365 1.6218 1.9807 0.5859  0.9451  0.5660  234 LEU A C   
1855 O  O   . LEU A 234 ? 2.0604 1.6149 2.0129 0.6042  0.9402  0.5714  234 LEU A O   
1856 C  CB  . LEU A 234 ? 1.9653 1.6496 2.0656 0.6208  1.0333  0.5866  234 LEU A CB  
1857 C  CG  . LEU A 234 ? 1.7972 1.5791 1.9844 0.5752  1.0043  0.5894  234 LEU A CG  
1858 C  CD1 . LEU A 234 ? 1.7171 1.5512 1.9999 0.5737  1.0095  0.5992  234 LEU A CD1 
1859 C  CD2 . LEU A 234 ? 1.7474 1.5751 1.9618 0.5403  0.9568  0.5934  234 LEU A CD2 
1860 N  N   . PRO A 235 ? 1.9790 1.5845 1.8898 0.5443  0.8979  0.5597  235 PRO A N   
1861 C  CA  . PRO A 235 ? 2.0055 1.5956 1.8827 0.5159  0.8376  0.5587  235 PRO A CA  
1862 C  C   . PRO A 235 ? 1.9089 1.5902 1.8973 0.4907  0.8087  0.5714  235 PRO A C   
1863 O  O   . PRO A 235 ? 1.8209 1.5864 1.9036 0.4833  0.8270  0.5784  235 PRO A O   
1864 C  CB  . PRO A 235 ? 2.0076 1.5992 1.8114 0.4822  0.8042  0.5501  235 PRO A CB  
1865 C  CG  . PRO A 235 ? 1.9437 1.6027 1.8025 0.4801  0.8346  0.5511  235 PRO A CG  
1866 C  CD  . PRO A 235 ? 1.9272 1.5737 1.8301 0.5222  0.8981  0.5550  235 PRO A CD  
1867 N  N   . PRO A 236 ? 1.9319 1.5978 1.9100 0.4747  0.7628  0.5753  236 PRO A N   
1868 C  CA  . PRO A 236 ? 1.8557 1.6104 1.9390 0.4489  0.7330  0.5890  236 PRO A CA  
1869 C  C   . PRO A 236 ? 1.7122 1.5604 1.8355 0.4022  0.7015  0.5876  236 PRO A C   
1870 O  O   . PRO A 236 ? 1.6018 1.4413 1.6595 0.3852  0.6877  0.5773  236 PRO A O   
1871 C  CB  . PRO A 236 ? 1.9051 1.6046 1.9412 0.4405  0.6867  0.5920  236 PRO A CB  
1872 C  CG  . PRO A 236 ? 2.0437 1.6163 1.9658 0.4768  0.7099  0.5812  236 PRO A CG  
1873 C  CD  . PRO A 236 ? 2.0320 1.5924 1.9003 0.4807  0.7382  0.5686  236 PRO A CD  
1874 N  N   . LEU A 237 ? 1.5597 1.5007 1.7925 0.3821  0.6909  0.5994  237 LEU A N   
1875 C  CA  . LEU A 237 ? 1.4747 1.5065 1.7504 0.3382  0.6616  0.5975  237 LEU A CA  
1876 C  C   . LEU A 237 ? 1.5664 1.6029 1.7919 0.3002  0.5964  0.5954  237 LEU A C   
1877 O  O   . LEU A 237 ? 1.6005 1.6705 1.7973 0.2738  0.5748  0.5878  237 LEU A O   
1878 C  CB  . LEU A 237 ? 1.3876 1.5143 1.7897 0.3244  0.6674  0.6110  237 LEU A CB  
1879 C  CG  . LEU A 237 ? 1.2633 1.4860 1.7180 0.2795  0.6413  0.6084  237 LEU A CG  
1880 C  CD1 . LEU A 237 ? 1.2555 1.4757 1.6773 0.2826  0.6695  0.5949  237 LEU A CD1 
1881 C  CD2 . LEU A 237 ? 1.2011 1.5092 1.7756 0.2650  0.6475  0.6234  237 LEU A CD2 
1882 N  N   . ARG A 238 ? 1.7223 1.7264 1.9357 0.2975  0.5646  0.6035  238 ARG A N   
1883 C  CA  . ARG A 238 ? 1.7812 1.7857 1.9440 0.2592  0.5001  0.6044  238 ARG A CA  
1884 C  C   . ARG A 238 ? 2.0320 1.9235 2.0645 0.2731  0.4944  0.5960  238 ARG A C   
1885 O  O   . ARG A 238 ? 2.1045 1.9190 2.0936 0.2857  0.4831  0.5996  238 ARG A O   
1886 C  CB  . ARG A 238 ? 1.6938 1.7305 1.9197 0.2428  0.4649  0.6202  238 ARG A CB  
1887 C  CG  . ARG A 238 ? 1.5140 1.6731 1.8584 0.2142  0.4555  0.6290  238 ARG A CG  
1888 C  CD  . ARG A 238 ? 1.4162 1.6460 1.7507 0.1701  0.4182  0.6220  238 ARG A CD  
1889 N  NE  . ARG A 238 ? 1.3655 1.6088 1.6706 0.1320  0.3527  0.6290  238 ARG A NE  
1890 C  CZ  . ARG A 238 ? 1.3443 1.6459 1.6284 0.0928  0.3119  0.6258  238 ARG A CZ  
1891 N  NH1 . ARG A 238 ? 1.3863 1.7012 1.6446 0.0574  0.2522  0.6349  238 ARG A NH1 
1892 N  NH2 . ARG A 238 ? 1.3459 1.6928 1.6337 0.0897  0.3311  0.6147  238 ARG A NH2 
1893 N  N   . GLY A 239 ? 2.1129 1.9928 2.0795 0.2701  0.5024  0.5852  239 GLY A N   
1894 C  CA  . GLY A 239 ? 2.2428 2.0228 2.0818 0.2782  0.4974  0.5777  239 GLY A CA  
1895 C  C   . GLY A 239 ? 2.3351 2.0280 2.1353 0.3286  0.5580  0.5697  239 GLY A C   
1896 O  O   . GLY A 239 ? 2.4101 2.0320 2.1980 0.3571  0.5736  0.5710  239 GLY A O   
1897 O  OXT . GLY A 239 ? 2.3232 2.0145 2.1021 0.3433  0.5936  0.5624  239 GLY A OXT 
1898 N  N   . GLN B 1   ? 1.8851 2.0264 1.6412 0.0604  0.0820  -0.2515 84  GLN B N   
1899 C  CA  . GLN B 1   ? 1.9065 2.0620 1.7255 0.0455  0.0943  -0.2591 84  GLN B CA  
1900 C  C   . GLN B 1   ? 1.9428 2.1102 1.8570 0.0484  0.0744  -0.2859 84  GLN B C   
1901 O  O   . GLN B 1   ? 1.9693 2.1547 1.9080 0.0623  0.0622  -0.3217 84  GLN B O   
1902 C  CB  . GLN B 1   ? 1.9168 2.1040 1.7074 0.0516  0.1223  -0.2799 84  GLN B CB  
1903 C  CG  . GLN B 1   ? 1.8793 2.0814 1.7244 0.0331  0.1417  -0.2843 84  GLN B CG  
1904 C  CD  . GLN B 1   ? 1.8159 2.0646 1.7074 0.0428  0.1467  -0.3306 84  GLN B CD  
1905 O  OE1 . GLN B 1   ? 1.7487 2.0127 1.7050 0.0526  0.1242  -0.3595 84  GLN B OE1 
1906 N  NE2 . GLN B 1   ? 1.8199 2.0889 1.6832 0.0392  0.1815  -0.3395 84  GLN B NE2 
1907 N  N   . GLY B 2   ? 1.9708 2.1296 1.9413 0.0381  0.0735  -0.2708 85  GLY B N   
1908 C  CA  . GLY B 2   ? 1.9745 2.1293 2.0302 0.0456  0.0616  -0.2830 85  GLY B CA  
1909 C  C   . GLY B 2   ? 1.9804 2.1022 2.0524 0.0427  0.0518  -0.2419 85  GLY B C   
1910 O  O   . GLY B 2   ? 1.9769 2.1074 2.0848 0.0466  0.0519  -0.2319 85  GLY B O   
1911 N  N   . ARG B 3   ? 1.9858 2.0756 2.0299 0.0398  0.0425  -0.2206 86  ARG B N   
1912 C  CA  . ARG B 3   ? 1.9306 1.9916 1.9673 0.0371  0.0346  -0.1789 86  ARG B CA  
1913 C  C   . ARG B 3   ? 1.9386 1.9895 2.0383 0.0532  0.0328  -0.1661 86  ARG B C   
1914 O  O   . ARG B 3   ? 1.9267 1.9997 2.0376 0.0600  0.0308  -0.1578 86  ARG B O   
1915 C  CB  . ARG B 3   ? 1.8587 1.9315 1.8461 0.0237  0.0384  -0.1597 86  ARG B CB  
1916 C  CG  . ARG B 3   ? 1.8179 1.8939 1.7402 0.0131  0.0512  -0.1669 86  ARG B CG  
1917 C  CD  . ARG B 3   ? 1.7729 1.8694 1.6807 -0.0006 0.0717  -0.1670 86  ARG B CD  
1918 N  NE  . ARG B 3   ? 1.7683 1.8663 1.6209 -0.0029 0.0953  -0.1764 86  ARG B NE  
1919 C  CZ  . ARG B 3   ? 1.7437 1.8501 1.5784 -0.0167 0.1263  -0.1773 86  ARG B CZ  
1920 N  NH1 . ARG B 3   ? 1.6910 1.8155 1.5700 -0.0324 0.1328  -0.1792 86  ARG B NH1 
1921 N  NH2 . ARG B 3   ? 1.7657 1.8652 1.5393 -0.0123 0.1533  -0.1785 86  ARG B NH2 
1922 N  N   . ASP B 4   ? 1.9857 2.0035 2.1288 0.0623  0.0363  -0.1654 87  ASP B N   
1923 C  CA  . ASP B 4   ? 2.0622 2.0561 2.2567 0.0845  0.0420  -0.1427 87  ASP B CA  
1924 C  C   . ASP B 4   ? 2.0810 2.0213 2.2991 0.0873  0.0537  -0.1255 87  ASP B C   
1925 O  O   . ASP B 4   ? 2.0762 2.0088 2.2938 0.0713  0.0560  -0.1480 87  ASP B O   
1926 C  CB  . ASP B 4   ? 2.1330 2.1446 2.3936 0.0981  0.0510  -0.1736 87  ASP B CB  
1927 C  CG  . ASP B 4   ? 2.1356 2.1830 2.3967 0.1132  0.0428  -0.1647 87  ASP B CG  
1928 O  OD1 . ASP B 4   ? 2.1253 2.1801 2.3467 0.1185  0.0307  -0.1327 87  ASP B OD1 
1929 O  OD2 . ASP B 4   ? 2.1221 2.1968 2.4287 0.1209  0.0478  -0.1951 87  ASP B OD2 
1930 N  N   . LYS B 5   ? 2.0755 1.9807 2.3171 0.1119  0.0638  -0.0872 88  LYS B N   
1931 C  CA  . LYS B 5   ? 2.1099 1.9569 2.3591 0.1175  0.0818  -0.0540 88  LYS B CA  
1932 C  C   . LYS B 5   ? 2.3127 2.1602 2.5067 0.0930  0.0710  -0.0502 88  LYS B C   
1933 O  O   . LYS B 5   ? 2.2425 2.0795 2.4599 0.0744  0.0788  -0.0800 88  LYS B O   
1934 C  CB  . LYS B 5   ? 1.9084 1.7130 2.2457 0.1169  0.1141  -0.0789 88  LYS B CB  
1935 C  CG  . LYS B 5   ? 1.7158 1.4477 2.0729 0.1313  0.1469  -0.0335 88  LYS B CG  
1936 C  CD  . LYS B 5   ? 1.5584 1.2489 2.0084 0.1155  0.1846  -0.0703 88  LYS B CD  
1937 C  CE  . LYS B 5   ? 1.5338 1.1469 1.9978 0.1239  0.2256  -0.0230 88  LYS B CE  
1938 N  NZ  . LYS B 5   ? 1.4793 1.0940 1.9186 0.0951  0.2222  -0.0328 88  LYS B NZ  
1939 N  N   . ASP B 6   ? 2.6003 2.4660 2.7273 0.0941  0.0524  -0.0201 89  ASP B N   
1940 C  CA  . ASP B 6   ? 2.6233 2.4887 2.6981 0.0726  0.0425  -0.0154 89  ASP B CA  
1941 C  C   . ASP B 6   ? 2.6819 2.4982 2.7572 0.0800  0.0591  0.0205  89  ASP B C   
1942 O  O   . ASP B 6   ? 2.7576 2.5640 2.8090 0.1037  0.0606  0.0627  89  ASP B O   
1943 C  CB  . ASP B 6   ? 2.6283 2.5352 2.6432 0.0666  0.0209  -0.0074 89  ASP B CB  
1944 C  CG  . ASP B 6   ? 2.6606 2.5750 2.6538 0.0900  0.0140  0.0302  89  ASP B CG  
1945 O  OD1 . ASP B 6   ? 2.6489 2.5508 2.6054 0.0881  0.0113  0.0543  89  ASP B OD1 
1946 O  OD2 . ASP B 6   ? 2.6661 2.6043 2.6790 0.1139  0.0100  0.0327  89  ASP B OD2 
1947 N  N   . CYS B 7   ? 2.4704 2.2607 2.5746 0.0626  0.0731  0.0002  90  CYS B N   
1948 C  CA  . CYS B 7   ? 2.1908 1.9297 2.3088 0.0657  0.0990  0.0288  90  CYS B CA  
1949 C  C   . CYS B 7   ? 2.0290 1.7732 2.0803 0.0564  0.0849  0.0521  90  CYS B C   
1950 O  O   . CYS B 7   ? 1.9788 1.6944 2.0075 0.0713  0.0988  0.0956  90  CYS B O   
1951 C  CB  . CYS B 7   ? 2.0096 1.7248 2.2049 0.0484  0.1238  -0.0136 90  CYS B CB  
1952 S  SG  . CYS B 7   ? 1.9003 1.5687 2.1985 0.0635  0.1679  -0.0212 90  CYS B SG  
1953 N  N   . VAL B 8   ? 1.9213 1.6998 1.9387 0.0355  0.0603  0.0249  91  VAL B N   
1954 C  CA  . VAL B 8   ? 1.8289 1.6103 1.7935 0.0240  0.0489  0.0390  91  VAL B CA  
1955 C  C   . VAL B 8   ? 1.6716 1.4944 1.5804 0.0184  0.0223  0.0363  91  VAL B C   
1956 O  O   . VAL B 8   ? 1.7058 1.5481 1.6030 0.0067  0.0114  0.0070  91  VAL B O   
1957 C  CB  . VAL B 8   ? 1.8757 1.6483 1.8618 0.0054  0.0527  0.0073  91  VAL B CB  
1958 C  CG1 . VAL B 8   ? 1.8512 1.6281 1.7818 -0.0043 0.0395  0.0221  91  VAL B CG1 
1959 C  CG2 . VAL B 8   ? 1.9481 1.6780 2.0041 0.0059  0.0882  0.0051  91  VAL B CG2 
1960 N  N   . GLU B 9   ? 1.5148 1.3527 1.3905 0.0291  0.0148  0.0645  92  GLU B N   
1961 C  CA  . GLU B 9   ? 1.4082 1.2808 1.2409 0.0179  -0.0028 0.0594  92  GLU B CA  
1962 C  C   . GLU B 9   ? 1.4751 1.3346 1.2769 0.0022  -0.0056 0.0627  92  GLU B C   
1963 O  O   . GLU B 9   ? 1.6031 1.4377 1.4075 0.0060  0.0035  0.0800  92  GLU B O   
1964 C  CB  . GLU B 9   ? 1.3730 1.2777 1.1933 0.0367  -0.0111 0.0775  92  GLU B CB  
1965 C  CG  . GLU B 9   ? 1.4532 1.3345 1.2754 0.0648  -0.0006 0.1129  92  GLU B CG  
1966 C  CD  . GLU B 9   ? 1.5224 1.4465 1.3209 0.0937  -0.0142 0.1296  92  GLU B CD  
1967 O  OE1 . GLU B 9   ? 1.5372 1.4948 1.3046 0.0855  -0.0280 0.1237  92  GLU B OE1 
1968 O  OE2 . GLU B 9   ? 1.5302 1.4561 1.3433 0.1276  -0.0108 0.1460  92  GLU B OE2 
1969 N  N   . CYS B 10  ? 1.3388 1.2111 1.1126 -0.0140 -0.0135 0.0472  93  CYS B N   
1970 C  CA  . CYS B 10  ? 1.1595 1.0212 0.9030 -0.0270 -0.0170 0.0487  93  CYS B CA  
1971 C  C   . CYS B 10  ? 1.0316 0.8658 0.7900 -0.0281 -0.0130 0.0425  93  CYS B C   
1972 O  O   . CYS B 10  ? 0.9980 0.8171 0.7643 -0.0263 -0.0058 0.0579  93  CYS B O   
1973 C  CB  . CYS B 10  ? 1.1420 1.0192 0.8679 -0.0262 -0.0208 0.0663  93  CYS B CB  
1974 S  SG  . CYS B 10  ? 1.2515 1.1336 0.9454 -0.0464 -0.0241 0.0572  93  CYS B SG  
1975 N  N   . PRO B 11  ? 1.0351 0.8674 0.7994 -0.0287 -0.0159 0.0165  94  PRO B N   
1976 C  CA  . PRO B 11  ? 1.0468 0.8672 0.8350 -0.0294 -0.0150 -0.0027 94  PRO B CA  
1977 C  C   . PRO B 11  ? 1.0687 0.8795 0.8320 -0.0370 -0.0187 0.0064  94  PRO B C   
1978 O  O   . PRO B 11  ? 1.0562 0.8543 0.8497 -0.0405 -0.0100 0.0023  94  PRO B O   
1979 C  CB  . PRO B 11  ? 0.8768 0.7150 0.6587 -0.0211 -0.0252 -0.0365 94  PRO B CB  
1980 C  CG  . PRO B 11  ? 0.9106 0.7615 0.6905 -0.0170 -0.0220 -0.0341 94  PRO B CG  
1981 C  CD  . PRO B 11  ? 0.9391 0.7875 0.6964 -0.0243 -0.0184 -0.0015 94  PRO B CD  
1982 N  N   . PRO B 12  ? 1.0495 0.8637 0.7653 -0.0412 -0.0266 0.0164  95  PRO B N   
1983 C  CA  . PRO B 12  ? 1.0410 0.8463 0.7395 -0.0483 -0.0291 0.0222  95  PRO B CA  
1984 C  C   . PRO B 12  ? 1.0708 0.8723 0.7809 -0.0535 -0.0199 0.0425  95  PRO B C   
1985 O  O   . PRO B 12  ? 1.1229 0.9191 0.8249 -0.0597 -0.0198 0.0437  95  PRO B O   
1986 C  CB  . PRO B 12  ? 1.0403 0.8460 0.6954 -0.0526 -0.0314 0.0297  95  PRO B CB  
1987 C  CG  . PRO B 12  ? 1.0499 0.8674 0.7037 -0.0514 -0.0265 0.0322  95  PRO B CG  
1988 C  CD  . PRO B 12  ? 1.0476 0.8694 0.7283 -0.0402 -0.0284 0.0173  95  PRO B CD  
1989 N  N   . SER B 13  ? 1.0047 0.8095 0.7291 -0.0466 -0.0113 0.0596  96  SER B N   
1990 C  CA  . SER B 13  ? 0.9264 0.7245 0.6521 -0.0415 0.0014  0.0839  96  SER B CA  
1991 C  C   . SER B 13  ? 0.8984 0.6684 0.6601 -0.0448 0.0205  0.0787  96  SER B C   
1992 O  O   . SER B 13  ? 1.0354 0.7937 0.7918 -0.0427 0.0368  0.0989  96  SER B O   
1993 C  CB  . SER B 13  ? 0.9061 0.7123 0.6346 -0.0231 0.0072  0.1063  96  SER B CB  
1994 O  OG  . SER B 13  ? 1.0719 0.8571 0.8422 -0.0169 0.0203  0.1013  96  SER B OG  
1995 N  N   . ARG B 14  ? 0.8911 0.6551 0.6920 -0.0490 0.0211  0.0477  97  ARG B N   
1996 C  CA  . ARG B 14  ? 0.9179 0.6638 0.7721 -0.0559 0.0410  0.0275  97  ARG B CA  
1997 C  C   . ARG B 14  ? 0.9323 0.6887 0.7815 -0.0652 0.0291  0.0031  97  ARG B C   
1998 O  O   . ARG B 14  ? 0.9222 0.6765 0.8247 -0.0717 0.0405  -0.0290 97  ARG B O   
1999 C  CB  . ARG B 14  ? 0.9678 0.7159 0.8805 -0.0541 0.0459  -0.0077 97  ARG B CB  
2000 C  CG  . ARG B 14  ? 1.0530 0.7949 0.9717 -0.0430 0.0528  0.0104  97  ARG B CG  
2001 C  CD  . ARG B 14  ? 1.1839 0.8868 1.1589 -0.0399 0.0936  0.0249  97  ARG B CD  
2002 N  NE  . ARG B 14  ? 1.2414 0.9403 1.3014 -0.0505 0.1114  -0.0250 97  ARG B NE  
2003 C  CZ  . ARG B 14  ? 1.2328 0.9510 1.3354 -0.0480 0.1045  -0.0636 97  ARG B CZ  
2004 N  NH1 . ARG B 14  ? 1.2012 0.9381 1.2649 -0.0362 0.0827  -0.0527 97  ARG B NH1 
2005 N  NH2 . ARG B 14  ? 1.2207 0.9453 1.4108 -0.0579 0.1209  -0.1192 97  ARG B NH2 
2006 N  N   . GLY B 15  ? 1.0059 0.7748 0.8004 -0.0657 0.0085  0.0130  98  GLY B N   
2007 C  CA  . GLY B 15  ? 0.9807 0.7557 0.7674 -0.0707 -0.0017 -0.0051 98  GLY B CA  
2008 C  C   . GLY B 15  ? 0.9676 0.7315 0.7611 -0.0801 0.0184  0.0095  98  GLY B C   
2009 O  O   . GLY B 15  ? 1.0638 0.8098 0.8779 -0.0807 0.0462  0.0291  98  GLY B O   
2010 N  N   . GLU B 16  ? 0.9527 0.7245 0.7256 -0.0848 0.0075  0.0019  99  GLU B N   
2011 C  CA  . GLU B 16  ? 0.9760 0.7426 0.7533 -0.0937 0.0263  0.0104  99  GLU B CA  
2012 C  C   . GLU B 16  ? 1.0176 0.7970 0.7603 -0.0969 0.0085  0.0060  99  GLU B C   
2013 O  O   . GLU B 16  ? 1.0227 0.8067 0.7509 -0.0916 -0.0137 -0.0093 99  GLU B O   
2014 C  CB  . GLU B 16  ? 1.0103 0.7697 0.8524 -0.1017 0.0471  -0.0195 99  GLU B CB  
2015 C  CG  . GLU B 16  ? 1.1015 0.8824 0.9707 -0.0981 0.0227  -0.0683 99  GLU B CG  
2016 C  CD  . GLU B 16  ? 1.3113 1.0983 1.2538 -0.1085 0.0428  -0.1085 99  GLU B CD  
2017 O  OE1 . GLU B 16  ? 1.4081 1.1805 1.3614 -0.1218 0.0729  -0.0948 99  GLU B OE1 
2018 O  OE2 . GLU B 16  ? 1.4070 1.2184 1.3986 -0.1020 0.0300  -0.1579 99  GLU B OE2 
2019 N  N   . MSE B 17  ? 0.8808 0.6641 0.6089 -0.1028 0.0221  0.0206  100 MSE B N   
2020 C  CA  . MSE B 17  ? 0.9400 0.7363 0.6488 -0.1084 0.0107  0.0100  100 MSE B CA  
2021 C  C   . MSE B 17  ? 0.9021 0.6968 0.6481 -0.1144 0.0156  -0.0196 100 MSE B C   
2022 O  O   . MSE B 17  ? 0.8844 0.6717 0.6683 -0.1198 0.0401  -0.0249 100 MSE B O   
2023 C  CB  . MSE B 17  ? 1.0283 0.8426 0.7046 -0.1092 0.0204  0.0312  100 MSE B CB  
2024 C  CG  . MSE B 17  ? 1.2391 1.0703 0.8844 -0.1004 0.0118  0.0507  100 MSE B CG  
2025 SE SE  . MSE B 17  ? 1.4160 1.2934 1.0206 -0.0921 0.0167  0.0630  100 MSE B SE  
2026 C  CE  . MSE B 17  ? 1.2362 1.1267 0.8515 -0.1117 0.0051  0.0248  100 MSE B CE  
2027 N  N   . ALA B 18  ? 0.8630 0.6633 0.6028 -0.1124 -0.0040 -0.0400 101 ALA B N   
2028 C  CA  . ALA B 18  ? 0.8832 0.6901 0.6602 -0.1133 -0.0051 -0.0738 101 ALA B CA  
2029 C  C   . ALA B 18  ? 0.9459 0.7552 0.7016 -0.1095 -0.0217 -0.0829 101 ALA B C   
2030 O  O   . ALA B 18  ? 0.9036 0.7041 0.6231 -0.1056 -0.0313 -0.0674 101 ALA B O   
2031 C  CB  . ALA B 18  ? 0.8588 0.6708 0.6736 -0.1008 -0.0173 -0.1050 101 ALA B CB  
2032 N  N   . ILE B 19  ? 0.9601 0.7802 0.7466 -0.1114 -0.0204 -0.1112 102 ILE B N   
2033 C  CA  . ILE B 19  ? 0.9279 0.7467 0.7037 -0.1034 -0.0354 -0.1244 102 ILE B CA  
2034 C  C   . ILE B 19  ? 0.8785 0.6864 0.6418 -0.0744 -0.0606 -0.1332 102 ILE B C   
2035 O  O   . ILE B 19  ? 1.0937 0.9150 0.8803 -0.0595 -0.0714 -0.1544 102 ILE B O   
2036 C  CB  . ILE B 19  ? 0.9525 0.7899 0.7691 -0.1113 -0.0267 -0.1552 102 ILE B CB  
2037 C  CG1 . ILE B 19  ? 0.8681 0.7150 0.6866 -0.1346 0.0044  -0.1411 102 ILE B CG1 
2038 C  CG2 . ILE B 19  ? 0.9417 0.7754 0.7503 -0.1017 -0.0403 -0.1683 102 ILE B CG2 
2039 C  CD1 . ILE B 19  ? 0.8727 0.7369 0.7351 -0.1453 0.0223  -0.1708 102 ILE B CD1 
2040 N  N   . ALA B 20  ? 1.2312 0.8698 1.1822 -0.4211 0.0471  0.4146  103 ALA B N   
2041 C  CA  . ALA B 20  ? 1.3167 0.8272 1.1955 -0.4115 0.0728  0.3994  103 ALA B CA  
2042 C  C   . ALA B 20  ? 1.8548 1.4038 1.6654 -0.4132 0.0289  0.4688  103 ALA B C   
2043 O  O   . ALA B 20  ? 1.8508 1.3980 1.6268 -0.4269 0.0131  0.4706  103 ALA B O   
2044 C  CB  . ALA B 20  ? 1.3593 0.7512 1.2316 -0.3875 0.1185  0.3647  103 ALA B CB  
2045 N  N   . ASN B 21  ? 1.7657 1.3683 1.5745 -0.3821 0.0064  0.5166  104 ASN B N   
2046 C  CA  . ASN B 21  ? 1.7672 1.4437 1.5371 -0.3503 -0.0417 0.5610  104 ASN B CA  
2047 C  C   . ASN B 21  ? 1.9261 1.4094 1.5723 -0.3692 -0.0429 0.5754  104 ASN B C   
2048 O  O   . ASN B 21  ? 1.9855 1.4970 1.5847 -0.3763 -0.0842 0.6161  104 ASN B O   
2049 C  CB  . ASN B 21  ? 1.6392 1.4970 1.4416 -0.3887 -0.0863 0.6118  104 ASN B CB  
2050 C  CG  . ASN B 21  ? 1.4452 1.5148 1.3502 -0.3694 -0.0957 0.6033  104 ASN B CG  
2051 O  OD1 . ASN B 21  ? 1.4307 1.5974 1.3623 -0.4284 -0.1137 0.6298  104 ASN B OD1 
2052 N  ND2 . ASN B 21  ? 1.3216 1.4590 1.2776 -0.2911 -0.0872 0.5655  104 ASN B ND2 
2053 N  N   . ASN B 22  ? 2.0769 1.3828 1.6791 -0.3675 0.0072  0.5219  105 ASN B N   
2054 C  CA  . ASN B 22  ? 2.4073 1.5756 1.9212 -0.3655 0.0166  0.5015  105 ASN B CA  
2055 C  C   . ASN B 22  ? 2.6521 1.7087 2.0628 -0.3238 -0.0273 0.5385  105 ASN B C   
2056 O  O   . ASN B 22  ? 2.7114 1.6261 2.0520 -0.3192 -0.0101 0.5051  105 ASN B O   
2057 C  CB  . ASN B 22  ? 2.4446 1.5436 1.9932 -0.3799 0.0771  0.4233  105 ASN B CB  
2058 C  CG  . ASN B 22  ? 2.3544 1.5329 1.9797 -0.4076 0.0932  0.3892  105 ASN B CG  
2059 O  OD1 . ASN B 22  ? 2.2196 1.4832 1.9269 -0.4098 0.0982  0.3784  105 ASN B OD1 
2060 N  ND2 . ASN B 22  ? 2.3997 1.5410 1.9888 -0.4280 0.0948  0.3713  105 ASN B ND2 
2061 N  N   . GLY B 23  ? 2.7334 1.9523 2.2052 -0.2551 -0.0806 0.5609  106 GLY B N   
2062 C  CA  . GLY B 23  ? 2.9058 2.0995 2.3507 -0.1658 -0.1274 0.5508  106 GLY B CA  
2063 C  C   . GLY B 23  ? 3.0025 2.0479 2.4230 -0.1393 -0.0876 0.5004  106 GLY B C   
2064 O  O   . GLY B 23  ? 3.2487 2.1273 2.5688 -0.1076 -0.1148 0.4949  106 GLY B O   
2065 N  N   . LYS B 24  ? 2.7521 1.8512 2.2600 -0.1550 -0.0273 0.4630  107 LYS B N   
2066 C  CA  . LYS B 24  ? 2.6496 1.6170 2.1435 -0.1418 0.0215  0.4103  107 LYS B CA  
2067 C  C   . LYS B 24  ? 2.6321 1.7033 2.2053 -0.0352 -0.0058 0.3806  107 LYS B C   
2068 O  O   . LYS B 24  ? 2.6952 1.8236 2.2644 0.0338  -0.0744 0.3951  107 LYS B O   
2069 C  CB  . LYS B 24  ? 2.3932 1.3745 1.9539 -0.2017 0.0931  0.3749  107 LYS B CB  
2070 C  CG  . LYS B 24  ? 2.0887 1.3058 1.7871 -0.1964 0.0847  0.3844  107 LYS B CG  
2071 C  CD  . LYS B 24  ? 1.9083 1.1374 1.6900 -0.2153 0.1411  0.3323  107 LYS B CD  
2072 C  CE  . LYS B 24  ? 1.6291 1.0651 1.5234 -0.2229 0.1230  0.3475  107 LYS B CE  
2073 N  NZ  . LYS B 24  ? 1.4071 0.8263 1.3695 -0.2524 0.1661  0.2988  107 LYS B NZ  
2074 N  N   . GLY B 25  ? 2.4971 1.5937 2.1466 -0.0192 0.0445  0.3323  108 GLY B N   
2075 C  CA  . GLY B 25  ? 2.3587 1.5869 2.1068 0.0774  0.0266  0.2981  108 GLY B CA  
2076 C  C   . GLY B 25  ? 2.0938 1.5393 1.9865 0.0740  0.0561  0.2826  108 GLY B C   
2077 O  O   . GLY B 25  ? 1.9902 1.3997 1.8991 0.0086  0.1078  0.2717  108 GLY B O   
2078 N  N   . HIS B 26  ? 1.9762 1.6438 1.9690 0.1419  0.0177  0.2770  109 HIS B N   
2079 C  CA  . HIS B 26  ? 1.6839 1.5671 1.7995 0.1329  0.0366  0.2668  109 HIS B CA  
2080 C  C   . HIS B 26  ? 1.5729 1.4607 1.7569 0.1819  0.0746  0.2093  109 HIS B C   
2081 O  O   . HIS B 26  ? 1.7351 1.4256 1.8622 0.1904  0.1053  0.1807  109 HIS B O   
2082 C  CB  . HIS B 26  ? 1.5627 1.7007 1.7468 0.1655  -0.0182 0.2844  109 HIS B CB  
2083 C  CG  . HIS B 26  ? 1.6432 1.7483 1.7530 0.1680  -0.0731 0.3221  109 HIS B CG  
2084 N  ND1 . HIS B 26  ? 1.6974 1.6811 1.7164 0.0883  -0.0711 0.3712  109 HIS B ND1 
2085 C  CD2 . HIS B 26  ? 1.6927 1.8640 1.8067 0.2435  -0.1359 0.3125  109 HIS B CD2 
2086 C  CE1 . HIS B 26  ? 1.7798 1.7543 1.7447 0.1115  -0.1278 0.3961  109 HIS B CE1 
2087 N  NE2 . HIS B 26  ? 1.7904 1.8763 1.8127 0.2072  -0.1710 0.3598  109 HIS B NE2 
2088 N  N   . SER B 27  ? 1.3484 1.4584 1.6468 0.2068  0.0740  0.1914  110 SER B N   
2089 C  CA  . SER B 27  ? 1.2284 1.3725 1.6031 0.2552  0.1073  0.1367  110 SER B CA  
2090 C  C   . SER B 27  ? 1.1119 1.1126 1.4783 0.2003  0.1678  0.1171  110 SER B C   
2091 O  O   . SER B 27  ? 1.1644 0.9542 1.4443 0.1576  0.1930  0.1189  110 SER B O   
2092 C  CB  . SER B 27  ? 1.3447 1.4068 1.7027 0.3479  0.0900  0.0981  110 SER B CB  
2093 O  OG  . SER B 27  ? 1.1569 1.2055 1.5726 0.3860  0.1300  0.0453  110 SER B OG  
2094 N  N   . MSE B 28  ? 1.0461 1.1640 1.5029 0.2003  0.1897  0.0913  111 MSE B N   
2095 C  CA  . MSE B 28  ? 1.0100 1.0223 1.4789 0.1509  0.2362  0.0658  111 MSE B CA  
2096 C  C   . MSE B 28  ? 1.1064 0.9725 1.5757 0.1917  0.2836  0.0054  111 MSE B C   
2097 O  O   . MSE B 28  ? 1.1059 0.8716 1.5862 0.1550  0.3252  -0.0291 111 MSE B O   
2098 C  CB  . MSE B 28  ? 0.8578 1.0478 1.4134 0.1288  0.2288  0.0667  111 MSE B CB  
2099 C  CG  . MSE B 28  ? 0.9003 1.2842 1.5373 0.1986  0.2191  0.0422  111 MSE B CG  
2100 SE SE  . MSE B 28  ? 0.9446 1.5808 1.6565 0.1464  0.1953  0.0615  111 MSE B SE  
2101 C  CE  . MSE B 28  ? 0.6606 1.1018 1.3450 0.0600  0.2115  0.0628  111 MSE B CE  
2102 N  N   . SER B 29  ? 1.2683 1.1219 1.7273 0.2679  0.2727  -0.0127 112 SER B N   
2103 C  CA  . SER B 29  ? 1.3866 1.1367 1.8576 0.3143  0.3111  -0.0705 112 SER B CA  
2104 C  C   . SER B 29  ? 1.5240 1.0276 1.8759 0.3081  0.3257  -0.0800 112 SER B C   
2105 O  O   . SER B 29  ? 1.6271 1.0393 1.9584 0.3190  0.3484  -0.1247 112 SER B O   
2106 C  CB  . SER B 29  ? 1.4803 1.3950 2.0343 0.4093  0.2861  -0.0963 112 SER B CB  
2107 O  OG  . SER B 29  ? 1.4603 1.5978 2.1169 0.4039  0.2821  -0.0960 112 SER B OG  
2108 N  N   . ASP B 30  ? 1.5600 0.9732 1.8105 0.2735  0.2967  -0.0354 113 ASP B N   
2109 C  CA  . ASP B 30  ? 1.6164 0.7839 1.7321 0.2551  0.3057  -0.0405 113 ASP B CA  
2110 C  C   . ASP B 30  ? 1.5152 0.5586 1.5898 0.1681  0.3654  -0.0759 113 ASP B C   
2111 O  O   . ASP B 30  ? 1.3754 0.4927 1.5055 0.1150  0.3889  -0.0824 113 ASP B O   
2112 C  CB  . ASP B 30  ? 1.7703 0.8769 1.7808 0.2285  0.2554  0.0176  113 ASP B CB  
2113 C  CG  . ASP B 30  ? 1.8378 1.1540 1.9127 0.2897  0.1860  0.0512  113 ASP B CG  
2114 O  OD1 . ASP B 30  ? 1.8298 1.2694 1.9841 0.3774  0.1593  0.0241  113 ASP B OD1 
2115 O  OD2 . ASP B 30  ? 1.8932 1.2565 1.9412 0.2481  0.1585  0.0993  113 ASP B OD2 
2116 N  N   . LEU B 31  ? 1.1965 0.7628 0.9852 0.0490  0.1866  -0.2150 114 LEU B N   
2117 C  CA  . LEU B 31  ? 1.1805 0.7675 0.9678 0.0163  0.1447  -0.2206 114 LEU B CA  
2118 C  C   . LEU B 31  ? 1.1270 0.7848 0.9681 0.0147  0.1213  -0.1873 114 LEU B C   
2119 O  O   . LEU B 31  ? 1.1267 0.8179 0.9560 -0.0048 0.0917  -0.1875 114 LEU B O   
2120 C  CB  . LEU B 31  ? 1.2002 0.7425 1.0025 0.0023  0.1403  -0.2317 114 LEU B CB  
2121 C  CG  . LEU B 31  ? 1.1622 0.7179 0.9618 -0.0331 0.1009  -0.2393 114 LEU B CG  
2122 C  CD1 . LEU B 31  ? 1.2111 0.7499 0.9367 -0.0563 0.0855  -0.2711 114 LEU B CD1 
2123 C  CD2 . LEU B 31  ? 1.2377 0.7525 1.0666 -0.0428 0.1017  -0.2418 114 LEU B CD2 
2124 N  N   . SER B 32  ? 1.0863 0.7669 0.9859 0.0348  0.1340  -0.1579 115 SER B N   
2125 C  CA  . SER B 32  ? 0.9498 0.6893 0.8927 0.0323  0.1126  -0.1292 115 SER B CA  
2126 C  C   . SER B 32  ? 0.9307 0.7051 0.8480 0.0323  0.1064  -0.1260 115 SER B C   
2127 O  O   . SER B 32  ? 0.8530 0.6620 0.7738 0.0187  0.0805  -0.1185 115 SER B O   
2128 C  CB  . SER B 32  ? 1.0373 0.7934 1.0419 0.0520  0.1267  -0.0988 115 SER B CB  
2129 O  OG  . SER B 32  ? 1.1444 0.9388 1.1878 0.0421  0.1007  -0.0772 115 SER B OG  
2130 N  N   . ALA B 33  ? 1.0093 0.7738 0.9008 0.0493  0.1326  -0.1298 116 ALA B N   
2131 C  CA  . ALA B 33  ? 0.8956 0.6937 0.7663 0.0518  0.1301  -0.1218 116 ALA B CA  
2132 C  C   . ALA B 33  ? 0.9593 0.7537 0.7685 0.0330  0.1108  -0.1446 116 ALA B C   
2133 O  O   . ALA B 33  ? 0.9555 0.7883 0.7630 0.0249  0.0907  -0.1335 116 ALA B O   
2134 C  CB  . ALA B 33  ? 0.9013 0.6927 0.7656 0.0773  0.1670  -0.1148 116 ALA B CB  
2135 N  N   . ARG B 34  ? 1.0172 0.7647 0.7754 0.0251  0.1162  -0.1754 117 ARG B N   
2136 C  CA  . ARG B 34  ? 1.0155 0.7619 0.7133 0.0037  0.0941  -0.1963 117 ARG B CA  
2137 C  C   . ARG B 34  ? 1.0003 0.7789 0.7238 -0.0202 0.0563  -0.1894 117 ARG B C   
2138 O  O   . ARG B 34  ? 1.0052 0.8174 0.7081 -0.0321 0.0343  -0.1857 117 ARG B O   
2139 C  CB  . ARG B 34  ? 1.0988 0.7807 0.7349 -0.0040 0.1054  -0.2333 117 ARG B CB  
2140 C  CG  . ARG B 34  ? 1.2524 0.8939 0.8618 0.0239  0.1499  -0.2411 117 ARG B CG  
2141 C  CD  . ARG B 34  ? 1.3411 0.9151 0.8646 0.0147  0.1601  -0.2827 117 ARG B CD  
2142 N  NE  . ARG B 34  ? 1.4067 0.9550 0.9177 -0.0188 0.1291  -0.3055 117 ARG B NE  
2143 C  CZ  . ARG B 34  ? 1.4665 0.9695 1.0035 -0.0227 0.1357  -0.3154 117 ARG B CZ  
2144 N  NH1 . ARG B 34  ? 1.4476 0.9276 1.0246 0.0065  0.1720  -0.3037 117 ARG B NH1 
2145 N  NH2 . ARG B 34  ? 1.5966 1.0801 1.1239 -0.0561 0.1060  -0.3336 117 ARG B NH2 
2146 N  N   . TYR B 35  ? 0.9649 0.7362 0.7351 -0.0257 0.0502  -0.1843 118 TYR B N   
2147 C  CA  . TYR B 35  ? 0.9114 0.7146 0.7090 -0.0452 0.0192  -0.1745 118 TYR B CA  
2148 C  C   . TYR B 35  ? 0.9281 0.7838 0.7584 -0.0363 0.0109  -0.1456 118 TYR B C   
2149 O  O   . TYR B 35  ? 0.9327 0.8220 0.7639 -0.0482 -0.0115 -0.1377 118 TYR B O   
2150 C  CB  . TYR B 35  ? 0.9348 0.7166 0.7726 -0.0510 0.0181  -0.1733 118 TYR B CB  
2151 C  CG  . TYR B 35  ? 0.9025 0.7162 0.7681 -0.0695 -0.0096 -0.1618 118 TYR B CG  
2152 C  CD1 . TYR B 35  ? 0.8292 0.6729 0.7424 -0.0615 -0.0132 -0.1361 118 TYR B CD1 
2153 C  CD2 . TYR B 35  ? 0.9334 0.7478 0.7763 -0.0955 -0.0318 -0.1755 118 TYR B CD2 
2154 C  CE1 . TYR B 35  ? 0.8541 0.7254 0.7897 -0.0751 -0.0334 -0.1245 118 TYR B CE1 
2155 C  CE2 . TYR B 35  ? 0.8960 0.7445 0.7704 -0.1104 -0.0538 -0.1606 118 TYR B CE2 
2156 C  CZ  . TYR B 35  ? 0.8887 0.7644 0.8084 -0.0982 -0.0521 -0.1352 118 TYR B CZ  
2157 O  OH  . TYR B 35  ? 0.8377 0.7456 0.7859 -0.1097 -0.0691 -0.1195 118 TYR B OH  
2158 N  N   . GLN B 36  ? 0.9015 0.7637 0.7607 -0.0159 0.0291  -0.1284 119 GLN B N   
2159 C  CA  . GLN B 36  ? 0.8630 0.7657 0.7496 -0.0096 0.0220  -0.1034 119 GLN B CA  
2160 C  C   . GLN B 36  ? 0.8963 0.8222 0.7490 -0.0086 0.0181  -0.1007 119 GLN B C   
2161 O  O   . GLN B 36  ? 0.8624 0.8195 0.7248 -0.0124 0.0025  -0.0863 119 GLN B O   
2162 C  CB  . GLN B 36  ? 0.8797 0.7836 0.8038 0.0079  0.0401  -0.0858 119 GLN B CB  
2163 C  CG  . GLN B 36  ? 0.7857 0.7204 0.7430 0.0092  0.0293  -0.0621 119 GLN B CG  
2164 C  CD  . GLN B 36  ? 0.8138 0.7477 0.8163 0.0160  0.0352  -0.0463 119 GLN B CD  
2165 O  OE1 . GLN B 36  ? 0.8915 0.8115 0.9118 0.0128  0.0325  -0.0484 119 GLN B OE1 
2166 N  NE2 . GLN B 36  ? 0.8567 0.8075 0.8800 0.0241  0.0418  -0.0278 119 GLN B NE2 
2167 N  N   . GLN B 37  ? 0.9471 0.8569 0.7579 -0.0020 0.0341  -0.1129 120 GLN B N   
2168 C  CA  . GLN B 37  ? 0.8670 0.8002 0.6427 0.0002  0.0315  -0.1072 120 GLN B CA  
2169 C  C   . GLN B 37  ? 0.8909 0.8414 0.6395 -0.0196 0.0034  -0.1143 120 GLN B C   
2170 O  O   . GLN B 37  ? 0.9694 0.9549 0.7126 -0.0189 -0.0074 -0.0979 120 GLN B O   
2171 C  CB  . GLN B 37  ? 0.8242 0.7335 0.5545 0.0127  0.0576  -0.1190 120 GLN B CB  
2172 C  CG  . GLN B 37  ? 0.8460 0.7802 0.5376 0.0177  0.0584  -0.1094 120 GLN B CG  
2173 C  CD  . GLN B 37  ? 0.9919 0.9093 0.6552 0.0378  0.0927  -0.1098 120 GLN B CD  
2174 O  OE1 . GLN B 37  ? 1.0512 0.9552 0.7489 0.0531  0.1173  -0.1031 120 GLN B OE1 
2175 N  NE2 . GLN B 37  ? 1.0709 0.9915 0.6716 0.0384  0.0950  -0.1151 120 GLN B NE2 
2176 N  N   . TRP B 38  ? 0.9301 0.8583 0.6663 -0.0378 -0.0091 -0.1356 121 TRP B N   
2177 C  CA  . TRP B 38  ? 0.9694 0.9186 0.6859 -0.0604 -0.0386 -0.1402 121 TRP B CA  
2178 C  C   . TRP B 38  ? 0.8762 0.8654 0.6436 -0.0642 -0.0566 -0.1166 121 TRP B C   
2179 O  O   . TRP B 38  ? 0.9160 0.9431 0.6793 -0.0727 -0.0767 -0.1047 121 TRP B O   
2180 C  CB  . TRP B 38  ? 1.0287 0.9374 0.7187 -0.0817 -0.0462 -0.1702 121 TRP B CB  
2181 C  CG  . TRP B 38  ? 1.0846 1.0155 0.7633 -0.1105 -0.0801 -0.1742 121 TRP B CG  
2182 C  CD1 . TRP B 38  ? 1.1955 1.1390 0.8210 -0.1264 -0.0989 -0.1829 121 TRP B CD1 
2183 C  CD2 . TRP B 38  ? 1.0608 1.0077 0.7846 -0.1279 -0.0998 -0.1666 121 TRP B CD2 
2184 N  NE1 . TRP B 38  ? 1.1477 1.1175 0.7876 -0.1543 -0.1316 -0.1801 121 TRP B NE1 
2185 C  CE2 . TRP B 38  ? 1.0411 1.0133 0.7429 -0.1549 -0.1308 -0.1696 121 TRP B CE2 
2186 C  CE3 . TRP B 38  ? 1.0304 0.9750 0.8105 -0.1236 -0.0944 -0.1555 121 TRP B CE3 
2187 C  CZ2 . TRP B 38  ? 0.9409 0.9385 0.6823 -0.1769 -0.1545 -0.1600 121 TRP B CZ2 
2188 C  CZ3 . TRP B 38  ? 0.9377 0.9038 0.7505 -0.1438 -0.1157 -0.1474 121 TRP B CZ3 
2189 C  CH2 . TRP B 38  ? 0.8948 0.8880 0.6915 -0.1699 -0.1446 -0.1489 121 TRP B CH2 
2190 N  N   . VAL B 39  ? 0.8135 0.7954 0.6275 -0.0570 -0.0489 -0.1081 122 VAL B N   
2191 C  CA  . VAL B 39  ? 0.8496 0.8629 0.7053 -0.0576 -0.0608 -0.0869 122 VAL B CA  
2192 C  C   . VAL B 39  ? 0.9292 0.9685 0.7950 -0.0403 -0.0548 -0.0638 122 VAL B C   
2193 O  O   . VAL B 39  ? 0.8724 0.9443 0.7504 -0.0402 -0.0661 -0.0464 122 VAL B O   
2194 C  CB  . VAL B 39  ? 0.8684 0.8618 0.7615 -0.0568 -0.0551 -0.0864 122 VAL B CB  
2195 C  CG1 . VAL B 39  ? 0.7164 0.7365 0.6444 -0.0525 -0.0613 -0.0644 122 VAL B CG1 
2196 C  CG2 . VAL B 39  ? 1.0029 0.9723 0.8917 -0.0758 -0.0628 -0.1050 122 VAL B CG2 
2197 N  N   . THR B 40  ? 1.0143 1.0393 0.8780 -0.0252 -0.0357 -0.0614 123 THR B N   
2198 C  CA  . THR B 40  ? 0.9458 0.9873 0.8248 -0.0109 -0.0287 -0.0394 123 THR B CA  
2199 C  C   . THR B 40  ? 0.9543 1.0133 0.8032 -0.0042 -0.0253 -0.0313 123 THR B C   
2200 O  O   . THR B 40  ? 0.9303 1.0073 0.7913 0.0052  -0.0237 -0.0101 123 THR B O   
2201 C  CB  . THR B 40  ? 0.8745 0.8960 0.7774 -0.0009 -0.0122 -0.0357 123 THR B CB  
2202 O  OG1 . THR B 40  ? 0.9933 0.9989 0.8761 0.0051  0.0045  -0.0453 123 THR B OG1 
2203 C  CG2 . THR B 40  ? 0.9075 0.9133 0.8376 -0.0068 -0.0162 -0.0410 123 THR B CG2 
2204 N  N   . ASN B 41  ? 0.9685 1.0189 0.7754 -0.0083 -0.0228 -0.0472 124 ASN B N   
2205 C  CA  . ASN B 41  ? 0.9884 1.0520 0.7591 -0.0002 -0.0158 -0.0394 124 ASN B CA  
2206 C  C   . ASN B 41  ? 0.9445 1.0040 0.7334 0.0179  0.0076  -0.0229 124 ASN B C   
2207 O  O   . ASN B 41  ? 0.8684 0.9462 0.6453 0.0272  0.0137  -0.0048 124 ASN B O   
2208 C  CB  . ASN B 41  ? 1.0113 1.1146 0.7755 -0.0036 -0.0349 -0.0213 124 ASN B CB  
2209 C  CG  . ASN B 41  ? 1.2182 1.3313 0.9349 -0.0202 -0.0537 -0.0358 124 ASN B CG  
2210 O  OD1 . ASN B 41  ? 1.3322 1.4394 0.9984 -0.0187 -0.0475 -0.0434 124 ASN B OD1 
2211 N  ND2 . ASN B 41  ? 1.3365 1.4644 1.0674 -0.0375 -0.0772 -0.0391 124 ASN B ND2 
2212 N  N   . PHE B 42  ? 0.8761 0.9143 0.6976 0.0218  0.0198  -0.0260 125 PHE B N   
2213 C  CA  . PHE B 42  ? 0.8217 0.8568 0.6664 0.0351  0.0407  -0.0104 125 PHE B CA  
2214 C  C   . PHE B 42  ? 0.8480 0.8643 0.6687 0.0435  0.0637  -0.0222 125 PHE B C   
2215 O  O   . PHE B 42  ? 0.9154 0.9072 0.7267 0.0392  0.0656  -0.0438 125 PHE B O   
2216 C  CB  . PHE B 42  ? 0.8667 0.8939 0.7624 0.0333  0.0383  -0.0036 125 PHE B CB  
2217 C  CG  . PHE B 42  ? 0.8598 0.8992 0.7794 0.0324  0.0284  0.0153  125 PHE B CG  
2218 C  CD1 . PHE B 42  ? 0.8316 0.8860 0.7378 0.0297  0.0144  0.0192  125 PHE B CD1 
2219 C  CD2 . PHE B 42  ? 0.7882 0.8223 0.7439 0.0339  0.0333  0.0298  125 PHE B CD2 
2220 C  CE1 . PHE B 42  ? 0.7128 0.7710 0.6387 0.0322  0.0101  0.0360  125 PHE B CE1 
2221 C  CE2 . PHE B 42  ? 0.7145 0.7489 0.6848 0.0321  0.0255  0.0434  125 PHE B CE2 
2222 C  CZ  . PHE B 42  ? 0.6694 0.7128 0.6234 0.0331  0.0163  0.0459  125 PHE B CZ  
2223 N  N   . PRO B 43  ? 0.8205 0.8447 0.6303 0.0567  0.0842  -0.0079 126 PRO B N   
2224 C  CA  . PRO B 43  ? 0.8429 0.8476 0.6315 0.0689  0.1125  -0.0170 126 PRO B CA  
2225 C  C   . PRO B 43  ? 0.8054 0.7980 0.6469 0.0745  0.1255  -0.0130 126 PRO B C   
2226 O  O   . PRO B 43  ? 0.7925 0.8007 0.6874 0.0737  0.1215  0.0085  126 PRO B O   
2227 C  CB  . PRO B 43  ? 0.8115 0.8356 0.5868 0.0825  0.1315  0.0059  126 PRO B CB  
2228 C  CG  . PRO B 43  ? 0.8004 0.8496 0.6147 0.0779  0.1158  0.0313  126 PRO B CG  
2229 C  CD  . PRO B 43  ? 0.7492 0.7989 0.5634 0.0625  0.0852  0.0185  126 PRO B CD  
2230 N  N   . PHE B 44  ? 0.8381 0.8012 0.6634 0.0791  0.1400  -0.0334 127 PHE B N   
2231 C  CA  . PHE B 44  ? 0.7579 0.7121 0.6341 0.0880  0.1557  -0.0259 127 PHE B CA  
2232 C  C   . PHE B 44  ? 0.9158 0.8909 0.8252 0.1050  0.1822  0.0033  127 PHE B C   
2233 O  O   . PHE B 44  ? 0.9664 0.9443 0.8396 0.1167  0.2032  0.0068  127 PHE B O   
2234 C  CB  . PHE B 44  ? 0.8096 0.7223 0.6561 0.0936  0.1721  -0.0526 127 PHE B CB  
2235 C  CG  . PHE B 44  ? 0.7973 0.7013 0.6986 0.1052  0.1892  -0.0424 127 PHE B CG  
2236 C  CD1 . PHE B 44  ? 0.8275 0.7289 0.7430 0.1288  0.2270  -0.0291 127 PHE B CD1 
2237 C  CD2 . PHE B 44  ? 0.8421 0.7433 0.7823 0.0939  0.1687  -0.0427 127 PHE B CD2 
2238 C  CE1 . PHE B 44  ? 0.8167 0.7160 0.7896 0.1410  0.2425  -0.0145 127 PHE B CE1 
2239 C  CE2 . PHE B 44  ? 0.8343 0.7317 0.8265 0.1049  0.1825  -0.0291 127 PHE B CE2 
2240 C  CZ  . PHE B 44  ? 0.8996 0.7976 0.9108 0.1285  0.2187  -0.0141 127 PHE B CZ  
2241 N  N   . PRO B 45  ? 0.8344 0.8268 0.8129 0.1055  0.1813  0.0267  128 PRO B N   
2242 C  CA  . PRO B 45  ? 0.8532 0.8452 0.8735 0.0925  0.1572  0.0269  128 PRO B CA  
2243 C  C   . PRO B 45  ? 0.7918 0.8053 0.8378 0.0764  0.1294  0.0419  128 PRO B C   
2244 O  O   . PRO B 45  ? 0.7924 0.8157 0.8871 0.0692  0.1173  0.0565  128 PRO B O   
2245 C  CB  . PRO B 45  ? 0.9414 0.9404 1.0174 0.1057  0.1779  0.0467  128 PRO B CB  
2246 C  CG  . PRO B 45  ? 0.8946 0.9182 0.9857 0.1177  0.2011  0.0722  128 PRO B CG  
2247 C  CD  . PRO B 45  ? 0.8554 0.8696 0.8767 0.1208  0.2083  0.0570  128 PRO B CD  
2248 N  N   . HIS B 46  ? 0.7403 0.7593 0.7521 0.0712  0.1197  0.0392  129 HIS B N   
2249 C  CA  . HIS B 46  ? 0.6654 0.6973 0.6972 0.0593  0.0991  0.0535  129 HIS B CA  
2250 C  C   . HIS B 46  ? 0.7152 0.7367 0.7424 0.0458  0.0726  0.0388  129 HIS B C   
2251 O  O   . HIS B 46  ? 0.8025 0.8127 0.7980 0.0436  0.0668  0.0177  129 HIS B O   
2252 C  CB  . HIS B 46  ? 0.6369 0.6793 0.6385 0.0627  0.1026  0.0614  129 HIS B CB  
2253 C  CG  . HIS B 46  ? 0.7021 0.7566 0.7057 0.0767  0.1306  0.0792  129 HIS B CG  
2254 N  ND1 . HIS B 46  ? 0.7370 0.8075 0.7839 0.0763  0.1374  0.1083  129 HIS B ND1 
2255 C  CD2 . HIS B 46  ? 0.8034 0.8548 0.7693 0.0912  0.1549  0.0726  129 HIS B CD2 
2256 C  CE1 . HIS B 46  ? 0.8214 0.9030 0.8627 0.0913  0.1661  0.1220  129 HIS B CE1 
2257 N  NE2 . HIS B 46  ? 0.8390 0.9079 0.8276 0.1018  0.1783  0.0999  129 HIS B NE2 
2258 N  N   . GLU B 47  ? 0.7503 0.7743 0.8083 0.0356  0.0568  0.0504  130 GLU B N   
2259 C  CA  . GLU B 47  ? 0.7371 0.7514 0.7882 0.0247  0.0348  0.0401  130 GLU B CA  
2260 C  C   . GLU B 47  ? 0.7253 0.7389 0.7801 0.0186  0.0249  0.0522  130 GLU B C   
2261 O  O   . GLU B 47  ? 0.7008 0.7213 0.7615 0.0220  0.0343  0.0675  130 GLU B O   
2262 C  CB  . GLU B 47  ? 0.6343 0.6420 0.7124 0.0187  0.0263  0.0381  130 GLU B CB  
2263 C  CG  . GLU B 47  ? 0.6017 0.6017 0.6750 0.0257  0.0372  0.0250  130 GLU B CG  
2264 C  CD  . GLU B 47  ? 0.6237 0.6200 0.7296 0.0223  0.0309  0.0293  130 GLU B CD  
2265 O  OE1 . GLU B 47  ? 0.6412 0.6416 0.7658 0.0121  0.0138  0.0395  130 GLU B OE1 
2266 O  OE2 . GLU B 47  ? 0.6728 0.6597 0.7830 0.0301  0.0434  0.0228  130 GLU B OE2 
2267 N  N   . TRP B 48  ? 0.7145 0.7163 0.7643 0.0106  0.0087  0.0461  131 TRP B N   
2268 C  CA  . TRP B 48  ? 0.6627 0.6536 0.7082 0.0067  0.0021  0.0538  131 TRP B CA  
2269 C  C   . TRP B 48  ? 0.7053 0.6802 0.7694 -0.0064 -0.0108 0.0570  131 TRP B C   
2270 O  O   . TRP B 48  ? 0.7770 0.7465 0.8407 -0.0116 -0.0211 0.0481  131 TRP B O   
2271 C  CB  . TRP B 48  ? 0.6722 0.6605 0.6908 0.0106  -0.0030 0.0453  131 TRP B CB  
2272 C  CG  . TRP B 48  ? 0.7697 0.7447 0.7811 0.0129  -0.0026 0.0548  131 TRP B CG  
2273 C  CD1 . TRP B 48  ? 0.7284 0.6804 0.7318 0.0099  -0.0091 0.0517  131 TRP B CD1 
2274 C  CD2 . TRP B 48  ? 0.7898 0.7691 0.7990 0.0205  0.0076  0.0700  131 TRP B CD2 
2275 N  NE1 . TRP B 48  ? 0.6521 0.5900 0.6490 0.0159  -0.0022 0.0626  131 TRP B NE1 
2276 C  CE2 . TRP B 48  ? 0.7525 0.7084 0.7555 0.0221  0.0072  0.0754  131 TRP B CE2 
2277 C  CE3 . TRP B 48  ? 0.8197 0.8186 0.8292 0.0273  0.0192  0.0806  131 TRP B CE3 
2278 C  CZ2 . TRP B 48  ? 0.7759 0.7270 0.7781 0.0302  0.0174  0.0924  131 TRP B CZ2 
2279 C  CZ3 . TRP B 48  ? 0.7490 0.7475 0.7564 0.0346  0.0279  0.0988  131 TRP B CZ3 
2280 C  CH2 . TRP B 48  ? 0.6890 0.6637 0.6955 0.0359  0.0266  0.1053  131 TRP B CH2 
2281 N  N   . PHE B 49  ? 0.7031 0.6697 0.7816 -0.0135 -0.0115 0.0705  132 PHE B N   
2282 C  CA  . PHE B 49  ? 0.7080 0.6571 0.7994 -0.0307 -0.0275 0.0737  132 PHE B CA  
2283 C  C   . PHE B 49  ? 0.8201 0.7353 0.8855 -0.0349 -0.0316 0.0702  132 PHE B C   
2284 O  O   . PHE B 49  ? 0.9289 0.8360 0.9955 -0.0326 -0.0227 0.0804  132 PHE B O   
2285 C  CB  . PHE B 49  ? 0.6309 0.5950 0.7636 -0.0398 -0.0269 0.0931  132 PHE B CB  
2286 C  CG  . PHE B 49  ? 0.6238 0.5793 0.7745 -0.0613 -0.0486 0.0978  132 PHE B CG  
2287 C  CD1 . PHE B 49  ? 0.7193 0.6877 0.8820 -0.0647 -0.0596 0.0958  132 PHE B CD1 
2288 C  CD2 . PHE B 49  ? 0.7017 0.6351 0.8564 -0.0795 -0.0593 0.1052  132 PHE B CD2 
2289 C  CE1 . PHE B 49  ? 0.6841 0.6492 0.8613 -0.0859 -0.0831 0.1027  132 PHE B CE1 
2290 C  CE2 . PHE B 49  ? 0.8873 0.8126 1.0536 -0.1035 -0.0838 0.1088  132 PHE B CE2 
2291 C  CZ  . PHE B 49  ? 0.7274 0.6715 0.9044 -0.1066 -0.0967 0.1083  132 PHE B CZ  
2292 N  N   . TRP B 50  ? 0.7873 0.6803 0.8279 -0.0392 -0.0422 0.0570  133 TRP B N   
2293 C  CA  . TRP B 50  ? 0.7551 0.6077 0.7659 -0.0413 -0.0430 0.0515  133 TRP B CA  
2294 C  C   . TRP B 50  ? 0.7993 0.6264 0.7886 -0.0547 -0.0594 0.0399  133 TRP B C   
2295 O  O   . TRP B 50  ? 0.8037 0.6481 0.7938 -0.0541 -0.0658 0.0348  133 TRP B O   
2296 C  CB  . TRP B 50  ? 0.7234 0.5760 0.7121 -0.0209 -0.0282 0.0483  133 TRP B CB  
2297 C  CG  . TRP B 50  ? 0.8427 0.6508 0.7997 -0.0185 -0.0245 0.0425  133 TRP B CG  
2298 C  CD1 . TRP B 50  ? 0.9609 0.7331 0.9102 -0.0196 -0.0176 0.0481  133 TRP B CD1 
2299 C  CD2 . TRP B 50  ? 0.8677 0.6576 0.7949 -0.0133 -0.0243 0.0305  133 TRP B CD2 
2300 N  NE1 . TRP B 50  ? 1.0325 0.7612 0.9460 -0.0141 -0.0117 0.0382  133 TRP B NE1 
2301 C  CE2 . TRP B 50  ? 0.9306 0.6715 0.8296 -0.0094 -0.0151 0.0280  133 TRP B CE2 
2302 C  CE3 . TRP B 50  ? 0.8892 0.6978 0.8112 -0.0107 -0.0288 0.0231  133 TRP B CE3 
2303 C  CZ2 . TRP B 50  ? 0.9800 0.6909 0.8431 -0.0008 -0.0080 0.0179  133 TRP B CZ2 
2304 C  CZ3 . TRP B 50  ? 0.8979 0.6813 0.7881 -0.0039 -0.0235 0.0154  133 TRP B CZ3 
2305 C  CH2 . TRP B 50  ? 0.9597 0.6953 0.8195 0.0020  -0.0122 0.0126  133 TRP B CH2 
2306 N  N   . SER B 51  ? 0.8479 0.6306 0.8145 -0.0673 -0.0657 0.0358  134 SER B N   
2307 C  CA  . SER B 51  ? 0.8450 0.5953 0.7785 -0.0821 -0.0821 0.0233  134 SER B CA  
2308 C  C   . SER B 51  ? 0.8525 0.6305 0.8111 -0.0999 -0.1041 0.0292  134 SER B C   
2309 O  O   . SER B 51  ? 0.9679 0.7398 0.9039 -0.1059 -0.1166 0.0218  134 SER B O   
2310 C  CB  . SER B 51  ? 0.8597 0.5985 0.7559 -0.0652 -0.0719 0.0110  134 SER B CB  
2311 O  OG  . SER B 51  ? 0.8807 0.5760 0.7313 -0.0771 -0.0824 -0.0020 134 SER B OG  
2312 N  N   . GLY B 52  ? 0.8155 0.6261 0.8226 -0.1067 -0.1073 0.0456  135 GLY B N   
2313 C  CA  . GLY B 52  ? 0.7723 0.6138 0.8139 -0.1219 -0.1263 0.0576  135 GLY B CA  
2314 C  C   . GLY B 52  ? 0.7905 0.6702 0.8512 -0.1071 -0.1212 0.0604  135 GLY B C   
2315 O  O   . GLY B 52  ? 0.8317 0.7385 0.9243 -0.1162 -0.1349 0.0734  135 GLY B O   
2316 N  N   . THR B 53  ? 0.7056 0.5886 0.7506 -0.0855 -0.1027 0.0505  136 THR B N   
2317 C  CA  . THR B 53  ? 0.8398 0.7509 0.8999 -0.0734 -0.0972 0.0508  136 THR B CA  
2318 C  C   . THR B 53  ? 0.8599 0.7918 0.9360 -0.0556 -0.0756 0.0515  136 THR B C   
2319 O  O   . THR B 53  ? 0.8430 0.7692 0.9123 -0.0501 -0.0647 0.0517  136 THR B O   
2320 C  CB  . THR B 53  ? 0.9694 0.8651 0.9928 -0.0681 -0.0984 0.0377  136 THR B CB  
2321 O  OG1 . THR B 53  ? 1.1098 0.9889 1.1048 -0.0558 -0.0837 0.0274  136 THR B OG1 
2322 C  CG2 . THR B 53  ? 1.0358 0.9078 1.0324 -0.0853 -0.1190 0.0359  136 THR B CG2 
2323 N  N   . TRP B 54  ? 0.8342 0.7876 0.9285 -0.0469 -0.0695 0.0522  137 TRP B N   
2324 C  CA  . TRP B 54  ? 0.6547 0.6234 0.7561 -0.0319 -0.0503 0.0497  137 TRP B CA  
2325 C  C   . TRP B 54  ? 0.5818 0.5451 0.6547 -0.0234 -0.0452 0.0342  137 TRP B C   
2326 O  O   . TRP B 54  ? 0.7052 0.6632 0.7708 -0.0257 -0.0522 0.0289  137 TRP B O   
2327 C  CB  . TRP B 54  ? 0.6132 0.6024 0.7508 -0.0269 -0.0434 0.0591  137 TRP B CB  
2328 C  CG  . TRP B 54  ? 0.5616 0.5673 0.7366 -0.0311 -0.0419 0.0791  137 TRP B CG  
2329 C  CD1 . TRP B 54  ? 0.5625 0.5805 0.7713 -0.0435 -0.0570 0.0966  137 TRP B CD1 
2330 C  CD2 . TRP B 54  ? 0.5114 0.5275 0.6969 -0.0238 -0.0248 0.0872  137 TRP B CD2 
2331 N  NE1 . TRP B 54  ? 0.5441 0.5815 0.7895 -0.0452 -0.0503 0.1161  137 TRP B NE1 
2332 C  CE2 . TRP B 54  ? 0.4913 0.5266 0.7222 -0.0322 -0.0287 0.1107  137 TRP B CE2 
2333 C  CE3 . TRP B 54  ? 0.5413 0.5554 0.7024 -0.0116 -0.0072 0.0793  137 TRP B CE3 
2334 C  CZ2 . TRP B 54  ? 0.4867 0.5381 0.7415 -0.0276 -0.0126 0.1270  137 TRP B CZ2 
2335 C  CZ3 . TRP B 54  ? 0.6533 0.6813 0.8316 -0.0063 0.0083  0.0944  137 TRP B CZ3 
2336 C  CH2 . TRP B 54  ? 0.5742 0.6201 0.8001 -0.0136 0.0071  0.1182  137 TRP B CH2 
2337 N  N   . TRP B 55  ? 0.5985 0.5660 0.6573 -0.0147 -0.0338 0.0298  138 TRP B N   
2338 C  CA  . TRP B 55  ? 0.6521 0.6224 0.6897 -0.0089 -0.0308 0.0184  138 TRP B CA  
2339 C  C   . TRP B 55  ? 0.7368 0.7200 0.7720 -0.0016 -0.0189 0.0141  138 TRP B C   
2340 O  O   . TRP B 55  ? 0.8204 0.8100 0.8590 0.0030  -0.0096 0.0215  138 TRP B O   
2341 C  CB  . TRP B 55  ? 0.6813 0.6450 0.6972 -0.0060 -0.0315 0.0190  138 TRP B CB  
2342 C  CG  . TRP B 55  ? 0.7013 0.6421 0.7103 -0.0120 -0.0386 0.0224  138 TRP B CG  
2343 C  CD1 . TRP B 55  ? 0.6912 0.6182 0.7056 -0.0183 -0.0409 0.0298  138 TRP B CD1 
2344 C  CD2 . TRP B 55  ? 0.7051 0.6304 0.6960 -0.0134 -0.0437 0.0177  138 TRP B CD2 
2345 N  NE1 . TRP B 55  ? 0.6253 0.5244 0.6208 -0.0254 -0.0490 0.0268  138 TRP B NE1 
2346 C  CE2 . TRP B 55  ? 0.6810 0.5784 0.6595 -0.0207 -0.0492 0.0194  138 TRP B CE2 
2347 C  CE3 . TRP B 55  ? 0.7171 0.6485 0.7003 -0.0099 -0.0434 0.0130  138 TRP B CE3 
2348 C  CZ2 . TRP B 55  ? 0.7300 0.6019 0.6807 -0.0226 -0.0527 0.0143  138 TRP B CZ2 
2349 C  CZ3 . TRP B 55  ? 0.7139 0.6257 0.6765 -0.0103 -0.0451 0.0117  138 TRP B CZ3 
2350 C  CH2 . TRP B 55  ? 0.7375 0.6182 0.6802 -0.0156 -0.0489 0.0112  138 TRP B CH2 
2351 N  N   . ASP B 56  ? 0.6857 0.6701 0.7122 -0.0016 -0.0187 0.0021  139 ASP B N   
2352 C  CA  . ASP B 56  ? 0.7021 0.6905 0.7165 0.0031  -0.0081 -0.0065 139 ASP B CA  
2353 C  C   . ASP B 56  ? 0.7523 0.7535 0.7424 0.0067  -0.0066 -0.0053 139 ASP B C   
2354 O  O   . ASP B 56  ? 0.8298 0.8353 0.8066 0.0125  0.0044  -0.0060 139 ASP B O   
2355 C  CB  . ASP B 56  ? 0.7344 0.7140 0.7429 -0.0017 -0.0104 -0.0214 139 ASP B CB  
2356 C  CG  . ASP B 56  ? 0.7773 0.7440 0.8104 -0.0004 -0.0052 -0.0203 139 ASP B CG  
2357 O  OD1 . ASP B 56  ? 0.8243 0.7946 0.8804 0.0039  -0.0009 -0.0069 139 ASP B OD1 
2358 O  OD2 . ASP B 56  ? 0.7711 0.7252 0.8038 -0.0044 -0.0058 -0.0304 139 ASP B OD2 
2359 N  N   . GLY B 57  ? 0.7456 0.7540 0.7293 0.0051  -0.0158 -0.0010 140 GLY B N   
2360 C  CA  . GLY B 57  ? 0.8013 0.8265 0.7670 0.0098  -0.0157 0.0053  140 GLY B CA  
2361 C  C   . GLY B 57  ? 0.7986 0.8252 0.7695 0.0135  -0.0192 0.0178  140 GLY B C   
2362 O  O   . GLY B 57  ? 0.7504 0.7612 0.7319 0.0113  -0.0217 0.0185  140 GLY B O   
2363 N  N   . PHE B 58  ? 0.8727 0.9170 0.8332 0.0203  -0.0182 0.0287  141 PHE B N   
2364 C  CA  . PHE B 58  ? 0.8471 0.8899 0.8126 0.0283  -0.0165 0.0431  141 PHE B CA  
2365 C  C   . PHE B 58  ? 0.8210 0.8952 0.7787 0.0351  -0.0189 0.0558  141 PHE B C   
2366 O  O   . PHE B 58  ? 0.7797 0.8648 0.7279 0.0407  -0.0143 0.0659  141 PHE B O   
2367 C  CB  . PHE B 58  ? 0.8160 0.8358 0.7870 0.0325  -0.0074 0.0525  141 PHE B CB  
2368 C  CG  . PHE B 58  ? 0.8529 0.8636 0.8237 0.0431  -0.0012 0.0673  141 PHE B CG  
2369 C  CD1 . PHE B 58  ? 0.8445 0.8485 0.8149 0.0472  -0.0017 0.0669  141 PHE B CD1 
2370 C  CD2 . PHE B 58  ? 0.9266 0.9331 0.8981 0.0508  0.0082  0.0834  141 PHE B CD2 
2371 C  CE1 . PHE B 58  ? 0.8503 0.8407 0.8194 0.0607  0.0088  0.0807  141 PHE B CE1 
2372 C  CE2 . PHE B 58  ? 0.9513 0.9431 0.9231 0.0626  0.0168  0.0978  141 PHE B CE2 
2373 C  CZ  . PHE B 58  ? 0.9115 0.8936 0.8813 0.0685  0.0180  0.0957  141 PHE B CZ  
2374 N  N   . ASP B 59  ? 0.8342 0.9263 0.7983 0.0347  -0.0261 0.0588  142 ASP B N   
2375 C  CA  . ASP B 59  ? 0.8444 0.9742 0.8090 0.0405  -0.0313 0.0762  142 ASP B CA  
2376 C  C   . ASP B 59  ? 0.8955 1.0194 0.8712 0.0587  -0.0185 0.0982  142 ASP B C   
2377 O  O   . ASP B 59  ? 0.8814 1.0033 0.8707 0.0660  -0.0138 0.1051  142 ASP B O   
2378 C  CB  . ASP B 59  ? 0.8774 1.0333 0.8520 0.0304  -0.0449 0.0732  142 ASP B CB  
2379 C  CG  . ASP B 59  ? 1.0265 1.2299 1.0004 0.0287  -0.0578 0.0890  142 ASP B CG  
2380 O  OD1 . ASP B 59  ? 1.1049 1.3248 1.0809 0.0433  -0.0524 0.1118  142 ASP B OD1 
2381 O  OD2 . ASP B 59  ? 1.0986 1.3224 1.0703 0.0114  -0.0747 0.0800  142 ASP B OD2 
2382 N  N   . GLU B 60  ? 0.9211 1.0392 0.8904 0.0675  -0.0100 0.1102  143 GLU B N   
2383 C  CA  . GLU B 60  ? 0.8906 0.9912 0.8689 0.0849  0.0052  0.1300  143 GLU B CA  
2384 C  C   . GLU B 60  ? 0.8966 1.0298 0.8904 0.0998  0.0069  0.1540  143 GLU B C   
2385 O  O   . GLU B 60  ? 0.8346 0.9450 0.8380 0.1134  0.0211  0.1617  143 GLU B O   
2386 C  CB  . GLU B 60  ? 0.8900 0.9813 0.8617 0.0899  0.0138  0.1415  143 GLU B CB  
2387 C  CG  . GLU B 60  ? 0.9319 1.0067 0.9131 0.1087  0.0300  0.1661  143 GLU B CG  
2388 C  CD  . GLU B 60  ? 1.1121 1.1544 1.0912 0.1081  0.0409  0.1708  143 GLU B CD  
2389 O  OE1 . GLU B 60  ? 1.2097 1.2092 1.1937 0.1147  0.0540  0.1760  143 GLU B OE1 
2390 O  OE2 . GLU B 60  ? 1.1744 1.2316 1.1461 0.1005  0.0376  0.1693  143 GLU B OE2 
2391 N  N   . PRO B 61  ? 0.8896 1.0749 0.8863 0.0985  -0.0063 0.1680  144 PRO B N   
2392 C  CA  . PRO B 61  ? 0.9047 1.1284 0.9261 0.1130  -0.0054 0.1964  144 PRO B CA  
2393 C  C   . PRO B 61  ? 0.9457 1.1681 0.9856 0.1132  -0.0028 0.1915  144 PRO B C   
2394 O  O   . PRO B 61  ? 1.0215 1.2509 1.0834 0.1333  0.0118  0.2143  144 PRO B O   
2395 C  CB  . PRO B 61  ? 0.8526 1.1345 0.8691 0.1019  -0.0283 0.2062  144 PRO B CB  
2396 C  CG  . PRO B 61  ? 0.8323 1.0975 0.8164 0.0935  -0.0301 0.1924  144 PRO B CG  
2397 C  CD  . PRO B 61  ? 0.8397 1.0512 0.8155 0.0855  -0.0211 0.1624  144 PRO B CD  
2398 N  N   . ARG B 62  ? 0.8658 1.0787 0.8981 0.0933  -0.0138 0.1645  145 ARG B N   
2399 C  CA  . ARG B 62  ? 0.7904 0.9984 0.8375 0.0928  -0.0096 0.1598  145 ARG B CA  
2400 C  C   . ARG B 62  ? 0.7756 0.9225 0.8073 0.0979  0.0073  0.1429  145 ARG B C   
2401 O  O   . ARG B 62  ? 0.6985 0.8359 0.7362 0.1009  0.0149  0.1406  145 ARG B O   
2402 C  CB  . ARG B 62  ? 0.8053 1.0344 0.8541 0.0678  -0.0306 0.1423  145 ARG B CB  
2403 C  CG  . ARG B 62  ? 0.8035 1.0925 0.8657 0.0567  -0.0521 0.1566  145 ARG B CG  
2404 C  CD  . ARG B 62  ? 0.7413 1.0310 0.7896 0.0280  -0.0729 0.1304  145 ARG B CD  
2405 N  NE  . ARG B 62  ? 0.7473 1.0143 0.8056 0.0202  -0.0690 0.1157  145 ARG B NE  
2406 C  CZ  . ARG B 62  ? 0.7826 1.0146 0.8229 0.0055  -0.0723 0.0876  145 ARG B CZ  
2407 N  NH1 . ARG B 62  ? 0.8395 1.0542 0.8511 -0.0018 -0.0771 0.0701  145 ARG B NH1 
2408 N  NH2 . ARG B 62  ? 0.6962 0.9115 0.7481 0.0002  -0.0685 0.0797  145 ARG B NH2 
2409 N  N   . CYS B 63  ? 0.7962 0.9037 0.8078 0.0973  0.0124  0.1325  146 CYS B N   
2410 C  CA  . CYS B 63  ? 0.8492 0.8995 0.8432 0.0957  0.0220  0.1149  146 CYS B CA  
2411 C  C   . CYS B 63  ? 0.8810 0.9254 0.8713 0.0797  0.0123  0.0945  146 CYS B C   
2412 O  O   . CYS B 63  ? 0.9059 0.9200 0.8864 0.0823  0.0206  0.0877  146 CYS B O   
2413 C  CB  . CYS B 63  ? 0.8872 0.9051 0.8774 0.1168  0.0444  0.1263  146 CYS B CB  
2414 S  SG  . CYS B 63  ? 0.9990 0.9388 0.9571 0.1110  0.0525  0.1054  146 CYS B SG  
2415 N  N   . THR B 64  ? 0.8886 0.9594 0.8836 0.0634  -0.0042 0.0849  147 THR B N   
2416 C  CA  . THR B 64  ? 0.8118 0.8771 0.8069 0.0482  -0.0131 0.0677  147 THR B CA  
2417 C  C   . THR B 64  ? 0.8091 0.8567 0.7945 0.0355  -0.0201 0.0509  147 THR B C   
2418 O  O   . THR B 64  ? 0.8338 0.8962 0.8160 0.0327  -0.0243 0.0507  147 THR B O   
2419 C  CB  . THR B 64  ? 0.8004 0.9081 0.8128 0.0395  -0.0247 0.0716  147 THR B CB  
2420 O  OG1 . THR B 64  ? 0.9169 1.0477 0.9470 0.0526  -0.0164 0.0924  147 THR B OG1 
2421 C  CG2 . THR B 64  ? 0.8192 0.9160 0.8333 0.0239  -0.0320 0.0551  147 THR B CG2 
2422 N  N   . LEU B 65  ? 0.7384 0.7564 0.7188 0.0290  -0.0204 0.0392  148 LEU B N   
2423 C  CA  . LEU B 65  ? 0.7954 0.8014 0.7752 0.0184  -0.0257 0.0274  148 LEU B CA  
2424 C  C   . LEU B 65  ? 0.8034 0.8217 0.7907 0.0076  -0.0338 0.0170  148 LEU B C   
2425 O  O   . LEU B 65  ? 0.8109 0.8319 0.8038 0.0045  -0.0363 0.0165  148 LEU B O   
2426 C  CB  . LEU B 65  ? 0.8158 0.7874 0.7897 0.0152  -0.0250 0.0237  148 LEU B CB  
2427 C  CG  . LEU B 65  ? 0.8166 0.7644 0.7798 0.0224  -0.0172 0.0310  148 LEU B CG  
2428 C  CD1 . LEU B 65  ? 0.8974 0.8103 0.8426 0.0216  -0.0158 0.0270  148 LEU B CD1 
2429 C  CD2 . LEU B 65  ? 0.7842 0.7257 0.7541 0.0171  -0.0180 0.0327  148 LEU B CD2 
2430 N  N   . LEU B 66  ? 0.8096 0.8319 0.7959 0.0025  -0.0356 0.0092  149 LEU B N   
2431 C  CA  . LEU B 66  ? 0.7728 0.8000 0.7614 -0.0074 -0.0411 -0.0027 149 LEU B CA  
2432 C  C   . LEU B 66  ? 0.7760 0.7819 0.7724 -0.0108 -0.0384 -0.0105 149 LEU B C   
2433 O  O   . LEU B 66  ? 0.8618 0.8582 0.8617 -0.0068 -0.0332 -0.0068 149 LEU B O   
2434 C  CB  . LEU B 66  ? 0.8076 0.8515 0.7816 -0.0098 -0.0434 -0.0074 149 LEU B CB  
2435 C  CG  . LEU B 66  ? 0.8803 0.9529 0.8495 -0.0052 -0.0476 0.0060  149 LEU B CG  
2436 C  CD1 . LEU B 66  ? 0.9718 1.0599 0.9189 -0.0090 -0.0520 0.0016  149 LEU B CD1 
2437 C  CD2 . LEU B 66  ? 0.9013 0.9924 0.8857 -0.0097 -0.0552 0.0126  149 LEU B CD2 
2438 N  N   . GLU B 67  ? 0.7348 0.7351 0.7384 -0.0186 -0.0417 -0.0184 150 GLU B N   
2439 C  CA  . GLU B 67  ? 0.7449 0.7271 0.7598 -0.0199 -0.0375 -0.0236 150 GLU B CA  
2440 C  C   . GLU B 67  ? 0.7507 0.7256 0.7639 -0.0283 -0.0383 -0.0366 150 GLU B C   
2441 O  O   . GLU B 67  ? 0.8498 0.8313 0.8659 -0.0368 -0.0459 -0.0370 150 GLU B O   
2442 C  CB  . GLU B 67  ? 0.8131 0.7867 0.8423 -0.0202 -0.0407 -0.0145 150 GLU B CB  
2443 C  CG  . GLU B 67  ? 0.8547 0.8157 0.9025 -0.0201 -0.0374 -0.0136 150 GLU B CG  
2444 C  CD  . GLU B 67  ? 0.8921 0.8536 0.9504 -0.0147 -0.0333 -0.0059 150 GLU B CD  
2445 O  OE1 . GLU B 67  ? 0.9103 0.8677 0.9907 -0.0127 -0.0302 0.0004  150 GLU B OE1 
2446 O  OE2 . GLU B 67  ? 0.9186 0.8864 0.9673 -0.0124 -0.0326 -0.0031 150 GLU B OE2 
2447 N  N   . ALA B 68  ? 0.7023 0.6613 0.7111 -0.0261 -0.0289 -0.0467 151 ALA B N   
2448 C  CA  . ALA B 68  ? 0.6969 0.6370 0.6968 -0.0344 -0.0272 -0.0631 151 ALA B CA  
2449 C  C   . ALA B 68  ? 0.8087 0.7237 0.8294 -0.0299 -0.0166 -0.0628 151 ALA B C   
2450 O  O   . ALA B 68  ? 0.8887 0.8027 0.9241 -0.0179 -0.0067 -0.0534 151 ALA B O   
2451 C  CB  . ALA B 68  ? 0.7098 0.6446 0.6764 -0.0341 -0.0215 -0.0779 151 ALA B CB  
2452 N  N   . LYS B 69  ? 0.8116 0.7084 0.8379 -0.0397 -0.0189 -0.0701 152 LYS B N   
2453 C  CA  . LYS B 69  ? 0.7257 0.5964 0.7744 -0.0348 -0.0080 -0.0674 152 LYS B CA  
2454 C  C   . LYS B 69  ? 0.8048 0.6388 0.8368 -0.0437 -0.0016 -0.0891 152 LYS B C   
2455 O  O   . LYS B 69  ? 0.7865 0.6186 0.8108 -0.0617 -0.0142 -0.0974 152 LYS B O   
2456 C  CB  . LYS B 69  ? 0.6691 0.5491 0.7451 -0.0379 -0.0167 -0.0494 152 LYS B CB  
2457 C  CG  . LYS B 69  ? 0.7191 0.6250 0.8043 -0.0307 -0.0231 -0.0307 152 LYS B CG  
2458 C  CD  . LYS B 69  ? 0.8186 0.7231 0.9211 -0.0177 -0.0138 -0.0207 152 LYS B CD  
2459 C  CE  . LYS B 69  ? 0.8386 0.7658 0.9431 -0.0156 -0.0230 -0.0067 152 LYS B CE  
2460 N  NZ  . LYS B 69  ? 0.9328 0.8653 1.0624 -0.0065 -0.0171 0.0073  152 LYS B NZ  
2461 N  N   . ALA B 70  ? 0.9107 0.7141 0.9378 -0.0316 0.0189  -0.0975 153 ALA B N   
2462 C  CA  . ALA B 70  ? 0.9763 0.7335 0.9758 -0.0391 0.0284  -0.1232 153 ALA B CA  
2463 C  C   . ALA B 70  ? 1.0783 0.7985 1.1044 -0.0382 0.0388  -0.1205 153 ALA B C   
2464 O  O   . ALA B 70  ? 1.2232 0.9354 1.2572 -0.0564 0.0260  -0.1222 153 ALA B O   
2465 C  CB  . ALA B 70  ? 1.0612 0.7987 1.0292 -0.0241 0.0501  -0.1370 153 ALA B CB  
2466 N  N   . ASN B 71  ? 1.0556 0.7552 1.1001 -0.0164 0.0631  -0.1128 154 ASN B N   
2467 C  CA  . ASN B 71  ? 1.0733 0.7294 1.1406 -0.0113 0.0790  -0.1106 154 ASN B CA  
2468 C  C   . ASN B 71  ? 1.0376 0.7235 1.1578 -0.0046 0.0721  -0.0760 154 ASN B C   
2469 O  O   . ASN B 71  ? 1.0391 0.7488 1.1885 0.0145  0.0800  -0.0530 154 ASN B O   
2470 C  CB  . ASN B 71  ? 1.0570 0.6729 1.1157 0.0119  0.1130  -0.1190 154 ASN B CB  
2471 C  CG  . ASN B 71  ? 1.2121 0.7710 1.2877 0.0180  0.1335  -0.1210 154 ASN B CG  
2472 O  OD1 . ASN B 71  ? 1.2335 0.7684 1.3092 -0.0021 0.1218  -0.1284 154 ASN B OD1 
2473 N  ND2 . ASN B 71  ? 1.3294 0.8664 1.4229 0.0468  0.1662  -0.1117 154 ASN B ND2 
2474 N  N   . TYR B 72  ? 0.9920 0.6781 1.1245 -0.0216 0.0568  -0.0705 155 TYR B N   
2475 C  CA  . TYR B 72  ? 0.9131 0.6230 1.0876 -0.0164 0.0505  -0.0381 155 TYR B CA  
2476 C  C   . TYR B 72  ? 1.0238 0.7044 1.2161 -0.0275 0.0508  -0.0333 155 TYR B C   
2477 O  O   . TYR B 72  ? 1.0851 0.7824 1.3101 -0.0222 0.0474  -0.0044 155 TYR B O   
2478 C  CB  . TYR B 72  ? 0.8490 0.6124 1.0214 -0.0235 0.0271  -0.0249 155 TYR B CB  
2479 C  CG  . TYR B 72  ? 0.8689 0.6644 1.0417 -0.0101 0.0263  -0.0158 155 TYR B CG  
2480 C  CD1 . TYR B 72  ? 0.8455 0.6608 1.0512 0.0035  0.0273  0.0120  155 TYR B CD1 
2481 C  CD2 . TYR B 72  ? 0.8562 0.6640 0.9985 -0.0126 0.0232  -0.0325 155 TYR B CD2 
2482 C  CE1 . TYR B 72  ? 0.7842 0.6291 0.9941 0.0116  0.0243  0.0214  155 TYR B CE1 
2483 C  CE2 . TYR B 72  ? 0.8181 0.6531 0.9641 -0.0021 0.0231  -0.0225 155 TYR B CE2 
2484 C  CZ  . TYR B 72  ? 0.8277 0.6804 1.0084 0.0087  0.0233  0.0038  155 TYR B CZ  
2485 O  OH  . TYR B 72  ? 0.8621 0.7422 1.0502 0.0152  0.0211  0.0148  155 TYR B OH  
2486 N  N   . ALA B 73  ? 1.0544 0.6912 1.2249 -0.0442 0.0538  -0.0595 156 ALA B N   
2487 C  CA  . ALA B 73  ? 0.9823 0.5902 1.1725 -0.0586 0.0531  -0.0540 156 ALA B CA  
2488 C  C   . ALA B 73  ? 0.9818 0.5538 1.2064 -0.0391 0.0765  -0.0357 156 ALA B C   
2489 O  O   . ALA B 73  ? 1.1137 0.6766 1.3674 -0.0450 0.0756  -0.0164 156 ALA B O   
2490 C  CB  . ALA B 73  ? 1.0236 0.5889 1.1811 -0.0850 0.0488  -0.0883 156 ALA B CB  
2491 N  N   . PHE B 74  ? 0.9580 0.5118 1.1833 -0.0144 0.0990  -0.0377 157 PHE B N   
2492 C  CA  . PHE B 74  ? 1.0089 0.5283 1.2711 0.0079  0.1247  -0.0177 157 PHE B CA  
2493 C  C   . PHE B 74  ? 1.0139 0.5814 1.3245 0.0206  0.1167  0.0283  157 PHE B C   
2494 O  O   . PHE B 74  ? 1.1470 0.6932 1.4956 0.0380  0.1347  0.0527  157 PHE B O   
2495 C  CB  . PHE B 74  ? 0.9679 0.4619 1.2212 0.0341  0.1538  -0.0282 157 PHE B CB  
2496 C  CG  . PHE B 74  ? 0.9404 0.4959 1.2040 0.0505  0.1488  -0.0109 157 PHE B CG  
2497 C  CD1 . PHE B 74  ? 0.9651 0.5583 1.1946 0.0369  0.1282  -0.0267 157 PHE B CD1 
2498 C  CD2 . PHE B 74  ? 0.8745 0.4506 1.1855 0.0787  0.1644  0.0236  157 PHE B CD2 
2499 C  CE1 . PHE B 74  ? 0.8758 0.5205 1.1162 0.0497  0.1239  -0.0104 157 PHE B CE1 
2500 C  CE2 . PHE B 74  ? 0.8269 0.4598 1.1511 0.0897  0.1575  0.0407  157 PHE B CE2 
2501 C  CZ  . PHE B 74  ? 0.7912 0.4555 1.0790 0.0743  0.1375  0.0225  157 PHE B CZ  
2502 N  N   . LEU B 75  ? 0.8831 0.5119 1.1907 0.0126  0.0908  0.0412  158 LEU B N   
2503 C  CA  . LEU B 75  ? 0.8569 0.5295 1.1977 0.0196  0.0786  0.0817  158 LEU B CA  
2504 C  C   . LEU B 75  ? 0.9255 0.6046 1.2678 0.0005  0.0638  0.0922  158 LEU B C   
2505 O  O   . LEU B 75  ? 0.8572 0.5695 1.2188 0.0048  0.0536  0.1254  158 LEU B O   
2506 C  CB  . LEU B 75  ? 0.7470 0.4771 1.0797 0.0234  0.0611  0.0901  158 LEU B CB  
2507 C  CG  . LEU B 75  ? 0.8269 0.5581 1.1589 0.0399  0.0751  0.0809  158 LEU B CG  
2508 C  CD1 . LEU B 75  ? 0.7330 0.5152 1.0507 0.0360  0.0551  0.0831  158 LEU B CD1 
2509 C  CD2 . LEU B 75  ? 0.8625 0.5873 1.2419 0.0659  0.0960  0.1100  158 LEU B CD2 
2510 N  N   . PHE B 76  ? 0.9624 0.6127 1.2846 -0.0210 0.0619  0.0666  159 PHE B N   
2511 C  CA  . PHE B 76  ? 0.9240 0.5785 1.2544 -0.0397 0.0519  0.0782  159 PHE B CA  
2512 C  C   . PHE B 76  ? 1.0367 0.6290 1.3846 -0.0475 0.0684  0.0732  159 PHE B C   
2513 O  O   . PHE B 76  ? 1.1198 0.6606 1.4562 -0.0456 0.0842  0.0468  159 PHE B O   
2514 C  CB  . PHE B 76  ? 0.8958 0.5758 1.1963 -0.0623 0.0331  0.0578  159 PHE B CB  
2515 C  CG  . PHE B 76  ? 0.8862 0.6168 1.1650 -0.0554 0.0194  0.0582  159 PHE B CG  
2516 C  CD1 . PHE B 76  ? 0.7883 0.5617 1.0674 -0.0545 0.0072  0.0820  159 PHE B CD1 
2517 C  CD2 . PHE B 76  ? 0.9382 0.6694 1.1930 -0.0500 0.0203  0.0344  159 PHE B CD2 
2518 C  CE1 . PHE B 76  ? 0.8159 0.6262 1.0718 -0.0494 -0.0043 0.0801  159 PHE B CE1 
2519 C  CE2 . PHE B 76  ? 0.8450 0.6181 1.0823 -0.0449 0.0085  0.0358  159 PHE B CE2 
2520 C  CZ  . PHE B 76  ? 0.8322 0.6423 1.0700 -0.0452 -0.0041 0.0576  159 PHE B CZ  
2521 N  N   . VAL B 77  ? 1.0835 0.6772 1.4568 -0.0562 0.0662  0.0988  160 VAL B N   
2522 C  CA  . VAL B 77  ? 1.2391 0.7730 1.6285 -0.0712 0.0784  0.0928  160 VAL B CA  
2523 C  C   . VAL B 77  ? 1.2742 0.8105 1.6424 -0.1050 0.0614  0.0668  160 VAL B C   
2524 O  O   . VAL B 77  ? 1.2042 0.7962 1.5674 -0.1139 0.0437  0.0768  160 VAL B O   
2525 C  CB  . VAL B 77  ? 1.2683 0.8010 1.7002 -0.0642 0.0863  0.1366  160 VAL B CB  
2526 C  CG1 . VAL B 77  ? 1.2526 0.8080 1.7046 -0.0312 0.0943  0.1685  160 VAL B CG1 
2527 C  CG2 . VAL B 77  ? 1.2718 0.8534 1.7076 -0.0800 0.0692  0.1582  160 VAL B CG2 
2528 N  N   . PRO B 78  ? 1.3913 0.8695 1.7442 -0.1241 0.0659  0.0332  161 PRO B N   
2529 C  CA  . PRO B 78  ? 1.4632 0.9520 1.7925 -0.1573 0.0449  0.0067  161 PRO B CA  
2530 C  C   . PRO B 78  ? 1.5035 1.0192 1.8633 -0.1820 0.0320  0.0299  161 PRO B C   
2531 O  O   . PRO B 78  ? 1.5285 1.1036 1.8844 -0.1917 0.0141  0.0358  161 PRO B O   
2532 C  CB  . PRO B 78  ? 1.6330 1.0418 1.9362 -0.1722 0.0541  -0.0334 161 PRO B CB  
2533 C  CG  . PRO B 78  ? 1.6420 1.0085 1.9456 -0.1379 0.0829  -0.0326 161 PRO B CG  
2534 C  CD  . PRO B 78  ? 1.5438 0.9431 1.8946 -0.1152 0.0905  0.0158  161 PRO B CD  
2535 N  N   . LEU B 79  ? 1.4814 0.9535 1.8743 -0.1907 0.0436  0.0457  162 LEU B N   
2536 C  CA  . LEU B 79  ? 1.4450 0.9354 1.8701 -0.2189 0.0331  0.0663  162 LEU B CA  
2537 C  C   . LEU B 79  ? 1.3113 0.8748 1.7577 -0.2047 0.0301  0.1090  162 LEU B C   
2538 O  O   . LEU B 79  ? 1.3571 0.9581 1.8227 -0.2253 0.0193  0.1245  162 LEU B O   
2539 C  CB  . LEU B 79  ? 1.5644 0.9840 2.0210 -0.2311 0.0488  0.0743  162 LEU B CB  
2540 C  CG  . LEU B 79  ? 1.6649 0.9955 2.0948 -0.2447 0.0565  0.0304  162 LEU B CG  
2541 C  CD1 . LEU B 79  ? 1.6543 0.9193 2.1029 -0.2375 0.0792  0.0437  162 LEU B CD1 
2542 C  CD2 . LEU B 79  ? 1.6950 1.0187 2.1061 -0.2901 0.0315  -0.0017 162 LEU B CD2 
2543 N  N   . LEU B 80  ? 1.2138 0.7988 1.6561 -0.1709 0.0392  0.1290  163 LEU B N   
2544 C  CA  . LEU B 80  ? 1.1927 0.8346 1.6475 -0.1572 0.0384  0.1696  163 LEU B CA  
2545 C  C   . LEU B 80  ? 1.1803 0.8827 1.6023 -0.1473 0.0252  0.1641  163 LEU B C   
2546 O  O   . LEU B 80  ? 1.1904 0.9389 1.6133 -0.1405 0.0236  0.1921  163 LEU B O   
2547 C  CB  . LEU B 80  ? 1.1763 0.8062 1.6467 -0.1289 0.0536  0.2007  163 LEU B CB  
2548 C  CG  . LEU B 80  ? 1.2418 0.8167 1.7512 -0.1289 0.0719  0.2213  163 LEU B CG  
2549 C  CD1 . LEU B 80  ? 1.3238 0.8225 1.8325 -0.1393 0.0817  0.1855  163 LEU B CD1 
2550 C  CD2 . LEU B 80  ? 1.2521 0.8384 1.7736 -0.0962 0.0820  0.2576  163 LEU B CD2 
2551 N  N   . GLY B 81  ? 1.1515 0.8514 1.5423 -0.1456 0.0177  0.1294  164 GLY B N   
2552 C  CA  . GLY B 81  ? 1.0005 0.7514 1.3615 -0.1369 0.0063  0.1233  164 GLY B CA  
2553 C  C   . GLY B 81  ? 0.9392 0.7154 1.2866 -0.1094 0.0084  0.1422  164 GLY B C   
2554 O  O   . GLY B 81  ? 0.9580 0.7746 1.2811 -0.1029 0.0002  0.1427  164 GLY B O   
2555 N  N   . VAL B 82  ? 0.9466 0.6999 1.3095 -0.0937 0.0185  0.1590  165 VAL B N   
2556 C  CA  . VAL B 82  ? 0.9333 0.7129 1.2856 -0.0710 0.0162  0.1792  165 VAL B CA  
2557 C  C   . VAL B 82  ? 0.8802 0.6373 1.2334 -0.0561 0.0213  0.1654  165 VAL B C   
2558 O  O   . VAL B 82  ? 0.9275 0.6388 1.2947 -0.0588 0.0333  0.1493  165 VAL B O   
2559 C  CB  . VAL B 82  ? 0.9886 0.7749 1.3621 -0.0631 0.0220  0.2217  165 VAL B CB  
2560 C  CG1 . VAL B 82  ? 0.9823 0.7912 1.3564 -0.0764 0.0215  0.2375  165 VAL B CG1 
2561 C  CG2 . VAL B 82  ? 0.9566 0.6960 1.3685 -0.0595 0.0374  0.2327  165 VAL B CG2 
2562 N  N   . PRO B 83  ? 0.8163 0.6024 1.1546 -0.0410 0.0135  0.1709  166 PRO B N   
2563 C  CA  . PRO B 83  ? 0.8262 0.5982 1.1748 -0.0249 0.0205  0.1657  166 PRO B CA  
2564 C  C   . PRO B 83  ? 0.8584 0.6115 1.2463 -0.0099 0.0336  0.1968  166 PRO B C   
2565 O  O   . PRO B 83  ? 0.8394 0.6019 1.2420 -0.0094 0.0324  0.2285  166 PRO B O   
2566 C  CB  . PRO B 83  ? 0.7881 0.6036 1.1144 -0.0173 0.0048  0.1698  166 PRO B CB  
2567 C  CG  . PRO B 83  ? 0.7500 0.5905 1.0441 -0.0305 -0.0076 0.1631  166 PRO B CG  
2568 C  CD  . PRO B 83  ? 0.7933 0.6239 1.1015 -0.0398 -0.0016 0.1782  166 PRO B CD  
2569 N  N   . ARG B 84  ? 0.9012 0.6276 1.3065 0.0045  0.0486  0.1897  167 ARG B N   
2570 C  CA  . ARG B 84  ? 0.9530 0.6676 1.4006 0.0248  0.0626  0.2236  167 ARG B CA  
2571 C  C   . ARG B 84  ? 0.9572 0.7287 1.4119 0.0358  0.0449  0.2591  167 ARG B C   
2572 O  O   . ARG B 84  ? 0.8743 0.6782 1.3096 0.0361  0.0311  0.2491  167 ARG B O   
2573 C  CB  . ARG B 84  ? 0.9233 0.5973 1.3866 0.0412  0.0866  0.2079  167 ARG B CB  
2574 C  CG  . ARG B 84  ? 0.9944 0.6086 1.4353 0.0267  0.1004  0.1649  167 ARG B CG  
2575 C  CD  . ARG B 84  ? 1.1184 0.6814 1.5704 0.0464  0.1302  0.1517  167 ARG B CD  
2576 N  NE  . ARG B 84  ? 1.1713 0.6798 1.5851 0.0303  0.1390  0.1035  167 ARG B NE  
2577 C  CZ  . ARG B 84  ? 1.2161 0.6620 1.6270 0.0154  0.1497  0.0878  167 ARG B CZ  
2578 N  NH1 . ARG B 84  ? 1.1619 0.5916 1.6101 0.0166  0.1559  0.1185  167 ARG B NH1 
2579 N  NH2 . ARG B 84  ? 1.3474 0.7463 1.7169 -0.0024 0.1531  0.0424  167 ARG B NH2 
2580 N  N   . PRO B 85  ? 0.9810 0.7303 0.9138 0.0007  0.2927  0.1459  168 PRO B N   
2581 C  CA  . PRO B 85  ? 1.0290 0.7861 0.9316 0.0201  0.2729  0.1552  168 PRO B CA  
2582 C  C   . PRO B 85  ? 1.0305 0.8041 0.9344 0.0251  0.2420  0.1654  168 PRO B C   
2583 O  O   . PRO B 85  ? 1.0259 0.8132 0.9172 0.0317  0.2119  0.1645  168 PRO B O   
2584 C  CB  . PRO B 85  ? 1.0891 0.8217 0.9593 0.0383  0.3045  0.1737  168 PRO B CB  
2585 C  CG  . PRO B 85  ? 1.0436 0.7577 0.9330 0.0254  0.3422  0.1680  168 PRO B CG  
2586 C  CD  . PRO B 85  ? 0.9626 0.6834 0.8872 0.0026  0.3337  0.1554  168 PRO B CD  
2587 N  N   . TRP B 86  ? 1.0085 0.7786 0.9276 0.0219  0.2491  0.1757  169 TRP B N   
2588 C  CA  . TRP B 86  ? 0.9238 0.7116 0.8522 0.0280  0.2242  0.1902  169 TRP B CA  
2589 C  C   . TRP B 86  ? 0.9063 0.7158 0.8619 0.0150  0.1937  0.1744  169 TRP B C   
2590 O  O   . TRP B 86  ? 0.9139 0.7412 0.8830 0.0191  0.1705  0.1862  169 TRP B O   
2591 C  CB  . TRP B 86  ? 0.8448 0.6166 0.7771 0.0331  0.2483  0.2100  169 TRP B CB  
2592 C  CG  . TRP B 86  ? 0.8813 0.6343 0.8269 0.0171  0.2656  0.1938  169 TRP B CG  
2593 C  CD1 . TRP B 86  ? 0.8865 0.6191 0.8265 0.0120  0.2879  0.1794  169 TRP B CD1 
2594 C  CD2 . TRP B 86  ? 0.9179 0.6750 0.8843 0.0055  0.2527  0.1846  169 TRP B CD2 
2595 N  NE1 . TRP B 86  ? 0.8500 0.5722 0.8023 -0.0036 0.2880  0.1622  169 TRP B NE1 
2596 C  CE2 . TRP B 86  ? 0.8500 0.5864 0.8158 -0.0066 0.2673  0.1647  169 TRP B CE2 
2597 C  CE3 . TRP B 86  ? 0.9067 0.6893 0.8933 0.0057  0.2223  0.1849  169 TRP B CE3 
2598 C  CZ2 . TRP B 86  ? 0.8384 0.5685 0.8140 -0.0179 0.2600  0.1523  169 TRP B CZ2 
2599 C  CZ3 . TRP B 86  ? 0.8559 0.6331 0.8557 -0.0040 0.2187  0.1737  169 TRP B CZ3 
2600 C  CH2 . TRP B 86  ? 0.8535 0.6008 0.8440 -0.0155 0.2397  0.1597  169 TRP B CH2 
2601 N  N   . ALA B 87  ? 0.9228 0.7328 0.8900 0.0004  0.1940  0.1502  170 ALA B N   
2602 C  CA  . ALA B 87  ? 0.9257 0.7542 0.9172 -0.0101 0.1689  0.1354  170 ALA B CA  
2603 C  C   . ALA B 87  ? 0.8984 0.7388 0.8850 -0.0117 0.1493  0.1194  170 ALA B C   
2604 O  O   . ALA B 87  ? 0.9292 0.7824 0.9348 -0.0205 0.1343  0.1044  170 ALA B O   
2605 C  CB  . ALA B 87  ? 0.8731 0.6935 0.8823 -0.0247 0.1822  0.1216  170 ALA B CB  
2606 N  N   . ARG B 88  ? 0.8290 0.6615 0.7856 -0.0010 0.1509  0.1233  171 ARG B N   
2607 C  CA  . ARG B 88  ? 0.8711 0.7049 0.8129 0.0003  0.1369  0.1085  171 ARG B CA  
2608 C  C   . ARG B 88  ? 0.9381 0.7862 0.8878 -0.0026 0.1002  0.1040  171 ARG B C   
2609 O  O   . ARG B 88  ? 0.9483 0.8004 0.9035 -0.0078 0.0898  0.0875  171 ARG B O   
2610 C  CB  . ARG B 88  ? 0.8942 0.7089 0.7915 0.0160  0.1458  0.1157  171 ARG B CB  
2611 C  CG  . ARG B 88  ? 0.9229 0.7284 0.7916 0.0214  0.1329  0.1020  171 ARG B CG  
2612 C  CD  . ARG B 88  ? 0.9507 0.7574 0.8375 0.0151  0.1531  0.0869  171 ARG B CD  
2613 N  NE  . ARG B 88  ? 1.0106 0.8143 0.8838 0.0170  0.1356  0.0727  171 ARG B NE  
2614 C  CZ  . ARG B 88  ? 1.0135 0.8205 0.9007 0.0151  0.1496  0.0616  171 ARG B CZ  
2615 N  NH1 . ARG B 88  ? 1.0856 0.9030 1.0057 0.0086  0.1779  0.0626  171 ARG B NH1 
2616 N  NH2 . ARG B 88  ? 0.9742 0.7736 0.8439 0.0195  0.1355  0.0506  171 ARG B NH2 
2617 N  N   . ALA B 89  ? 0.9567 0.8130 0.9103 0.0009  0.0817  0.1204  172 ALA B N   
2618 C  CA  . ALA B 89  ? 0.8834 0.7532 0.8503 -0.0037 0.0467  0.1183  172 ALA B CA  
2619 C  C   . ALA B 89  ? 0.8350 0.7177 0.8401 -0.0143 0.0444  0.1089  172 ALA B C   
2620 O  O   . ALA B 89  ? 0.8655 0.7523 0.8769 -0.0194 0.0247  0.0965  172 ALA B O   
2621 C  CB  . ALA B 89  ? 0.8627 0.7445 0.8367 0.0015  0.0288  0.1422  172 ALA B CB  
2622 N  N   . LYS B 90  ? 0.8221 0.7068 0.8479 -0.0166 0.0648  0.1146  173 LYS B N   
2623 C  CA  . LYS B 90  ? 0.7025 0.5957 0.7571 -0.0240 0.0631  0.1060  173 LYS B CA  
2624 C  C   . LYS B 90  ? 0.7660 0.6590 0.8195 -0.0304 0.0687  0.0832  173 LYS B C   
2625 O  O   . LYS B 90  ? 0.7865 0.6891 0.8565 -0.0342 0.0566  0.0729  173 LYS B O   
2626 C  CB  . LYS B 90  ? 0.6313 0.5181 0.6972 -0.0233 0.0834  0.1175  173 LYS B CB  
2627 C  CG  . LYS B 90  ? 0.6416 0.5310 0.7273 -0.0286 0.0831  0.1084  173 LYS B CG  
2628 C  CD  . LYS B 90  ? 0.6815 0.5653 0.7786 -0.0217 0.0900  0.1283  173 LYS B CD  
2629 C  CE  . LYS B 90  ? 0.8458 0.7300 0.9569 -0.0232 0.0863  0.1202  173 LYS B CE  
2630 N  NZ  . LYS B 90  ? 0.9969 0.8806 1.1247 -0.0125 0.0868  0.1434  173 LYS B NZ  
2631 N  N   . VAL B 91  ? 0.7654 0.6487 0.8026 -0.0304 0.0887  0.0774  174 VAL B N   
2632 C  CA  . VAL B 91  ? 0.7683 0.6560 0.8108 -0.0353 0.0956  0.0599  174 VAL B CA  
2633 C  C   . VAL B 91  ? 0.7774 0.6648 0.8053 -0.0300 0.0789  0.0516  174 VAL B C   
2634 O  O   . VAL B 91  ? 0.8750 0.7718 0.9161 -0.0324 0.0745  0.0394  174 VAL B O   
2635 C  CB  . VAL B 91  ? 0.8164 0.6941 0.8508 -0.0362 0.1238  0.0598  174 VAL B CB  
2636 C  CG1 . VAL B 91  ? 0.8410 0.7266 0.8835 -0.0380 0.1314  0.0467  174 VAL B CG1 
2637 C  CG2 . VAL B 91  ? 0.7871 0.6602 0.8369 -0.0453 0.1401  0.0629  174 VAL B CG2 
2638 N  N   . LYS B 92  ? 0.7735 0.6475 0.7707 -0.0222 0.0687  0.0581  175 LYS B N   
2639 C  CA  . LYS B 92  ? 0.8132 0.6760 0.7850 -0.0174 0.0525  0.0486  175 LYS B CA  
2640 C  C   . LYS B 92  ? 0.8617 0.7344 0.8549 -0.0233 0.0284  0.0430  175 LYS B C   
2641 O  O   . LYS B 92  ? 0.9457 0.8152 0.9367 -0.0226 0.0258  0.0302  175 LYS B O   
2642 C  CB  . LYS B 92  ? 0.8447 0.6882 0.7745 -0.0089 0.0412  0.0568  175 LYS B CB  
2643 C  CG  . LYS B 92  ? 0.9547 0.7755 0.8453 -0.0042 0.0224  0.0454  175 LYS B CG  
2644 C  CD  . LYS B 92  ? 1.0390 0.8419 0.8874 0.0022  0.0027  0.0537  175 LYS B CD  
2645 C  CE  . LYS B 92  ? 1.0635 0.8324 0.8590 0.0073  -0.0153 0.0397  175 LYS B CE  
2646 N  NZ  . LYS B 92  ? 1.0628 0.8055 0.8204 0.0212  0.0145  0.0314  175 LYS B NZ  
2647 N  N   . SER B 93  ? 0.8425 0.7265 0.8582 -0.0276 0.0137  0.0548  176 SER B N   
2648 C  CA  . SER B 93  ? 0.8537 0.7450 0.8915 -0.0324 -0.0080 0.0527  176 SER B CA  
2649 C  C   . SER B 93  ? 0.8426 0.7478 0.9110 -0.0347 0.0019  0.0459  176 SER B C   
2650 O  O   . SER B 93  ? 0.8729 0.7781 0.9475 -0.0350 -0.0062 0.0361  176 SER B O   
2651 C  CB  . SER B 93  ? 0.7740 0.6750 0.8315 -0.0346 -0.0250 0.0718  176 SER B CB  
2652 O  OG  . SER B 93  ? 0.7957 0.7081 0.8770 -0.0331 -0.0078 0.0851  176 SER B OG  
2653 N  N   . ASP B 94  ? 0.8279 0.7419 0.9118 -0.0357 0.0193  0.0510  177 ASP B N   
2654 C  CA  . ASP B 94  ? 0.8233 0.7487 0.9317 -0.0374 0.0242  0.0458  177 ASP B CA  
2655 C  C   . ASP B 94  ? 0.8261 0.7578 0.9342 -0.0383 0.0345  0.0301  177 ASP B C   
2656 O  O   . ASP B 94  ? 0.8271 0.7697 0.9517 -0.0375 0.0313  0.0235  177 ASP B O   
2657 C  CB  . ASP B 94  ? 0.8446 0.7697 0.9622 -0.0384 0.0371  0.0562  177 ASP B CB  
2658 C  CG  . ASP B 94  ? 0.8672 0.7912 0.9961 -0.0344 0.0295  0.0759  177 ASP B CG  
2659 O  OD1 . ASP B 94  ? 0.8888 0.8069 1.0207 -0.0320 0.0426  0.0872  177 ASP B OD1 
2660 O  OD2 . ASP B 94  ? 0.9022 0.8300 1.0377 -0.0338 0.0109  0.0810  177 ASP B OD2 
2661 N  N   . LEU B 95  ? 0.8104 0.7368 0.9024 -0.0383 0.0481  0.0264  178 LEU B N   
2662 C  CA  . LEU B 95  ? 0.7639 0.7017 0.8659 -0.0395 0.0614  0.0162  178 LEU B CA  
2663 C  C   . LEU B 95  ? 0.8528 0.7825 0.9356 -0.0316 0.0658  0.0106  178 LEU B C   
2664 O  O   . LEU B 95  ? 0.9042 0.8464 1.0003 -0.0287 0.0703  0.0039  178 LEU B O   
2665 C  CB  . LEU B 95  ? 0.7318 0.6707 0.8398 -0.0467 0.0807  0.0184  178 LEU B CB  
2666 C  CG  . LEU B 95  ? 0.7142 0.6537 0.8349 -0.0546 0.0813  0.0215  178 LEU B CG  
2667 C  CD1 . LEU B 95  ? 0.7403 0.6732 0.8625 -0.0634 0.1017  0.0223  178 LEU B CD1 
2668 C  CD2 . LEU B 95  ? 0.6664 0.6225 0.8081 -0.0570 0.0708  0.0135  178 LEU B CD2 
2669 N  N   . LEU B 96  ? 0.7984 0.7054 0.8467 -0.0261 0.0654  0.0142  179 LEU B N   
2670 C  CA  . LEU B 96  ? 0.7657 0.6554 0.7844 -0.0158 0.0749  0.0095  179 LEU B CA  
2671 C  C   . LEU B 96  ? 0.7709 0.6407 0.7641 -0.0104 0.0558  0.0029  179 LEU B C   
2672 O  O   . LEU B 96  ? 0.8935 0.7624 0.8877 -0.0044 0.0604  -0.0041 179 LEU B O   
2673 C  CB  . LEU B 96  ? 0.8841 0.7534 0.8700 -0.0103 0.0882  0.0166  179 LEU B CB  
2674 C  CG  . LEU B 96  ? 0.8981 0.7797 0.9059 -0.0144 0.1147  0.0222  179 LEU B CG  
2675 C  CD1 . LEU B 96  ? 0.9705 0.8275 0.9415 -0.0032 0.1347  0.0293  179 LEU B CD1 
2676 C  CD2 . LEU B 96  ? 0.7881 0.6948 0.8348 -0.0182 0.1276  0.0168  179 LEU B CD2 
2677 N  N   . GLN B 97  ? 0.6923 0.5457 0.6641 -0.0128 0.0343  0.0059  180 GLN B N   
2678 C  CA  . GLN B 97  ? 0.7929 0.6210 0.7365 -0.0107 0.0144  -0.0019 180 GLN B CA  
2679 C  C   . GLN B 97  ? 0.8534 0.6949 0.8306 -0.0162 0.0019  -0.0054 180 GLN B C   
2680 O  O   . GLN B 97  ? 0.9783 0.7978 0.9368 -0.0140 -0.0078 -0.0139 180 GLN B O   
2681 C  CB  . GLN B 97  ? 0.8809 0.6898 0.7943 -0.0138 -0.0089 0.0030  180 GLN B CB  
2682 C  CG  . GLN B 97  ? 0.9416 0.7722 0.8923 -0.0249 -0.0297 0.0140  180 GLN B CG  
2683 C  CD  . GLN B 97  ? 1.1121 0.9284 1.0376 -0.0282 -0.0565 0.0204  180 GLN B CD  
2684 O  OE1 . GLN B 97  ? 1.0964 0.8806 0.9691 -0.0230 -0.0644 0.0129  180 GLN B OE1 
2685 N  NE2 . GLN B 97  ? 1.2049 1.0443 1.1669 -0.0356 -0.0708 0.0358  180 GLN B NE2 
2686 N  N   . LYS B 98  ? 0.7995 0.6714 0.8210 -0.0220 0.0036  0.0012  181 LYS B N   
2687 C  CA  . LYS B 98  ? 0.7713 0.6555 0.8226 -0.0229 -0.0024 -0.0010 181 LYS B CA  
2688 C  C   . LYS B 98  ? 0.8627 0.7532 0.9176 -0.0143 0.0140  -0.0093 181 LYS B C   
2689 O  O   . LYS B 98  ? 0.9966 0.8825 1.0562 -0.0102 0.0100  -0.0137 181 LYS B O   
2690 C  CB  . LYS B 98  ? 0.8319 0.7410 0.9206 -0.0278 -0.0026 0.0090  181 LYS B CB  
2691 C  CG  . LYS B 98  ? 0.8429 0.7607 0.9589 -0.0265 -0.0098 0.0104  181 LYS B CG  
2692 C  CD  . LYS B 98  ? 0.9304 0.8605 1.0722 -0.0292 -0.0120 0.0239  181 LYS B CD  
2693 C  CE  . LYS B 98  ? 0.9087 0.8313 1.0485 -0.0347 -0.0249 0.0364  181 LYS B CE  
2694 N  NZ  . LYS B 98  ? 0.8280 0.7609 0.9949 -0.0338 -0.0232 0.0537  181 LYS B NZ  
2695 N  N   . ALA B 99  ? 0.8042 0.7062 0.8603 -0.0111 0.0339  -0.0094 182 ALA B N   
2696 C  CA  . ALA B 99  ? 0.7743 0.6867 0.8386 -0.0018 0.0503  -0.0135 182 ALA B CA  
2697 C  C   . ALA B 99  ? 0.8039 0.6815 0.8256 0.0098  0.0570  -0.0188 182 ALA B C   
2698 O  O   . ALA B 99  ? 0.8136 0.6908 0.8372 0.0204  0.0666  -0.0214 182 ALA B O   
2699 C  CB  . ALA B 99  ? 0.7471 0.6851 0.8340 -0.0041 0.0690  -0.0098 182 ALA B CB  
2700 N  N   . GLU B 100 ? 0.8214 0.6667 0.8003 0.0099  0.0526  -0.0197 183 GLU B N   
2701 C  CA  . GLU B 100 ? 0.8964 0.6972 0.8217 0.0214  0.0561  -0.0265 183 GLU B CA  
2702 C  C   . GLU B 100 ? 0.9176 0.6960 0.8323 0.0193  0.0372  -0.0343 183 GLU B C   
2703 O  O   . GLU B 100 ? 0.9017 0.6513 0.7881 0.0310  0.0470  -0.0404 183 GLU B O   
2704 C  CB  . GLU B 100 ? 0.9433 0.7126 0.8198 0.0218  0.0508  -0.0260 183 GLU B CB  
2705 C  CG  . GLU B 100 ? 1.1654 0.8787 0.9727 0.0348  0.0533  -0.0344 183 GLU B CG  
2706 C  CD  . GLU B 100 ? 1.3347 1.0135 1.0904 0.0309  0.0305  -0.0368 183 GLU B CD  
2707 O  OE1 . GLU B 100 ? 1.3886 1.0912 1.1699 0.0176  0.0111  -0.0305 183 GLU B OE1 
2708 O  OE2 . GLU B 100 ? 1.4319 1.0585 1.1191 0.0426  0.0320  -0.0441 183 GLU B OE2 
2709 N  N   . VAL B 101 ? 0.9095 0.6987 0.8479 0.0054  0.0126  -0.0326 184 VAL B N   
2710 C  CA  . VAL B 101 ? 0.8773 0.6483 0.8163 0.0013  -0.0042 -0.0381 184 VAL B CA  
2711 C  C   . VAL B 101 ? 0.8423 0.6335 0.8133 0.0103  0.0112  -0.0375 184 VAL B C   
2712 O  O   . VAL B 101 ? 0.7819 0.5459 0.7354 0.0170  0.0137  -0.0438 184 VAL B O   
2713 C  CB  . VAL B 101 ? 0.7154 0.4986 0.6818 -0.0148 -0.0309 -0.0316 184 VAL B CB  
2714 C  CG1 . VAL B 101 ? 0.6415 0.4162 0.6274 -0.0194 -0.0431 -0.0335 184 VAL B CG1 
2715 C  CG2 . VAL B 101 ? 0.7194 0.4777 0.6487 -0.0224 -0.0510 -0.0323 184 VAL B CG2 
2716 N  N   . HIS B 102 ? 0.7580 0.5948 0.7732 0.0110  0.0212  -0.0299 185 HIS B N   
2717 C  CA  . HIS B 102 ? 0.7481 0.6093 0.7934 0.0211  0.0337  -0.0280 185 HIS B CA  
2718 C  C   . HIS B 102 ? 0.8192 0.6659 0.8418 0.0377  0.0558  -0.0307 185 HIS B C   
2719 O  O   . HIS B 102 ? 0.8457 0.6867 0.8709 0.0488  0.0631  -0.0312 185 HIS B O   
2720 C  CB  . HIS B 102 ? 0.7751 0.6835 0.8624 0.0178  0.0382  -0.0211 185 HIS B CB  
2721 C  CG  . HIS B 102 ? 0.7800 0.7037 0.8954 0.0106  0.0237  -0.0163 185 HIS B CG  
2722 N  ND1 . HIS B 102 ? 0.7007 0.6581 0.8465 0.0092  0.0255  -0.0118 185 HIS B ND1 
2723 C  CD2 . HIS B 102 ? 0.6950 0.6022 0.8119 0.0053  0.0083  -0.0140 185 HIS B CD2 
2724 C  CE1 . HIS B 102 ? 0.6289 0.5864 0.7882 0.0063  0.0146  -0.0065 185 HIS B CE1 
2725 N  NE2 . HIS B 102 ? 0.6196 0.5500 0.7668 0.0038  0.0051  -0.0063 185 HIS B NE2 
2726 N  N   . SER B 103 ? 0.8211 0.6598 0.8209 0.0420  0.0700  -0.0302 186 SER B N   
2727 C  CA  . SER B 103 ? 0.8205 0.6442 0.7991 0.0610  0.0960  -0.0290 186 SER B CA  
2728 C  C   . SER B 103 ? 0.8843 0.6463 0.8056 0.0690  0.0949  -0.0381 186 SER B C   
2729 O  O   . SER B 103 ? 0.9357 0.6834 0.8464 0.0862  0.1140  -0.0368 186 SER B O   
2730 C  CB  . SER B 103 ? 0.8438 0.6702 0.8118 0.0647  0.1141  -0.0239 186 SER B CB  
2731 O  OG  . SER B 103 ? 0.9436 0.7476 0.8851 0.0858  0.1424  -0.0201 186 SER B OG  
2732 N  N   . ASP B 104 ? 0.8889 0.6126 0.7721 0.0566  0.0720  -0.0468 187 ASP B N   
2733 C  CA  . ASP B 104 ? 1.0153 0.6731 0.8373 0.0605  0.0666  -0.0583 187 ASP B CA  
2734 C  C   . ASP B 104 ? 1.0549 0.7050 0.8938 0.0589  0.0596  -0.0616 187 ASP B C   
2735 O  O   . ASP B 104 ? 1.1505 0.7506 0.9470 0.0695  0.0693  -0.0686 187 ASP B O   
2736 C  CB  . ASP B 104 ? 1.1074 0.7310 0.8886 0.0450  0.0379  -0.0664 187 ASP B CB  
2737 C  CG  . ASP B 104 ? 1.3151 0.9271 1.0586 0.0525  0.0489  -0.0641 187 ASP B CG  
2738 O  OD1 . ASP B 104 ? 1.3842 0.9929 1.1146 0.0401  0.0266  -0.0648 187 ASP B OD1 
2739 O  OD2 . ASP B 104 ? 1.4384 1.0455 1.1674 0.0722  0.0814  -0.0593 187 ASP B OD2 
2740 N  N   . LYS B 105 ? 1.0223 0.7160 0.9186 0.0474  0.0456  -0.0558 188 LYS B N   
2741 C  CA  . LYS B 105 ? 0.9876 0.6743 0.9033 0.0462  0.0399  -0.0567 188 LYS B CA  
2742 C  C   . LYS B 105 ? 0.9327 0.6501 0.8799 0.0655  0.0647  -0.0482 188 LYS B C   
2743 O  O   . LYS B 105 ? 0.9942 0.6936 0.9434 0.0718  0.0689  -0.0487 188 LYS B O   
2744 C  CB  . LYS B 105 ? 0.9213 0.6348 0.8805 0.0271  0.0143  -0.0520 188 LYS B CB  
2745 C  CG  . LYS B 105 ? 0.9134 0.6011 0.8494 0.0075  -0.0140 -0.0574 188 LYS B CG  
2746 C  CD  . LYS B 105 ? 0.9012 0.5671 0.8505 -0.0072 -0.0359 -0.0591 188 LYS B CD  
2747 C  CE  . LYS B 105 ? 1.0068 0.6520 0.9382 -0.0279 -0.0684 -0.0628 188 LYS B CE  
2748 N  NZ  . LYS B 105 ? 1.1778 0.7563 1.0393 -0.0308 -0.0781 -0.0798 188 LYS B NZ  
2749 N  N   . ALA B 106 ? 0.9172 0.6806 0.8906 0.0748  0.0806  -0.0395 189 ALA B N   
2750 C  CA  . ALA B 106 ? 0.8884 0.6886 0.8958 0.0931  0.1008  -0.0294 189 ALA B CA  
2751 C  C   . ALA B 106 ? 0.9507 0.7182 0.9215 0.1152  0.1290  -0.0283 189 ALA B C   
2752 O  O   . ALA B 106 ? 1.0147 0.7997 0.9878 0.1264  0.1489  -0.0210 189 ALA B O   
2753 C  CB  . ALA B 106 ? 0.8453 0.7091 0.8998 0.0903  0.1018  -0.0207 189 ALA B CB  
2754 N  N   . ARG B 107 ? 0.9288 0.6452 0.8661 0.1220  0.1331  -0.0341 190 ARG B N   
2755 C  CA  . ARG B 107 ? 0.9481 0.6186 0.8397 0.1448  0.1620  -0.0335 190 ARG B CA  
2756 C  C   . ARG B 107 ? 1.0322 0.6839 0.9261 0.1574  0.1719  -0.0314 190 ARG B C   
2757 O  O   . ARG B 107 ? 1.0716 0.7208 0.9827 0.1434  0.1518  -0.0359 190 ARG B O   
2758 C  CB  . ARG B 107 ? 0.9904 0.5852 0.8060 0.1388  0.1571  -0.0484 190 ARG B CB  
2759 C  CG  . ARG B 107 ? 0.8834 0.4338 0.6755 0.1155  0.1253  -0.0639 190 ARG B CG  
2760 C  CD  . ARG B 107 ? 1.0167 0.4944 0.7298 0.1090  0.1158  -0.0792 190 ARG B CD  
2761 N  NE  . ARG B 107 ? 1.1201 0.5432 0.8046 0.0897  0.0889  -0.0943 190 ARG B NE  
2762 C  CZ  . ARG B 107 ? 1.2408 0.5924 0.8524 0.0803  0.0726  -0.1107 190 ARG B CZ  
2763 N  NH1 . ARG B 107 ? 1.2351 0.5423 0.8308 0.0592  0.0450  -0.1238 190 ARG B NH1 
2764 N  NH2 . ARG B 107 ? 1.4090 0.7323 0.9633 0.0920  0.0834  -0.1135 190 ARG B NH2 
2765 N  N   . PRO B 108 ? 0.9929 0.6310 0.8717 0.1857  0.2056  -0.0220 191 PRO B N   
2766 C  CA  . PRO B 108 ? 0.9471 0.5858 0.8087 0.2069  0.2359  -0.0120 191 PRO B CA  
2767 C  C   . PRO B 108 ? 0.9258 0.6541 0.8587 0.2131  0.2423  0.0063  191 PRO B C   
2768 O  O   . PRO B 108 ? 0.9666 0.7507 0.9546 0.2082  0.2284  0.0121  191 PRO B O   
2769 C  CB  . PRO B 108 ? 0.9763 0.5658 0.8013 0.2358  0.2695  -0.0063 191 PRO B CB  
2770 C  CG  . PRO B 108 ? 0.9518 0.5211 0.7816 0.2283  0.2557  -0.0133 191 PRO B CG  
2771 C  CD  . PRO B 108 ? 0.9731 0.5974 0.8572 0.2017  0.2198  -0.0166 191 PRO B CD  
2772 N  N   . THR B 109 ? 0.9058 0.6448 0.8362 0.2237  0.2631  0.0157  192 THR B N   
2773 C  CA  . THR B 109 ? 0.8510 0.6736 0.8520 0.2259  0.2681  0.0330  192 THR B CA  
2774 C  C   . THR B 109 ? 0.8880 0.7169 0.8931 0.2577  0.3101  0.0543  192 THR B C   
2775 O  O   . THR B 109 ? 0.9757 0.7632 0.9379 0.2673  0.3323  0.0558  192 THR B O   
2776 C  CB  . THR B 109 ? 0.8613 0.7026 0.8721 0.2024  0.2507  0.0267  192 THR B CB  
2777 O  OG1 . THR B 109 ? 0.8838 0.7154 0.8884 0.1757  0.2147  0.0097  192 THR B OG1 
2778 C  CG2 . THR B 109 ? 0.7057 0.6318 0.7933 0.1997  0.2522  0.0427  192 THR B CG2 
2779 N  N   . PRO B 110 ? 0.8932 0.7726 0.9480 0.2771  0.3236  0.0732  193 PRO B N   
2780 C  CA  . PRO B 110 ? 0.8660 0.7942 0.9677 0.2728  0.3021  0.0750  193 PRO B CA  
2781 C  C   . PRO B 110 ? 0.9280 0.7958 0.9836 0.2737  0.2954  0.0610  193 PRO B C   
2782 O  O   . PRO B 110 ? 1.0295 0.8185 1.0184 0.2814  0.3114  0.0523  193 PRO B O   
2783 C  CB  . PRO B 110 ? 0.8421 0.8283 0.9956 0.3019  0.3282  0.1033  193 PRO B CB  
2784 C  CG  . PRO B 110 ? 0.7799 0.7166 0.8911 0.3281  0.3707  0.1143  193 PRO B CG  
2785 C  CD  . PRO B 110 ? 0.8011 0.6934 0.8687 0.3097  0.3659  0.0986  193 PRO B CD  
2786 N  N   . PRO B 111 ? 0.8970 0.7971 0.9854 0.2660  0.2726  0.0592  194 PRO B N   
2787 C  CA  . PRO B 111 ? 0.8186 0.8025 0.9747 0.2579  0.2511  0.0674  194 PRO B CA  
2788 C  C   . PRO B 111 ? 0.7814 0.7773 0.9471 0.2246  0.2153  0.0513  194 PRO B C   
2789 O  O   . PRO B 111 ? 0.8709 0.9280 1.0841 0.2160  0.1966  0.0557  194 PRO B O   
2790 C  CB  . PRO B 111 ? 0.8634 0.8554 1.0304 0.2763  0.2535  0.0752  194 PRO B CB  
2791 C  CG  . PRO B 111 ? 0.8333 0.7413 0.9416 0.2726  0.2563  0.0597  194 PRO B CG  
2792 C  CD  . PRO B 111 ? 0.8711 0.7183 0.9260 0.2700  0.2717  0.0508  194 PRO B CD  
2793 N  N   . VAL B 112 ? 0.7871 0.7244 0.9070 0.2068  0.2052  0.0338  195 VAL B N   
2794 C  CA  . VAL B 112 ? 0.7679 0.7123 0.8955 0.1781  0.1737  0.0213  195 VAL B CA  
2795 C  C   . VAL B 112 ? 0.7350 0.7096 0.8797 0.1636  0.1690  0.0213  195 VAL B C   
2796 O  O   . VAL B 112 ? 0.7680 0.7119 0.8819 0.1644  0.1828  0.0191  195 VAL B O   
2797 C  CB  . VAL B 112 ? 0.7774 0.6533 0.8566 0.1643  0.1624  0.0054  195 VAL B CB  
2798 C  CG1 . VAL B 112 ? 0.7000 0.5907 0.7983 0.1403  0.1323  -0.0013 195 VAL B CG1 
2799 C  CG2 . VAL B 112 ? 0.7723 0.6055 0.8282 0.1805  0.1756  0.0059  195 VAL B CG2 
2800 N  N   . PHE B 113 ? 0.6854 0.7152 0.8750 0.1511  0.1508  0.0237  196 PHE B N   
2801 C  CA  . PHE B 113 ? 0.6808 0.7382 0.8902 0.1334  0.1439  0.0226  196 PHE B CA  
2802 C  C   . PHE B 113 ? 0.7012 0.7592 0.9126 0.1101  0.1164  0.0122  196 PHE B C   
2803 O  O   . PHE B 113 ? 0.7878 0.8375 0.9963 0.1096  0.1031  0.0092  196 PHE B O   
2804 C  CB  . PHE B 113 ? 0.6266 0.7513 0.8919 0.1389  0.1491  0.0367  196 PHE B CB  
2805 C  CG  . PHE B 113 ? 0.4906 0.6220 0.7629 0.1629  0.1800  0.0520  196 PHE B CG  
2806 C  CD1 . PHE B 113 ? 0.5123 0.6348 0.7796 0.1638  0.2008  0.0572  196 PHE B CD1 
2807 C  CD2 . PHE B 113 ? 0.5877 0.7334 0.8714 0.1875  0.1915  0.0640  196 PHE B CD2 
2808 C  CE1 . PHE B 113 ? 0.5434 0.6702 0.8175 0.1892  0.2337  0.0748  196 PHE B CE1 
2809 C  CE2 . PHE B 113 ? 0.5449 0.6967 0.8363 0.2126  0.2235  0.0816  196 PHE B CE2 
2810 C  CZ  . PHE B 113 ? 0.5518 0.6937 0.8386 0.2136  0.2453  0.0874  196 PHE B CZ  
2811 N  N   . VAL B 114 ? 0.6717 0.7380 0.8885 0.0925  0.1111  0.0089  197 VAL B N   
2812 C  CA  . VAL B 114 ? 0.7409 0.8064 0.9585 0.0721  0.0893  0.0015  197 VAL B CA  
2813 C  C   . VAL B 114 ? 0.7975 0.9011 1.0467 0.0580  0.0868  0.0035  197 VAL B C   
2814 O  O   . VAL B 114 ? 0.8152 0.9269 1.0723 0.0586  0.1029  0.0080  197 VAL B O   
2815 C  CB  . VAL B 114 ? 0.7727 0.7867 0.9478 0.0628  0.0843  -0.0066 197 VAL B CB  
2816 C  CG1 . VAL B 114 ? 0.8662 0.8565 1.0145 0.0658  0.1014  -0.0070 197 VAL B CG1 
2817 C  CG2 . VAL B 114 ? 0.7367 0.7537 0.9170 0.0439  0.0660  -0.0099 197 VAL B CG2 
2818 N  N   . GLU B 115 ? 0.7348 0.8582 1.0010 0.0461  0.0683  0.0007  198 GLU B N   
2819 C  CA  . GLU B 115 ? 0.6413 0.7950 0.9349 0.0296  0.0628  0.0002  198 GLU B CA  
2820 C  C   . GLU B 115 ? 0.6822 0.8139 0.9582 0.0130  0.0500  -0.0066 198 GLU B C   
2821 O  O   . GLU B 115 ? 0.7735 0.8857 1.0321 0.0157  0.0396  -0.0085 198 GLU B O   
2822 C  CB  . GLU B 115 ? 0.6038 0.8055 0.9350 0.0321  0.0520  0.0039  198 GLU B CB  
2823 C  CG  . GLU B 115 ? 0.6589 0.8932 1.0185 0.0486  0.0662  0.0151  198 GLU B CG  
2824 C  CD  . GLU B 115 ? 0.7206 1.0063 1.1182 0.0516  0.0507  0.0202  198 GLU B CD  
2825 O  OE1 . GLU B 115 ? 0.7162 1.0047 1.1089 0.0416  0.0284  0.0127  198 GLU B OE1 
2826 O  OE2 . GLU B 115 ? 0.7521 1.0741 1.1818 0.0657  0.0607  0.0327  198 GLU B OE2 
2827 N  N   . TRP B 116 ? 0.6449 0.7791 0.9275 -0.0028 0.0537  -0.0081 199 TRP B N   
2828 C  CA  . TRP B 116 ? 0.6173 0.7309 0.8843 -0.0177 0.0458  -0.0123 199 TRP B CA  
2829 C  C   . TRP B 116 ? 0.7020 0.8407 0.9943 -0.0333 0.0385  -0.0154 199 TRP B C   
2830 O  O   . TRP B 116 ? 0.7976 0.9569 1.1158 -0.0420 0.0477  -0.0136 199 TRP B O   
2831 C  CB  . TRP B 116 ? 0.6269 0.7112 0.8707 -0.0222 0.0581  -0.0112 199 TRP B CB  
2832 C  CG  . TRP B 116 ? 0.6385 0.6890 0.8493 -0.0138 0.0550  -0.0109 199 TRP B CG  
2833 C  CD1 . TRP B 116 ? 0.6136 0.6545 0.8138 0.0001  0.0550  -0.0110 199 TRP B CD1 
2834 C  CD2 . TRP B 116 ? 0.6849 0.7068 0.8714 -0.0197 0.0502  -0.0096 199 TRP B CD2 
2835 N  NE1 . TRP B 116 ? 0.5411 0.5483 0.7128 0.0001  0.0479  -0.0115 199 TRP B NE1 
2836 C  CE2 . TRP B 116 ? 0.6682 0.6670 0.8336 -0.0115 0.0439  -0.0096 199 TRP B CE2 
2837 C  CE3 . TRP B 116 ? 0.6753 0.6885 0.8567 -0.0310 0.0510  -0.0073 199 TRP B CE3 
2838 C  CZ2 . TRP B 116 ? 0.7513 0.7250 0.8965 -0.0155 0.0350  -0.0066 199 TRP B CZ2 
2839 C  CZ3 . TRP B 116 ? 0.7000 0.6881 0.8592 -0.0316 0.0455  -0.0026 199 TRP B CZ3 
2840 C  CH2 . TRP B 116 ? 0.7395 0.7112 0.8836 -0.0246 0.0358  -0.0020 199 TRP B CH2 
2841 N  N   . HIS B 117 ? 0.6523 0.7864 0.9362 -0.0369 0.0228  -0.0195 200 HIS B N   
2842 C  CA  . HIS B 117 ? 0.6721 0.8220 0.9706 -0.0524 0.0111  -0.0253 200 HIS B CA  
2843 C  C   . HIS B 117 ? 0.7159 0.8309 0.9897 -0.0664 0.0132  -0.0289 200 HIS B C   
2844 O  O   . HIS B 117 ? 0.7270 0.8114 0.9710 -0.0595 0.0123  -0.0269 200 HIS B O   
2845 C  CB  . HIS B 117 ? 0.6217 0.7859 0.9192 -0.0436 -0.0079 -0.0277 200 HIS B CB  
2846 C  CG  . HIS B 117 ? 0.5644 0.7685 0.8908 -0.0299 -0.0099 -0.0224 200 HIS B CG  
2847 N  ND1 . HIS B 117 ? 0.5637 0.7632 0.8833 -0.0090 -0.0005 -0.0158 200 HIS B ND1 
2848 C  CD2 . HIS B 117 ? 0.5941 0.8436 0.9580 -0.0338 -0.0196 -0.0212 200 HIS B CD2 
2849 C  CE1 . HIS B 117 ? 0.6073 0.8453 0.9556 0.0019  -0.0012 -0.0100 200 HIS B CE1 
2850 N  NE2 . HIS B 117 ? 0.6258 0.8984 1.0043 -0.0125 -0.0135 -0.0120 200 HIS B NE2 
2851 N  N   . PHE B 118 ? 0.7262 0.8456 1.0153 -0.0854 0.0181  -0.0323 201 PHE B N   
2852 C  CA  . PHE B 118 ? 0.6831 0.7673 0.9494 -0.0985 0.0251  -0.0345 201 PHE B CA  
2853 C  C   . PHE B 118 ? 0.7046 0.7848 0.9688 -0.1152 0.0102  -0.0448 201 PHE B C   
2854 O  O   . PHE B 118 ? 0.7296 0.8420 1.0271 -0.1279 -0.0003 -0.0498 201 PHE B O   
2855 C  CB  . PHE B 118 ? 0.6521 0.7340 0.9310 -0.1072 0.0461  -0.0302 201 PHE B CB  
2856 C  CG  . PHE B 118 ? 0.6549 0.7290 0.9217 -0.0911 0.0596  -0.0217 201 PHE B CG  
2857 C  CD1 . PHE B 118 ? 0.6193 0.6593 0.8522 -0.0852 0.0654  -0.0169 201 PHE B CD1 
2858 C  CD2 . PHE B 118 ? 0.6242 0.7233 0.9115 -0.0811 0.0659  -0.0178 201 PHE B CD2 
2859 C  CE1 . PHE B 118 ? 0.6293 0.6599 0.8472 -0.0723 0.0727  -0.0108 201 PHE B CE1 
2860 C  CE2 . PHE B 118 ? 0.5748 0.6576 0.8409 -0.0664 0.0769  -0.0123 201 PHE B CE2 
2861 C  CZ  . PHE B 118 ? 0.6063 0.6547 0.8367 -0.0633 0.0780  -0.0100 201 PHE B CZ  
2862 N  N   . LEU B 119 ? 0.6890 0.7281 0.9134 -0.1148 0.0090  -0.0469 202 LEU B N   
2863 C  CA  . LEU B 119 ? 0.6884 0.7092 0.8967 -0.1305 -0.0039 -0.0583 202 LEU B CA  
2864 C  C   . LEU B 119 ? 0.7277 0.7406 0.9508 -0.1560 0.0058  -0.0634 202 LEU B C   
2865 O  O   . LEU B 119 ? 0.8170 0.8336 1.0490 -0.1762 -0.0094 -0.0751 202 LEU B O   
2866 C  CB  . LEU B 119 ? 0.6971 0.6685 0.8533 -0.1191 -0.0016 -0.0565 202 LEU B CB  
2867 C  CG  . LEU B 119 ? 0.7910 0.7198 0.9110 -0.1336 -0.0065 -0.0674 202 LEU B CG  
2868 C  CD1 . LEU B 119 ? 0.8236 0.7691 0.9448 -0.1422 -0.0357 -0.0818 202 LEU B CD1 
2869 C  CD2 . LEU B 119 ? 0.8034 0.6807 0.8726 -0.1161 0.0055  -0.0591 202 LEU B CD2 
2870 N  N   . GLN B 120 ? 0.7233 0.7247 0.9491 -0.1556 0.0301  -0.0546 203 GLN B N   
2871 C  CA  . GLN B 120 ? 0.8049 0.7908 1.0402 -0.1766 0.0458  -0.0566 203 GLN B CA  
2872 C  C   . GLN B 120 ? 0.8414 0.8678 1.1273 -0.1817 0.0567  -0.0508 203 GLN B C   
2873 O  O   . GLN B 120 ? 0.8149 0.8581 1.1073 -0.1635 0.0660  -0.0409 203 GLN B O   
2874 C  CB  . GLN B 120 ? 0.8303 0.7697 1.0278 -0.1694 0.0691  -0.0478 203 GLN B CB  
2875 C  CG  . GLN B 120 ? 0.8696 0.7620 1.0180 -0.1658 0.0654  -0.0508 203 GLN B CG  
2876 C  CD  . GLN B 120 ? 0.8509 0.7198 0.9700 -0.1431 0.0796  -0.0350 203 GLN B CD  
2877 O  OE1 . GLN B 120 ? 0.8138 0.6901 0.9419 -0.1357 0.0946  -0.0235 203 GLN B OE1 
2878 N  NE2 . GLN B 120 ? 0.8834 0.7238 0.9675 -0.1312 0.0747  -0.0330 203 GLN B NE2 
2879 N  N   . ARG B 121 ? 0.8947 0.9334 1.2155 -0.2065 0.0565  -0.0563 204 ARG B N   
2880 C  CA  . ARG B 121 ? 0.9141 0.9914 1.2887 -0.2108 0.0711  -0.0475 204 ARG B CA  
2881 C  C   . ARG B 121 ? 0.8835 0.9377 1.2444 -0.1998 0.1046  -0.0350 204 ARG B C   
2882 O  O   . ARG B 121 ? 0.8453 0.9218 1.2239 -0.1848 0.1188  -0.0240 204 ARG B O   
2883 C  CB  . ARG B 121 ? 1.0452 1.1393 1.4657 -0.2427 0.0640  -0.0544 204 ARG B CB  
2884 C  CG  . ARG B 121 ? 1.1621 1.3138 1.6535 -0.2460 0.0701  -0.0435 204 ARG B CG  
2885 C  CD  . ARG B 121 ? 1.2771 1.4296 1.8132 -0.2732 0.0872  -0.0408 204 ARG B CD  
2886 N  NE  . ARG B 121 ? 1.3729 1.4807 1.8797 -0.2668 0.1232  -0.0331 204 ARG B NE  
2887 C  CZ  . ARG B 121 ? 1.4324 1.5116 1.9475 -0.2894 0.1403  -0.0346 204 ARG B CZ  
2888 N  NH1 . ARG B 121 ? 1.4523 1.5412 2.0054 -0.3232 0.1223  -0.0452 204 ARG B NH1 
2889 N  NH2 . ARG B 121 ? 1.4588 1.4983 1.9436 -0.2786 0.1744  -0.0252 204 ARG B NH2 
2890 N  N   . ILE B 122 ? 0.9331 0.9397 1.2582 -0.2052 0.1185  -0.0357 205 ILE B N   
2891 C  CA  . ILE B 122 ? 0.9197 0.9033 1.2290 -0.1943 0.1498  -0.0228 205 ILE B CA  
2892 C  C   . ILE B 122 ? 0.8214 0.8079 1.1045 -0.1656 0.1507  -0.0139 205 ILE B C   
2893 O  O   . ILE B 122 ? 0.7671 0.7567 1.0514 -0.1528 0.1701  -0.0033 205 ILE B O   
2894 C  CB  . ILE B 122 ? 1.0329 0.9637 1.3046 -0.2023 0.1634  -0.0237 205 ILE B CB  
2895 C  CG1 . ILE B 122 ? 1.0784 0.9850 1.3225 -0.1837 0.1916  -0.0081 205 ILE B CG1 
2896 C  CG2 . ILE B 122 ? 1.1029 1.0090 1.3346 -0.1994 0.1430  -0.0320 205 ILE B CG2 
2897 C  CD1 . ILE B 122 ? 1.2178 1.1342 1.4917 -0.1859 0.2192  0.0014  205 ILE B CD1 
2898 N  N   . VAL B 123 ? 0.8511 0.8339 1.1087 -0.1550 0.1297  -0.0180 206 VAL B N   
2899 C  CA  . VAL B 123 ? 0.7566 0.7418 0.9933 -0.1315 0.1268  -0.0108 206 VAL B CA  
2900 C  C   . VAL B 123 ? 0.7988 0.8215 1.0644 -0.1234 0.1231  -0.0102 206 VAL B C   
2901 O  O   . VAL B 123 ? 0.8273 0.8480 1.0797 -0.1067 0.1317  -0.0032 206 VAL B O   
2902 C  CB  . VAL B 123 ? 0.6534 0.6246 0.8622 -0.1233 0.1081  -0.0131 206 VAL B CB  
2903 C  CG1 . VAL B 123 ? 0.6259 0.5976 0.8175 -0.1027 0.1040  -0.0054 206 VAL B CG1 
2904 C  CG2 . VAL B 123 ? 0.6773 0.6087 0.8569 -0.1287 0.1162  -0.0109 206 VAL B CG2 
2905 N  N   . TYR B 124 ? 0.8294 0.8848 1.1321 -0.1342 0.1100  -0.0169 207 TYR B N   
2906 C  CA  . TYR B 124 ? 0.7769 0.8701 1.1101 -0.1242 0.1089  -0.0133 207 TYR B CA  
2907 C  C   . TYR B 124 ? 0.7754 0.8751 1.1287 -0.1210 0.1368  -0.0026 207 TYR B C   
2908 O  O   . TYR B 124 ? 0.8272 0.9317 1.1745 -0.1018 0.1467  0.0044  207 TYR B O   
2909 C  CB  . TYR B 124 ? 0.7901 0.9216 1.1633 -0.1366 0.0880  -0.0200 207 TYR B CB  
2910 C  CG  . TYR B 124 ? 0.8500 1.0269 1.2740 -0.1330 0.0956  -0.0115 207 TYR B CG  
2911 C  CD1 . TYR B 124 ? 0.8617 1.0542 1.2840 -0.1099 0.0973  -0.0052 207 TYR B CD1 
2912 C  CD2 . TYR B 124 ? 0.8801 1.0829 1.3560 -0.1526 0.1032  -0.0080 207 TYR B CD2 
2913 C  CE1 . TYR B 124 ? 0.8705 1.1025 1.3383 -0.1031 0.1084  0.0058  207 TYR B CE1 
2914 C  CE2 . TYR B 124 ? 0.8588 1.1069 1.3880 -0.1474 0.1128  0.0042  207 TYR B CE2 
2915 C  CZ  . TYR B 124 ? 0.8421 1.1043 1.3655 -0.1211 0.1165  0.0118  207 TYR B CZ  
2916 O  OH  . TYR B 124 ? 0.7909 1.0963 1.3662 -0.1125 0.1300  0.0270  207 TYR B OH  
2917 N  N   . GLU B 125 ? 0.7620 0.8572 1.1364 -0.1387 0.1519  -0.0007 208 GLU B N   
2918 C  CA  . GLU B 125 ? 0.7890 0.8922 1.1890 -0.1350 0.1819  0.0120  208 GLU B CA  
2919 C  C   . GLU B 125 ? 0.7593 0.8264 1.1093 -0.1124 0.2028  0.0203  208 GLU B C   
2920 O  O   . GLU B 125 ? 0.7653 0.8363 1.1179 -0.0957 0.2235  0.0309  208 GLU B O   
2921 C  CB  . GLU B 125 ? 0.8351 0.9375 1.2700 -0.1606 0.1944  0.0126  208 GLU B CB  
2922 C  CG  . GLU B 125 ? 0.9498 1.1025 1.4581 -0.1777 0.1893  0.0151  208 GLU B CG  
2923 C  CD  . GLU B 125 ? 1.1340 1.2852 1.6706 -0.2119 0.1788  0.0055  208 GLU B CD  
2924 O  OE1 . GLU B 125 ? 1.2129 1.3188 1.7151 -0.2203 0.1892  0.0011  208 GLU B OE1 
2925 O  OE2 . GLU B 125 ? 1.2030 1.3969 1.7952 -0.2304 0.1597  0.0026  208 GLU B OE2 
2926 N  N   . TYR B 126 ? 0.7305 0.7613 1.0327 -0.1100 0.1974  0.0169  209 TYR B N   
2927 C  CA  . TYR B 126 ? 0.7585 0.7572 1.0114 -0.0892 0.2108  0.0246  209 TYR B CA  
2928 C  C   . TYR B 126 ? 0.8152 0.8167 1.0450 -0.0696 0.1977  0.0230  209 TYR B C   
2929 O  O   . TYR B 126 ? 0.9053 0.8958 1.1154 -0.0518 0.2138  0.0299  209 TYR B O   
2930 C  CB  . TYR B 126 ? 0.7501 0.7156 0.9645 -0.0914 0.2063  0.0242  209 TYR B CB  
2931 C  CG  . TYR B 126 ? 0.7922 0.7300 0.9555 -0.0704 0.2100  0.0317  209 TYR B CG  
2932 C  CD1 . TYR B 126 ? 0.7900 0.7223 0.9259 -0.0615 0.1854  0.0285  209 TYR B CD1 
2933 C  CD2 . TYR B 126 ? 0.8167 0.7338 0.9598 -0.0593 0.2372  0.0426  209 TYR B CD2 
2934 C  CE1 . TYR B 126 ? 0.8169 0.7256 0.9083 -0.0453 0.1834  0.0347  209 TYR B CE1 
2935 C  CE2 . TYR B 126 ? 0.8502 0.7411 0.9415 -0.0399 0.2363  0.0488  209 TYR B CE2 
2936 C  CZ  . TYR B 126 ? 0.8708 0.7587 0.9374 -0.0345 0.2072  0.0441  209 TYR B CZ  
2937 O  OH  . TYR B 126 ? 0.9447 0.8081 0.9618 -0.0181 0.2011  0.0496  209 TYR B OH  
2938 N  N   . CYS B 127 ? 0.8024 0.8135 1.0306 -0.0717 0.1703  0.0142  210 CYS B N   
2939 C  CA  . CYS B 127 ? 0.7945 0.8016 0.9982 -0.0548 0.1575  0.0122  210 CYS B CA  
2940 C  C   . CYS B 127 ? 0.7703 0.7989 0.9957 -0.0441 0.1681  0.0151  210 CYS B C   
2941 O  O   . CYS B 127 ? 0.7609 0.7702 0.9542 -0.0259 0.1750  0.0176  210 CYS B O   
2942 C  CB  . CYS B 127 ? 0.7711 0.7846 0.9749 -0.0592 0.1299  0.0045  210 CYS B CB  
2943 S  SG  . CYS B 127 ? 0.7826 0.7666 0.9554 -0.0639 0.1200  0.0061  210 CYS B SG  
2944 N  N   . ALA B 128 ? 0.6935 0.7604 0.9719 -0.0547 0.1692  0.0157  211 ALA B N   
2945 C  CA  . ALA B 128 ? 0.6127 0.7064 0.9193 -0.0427 0.1801  0.0224  211 ALA B CA  
2946 C  C   . ALA B 128 ? 0.7419 0.8176 1.0355 -0.0275 0.2135  0.0346  211 ALA B C   
2947 O  O   . ALA B 128 ? 0.8541 0.9245 1.1343 -0.0067 0.2258  0.0403  211 ALA B O   
2948 C  CB  . ALA B 128 ? 0.5239 0.6674 0.8967 -0.0592 0.1733  0.0235  211 ALA B CB  
2949 N  N   . ALA B 129 ? 0.7779 0.8392 1.0711 -0.0354 0.2314  0.0397  212 ALA B N   
2950 C  CA  . ALA B 129 ? 0.7849 0.8224 1.0576 -0.0175 0.2658  0.0527  212 ALA B CA  
2951 C  C   . ALA B 129 ? 0.8670 0.8542 1.0611 0.0029  0.2639  0.0494  212 ALA B C   
2952 O  O   . ALA B 129 ? 0.9048 0.8678 1.0672 0.0256  0.2864  0.0573  212 ALA B O   
2953 C  CB  . ALA B 129 ? 0.7356 0.7694 1.0294 -0.0309 0.2871  0.0601  212 ALA B CB  
2954 N  N   . GLU B 130 ? 0.8293 0.7990 0.9906 -0.0044 0.2370  0.0387  213 GLU B N   
2955 C  CA  . GLU B 130 ? 0.8595 0.7863 0.9519 0.0112  0.2277  0.0349  213 GLU B CA  
2956 C  C   . GLU B 130 ? 0.8863 0.8070 0.9604 0.0253  0.2190  0.0298  213 GLU B C   
2957 O  O   . GLU B 130 ? 0.9427 0.8236 0.9608 0.0440  0.2258  0.0299  213 GLU B O   
2958 C  CB  . GLU B 130 ? 0.9071 0.8253 0.9828 -0.0011 0.2002  0.0282  213 GLU B CB  
2959 C  CG  . GLU B 130 ? 1.0051 0.9174 1.0843 -0.0108 0.2115  0.0345  213 GLU B CG  
2960 C  CD  . GLU B 130 ? 1.0949 0.9743 1.1328 0.0057  0.2371  0.0446  213 GLU B CD  
2961 O  OE1 . GLU B 130 ? 1.0883 0.9365 1.0702 0.0221  0.2298  0.0436  213 GLU B OE1 
2962 O  OE2 . GLU B 130 ? 1.0913 0.9736 1.1509 0.0022  0.2644  0.0536  213 GLU B OE2 
2963 N  N   . TYR B 131 ? 0.8467 0.8021 0.9626 0.0176  0.2043  0.0249  214 TYR B N   
2964 C  CA  . TYR B 131 ? 0.7656 0.7148 0.8669 0.0318  0.1990  0.0213  214 TYR B CA  
2965 C  C   . TYR B 131 ? 0.8283 0.7729 0.9287 0.0523  0.2321  0.0324  214 TYR B C   
2966 O  O   . TYR B 131 ? 0.8627 0.7728 0.9173 0.0715  0.2378  0.0308  214 TYR B O   
2967 C  CB  . TYR B 131 ? 0.6524 0.6420 0.8003 0.0213  0.1787  0.0164  214 TYR B CB  
2968 C  CG  . TYR B 131 ? 0.6253 0.6186 0.7761 0.0037  0.1509  0.0082  214 TYR B CG  
2969 C  CD1 . TYR B 131 ? 0.6544 0.6130 0.7616 0.0021  0.1389  0.0048  214 TYR B CD1 
2970 C  CD2 . TYR B 131 ? 0.6353 0.6658 0.8311 -0.0095 0.1370  0.0057  214 TYR B CD2 
2971 C  CE1 . TYR B 131 ? 0.6399 0.6025 0.7532 -0.0110 0.1177  0.0015  214 TYR B CE1 
2972 C  CE2 . TYR B 131 ? 0.5971 0.6248 0.7902 -0.0219 0.1160  0.0002  214 TYR B CE2 
2973 C  CZ  . TYR B 131 ? 0.6207 0.6152 0.7749 -0.0219 0.1084  -0.0006 214 TYR B CZ  
2974 O  OH  . TYR B 131 ? 0.6675 0.6598 0.8224 -0.0314 0.0916  -0.0021 214 TYR B OH  
2975 N  N   . LEU B 132 ? 0.8402 0.8169 0.9913 0.0487  0.2554  0.0448  215 LEU B N   
2976 C  CA  . LEU B 132 ? 0.9221 0.8951 1.0774 0.0703  0.2926  0.0604  215 LEU B CA  
2977 C  C   . LEU B 132 ? 1.0406 0.9521 1.1205 0.0901  0.3130  0.0632  215 LEU B C   
2978 O  O   . LEU B 132 ? 0.9664 0.8468 1.0091 0.1161  0.3368  0.0702  215 LEU B O   
2979 C  CB  . LEU B 132 ? 0.9430 0.9658 1.1768 0.0585  0.3119  0.0749  215 LEU B CB  
2980 C  CG  . LEU B 132 ? 0.9410 1.0260 1.2507 0.0510  0.3044  0.0802  215 LEU B CG  
2981 C  CD1 . LEU B 132 ? 0.9017 1.0347 1.2879 0.0261  0.3064  0.0871  215 LEU B CD1 
2982 C  CD2 . LEU B 132 ? 1.0511 1.1388 1.3660 0.0794  0.3335  0.0966  215 LEU B CD2 
2983 N  N   . ARG B 133 ? 1.1441 1.0343 1.1958 0.0804  0.3047  0.0587  216 ARG B N   
2984 C  CA  . ARG B 133 ? 1.1845 1.0159 1.1587 0.0998  0.3196  0.0610  216 ARG B CA  
2985 C  C   . ARG B 133 ? 1.1796 0.9627 1.0783 0.1117  0.2978  0.0474  216 ARG B C   
2986 O  O   . ARG B 133 ? 1.2595 0.9889 1.0883 0.1355  0.3145  0.0496  216 ARG B O   
2987 C  CB  . ARG B 133 ? 1.1874 1.0127 1.1538 0.0866  0.3138  0.0611  216 ARG B CB  
2988 C  CG  . ARG B 133 ? 1.3054 1.0742 1.1946 0.1080  0.3308  0.0665  216 ARG B CG  
2989 C  CD  . ARG B 133 ? 1.3927 1.1660 1.2954 0.0990  0.3426  0.0750  216 ARG B CD  
2990 N  NE  . ARG B 133 ? 1.4952 1.2365 1.3378 0.0994  0.3183  0.0687  216 ARG B NE  
2991 C  CZ  . ARG B 133 ? 1.4780 1.2392 1.3423 0.0784  0.2927  0.0637  216 ARG B CZ  
2992 N  NH1 . ARG B 133 ? 1.4197 1.2259 1.3557 0.0553  0.2876  0.0617  216 ARG B NH1 
2993 N  NH2 . ARG B 133 ? 1.5607 1.2955 1.3730 0.0817  0.2722  0.0620  216 ARG B NH2 
2994 N  N   . MSE B 134 ? 1.0633 0.8608 0.9729 0.0958  0.2613  0.0336  217 MSE B N   
2995 C  CA  . MSE B 134 ? 1.1029 0.8569 0.9503 0.1023  0.2379  0.0202  217 MSE B CA  
2996 C  C   . MSE B 134 ? 1.1201 0.8684 0.9670 0.1174  0.2500  0.0200  217 MSE B C   
2997 O  O   . MSE B 134 ? 1.0750 0.7795 0.8670 0.1251  0.2367  0.0090  217 MSE B O   
2998 C  CB  . MSE B 134 ? 1.0702 0.8409 0.9333 0.0793  0.1965  0.0086  217 MSE B CB  
2999 C  CG  . MSE B 134 ? 1.1755 0.9204 0.9964 0.0732  0.1771  0.0058  217 MSE B CG  
3000 SE SE  . MSE B 134 ? 1.2061 0.9732 1.0536 0.0477  0.1290  -0.0032 217 MSE B SE  
3001 C  CE  . MSE B 134 ? 0.9863 0.8217 0.9283 0.0323  0.1378  0.0018  217 MSE B CE  
3002 N  N   . GLY B 135 ? 1.0944 0.8872 1.0044 0.1213  0.2748  0.0329  218 GLY B N   
3003 C  CA  . GLY B 135 ? 1.0679 0.8608 0.9839 0.1393  0.2918  0.0379  218 GLY B CA  
3004 C  C   . GLY B 135 ? 1.0136 0.8212 0.9455 0.1303  0.2635  0.0265  218 GLY B C   
3005 O  O   . GLY B 135 ? 1.0537 0.8271 0.9483 0.1469  0.2693  0.0233  218 GLY B O   
3006 N  N   . LEU B 136 ? 0.8971 0.7499 0.8799 0.1060  0.2354  0.0209  219 LEU B N   
3007 C  CA  . LEU B 136 ? 0.8756 0.7453 0.8783 0.0988  0.2110  0.0126  219 LEU B CA  
3008 C  C   . LEU B 136 ? 0.9434 0.8643 1.0079 0.1068  0.2266  0.0248  219 LEU B C   
3009 O  O   . LEU B 136 ? 1.0099 0.9871 1.1380 0.0922  0.2166  0.0283  219 LEU B O   
3010 C  CB  . LEU B 136 ? 0.8437 0.7356 0.8696 0.0736  0.1781  0.0041  219 LEU B CB  
3011 C  CG  . LEU B 136 ? 0.8585 0.7156 0.8401 0.0643  0.1638  -0.0022 219 LEU B CG  
3012 C  CD1 . LEU B 136 ? 0.7856 0.6690 0.7981 0.0425  0.1365  -0.0061 219 LEU B CD1 
3013 C  CD2 . LEU B 136 ? 0.8473 0.6432 0.7571 0.0737  0.1544  -0.0118 219 LEU B CD2 
3014 N  N   . ALA B 137 ? 0.9575 0.8559 0.9998 0.1317  0.2513  0.0318  220 ALA B N   
3015 C  CA  . ALA B 137 ? 0.8451 0.7933 0.9465 0.1442  0.2707  0.0484  220 ALA B CA  
3016 C  C   . ALA B 137 ? 0.8714 0.8585 1.0123 0.1365  0.2462  0.0442  220 ALA B C   
3017 O  O   . ALA B 137 ? 0.9435 0.9931 1.1519 0.1349  0.2472  0.0558  220 ALA B O   
3018 C  CB  . ALA B 137 ? 0.8124 0.7198 0.8734 0.1766  0.3070  0.0592  220 ALA B CB  
3019 N  N   . ASN B 138 ? 0.8757 0.8274 0.9769 0.1321  0.2238  0.0289  221 ASN B N   
3020 C  CA  . ASN B 138 ? 0.7830 0.7635 0.9144 0.1286  0.2040  0.0261  221 ASN B CA  
3021 C  C   . ASN B 138 ? 0.7477 0.7650 0.9151 0.1031  0.1737  0.0193  221 ASN B C   
3022 O  O   . ASN B 138 ? 0.7460 0.7812 0.9312 0.1003  0.1557  0.0162  221 ASN B O   
3023 C  CB  . ASN B 138 ? 0.8120 0.7351 0.8884 0.1361  0.1973  0.0149  221 ASN B CB  
3024 C  CG  . ASN B 138 ? 0.8337 0.7134 0.8665 0.1175  0.1731  -0.0012 221 ASN B CG  
3025 O  OD1 . ASN B 138 ? 0.8077 0.6863 0.8341 0.1056  0.1689  -0.0030 221 ASN B OD1 
3026 N  ND2 . ASN B 138 ? 0.8338 0.6785 0.8394 0.1153  0.1576  -0.0111 221 ASN B ND2 
3027 N  N   . LEU B 139 ? 0.7906 0.8153 0.9653 0.0868  0.1704  0.0178  222 LEU B N   
3028 C  CA  . LEU B 139 ? 0.6835 0.7335 0.8840 0.0638  0.1455  0.0117  222 LEU B CA  
3029 C  C   . LEU B 139 ? 0.6931 0.7930 0.9478 0.0535  0.1518  0.0200  222 LEU B C   
3030 O  O   . LEU B 139 ? 0.8331 0.9297 1.0899 0.0549  0.1727  0.0270  222 LEU B O   
3031 C  CB  . LEU B 139 ? 0.6472 0.6558 0.8051 0.0514  0.1341  0.0023  222 LEU B CB  
3032 C  CG  . LEU B 139 ? 0.6294 0.6504 0.8015 0.0318  0.1095  -0.0034 222 LEU B CG  
3033 C  CD1 . LEU B 139 ? 0.6142 0.5927 0.7440 0.0275  0.0939  -0.0104 222 LEU B CD1 
3034 C  CD2 . LEU B 139 ? 0.6061 0.6478 0.8018 0.0170  0.1138  -0.0006 222 LEU B CD2 
3035 N  N   . LYS B 140 ? 0.6662 0.8093 0.9632 0.0432  0.1334  0.0194  223 LYS B N   
3036 C  CA  . LYS B 140 ? 0.6558 0.8463 1.0067 0.0284  0.1321  0.0248  223 LYS B CA  
3037 C  C   . LYS B 140 ? 0.6811 0.8702 1.0313 0.0053  0.1089  0.0137  223 LYS B C   
3038 O  O   . LYS B 140 ? 0.7794 0.9573 1.1110 0.0045  0.0894  0.0060  223 LYS B O   
3039 C  CB  . LYS B 140 ? 0.6295 0.8740 1.0308 0.0365  0.1284  0.0344  223 LYS B CB  
3040 C  CG  . LYS B 140 ? 0.7346 1.0030 1.1676 0.0524  0.1572  0.0524  223 LYS B CG  
3041 C  CD  . LYS B 140 ? 0.7830 1.1085 1.2672 0.0627  0.1511  0.0644  223 LYS B CD  
3042 C  CE  . LYS B 140 ? 0.7991 1.1556 1.3256 0.0790  0.1819  0.0872  223 LYS B CE  
3043 N  NZ  . LYS B 140 ? 0.8330 1.2443 1.4059 0.0942  0.1773  0.1020  223 LYS B NZ  
3044 N  N   . ALA B 141 ? 0.6397 0.8366 1.0090 -0.0122 0.1140  0.0144  224 ALA B N   
3045 C  CA  . ALA B 141 ? 0.6113 0.8019 0.9778 -0.0338 0.0967  0.0050  224 ALA B CA  
3046 C  C   . ALA B 141 ? 0.6670 0.9031 1.0851 -0.0506 0.0839  0.0049  224 ALA B C   
3047 O  O   . ALA B 141 ? 0.6728 0.9454 1.1374 -0.0518 0.0950  0.0148  224 ALA B O   
3048 C  CB  . ALA B 141 ? 0.5932 0.7507 0.9365 -0.0425 0.1115  0.0048  224 ALA B CB  
3049 N  N   . PHE B 142 ? 0.6964 0.9290 1.1058 -0.0633 0.0602  -0.0055 225 PHE B N   
3050 C  CA  . PHE B 142 ? 0.6900 0.9580 1.1377 -0.0814 0.0412  -0.0093 225 PHE B CA  
3051 C  C   . PHE B 142 ? 0.7117 0.9486 1.1351 -0.1023 0.0303  -0.0210 225 PHE B C   
3052 O  O   . PHE B 142 ? 0.7475 0.9433 1.1245 -0.0970 0.0298  -0.0255 225 PHE B O   
3053 C  CB  . PHE B 142 ? 0.6523 0.9489 1.1081 -0.0701 0.0189  -0.0099 225 PHE B CB  
3054 C  CG  . PHE B 142 ? 0.7052 1.0332 1.1858 -0.0479 0.0304  0.0033  225 PHE B CG  
3055 C  CD1 . PHE B 142 ? 0.6988 1.0825 1.2393 -0.0505 0.0297  0.0140  225 PHE B CD1 
3056 C  CD2 . PHE B 142 ? 0.8014 1.1024 1.2468 -0.0243 0.0422  0.0061  225 PHE B CD2 
3057 C  CE1 . PHE B 142 ? 0.7944 1.2056 1.3570 -0.0266 0.0442  0.0292  225 PHE B CE1 
3058 C  CE2 . PHE B 142 ? 0.8558 1.1779 1.3177 -0.0023 0.0559  0.0183  225 PHE B CE2 
3059 C  CZ  . PHE B 142 ? 0.8464 1.2234 1.3659 -0.0016 0.0587  0.0308  225 PHE B CZ  
3060 N  N   . TRP B 143 ? 0.6834 0.9394 1.1404 -0.1262 0.0223  -0.0248 226 TRP B N   
3061 C  CA  . TRP B 143 ? 0.6492 0.8758 1.0823 -0.1467 0.0076  -0.0380 226 TRP B CA  
3062 C  C   . TRP B 143 ? 0.7048 0.9503 1.1371 -0.1479 -0.0248 -0.0461 226 TRP B C   
3063 O  O   . TRP B 143 ? 0.8022 1.0887 1.2782 -0.1625 -0.0422 -0.0474 226 TRP B O   
3064 C  CB  . TRP B 143 ? 0.5953 0.8240 1.0603 -0.1741 0.0163  -0.0393 226 TRP B CB  
3065 C  CG  . TRP B 143 ? 0.5976 0.7894 1.0336 -0.1960 0.0022  -0.0539 226 TRP B CG  
3066 C  CD1 . TRP B 143 ? 0.6941 0.8365 1.0691 -0.1890 -0.0015 -0.0611 226 TRP B CD1 
3067 C  CD2 . TRP B 143 ? 0.6726 0.8700 1.1378 -0.2279 -0.0088 -0.0623 226 TRP B CD2 
3068 N  NE1 . TRP B 143 ? 0.7246 0.8365 1.0820 -0.2123 -0.0118 -0.0738 226 TRP B NE1 
3069 C  CE2 . TRP B 143 ? 0.7320 0.8752 1.1426 -0.2381 -0.0181 -0.0764 226 TRP B CE2 
3070 C  CE3 . TRP B 143 ? 0.7090 0.9511 1.2433 -0.2494 -0.0110 -0.0582 226 TRP B CE3 
3071 C  CZ2 . TRP B 143 ? 0.7287 0.8546 1.1442 -0.2700 -0.0306 -0.0894 226 TRP B CZ2 
3072 C  CZ3 . TRP B 143 ? 0.7170 0.9479 1.2647 -0.2835 -0.0255 -0.0705 226 TRP B CZ3 
3073 C  CH2 . TRP B 143 ? 0.7406 0.9108 1.2255 -0.2941 -0.0358 -0.0874 226 TRP B CH2 
3074 N  N   . ASN B 144 ? 0.6629 0.8792 1.0465 -0.1317 -0.0334 -0.0502 227 ASN B N   
3075 C  CA  . ASN B 144 ? 0.6978 0.9256 1.0694 -0.1251 -0.0611 -0.0559 227 ASN B CA  
3076 C  C   . ASN B 144 ? 0.7329 0.9074 1.0486 -0.1313 -0.0706 -0.0675 227 ASN B C   
3077 O  O   . ASN B 144 ? 0.8525 0.9932 1.1257 -0.1122 -0.0647 -0.0649 227 ASN B O   
3078 C  CB  . ASN B 144 ? 0.7031 0.9432 1.0677 -0.0945 -0.0582 -0.0468 227 ASN B CB  
3079 C  CG  . ASN B 144 ? 0.7568 1.0264 1.1257 -0.0849 -0.0844 -0.0482 227 ASN B CG  
3080 O  OD1 . ASN B 144 ? 0.8087 1.1112 1.2063 -0.1011 -0.1059 -0.0527 227 ASN B OD1 
3081 N  ND2 . ASN B 144 ? 0.8367 1.0951 1.1781 -0.0586 -0.0834 -0.0434 227 ASN B ND2 
3082 N  N   . PRO B 145 ? 0.6722 0.8353 0.9868 -0.1574 -0.0836 -0.0793 228 PRO B N   
3083 C  CA  . PRO B 145 ? 0.7416 0.8448 0.9954 -0.1620 -0.0888 -0.0901 228 PRO B CA  
3084 C  C   . PRO B 145 ? 0.8144 0.9113 1.0325 -0.1493 -0.1156 -0.0967 228 PRO B C   
3085 O  O   . PRO B 145 ? 0.8360 0.9779 1.0815 -0.1499 -0.1401 -0.0986 228 PRO B O   
3086 C  CB  . PRO B 145 ? 0.7411 0.8334 1.0087 -0.1966 -0.0930 -0.1012 228 PRO B CB  
3087 C  CG  . PRO B 145 ? 0.7204 0.8795 1.0575 -0.2103 -0.1083 -0.0992 228 PRO B CG  
3088 C  CD  . PRO B 145 ? 0.6838 0.8845 1.0535 -0.1849 -0.0921 -0.0823 228 PRO B CD  
3089 N  N   . MSE B 146 ? 0.8887 0.9285 1.0444 -0.1357 -0.1092 -0.0981 229 MSE B N   
3090 C  CA  . MSE B 146 ? 0.9806 1.0012 1.0894 -0.1176 -0.1282 -0.1021 229 MSE B CA  
3091 C  C   . MSE B 146 ? 1.0754 1.0658 1.1468 -0.1377 -0.1546 -0.1209 229 MSE B C   
3092 O  O   . MSE B 146 ? 1.1121 1.0615 1.1643 -0.1594 -0.1475 -0.1298 229 MSE B O   
3093 C  CB  . MSE B 146 ? 1.0544 1.0249 1.1142 -0.0912 -0.1057 -0.0917 229 MSE B CB  
3094 C  CG  . MSE B 146 ? 1.1389 1.1118 1.1759 -0.0603 -0.1130 -0.0847 229 MSE B CG  
3095 SE SE  . MSE B 146 ? 1.2609 1.1781 1.2550 -0.0284 -0.0802 -0.0658 229 MSE B SE  
3096 C  CE  . MSE B 146 ? 1.2650 1.1056 1.1999 -0.0443 -0.0688 -0.0739 229 MSE B CE  
3097 N  N   . PRO B 147 ? 1.1338 1.1402 1.1903 -0.1298 -0.1853 -0.1271 230 PRO B N   
3098 C  CA  . PRO B 147 ? 1.2145 1.1830 1.2214 -0.1471 -0.2149 -0.1469 230 PRO B CA  
3099 C  C   . PRO B 147 ? 1.3751 1.2537 1.2984 -0.1380 -0.1968 -0.1510 230 PRO B C   
3100 O  O   . PRO B 147 ? 1.5596 1.4094 1.4461 -0.1053 -0.1765 -0.1381 230 PRO B O   
3101 C  CB  . PRO B 147 ? 1.2093 1.2098 1.2068 -0.1279 -0.2465 -0.1472 230 PRO B CB  
3102 C  CG  . PRO B 147 ? 1.1342 1.2094 1.2046 -0.1144 -0.2378 -0.1297 230 PRO B CG  
3103 C  CD  . PRO B 147 ? 1.1139 1.1743 1.1981 -0.1056 -0.1957 -0.1164 230 PRO B CD  
3104 N  N   . GLY B 148 ? 1.3750 1.2078 1.2704 -0.1670 -0.2023 -0.1675 231 GLY B N   
3105 C  CA  . GLY B 148 ? 1.3902 1.1326 1.2055 -0.1607 -0.1821 -0.1712 231 GLY B CA  
3106 C  C   . GLY B 148 ? 1.3324 1.0505 1.1634 -0.1744 -0.1466 -0.1651 231 GLY B C   
3107 O  O   . GLY B 148 ? 1.4301 1.0731 1.2008 -0.1800 -0.1328 -0.1719 231 GLY B O   
3108 N  N   . THR B 149 ? 1.2100 0.9856 1.1151 -0.1779 -0.1301 -0.1519 232 THR B N   
3109 C  CA  . THR B 149 ? 1.1960 0.9532 1.1174 -0.1894 -0.0974 -0.1448 232 THR B CA  
3110 C  C   . THR B 149 ? 1.1449 0.9022 1.0920 -0.2305 -0.1078 -0.1610 232 THR B C   
3111 O  O   . THR B 149 ? 1.2061 1.0005 1.1836 -0.2521 -0.1414 -0.1742 232 THR B O   
3112 C  CB  . THR B 149 ? 1.1514 0.9646 1.1345 -0.1761 -0.0770 -0.1251 232 THR B CB  
3113 O  OG1 . THR B 149 ? 1.1720 1.0536 1.2260 -0.1950 -0.0927 -0.1284 232 THR B OG1 
3114 C  CG2 . THR B 149 ? 1.0160 0.8414 0.9878 -0.1402 -0.0744 -0.1110 232 THR B CG2 
3115 N  N   . ASP B 150 ? 1.4106 1.2460 1.1857 -0.4512 -0.2479 0.0432  233 ASP B N   
3116 C  CA  . ASP B 150 ? 1.4438 1.3108 1.2571 -0.5227 -0.1873 -0.0040 233 ASP B CA  
3117 C  C   . ASP B 150 ? 1.4543 1.3238 1.2623 -0.4973 -0.1678 0.0139  233 ASP B C   
3118 O  O   . ASP B 150 ? 1.5581 1.5072 1.4110 -0.5463 -0.1244 -0.0288 233 ASP B O   
3119 C  CB  . ASP B 150 ? 1.6153 1.3149 1.4037 -0.5830 -0.1408 -0.0104 233 ASP B CB  
3120 C  CG  . ASP B 150 ? 1.8062 1.3006 1.5194 -0.5420 -0.1481 0.0585  233 ASP B CG  
3121 O  OD1 . ASP B 150 ? 1.9036 1.2837 1.5968 -0.5717 -0.1017 0.0684  233 ASP B OD1 
3122 O  OD2 . ASP B 150 ? 1.8752 1.3290 1.5497 -0.4789 -0.1999 0.1036  233 ASP B OD2 
3123 N  N   . GLU B 151 ? 1.4263 1.2098 1.1793 -0.4250 -0.1957 0.0734  234 GLU B N   
3124 C  CA  . GLU B 151 ? 1.3413 1.1384 1.0895 -0.3966 -0.1775 0.0886  234 GLU B CA  
3125 C  C   . GLU B 151 ? 1.2647 1.2780 1.0870 -0.3697 -0.1922 0.0650  234 GLU B C   
3126 O  O   . GLU B 151 ? 1.2859 1.3657 1.1418 -0.3791 -0.1582 0.0479  234 GLU B O   
3127 C  CB  . GLU B 151 ? 1.3058 0.9555 0.9718 -0.3302 -0.2018 0.1558  234 GLU B CB  
3128 C  CG  . GLU B 151 ? 1.4079 0.8511 1.0017 -0.3588 -0.1757 0.1863  234 GLU B CG  
3129 C  CD  . GLU B 151 ? 1.4381 0.8379 1.0163 -0.3851 -0.1248 0.1839  234 GLU B CD  
3130 O  OE1 . GLU B 151 ? 1.4817 0.7264 1.0057 -0.4168 -0.0988 0.2076  234 GLU B OE1 
3131 O  OE2 . GLU B 151 ? 1.4358 0.9586 1.0575 -0.3738 -0.1103 0.1606  234 GLU B OE2 
3132 N  N   . HIS B 152 ? 1.2120 1.3394 1.0627 -0.3361 -0.2420 0.0662  235 HIS B N   
3133 C  CA  . HIS B 152 ? 1.1774 1.5258 1.1066 -0.3111 -0.2593 0.0490  235 HIS B CA  
3134 C  C   . HIS B 152 ? 1.2402 1.7412 1.2460 -0.3913 -0.2264 -0.0183 235 HIS B C   
3135 O  O   . HIS B 152 ? 1.2310 1.8940 1.3047 -0.3865 -0.2161 -0.0356 235 HIS B O   
3136 C  CB  . HIS B 152 ? 1.1235 1.5525 1.0588 -0.2584 -0.3222 0.0713  235 HIS B CB  
3137 C  CG  . HIS B 152 ? 1.1153 1.7644 1.1279 -0.2168 -0.3462 0.0714  235 HIS B CG  
3138 N  ND1 . HIS B 152 ? 1.1472 1.8423 1.1871 -0.1681 -0.3300 0.0929  235 HIS B ND1 
3139 C  CD2 . HIS B 152 ? 1.1022 1.9415 1.1732 -0.2172 -0.3841 0.0555  235 HIS B CD2 
3140 C  CE1 . HIS B 152 ? 1.1146 2.0200 1.2330 -0.1359 -0.3566 0.0937  235 HIS B CE1 
3141 N  NE2 . HIS B 152 ? 1.0713 2.0713 1.2081 -0.1656 -0.3922 0.0725  235 HIS B NE2 
3142 N  N   . ASP B 153 ? 1.2891 1.7426 1.2879 -0.4665 -0.2065 -0.0572 236 ASP B N   
3143 C  CA  . ASP B 153 ? 1.3510 1.9364 1.4155 -0.5522 -0.1682 -0.1262 236 ASP B CA  
3144 C  C   . ASP B 153 ? 1.4565 2.0150 1.5342 -0.5845 -0.1087 -0.1437 236 ASP B C   
3145 O  O   . ASP B 153 ? 1.4620 2.1824 1.6102 -0.6286 -0.0838 -0.1911 236 ASP B O   
3146 C  CB  . ASP B 153 ? 1.3635 1.8756 1.4106 -0.6263 -0.1504 -0.1632 236 ASP B CB  
3147 C  CG  . ASP B 153 ? 1.3067 1.8281 1.3340 -0.5977 -0.2055 -0.1467 236 ASP B CG  
3148 O  OD1 . ASP B 153 ? 1.2682 1.6220 1.2423 -0.6063 -0.2026 -0.1319 236 ASP B OD1 
3149 O  OD2 . ASP B 153 ? 1.2615 1.9600 1.3286 -0.5663 -0.2511 -0.1460 236 ASP B OD2 
3150 N  N   . ASP B 154 ? 1.5188 1.8797 1.5287 -0.5656 -0.0859 -0.1057 237 ASP B N   
3151 C  CA  . ASP B 154 ? 1.5811 1.9083 1.5951 -0.5927 -0.0300 -0.1178 237 ASP B CA  
3152 C  C   . ASP B 154 ? 1.5648 2.0043 1.6145 -0.5322 -0.0384 -0.0993 237 ASP B C   
3153 O  O   . ASP B 154 ? 1.5841 2.0964 1.6778 -0.5624 0.0048  -0.1293 237 ASP B O   
3154 C  CB  . ASP B 154 ? 1.6405 1.7239 1.5660 -0.5951 -0.0045 -0.0791 237 ASP B CB  
3155 C  CG  . ASP B 154 ? 1.6724 1.6285 1.5631 -0.6374 -0.0006 -0.0817 237 ASP B CG  
3156 O  OD1 . ASP B 154 ? 1.6997 1.7512 1.6353 -0.6806 -0.0038 -0.1263 237 ASP B OD1 
3157 O  OD2 . ASP B 154 ? 1.6888 1.4513 1.5083 -0.6291 0.0074  -0.0382 237 ASP B OD2 
3158 N  N   . TYR B 155 ? 1.5779 2.0303 1.6119 -0.4470 -0.0893 -0.0503 238 TYR B N   
3159 C  CA  . TYR B 155 ? 1.6216 2.1649 1.6900 -0.3827 -0.0920 -0.0271 238 TYR B CA  
3160 C  C   . TYR B 155 ? 1.5941 2.3954 1.7745 -0.3944 -0.0957 -0.0653 238 TYR B C   
3161 O  O   . TYR B 155 ? 1.6191 2.5057 1.8522 -0.4006 -0.0588 -0.0821 238 TYR B O   
3162 C  CB  . TYR B 155 ? 1.6370 2.1241 1.6605 -0.2903 -0.1422 0.0346  238 TYR B CB  
3163 C  CG  . TYR B 155 ? 1.6391 2.2387 1.7106 -0.2169 -0.1470 0.0600  238 TYR B CG  
3164 C  CD1 . TYR B 155 ? 1.6095 2.3992 1.7534 -0.1708 -0.1900 0.0679  238 TYR B CD1 
3165 C  CD2 . TYR B 155 ? 1.6958 2.2106 1.7411 -0.1943 -0.1058 0.0780  238 TYR B CD2 
3166 C  CE1 . TYR B 155 ? 1.5934 2.4848 1.7895 -0.0994 -0.1902 0.0963  238 TYR B CE1 
3167 C  CE2 . TYR B 155 ? 1.6791 2.2896 1.7729 -0.1263 -0.1024 0.1010  238 TYR B CE2 
3168 C  CZ  . TYR B 155 ? 1.6365 2.4348 1.8093 -0.0766 -0.1439 0.1117  238 TYR B CZ  
3169 O  OH  . TYR B 155 ? 1.6565 2.5495 1.8859 -0.0048 -0.1365 0.1396  238 TYR B OH  
3170 N  N   . GLN B 156 ? 1.5365 2.4700 1.7553 -0.3992 -0.1400 -0.0784 239 GLN B N   
3171 C  CA  . GLN B 156 ? 1.5393 2.7332 1.8644 -0.4149 -0.1492 -0.1114 239 GLN B CA  
3172 C  C   . GLN B 156 ? 1.6273 2.8906 1.9975 -0.5144 -0.0963 -0.1801 239 GLN B C   
3173 O  O   . GLN B 156 ? 1.6232 3.1023 2.0855 -0.5331 -0.0926 -0.2093 239 GLN B O   
3174 C  CB  . GLN B 156 ? 1.4921 2.8071 1.8372 -0.4057 -0.2098 -0.1097 239 GLN B CB  
3175 C  CG  . GLN B 156 ? 1.5625 2.7706 1.8523 -0.4696 -0.2128 -0.1378 239 GLN B CG  
3176 C  CD  . GLN B 156 ? 1.5739 2.8471 1.8572 -0.4396 -0.2763 -0.1193 239 GLN B CD  
3177 O  OE1 . GLN B 156 ? 1.5671 2.9143 1.8663 -0.3575 -0.3208 -0.0718 239 GLN B OE1 
3178 N  NE2 . GLN B 156 ? 1.5743 2.8166 1.8343 -0.5066 -0.2772 -0.1566 239 GLN B NE2 
3179 N  N   . GLU B 157 ? 1.6696 2.7584 1.9799 -0.5786 -0.0543 -0.2045 240 GLU B N   
3180 C  CA  . GLU B 157 ? 1.6610 2.7941 2.0087 -0.6717 0.0053  -0.2681 240 GLU B CA  
3181 C  C   . GLU B 157 ? 1.6840 2.8505 2.0666 -0.6576 0.0469  -0.2673 240 GLU B C   
3182 O  O   . GLU B 157 ? 1.6629 3.0028 2.1269 -0.7015 0.0728  -0.3125 240 GLU B O   
3183 C  CB  . GLU B 157 ? 1.6594 2.5805 1.9336 -0.7354 0.0443  -0.2849 240 GLU B CB  
3184 C  CG  . GLU B 157 ? 1.6117 2.5595 1.8887 -0.7986 0.0351  -0.3253 240 GLU B CG  
3185 C  CD  . GLU B 157 ? 1.6446 2.4078 1.8727 -0.8732 0.0918  -0.3512 240 GLU B CD  
3186 O  OE1 . GLU B 157 ? 1.6744 2.3311 1.8812 -0.8907 0.1422  -0.3494 240 GLU B OE1 
3187 O  OE2 . GLU B 157 ? 1.6412 2.3636 1.8528 -0.9139 0.0883  -0.3718 240 GLU B OE2 
3188 N  N   . THR B 158 ? 1.7576 2.7627 2.0791 -0.5993 0.0555  -0.2174 241 THR B N   
3189 C  CA  . THR B 158 ? 1.8222 2.8345 2.1663 -0.5891 0.1018  -0.2174 241 THR B CA  
3190 C  C   . THR B 158 ? 1.9903 3.1787 2.4120 -0.5127 0.0781  -0.1919 241 THR B C   
3191 O  O   . THR B 158 ? 2.0271 3.3191 2.5141 -0.5214 0.1167  -0.2121 241 THR B O   
3192 C  CB  . THR B 158 ? 1.7316 2.4926 1.9713 -0.5694 0.1277  -0.1779 241 THR B CB  
3193 O  OG1 . THR B 158 ? 1.6521 2.3431 1.8449 -0.4791 0.0822  -0.1153 241 THR B OG1 
3194 C  CG2 . THR B 158 ? 1.6996 2.2845 1.8665 -0.6354 0.1461  -0.1906 241 THR B CG2 
3195 N  N   . ARG B 159 ? 2.1239 3.3512 2.5447 -0.4372 0.0185  -0.1468 242 ARG B N   
3196 C  CA  . ARG B 159 ? 2.0769 3.4842 2.5825 -0.3630 -0.0029 -0.1191 242 ARG B CA  
3197 C  C   . ARG B 159 ? 2.0938 3.7768 2.7139 -0.3949 -0.0231 -0.1552 242 ARG B C   
3198 O  O   . ARG B 159 ? 2.1116 3.9742 2.8235 -0.3448 -0.0313 -0.1373 242 ARG B O   
3199 C  CB  . ARG B 159 ? 1.9814 3.3272 2.4440 -0.2682 -0.0560 -0.0541 242 ARG B CB  
3200 C  CG  . ARG B 159 ? 1.8966 3.3548 2.4262 -0.1764 -0.0611 -0.0112 242 ARG B CG  
3201 C  CD  . ARG B 159 ? 1.8776 3.3132 2.4319 -0.1784 0.0058  -0.0210 242 ARG B CD  
3202 N  NE  . ARG B 159 ? 1.8041 3.3004 2.4087 -0.0843 0.0095  0.0258  242 ARG B NE  
3203 C  CZ  . ARG B 159 ? 1.7272 3.4441 2.4580 -0.0587 0.0185  0.0245  242 ARG B CZ  
3204 N  NH1 . ARG B 159 ? 1.7005 3.6067 2.5172 -0.1242 0.0213  -0.0234 242 ARG B NH1 
3205 N  NH2 . ARG B 159 ? 1.6996 3.4494 2.4734 0.0315  0.0273  0.0720  242 ARG B NH2 
3206 N  N   . ALA B 160 ? 2.1164 3.8399 2.7352 -0.4783 -0.0292 -0.2044 243 ALA B N   
3207 C  CA  . ALA B 160 ? 1.9741 3.9562 2.6948 -0.5319 -0.0375 -0.2505 243 ALA B CA  
3208 C  C   . ALA B 160 ? 1.9258 3.9427 2.6816 -0.6235 0.0281  -0.3153 243 ALA B C   
3209 O  O   . ALA B 160 ? 1.9378 4.1844 2.7887 -0.6671 0.0298  -0.3538 243 ALA B O   
3210 C  CB  . ALA B 160 ? 1.9597 3.9890 2.6617 -0.5744 -0.0826 -0.2710 243 ALA B CB  
3211 N  N   . LYS B 161 ? 2.6284 2.8738 2.1030 0.0083  0.8744  0.0572  244 LYS B N   
3212 C  CA  . LYS B 161 ? 2.4283 2.7743 1.9306 0.0243  0.8610  0.1472  244 LYS B CA  
3213 C  C   . LYS B 161 ? 2.6429 3.2277 2.2002 0.0015  0.9000  0.0923  244 LYS B C   
3214 O  O   . LYS B 161 ? 2.6618 3.3752 2.2403 0.0125  0.8955  0.1602  244 LYS B O   
3215 C  CB  . LYS B 161 ? 2.4030 2.8187 1.8452 0.0522  0.8400  0.2514  244 LYS B CB  
3216 C  CG  . LYS B 161 ? 2.2939 2.4731 1.6819 0.0785  0.7977  0.3202  244 LYS B CG  
3217 C  CD  . LYS B 161 ? 2.1759 2.1075 1.5994 0.0868  0.7661  0.3454  244 LYS B CD  
3218 C  CE  . LYS B 161 ? 2.1016 1.7822 1.4723 0.1051  0.7321  0.3772  244 LYS B CE  
3219 N  NZ  . LYS B 161 ? 2.1080 1.7692 1.4418 0.0878  0.7550  0.2847  244 LYS B NZ  
3220 N  N   . GLU B 162 ? 2.8895 3.5388 2.4695 -0.0297 0.9383  -0.0285 245 GLU B N   
3221 C  CA  . GLU B 162 ? 2.9519 3.7794 2.5951 -0.0528 0.9727  -0.0889 245 GLU B CA  
3222 C  C   . GLU B 162 ? 3.0879 3.7679 2.7971 -0.0615 0.9659  -0.1161 245 GLU B C   
3223 O  O   . GLU B 162 ? 3.0980 3.8983 2.8647 -0.0715 0.9822  -0.1283 245 GLU B O   
3224 C  CB  . GLU B 162 ? 2.9133 3.8929 2.5525 -0.0813 1.0152  -0.2057 245 GLU B CB  
3225 C  CG  . GLU B 162 ? 2.8694 4.0112 2.4909 -0.0631 0.9919  -0.1702 245 GLU B CG  
3226 C  CD  . GLU B 162 ? 2.8272 4.0710 2.4548 -0.0490 0.9801  -0.0728 245 GLU B CD  
3227 O  OE1 . GLU B 162 ? 2.8187 4.0346 2.3956 -0.0300 0.9588  0.0118  245 GLU B OE1 
3228 O  OE2 . GLU B 162 ? 2.8136 4.1603 2.4970 -0.0561 0.9853  -0.0794 245 GLU B OE2 
3229 N  N   . GLN B 163 ? 3.1364 3.5598 2.8383 -0.0578 0.9425  -0.1261 246 GLN B N   
3230 C  CA  . GLN B 163 ? 3.1017 3.3571 2.8616 -0.0612 0.9286  -0.1353 246 GLN B CA  
3231 C  C   . GLN B 163 ? 3.1006 3.2756 2.8746 -0.0327 0.8888  -0.0132 246 GLN B C   
3232 O  O   . GLN B 163 ? 3.1252 3.1706 2.9501 -0.0333 0.8750  -0.0088 246 GLN B O   
3233 C  CB  . GLN B 163 ? 3.1089 3.1160 2.8537 -0.0670 0.9172  -0.1892 246 GLN B CB  
3234 C  CG  . GLN B 163 ? 3.0828 2.9484 2.7536 -0.0441 0.8871  -0.1313 246 GLN B CG  
3235 C  CD  . GLN B 163 ? 3.0701 2.7107 2.7375 -0.0155 0.8376  -0.0301 246 GLN B CD  
3236 O  OE1 . GLN B 163 ? 3.0843 2.5416 2.7893 -0.0190 0.8241  -0.0488 246 GLN B OE1 
3237 N  NE2 . GLN B 163 ? 3.0570 2.7099 2.6791 0.0132  0.8100  0.0780  246 GLN B NE2 
3238 N  N   . GLU B 164 ? 3.1030 3.3491 2.8329 -0.0078 0.8696  0.0855  247 GLU B N   
3239 C  CA  . GLU B 164 ? 3.0033 3.2261 2.7490 0.0181  0.8367  0.2023  247 GLU B CA  
3240 C  C   . GLU B 164 ? 3.0193 3.5041 2.7969 0.0149  0.8582  0.2252  247 GLU B C   
3241 O  O   . GLU B 164 ? 2.9960 3.4794 2.8045 0.0307  0.8373  0.3064  247 GLU B O   
3242 C  CB  . GLU B 164 ? 2.8582 2.9794 2.5360 0.0500  0.7979  0.3062  247 GLU B CB  
3243 C  CG  . GLU B 164 ? 2.7534 2.7010 2.4446 0.0772  0.7514  0.4139  247 GLU B CG  
3244 C  CD  . GLU B 164 ? 2.6645 2.7604 2.3531 0.0985  0.7382  0.5207  247 GLU B CD  
3245 O  OE1 . GLU B 164 ? 2.6476 2.6163 2.3417 0.1228  0.6990  0.6178  247 GLU B OE1 
3246 O  OE2 . GLU B 164 ? 2.6175 2.9568 2.2985 0.0909  0.7669  0.5078  247 GLU B OE2 
3247 N  N   . GLU B 165 ? 3.0781 3.7855 2.8483 -0.0049 0.8991  0.1560  248 GLU B N   
3248 C  CA  . GLU B 165 ? 3.0133 3.9794 2.8170 -0.0120 0.9253  0.1603  248 GLU B CA  
3249 C  C   . GLU B 165 ? 3.0222 4.0682 2.8935 -0.0426 0.9617  0.0577  248 GLU B C   
3250 O  O   . GLU B 165 ? 3.0161 4.2090 2.9348 -0.0456 0.9739  0.0740  248 GLU B O   
3251 C  CB  . GLU B 165 ? 2.9749 4.1548 2.7264 -0.0131 0.9474  0.1554  248 GLU B CB  
3252 C  CG  . GLU B 165 ? 2.9164 4.3468 2.6880 -0.0109 0.9612  0.1954  248 GLU B CG  
3253 C  CD  . GLU B 165 ? 2.8760 4.2937 2.6203 0.0215  0.9207  0.3290  248 GLU B CD  
3254 O  OE1 . GLU B 165 ? 2.8773 4.0984 2.6178 0.0432  0.8872  0.4028  248 GLU B OE1 
3255 O  OE2 . GLU B 165 ? 2.8756 4.4097 2.6094 0.0221  0.8946  0.3448  248 GLU B OE2 
3256 N  N   . MSE B 166 ? 2.9490 3.9023 2.8257 -0.0650 0.9792  -0.0471 249 MSE B N   
3257 C  CA  . MSE B 166 ? 2.8129 3.8115 2.7543 -0.0939 1.0112  -0.1473 249 MSE B CA  
3258 C  C   . MSE B 166 ? 2.7911 3.5400 2.7731 -0.0926 0.9868  -0.1488 249 MSE B C   
3259 O  O   . MSE B 166 ? 2.8016 3.4299 2.7952 -0.1113 0.9973  -0.2373 249 MSE B O   
3260 C  CB  . MSE B 166 ? 2.6698 3.7475 2.5943 -0.1221 1.0501  -0.2697 249 MSE B CB  
3261 C  CG  . MSE B 166 ? 2.5190 3.6890 2.5069 -0.1509 1.0827  -0.3733 249 MSE B CG  
3262 SE SE  . MSE B 166 ? 2.4502 3.8763 2.4465 -0.1419 1.0616  -0.3714 249 MSE B SE  
3263 C  CE  . MSE B 166 ? 2.4479 3.8539 2.5045 -0.1728 1.0666  -0.4995 249 MSE B CE  
3264 N  N   . LYS B 167 ? 2.7300 3.4006 2.7330 -0.0700 0.9533  -0.0485 250 LYS B N   
3265 C  CA  . LYS B 167 ? 2.6399 3.0807 2.6843 -0.0663 0.9275  -0.0379 250 LYS B CA  
3266 C  C   . LYS B 167 ? 2.5765 3.0355 2.6611 -0.0477 0.9048  0.0604  250 LYS B C   
3267 O  O   . LYS B 167 ? 2.5920 3.0176 2.7415 -0.0570 0.9083  0.0396  250 LYS B O   
3268 C  CB  . LYS B 167 ? 2.6343 2.8160 2.6299 -0.0506 0.8920  -0.0091 250 LYS B CB  
3269 C  CG  . LYS B 167 ? 2.6150 2.5473 2.6507 -0.0502 0.8682  -0.0152 250 LYS B CG  
3270 C  CD  . LYS B 167 ? 2.5498 2.4755 2.6316 -0.0832 0.9020  -0.1439 250 LYS B CD  
3271 C  CE  . LYS B 167 ? 2.5047 2.1851 2.6283 -0.0830 0.8786  -0.1500 250 LYS B CE  
3272 N  NZ  . LYS B 167 ? 2.4661 2.1820 2.6565 -0.0795 0.8724  -0.1072 250 LYS B NZ  
3273 N  N   . ARG B 168 ? 2.5614 3.0736 2.6080 -0.0213 0.8815  0.1681  251 ARG B N   
3274 C  CA  . ARG B 168 ? 2.4030 2.9553 2.4844 -0.0030 0.8611  0.2657  251 ARG B CA  
3275 C  C   . ARG B 168 ? 2.4140 3.2431 2.5339 -0.0158 0.8965  0.2465  251 ARG B C   
3276 O  O   . ARG B 168 ? 2.3382 3.2090 2.5045 -0.0076 0.8875  0.3034  251 ARG B O   
3277 C  CB  . ARG B 168 ? 2.2196 2.7242 2.2453 0.0305  0.8221  0.3895  251 ARG B CB  
3278 C  CG  . ARG B 168 ? 2.1503 2.4132 2.1220 0.0438  0.7909  0.4063  251 ARG B CG  
3279 C  CD  . ARG B 168 ? 2.1147 2.2294 2.0685 0.0777  0.7402  0.5363  251 ARG B CD  
3280 N  NE  . ARG B 168 ? 2.1154 1.9862 2.0207 0.0905  0.7095  0.5508  251 ARG B NE  
3281 C  CZ  . ARG B 168 ? 2.1014 1.7401 2.0291 0.0871  0.6928  0.5223  251 ARG B CZ  
3282 N  NH1 . ARG B 168 ? 2.0846 1.7029 2.0831 0.0711  0.7037  0.4776  251 ARG B NH1 
3283 N  NH2 . ARG B 168 ? 2.0937 1.5203 1.9728 0.0999  0.6652  0.5385  251 ARG B NH2 
3284 N  N   . PHE B 169 ? 2.4665 3.4838 2.5683 -0.0355 0.9362  0.1683  252 PHE B N   
3285 C  CA  . PHE B 169 ? 2.4488 3.7371 2.5832 -0.0485 0.9721  0.1443  252 PHE B CA  
3286 C  C   . PHE B 169 ? 2.4834 3.7847 2.6957 -0.0710 0.9946  0.0722  252 PHE B C   
3287 O  O   . PHE B 169 ? 2.5294 3.6500 2.7647 -0.0823 0.9908  0.0151  252 PHE B O   
3288 C  CB  . PHE B 169 ? 2.4010 3.8744 2.4925 -0.0642 1.0080  0.0751  252 PHE B CB  
3289 C  CG  . PHE B 169 ? 2.3699 3.8595 2.4845 -0.0972 1.0454  -0.0621 252 PHE B CG  
3290 C  CD1 . PHE B 169 ? 2.3380 4.0262 2.4785 -0.1150 1.0752  -0.1299 252 PHE B CD1 
3291 C  CD2 . PHE B 169 ? 2.3727 3.6414 2.4805 -0.1053 1.0363  -0.1180 252 PHE B CD2 
3292 C  CE1 . PHE B 169 ? 2.3360 3.9930 2.4933 -0.1359 1.0861  -0.2418 252 PHE B CE1 
3293 C  CE2 . PHE B 169 ? 2.3612 3.6446 2.4903 -0.1356 1.0705  -0.2440 252 PHE B CE2 
3294 C  CZ  . PHE B 169 ? 2.3370 3.8304 2.4914 -0.1520 1.0990  -0.3070 252 PHE B CZ  
# 
