data_9C0N
# 
_entry.id   9C0N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9C0N         pdb_00009c0n 10.2210/pdb9c0n/pdb 
WWPDB D_1000284492 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.year'                    
5 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C0N 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-26 
_pdbx_database_status.SG_entry                        N 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matthias.fellner@otago.ac.nz 
_pdbx_contact_author.name_first         Matthias 
_pdbx_contact_author.name_last          Fellner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3192-6984 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fellner, M.'   1 0000-0003-3192-6984 
'Randall, G.T.' 2 0009-0007-5009-3056 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proteins 
_citation.journal_id_ASTM           PSFGEY 
_citation.journal_id_CSD            0867 
_citation.journal_id_ISSN           1097-0134 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            93 
_citation.language                  ? 
_citation.page_first                1009 
_citation.page_last                 1021 
_citation.title                     
'Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/prot.26785 
_citation.pdbx_database_id_PubMed   39726198 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fellner, M.'     1 ? 
primary 'Randall, G.'     2 ? 
primary 'Bitac, I.R.C.G.' 3 ? 
primary 'Warrender, A.K.' 4 ? 
primary 'Sethi, A.'       5 ? 
primary 'Jelinek, R.'     6 ? 
primary 'Kass, I.'        7 ? 
# 
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 'Alpha/beta fold hydrolase' 27686.197 1   3.1.1.1 'N-terminal GPG from expression tag' ? ? 
2 non-polymer syn 'CALCIUM ION'               40.078    4   ?       ?                                    ? ? 
3 water       nat water                       18.015    119 ?       ?                                    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carboxylesterase,Esterase/lipase family protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGMRIKTPSPSYLKGTNGHAILLLHSFTGTNRDVKHLAAELNDQGFSCYAPNYPGHGLLLKDFMTYNVDDWWEEVEKAY
QFLVNEGYESISATGVSLGGLMTLKLAQHYPLKRIAVMSAPKEKSDDGLIEHLVYYSQRMSNILNLDQQASSAQLAAIDD
YEGEITKFQHFIDDIMTNLNVIKMPANILFGGKDAPSYETSAHFIYEHLGSVDKELNGLKDSHHLMTHGEGRDILEENVI
RFFNALT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGMRIKTPSPSYLKGTNGHAILLLHSFTGTNRDVKHLAAELNDQGFSCYAPNYPGHGLLLKDFMTYNVDDWWEEVEKAY
QFLVNEGYESISATGVSLGGLMTLKLAQHYPLKRIAVMSAPKEKSDDGLIEHLVYYSQRMSNILNLDQQASSAQLAAIDD
YEGEITKFQHFIDDIMTNLNVIKMPANILFGGKDAPSYETSAHFIYEHLGSVDKELNGLKDSHHLMTHGEGRDILEENVI
RFFNALT
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION' CA  
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   MET n 
1 5   ARG n 
1 6   ILE n 
1 7   LYS n 
1 8   THR n 
1 9   PRO n 
1 10  SER n 
1 11  PRO n 
1 12  SER n 
1 13  TYR n 
1 14  LEU n 
1 15  LYS n 
1 16  GLY n 
1 17  THR n 
1 18  ASN n 
1 19  GLY n 
1 20  HIS n 
1 21  ALA n 
1 22  ILE n 
1 23  LEU n 
1 24  LEU n 
1 25  LEU n 
1 26  HIS n 
1 27  SER n 
1 28  PHE n 
1 29  THR n 
1 30  GLY n 
1 31  THR n 
1 32  ASN n 
1 33  ARG n 
1 34  ASP n 
1 35  VAL n 
1 36  LYS n 
1 37  HIS n 
1 38  LEU n 
1 39  ALA n 
1 40  ALA n 
1 41  GLU n 
1 42  LEU n 
1 43  ASN n 
1 44  ASP n 
1 45  GLN n 
1 46  GLY n 
1 47  PHE n 
1 48  SER n 
1 49  CYS n 
1 50  TYR n 
1 51  ALA n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  PRO n 
1 56  GLY n 
1 57  HIS n 
1 58  GLY n 
1 59  LEU n 
1 60  LEU n 
1 61  LEU n 
1 62  LYS n 
1 63  ASP n 
1 64  PHE n 
1 65  MET n 
1 66  THR n 
1 67  TYR n 
1 68  ASN n 
1 69  VAL n 
1 70  ASP n 
1 71  ASP n 
1 72  TRP n 
1 73  TRP n 
1 74  GLU n 
1 75  GLU n 
1 76  VAL n 
1 77  GLU n 
1 78  LYS n 
1 79  ALA n 
1 80  TYR n 
1 81  GLN n 
1 82  PHE n 
1 83  LEU n 
1 84  VAL n 
1 85  ASN n 
1 86  GLU n 
1 87  GLY n 
1 88  TYR n 
1 89  GLU n 
1 90  SER n 
1 91  ILE n 
1 92  SER n 
1 93  ALA n 
1 94  THR n 
1 95  GLY n 
1 96  VAL n 
1 97  SER n 
1 98  LEU n 
1 99  GLY n 
1 100 GLY n 
1 101 LEU n 
1 102 MET n 
1 103 THR n 
1 104 LEU n 
1 105 LYS n 
1 106 LEU n 
1 107 ALA n 
1 108 GLN n 
1 109 HIS n 
1 110 TYR n 
1 111 PRO n 
1 112 LEU n 
1 113 LYS n 
1 114 ARG n 
1 115 ILE n 
1 116 ALA n 
1 117 VAL n 
1 118 MET n 
1 119 SER n 
1 120 ALA n 
1 121 PRO n 
1 122 LYS n 
1 123 GLU n 
1 124 LYS n 
1 125 SER n 
1 126 ASP n 
1 127 ASP n 
1 128 GLY n 
1 129 LEU n 
1 130 ILE n 
1 131 GLU n 
1 132 HIS n 
1 133 LEU n 
1 134 VAL n 
1 135 TYR n 
1 136 TYR n 
1 137 SER n 
1 138 GLN n 
1 139 ARG n 
1 140 MET n 
1 141 SER n 
1 142 ASN n 
1 143 ILE n 
1 144 LEU n 
1 145 ASN n 
1 146 LEU n 
1 147 ASP n 
1 148 GLN n 
1 149 GLN n 
1 150 ALA n 
1 151 SER n 
1 152 SER n 
1 153 ALA n 
1 154 GLN n 
1 155 LEU n 
1 156 ALA n 
1 157 ALA n 
1 158 ILE n 
1 159 ASP n 
1 160 ASP n 
1 161 TYR n 
1 162 GLU n 
1 163 GLY n 
1 164 GLU n 
1 165 ILE n 
1 166 THR n 
1 167 LYS n 
1 168 PHE n 
1 169 GLN n 
1 170 HIS n 
1 171 PHE n 
1 172 ILE n 
1 173 ASP n 
1 174 ASP n 
1 175 ILE n 
1 176 MET n 
1 177 THR n 
1 178 ASN n 
1 179 LEU n 
1 180 ASN n 
1 181 VAL n 
1 182 ILE n 
1 183 LYS n 
1 184 MET n 
1 185 PRO n 
1 186 ALA n 
1 187 ASN n 
1 188 ILE n 
1 189 LEU n 
1 190 PHE n 
1 191 GLY n 
1 192 GLY n 
1 193 LYS n 
1 194 ASP n 
1 195 ALA n 
1 196 PRO n 
1 197 SER n 
1 198 TYR n 
1 199 GLU n 
1 200 THR n 
1 201 SER n 
1 202 ALA n 
1 203 HIS n 
1 204 PHE n 
1 205 ILE n 
1 206 TYR n 
1 207 GLU n 
1 208 HIS n 
1 209 LEU n 
1 210 GLY n 
1 211 SER n 
1 212 VAL n 
1 213 ASP n 
1 214 LYS n 
1 215 GLU n 
1 216 LEU n 
1 217 ASN n 
1 218 GLY n 
1 219 LEU n 
1 220 LYS n 
1 221 ASP n 
1 222 SER n 
1 223 HIS n 
1 224 HIS n 
1 225 LEU n 
1 226 MET n 
1 227 THR n 
1 228 HIS n 
1 229 GLY n 
1 230 GLU n 
1 231 GLY n 
1 232 ARG n 
1 233 ASP n 
1 234 ILE n 
1 235 LEU n 
1 236 GLU n 
1 237 GLU n 
1 238 ASN n 
1 239 VAL n 
1 240 ILE n 
1 241 ARG n 
1 242 PHE n 
1 243 PHE n 
1 244 ASN n 
1 245 ALA n 
1 246 LEU n 
1 247 THR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   247 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;est_2, est_1, BN1321_100022, C7M54_03125, DD547_00417, EP54_01625, EQ90_13375, FAF17_11905, GO814_02325, GO941_12735, GO942_04080, GQX37_00145, HMPREF3211_01442, NCTC10702_00834, NCTC13131_05910, SAMEA2078260_02464, SAMEA2078588_01365, SAMEA2080344_01425, SAMEA2081063_02567, SAMEA4008575_01596, SAMEA70146418_02725
;
_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      'Staphylococcus aureus USA300-CA-263' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1385529 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
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   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   PRO 2   -1  ?   ?   ?   A . n 
A 1 3   GLY 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   ?   ?   ?   A . n 
A 1 5   ARG 5   2   ?   ?   ?   A . n 
A 1 6   ILE 6   3   3   ILE ILE A . n 
A 1 7   LYS 7   4   4   LYS LYS A . n 
A 1 8   THR 8   5   5   THR THR A . n 
A 1 9   PRO 9   6   6   PRO PRO A . n 
A 1 10  SER 10  7   7   SER SER A . n 
A 1 11  PRO 11  8   8   PRO PRO A . n 
A 1 12  SER 12  9   9   SER SER A . n 
A 1 13  TYR 13  10  10  TYR TYR A . n 
A 1 14  LEU 14  11  11  LEU LEU A . n 
A 1 15  LYS 15  12  12  LYS LYS A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  THR 17  14  14  THR THR A . n 
A 1 18  ASN 18  15  15  ASN ASN A . n 
A 1 19  GLY 19  16  16  GLY GLY A . n 
A 1 20  HIS 20  17  17  HIS HIS A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  ILE 22  19  19  ILE ILE A . n 
A 1 23  LEU 23  20  20  LEU LEU A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  LEU 25  22  22  LEU LEU A . n 
A 1 26  HIS 26  23  23  HIS HIS A . n 
A 1 27  SER 27  24  24  SER SER A . n 
A 1 28  PHE 28  25  25  PHE PHE A . n 
A 1 29  THR 29  26  26  THR THR A . n 
A 1 30  GLY 30  27  27  GLY GLY A . n 
A 1 31  THR 31  28  28  THR THR A . n 
A 1 32  ASN 32  29  29  ASN ASN A . n 
A 1 33  ARG 33  30  30  ARG ARG A . n 
A 1 34  ASP 34  31  31  ASP ASP A . n 
A 1 35  VAL 35  32  32  VAL VAL A . n 
A 1 36  LYS 36  33  33  LYS LYS A . n 
A 1 37  HIS 37  34  34  HIS HIS A . n 
A 1 38  LEU 38  35  35  LEU LEU A . n 
A 1 39  ALA 39  36  36  ALA ALA A . n 
A 1 40  ALA 40  37  37  ALA ALA A . n 
A 1 41  GLU 41  38  38  GLU GLU A . n 
A 1 42  LEU 42  39  39  LEU LEU A . n 
A 1 43  ASN 43  40  40  ASN ASN A . n 
A 1 44  ASP 44  41  41  ASP ASP A . n 
A 1 45  GLN 45  42  42  GLN GLN A . n 
A 1 46  GLY 46  43  43  GLY GLY A . n 
A 1 47  PHE 47  44  44  PHE PHE A . n 
A 1 48  SER 48  45  45  SER SER A . n 
A 1 49  CYS 49  46  46  CYS CYS A . n 
A 1 50  TYR 50  47  47  TYR TYR A . n 
A 1 51  ALA 51  48  48  ALA ALA A . n 
A 1 52  PRO 52  49  49  PRO PRO A . n 
A 1 53  ASN 53  50  50  ASN ASN A . n 
A 1 54  TYR 54  51  51  TYR TYR A . n 
A 1 55  PRO 55  52  52  PRO PRO A . n 
A 1 56  GLY 56  53  53  GLY GLY A . n 
A 1 57  HIS 57  54  54  HIS HIS A . n 
A 1 58  GLY 58  55  55  GLY GLY A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  LEU 60  57  57  LEU LEU A . n 
A 1 61  LEU 61  58  58  LEU LEU A . n 
A 1 62  LYS 62  59  59  LYS LYS A . n 
A 1 63  ASP 63  60  60  ASP ASP A . n 
A 1 64  PHE 64  61  61  PHE PHE A . n 
A 1 65  MET 65  62  62  MET MET A . n 
A 1 66  THR 66  63  63  THR THR A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  ASN 68  65  65  ASN ASN A . n 
A 1 69  VAL 69  66  66  VAL VAL A . n 
A 1 70  ASP 70  67  67  ASP ASP A . n 
A 1 71  ASP 71  68  68  ASP ASP A . n 
A 1 72  TRP 72  69  69  TRP TRP A . n 
A 1 73  TRP 73  70  70  TRP TRP A . n 
A 1 74  GLU 74  71  71  GLU GLU A . n 
A 1 75  GLU 75  72  72  GLU GLU A . n 
A 1 76  VAL 76  73  73  VAL VAL A . n 
A 1 77  GLU 77  74  74  GLU GLU A . n 
A 1 78  LYS 78  75  75  LYS LYS A . n 
A 1 79  ALA 79  76  76  ALA ALA A . n 
A 1 80  TYR 80  77  77  TYR TYR A . n 
A 1 81  GLN 81  78  78  GLN GLN A . n 
A 1 82  PHE 82  79  79  PHE PHE A . n 
A 1 83  LEU 83  80  80  LEU LEU A . n 
A 1 84  VAL 84  81  81  VAL VAL A . n 
A 1 85  ASN 85  82  82  ASN ASN A . n 
A 1 86  GLU 86  83  83  GLU GLU A . n 
A 1 87  GLY 87  84  84  GLY GLY A . n 
A 1 88  TYR 88  85  85  TYR TYR A . n 
A 1 89  GLU 89  86  86  GLU GLU A . n 
A 1 90  SER 90  87  87  SER SER A . n 
A 1 91  ILE 91  88  88  ILE ILE A . n 
A 1 92  SER 92  89  89  SER SER A . n 
A 1 93  ALA 93  90  90  ALA ALA A . n 
A 1 94  THR 94  91  91  THR THR A . n 
A 1 95  GLY 95  92  92  GLY GLY A . n 
A 1 96  VAL 96  93  93  VAL VAL A . n 
A 1 97  SER 97  94  94  SER SER A . n 
A 1 98  LEU 98  95  95  LEU LEU A . n 
A 1 99  GLY 99  96  96  GLY GLY A . n 
A 1 100 GLY 100 97  97  GLY GLY A . n 
A 1 101 LEU 101 98  98  LEU LEU A . n 
A 1 102 MET 102 99  99  MET MET A . n 
A 1 103 THR 103 100 100 THR THR A . n 
A 1 104 LEU 104 101 101 LEU LEU A . n 
A 1 105 LYS 105 102 102 LYS LYS A . n 
A 1 106 LEU 106 103 103 LEU LEU A . n 
A 1 107 ALA 107 104 104 ALA ALA A . n 
A 1 108 GLN 108 105 105 GLN GLN A . n 
A 1 109 HIS 109 106 106 HIS HIS A . n 
A 1 110 TYR 110 107 107 TYR TYR A . n 
A 1 111 PRO 111 108 108 PRO PRO A . n 
A 1 112 LEU 112 109 109 LEU LEU A . n 
A 1 113 LYS 113 110 110 LYS LYS A . n 
A 1 114 ARG 114 111 111 ARG ARG A . n 
A 1 115 ILE 115 112 112 ILE ILE A . n 
A 1 116 ALA 116 113 113 ALA ALA A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 MET 118 115 115 MET MET A . n 
A 1 119 SER 119 116 116 SER SER A . n 
A 1 120 ALA 120 117 117 ALA ALA A . n 
A 1 121 PRO 121 118 118 PRO PRO A . n 
A 1 122 LYS 122 119 119 LYS LYS A . n 
A 1 123 GLU 123 120 120 GLU GLU A . n 
A 1 124 LYS 124 121 121 LYS LYS A . n 
A 1 125 SER 125 122 122 SER SER A . n 
A 1 126 ASP 126 123 123 ASP ASP A . n 
A 1 127 ASP 127 124 124 ASP ASP A . n 
A 1 128 GLY 128 125 125 GLY GLY A . n 
A 1 129 LEU 129 126 126 LEU LEU A . n 
A 1 130 ILE 130 127 127 ILE ILE A . n 
A 1 131 GLU 131 128 128 GLU GLU A . n 
A 1 132 HIS 132 129 129 HIS HIS A . n 
A 1 133 LEU 133 130 130 LEU LEU A . n 
A 1 134 VAL 134 131 131 VAL VAL A . n 
A 1 135 TYR 135 132 132 TYR TYR A . n 
A 1 136 TYR 136 133 133 TYR TYR A . n 
A 1 137 SER 137 134 134 SER SER A . n 
A 1 138 GLN 138 135 135 GLN GLN A . n 
A 1 139 ARG 139 136 136 ARG ARG A . n 
A 1 140 MET 140 137 137 MET MET A . n 
A 1 141 SER 141 138 138 SER SER A . n 
A 1 142 ASN 142 139 139 ASN ASN A . n 
A 1 143 ILE 143 140 140 ILE ILE A . n 
A 1 144 LEU 144 141 141 LEU LEU A . n 
A 1 145 ASN 145 142 142 ASN ASN A . n 
A 1 146 LEU 146 143 143 LEU LEU A . n 
A 1 147 ASP 147 144 144 ASP ASP A . n 
A 1 148 GLN 148 145 145 GLN GLN A . n 
A 1 149 GLN 149 146 146 GLN GLN A . n 
A 1 150 ALA 150 147 147 ALA ALA A . n 
A 1 151 SER 151 148 148 SER SER A . n 
A 1 152 SER 152 149 149 SER SER A . n 
A 1 153 ALA 153 150 150 ALA ALA A . n 
A 1 154 GLN 154 151 151 GLN GLN A . n 
A 1 155 LEU 155 152 152 LEU LEU A . n 
A 1 156 ALA 156 153 153 ALA ALA A . n 
A 1 157 ALA 157 154 154 ALA ALA A . n 
A 1 158 ILE 158 155 155 ILE ILE A . n 
A 1 159 ASP 159 156 156 ASP ASP A . n 
A 1 160 ASP 160 157 157 ASP ASP A . n 
A 1 161 TYR 161 158 158 TYR TYR A . n 
A 1 162 GLU 162 159 159 GLU GLU A . n 
A 1 163 GLY 163 160 160 GLY GLY A . n 
A 1 164 GLU 164 161 161 GLU GLU A . n 
A 1 165 ILE 165 162 162 ILE ILE A . n 
A 1 166 THR 166 163 163 THR THR A . n 
A 1 167 LYS 167 164 164 LYS LYS A . n 
A 1 168 PHE 168 165 165 PHE PHE A . n 
A 1 169 GLN 169 166 166 GLN GLN A . n 
A 1 170 HIS 170 167 167 HIS HIS A . n 
A 1 171 PHE 171 168 168 PHE PHE A . n 
A 1 172 ILE 172 169 169 ILE ILE A . n 
A 1 173 ASP 173 170 170 ASP ASP A . n 
A 1 174 ASP 174 171 171 ASP ASP A . n 
A 1 175 ILE 175 172 172 ILE ILE A . n 
A 1 176 MET 176 173 173 MET MET A . n 
A 1 177 THR 177 174 174 THR THR A . n 
A 1 178 ASN 178 175 175 ASN ASN A . n 
A 1 179 LEU 179 176 176 LEU LEU A . n 
A 1 180 ASN 180 177 177 ASN ASN A . n 
A 1 181 VAL 181 178 178 VAL VAL A . n 
A 1 182 ILE 182 179 179 ILE ILE A . n 
A 1 183 LYS 183 180 180 LYS LYS A . n 
A 1 184 MET 184 181 181 MET MET A . n 
A 1 185 PRO 185 182 182 PRO PRO A . n 
A 1 186 ALA 186 183 183 ALA ALA A . n 
A 1 187 ASN 187 184 184 ASN ASN A . n 
A 1 188 ILE 188 185 185 ILE ILE A . n 
A 1 189 LEU 189 186 186 LEU LEU A . n 
A 1 190 PHE 190 187 187 PHE PHE A . n 
A 1 191 GLY 191 188 188 GLY GLY A . n 
A 1 192 GLY 192 189 189 GLY GLY A . n 
A 1 193 LYS 193 190 190 LYS LYS A . n 
A 1 194 ASP 194 191 191 ASP ASP A . n 
A 1 195 ALA 195 192 192 ALA ALA A . n 
A 1 196 PRO 196 193 193 PRO PRO A . n 
A 1 197 SER 197 194 194 SER SER A . n 
A 1 198 TYR 198 195 195 TYR TYR A . n 
A 1 199 GLU 199 196 196 GLU GLU A . n 
A 1 200 THR 200 197 197 THR THR A . n 
A 1 201 SER 201 198 198 SER SER A . n 
A 1 202 ALA 202 199 199 ALA ALA A . n 
A 1 203 HIS 203 200 200 HIS HIS A . n 
A 1 204 PHE 204 201 201 PHE PHE A . n 
A 1 205 ILE 205 202 202 ILE ILE A . n 
A 1 206 TYR 206 203 203 TYR TYR A . n 
A 1 207 GLU 207 204 204 GLU GLU A . n 
A 1 208 HIS 208 205 205 HIS HIS A . n 
A 1 209 LEU 209 206 206 LEU LEU A . n 
A 1 210 GLY 210 207 207 GLY GLY A . n 
A 1 211 SER 211 208 208 SER SER A . n 
A 1 212 VAL 212 209 209 VAL VAL A . n 
A 1 213 ASP 213 210 210 ASP ASP A . n 
A 1 214 LYS 214 211 211 LYS LYS A . n 
A 1 215 GLU 215 212 212 GLU GLU A . n 
A 1 216 LEU 216 213 213 LEU LEU A . n 
A 1 217 ASN 217 214 214 ASN ASN A . n 
A 1 218 GLY 218 215 215 GLY GLY A . n 
A 1 219 LEU 219 216 216 LEU LEU A . n 
A 1 220 LYS 220 217 217 LYS LYS A . n 
A 1 221 ASP 221 218 218 ASP ASP A . n 
A 1 222 SER 222 219 219 SER SER A . n 
A 1 223 HIS 223 220 220 HIS HIS A . n 
A 1 224 HIS 224 221 221 HIS HIS A . n 
A 1 225 LEU 225 222 222 LEU LEU A . n 
A 1 226 MET 226 223 223 MET MET A . n 
A 1 227 THR 227 224 224 THR THR A . n 
A 1 228 HIS 228 225 225 HIS HIS A . n 
A 1 229 GLY 229 226 226 GLY GLY A . n 
A 1 230 GLU 230 227 227 GLU GLU A . n 
A 1 231 GLY 231 228 228 GLY GLY A . n 
A 1 232 ARG 232 229 229 ARG ARG A . n 
A 1 233 ASP 233 230 230 ASP ASP A . n 
A 1 234 ILE 234 231 231 ILE ILE A . n 
A 1 235 LEU 235 232 232 LEU LEU A . n 
A 1 236 GLU 236 233 233 GLU GLU A . n 
A 1 237 GLU 237 234 234 GLU GLU A . n 
A 1 238 ASN 238 235 235 ASN ASN A . n 
A 1 239 VAL 239 236 236 VAL VAL A . n 
A 1 240 ILE 240 237 237 ILE ILE A . n 
A 1 241 ARG 241 238 238 ARG ARG A . n 
A 1 242 PHE 242 239 239 PHE PHE A . n 
A 1 243 PHE 243 240 240 PHE PHE A . n 
A 1 244 ASN 244 241 241 ASN ASN A . n 
A 1 245 ALA 245 242 242 ALA ALA A . n 
A 1 246 LEU 246 243 243 LEU LEU A . n 
A 1 247 THR 247 244 244 THR THR A . 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 
B 2 CA  1   301 1   CA  CA  A . 
C 2 CA  1   302 2   CA  CA  A . 
D 2 CA  1   303 3   CA  CA  A . 
E 2 CA  1   304 4   CA  CA  A . 
F 3 HOH 1   401 11  HOH HOH A . 
F 3 HOH 2   402 114 HOH HOH A . 
F 3 HOH 3   403 45  HOH HOH A . 
F 3 HOH 4   404 65  HOH HOH A . 
F 3 HOH 5   405 116 HOH HOH A . 
F 3 HOH 6   406 75  HOH HOH A . 
F 3 HOH 7   407 96  HOH HOH A . 
F 3 HOH 8   408 13  HOH HOH A . 
F 3 HOH 9   409 113 HOH HOH A . 
F 3 HOH 10  410 4   HOH HOH A . 
F 3 HOH 11  411 59  HOH HOH A . 
F 3 HOH 12  412 33  HOH HOH A . 
F 3 HOH 13  413 41  HOH HOH A . 
F 3 HOH 14  414 61  HOH HOH A . 
F 3 HOH 15  415 3   HOH HOH A . 
F 3 HOH 16  416 95  HOH HOH A . 
F 3 HOH 17  417 28  HOH HOH A . 
F 3 HOH 18  418 69  HOH HOH A . 
F 3 HOH 19  419 42  HOH HOH A . 
F 3 HOH 20  420 10  HOH HOH A . 
F 3 HOH 21  421 99  HOH HOH A . 
F 3 HOH 22  422 67  HOH HOH A . 
F 3 HOH 23  423 6   HOH HOH A . 
F 3 HOH 24  424 29  HOH HOH A . 
F 3 HOH 25  425 63  HOH HOH A . 
F 3 HOH 26  426 102 HOH HOH A . 
F 3 HOH 27  427 66  HOH HOH A . 
F 3 HOH 28  428 84  HOH HOH A . 
F 3 HOH 29  429 55  HOH HOH A . 
F 3 HOH 30  430 8   HOH HOH A . 
F 3 HOH 31  431 88  HOH HOH A . 
F 3 HOH 32  432 60  HOH HOH A . 
F 3 HOH 33  433 98  HOH HOH A . 
F 3 HOH 34  434 78  HOH HOH A . 
F 3 HOH 35  435 27  HOH HOH A . 
F 3 HOH 36  436 118 HOH HOH A . 
F 3 HOH 37  437 104 HOH HOH A . 
F 3 HOH 38  438 73  HOH HOH A . 
F 3 HOH 39  439 44  HOH HOH A . 
F 3 HOH 40  440 34  HOH HOH A . 
F 3 HOH 41  441 38  HOH HOH A . 
F 3 HOH 42  442 111 HOH HOH A . 
F 3 HOH 43  443 90  HOH HOH A . 
F 3 HOH 44  444 37  HOH HOH A . 
F 3 HOH 45  445 35  HOH HOH A . 
F 3 HOH 46  446 24  HOH HOH A . 
F 3 HOH 47  447 83  HOH HOH A . 
F 3 HOH 48  448 121 HOH HOH A . 
F 3 HOH 49  449 18  HOH HOH A . 
F 3 HOH 50  450 2   HOH HOH A . 
F 3 HOH 51  451 12  HOH HOH A . 
F 3 HOH 52  452 64  HOH HOH A . 
F 3 HOH 53  453 103 HOH HOH A . 
F 3 HOH 54  454 36  HOH HOH A . 
F 3 HOH 55  455 15  HOH HOH A . 
F 3 HOH 56  456 70  HOH HOH A . 
F 3 HOH 57  457 72  HOH HOH A . 
F 3 HOH 58  458 74  HOH HOH A . 
F 3 HOH 59  459 51  HOH HOH A . 
F 3 HOH 60  460 7   HOH HOH A . 
F 3 HOH 61  461 57  HOH HOH A . 
F 3 HOH 62  462 120 HOH HOH A . 
F 3 HOH 63  463 71  HOH HOH A . 
F 3 HOH 64  464 1   HOH HOH A . 
F 3 HOH 65  465 30  HOH HOH A . 
F 3 HOH 66  466 58  HOH HOH A . 
F 3 HOH 67  467 16  HOH HOH A . 
F 3 HOH 68  468 25  HOH HOH A . 
F 3 HOH 69  469 101 HOH HOH A . 
F 3 HOH 70  470 23  HOH HOH A . 
F 3 HOH 71  471 48  HOH HOH A . 
F 3 HOH 72  472 52  HOH HOH A . 
F 3 HOH 73  473 50  HOH HOH A . 
F 3 HOH 74  474 22  HOH HOH A . 
F 3 HOH 75  475 39  HOH HOH A . 
F 3 HOH 76  476 9   HOH HOH A . 
F 3 HOH 77  477 19  HOH HOH A . 
F 3 HOH 78  478 56  HOH HOH A . 
F 3 HOH 79  479 14  HOH HOH A . 
F 3 HOH 80  480 26  HOH HOH A . 
F 3 HOH 81  481 49  HOH HOH A . 
F 3 HOH 82  482 81  HOH HOH A . 
F 3 HOH 83  483 68  HOH HOH A . 
F 3 HOH 84  484 20  HOH HOH A . 
F 3 HOH 85  485 87  HOH HOH A . 
F 3 HOH 86  486 85  HOH HOH A . 
F 3 HOH 87  487 79  HOH HOH A . 
F 3 HOH 88  488 105 HOH HOH A . 
F 3 HOH 89  489 110 HOH HOH A . 
F 3 HOH 90  490 108 HOH HOH A . 
F 3 HOH 91  491 17  HOH HOH A . 
F 3 HOH 92  492 5   HOH HOH A . 
F 3 HOH 93  493 54  HOH HOH A . 
F 3 HOH 94  494 100 HOH HOH A . 
F 3 HOH 95  495 109 HOH HOH A . 
F 3 HOH 96  496 115 HOH HOH A . 
F 3 HOH 97  497 91  HOH HOH A . 
F 3 HOH 98  498 76  HOH HOH A . 
F 3 HOH 99  499 93  HOH HOH A . 
F 3 HOH 100 500 53  HOH HOH A . 
F 3 HOH 101 501 124 HOH HOH A . 
F 3 HOH 102 502 31  HOH HOH A . 
F 3 HOH 103 503 32  HOH HOH A . 
F 3 HOH 104 504 21  HOH HOH A . 
F 3 HOH 105 505 119 HOH HOH A . 
F 3 HOH 106 506 123 HOH HOH A . 
F 3 HOH 107 507 47  HOH HOH A . 
F 3 HOH 108 508 107 HOH HOH A . 
F 3 HOH 109 509 82  HOH HOH A . 
F 3 HOH 110 510 46  HOH HOH A . 
F 3 HOH 111 511 89  HOH HOH A . 
F 3 HOH 112 512 112 HOH HOH A . 
F 3 HOH 113 513 77  HOH HOH A . 
F 3 HOH 114 514 117 HOH HOH A . 
F 3 HOH 115 515 86  HOH HOH A . 
F 3 HOH 116 516 106 HOH HOH A . 
F 3 HOH 117 517 80  HOH HOH A . 
F 3 HOH 118 518 40  HOH HOH A . 
F 3 HOH 119 519 62  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.8       2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3       4 
# 
_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                     9C0N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.656 
_cell.length_a_esd                 ? 
_cell.length_b                     61.736 
_cell.length_b_esd                 ? 
_cell.length_c                     77.177 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9C0N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9C0N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.71 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 uL 10 mg/mL FphI (10 mM HEPES pH 7.5, 100 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 200mM Calcium chloride hexahydrate, 100mM HEPES pH 7.0, 20 % w/v PEG 6000.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     295 
_diffrn.ambient_temp_details             'Room temperature data collection' 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C0N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               48.21 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     28252 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.055 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       146228 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.049 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6850 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1435 
_reflns_shell.percent_possible_obs                          98.5 
_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                               4.8 
_reflns_shell.pdbx_chi_squared                              0.94 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.3 
_reflns_shell.pdbx_Rrim_I_all                               1.263 
_reflns_shell.pdbx_Rpim_I_all                               0.559 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.660 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.127 
_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                                 9C0N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             40.06 
_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                     28197 
_refine.ls_number_reflns_R_free                  1395 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1504 
_refine.ls_R_factor_R_free                       0.1700 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1493 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 18.21 
_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                            0.16 
_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.pdbx_number_atoms_protein        1915 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             119 
_refine_hist.number_atoms_total               2038 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        40.06 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010 ? 2092 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.044 ? 2852 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.306 ? 288  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061 ? 306  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 380  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.76  . . 126 2643 99.00  . . . . 0.2607 . . . . . . . . . . . 0.3109 
'X-RAY DIFFRACTION' 1.76 1.83  . . 133 2614 100.00 . . . . 0.2340 . . . . . . . . . . . 0.2916 
'X-RAY DIFFRACTION' 1.83 1.91  . . 140 2637 100.00 . . . . 0.2228 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 1.91 2.02  . . 154 2640 100.00 . . . . 0.1655 . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 2.02 2.14  . . 137 2677 99.00  . . . . 0.1523 . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 2.14 2.31  . . 155 2647 100.00 . . . . 0.1554 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 2.31 2.54  . . 124 2700 100.00 . . . . 0.1446 . . . . . . . . . . . 0.1798 
'X-RAY DIFFRACTION' 2.54 2.91  . . 148 2697 100.00 . . . . 0.1498 . . . . . . . . . . . 0.1772 
'X-RAY DIFFRACTION' 2.91 3.66  . . 126 2714 99.00  . . . . 0.1396 . . . . . . . . . . . 0.1779 
'X-RAY DIFFRACTION' 3.66 40.06 . . 152 2833 99.00  . . . . 0.1317 . . . . . . . . . . . 0.1385 
# 
_struct.entry_id                     9C0N 
_struct.title                        
'FphI, Staphylococcus aureus fluorophosphonate-binding serine hydrolases I, apo form at room temperature' 
_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        9C0N 
_struct_keywords.text            
;FphI, Staphylococcus aureus, S. aureus, fluorophosphonate-binding, serine hydrolases, lipase, room temperature, humidity, humidifier, HYDROLASE
;
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    X5DUZ9_STAAU 
_struct_ref.pdbx_db_accession          X5DUZ9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRIKTPSPSYLKGTNGHAILLLHSFTGTNRDVKHLAAELNDQGFSCYAPNYPGHGLLLKDFMTYNVDDWWEEVEKAYQFL
VNEGYESISATGVSLGGLMTLKLAQHYPLKRIAVMSAPKEKSDDGLIEHLVYYSQRMSNILNLDQQASSAQLAAIDDYEG
EITKFQHFIDDIMTNLNVIKMPANILFGGKDAPSYETSAHFIYEHLGSVDKELNGLKDSHHLMTHGEGRDILEENVIRFF
NALT
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9C0N 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 247 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             X5DUZ9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  244 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       244 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9C0N GLY A 1 ? UNP X5DUZ9 ? ? 'expression tag' -2 1 
1 9C0N PRO A 2 ? UNP X5DUZ9 ? ? 'expression tag' -1 2 
1 9C0N GLY A 3 ? UNP X5DUZ9 ? ? 'expression tag' 0  3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 THR A 31  ? ASP A 34  ? THR A 28  ASP A 31  5 ? 4  
HELX_P HELX_P2  AA2 VAL A 35  ? GLN A 45  ? VAL A 32  GLN A 42  1 ? 11 
HELX_P HELX_P3  AA3 LEU A 60  ? MET A 65  ? LEU A 57  MET A 62  1 ? 6  
HELX_P HELX_P4  AA4 ASN A 68  ? GLY A 87  ? ASN A 65  GLY A 84  1 ? 20 
HELX_P HELX_P5  AA5 SER A 97  ? TYR A 110 ? SER A 94  TYR A 107 1 ? 14 
HELX_P HELX_P6  AA6 SER A 125 ? LEU A 144 ? SER A 122 LEU A 141 1 ? 20 
HELX_P HELX_P7  AA7 ASP A 147 ? ALA A 157 ? ASP A 144 ALA A 154 1 ? 11 
HELX_P HELX_P8  AA8 ILE A 158 ? ASP A 160 ? ILE A 155 ASP A 157 5 ? 3  
HELX_P HELX_P9  AA9 TYR A 161 ? ASN A 178 ? TYR A 158 ASN A 175 1 ? 18 
HELX_P HELX_P10 AB1 LEU A 179 ? ILE A 182 ? LEU A 176 ILE A 179 5 ? 4  
HELX_P HELX_P11 AB2 ALA A 195 ? LEU A 209 ? ALA A 192 LEU A 206 1 ? 15 
HELX_P HELX_P12 AB3 GLY A 231 ? ASN A 244 ? GLY A 228 ASN A 241 1 ? 14 
HELX_P HELX_P13 AB4 ALA A 245 ? THR A 247 ? ALA A 242 THR A 244 5 ? 3  
# 
_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 
metalc1  metalc ? ? A GLU 41  OE1 ? ? ? 1_555 C CA  . CA ? ? A GLU 38  A CA  302 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc2  metalc ? ? A GLU 41  OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 38  A CA  302 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc3  metalc ? ? A ASN 43  OD1 ? ? ? 1_555 B CA  . CA ? ? A ASN 40  A CA  301 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc4  metalc ? ? A ASP 44  OD1 ? ? ? 1_555 B CA  . CA ? ? A ASP 41  A CA  301 1_555 ? ? ? ? ? ? ? 2.502 ? ? 
metalc5  metalc ? ? A ASP 71  OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 68  A CA  303 2_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc6  metalc ? ? A GLU 77  OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 74  A CA  302 3_545 ? ? ? ? ? ? ? 2.638 ? ? 
metalc7  metalc ? ? A ASP 160 O   ? ? ? 1_555 E CA  . CA ? ? A ASP 157 A CA  304 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc8  metalc ? ? A GLU 164 OE1 A ? ? 1_555 E CA  . CA ? ? A GLU 161 A CA  304 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc9  metalc ? ? A GLU 164 OE2 A ? ? 1_555 E CA  . CA ? ? A GLU 161 A CA  304 1_555 ? ? ? ? ? ? ? 2.533 ? ? 
metalc10 metalc ? ? A ASP 174 OD1 B ? ? 1_555 B CA  . CA ? ? A ASP 171 A CA  301 3_545 ? ? ? ? ? ? ? 2.728 ? ? 
metalc11 metalc ? ? A ASP 174 OD2 B ? ? 1_555 B CA  . CA ? ? A ASP 171 A CA  301 3_545 ? ? ? ? ? ? ? 2.497 ? ? 
metalc12 metalc ? ? A GLU 199 OE1 ? ? ? 1_555 D CA  . CA ? ? A GLU 196 A CA  303 1_555 ? ? ? ? ? ? ? 2.612 ? ? 
metalc13 metalc ? ? A GLU 199 OE2 ? ? ? 1_555 D CA  . CA ? ? A GLU 196 A CA  303 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc14 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 449 3_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc15 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 464 3_555 ? ? ? ? ? ? ? 2.514 ? ? 
metalc16 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 479 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
metalc17 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 409 3_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc18 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 416 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc19 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 477 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc20 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 512 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc21 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 402 2_554 ? ? ? ? ? ? ? 2.445 ? ? 
metalc22 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 405 2_554 ? ? ? ? ? ? ? 2.416 ? ? 
metalc23 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 447 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc24 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 496 2_554 ? ? ? ? ? ? ? 2.472 ? ? 
metalc25 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 501 1_555 ? ? ? ? ? ? ? 2.567 ? ? 
metalc26 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 506 1_555 ? ? ? ? ? ? ? 2.761 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OE2 ? A GLU 41  ? A GLU 38  ? 1_555 51.2  ? 
2  OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OE2 ? A GLU 77  ? A GLU 74  ? 1_555 24.3  ? 
3  OE2 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OE2 ? A GLU 77  ? A GLU 74  ? 1_555 31.0  ? 
4  OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 409 ? 3_555 142.8 ? 
5  OE2 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 409 ? 3_555 162.1 ? 
6  OE2 ? A GLU 77  ? A GLU 74  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 409 ? 3_555 155.2 ? 
7  OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 416 ? 1_555 64.0  ? 
8  OE2 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 416 ? 1_555 113.0 ? 
9  OE2 ? A GLU 77  ? A GLU 74  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 416 ? 1_555 88.1  ? 
10 O   ? F HOH .   ? A HOH 409 ? 3_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 416 ? 1_555 84.4  ? 
11 OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 477 ? 1_555 90.5  ? 
12 OE2 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 477 ? 1_555 85.3  ? 
13 OE2 ? A GLU 77  ? A GLU 74  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 477 ? 1_555 77.3  ? 
14 O   ? F HOH .   ? A HOH 409 ? 3_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 477 ? 1_555 83.8  ? 
15 O   ? F HOH .   ? A HOH 416 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 477 ? 1_555 112.3 ? 
16 OE1 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 85.7  ? 
17 OE2 ? A GLU 41  ? A GLU 38  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 93.7  ? 
18 OE2 ? A GLU 77  ? A GLU 74  ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 99.7  ? 
19 O   ? F HOH .   ? A HOH 409 ? 3_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 98.2  ? 
20 O   ? F HOH .   ? A HOH 416 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 64.4  ? 
21 O   ? F HOH .   ? A HOH 477 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 512 ? 1_555 175.9 ? 
22 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 113.8 ? 
23 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD1 B A ASP 174 ? A ASP 171 ? 1_555 31.7  ? 
24 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD1 B A ASP 174 ? A ASP 171 ? 1_555 100.4 ? 
25 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD2 B A ASP 174 ? A ASP 171 ? 1_555 32.3  ? 
26 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD2 B A ASP 174 ? A ASP 171 ? 1_555 100.8 ? 
27 OD1 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD2 B A ASP 174 ? A ASP 171 ? 1_555 1.1   ? 
28 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 3_555 85.1  ? 
29 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 3_555 161.0 ? 
30 OD1 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 3_555 96.7  ? 
31 OD2 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 449 ? 3_555 96.0  ? 
32 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 3_555 140.1 ? 
33 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 3_555 89.0  ? 
34 OD1 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 3_555 115.7 ? 
35 OD2 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 3_555 114.8 ? 
36 O   ? F HOH .   ? A HOH 449 ? 3_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 464 ? 3_555 76.0  ? 
37 OD1 ? A ASN 43  ? A ASN 40  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 80.2  ? 
38 OD1 ? A ASP 44  ? A ASP 41  ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 82.4  ? 
39 OD1 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 48.8  ? 
40 OD2 B A ASP 174 ? A ASP 171 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 48.1  ? 
41 O   ? F HOH .   ? A HOH 449 ? 3_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 103.0 ? 
42 O   ? F HOH .   ? A HOH 464 ? 3_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 479 ? 1_555 70.5  ? 
43 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 41.4  ? 
44 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 44.6  ? 
45 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 3.3   ? 
46 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 402 ? 2_554 42.2  ? 
47 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 402 ? 2_554 3.1   ? 
48 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 402 ? 2_554 4.2   ? 
49 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 405 ? 2_554 44.5  ? 
50 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 405 ? 2_554 4.5   ? 
51 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 405 ? 2_554 3.0   ? 
52 O   ? F HOH .   ? A HOH 402 ? 2_554 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 405 ? 2_554 6.8   ? 
53 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 447 ? 1_555 39.1  ? 
54 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 447 ? 1_555 2.3   ? 
55 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 447 ? 1_555 5.6   ? 
56 O   ? F HOH .   ? A HOH 402 ? 2_554 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 447 ? 1_555 4.4   ? 
57 O   ? F HOH .   ? A HOH 405 ? 2_554 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 447 ? 1_555 6.2   ? 
58 OD1 ? A ASP 71  ? A ASP 68  ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 42.5  ? 
59 OE1 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 2.9   ? 
60 OE2 ? A GLU 199 ? A GLU 196 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 3.3   ? 
61 O   ? F HOH .   ? A HOH 402 ? 2_554 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 5.8   ? 
62 O   ? F HOH .   ? A HOH 405 ? 2_554 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 2.1   ? 
63 O   ? F HOH .   ? A HOH 447 ? 1_555 CA ? D CA . ? A CA 303 ? 2_555 O   ? F HOH .   ? A HOH 496 ? 2_554 4.2   ? 
64 O   ? A ASP 160 ? A ASP 157 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OE1 A A GLU 164 ? A GLU 161 ? 1_555 88.1  ? 
65 O   ? A ASP 160 ? A ASP 157 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OE2 A A GLU 164 ? A GLU 161 ? 1_555 124.1 ? 
66 OE1 A A GLU 164 ? A GLU 161 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OE2 A A GLU 164 ? A GLU 161 ? 1_555 53.1  ? 
67 O   ? A ASP 160 ? A ASP 157 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 501 ? 1_555 132.4 ? 
68 OE1 A A GLU 164 ? A GLU 161 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 501 ? 1_555 127.3 ? 
69 OE2 A A GLU 164 ? A GLU 161 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 501 ? 1_555 74.6  ? 
70 O   ? A ASP 160 ? A ASP 157 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 506 ? 1_555 70.8  ? 
71 OE1 A A GLU 164 ? A GLU 161 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 506 ? 1_555 80.4  ? 
72 OE2 A A GLU 164 ? A GLU 161 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 506 ? 1_555 126.9 ? 
73 O   ? F HOH .   ? A HOH 501 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 506 ? 1_555 137.3 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   7 
_struct_sheet.details          ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 12  ? LEU A 14  ? SER A 9   LEU A 11  
AA1 2 SER A 48  ? ALA A 51  ? SER A 45  ALA A 48  
AA1 3 HIS A 20  ? LEU A 25  ? HIS A 17  LEU A 22  
AA1 4 SER A 90  ? VAL A 96  ? SER A 87  VAL A 93  
AA1 5 ILE A 115 ? MET A 118 ? ILE A 112 MET A 115 
AA1 6 ALA A 186 ? GLY A 191 ? ALA A 183 GLY A 188 
AA1 7 LYS A 214 ? LEU A 219 ? LYS A 211 LEU A 216 
# 
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 LEU A 14  ? N LEU A 11  O CYS A 49  ? O CYS A 46  
AA1 2 3 O SER A 48  ? O SER A 45  N ILE A 22  ? N ILE A 19  
AA1 3 4 N LEU A 23  ? N LEU A 20  O THR A 94  ? O THR A 91  
AA1 4 5 N GLY A 95  ? N GLY A 92  O MET A 118 ? O MET A 115 
AA1 5 6 N VAL A 117 ? N VAL A 114 O LEU A 189 ? O LEU A 186 
AA1 6 7 N ILE A 188 ? N ILE A 185 O ASN A 217 ? O ASN A 214 
# 
_pdbx_entry_details.entry_id                   9C0N 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    405 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    496 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 SER A 94 ? ? 61.36 -120.09 
2 1 SER A 94 ? ? 56.35 -120.09 
# 
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 0.9558  11.1057 21.1209 0.2225 ? -0.0130 ? 0.0070  ? 0.1839 ? -0.0112 ? 0.2375 ? 3.6286 ? -1.4810 
? -0.0104 ? 2.5597 ? -0.0652 ? 2.2126 ? -0.0645 ? -0.1672 ? 0.3202  ? 0.1201  ? 0.0051  ? -0.0468 ? -0.2301 ? 0.0156  ? 0.0482  ? 
2 'X-RAY DIFFRACTION' ? refined 4.9491  0.6174  21.9708 0.2252 ? -0.0194 ? 0.0248  ? 0.1997 ? 0.0165  ? 0.2297 ? 1.2333 ? -0.1694 
? 0.6666  ? 1.6162 ? 0.3442  ? 2.3992 ? -0.0288 ? -0.0255 ? -0.1461 ? 0.1731  ? 0.0202  ? 0.0803  ? 0.0856  ? 0.1031  ? -0.0030 ? 
3 'X-RAY DIFFRACTION' ? refined 23.9415 12.1226 22.1709 0.4902 ? -0.2313 ? 0.0286  ? 0.9389 ? 0.0088  ? 0.5109 ? 5.3966 ? 0.0803  
? 0.6714  ? 2.8095 ? 1.5657  ? 5.3617 ? -0.0720 ? 0.0551  ? 0.8532  ? -0.5167 ? -0.0420 ? -0.1740 ? -0.8273 ? 1.2090  ? 0.0981  ? 
4 'X-RAY DIFFRACTION' ? refined 20.9638 -2.2400 22.0545 0.2720 ? 0.0188  ? -0.0533 ? 0.5464 ? -0.0520 ? 0.3563 ? 3.0372 ? 1.8817  
? 0.6153  ? 4.5795 ? 0.7303  ? 3.2555 ? 0.0179  ? -0.2260 ? -0.0940 ? 0.5432  ? 0.1014  ? -0.6044 ? 0.0692  ? 1.0777  ? -0.1446 ? 
5 'X-RAY DIFFRACTION' ? refined 7.6856  2.2366  4.4710  0.3141 ? -0.0091 ? 0.0302  ? 0.2848 ? 0.0150  ? 0.2055 ? 2.8181 ? -0.2871 
? -0.7960 ? 3.5388 ? 0.0832  ? 2.7688 ? 0.1655  ? 0.1453  ? 0.2049  ? -0.4065 ? -0.1079 ? -0.2219 ? -0.3553 ? 0.2988  ? -0.0508 ? 
6 'X-RAY DIFFRACTION' ? refined -3.5266 9.8506  6.9641  0.3433 ? 0.0415  ? -0.0219 ? 0.2639 ? 0.0103  ? 0.3418 ? 3.7250 ? 3.6932  
? -0.6549 ? 3.8234 ? -0.2864 ? 6.6252 ? 0.0330  ? 0.3177  ? 0.6118  ? -0.6641 ? 0.0752  ? 0.6886  ? -0.6401 ? -0.3677 ? -0.0606 ? 
# 
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 3 through 42 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 43 through 122 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 123 through 144 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 145 through 178 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 179 through 228 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 229 through 244 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2 ? A GLY 1 
2 1 Y 1 A PRO -1 ? A PRO 2 
3 1 Y 1 A GLY 0  ? A GLY 3 
4 1 Y 1 A MET 1  ? A MET 4 
5 1 Y 1 A ARG 2  ? A ARG 5 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Capability Build Funding - New Zealand Synchrotron Group Ltd' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8G0N 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C0N 
_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]   0.018991 
_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]   0.016198 
_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]   0.012957 
_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  
CA 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ILE A 1 6   ? 14.863  17.760  35.021 1.00 70.98  ? 3   ILE A N    1 
ATOM   2    C  CA   . ILE A 1 6   ? 14.927  16.704  34.007 1.00 79.20  ? 3   ILE A CA   1 
ATOM   3    C  C    . ILE A 1 6   ? 14.134  15.457  34.373 1.00 66.42  ? 3   ILE A C    1 
ATOM   4    O  O    . ILE A 1 6   ? 14.469  14.751  35.326 1.00 64.26  ? 3   ILE A O    1 
ATOM   5    C  CB   . ILE A 1 6   ? 16.397  16.289  33.743 1.00 72.23  ? 3   ILE A CB   1 
ATOM   6    C  CG1  . ILE A 1 6   ? 17.100  17.304  32.853 1.00 92.58  ? 3   ILE A CG1  1 
ATOM   7    C  CG2  . ILE A 1 6   ? 16.487  14.914  33.089 1.00 60.01  ? 3   ILE A CG2  1 
ATOM   8    C  CD1  . ILE A 1 6   ? 16.408  17.489  31.507 1.00 98.74  ? 3   ILE A CD1  1 
ATOM   9    H  HA   . ILE A 1 6   ? 14.523  17.080  33.210 1.00 95.07  ? 3   ILE A HA   1 
ATOM   10   H  HB   . ILE A 1 6   ? 16.833  16.257  34.608 1.00 86.71  ? 3   ILE A HB   1 
ATOM   11   H  HG12 . ILE A 1 6   ? 17.114  18.163  33.304 1.00 111.13 ? 3   ILE A HG12 1 
ATOM   12   H  HG13 . ILE A 1 6   ? 18.007  17.003  32.686 1.00 111.13 ? 3   ILE A HG13 1 
ATOM   13   H  HG21 . ILE A 1 6   ? 17.417  14.714  32.900 1.00 72.05  ? 3   ILE A HG21 1 
ATOM   14   H  HG22 . ILE A 1 6   ? 16.122  14.251  33.696 1.00 72.05  ? 3   ILE A HG22 1 
ATOM   15   H  HG23 . ILE A 1 6   ? 15.976  14.922  32.264 1.00 72.05  ? 3   ILE A HG23 1 
ATOM   16   H  HD11 . ILE A 1 6   ? 16.928  18.104  30.967 1.00 118.53 ? 3   ILE A HD11 1 
ATOM   17   H  HD12 . ILE A 1 6   ? 16.347  16.629  31.063 1.00 118.53 ? 3   ILE A HD12 1 
ATOM   18   H  HD13 . ILE A 1 6   ? 15.519  17.848  31.655 1.00 118.53 ? 3   ILE A HD13 1 
ATOM   19   N  N    . LYS A 1 7   ? 13.117  15.134  33.585 1.00 71.04  ? 4   LYS A N    1 
ATOM   20   C  CA   . LYS A 1 7   ? 12.356  13.935  33.878 1.00 64.05  ? 4   LYS A CA   1 
ATOM   21   C  C    . LYS A 1 7   ? 11.853  13.338  32.576 1.00 57.01  ? 4   LYS A C    1 
ATOM   22   O  O    . LYS A 1 7   ? 11.804  14.007  31.545 1.00 56.42  ? 4   LYS A O    1 
ATOM   23   C  CB   . LYS A 1 7   ? 11.191  14.231  34.828 1.00 67.36  ? 4   LYS A CB   1 
ATOM   24   C  CG   . LYS A 1 7   ? 10.788  12.997  35.615 1.00 94.10  ? 4   LYS A CG   1 
ATOM   25   C  CD   . LYS A 1 7   ? 9.341   12.993  36.059 1.00 101.44 ? 4   LYS A CD   1 
ATOM   26   C  CE   . LYS A 1 7   ? 8.799   11.560  36.026 1.00 107.15 ? 4   LYS A CE   1 
ATOM   27   N  NZ   . LYS A 1 7   ? 8.710   11.007  34.629 1.00 74.79  ? 4   LYS A NZ   1 
ATOM   28   H  H    . LYS A 1 7   ? 12.858  15.581  32.897 1.00 85.29  ? 4   LYS A H    1 
ATOM   29   H  HA   . LYS A 1 7   ? 12.933  13.280  34.302 1.00 76.89  ? 4   LYS A HA   1 
ATOM   30   H  HB2  . LYS A 1 7   ? 11.457  14.921  35.457 1.00 80.87  ? 4   LYS A HB2  1 
ATOM   31   H  HB3  . LYS A 1 7   ? 10.425  14.529  34.314 1.00 80.87  ? 4   LYS A HB3  1 
ATOM   32   H  HG2  . LYS A 1 7   ? 10.928  12.214  35.059 1.00 112.95 ? 4   LYS A HG2  1 
ATOM   33   H  HG3  . LYS A 1 7   ? 11.340  12.941  36.411 1.00 112.95 ? 4   LYS A HG3  1 
ATOM   34   H  HD2  . LYS A 1 7   ? 9.274   13.332  36.965 1.00 121.76 ? 4   LYS A HD2  1 
ATOM   35   H  HD3  . LYS A 1 7   ? 8.811   13.541  35.460 1.00 121.76 ? 4   LYS A HD3  1 
ATOM   36   H  HE2  . LYS A 1 7   ? 9.389   10.986  36.539 1.00 128.61 ? 4   LYS A HE2  1 
ATOM   37   H  HE3  . LYS A 1 7   ? 7.908   11.549  36.410 1.00 128.61 ? 4   LYS A HE3  1 
ATOM   38   H  HZ1  . LYS A 1 7   ? 8.315   10.210  34.641 1.00 89.78  ? 4   LYS A HZ1  1 
ATOM   39   H  HZ2  . LYS A 1 7   ? 8.236   11.557  34.113 1.00 89.78  ? 4   LYS A HZ2  1 
ATOM   40   H  HZ3  . LYS A 1 7   ? 9.526   10.920  34.284 1.00 89.78  ? 4   LYS A HZ3  1 
ATOM   41   N  N    . THR A 1 8   ? 11.519  12.053  32.622 1.00 46.58  ? 5   THR A N    1 
ATOM   42   C  CA   . THR A 1 8   ? 10.823  11.432  31.502 1.00 45.66  ? 5   THR A CA   1 
ATOM   43   C  C    . THR A 1 8   ? 9.446   12.066  31.379 1.00 39.86  ? 5   THR A C    1 
ATOM   44   O  O    . THR A 1 8   ? 8.715   12.159  32.378 1.00 41.37  ? 5   THR A O    1 
ATOM   45   C  CB   . THR A 1 8   ? 10.696  9.910   31.696 1.00 46.28  ? 5   THR A CB   1 
ATOM   46   O  OG1  . THR A 1 8   ? 12.004  9.324   31.682 1.00 45.64  ? 5   THR A OG1  1 
ATOM   47   C  CG2  . THR A 1 8   ? 9.860   9.254   30.615 1.00 44.88  ? 5   THR A CG2  1 
ATOM   48   H  H    . THR A 1 8   ? 11.682  11.525  33.282 1.00 55.93  ? 5   THR A H    1 
ATOM   49   H  HA   . THR A 1 8   ? 11.323  11.574  30.683 1.00 54.83  ? 5   THR A HA   1 
ATOM   50   H  HB   . THR A 1 8   ? 10.251  9.749   32.543 1.00 55.57  ? 5   THR A HB   1 
ATOM   51   H  HG1  . THR A 1 8   ? 11.945  8.489   31.744 1.00 54.81  ? 5   THR A HG1  1 
ATOM   52   H  HG21 . THR A 1 8   ? 10.297  8.447   30.302 1.00 53.89  ? 5   THR A HG21 1 
ATOM   53   H  HG22 . THR A 1 8   ? 8.986   9.024   30.966 1.00 53.89  ? 5   THR A HG22 1 
ATOM   54   H  HG23 . THR A 1 8   ? 9.749   9.862   29.867 1.00 53.89  ? 5   THR A HG23 1 
ATOM   55   N  N    . PRO A 1 9   ? 9.055   12.519  30.201 1.00 37.46  ? 6   PRO A N    1 
ATOM   56   C  CA   . PRO A 1 9   ? 7.719   13.086  30.059 1.00 32.16  ? 6   PRO A CA   1 
ATOM   57   C  C    . PRO A 1 9   ? 6.634   12.080  30.419 1.00 35.54  ? 6   PRO A C    1 
ATOM   58   O  O    . PRO A 1 9   ? 6.777   10.869  30.238 1.00 35.03  ? 6   PRO A O    1 
ATOM   59   C  CB   . PRO A 1 9   ? 7.635   13.431  28.562 1.00 40.19  ? 6   PRO A CB   1 
ATOM   60   C  CG   . PRO A 1 9   ? 8.976   13.215  28.006 1.00 40.46  ? 6   PRO A CG   1 
ATOM   61   C  CD   . PRO A 1 9   ? 9.913   12.765  29.023 1.00 40.32  ? 6   PRO A CD   1 
ATOM   62   H  HA   . PRO A 1 9   ? 7.636   13.882  30.607 1.00 38.63  ? 6   PRO A HA   1 
ATOM   63   H  HB2  . PRO A 1 9   ? 6.990   12.849  28.131 1.00 48.26  ? 6   PRO A HB2  1 
ATOM   64   H  HB3  . PRO A 1 9   ? 7.368   14.357  28.458 1.00 48.26  ? 6   PRO A HB3  1 
ATOM   65   H  HG2  . PRO A 1 9   ? 8.910   12.544  27.309 1.00 48.59  ? 6   PRO A HG2  1 
ATOM   66   H  HG3  . PRO A 1 9   ? 9.287   14.054  27.631 1.00 48.59  ? 6   PRO A HG3  1 
ATOM   67   H  HD2  . PRO A 1 9   ? 10.357  11.949  28.744 1.00 48.42  ? 6   PRO A HD2  1 
ATOM   68   H  HD3  . PRO A 1 9   ? 10.571  13.452  29.213 1.00 48.42  ? 6   PRO A HD3  1 
ATOM   69   N  N    . SER A 1 10  ? 5.513   12.604  30.815 1.00 35.03  ? 7   SER A N    1 
ATOM   70   C  CA   . SER A 1 10  ? 4.346   11.806  31.072 1.00 34.61  ? 7   SER A CA   1 
ATOM   71   C  C    . SER A 1 10  ? 3.665   11.397  29.773 1.00 30.67  ? 7   SER A C    1 
ATOM   72   O  O    . SER A 1 10  ? 3.834   12.034  28.726 1.00 29.42  ? 7   SER A O    1 
ATOM   73   C  CB   . SER A 1 10  ? 3.371   12.615  31.917 1.00 38.08  ? 7   SER A CB   1 
ATOM   74   O  OG   . SER A 1 10  ? 3.046   13.796  31.199 1.00 42.71  ? 7   SER A OG   1 
ATOM   75   H  H    . SER A 1 10  ? 5.393   13.445  30.947 1.00 42.07  ? 7   SER A H    1 
ATOM   76   H  HA   . SER A 1 10  ? 4.598   10.999  31.548 1.00 41.57  ? 7   SER A HA   1 
ATOM   77   H  HB2  . SER A 1 10  ? 2.566   12.096  32.075 1.00 45.73  ? 7   SER A HB2  1 
ATOM   78   H  HB3  . SER A 1 10  ? 3.786   12.849  32.762 1.00 45.73  ? 7   SER A HB3  1 
ATOM   79   H  HG   . SER A 1 10  ? 2.478   14.245  31.625 1.00 51.29  ? 7   SER A HG   1 
ATOM   80   N  N    . PRO A 1 11  ? 2.856   10.343  29.806 1.00 28.63  ? 8   PRO A N    1 
ATOM   81   C  CA   . PRO A 1 11  ? 2.097   9.987   28.605 1.00 24.67  ? 8   PRO A CA   1 
ATOM   82   C  C    . PRO A 1 11  ? 1.070   11.057  28.238 1.00 29.05  ? 8   PRO A C    1 
ATOM   83   O  O    . PRO A 1 11  ? 0.658   11.886  29.052 1.00 29.30  ? 8   PRO A O    1 
ATOM   84   C  CB   . PRO A 1 11  ? 1.425   8.651   28.963 1.00 33.46  ? 8   PRO A CB   1 
ATOM   85   C  CG   . PRO A 1 11  ? 1.426   8.600   30.456 1.00 38.93  ? 8   PRO A CG   1 
ATOM   86   C  CD   . PRO A 1 11  ? 2.620   9.393   30.913 1.00 34.17  ? 8   PRO A CD   1 
ATOM   87   H  HA   . PRO A 1 11  ? 2.698   9.848   27.856 1.00 29.63  ? 8   PRO A HA   1 
ATOM   88   H  HB2  . PRO A 1 11  ? 0.520   8.634   28.616 1.00 40.19  ? 8   PRO A HB2  1 
ATOM   89   H  HB3  . PRO A 1 11  ? 1.936   7.915   28.591 1.00 40.19  ? 8   PRO A HB3  1 
ATOM   90   H  HG2  . PRO A 1 11  ? 0.607   8.994   30.794 1.00 46.76  ? 8   PRO A HG2  1 
ATOM   91   H  HG3  . PRO A 1 11  ? 1.497   7.678   30.750 1.00 46.76  ? 8   PRO A HG3  1 
ATOM   92   H  HD2  . PRO A 1 11  ? 2.423   9.866   31.736 1.00 41.04  ? 8   PRO A HD2  1 
ATOM   93   H  HD3  . PRO A 1 11  ? 3.388   8.814   31.038 1.00 41.04  ? 8   PRO A HD3  1 
ATOM   94   N  N    A SER A 1 12  ? 0.653   11.004  26.975 0.42 25.06  ? 9   SER A N    1 
ATOM   95   N  N    B SER A 1 12  ? 0.683   11.052  26.959 0.58 24.98  ? 9   SER A N    1 
ATOM   96   C  CA   A SER A 1 12  ? -0.295  11.948  26.401 0.42 27.78  ? 9   SER A CA   1 
ATOM   97   C  CA   B SER A 1 12  ? -0.324  11.978  26.457 0.58 27.81  ? 9   SER A CA   1 
ATOM   98   C  C    A SER A 1 12  ? -1.517  11.200  25.897 0.42 26.41  ? 9   SER A C    1 
ATOM   99   C  C    B SER A 1 12  ? -1.514  11.214  25.912 0.58 26.33  ? 9   SER A C    1 
ATOM   100  O  O    A SER A 1 12  ? -1.397  10.327  25.027 0.42 25.28  ? 9   SER A O    1 
ATOM   101  O  O    B SER A 1 12  ? -1.366  10.350  25.036 0.58 25.34  ? 9   SER A O    1 
ATOM   102  C  CB   A SER A 1 12  ? 0.369   12.734  25.272 0.42 28.18  ? 9   SER A CB   1 
ATOM   103  C  CB   B SER A 1 12  ? 0.258   12.891  25.378 0.58 27.56  ? 9   SER A CB   1 
ATOM   104  O  OG   A SER A 1 12  ? -0.464  13.774  24.849 0.42 32.20  ? 9   SER A OG   1 
ATOM   105  O  OG   B SER A 1 12  ? 1.095   13.827  26.007 0.58 31.45  ? 9   SER A OG   1 
ATOM   106  H  H    A SER A 1 12  ? 0.916   10.408  26.414 0.42 30.11  ? 9   SER A H    1 
ATOM   107  H  H    B SER A 1 12  ? 0.995   10.516  26.363 0.58 30.01  ? 9   SER A H    1 
ATOM   108  H  HA   A SER A 1 12  ? -0.598  12.567  27.084 0.42 33.37  ? 9   SER A HA   1 
ATOM   109  H  HA   B SER A 1 12  ? -0.638  12.527  27.192 0.58 33.41  ? 9   SER A HA   1 
ATOM   110  H  HB2  A SER A 1 12  ? 1.205   13.107  25.593 0.42 33.85  ? 9   SER A HB2  1 
ATOM   111  H  HB2  B SER A 1 12  ? 0.773   12.365  24.747 0.58 33.11  ? 9   SER A HB2  1 
ATOM   112  H  HB3  A SER A 1 12  ? 0.537   12.138  24.525 0.42 33.85  ? 9   SER A HB3  1 
ATOM   113  H  HB3  B SER A 1 12  ? -0.460  13.352  24.918 0.58 33.11  ? 9   SER A HB3  1 
ATOM   114  H  HG   A SER A 1 12  ? -0.078  14.229  24.258 0.42 38.67  ? 9   SER A HG   1 
ATOM   115  H  HG   B SER A 1 12  ? 1.451   14.326  25.432 0.58 37.77  ? 9   SER A HG   1 
ATOM   116  N  N    . TYR A 1 13  ? -2.693  11.548  26.427 1.00 25.43  ? 10  TYR A N    1 
ATOM   117  C  CA   . TYR A 1 13  ? -3.940  10.864  26.091 1.00 23.07  ? 10  TYR A CA   1 
ATOM   118  C  C    . TYR A 1 13  ? -4.932  11.888  25.560 1.00 26.56  ? 10  TYR A C    1 
ATOM   119  O  O    . TYR A 1 13  ? -5.363  12.785  26.296 1.00 26.86  ? 10  TYR A O    1 
ATOM   120  C  CB   . TYR A 1 13  ? -4.492  10.155  27.320 1.00 26.38  ? 10  TYR A CB   1 
ATOM   121  C  CG   . TYR A 1 13  ? -5.780  9.382   27.117 1.00 25.29  ? 10  TYR A CG   1 
ATOM   122  C  CD1  . TYR A 1 13  ? -6.082  8.770   25.914 1.00 28.46  ? 10  TYR A CD1  1 
ATOM   123  C  CD2  . TYR A 1 13  ? -6.670  9.233   28.173 1.00 30.41  ? 10  TYR A CD2  1 
ATOM   124  C  CE1  . TYR A 1 13  ? -7.268  8.053   25.745 1.00 28.01  ? 10  TYR A CE1  1 
ATOM   125  C  CE2  . TYR A 1 13  ? -7.851  8.517   28.023 1.00 37.39  ? 10  TYR A CE2  1 
ATOM   126  C  CZ   . TYR A 1 13  ? -8.133  7.926   26.805 1.00 39.36  ? 10  TYR A CZ   1 
ATOM   127  O  OH   . TYR A 1 13  ? -9.288  7.221   26.647 1.00 36.55  ? 10  TYR A OH   1 
ATOM   128  H  H    A TYR A 1 13  ? -2.792  12.188  26.993 0.42 30.55  ? 10  TYR A H    1 
ATOM   129  H  H    B TYR A 1 13  ? -2.801  12.188  26.992 0.58 30.55  ? 10  TYR A H    1 
ATOM   130  H  HA   . TYR A 1 13  ? -3.780  10.213  25.390 1.00 27.72  ? 10  TYR A HA   1 
ATOM   131  H  HB2  . TYR A 1 13  ? -3.824  9.524   27.631 1.00 31.69  ? 10  TYR A HB2  1 
ATOM   132  H  HB3  . TYR A 1 13  ? -4.662  10.822  28.004 1.00 31.69  ? 10  TYR A HB3  1 
ATOM   133  H  HD1  . TYR A 1 13  ? -5.484  8.838   25.205 1.00 34.19  ? 10  TYR A HD1  1 
ATOM   134  H  HD2  . TYR A 1 13  ? -6.472  9.619   28.996 1.00 36.53  ? 10  TYR A HD2  1 
ATOM   135  H  HE1  . TYR A 1 13  ? -7.469  7.665   24.924 1.00 33.64  ? 10  TYR A HE1  1 
ATOM   136  H  HE2  . TYR A 1 13  ? -8.446  8.435   28.733 1.00 44.90  ? 10  TYR A HE2  1 
ATOM   137  H  HH   . TYR A 1 13  ? -9.666  7.118   27.390 1.00 43.90  ? 10  TYR A HH   1 
ATOM   138  N  N    . LEU A 1 14  ? -5.265  11.768  24.282 1.00 22.82  ? 11  LEU A N    1 
ATOM   139  C  CA   . LEU A 1 14  ? -6.284  12.602  23.665 1.00 25.11  ? 11  LEU A CA   1 
ATOM   140  C  C    . LEU A 1 14  ? -7.548  11.774  23.468 1.00 25.48  ? 11  LEU A C    1 
ATOM   141  O  O    . LEU A 1 14  ? -7.533  10.770  22.752 1.00 27.69  ? 11  LEU A O    1 
ATOM   142  C  CB   . LEU A 1 14  ? -5.782  13.117  22.333 1.00 24.56  ? 11  LEU A CB   1 
ATOM   143  C  CG   . LEU A 1 14  ? -4.668  14.127  22.378 1.00 26.38  ? 11  LEU A CG   1 
ATOM   144  C  CD1  . LEU A 1 14  ? -4.018  14.184  21.001 1.00 36.67  ? 11  LEU A CD1  1 
ATOM   145  C  CD2  . LEU A 1 14  ? -5.150  15.487  22.709 1.00 36.13  ? 11  LEU A CD2  1 
ATOM   146  H  H    . LEU A 1 14  ? -4.908  11.201  23.743 1.00 27.41  ? 11  LEU A H    1 
ATOM   147  H  HA   . LEU A 1 14  ? -6.499  13.351  24.242 1.00 30.17  ? 11  LEU A HA   1 
ATOM   148  H  HB2  . LEU A 1 14  ? -5.459  12.360  21.821 1.00 29.51  ? 11  LEU A HB2  1 
ATOM   149  H  HB3  . LEU A 1 14  ? -6.527  13.535  21.873 1.00 29.51  ? 11  LEU A HB3  1 
ATOM   150  H  HG   . LEU A 1 14  ? -4.041  13.858  23.067 1.00 31.69  ? 11  LEU A HG   1 
ATOM   151  H  HD11 . LEU A 1 14  ? -3.249  14.775  21.038 1.00 44.04  ? 11  LEU A HD11 1 
ATOM   152  H  HD12 . LEU A 1 14  ? -3.736  13.291  20.747 1.00 44.04  ? 11  LEU A HD12 1 
ATOM   153  H  HD13 . LEU A 1 14  ? -4.663  14.522  20.360 1.00 44.04  ? 11  LEU A HD13 1 
ATOM   154  H  HD21 . LEU A 1 14  ? -4.438  16.124  22.539 1.00 43.39  ? 11  LEU A HD21 1 
ATOM   155  H  HD22 . LEU A 1 14  ? -5.918  15.694  22.153 1.00 43.39  ? 11  LEU A HD22 1 
ATOM   156  H  HD23 . LEU A 1 14  ? -5.402  15.514  23.645 1.00 43.39  ? 11  LEU A HD23 1 
ATOM   157  N  N    . LYS A 1 15  ? -8.617  12.158  24.156 1.00 24.32  ? 12  LYS A N    1 
ATOM   158  C  CA   . LYS A 1 15  ? -9.896  11.478  24.011 1.00 25.72  ? 12  LYS A CA   1 
ATOM   159  C  C    . LYS A 1 15  ? -10.618 12.005  22.782 1.00 29.96  ? 12  LYS A C    1 
ATOM   160  O  O    . LYS A 1 15  ? -10.776 13.223  22.611 1.00 28.03  ? 12  LYS A O    1 
ATOM   161  C  CB   . LYS A 1 15  ? -10.762 11.654  25.269 1.00 27.63  ? 12  LYS A CB   1 
ATOM   162  C  CG   . LYS A 1 15  ? -10.148 10.978  26.494 1.00 41.02  ? 12  LYS A CG   1 
ATOM   163  C  CD   . LYS A 1 15  ? -10.331 11.752  27.825 1.00 55.55  ? 12  LYS A CD   1 
ATOM   164  C  CE   . LYS A 1 15  ? -9.656  13.149  27.823 1.00 66.49  ? 12  LYS A CE   1 
ATOM   165  N  NZ   . LYS A 1 15  ? -8.145  13.193  27.770 1.00 42.63  ? 12  LYS A NZ   1 
ATOM   166  H  H    . LYS A 1 15  ? -8.626  12.812  24.715 1.00 29.22  ? 12  LYS A H    1 
ATOM   167  H  HA   . LYS A 1 15  ? -9.743  10.527  23.896 1.00 30.90  ? 12  LYS A HA   1 
ATOM   168  H  HB2  . LYS A 1 15  ? -10.854 12.601  25.461 1.00 33.19  ? 12  LYS A HB2  1 
ATOM   169  H  HB3  . LYS A 1 15  ? -11.634 11.261  25.111 1.00 33.19  ? 12  LYS A HB3  1 
ATOM   170  H  HG2  . LYS A 1 15  ? -10.561 10.107  26.605 1.00 49.26  ? 12  LYS A HG2  1 
ATOM   171  H  HG3  . LYS A 1 15  ? -9.195  10.876  26.345 1.00 49.26  ? 12  LYS A HG3  1 
ATOM   172  H  HD2  . LYS A 1 15  ? -11.279 11.880  27.985 1.00 66.69  ? 12  LYS A HD2  1 
ATOM   173  H  HD3  . LYS A 1 15  ? -9.940  11.234  28.545 1.00 66.69  ? 12  LYS A HD3  1 
ATOM   174  H  HE2  . LYS A 1 15  ? -9.978  13.635  27.048 1.00 79.83  ? 12  LYS A HE2  1 
ATOM   175  H  HE3  . LYS A 1 15  ? -9.921  13.609  28.635 1.00 79.83  ? 12  LYS A HE3  1 
ATOM   176  H  HZ1  . LYS A 1 15  ? -7.867  14.037  27.725 1.00 51.18  ? 12  LYS A HZ1  1 
ATOM   177  H  HZ2  . LYS A 1 15  ? -7.804  12.815  28.500 1.00 51.18  ? 12  LYS A HZ2  1 
ATOM   178  H  HZ3  . LYS A 1 15  ? -7.853  12.754  27.054 1.00 51.18  ? 12  LYS A HZ3  1 
ATOM   179  N  N    . GLY A 1 16  ? -11.063 11.085  21.933 1.00 28.18  ? 13  GLY A N    1 
ATOM   180  C  CA   . GLY A 1 16  ? -11.827 11.409  20.754 1.00 32.42  ? 13  GLY A CA   1 
ATOM   181  C  C    . GLY A 1 16  ? -13.259 10.933  20.882 1.00 33.00  ? 13  GLY A C    1 
ATOM   182  O  O    . GLY A 1 16  ? -13.729 10.557  21.954 1.00 34.95  ? 13  GLY A O    1 
ATOM   183  H  H    . GLY A 1 16  ? -10.927 10.241  22.029 1.00 33.86  ? 13  GLY A H    1 
ATOM   184  H  HA2  . GLY A 1 16  ? -11.829 12.370  20.622 1.00 38.94  ? 13  GLY A HA2  1 
ATOM   185  H  HA3  . GLY A 1 16  ? -11.426 10.984  19.980 1.00 38.94  ? 13  GLY A HA3  1 
ATOM   186  N  N    . THR A 1 17  ? -13.955 10.967  19.768 1.00 33.67  ? 14  THR A N    1 
ATOM   187  C  CA   . THR A 1 17  ? -15.384 10.730  19.768 1.00 33.56  ? 14  THR A CA   1 
ATOM   188  C  C    . THR A 1 17  ? -15.831 9.526   18.947 1.00 35.87  ? 14  THR A C    1 
ATOM   189  O  O    . THR A 1 17  ? -16.997 9.139   19.078 1.00 38.29  ? 14  THR A O    1 
ATOM   190  C  CB   . THR A 1 17  ? -16.125 11.968  19.230 1.00 39.29  ? 14  THR A CB   1 
ATOM   191  O  OG1  . THR A 1 17  ? -15.570 12.338  17.959 1.00 38.15  ? 14  THR A OG1  1 
ATOM   192  C  CG2  . THR A 1 17  ? -16.001 13.131  20.205 1.00 43.60  ? 14  THR A CG2  1 
ATOM   193  H  H    . THR A 1 17  ? -13.622 11.126  18.991 1.00 40.43  ? 14  THR A H    1 
ATOM   194  H  HA   . THR A 1 17  ? -15.654 10.573  20.686 1.00 40.31  ? 14  THR A HA   1 
ATOM   195  H  HB   . THR A 1 17  ? -17.068 11.767  19.123 1.00 47.18  ? 14  THR A HB   1 
ATOM   196  H  HG1  . THR A 1 17  ? -15.880 13.079  17.715 1.00 45.81  ? 14  THR A HG1  1 
ATOM   197  H  HG21 . THR A 1 17  ? -16.474 13.904  19.860 1.00 52.36  ? 14  THR A HG21 1 
ATOM   198  H  HG22 . THR A 1 17  ? -16.381 12.886  21.063 1.00 52.36  ? 14  THR A HG22 1 
ATOM   199  H  HG23 . THR A 1 17  ? -15.067 13.362  20.328 1.00 52.36  ? 14  THR A HG23 1 
ATOM   200  N  N    . ASN A 1 18  ? -14.975 8.933   18.105 1.00 34.48  ? 15  ASN A N    1 
ATOM   201  C  CA   . ASN A 1 18  ? -15.459 7.978   17.108 1.00 36.16  ? 15  ASN A CA   1 
ATOM   202  C  C    . ASN A 1 18  ? -15.326 6.533   17.560 1.00 36.86  ? 15  ASN A C    1 
ATOM   203  O  O    . ASN A 1 18  ? -15.719 5.635   16.815 1.00 39.69  ? 15  ASN A O    1 
ATOM   204  C  CB   . ASN A 1 18  ? -14.776 8.172   15.733 1.00 31.33  ? 15  ASN A CB   1 
ATOM   205  C  CG   . ASN A 1 18  ? -13.271 7.853   15.721 1.00 30.03  ? 15  ASN A CG   1 
ATOM   206  O  OD1  . ASN A 1 18  ? -12.722 7.248   16.638 1.00 31.25  ? 15  ASN A OD1  1 
ATOM   207  N  ND2  . ASN A 1 18  ? -12.603 8.295   14.666 1.00 33.95  ? 15  ASN A ND2  1 
ATOM   208  H  H    . ASN A 1 18  ? -14.126 9.068   18.094 1.00 41.42  ? 15  ASN A H    1 
ATOM   209  H  HA   . ASN A 1 18  ? -16.400 8.164   16.964 1.00 43.43  ? 15  ASN A HA   1 
ATOM   210  H  HB2  . ASN A 1 18  ? -15.205 7.587   15.089 1.00 37.64  ? 15  ASN A HB2  1 
ATOM   211  H  HB3  . ASN A 1 18  ? -14.882 9.097   15.462 1.00 37.64  ? 15  ASN A HB3  1 
ATOM   212  H  HD21 . ASN A 1 18  ? -11.758 8.149   14.600 1.00 40.77  ? 15  ASN A HD21 1 
ATOM   213  H  HD22 . ASN A 1 18  ? -13.014 8.728   14.047 1.00 40.77  ? 15  ASN A HD22 1 
ATOM   214  N  N    . GLY A 1 19  ? -14.795 6.293   18.767 1.00 34.22  ? 16  GLY A N    1 
ATOM   215  C  CA   . GLY A 1 19  ? -14.721 4.969   19.352 1.00 33.21  ? 16  GLY A CA   1 
ATOM   216  C  C    . GLY A 1 19  ? -13.498 4.161   18.969 1.00 35.51  ? 16  GLY A C    1 
ATOM   217  O  O    . GLY A 1 19  ? -13.340 3.031   19.465 1.00 38.89  ? 16  GLY A O    1 
ATOM   218  H  H    . GLY A 1 19  ? -14.465 6.906   19.273 1.00 41.10  ? 16  GLY A H    1 
ATOM   219  H  HA2  . GLY A 1 19  ? -14.725 5.058   20.318 1.00 39.88  ? 16  GLY A HA2  1 
ATOM   220  H  HA3  . GLY A 1 19  ? -15.504 4.466   19.078 1.00 39.88  ? 16  GLY A HA3  1 
ATOM   221  N  N    . HIS A 1 20  ? -12.647 4.686   18.099 1.00 30.62  ? 17  HIS A N    1 
ATOM   222  C  CA   . HIS A 1 20  ? -11.414 4.024   17.685 1.00 27.52  ? 17  HIS A CA   1 
ATOM   223  C  C    . HIS A 1 20  ? -10.243 4.673   18.393 1.00 31.62  ? 17  HIS A C    1 
ATOM   224  O  O    . HIS A 1 20  ? -10.187 5.900   18.517 1.00 32.03  ? 17  HIS A O    1 
ATOM   225  C  CB   . HIS A 1 20  ? -11.208 4.149   16.185 1.00 27.98  ? 17  HIS A CB   1 
ATOM   226  C  CG   . HIS A 1 20  ? -12.314 3.554   15.374 1.00 34.29  ? 17  HIS A CG   1 
ATOM   227  N  ND1  . HIS A 1 20  ? -12.430 2.196   15.145 1.00 36.20  ? 17  HIS A ND1  1 
ATOM   228  C  CD2  . HIS A 1 20  ? -13.388 4.132   14.784 1.00 36.42  ? 17  HIS A CD2  1 
ATOM   229  C  CE1  . HIS A 1 20  ? -13.511 1.969   14.419 1.00 36.76  ? 17  HIS A CE1  1 
ATOM   230  N  NE2  . HIS A 1 20  ? -14.110 3.125   14.187 1.00 39.19  ? 17  HIS A NE2  1 
ATOM   231  H  H    . HIS A 1 20  ? -12.763 5.449   17.721 1.00 36.78  ? 17  HIS A H    1 
ATOM   232  H  HA   . HIS A 1 20  ? -11.456 3.083   17.915 1.00 33.06  ? 17  HIS A HA   1 
ATOM   233  H  HB2  . HIS A 1 20  ? -11.146 5.089   15.956 1.00 33.61  ? 17  HIS A HB2  1 
ATOM   234  H  HB3  . HIS A 1 20  ? -10.387 3.693   15.944 1.00 33.61  ? 17  HIS A HB3  1 
ATOM   235  H  HD2  . HIS A 1 20  ? -13.597 5.038   14.783 1.00 43.73  ? 17  HIS A HD2  1 
ATOM   236  H  HE1  . HIS A 1 20  ? -13.801 1.137   14.122 1.00 44.15  ? 17  HIS A HE1  1 
ATOM   237  H  HE2  . HIS A 1 20  ? -14.834 3.231   13.736 1.00 47.06  ? 17  HIS A HE2  1 
ATOM   238  N  N    . ALA A 1 21  ? -9.291  3.852   18.815 1.00 26.46  ? 18  ALA A N    1 
ATOM   239  C  CA   . ALA A 1 21  ? -8.094  4.337   19.490 1.00 21.85  ? 18  ALA A CA   1 
ATOM   240  C  C    . ALA A 1 21  ? -6.846  3.976   18.701 1.00 23.88  ? 18  ALA A C    1 
ATOM   241  O  O    . ALA A 1 21  ? -6.757  2.897   18.091 1.00 24.89  ? 18  ALA A O    1 
ATOM   242  C  CB   . ALA A 1 21  ? -8.005  3.766   20.901 1.00 25.18  ? 18  ALA A CB   1 
ATOM   243  H  H    . ALA A 1 21  ? -9.316  2.997   18.721 1.00 31.78  ? 18  ALA A H    1 
ATOM   244  H  HA   . ALA A 1 21  ? -8.130  5.305   19.544 1.00 26.26  ? 18  ALA A HA   1 
ATOM   245  H  HB1  . ALA A 1 21  ? -7.220  4.130   21.340 1.00 30.25  ? 18  ALA A HB1  1 
ATOM   246  H  HB2  . ALA A 1 21  ? -8.803  4.014   21.393 1.00 30.25  ? 18  ALA A HB2  1 
ATOM   247  H  HB3  . ALA A 1 21  ? -7.936  2.800   20.847 1.00 30.25  ? 18  ALA A HB3  1 
ATOM   248  N  N    . ILE A 1 22  ? -5.882  4.887   18.733 1.00 21.14  ? 19  ILE A N    1 
ATOM   249  C  CA   . ILE A 1 22  ? -4.598  4.714   18.071 1.00 19.93  ? 19  ILE A CA   1 
ATOM   250  C  C    . ILE A 1 22  ? -3.492  4.902   19.095 1.00 22.14  ? 19  ILE A C    1 
ATOM   251  O  O    . ILE A 1 22  ? -3.455  5.919   19.809 1.00 23.60  ? 19  ILE A O    1 
ATOM   252  C  CB   . ILE A 1 22  ? -4.420  5.690   16.892 1.00 22.05  ? 19  ILE A CB   1 
ATOM   253  C  CG1  . ILE A 1 22  ? -5.586  5.520   15.908 1.00 28.12  ? 19  ILE A CG1  1 
ATOM   254  C  CG2  . ILE A 1 22  ? -3.068  5.430   16.212 1.00 24.45  ? 19  ILE A CG2  1 
ATOM   255  C  CD1  . ILE A 1 22  ? -5.585  6.527   14.805 1.00 33.02  ? 19  ILE A CD1  1 
ATOM   256  H  H    . ILE A 1 22  ? -5.952  5.639   19.146 1.00 25.41  ? 19  ILE A H    1 
ATOM   257  H  HA   . ILE A 1 22  ? -4.541  3.808   17.728 1.00 23.95  ? 19  ILE A HA   1 
ATOM   258  H  HB   . ILE A 1 22  ? -4.426  6.604   17.215 1.00 26.49  ? 19  ILE A HB   1 
ATOM   259  H  HG12 . ILE A 1 22  ? -5.532  4.639   15.506 1.00 33.78  ? 19  ILE A HG12 1 
ATOM   260  H  HG13 . ILE A 1 22  ? -6.421  5.612   16.393 1.00 33.78  ? 19  ILE A HG13 1 
ATOM   261  H  HG21 . ILE A 1 22  ? -3.009  5.972   15.409 1.00 29.37  ? 19  ILE A HG21 1 
ATOM   262  H  HG22 . ILE A 1 22  ? -2.355  5.668   16.825 1.00 29.37  ? 19  ILE A HG22 1 
ATOM   263  H  HG23 . ILE A 1 22  ? -3.006  4.490   15.981 1.00 29.37  ? 19  ILE A HG23 1 
ATOM   264  H  HD11 . ILE A 1 22  ? -6.434  6.485   14.338 1.00 39.66  ? 19  ILE A HD11 1 
ATOM   265  H  HD12 . ILE A 1 22  ? -5.461  7.411   15.185 1.00 39.66  ? 19  ILE A HD12 1 
ATOM   266  H  HD13 . ILE A 1 22  ? -4.860  6.325   14.194 1.00 39.66  ? 19  ILE A HD13 1 
ATOM   267  N  N    A LEU A 1 23  ? -2.546  3.966   19.110 0.48 21.66  ? 20  LEU A N    1 
ATOM   268  N  N    B LEU A 1 23  ? -2.620  3.902   19.200 0.52 21.68  ? 20  LEU A N    1 
ATOM   269  C  CA   A LEU A 1 23  ? -1.343  4.028   19.935 0.48 22.23  ? 20  LEU A CA   1 
ATOM   270  C  CA   B LEU A 1 23  ? -1.349  4.067   19.880 0.52 22.25  ? 20  LEU A CA   1 
ATOM   271  C  C    A LEU A 1 23  ? -0.186  4.537   19.088 0.48 22.05  ? 20  LEU A C    1 
ATOM   272  C  C    B LEU A 1 23  ? -0.373  4.746   18.948 0.52 22.29  ? 20  LEU A C    1 
ATOM   273  O  O    A LEU A 1 23  ? 0.187   3.891   18.095 0.48 21.86  ? 20  LEU A O    1 
ATOM   274  O  O    B LEU A 1 23  ? -0.301  4.421   17.761 0.52 22.81  ? 20  LEU A O    1 
ATOM   275  C  CB   A LEU A 1 23  ? -1.028  2.641   20.496 0.48 22.23  ? 20  LEU A CB   1 
ATOM   276  C  CB   B LEU A 1 23  ? -0.760  2.727   20.294 0.52 22.43  ? 20  LEU A CB   1 
ATOM   277  C  CG   A LEU A 1 23  ? 0.121   2.525   21.487 0.48 22.91  ? 20  LEU A CG   1 
ATOM   278  C  CG   B LEU A 1 23  ? -1.516  2.018   21.404 0.52 22.86  ? 20  LEU A CG   1 
ATOM   279  C  CD1  A LEU A 1 23  ? -0.197  3.286   22.740 0.48 19.04  ? 20  LEU A CD1  1 
ATOM   280  C  CD1  B LEU A 1 23  ? -1.217  0.537   21.386 0.52 26.04  ? 20  LEU A CD1  1 
ATOM   281  C  CD2  A LEU A 1 23  ? 0.411   1.068   21.786 0.48 27.01  ? 20  LEU A CD2  1 
ATOM   282  C  CD2  B LEU A 1 23  ? -1.120  2.683   22.710 0.52 28.07  ? 20  LEU A CD2  1 
ATOM   283  H  H    A LEU A 1 23  ? -2.580  3.254   18.629 0.48 26.03  ? 20  LEU A H    1 
ATOM   284  H  H    B LEU A 1 23  ? -2.747  3.113   18.881 0.52 26.05  ? 20  LEU A H    1 
ATOM   285  H  HA   A LEU A 1 23  ? -1.474  4.647   20.670 0.48 26.71  ? 20  LEU A HA   1 
ATOM   286  H  HA   B LEU A 1 23  ? -1.485  4.599   20.680 0.52 26.74  ? 20  LEU A HA   1 
ATOM   287  H  HB2  A LEU A 1 23  ? -1.823  2.317   20.948 0.48 26.71  ? 20  LEU A HB2  1 
ATOM   288  H  HB2  B LEU A 1 23  ? -0.757  2.141   19.521 0.52 26.95  ? 20  LEU A HB2  1 
ATOM   289  H  HB3  A LEU A 1 23  ? -0.813  2.061   19.748 0.48 26.71  ? 20  LEU A HB3  1 
ATOM   290  H  HB3  B LEU A 1 23  ? 0.147   2.872   20.604 0.52 26.95  ? 20  LEU A HB3  1 
ATOM   291  H  HG   A LEU A 1 23  ? 0.923   2.912   21.103 0.48 27.53  ? 20  LEU A HG   1 
ATOM   292  H  HG   B LEU A 1 23  ? -2.477  2.088   21.294 0.52 27.47  ? 20  LEU A HG   1 
ATOM   293  H  HD11 A LEU A 1 23  ? 0.582   3.281   23.319 0.48 22.89  ? 20  LEU A HD11 1 
ATOM   294  H  HD11 B LEU A 1 23  ? -1.661  0.116   22.139 0.52 31.28  ? 20  LEU A HD11 1 
ATOM   295  H  HD12 A LEU A 1 23  ? -0.427  4.199   22.505 0.48 22.89  ? 20  LEU A HD12 1 
ATOM   296  H  HD12 B LEU A 1 23  ? -1.545  0.159   20.555 0.52 31.28  ? 20  LEU A HD12 1 
ATOM   297  H  HD13 A LEU A 1 23  ? -0.945  2.861   23.187 0.48 22.89  ? 20  LEU A HD13 1 
ATOM   298  H  HD13 B LEU A 1 23  ? -0.258  0.408   21.452 0.52 31.28  ? 20  LEU A HD13 1 
ATOM   299  H  HD21 A LEU A 1 23  ? 1.047   1.016   22.516 0.48 32.45  ? 20  LEU A HD21 1 
ATOM   300  H  HD21 B LEU A 1 23  ? -1.567  2.232   23.443 0.52 33.72  ? 20  LEU A HD21 1 
ATOM   301  H  HD22 A LEU A 1 23  ? -0.416  0.626   22.035 0.48 32.45  ? 20  LEU A HD22 1 
ATOM   302  H  HD22 B LEU A 1 23  ? -0.158  2.617   22.819 0.52 33.72  ? 20  LEU A HD22 1 
ATOM   303  H  HD23 A LEU A 1 23  ? 0.783   0.651   20.993 0.48 32.45  ? 20  LEU A HD23 1 
ATOM   304  H  HD23 B LEU A 1 23  ? -1.387  3.615   22.684 0.52 33.72  ? 20  LEU A HD23 1 
ATOM   305  N  N    . LEU A 1 24  ? 0.385   5.681   19.487 1.00 19.90  ? 21  LEU A N    1 
ATOM   306  C  CA   . LEU A 1 24  ? 1.460   6.339   18.746 1.00 20.55  ? 21  LEU A CA   1 
ATOM   307  C  C    . LEU A 1 24  ? 2.784   6.197   19.486 1.00 23.50  ? 21  LEU A C    1 
ATOM   308  O  O    . LEU A 1 24  ? 2.885   6.594   20.655 1.00 21.92  ? 21  LEU A O    1 
ATOM   309  C  CB   . LEU A 1 24  ? 1.155   7.807   18.493 1.00 21.39  ? 21  LEU A CB   1 
ATOM   310  C  CG   . LEU A 1 24  ? -0.078  8.105   17.652 1.00 23.23  ? 21  LEU A CG   1 
ATOM   311  C  CD1  . LEU A 1 24  ? -1.252  8.438   18.560 1.00 25.94  ? 21  LEU A CD1  1 
ATOM   312  C  CD2  . LEU A 1 24  ? 0.191   9.244   16.674 1.00 27.12  ? 21  LEU A CD2  1 
ATOM   313  H  H    A LEU A 1 24  ? 0.158   6.102   20.202 0.48 23.91  ? 21  LEU A H    1 
ATOM   314  H  H    B LEU A 1 24  ? 0.300   5.961   20.295 0.52 23.91  ? 21  LEU A H    1 
ATOM   315  H  HA   . LEU A 1 24  ? 1.549   5.889   17.892 1.00 24.69  ? 21  LEU A HA   1 
ATOM   316  H  HB2  . LEU A 1 24  ? 1.026   8.240   19.351 1.00 25.70  ? 21  LEU A HB2  1 
ATOM   317  H  HB3  . LEU A 1 24  ? 1.915   8.198   18.034 1.00 25.70  ? 21  LEU A HB3  1 
ATOM   318  H  HG   . LEU A 1 24  ? -0.306  7.322   17.127 1.00 27.91  ? 21  LEU A HG   1 
ATOM   319  H  HD11 . LEU A 1 24  ? -2.051  8.543   18.019 1.00 31.16  ? 21  LEU A HD11 1 
ATOM   320  H  HD12 . LEU A 1 24  ? -1.376  7.715   19.195 1.00 31.16  ? 21  LEU A HD12 1 
ATOM   321  H  HD13 . LEU A 1 24  ? -1.062  9.264   19.032 1.00 31.16  ? 21  LEU A HD13 1 
ATOM   322  H  HD21 . LEU A 1 24  ? -0.625  9.442   16.188 1.00 32.58  ? 21  LEU A HD21 1 
ATOM   323  H  HD22 . LEU A 1 24  ? 0.479   10.025  17.171 1.00 32.58  ? 21  LEU A HD22 1 
ATOM   324  H  HD23 . LEU A 1 24  ? 0.886   8.971   16.055 1.00 32.58  ? 21  LEU A HD23 1 
ATOM   325  N  N    . LEU A 1 25  ? 3.792   5.641   18.803 1.00 20.09  ? 22  LEU A N    1 
ATOM   326  C  CA   . LEU A 1 25  ? 5.042   5.196   19.431 1.00 22.38  ? 22  LEU A CA   1 
ATOM   327  C  C    . LEU A 1 25  ? 6.238   5.909   18.806 1.00 20.76  ? 22  LEU A C    1 
ATOM   328  O  O    . LEU A 1 25  ? 6.409   5.931   17.570 1.00 21.07  ? 22  LEU A O    1 
ATOM   329  C  CB   . LEU A 1 25  ? 5.199   3.664   19.302 1.00 21.62  ? 22  LEU A CB   1 
ATOM   330  C  CG   . LEU A 1 25  ? 3.988   2.925   19.849 1.00 23.07  ? 22  LEU A CG   1 
ATOM   331  C  CD1  . LEU A 1 25  ? 3.967   1.486   19.566 1.00 28.13  ? 22  LEU A CD1  1 
ATOM   332  C  CD2  . LEU A 1 25  ? 3.901   3.121   21.367 1.00 24.17  ? 22  LEU A CD2  1 
ATOM   333  H  H    . LEU A 1 25  ? 3.775   5.509   17.953 1.00 24.15  ? 22  LEU A H    1 
ATOM   334  H  HA   . LEU A 1 25  ? 5.026   5.433   20.371 1.00 26.90  ? 22  LEU A HA   1 
ATOM   335  H  HB2  . LEU A 1 25  ? 5.301   3.432   18.366 1.00 25.98  ? 22  LEU A HB2  1 
ATOM   336  H  HB3  . LEU A 1 25  ? 5.981   3.381   19.802 1.00 25.98  ? 22  LEU A HB3  1 
ATOM   337  H  HG   . LEU A 1 25  ? 3.220   3.305   19.394 1.00 27.72  ? 22  LEU A HG   1 
ATOM   338  H  HD11 . LEU A 1 25  ? 3.106   1.125   19.829 1.00 33.79  ? 22  LEU A HD11 1 
ATOM   339  H  HD12 . LEU A 1 25  ? 4.107   1.349   18.616 1.00 33.79  ? 22  LEU A HD12 1 
ATOM   340  H  HD13 . LEU A 1 25  ? 4.674   1.055   20.071 1.00 33.79  ? 22  LEU A HD13 1 
ATOM   341  H  HD21 . LEU A 1 25  ? 3.270   2.482   21.733 1.00 29.04  ? 22  LEU A HD21 1 
ATOM   342  H  HD22 . LEU A 1 25  ? 4.779   2.978   21.755 1.00 29.04  ? 22  LEU A HD22 1 
ATOM   343  H  HD23 . LEU A 1 25  ? 3.602   4.025   21.553 1.00 29.04  ? 22  LEU A HD23 1 
ATOM   344  N  N    . HIS A 1 26  ? 7.084   6.479   19.658 1.00 18.31  ? 23  HIS A N    1 
ATOM   345  C  CA   . HIS A 1 26  ? 8.160   7.363   19.264 1.00 20.90  ? 23  HIS A CA   1 
ATOM   346  C  C    . HIS A 1 26  ? 9.472   6.630   18.957 1.00 21.07  ? 23  HIS A C    1 
ATOM   347  O  O    . HIS A 1 26  ? 9.613   5.417   19.046 1.00 21.29  ? 23  HIS A O    1 
ATOM   348  C  CB   . HIS A 1 26  ? 8.341   8.465   20.331 1.00 21.47  ? 23  HIS A CB   1 
ATOM   349  C  CG   . HIS A 1 26  ? 8.893   8.026   21.670 1.00 21.20  ? 23  HIS A CG   1 
ATOM   350  N  ND1  . HIS A 1 26  ? 10.240  7.839   21.899 1.00 23.89  ? 23  HIS A ND1  1 
ATOM   351  C  CD2  . HIS A 1 26  ? 8.281   7.803   22.865 1.00 23.49  ? 23  HIS A CD2  1 
ATOM   352  C  CE1  . HIS A 1 26  ? 10.434  7.493   23.169 1.00 24.03  ? 23  HIS A CE1  1 
ATOM   353  N  NE2  . HIS A 1 26  ? 9.260   7.450   23.772 1.00 22.83  ? 23  HIS A NE2  1 
ATOM   354  H  H    . HIS A 1 26  ? 7.049   6.360   20.509 1.00 22.01  ? 23  HIS A H    1 
ATOM   355  H  HA   . HIS A 1 26  ? 7.903   7.772   18.423 1.00 25.12  ? 23  HIS A HA   1 
ATOM   356  H  HB2  . HIS A 1 26  ? 8.952   9.130   19.976 1.00 25.80  ? 23  HIS A HB2  1 
ATOM   357  H  HB3  . HIS A 1 26  ? 7.474   8.866   20.499 1.00 25.80  ? 23  HIS A HB3  1 
ATOM   358  H  HD1  . HIS A 1 26  ? 10.860  7.932   21.310 1.00 28.70  ? 23  HIS A HD1  1 
ATOM   359  H  HD2  . HIS A 1 26  ? 7.370   7.874   23.038 1.00 28.23  ? 23  HIS A HD2  1 
ATOM   360  H  HE1  . HIS A 1 26  ? 11.257  7.313   23.565 1.00 28.87  ? 23  HIS A HE1  1 
ATOM   361  N  N    . SER A 1 27  ? 10.448  7.415   18.547 1.00 22.01  ? 24  SER A N    1 
ATOM   362  C  CA   . SER A 1 27  ? 11.723  6.928   18.061 1.00 23.38  ? 24  SER A CA   1 
ATOM   363  C  C    . SER A 1 27  ? 12.697  6.623   19.199 1.00 26.88  ? 24  SER A C    1 
ATOM   364  O  O    . SER A 1 27  ? 12.528  7.057   20.352 1.00 26.52  ? 24  SER A O    1 
ATOM   365  C  CB   . SER A 1 27  ? 12.366  7.973   17.136 1.00 24.81  ? 24  SER A CB   1 
ATOM   366  O  OG   . SER A 1 27  ? 12.868  9.130   17.854 1.00 27.80  ? 24  SER A OG   1 
ATOM   367  H  H    . SER A 1 27  ? 10.397  8.274   18.540 1.00 26.44  ? 24  SER A H    1 
ATOM   368  H  HA   . SER A 1 27  ? 11.564  6.104   17.575 1.00 28.09  ? 24  SER A HA   1 
ATOM   369  H  HB2  . SER A 1 27  ? 13.106  7.556   16.668 1.00 29.81  ? 24  SER A HB2  1 
ATOM   370  H  HB3  . SER A 1 27  ? 11.698  8.273   16.499 1.00 29.81  ? 24  SER A HB3  1 
ATOM   371  H  HG   . SER A 1 27  ? 12.231  9.549   18.205 1.00 33.40  ? 24  SER A HG   1 
ATOM   372  N  N    . PHE A 1 28  ? 13.750  5.882   18.840 1.00 27.65  ? 25  PHE A N    1 
ATOM   373  C  CA   . PHE A 1 28  ? 14.872  5.599   19.733 1.00 33.52  ? 25  PHE A CA   1 
ATOM   374  C  C    . PHE A 1 28  ? 15.615  6.890   20.040 1.00 30.64  ? 25  PHE A C    1 
ATOM   375  O  O    . PHE A 1 28  ? 16.028  7.618   19.130 1.00 28.52  ? 25  PHE A O    1 
ATOM   376  C  CB   . PHE A 1 28  ? 15.818  4.599   19.073 1.00 31.70  ? 25  PHE A CB   1 
ATOM   377  C  CG   . PHE A 1 28  ? 17.021  4.230   19.902 1.00 33.80  ? 25  PHE A CG   1 
ATOM   378  C  CD1  . PHE A 1 28  ? 16.872  3.779   21.202 1.00 34.71  ? 25  PHE A CD1  1 
ATOM   379  C  CD2  . PHE A 1 28  ? 18.295  4.312   19.367 1.00 37.81  ? 25  PHE A CD2  1 
ATOM   380  C  CE1  . PHE A 1 28  ? 17.973  3.417   21.963 1.00 33.36  ? 25  PHE A CE1  1 
ATOM   381  C  CE2  . PHE A 1 28  ? 19.399  3.951   20.124 1.00 40.44  ? 25  PHE A CE2  1 
ATOM   382  C  CZ   . PHE A 1 28  ? 19.234  3.504   21.427 1.00 39.24  ? 25  PHE A CZ   1 
ATOM   383  H  H    . PHE A 1 28  ? 13.840  5.523   18.064 1.00 33.21  ? 25  PHE A H    1 
ATOM   384  H  HA   . PHE A 1 28  ? 14.549  5.216   20.564 1.00 40.25  ? 25  PHE A HA   1 
ATOM   385  H  HB2  . PHE A 1 28  ? 15.326  3.782   18.892 1.00 38.08  ? 25  PHE A HB2  1 
ATOM   386  H  HB3  . PHE A 1 28  ? 16.142  4.982   18.242 1.00 38.08  ? 25  PHE A HB3  1 
ATOM   387  H  HD1  . PHE A 1 28  ? 16.021  3.717   21.571 1.00 41.69  ? 25  PHE A HD1  1 
ATOM   388  H  HD2  . PHE A 1 28  ? 18.412  4.611   18.494 1.00 45.41  ? 25  PHE A HD2  1 
ATOM   389  H  HE1  . PHE A 1 28  ? 17.858  3.117   22.835 1.00 40.07  ? 25  PHE A HE1  1 
ATOM   390  H  HE2  . PHE A 1 28  ? 20.252  4.008   19.757 1.00 48.56  ? 25  PHE A HE2  1 
ATOM   391  H  HZ   . PHE A 1 28  ? 19.975  3.264   21.936 1.00 47.12  ? 25  PHE A HZ   1 
ATOM   392  N  N    . THR A 1 29  ? 15.783  7.169   21.329 1.00 25.26  ? 26  THR A N    1 
ATOM   393  C  CA   . THR A 1 29  ? 16.338  8.404   21.887 1.00 25.10  ? 26  THR A CA   1 
ATOM   394  C  C    . THR A 1 29  ? 15.436  9.621   21.693 1.00 29.77  ? 26  THR A C    1 
ATOM   395  O  O    . THR A 1 29  ? 15.831  10.744  22.054 1.00 32.87  ? 26  THR A O    1 
ATOM   396  C  CB   . THR A 1 29  ? 17.736  8.759   21.370 1.00 32.46  ? 26  THR A CB   1 
ATOM   397  O  OG1  . THR A 1 29  ? 17.659  9.328   20.054 1.00 33.91  ? 26  THR A OG1  1 
ATOM   398  C  CG2  . THR A 1 29  ? 18.687  7.566   21.420 1.00 35.25  ? 26  THR A CG2  1 
ATOM   399  H  H    . THR A 1 29  ? 15.564  6.615   21.949 1.00 30.35  ? 26  THR A H    1 
ATOM   400  H  HA   . THR A 1 29  ? 16.421  8.229   22.838 1.00 29.95  ? 26  THR A HA   1 
ATOM   401  H  HB   . THR A 1 29  ? 18.123  9.429   21.956 1.00 38.98  ? 26  THR A HB   1 
ATOM   402  H  HG1  . THR A 1 29  ? 17.328  8.772   19.519 1.00 40.73  ? 26  THR A HG1  1 
ATOM   403  H  HG21 . THR A 1 29  ? 19.583  7.846   21.178 1.00 42.34  ? 26  THR A HG21 1 
ATOM   404  H  HG22 . THR A 1 29  ? 18.705  7.193   22.315 1.00 42.34  ? 26  THR A HG22 1 
ATOM   405  H  HG23 . THR A 1 29  ? 18.392  6.881   20.799 1.00 42.34  ? 26  THR A HG23 1 
ATOM   406  N  N    . GLY A 1 30  ? 14.221  9.432   21.195 1.00 25.94  ? 27  GLY A N    1 
ATOM   407  C  CA   . GLY A 1 30  ? 13.238  10.495  21.099 1.00 25.69  ? 27  GLY A CA   1 
ATOM   408  C  C    . GLY A 1 30  ? 12.394  10.537  22.360 1.00 28.19  ? 27  GLY A C    1 
ATOM   409  O  O    . GLY A 1 30  ? 12.742  9.933   23.381 1.00 27.04  ? 27  GLY A O    1 
ATOM   410  H  H    . GLY A 1 30  ? 13.937  8.676   20.899 1.00 31.16  ? 27  GLY A H    1 
ATOM   411  H  HA2  . GLY A 1 30  ? 13.685  11.349  20.990 1.00 30.87  ? 27  GLY A HA2  1 
ATOM   412  H  HA3  . GLY A 1 30  ? 12.659  10.342  20.336 1.00 30.87  ? 27  GLY A HA3  1 
ATOM   413  N  N    . THR A 1 31  ? 11.249  11.227  22.267 1.00 25.55  ? 28  THR A N    1 
ATOM   414  C  CA   . THR A 1 31  ? 10.242  11.248  23.332 1.00 24.53  ? 28  THR A CA   1 
ATOM   415  C  C    . THR A 1 31  ? 8.896   11.311  22.638 1.00 27.31  ? 28  THR A C    1 
ATOM   416  O  O    . THR A 1 31  ? 8.836   11.439  21.417 1.00 22.89  ? 28  THR A O    1 
ATOM   417  C  CB   . THR A 1 31  ? 10.361  12.437  24.287 1.00 25.66  ? 28  THR A CB   1 
ATOM   418  O  OG1  . THR A 1 31  ? 10.041  13.641  23.579 1.00 29.51  ? 28  THR A OG1  1 
ATOM   419  C  CG2  . THR A 1 31  ? 11.763  12.546  24.919 1.00 30.36  ? 28  THR A CG2  1 
ATOM   420  H  H    . THR A 1 31  ? 11.031  11.699  21.582 1.00 30.70  ? 28  THR A H    1 
ATOM   421  H  HA   . THR A 1 31  ? 10.355  10.445  23.863 1.00 29.47  ? 28  THR A HA   1 
ATOM   422  H  HB   . THR A 1 31  ? 9.741   12.312  25.022 1.00 30.82  ? 28  THR A HB   1 
ATOM   423  H  HG1  . THR A 1 31  ? 10.190  14.309  24.066 1.00 35.45  ? 28  THR A HG1  1 
ATOM   424  H  HG21 . THR A 1 31  ? 11.810  13.329  25.489 1.00 36.46  ? 28  THR A HG21 1 
ATOM   425  H  HG22 . THR A 1 31  ? 11.948  11.757  25.453 1.00 36.46  ? 28  THR A HG22 1 
ATOM   426  H  HG23 . THR A 1 31  ? 12.435  12.620  24.224 1.00 36.46  ? 28  THR A HG23 1 
ATOM   427  N  N    A ASN A 1 32  ? 7.806   11.312  23.405 0.57 25.69  ? 29  ASN A N    1 
ATOM   428  N  N    B ASN A 1 32  ? 7.804   11.319  23.405 0.43 25.71  ? 29  ASN A N    1 
ATOM   429  C  CA   A ASN A 1 32  ? 6.496   11.355  22.761 0.57 27.15  ? 29  ASN A CA   1 
ATOM   430  C  CA   B ASN A 1 32  ? 6.501   11.421  22.755 0.43 27.10  ? 29  ASN A CA   1 
ATOM   431  C  C    A ASN A 1 32  ? 6.179   12.712  22.132 0.57 27.91  ? 29  ASN A C    1 
ATOM   432  C  C    B ASN A 1 32  ? 6.237   12.800  22.151 0.43 28.01  ? 29  ASN A C    1 
ATOM   433  O  O    A ASN A 1 32  ? 5.155   12.831  21.442 0.57 28.35  ? 29  ASN A O    1 
ATOM   434  O  O    B ASN A 1 32  ? 5.200   12.982  21.496 0.43 28.37  ? 29  ASN A O    1 
ATOM   435  C  CB   A ASN A 1 32  ? 5.384   10.922  23.726 0.57 28.41  ? 29  ASN A CB   1 
ATOM   436  C  CB   B ASN A 1 32  ? 5.370   11.020  23.708 0.43 28.45  ? 29  ASN A CB   1 
ATOM   437  C  CG   A ASN A 1 32  ? 5.075   11.941  24.808 0.57 29.66  ? 29  ASN A CG   1 
ATOM   438  C  CG   B ASN A 1 32  ? 5.501   11.616  25.095 0.43 26.04  ? 29  ASN A CG   1 
ATOM   439  O  OD1  A ASN A 1 32  ? 5.749   12.964  24.955 0.57 27.71  ? 29  ASN A OD1  1 
ATOM   440  O  OD1  B ASN A 1 32  ? 6.298   12.527  25.338 0.43 25.95  ? 29  ASN A OD1  1 
ATOM   441  N  ND2  A ASN A 1 32  ? 4.009   11.668  25.559 0.57 28.99  ? 29  ASN A ND2  1 
ATOM   442  N  ND2  B ASN A 1 32  ? 4.698   11.100  26.020 0.43 26.27  ? 29  ASN A ND2  1 
ATOM   443  H  H    A ASN A 1 32  ? 7.800   11.289  24.265 0.57 30.87  ? 29  ASN A H    1 
ATOM   444  H  H    B ASN A 1 32  ? 7.795   11.268  24.264 0.43 30.88  ? 29  ASN A H    1 
ATOM   445  H  HA   A ASN A 1 32  ? 6.496   10.702  22.044 0.57 32.62  ? 29  ASN A HA   1 
ATOM   446  H  HA   B ASN A 1 32  ? 6.481   10.779  22.028 0.43 32.56  ? 29  ASN A HA   1 
ATOM   447  H  HB2  A ASN A 1 32  ? 4.571   10.775  23.218 0.57 34.13  ? 29  ASN A HB2  1 
ATOM   448  H  HB2  B ASN A 1 32  ? 4.526   11.321  23.335 0.43 34.18  ? 29  ASN A HB2  1 
ATOM   449  H  HB3  A ASN A 1 32  ? 5.655   10.099  24.164 0.57 34.13  ? 29  ASN A HB3  1 
ATOM   450  H  HB3  B ASN A 1 32  ? 5.366   10.054  23.800 0.43 34.18  ? 29  ASN A HB3  1 
ATOM   451  H  HD21 A ASN A 1 32  ? 3.779   12.205  26.190 0.57 34.83  ? 29  ASN A HD21 1 
ATOM   452  H  HD21 B ASN A 1 32  ? 4.725   11.396  26.827 0.43 31.56  ? 29  ASN A HD21 1 
ATOM   453  H  HD22 A ASN A 1 32  ? 3.550   10.955  25.412 0.57 34.83  ? 29  ASN A HD22 1 
ATOM   454  H  HD22 B ASN A 1 32  ? 4.151   10.470  25.811 0.43 31.56  ? 29  ASN A HD22 1 
ATOM   455  N  N    A ARG A 1 33  ? 7.055   13.717  22.265 0.57 28.60  ? 30  ARG A N    1 
ATOM   456  N  N    B ARG A 1 33  ? 7.162   13.761  22.290 0.43 28.51  ? 30  ARG A N    1 
ATOM   457  C  CA   A ARG A 1 33  ? 6.940   14.908  21.425 0.57 30.75  ? 30  ARG A CA   1 
ATOM   458  C  CA   B ARG A 1 33  ? 7.112   14.951  21.444 0.43 30.99  ? 30  ARG A CA   1 
ATOM   459  C  C    A ARG A 1 33  ? 7.192   14.613  19.953 0.57 31.79  ? 30  ARG A C    1 
ATOM   460  C  C    B ARG A 1 33  ? 7.160   14.588  19.969 0.43 31.75  ? 30  ARG A C    1 
ATOM   461  O  O    A ARG A 1 33  ? 6.791   15.417  19.099 0.57 34.84  ? 30  ARG A O    1 
ATOM   462  O  O    B ARG A 1 33  ? 6.593   15.306  19.132 0.43 34.59  ? 30  ARG A O    1 
ATOM   463  C  CB   A ARG A 1 33  ? 7.904   15.974  21.951 0.57 33.06  ? 30  ARG A CB   1 
ATOM   464  C  CB   B ARG A 1 33  ? 8.272   15.883  21.795 0.43 33.45  ? 30  ARG A CB   1 
ATOM   465  C  CG   A ARG A 1 33  ? 7.612   16.411  23.370 0.57 33.10  ? 30  ARG A CG   1 
ATOM   466  C  CG   B ARG A 1 33  ? 8.350   17.167  20.954 0.43 41.95  ? 30  ARG A CG   1 
ATOM   467  C  CD   A ARG A 1 33  ? 8.430   17.643  23.748 0.57 43.90  ? 30  ARG A CD   1 
ATOM   468  C  CD   B ARG A 1 33  ? 9.466   18.049  21.489 0.43 47.15  ? 30  ARG A CD   1 
ATOM   469  N  NE   A ARG A 1 33  ? 9.820   17.296  24.027 0.57 46.84  ? 30  ARG A NE   1 
ATOM   470  N  NE   B ARG A 1 33  ? 9.763   19.202  20.651 0.43 44.96  ? 30  ARG A NE   1 
ATOM   471  C  CZ   A ARG A 1 33  ? 10.247  16.736  25.150 0.57 53.38  ? 30  ARG A CZ   1 
ATOM   472  C  CZ   B ARG A 1 33  ? 10.392  20.282  21.086 0.43 46.56  ? 30  ARG A CZ   1 
ATOM   473  N  NH1  A ARG A 1 33  ? 9.414   16.444  26.136 0.57 52.23  ? 30  ARG A NH1  1 
ATOM   474  N  NH1  B ARG A 1 33  ? 10.752  20.406  22.354 0.43 56.35  ? 30  ARG A NH1  1 
ATOM   475  N  NH2  A ARG A 1 33  ? 11.542  16.466  25.285 0.57 54.26  ? 30  ARG A NH2  1 
ATOM   476  N  NH2  B ARG A 1 33  ? 10.675  21.261  20.230 0.43 49.61  ? 30  ARG A NH2  1 
ATOM   477  H  H    A ARG A 1 33  ? 7.710   13.731  22.823 0.57 34.36  ? 30  ARG A H    1 
ATOM   478  H  H    B ARG A 1 33  ? 7.811   13.745  22.854 0.43 34.25  ? 30  ARG A H    1 
ATOM   479  H  HA   A ARG A 1 33  ? 6.039   15.263  21.480 0.57 36.94  ? 30  ARG A HA   1 
ATOM   480  H  HA   B ARG A 1 33  ? 6.280   15.422  21.610 0.43 37.23  ? 30  ARG A HA   1 
ATOM   481  H  HB2  A ARG A 1 33  ? 8.806   15.617  21.930 0.57 39.70  ? 30  ARG A HB2  1 
ATOM   482  H  HB2  B ARG A 1 33  ? 8.182   16.149  22.724 0.43 40.18  ? 30  ARG A HB2  1 
ATOM   483  H  HB3  A ARG A 1 33  ? 7.844   16.757  21.381 0.57 39.70  ? 30  ARG A HB3  1 
ATOM   484  H  HB3  B ARG A 1 33  ? 9.104   15.400  21.667 0.43 40.18  ? 30  ARG A HB3  1 
ATOM   485  H  HG2  A ARG A 1 33  ? 6.671   16.632  23.452 0.57 39.76  ? 30  ARG A HG2  1 
ATOM   486  H  HG2  B ARG A 1 33  ? 8.542   16.944  20.030 0.43 50.38  ? 30  ARG A HG2  1 
ATOM   487  H  HG3  A ARG A 1 33  ? 7.839   15.693  23.982 0.57 39.76  ? 30  ARG A HG3  1 
ATOM   488  H  HG3  B ARG A 1 33  ? 7.511   17.650  21.012 0.43 50.38  ? 30  ARG A HG3  1 
ATOM   489  H  HD2  A ARG A 1 33  ? 8.415   18.276  23.013 0.57 52.71  ? 30  ARG A HD2  1 
ATOM   490  H  HD2  B ARG A 1 33  ? 9.209   18.379  22.364 0.43 56.62  ? 30  ARG A HD2  1 
ATOM   491  H  HD3  A ARG A 1 33  ? 8.051   18.048  24.543 0.57 52.71  ? 30  ARG A HD3  1 
ATOM   492  H  HD3  B ARG A 1 33  ? 10.275  17.519  21.559 0.43 56.62  ? 30  ARG A HD3  1 
ATOM   493  H  HE   A ARG A 1 33  ? 10.403  17.468  23.419 0.57 56.24  ? 30  ARG A HE   1 
ATOM   494  H  HE   B ARG A 1 33  ? 9.516   19.181  19.827 0.43 53.99  ? 30  ARG A HE   1 
ATOM   495  H  HH11 A ARG A 1 33  ? 8.576   16.618  26.057 0.57 62.72  ? 30  ARG A HH11 1 
ATOM   496  H  HH11 B ARG A 1 33  ? 10.578  19.777  22.913 0.43 67.65  ? 30  ARG A HH11 1 
ATOM   497  H  HH12 A ARG A 1 33  ? 9.712   16.081  26.857 0.57 62.72  ? 30  ARG A HH12 1 
ATOM   498  H  HH12 B ARG A 1 33  ? 11.160  21.115  22.618 0.43 67.65  ? 30  ARG A HH12 1 
ATOM   499  H  HH21 A ARG A 1 33  ? 12.089  16.655  24.650 0.57 65.15  ? 30  ARG A HH21 1 
ATOM   500  H  HH21 B ARG A 1 33  ? 10.449  21.187  19.404 0.43 59.57  ? 30  ARG A HH21 1 
ATOM   501  H  HH22 A ARG A 1 33  ? 11.832  16.103  26.009 0.57 65.15  ? 30  ARG A HH22 1 
ATOM   502  H  HH22 B ARG A 1 33  ? 11.083  21.966  20.503 0.43 59.57  ? 30  ARG A HH22 1 
ATOM   503  N  N    . ASP A 1 34  ? 7.833   13.483  19.639 1.00 28.75  ? 31  ASP A N    1 
ATOM   504  C  CA   . ASP A 1 34  ? 7.980   13.058  18.252 1.00 32.01  ? 31  ASP A CA   1 
ATOM   505  C  C    . ASP A 1 34  ? 6.634   12.970  17.534 1.00 33.38  ? 31  ASP A C    1 
ATOM   506  O  O    . ASP A 1 34  ? 6.570   13.085  16.300 1.00 31.50  ? 31  ASP A O    1 
ATOM   507  C  CB   . ASP A 1 34  ? 8.595   11.650  18.130 1.00 29.38  ? 31  ASP A CB   1 
ATOM   508  C  CG   . ASP A 1 34  ? 10.056  11.553  18.483 1.00 33.52  ? 31  ASP A CG   1 
ATOM   509  O  OD1  . ASP A 1 34  ? 10.698  12.566  18.779 1.00 32.42  ? 31  ASP A OD1  1 
ATOM   510  O  OD2  . ASP A 1 34  ? 10.534  10.380  18.437 1.00 27.04  ? 31  ASP A OD2  1 
ATOM   511  H  H    A ASP A 1 34  ? 8.190   12.948  20.210 0.57 34.54  ? 31  ASP A H    1 
ATOM   512  H  H    B ASP A 1 34  ? 8.216   12.960  20.204 0.43 34.54  ? 31  ASP A H    1 
ATOM   513  H  HA   . ASP A 1 34  ? 8.566   13.714  17.844 1.00 38.45  ? 31  ASP A HA   1 
ATOM   514  H  HB2  . ASP A 1 34  ? 8.113   11.053  18.724 1.00 35.29  ? 31  ASP A HB2  1 
ATOM   515  H  HB3  . ASP A 1 34  ? 8.499   11.352  17.212 1.00 35.29  ? 31  ASP A HB3  1 
ATOM   516  N  N    . VAL A 1 35  ? 5.570   12.628  18.264 1.00 24.46  ? 32  VAL A N    1 
ATOM   517  C  CA   . VAL A 1 35  ? 4.293   12.271  17.663 1.00 24.35  ? 32  VAL A CA   1 
ATOM   518  C  C    . VAL A 1 35  ? 3.176   13.222  18.055 1.00 27.49  ? 32  VAL A C    1 
ATOM   519  O  O    . VAL A 1 35  ? 2.020   12.955  17.740 1.00 25.52  ? 32  VAL A O    1 
ATOM   520  C  CB   . VAL A 1 35  ? 3.908   10.800  17.966 1.00 23.56  ? 32  VAL A CB   1 
ATOM   521  C  CG1  . VAL A 1 35  ? 4.957   9.845   17.279 1.00 26.42  ? 32  VAL A CG1  1 
ATOM   522  C  CG2  . VAL A 1 35  ? 3.793   10.560  19.442 1.00 27.13  ? 32  VAL A CG2  1 
ATOM   523  H  H    . VAL A 1 35  ? 5.568   12.596  19.123 1.00 29.39  ? 32  VAL A H    1 
ATOM   524  H  HA   . VAL A 1 35  ? 4.395   12.350  16.702 1.00 29.26  ? 32  VAL A HA   1 
ATOM   525  H  HB   . VAL A 1 35  ? 3.032   10.601  17.599 1.00 28.31  ? 32  VAL A HB   1 
ATOM   526  H  HG11 . VAL A 1 35  ? 4.655   8.928   17.368 1.00 31.74  ? 32  VAL A HG11 1 
ATOM   527  H  HG12 . VAL A 1 35  ? 5.029   10.080  16.340 1.00 31.74  ? 32  VAL A HG12 1 
ATOM   528  H  HG13 . VAL A 1 35  ? 5.816   9.955   17.714 1.00 31.74  ? 32  VAL A HG13 1 
ATOM   529  H  HG21 . VAL A 1 35  ? 3.545   9.634   19.593 1.00 32.59  ? 32  VAL A HG21 1 
ATOM   530  H  HG22 . VAL A 1 35  ? 4.649   10.745  19.860 1.00 32.59  ? 32  VAL A HG22 1 
ATOM   531  H  HG23 . VAL A 1 35  ? 3.113   11.148  19.806 1.00 32.59  ? 32  VAL A HG23 1 
ATOM   532  N  N    . LYS A 1 36  ? 3.503   14.338  18.727 1.00 23.99  ? 33  LYS A N    1 
ATOM   533  C  CA   . LYS A 1 36  ? 2.470   15.218  19.252 1.00 25.54  ? 33  LYS A CA   1 
ATOM   534  C  C    . LYS A 1 36  ? 1.560   15.750  18.142 1.00 24.57  ? 33  LYS A C    1 
ATOM   535  O  O    . LYS A 1 36  ? 0.328   15.749  18.282 1.00 25.20  ? 33  LYS A O    1 
ATOM   536  C  CB   . LYS A 1 36  ? 3.141   16.354  20.017 1.00 23.37  ? 33  LYS A CB   1 
ATOM   537  C  CG   . LYS A 1 36  ? 2.171   17.401  20.565 1.00 22.94  ? 33  LYS A CG   1 
ATOM   538  C  CD   . LYS A 1 36  ? 2.834   18.471  21.355 1.00 29.26  ? 33  LYS A CD   1 
ATOM   539  C  CE   . LYS A 1 36  ? 1.789   19.316  22.093 1.00 28.63  ? 33  LYS A CE   1 
ATOM   540  N  NZ   . LYS A 1 36  ? 2.362   20.366  22.907 1.00 29.72  ? 33  LYS A NZ   1 
ATOM   541  H  H    . LYS A 1 36  ? 4.308   14.598  18.885 1.00 28.82  ? 33  LYS A H    1 
ATOM   542  H  HA   . LYS A 1 36  ? 1.900   14.725  19.862 1.00 30.68  ? 33  LYS A HA   1 
ATOM   543  H  HB2  . LYS A 1 36  ? 3.625   15.977  20.769 1.00 28.07  ? 33  LYS A HB2  1 
ATOM   544  H  HB3  . LYS A 1 36  ? 3.757   16.807  19.420 1.00 28.07  ? 33  LYS A HB3  1 
ATOM   545  H  HG2  . LYS A 1 36  ? 1.712   17.823  19.822 1.00 27.56  ? 33  LYS A HG2  1 
ATOM   546  H  HG3  . LYS A 1 36  ? 1.529   16.960  21.144 1.00 27.56  ? 33  LYS A HG3  1 
ATOM   547  H  HD2  . LYS A 1 36  ? 3.427   18.071  22.011 1.00 35.14  ? 33  LYS A HD2  1 
ATOM   548  H  HD3  . LYS A 1 36  ? 3.337   19.049  20.761 1.00 35.14  ? 33  LYS A HD3  1 
ATOM   549  H  HE2  . LYS A 1 36  ? 1.206   19.734  21.440 1.00 34.39  ? 33  LYS A HE2  1 
ATOM   550  H  HE3  . LYS A 1 36  ? 1.274   18.738  22.677 1.00 34.39  ? 33  LYS A HE3  1 
ATOM   551  H  HZ1  . LYS A 1 36  ? 1.716   20.831  23.304 1.00 35.70  ? 33  LYS A HZ1  1 
ATOM   552  H  HZ2  . LYS A 1 36  ? 2.890   20.014  23.531 1.00 35.70  ? 33  LYS A HZ2  1 
ATOM   553  H  HZ3  . LYS A 1 36  ? 2.844   20.916  22.399 1.00 35.70  ? 33  LYS A HZ3  1 
ATOM   554  N  N    . HIS A 1 37  ? 2.146   16.263  17.066 1.00 25.34  ? 34  HIS A N    1 
ATOM   555  C  CA   . HIS A 1 37  ? 1.313   16.884  16.032 1.00 22.91  ? 34  HIS A CA   1 
ATOM   556  C  C    . HIS A 1 37  ? 0.434   15.862  15.334 1.00 24.23  ? 34  HIS A C    1 
ATOM   557  O  O    . HIS A 1 37  ? -0.745  16.121  15.081 1.00 25.63  ? 34  HIS A O    1 
ATOM   558  C  CB   . HIS A 1 37  ? 2.153   17.621  14.997 1.00 24.41  ? 34  HIS A CB   1 
ATOM   559  C  CG   . HIS A 1 37  ? 1.330   18.503  14.106 1.00 28.71  ? 34  HIS A CG   1 
ATOM   560  N  ND1  . HIS A 1 37  ? 0.995   18.168  12.803 1.00 29.51  ? 34  HIS A ND1  1 
ATOM   561  C  CD2  . HIS A 1 37  ? 0.676   19.660  14.370 1.00 29.40  ? 34  HIS A CD2  1 
ATOM   562  C  CE1  . HIS A 1 37  ? 0.233   19.118  12.289 1.00 30.86  ? 34  HIS A CE1  1 
ATOM   563  N  NE2  . HIS A 1 37  ? 0.041   20.052  13.211 1.00 31.50  ? 34  HIS A NE2  1 
ATOM   564  H  H    . HIS A 1 37  ? 2.992   16.266  16.911 1.00 30.44  ? 34  HIS A H    1 
ATOM   565  H  HA   . HIS A 1 37  ? 0.751   17.538  16.477 1.00 27.52  ? 34  HIS A HA   1 
ATOM   566  H  HB2  . HIS A 1 37  ? 2.802   18.178  15.455 1.00 29.32  ? 34  HIS A HB2  1 
ATOM   567  H  HB3  . HIS A 1 37  ? 2.609   16.972  14.439 1.00 29.32  ? 34  HIS A HB3  1 
ATOM   568  H  HD1  . HIS A 1 37  ? 1.244   17.454  12.394 1.00 35.45  ? 34  HIS A HD1  1 
ATOM   569  H  HD2  . HIS A 1 37  ? 0.658   20.108  15.185 1.00 35.32  ? 34  HIS A HD2  1 
ATOM   570  H  HE1  . HIS A 1 37  ? -0.111  19.130  11.425 1.00 37.06  ? 34  HIS A HE1  1 
ATOM   571  N  N    . LEU A 1 38  ? 0.989   14.710  15.001 1.00 23.05  ? 35  LEU A N    1 
ATOM   572  C  CA   . LEU A 1 38  ? 0.200   13.659  14.348 1.00 21.79  ? 35  LEU A CA   1 
ATOM   573  C  C    . LEU A 1 38  ? -0.912  13.144  15.264 1.00 21.66  ? 35  LEU A C    1 
ATOM   574  O  O    . LEU A 1 38  ? -2.060  12.963  14.827 1.00 24.77  ? 35  LEU A O    1 
ATOM   575  C  CB   . LEU A 1 38  ? 1.129   12.522  13.931 1.00 24.96  ? 35  LEU A CB   1 
ATOM   576  C  CG   . LEU A 1 38  ? 0.432   11.314  13.315 1.00 27.35  ? 35  LEU A CG   1 
ATOM   577  C  CD1  . LEU A 1 38  ? -0.362  11.658  12.074 1.00 29.55  ? 35  LEU A CD1  1 
ATOM   578  C  CD2  . LEU A 1 38  ? 1.446   10.234  13.026 1.00 30.33  ? 35  LEU A CD2  1 
ATOM   579  H  H    . LEU A 1 38  ? 1.812   14.503  15.137 1.00 27.69  ? 35  LEU A H    1 
ATOM   580  H  HA   . LEU A 1 38  ? -0.223  14.022  13.554 1.00 26.18  ? 35  LEU A HA   1 
ATOM   581  H  HB2  . LEU A 1 38  ? 1.755   12.864  13.274 1.00 29.99  ? 35  LEU A HB2  1 
ATOM   582  H  HB3  . LEU A 1 38  ? 1.607   12.214  14.717 1.00 29.99  ? 35  LEU A HB3  1 
ATOM   583  H  HG   . LEU A 1 38  ? -0.215  10.982  13.957 1.00 32.86  ? 35  LEU A HG   1 
ATOM   584  H  HD11 . LEU A 1 38  ? -0.632  10.837  11.634 1.00 35.49  ? 35  LEU A HD11 1 
ATOM   585  H  HD12 . LEU A 1 38  ? -1.146  12.168  12.332 1.00 35.49  ? 35  LEU A HD12 1 
ATOM   586  H  HD13 . LEU A 1 38  ? 0.194   12.185  11.479 1.00 35.49  ? 35  LEU A HD13 1 
ATOM   587  H  HD21 . LEU A 1 38  ? 0.984   9.449   12.692 1.00 36.43  ? 35  LEU A HD21 1 
ATOM   588  H  HD22 . LEU A 1 38  ? 2.072   10.559  12.360 1.00 36.43  ? 35  LEU A HD22 1 
ATOM   589  H  HD23 . LEU A 1 38  ? 1.917   10.017  13.846 1.00 36.43  ? 35  LEU A HD23 1 
ATOM   590  N  N    . ALA A 1 39  ? -0.631  13.013  16.557 1.00 23.78  ? 36  ALA A N    1 
ATOM   591  C  CA   . ALA A 1 39  ? -1.687  12.629  17.477 1.00 22.15  ? 36  ALA A CA   1 
ATOM   592  C  C    . ALA A 1 39  ? -2.796  13.679  17.498 1.00 21.66  ? 36  ALA A C    1 
ATOM   593  O  O    . ALA A 1 39  ? -3.985  13.344  17.524 1.00 24.05  ? 36  ALA A O    1 
ATOM   594  C  CB   . ALA A 1 39  ? -1.105  12.461  18.890 1.00 24.39  ? 36  ALA A CB   1 
ATOM   595  H  H    . ALA A 1 39  ? 0.141   13.137  16.914 1.00 28.57  ? 36  ALA A H    1 
ATOM   596  H  HA   . ALA A 1 39  ? -2.064  11.783  17.192 1.00 26.61  ? 36  ALA A HA   1 
ATOM   597  H  HB1  . ALA A 1 39  ? -1.816  12.201  19.496 1.00 29.30  ? 36  ALA A HB1  1 
ATOM   598  H  HB2  . ALA A 1 39  ? -0.420  11.775  18.870 1.00 29.30  ? 36  ALA A HB2  1 
ATOM   599  H  HB3  . ALA A 1 39  ? -0.719  13.304  19.176 1.00 29.30  ? 36  ALA A HB3  1 
ATOM   600  N  N    . ALA A 1 40  ? -2.426  14.949  17.561 1.00 21.84  ? 37  ALA A N    1 
ATOM   601  C  CA   . ALA A 1 40  ? -3.421  16.014  17.590 1.00 23.98  ? 37  ALA A CA   1 
ATOM   602  C  C    . ALA A 1 40  ? -4.263  16.006  16.313 1.00 24.26  ? 37  ALA A C    1 
ATOM   603  O  O    . ALA A 1 40  ? -5.481  16.213  16.357 1.00 25.10  ? 37  ALA A O    1 
ATOM   604  C  CB   . ALA A 1 40  ? -2.718  17.345  17.783 1.00 24.18  ? 37  ALA A CB   1 
ATOM   605  H  H    . ALA A 1 40  ? -1.611  15.223  17.588 1.00 26.24  ? 37  ALA A H    1 
ATOM   606  H  HA   . ALA A 1 40  ? -4.027  15.884  18.336 1.00 28.81  ? 37  ALA A HA   1 
ATOM   607  H  HB1  . ALA A 1 40  ? -3.384  18.042  17.892 1.00 29.05  ? 37  ALA A HB1  1 
ATOM   608  H  HB2  . ALA A 1 40  ? -2.160  17.295  18.575 1.00 29.05  ? 37  ALA A HB2  1 
ATOM   609  H  HB3  . ALA A 1 40  ? -2.170  17.529  17.004 1.00 29.05  ? 37  ALA A HB3  1 
ATOM   610  N  N    . GLU A 1 41  ? -3.631  15.807  15.158 1.00 24.37  ? 38  GLU A N    1 
ATOM   611  C  CA   . GLU A 1 41  ? -4.395  15.820  13.915 1.00 24.96  ? 38  GLU A CA   1 
ATOM   612  C  C    . GLU A 1 41  ? -5.336  14.629  13.813 1.00 23.55  ? 38  GLU A C    1 
ATOM   613  O  O    . GLU A 1 41  ? -6.479  14.749  13.312 1.00 26.51  ? 38  GLU A O    1 
ATOM   614  C  CB   . GLU A 1 41  ? -3.425  15.875  12.733 1.00 25.19  ? 38  GLU A CB   1 
ATOM   615  C  CG   . GLU A 1 41  ? -2.725  17.248  12.547 1.00 28.48  ? 38  GLU A CG   1 
ATOM   616  C  CD   . GLU A 1 41  ? -3.656  18.391  12.153 1.00 36.55  ? 38  GLU A CD   1 
ATOM   617  O  OE1  . GLU A 1 41  ? -4.487  18.197  11.250 1.00 35.83  ? 38  GLU A OE1  1 
ATOM   618  O  OE2  . GLU A 1 41  ? -3.491  19.508  12.671 1.00 43.58  ? 38  GLU A OE2  1 
ATOM   619  H  H    . GLU A 1 41  ? -2.787  15.667  15.070 1.00 29.28  ? 38  GLU A H    1 
ATOM   620  H  HA   . GLU A 1 41  ? -4.953  16.613  13.888 1.00 29.98  ? 38  GLU A HA   1 
ATOM   621  H  HB2  . GLU A 1 41  ? -2.734  15.209  12.868 1.00 30.26  ? 38  GLU A HB2  1 
ATOM   622  H  HB3  . GLU A 1 41  ? -3.917  15.683  11.920 1.00 30.26  ? 38  GLU A HB3  1 
ATOM   623  H  HG2  . GLU A 1 41  ? -2.300  17.493  13.383 1.00 34.22  ? 38  GLU A HG2  1 
ATOM   624  H  HG3  . GLU A 1 41  ? -2.057  17.161  11.848 1.00 34.22  ? 38  GLU A HG3  1 
ATOM   625  N  N    . LEU A 1 42  ? -4.878  13.466  14.254 1.00 24.98  ? 39  LEU A N    1 
ATOM   626  C  CA   . LEU A 1 42  ? -5.754  12.303  14.291 1.00 25.64  ? 39  LEU A CA   1 
ATOM   627  C  C    . LEU A 1 42  ? -6.916  12.523  15.246 1.00 23.87  ? 39  LEU A C    1 
ATOM   628  O  O    . LEU A 1 42  ? -8.053  12.151  14.956 1.00 24.81  ? 39  LEU A O    1 
ATOM   629  C  CB   . LEU A 1 42  ? -4.963  11.052  14.680 1.00 25.41  ? 39  LEU A CB   1 
ATOM   630  C  CG   . LEU A 1 42  ? -4.157  10.444  13.546 1.00 25.56  ? 39  LEU A CG   1 
ATOM   631  C  CD1  . LEU A 1 42  ? -3.042  9.568   14.030 1.00 28.91  ? 39  LEU A CD1  1 
ATOM   632  C  CD2  . LEU A 1 42  ? -5.032  9.638   12.535 1.00 30.46  ? 39  LEU A CD2  1 
ATOM   633  H  H    . LEU A 1 42  ? -4.078  13.324  14.533 1.00 30.01  ? 39  LEU A H    1 
ATOM   634  H  HA   . LEU A 1 42  ? -6.117  12.158  13.403 1.00 30.81  ? 39  LEU A HA   1 
ATOM   635  H  HB2  . LEU A 1 42  ? -4.344  11.286  15.389 1.00 30.52  ? 39  LEU A HB2  1 
ATOM   636  H  HB3  . LEU A 1 42  ? -5.586  10.377  14.993 1.00 30.52  ? 39  LEU A HB3  1 
ATOM   637  H  HG   . LEU A 1 42  ? -3.774  11.202  13.077 1.00 30.71  ? 39  LEU A HG   1 
ATOM   638  H  HD11 . LEU A 1 42  ? -2.507  9.289   13.271 1.00 34.73  ? 39  LEU A HD11 1 
ATOM   639  H  HD12 . LEU A 1 42  ? -2.494  10.070  14.654 1.00 34.73  ? 39  LEU A HD12 1 
ATOM   640  H  HD13 . LEU A 1 42  ? -3.420  8.792   14.473 1.00 34.73  ? 39  LEU A HD13 1 
ATOM   641  H  HD21 . LEU A 1 42  ? -4.470  9.325   11.810 1.00 36.59  ? 39  LEU A HD21 1 
ATOM   642  H  HD22 . LEU A 1 42  ? -5.430  8.882   12.995 1.00 36.59  ? 39  LEU A HD22 1 
ATOM   643  H  HD23 . LEU A 1 42  ? -5.729  10.217  12.188 1.00 36.59  ? 39  LEU A HD23 1 
ATOM   644  N  N    . ASN A 1 43  ? -6.655  13.115  16.411 1.00 24.53  ? 40  ASN A N    1 
ATOM   645  C  CA   . ASN A 1 43  ? -7.751  13.384  17.343 1.00 23.53  ? 40  ASN A CA   1 
ATOM   646  C  C    . ASN A 1 43  ? -8.768  14.354  16.750 1.00 28.54  ? 40  ASN A C    1 
ATOM   647  O  O    . ASN A 1 43  ? -9.974  14.239  17.000 1.00 28.64  ? 40  ASN A O    1 
ATOM   648  C  CB   . ASN A 1 43  ? -7.173  13.919  18.648 1.00 22.98  ? 40  ASN A CB   1 
ATOM   649  C  CG   . ASN A 1 43  ? -8.243  14.331  19.606 1.00 26.53  ? 40  ASN A CG   1 
ATOM   650  O  OD1  . ASN A 1 43  ? -8.382  15.532  19.876 1.00 26.32  ? 40  ASN A OD1  1 
ATOM   651  N  ND2  . ASN A 1 43  ? -8.920  13.364  20.224 1.00 27.34  ? 40  ASN A ND2  1 
ATOM   652  H  H    . ASN A 1 43  ? -5.877  13.363  16.680 1.00 29.47  ? 40  ASN A H    1 
ATOM   653  H  HA   . ASN A 1 43  ? -8.225  12.559  17.533 1.00 28.27  ? 40  ASN A HA   1 
ATOM   654  H  HB2  . ASN A 1 43  ? -6.640  13.227  19.068 1.00 27.61  ? 40  ASN A HB2  1 
ATOM   655  H  HB3  . ASN A 1 43  ? -6.622  14.694  18.458 1.00 27.61  ? 40  ASN A HB3  1 
ATOM   656  H  HD21 . ASN A 1 43  ? -9.543  13.564  20.782 1.00 32.84  ? 40  ASN A HD21 1 
ATOM   657  H  HD22 . ASN A 1 43  ? -8.734  12.540  20.065 1.00 32.84  ? 40  ASN A HD22 1 
ATOM   658  N  N    . ASP A 1 44  ? -8.306  15.337  15.984 1.00 27.42  ? 41  ASP A N    1 
ATOM   659  C  CA   . ASP A 1 44  ? -9.238  16.252  15.348 1.00 30.54  ? 41  ASP A CA   1 
ATOM   660  C  C    . ASP A 1 44  ? -10.112 15.572  14.307 1.00 33.07  ? 41  ASP A C    1 
ATOM   661  O  O    . ASP A 1 44  ? -11.147 16.137  13.932 1.00 35.01  ? 41  ASP A O    1 
ATOM   662  C  CB   . ASP A 1 44  ? -8.464  17.413  14.751 1.00 30.03  ? 41  ASP A CB   1 
ATOM   663  C  CG   . ASP A 1 44  ? -8.146  18.463  15.796 1.00 40.52  ? 41  ASP A CG   1 
ATOM   664  O  OD1  . ASP A 1 44  ? -8.684  18.346  16.926 1.00 43.93  ? 41  ASP A OD1  1 
ATOM   665  O  OD2  . ASP A 1 44  ? -7.340  19.346  15.499 1.00 46.85  ? 41  ASP A OD2  1 
ATOM   666  H  H    . ASP A 1 44  ? -7.476  15.491  15.822 1.00 32.94  ? 41  ASP A H    1 
ATOM   667  H  HA   . ASP A 1 44  ? -9.845  16.613  16.014 1.00 36.69  ? 41  ASP A HA   1 
ATOM   668  H  HB2  . ASP A 1 44  ? -7.629  17.086  14.382 1.00 36.07  ? 41  ASP A HB2  1 
ATOM   669  H  HB3  . ASP A 1 44  ? -8.995  17.828  14.053 1.00 36.07  ? 41  ASP A HB3  1 
ATOM   670  N  N    . GLN A 1 45  ? -9.740  14.379  13.855 1.00 31.75  ? 42  GLN A N    1 
ATOM   671  C  CA   . GLN A 1 45  ? -10.607 13.580  12.989 1.00 33.65  ? 42  GLN A CA   1 
ATOM   672  C  C    . GLN A 1 45  ? -11.533 12.639  13.760 1.00 34.95  ? 42  GLN A C    1 
ATOM   673  O  O    . GLN A 1 45  ? -12.282 11.880  13.134 1.00 37.23  ? 42  GLN A O    1 
ATOM   674  C  CB   . GLN A 1 45  ? -9.769  12.765  12.005 1.00 35.67  ? 42  GLN A CB   1 
ATOM   675  C  CG   . GLN A 1 45  ? -8.915  13.605  11.100 1.00 38.34  ? 42  GLN A CG   1 
ATOM   676  C  CD   . GLN A 1 45  ? -9.679  14.109  9.906  1.00 44.50  ? 42  GLN A CD   1 
ATOM   677  O  OE1  . GLN A 1 45  ? -10.201 13.324  9.114  1.00 42.48  ? 42  GLN A OE1  1 
ATOM   678  N  NE2  . GLN A 1 45  ? -9.785  15.419  9.787  1.00 54.10  ? 42  GLN A NE2  1 
ATOM   679  H  H    . GLN A 1 45  ? -8.986  14.007  14.036 1.00 38.13  ? 42  GLN A H    1 
ATOM   680  H  HA   . GLN A 1 45  ? -11.162 14.190  12.479 1.00 40.41  ? 42  GLN A HA   1 
ATOM   681  H  HB2  . GLN A 1 45  ? -9.182  12.178  12.507 1.00 42.84  ? 42  GLN A HB2  1 
ATOM   682  H  HB3  . GLN A 1 45  ? -10.365 12.240  11.448 1.00 42.84  ? 42  GLN A HB3  1 
ATOM   683  H  HG2  . GLN A 1 45  ? -8.586  14.372  11.594 1.00 46.04  ? 42  GLN A HG2  1 
ATOM   684  H  HG3  . GLN A 1 45  ? -8.171  13.072  10.780 1.00 46.04  ? 42  GLN A HG3  1 
ATOM   685  H  HE21 . GLN A 1 45  ? -9.427  15.935  10.375 1.00 64.96  ? 42  GLN A HE21 1 
ATOM   686  H  HE22 . GLN A 1 45  ? -10.212 15.757  9.121  1.00 64.96  ? 42  GLN A HE22 1 
ATOM   687  N  N    . GLY A 1 46  ? -11.494 12.666  15.092 1.00 29.83  ? 43  GLY A N    1 
ATOM   688  C  CA   . GLY A 1 46  ? -12.368 11.855  15.919 1.00 33.96  ? 43  GLY A CA   1 
ATOM   689  C  C    . GLY A 1 46  ? -11.686 10.761  16.723 1.00 32.98  ? 43  GLY A C    1 
ATOM   690  O  O    . GLY A 1 46  ? -12.326 10.202  17.622 1.00 31.14  ? 43  GLY A O    1 
ATOM   691  H  H    . GLY A 1 46  ? -10.954 13.160  15.545 1.00 35.83  ? 43  GLY A H    1 
ATOM   692  H  HA2  . GLY A 1 46  ? -12.825 12.437  16.546 1.00 40.79  ? 43  GLY A HA2  1 
ATOM   693  H  HA3  . GLY A 1 46  ? -13.026 11.431  15.346 1.00 40.79  ? 43  GLY A HA3  1 
ATOM   694  N  N    . PHE A 1 47  ? -10.422 10.446  16.455 1.00 25.68  ? 44  PHE A N    1 
ATOM   695  C  CA   . PHE A 1 47  ? -9.763  9.324   17.093 1.00 25.96  ? 44  PHE A CA   1 
ATOM   696  C  C    . PHE A 1 47  ? -9.319  9.660   18.520 1.00 29.32  ? 44  PHE A C    1 
ATOM   697  O  O    . PHE A 1 47  ? -9.000  10.805  18.865 1.00 25.12  ? 44  PHE A O    1 
ATOM   698  C  CB   . PHE A 1 47  ? -8.541  8.853   16.291 1.00 27.17  ? 44  PHE A CB   1 
ATOM   699  C  CG   . PHE A 1 47  ? -8.900  8.260   14.978 1.00 27.61  ? 44  PHE A CG   1 
ATOM   700  C  CD1  . PHE A 1 47  ? -9.325  6.955   14.912 1.00 31.35  ? 44  PHE A CD1  1 
ATOM   701  C  CD2  . PHE A 1 47  ? -8.829  8.999   13.809 1.00 27.15  ? 44  PHE A CD2  1 
ATOM   702  C  CE1  . PHE A 1 47  ? -9.681  6.385   13.694 1.00 30.79  ? 44  PHE A CE1  1 
ATOM   703  C  CE2  . PHE A 1 47  ? -9.200  8.430   12.604 1.00 32.46  ? 44  PHE A CE2  1 
ATOM   704  C  CZ   . PHE A 1 47  ? -9.615  7.139   12.561 1.00 31.11  ? 44  PHE A CZ   1 
ATOM   705  H  H    . PHE A 1 47  ? -9.923  10.874  15.901 1.00 30.85  ? 44  PHE A H    1 
ATOM   706  H  HA   . PHE A 1 47  ? -10.402 8.595   17.134 1.00 31.19  ? 44  PHE A HA   1 
ATOM   707  H  HB2  . PHE A 1 47  ? -7.960  9.613   16.127 1.00 32.64  ? 44  PHE A HB2  1 
ATOM   708  H  HB3  . PHE A 1 47  ? -8.068  8.179   16.805 1.00 32.64  ? 44  PHE A HB3  1 
ATOM   709  H  HD1  . PHE A 1 47  ? -9.376  6.447   15.690 1.00 37.66  ? 44  PHE A HD1  1 
ATOM   710  H  HD2  . PHE A 1 47  ? -8.531  9.880   13.834 1.00 32.62  ? 44  PHE A HD2  1 
ATOM   711  H  HE1  . PHE A 1 47  ? -9.961  5.499   13.654 1.00 36.98  ? 44  PHE A HE1  1 
ATOM   712  H  HE2  . PHE A 1 47  ? -9.165  8.933   11.823 1.00 38.99  ? 44  PHE A HE2  1 
ATOM   713  H  HZ   . PHE A 1 47  ? -9.858  6.764   11.746 1.00 37.36  ? 44  PHE A HZ   1 
ATOM   714  N  N    . SER A 1 48  ? -9.335  8.644   19.368 1.00 26.39  ? 45  SER A N    1 
ATOM   715  C  CA   . SER A 1 48  ? -8.610  8.707   20.627 1.00 26.06  ? 45  SER A CA   1 
ATOM   716  C  C    . SER A 1 48  ? -7.169  8.296   20.347 1.00 26.70  ? 45  SER A C    1 
ATOM   717  O  O    . SER A 1 48  ? -6.900  7.341   19.606 1.00 26.55  ? 45  SER A O    1 
ATOM   718  C  CB   . SER A 1 48  ? -9.266  7.819   21.673 1.00 23.94  ? 45  SER A CB   1 
ATOM   719  O  OG   . SER A 1 48  ? -10.554 8.316   22.000 1.00 28.22  ? 45  SER A OG   1 
ATOM   720  H  H    . SER A 1 48  ? -9.759  7.906   19.238 1.00 31.71  ? 45  SER A H    1 
ATOM   721  H  HA   . SER A 1 48  ? -8.612  9.602   21.002 1.00 31.31  ? 45  SER A HA   1 
ATOM   722  H  HB2  . SER A 1 48  ? -9.353  6.920   21.318 1.00 28.76  ? 45  SER A HB2  1 
ATOM   723  H  HB3  . SER A 1 48  ? -8.717  7.808   22.472 1.00 28.76  ? 45  SER A HB3  1 
ATOM   724  H  HG   . SER A 1 48  ? -10.873 7.884   22.645 1.00 33.90  ? 45  SER A HG   1 
ATOM   725  N  N    . CYS A 1 49  ? -6.234  9.024   20.938 1.00 21.87  ? 46  CYS A N    1 
ATOM   726  C  CA   . CYS A 1 49  ? -4.810  8.802   20.720 1.00 22.28  ? 46  CYS A CA   1 
ATOM   727  C  C    . CYS A 1 49  ? -4.078  8.690   22.046 1.00 27.11  ? 46  CYS A C    1 
ATOM   728  O  O    . CYS A 1 49  ? -4.338  9.468   22.963 1.00 27.30  ? 46  CYS A O    1 
ATOM   729  C  CB   . CYS A 1 49  ? -4.239  9.959   19.928 1.00 24.73  ? 46  CYS A CB   1 
ATOM   730  S  SG   . CYS A 1 49  ? -4.954  10.054  18.304 1.00 26.66  ? 46  CYS A SG   1 
ATOM   731  H  H    . CYS A 1 49  ? -6.402  9.667   21.484 1.00 26.28  ? 46  CYS A H    1 
ATOM   732  H  HA   . CYS A 1 49  ? -4.673  7.968   20.244 1.00 26.77  ? 46  CYS A HA   1 
ATOM   733  H  HB2  . CYS A 1 49  ? -4.427  10.789  20.393 1.00 29.71  ? 46  CYS A HB2  1 
ATOM   734  H  HB3  . CYS A 1 49  ? -3.281  9.841   19.833 1.00 29.71  ? 46  CYS A HB3  1 
ATOM   735  H  HG   . CYS A 1 49  ? -4.535  11.032  17.749 1.00 32.03  ? 46  CYS A HG   1 
ATOM   736  N  N    . TYR A 1 50  ? -3.155  7.726   22.152 1.00 23.47  ? 47  TYR A N    1 
ATOM   737  C  CA   . TYR A 1 50  ? -2.341  7.558   23.361 1.00 22.66  ? 47  TYR A CA   1 
ATOM   738  C  C    . TYR A 1 50  ? -0.884  7.439   22.959 1.00 24.80  ? 47  TYR A C    1 
ATOM   739  O  O    . TYR A 1 50  ? -0.541  6.626   22.096 1.00 22.46  ? 47  TYR A O    1 
ATOM   740  C  CB   . TYR A 1 50  ? -2.800  6.344   24.139 1.00 22.02  ? 47  TYR A CB   1 
ATOM   741  C  CG   . TYR A 1 50  ? -2.183  6.251   25.516 1.00 23.18  ? 47  TYR A CG   1 
ATOM   742  C  CD1  . TYR A 1 50  ? -2.645  7.051   26.540 1.00 29.16  ? 47  TYR A CD1  1 
ATOM   743  C  CD2  . TYR A 1 50  ? -1.243  5.291   25.826 1.00 28.83  ? 47  TYR A CD2  1 
ATOM   744  C  CE1  . TYR A 1 50  ? -2.130  6.942   27.807 1.00 30.97  ? 47  TYR A CE1  1 
ATOM   745  C  CE2  . TYR A 1 50  ? -0.730  5.163   27.110 1.00 33.02  ? 47  TYR A CE2  1 
ATOM   746  C  CZ   . TYR A 1 50  ? -1.163  6.010   28.085 1.00 28.93  ? 47  TYR A CZ   1 
ATOM   747  O  OH   . TYR A 1 50  ? -0.693  5.943   29.403 1.00 29.99  ? 47  TYR A OH   1 
ATOM   748  H  H    . TYR A 1 50  ? -2.982  7.154   21.533 1.00 28.20  ? 47  TYR A H    1 
ATOM   749  H  HA   . TYR A 1 50  ? -2.421  8.333   23.939 1.00 27.22  ? 47  TYR A HA   1 
ATOM   750  H  HB2  . TYR A 1 50  ? -3.763  6.385   24.246 1.00 26.46  ? 47  TYR A HB2  1 
ATOM   751  H  HB3  . TYR A 1 50  ? -2.554  5.545   23.647 1.00 26.46  ? 47  TYR A HB3  1 
ATOM   752  H  HD1  . TYR A 1 50  ? -3.314  7.674   26.370 1.00 35.02  ? 47  TYR A HD1  1 
ATOM   753  H  HD2  . TYR A 1 50  ? -0.946  4.716   25.158 1.00 34.63  ? 47  TYR A HD2  1 
ATOM   754  H  HE1  . TYR A 1 50  ? -2.439  7.503   28.481 1.00 37.20  ? 47  TYR A HE1  1 
ATOM   755  H  HE2  . TYR A 1 50  ? -0.099  4.508   27.302 1.00 39.66  ? 47  TYR A HE2  1 
ATOM   756  H  HH   . TYR A 1 50  ? -0.033  5.426   29.447 1.00 36.02  ? 47  TYR A HH   1 
ATOM   757  N  N    . ALA A 1 51  ? -0.038  8.277   23.550 1.00 22.09  ? 48  ALA A N    1 
ATOM   758  C  CA   . ALA A 1 51  ? 1.382   8.361   23.192 1.00 20.65  ? 48  ALA A CA   1 
ATOM   759  C  C    . ALA A 1 51  ? 2.176   8.166   24.468 1.00 25.07  ? 48  ALA A C    1 
ATOM   760  O  O    . ALA A 1 51  ? 2.373   9.135   25.216 1.00 25.03  ? 48  ALA A O    1 
ATOM   761  C  CB   . ALA A 1 51  ? 1.728   9.683   22.526 1.00 25.05  ? 48  ALA A CB   1 
ATOM   762  H  H    . ALA A 1 51  ? -0.265  8.821   24.177 1.00 26.54  ? 48  ALA A H    1 
ATOM   763  H  HA   . ALA A 1 51  ? 1.606   7.662   22.558 1.00 24.82  ? 48  ALA A HA   1 
ATOM   764  H  HB1  . ALA A 1 51  ? 2.680   9.703   22.339 1.00 30.10  ? 48  ALA A HB1  1 
ATOM   765  H  HB2  . ALA A 1 51  ? 1.227   9.761   21.699 1.00 30.10  ? 48  ALA A HB2  1 
ATOM   766  H  HB3  . ALA A 1 51  ? 1.493   10.409  23.125 1.00 30.10  ? 48  ALA A HB3  1 
ATOM   767  N  N    . PRO A 1 52  ? 2.628   6.956   24.757 1.00 24.18  ? 49  PRO A N    1 
ATOM   768  C  CA   . PRO A 1 52  ? 3.488   6.744   25.919 1.00 22.20  ? 49  PRO A CA   1 
ATOM   769  C  C    . PRO A 1 52  ? 4.900   7.239   25.636 1.00 24.54  ? 49  PRO A C    1 
ATOM   770  O  O    . PRO A 1 52  ? 5.272   7.558   24.497 1.00 25.05  ? 49  PRO A O    1 
ATOM   771  C  CB   . PRO A 1 52  ? 3.436   5.225   26.109 1.00 24.52  ? 49  PRO A CB   1 
ATOM   772  C  CG   . PRO A 1 52  ? 3.322   4.690   24.718 1.00 26.25  ? 49  PRO A CG   1 
ATOM   773  C  CD   . PRO A 1 52  ? 2.371   5.695   24.017 1.00 25.69  ? 49  PRO A CD   1 
ATOM   774  H  HA   . PRO A 1 52  ? 3.145   7.178   26.716 1.00 26.67  ? 49  PRO A HA   1 
ATOM   775  H  HB2  . PRO A 1 52  ? 4.247   4.914   26.539 1.00 29.46  ? 49  PRO A HB2  1 
ATOM   776  H  HB3  . PRO A 1 52  ? 2.663   4.982   26.643 1.00 29.46  ? 49  PRO A HB3  1 
ATOM   777  H  HG2  . PRO A 1 52  ? 4.193   4.674   24.291 1.00 31.53  ? 49  PRO A HG2  1 
ATOM   778  H  HG3  . PRO A 1 52  ? 2.942   3.797   24.731 1.00 31.53  ? 49  PRO A HG3  1 
ATOM   779  H  HD2  . PRO A 1 52  ? 2.596   5.790   23.079 1.00 30.86  ? 49  PRO A HD2  1 
ATOM   780  H  HD3  . PRO A 1 52  ? 1.445   5.420   24.110 1.00 30.86  ? 49  PRO A HD3  1 
ATOM   781  N  N    . ASN A 1 53  ? 5.717   7.238   26.702 1.00 24.11  ? 50  ASN A N    1 
ATOM   782  C  CA   . ASN A 1 53  ? 7.139   7.547   26.602 1.00 23.26  ? 50  ASN A CA   1 
ATOM   783  C  C    . ASN A 1 53  ? 7.934   6.364   27.130 1.00 24.27  ? 50  ASN A C    1 
ATOM   784  O  O    . ASN A 1 53  ? 7.642   5.872   28.225 1.00 24.87  ? 50  ASN A O    1 
ATOM   785  C  CB   . ASN A 1 53  ? 7.420   8.830   27.381 1.00 28.43  ? 50  ASN A CB   1 
ATOM   786  C  CG   . ASN A 1 53  ? 8.613   9.528   26.867 1.00 35.35  ? 50  ASN A CG   1 
ATOM   787  O  OD1  . ASN A 1 53  ? 8.497   10.478  26.072 1.00 34.89  ? 50  ASN A OD1  1 
ATOM   788  N  ND2  . ASN A 1 53  ? 9.782   9.130   27.361 1.00 43.81  ? 50  ASN A ND2  1 
ATOM   789  H  H    . ASN A 1 53  ? 5.459   7.058   27.503 1.00 28.97  ? 50  ASN A H    1 
ATOM   790  H  HA   . ASN A 1 53  ? 7.420   7.681   25.683 1.00 27.94  ? 50  ASN A HA   1 
ATOM   791  H  HB2  . ASN A 1 53  ? 6.659   9.427   27.300 1.00 34.16  ? 50  ASN A HB2  1 
ATOM   792  H  HB3  . ASN A 1 53  ? 7.572   8.612   28.314 1.00 34.16  ? 50  ASN A HB3  1 
ATOM   793  H  HD21 . ASN A 1 53  ? 9.810   8.499   27.945 1.00 52.60  ? 50  ASN A HD21 1 
ATOM   794  H  HD22 . ASN A 1 53  ? 10.510  9.503   27.096 1.00 52.60  ? 50  ASN A HD22 1 
ATOM   795  N  N    . TYR A 1 54  ? 8.929   5.912   26.368 1.00 23.22  ? 51  TYR A N    1 
ATOM   796  C  CA   . TYR A 1 54  ? 9.697   4.760   26.797 1.00 23.31  ? 51  TYR A CA   1 
ATOM   797  C  C    . TYR A 1 54  ? 10.495  5.147   28.039 1.00 24.24  ? 51  TYR A C    1 
ATOM   798  O  O    . TYR A 1 54  ? 11.036  6.257   28.114 1.00 25.96  ? 51  TYR A O    1 
ATOM   799  C  CB   . TYR A 1 54  ? 10.691  4.256   25.741 1.00 23.73  ? 51  TYR A CB   1 
ATOM   800  C  CG   . TYR A 1 54  ? 10.106  3.996   24.372 1.00 21.09  ? 51  TYR A CG   1 
ATOM   801  C  CD1  . TYR A 1 54  ? 8.871   3.368   24.220 1.00 26.38  ? 51  TYR A CD1  1 
ATOM   802  C  CD2  . TYR A 1 54  ? 10.787  4.385   23.252 1.00 27.93  ? 51  TYR A CD2  1 
ATOM   803  C  CE1  . TYR A 1 54  ? 8.335   3.142   22.958 1.00 23.40  ? 51  TYR A CE1  1 
ATOM   804  C  CE2  . TYR A 1 54  ? 10.249  4.165   21.996 1.00 25.71  ? 51  TYR A CE2  1 
ATOM   805  C  CZ   . TYR A 1 54  ? 9.021   3.575   21.876 1.00 24.09  ? 51  TYR A CZ   1 
ATOM   806  O  OH   . TYR A 1 54  ? 8.490   3.381   20.585 1.00 23.81  ? 51  TYR A OH   1 
ATOM   807  H  H    A TYR A 1 54  ? 9.169   6.250   25.615 0.29 27.90  ? 51  TYR A H    1 
ATOM   808  H  H    B TYR A 1 54  ? 9.169   6.250   25.615 0.71 27.90  ? 51  TYR A H    1 
ATOM   809  H  HA   . TYR A 1 54  ? 9.076   4.036   26.971 1.00 28.01  ? 51  TYR A HA   1 
ATOM   810  H  HB2  . TYR A 1 54  ? 11.388  4.922   25.635 1.00 28.51  ? 51  TYR A HB2  1 
ATOM   811  H  HB3  . TYR A 1 54  ? 11.074  3.422   26.055 1.00 28.51  ? 51  TYR A HB3  1 
ATOM   812  H  HD1  . TYR A 1 54  ? 8.400   3.096   24.974 1.00 31.70  ? 51  TYR A HD1  1 
ATOM   813  H  HD2  . TYR A 1 54  ? 11.616  4.800   23.335 1.00 33.55  ? 51  TYR A HD2  1 
ATOM   814  H  HE1  . TYR A 1 54  ? 7.522   2.702   22.859 1.00 28.11  ? 51  TYR A HE1  1 
ATOM   815  H  HE2  . TYR A 1 54  ? 10.722  4.417   21.236 1.00 30.88  ? 51  TYR A HE2  1 
ATOM   816  H  HH   . TYR A 1 54  ? 9.039   3.644   20.006 1.00 28.61  ? 51  TYR A HH   1 
ATOM   817  N  N    . PRO A 1 55  ? 10.575  4.266   29.033 1.00 24.25  ? 52  PRO A N    1 
ATOM   818  C  CA   . PRO A 1 55  ? 11.391  4.567   30.219 1.00 23.24  ? 52  PRO A CA   1 
ATOM   819  C  C    . PRO A 1 55  ? 12.830  4.877   29.822 1.00 27.00  ? 52  PRO A C    1 
ATOM   820  O  O    . PRO A 1 55  ? 13.364  4.331   28.856 1.00 29.16  ? 52  PRO A O    1 
ATOM   821  C  CB   . PRO A 1 55  ? 11.296  3.293   31.065 1.00 30.60  ? 52  PRO A CB   1 
ATOM   822  C  CG   . PRO A 1 55  ? 10.120  2.546   30.575 1.00 29.88  ? 52  PRO A CG   1 
ATOM   823  C  CD   . PRO A 1 55  ? 9.700   3.094   29.205 1.00 24.22  ? 52  PRO A CD   1 
ATOM   824  H  HA   . PRO A 1 55  ? 11.016  5.310   30.717 1.00 27.92  ? 52  PRO A HA   1 
ATOM   825  H  HB2  . PRO A 1 55  ? 12.105  2.769   30.953 1.00 36.75  ? 52  PRO A HB2  1 
ATOM   826  H  HB3  . PRO A 1 55  ? 11.184  3.533   31.999 1.00 36.75  ? 52  PRO A HB3  1 
ATOM   827  H  HG2  . PRO A 1 55  ? 10.356  1.609   30.497 1.00 35.89  ? 52  PRO A HG2  1 
ATOM   828  H  HG3  . PRO A 1 55  ? 9.395   2.654   31.210 1.00 35.89  ? 52  PRO A HG3  1 
ATOM   829  H  HD2  . PRO A 1 55  ? 9.858   2.439   28.507 1.00 29.10  ? 52  PRO A HD2  1 
ATOM   830  H  HD3  . PRO A 1 55  ? 8.767   3.358   29.209 1.00 29.10  ? 52  PRO A HD3  1 
ATOM   831  N  N    . GLY A 1 56  ? 13.431  5.813   30.562 1.00 25.43  ? 53  GLY A N    1 
ATOM   832  C  CA   . GLY A 1 56  ? 14.781  6.268   30.321 1.00 30.64  ? 53  GLY A CA   1 
ATOM   833  C  C    . GLY A 1 56  ? 14.894  7.365   29.289 1.00 28.39  ? 53  GLY A C    1 
ATOM   834  O  O    . GLY A 1 56  ? 15.882  8.104   29.282 1.00 30.80  ? 53  GLY A O    1 
ATOM   835  H  H    . GLY A 1 56  ? 13.056  6.206   31.228 1.00 30.55  ? 53  GLY A H    1 
ATOM   836  H  HA2  . GLY A 1 56  ? 15.151  6.602   31.153 1.00 36.80  ? 53  GLY A HA2  1 
ATOM   837  H  HA3  . GLY A 1 56  ? 15.314  5.517   30.018 1.00 36.80  ? 53  GLY A HA3  1 
ATOM   838  N  N    . HIS A 1 57  ? 13.911  7.501   28.430 1.00 27.40  ? 54  HIS A N    1 
ATOM   839  C  CA   . HIS A 1 57  ? 14.008  8.468   27.350 1.00 27.15  ? 54  HIS A CA   1 
ATOM   840  C  C    . HIS A 1 57  ? 13.702  9.858   27.895 1.00 30.93  ? 54  HIS A C    1 
ATOM   841  O  O    . HIS A 1 57  ? 12.732  10.043  28.628 1.00 37.09  ? 54  HIS A O    1 
ATOM   842  C  CB   . HIS A 1 57  ? 13.067  8.084   26.233 1.00 26.95  ? 54  HIS A CB   1 
ATOM   843  C  CG   . HIS A 1 57  ? 13.591  6.996   25.343 1.00 27.17  ? 54  HIS A CG   1 
ATOM   844  N  ND1  . HIS A 1 57  ? 13.928  5.735   25.803 1.00 28.66  ? 54  HIS A ND1  1 
ATOM   845  C  CD2  . HIS A 1 57  ? 13.906  7.010   24.027 1.00 27.12  ? 54  HIS A CD2  1 
ATOM   846  C  CE1  . HIS A 1 57  ? 14.349  5.002   24.790 1.00 29.79  ? 54  HIS A CE1  1 
ATOM   847  N  NE2  . HIS A 1 57  ? 14.363  5.758   23.700 1.00 26.91  ? 54  HIS A NE2  1 
ATOM   848  H  H    . HIS A 1 57  ? 13.180  7.049   28.445 1.00 32.92  ? 54  HIS A H    1 
ATOM   849  H  HA   . HIS A 1 57  ? 14.904  8.485   26.980 1.00 32.61  ? 54  HIS A HA   1 
ATOM   850  H  HB2  . HIS A 1 57  ? 12.234  7.773   26.621 1.00 32.37  ? 54  HIS A HB2  1 
ATOM   851  H  HB3  . HIS A 1 57  ? 12.904  8.865   25.681 1.00 32.37  ? 54  HIS A HB3  1 
ATOM   852  H  HD1  . HIS A 1 57  ? 13.873  5.471   26.619 1.00 34.43  ? 54  HIS A HD1  1 
ATOM   853  H  HD2  . HIS A 1 57  ? 13.826  7.735   23.450 1.00 32.58  ? 54  HIS A HD2  1 
ATOM   854  H  HE1  . HIS A 1 57  ? 14.595  4.107   24.833 1.00 35.78  ? 54  HIS A HE1  1 
ATOM   855  N  N    . GLY A 1 58  ? 14.568  10.823  27.586 1.00 29.65  ? 55  GLY A N    1 
ATOM   856  C  CA   . GLY A 1 58  ? 14.511  12.133  28.187 1.00 32.91  ? 55  GLY A CA   1 
ATOM   857  C  C    . GLY A 1 58  ? 15.544  12.377  29.260 1.00 36.26  ? 55  GLY A C    1 
ATOM   858  O  O    . GLY A 1 58  ? 15.694  13.519  29.710 1.00 37.80  ? 55  GLY A O    1 
ATOM   859  H  H    . GLY A 1 58  ? 15.207  10.731  27.018 1.00 35.62  ? 55  GLY A H    1 
ATOM   860  H  HA2  . GLY A 1 58  ? 14.640  12.799  27.493 1.00 39.53  ? 55  GLY A HA2  1 
ATOM   861  H  HA3  . GLY A 1 58  ? 13.635  12.257  28.584 1.00 39.53  ? 55  GLY A HA3  1 
ATOM   862  N  N    . LEU A 1 59  ? 16.245  11.343  29.696 1.00 31.43  ? 56  LEU A N    1 
ATOM   863  C  CA   . LEU A 1 59  ? 17.237  11.455  30.744 1.00 29.98  ? 56  LEU A CA   1 
ATOM   864  C  C    . LEU A 1 59  ? 18.646  11.543  30.164 1.00 34.19  ? 56  LEU A C    1 
ATOM   865  O  O    . LEU A 1 59  ? 18.896  11.212  29.004 1.00 35.26  ? 56  LEU A O    1 
ATOM   866  C  CB   . LEU A 1 59  ? 17.135  10.249  31.694 1.00 38.44  ? 56  LEU A CB   1 
ATOM   867  C  CG   . LEU A 1 59  ? 15.765  9.971   32.309 1.00 36.51  ? 56  LEU A CG   1 
ATOM   868  C  CD1  . LEU A 1 59  ? 15.895  8.778   33.273 1.00 35.94  ? 56  LEU A CD1  1 
ATOM   869  C  CD2  . LEU A 1 59  ? 15.217  11.188  33.026 1.00 45.76  ? 56  LEU A CD2  1 
ATOM   870  H  H    . LEU A 1 59  ? 16.160  10.544  29.389 1.00 37.76  ? 56  LEU A H    1 
ATOM   871  H  HA   . LEU A 1 59  ? 17.077  12.268  31.248 1.00 36.01  ? 56  LEU A HA   1 
ATOM   872  H  HB2  . LEU A 1 59  ? 17.390  9.455   31.198 1.00 46.16  ? 56  LEU A HB2  1 
ATOM   873  H  HB3  . LEU A 1 59  ? 17.752  10.394  32.429 1.00 46.16  ? 56  LEU A HB3  1 
ATOM   874  H  HG   . LEU A 1 59  ? 15.130  9.755   31.608 1.00 43.85  ? 56  LEU A HG   1 
ATOM   875  H  HD11 . LEU A 1 59  ? 15.035  8.616   33.692 1.00 43.16  ? 56  LEU A HD11 1 
ATOM   876  H  HD12 . LEU A 1 59  ? 16.172  7.995   32.772 1.00 43.16  ? 56  LEU A HD12 1 
ATOM   877  H  HD13 . LEU A 1 59  ? 16.558  8.989   33.949 1.00 43.16  ? 56  LEU A HD13 1 
ATOM   878  H  HD21 . LEU A 1 59  ? 14.395  10.944  33.480 1.00 54.95  ? 56  LEU A HD21 1 
ATOM   879  H  HD22 . LEU A 1 59  ? 15.872  11.496  33.672 1.00 54.95  ? 56  LEU A HD22 1 
ATOM   880  H  HD23 . LEU A 1 59  ? 15.041  11.885  32.375 1.00 54.95  ? 56  LEU A HD23 1 
ATOM   881  N  N    . LEU A 1 60  ? 19.581  11.966  31.019 1.00 38.70  ? 57  LEU A N    1 
ATOM   882  C  CA   . LEU A 1 60  ? 20.990  11.940  30.649 1.00 41.32  ? 57  LEU A CA   1 
ATOM   883  C  C    . LEU A 1 60  ? 21.413  10.516  30.320 1.00 42.16  ? 57  LEU A C    1 
ATOM   884  O  O    . LEU A 1 60  ? 20.816  9.547   30.796 1.00 34.91  ? 57  LEU A O    1 
ATOM   885  C  CB   . LEU A 1 60  ? 21.852  12.507  31.783 1.00 43.48  ? 57  LEU A CB   1 
ATOM   886  C  CG   . LEU A 1 60  ? 21.585  13.990  32.061 1.00 53.32  ? 57  LEU A CG   1 
ATOM   887  C  CD1  . LEU A 1 60  ? 22.383  14.474  33.276 1.00 52.52  ? 57  LEU A CD1  1 
ATOM   888  C  CD2  . LEU A 1 60  ? 21.893  14.854  30.830 1.00 56.75  ? 57  LEU A CD2  1 
ATOM   889  H  H    . LEU A 1 60  ? 19.424  12.269  31.809 1.00 46.47  ? 57  LEU A H    1 
ATOM   890  H  HA   . LEU A 1 60  ? 21.136  12.493  29.866 1.00 49.62  ? 57  LEU A HA   1 
ATOM   891  H  HB2  . LEU A 1 60  ? 21.665  12.012  32.596 1.00 52.21  ? 57  LEU A HB2  1 
ATOM   892  H  HB3  . LEU A 1 60  ? 22.787  12.411  31.544 1.00 52.21  ? 57  LEU A HB3  1 
ATOM   893  H  HG   . LEU A 1 60  ? 20.642  14.095  32.263 1.00 64.02  ? 57  LEU A HG   1 
ATOM   894  H  HD11 . LEU A 1 60  ? 22.197  15.415  33.421 1.00 63.06  ? 57  LEU A HD11 1 
ATOM   895  H  HD12 . LEU A 1 60  ? 22.115  13.960  34.054 1.00 63.06  ? 57  LEU A HD12 1 
ATOM   896  H  HD13 . LEU A 1 60  ? 23.329  14.346  33.105 1.00 63.06  ? 57  LEU A HD13 1 
ATOM   897  H  HD21 . LEU A 1 60  ? 21.738  15.785  31.051 1.00 68.14  ? 57  LEU A HD21 1 
ATOM   898  H  HD22 . LEU A 1 60  ? 22.820  14.724  30.577 1.00 68.14  ? 57  LEU A HD22 1 
ATOM   899  H  HD23 . LEU A 1 60  ? 21.310  14.585  30.103 1.00 68.14  ? 57  LEU A HD23 1 
ATOM   900  N  N    . LEU A 1 61  ? 22.462  10.397  29.496 1.00 42.59  ? 58  LEU A N    1 
ATOM   901  C  CA   . LEU A 1 61  ? 22.817  9.102   28.922 1.00 38.62  ? 58  LEU A CA   1 
ATOM   902  C  C    . LEU A 1 61  ? 23.063  8.041   29.984 1.00 34.98  ? 58  LEU A C    1 
ATOM   903  O  O    . LEU A 1 61  ? 22.650  6.884   29.818 1.00 38.72  ? 58  LEU A O    1 
ATOM   904  C  CB   . LEU A 1 61  ? 24.060  9.219   28.037 1.00 46.11  ? 58  LEU A CB   1 
ATOM   905  C  CG   . LEU A 1 61  ? 24.251  8.035   27.074 1.00 49.00  ? 58  LEU A CG   1 
ATOM   906  C  CD1  . LEU A 1 61  ? 23.168  7.882   26.045 1.00 43.25  ? 58  LEU A CD1  1 
ATOM   907  C  CD2  . LEU A 1 61  ? 25.610  8.166   26.386 1.00 56.33  ? 58  LEU A CD2  1 
ATOM   908  H  H    . LEU A 1 61  ? 22.976  11.045  29.258 1.00 51.14  ? 58  LEU A H    1 
ATOM   909  H  HA   . LEU A 1 61  ? 22.065  8.823   28.377 1.00 46.38  ? 58  LEU A HA   1 
ATOM   910  H  HB2  . LEU A 1 61  ? 23.987  10.026  27.504 1.00 55.37  ? 58  LEU A HB2  1 
ATOM   911  H  HB3  . LEU A 1 61  ? 24.844  9.268   28.607 1.00 55.37  ? 58  LEU A HB3  1 
ATOM   912  H  HG   . LEU A 1 61  ? 24.206  7.226   27.608 1.00 58.83  ? 58  LEU A HG   1 
ATOM   913  H  HD11 . LEU A 1 61  ? 23.493  7.318   25.326 1.00 51.94  ? 58  LEU A HD11 1 
ATOM   914  H  HD12 . LEU A 1 61  ? 22.392  7.475   26.460 1.00 51.94  ? 58  LEU A HD12 1 
ATOM   915  H  HD13 . LEU A 1 61  ? 22.936  8.758   25.698 1.00 51.94  ? 58  LEU A HD13 1 
ATOM   916  H  HD21 . LEU A 1 61  ? 25.736  7.413   25.788 1.00 67.64  ? 58  LEU A HD21 1 
ATOM   917  H  HD22 . LEU A 1 61  ? 25.630  8.995   25.882 1.00 67.64  ? 58  LEU A HD22 1 
ATOM   918  H  HD23 . LEU A 1 61  ? 26.307  8.173   27.061 1.00 67.64  ? 58  LEU A HD23 1 
ATOM   919  N  N    . LYS A 1 62  ? 23.785  8.388   31.056 1.00 36.49  ? 59  LYS A N    1 
ATOM   920  C  CA   . LYS A 1 62  ? 24.125  7.375   32.043 1.00 42.44  ? 59  LYS A CA   1 
ATOM   921  C  C    . LYS A 1 62  ? 22.869  6.821   32.711 1.00 42.73  ? 59  LYS A C    1 
ATOM   922  O  O    . LYS A 1 62  ? 22.798  5.622   32.983 1.00 43.07  ? 59  LYS A O    1 
ATOM   923  C  CB   . LYS A 1 62  ? 25.098  7.944   33.077 1.00 49.04  ? 59  LYS A CB   1 
ATOM   924  C  CG   . LYS A 1 62  ? 25.702  6.882   33.993 1.00 74.14  ? 59  LYS A CG   1 
ATOM   925  C  CD   . LYS A 1 62  ? 26.622  7.527   35.037 1.00 92.23  ? 59  LYS A CD   1 
ATOM   926  C  CE   . LYS A 1 62  ? 26.921  6.590   36.204 1.00 78.61  ? 59  LYS A CE   1 
ATOM   927  N  NZ   . LYS A 1 62  ? 27.856  5.503   35.807 1.00 96.81  ? 59  LYS A NZ   1 
ATOM   928  H  H    . LYS A 1 62  ? 24.078  9.179   31.224 1.00 43.82  ? 59  LYS A H    1 
ATOM   929  H  HA   . LYS A 1 62  ? 24.575  6.639   31.599 1.00 50.96  ? 59  LYS A HA   1 
ATOM   930  H  HB2  . LYS A 1 62  ? 25.826  8.385   32.612 1.00 58.89  ? 59  LYS A HB2  1 
ATOM   931  H  HB3  . LYS A 1 62  ? 24.625  8.583   33.634 1.00 58.89  ? 59  LYS A HB3  1 
ATOM   932  H  HG2  . LYS A 1 62  ? 24.992  6.411   34.457 1.00 89.00  ? 59  LYS A HG2  1 
ATOM   933  H  HG3  . LYS A 1 62  ? 26.225  6.258   33.466 1.00 89.00  ? 59  LYS A HG3  1 
ATOM   934  H  HD2  . LYS A 1 62  ? 27.464  7.763   34.617 1.00 110.71 ? 59  LYS A HD2  1 
ATOM   935  H  HD3  . LYS A 1 62  ? 26.193  8.321   35.391 1.00 110.71 ? 59  LYS A HD3  1 
ATOM   936  H  HE2  . LYS A 1 62  ? 27.330  7.096   36.925 1.00 94.36  ? 59  LYS A HE2  1 
ATOM   937  H  HE3  . LYS A 1 62  ? 26.095  6.185   36.511 1.00 94.36  ? 59  LYS A HE3  1 
ATOM   938  H  HZ1  . LYS A 1 62  ? 28.016  4.970   36.502 1.00 116.20 ? 59  LYS A HZ1  1 
ATOM   939  H  HZ2  . LYS A 1 62  ? 27.500  5.021   35.149 1.00 116.20 ? 59  LYS A HZ2  1 
ATOM   940  H  HZ3  . LYS A 1 62  ? 28.626  5.851   35.527 1.00 116.20 ? 59  LYS A HZ3  1 
ATOM   941  N  N    . ASP A 1 63  ? 21.853  7.667   32.949 1.00 33.46  ? 60  ASP A N    1 
ATOM   942  C  CA   . ASP A 1 63  ? 20.567  7.164   33.440 1.00 31.08  ? 60  ASP A CA   1 
ATOM   943  C  C    . ASP A 1 63  ? 19.801  6.416   32.346 1.00 31.39  ? 60  ASP A C    1 
ATOM   944  O  O    . ASP A 1 63  ? 19.205  5.361   32.601 1.00 30.43  ? 60  ASP A O    1 
ATOM   945  C  CB   . ASP A 1 63  ? 19.736  8.319   33.996 1.00 30.70  ? 60  ASP A CB   1 
ATOM   946  C  CG   . ASP A 1 63  ? 20.418  9.030   35.171 1.00 41.38  ? 60  ASP A CG   1 
ATOM   947  O  OD1  . ASP A 1 63  ? 21.127  8.385   35.970 1.00 35.63  ? 60  ASP A OD1  1 
ATOM   948  O  OD2  . ASP A 1 63  ? 20.256  10.260  35.271 1.00 40.10  ? 60  ASP A OD2  1 
ATOM   949  H  H    A ASP A 1 63  ? 21.885  8.519   32.836 0.38 40.19  ? 60  ASP A H    1 
ATOM   950  H  H    B ASP A 1 63  ? 21.885  8.519   32.836 0.62 40.19  ? 60  ASP A H    1 
ATOM   951  H  HA   . ASP A 1 63  ? 20.732  6.536   34.161 1.00 37.33  ? 60  ASP A HA   1 
ATOM   952  H  HB2  . ASP A 1 63  ? 19.592  8.972   33.293 1.00 36.87  ? 60  ASP A HB2  1 
ATOM   953  H  HB3  . ASP A 1 63  ? 18.884  7.974   34.308 1.00 36.87  ? 60  ASP A HB3  1 
ATOM   954  N  N    . PHE A 1 64  ? 19.803  6.952   31.127 1.00 30.49  ? 61  PHE A N    1 
ATOM   955  C  CA   . PHE A 1 64  ? 19.159  6.299   29.983 1.00 29.74  ? 61  PHE A CA   1 
ATOM   956  C  C    . PHE A 1 64  ? 19.599  4.845   29.848 1.00 29.70  ? 61  PHE A C    1 
ATOM   957  O  O    . PHE A 1 64  ? 18.779  3.958   29.590 1.00 26.63  ? 61  PHE A O    1 
ATOM   958  C  CB   . PHE A 1 64  ? 19.507  7.098   28.733 1.00 31.38  ? 61  PHE A CB   1 
ATOM   959  C  CG   . PHE A 1 64  ? 18.932  6.570   27.449 1.00 31.58  ? 61  PHE A CG   1 
ATOM   960  C  CD1  . PHE A 1 64  ? 19.501  5.475   26.806 1.00 32.69  ? 61  PHE A CD1  1 
ATOM   961  C  CD2  . PHE A 1 64  ? 17.856  7.209   26.858 1.00 34.79  ? 61  PHE A CD2  1 
ATOM   962  C  CE1  . PHE A 1 64  ? 18.984  5.014   25.610 1.00 35.02  ? 61  PHE A CE1  1 
ATOM   963  C  CE2  . PHE A 1 64  ? 17.353  6.761   25.646 1.00 29.24  ? 61  PHE A CE2  1 
ATOM   964  C  CZ   . PHE A 1 64  ? 17.929  5.672   25.035 1.00 30.72  ? 61  PHE A CZ   1 
ATOM   965  H  H    . PHE A 1 64  ? 20.175  7.701   30.929 1.00 36.62  ? 61  PHE A H    1 
ATOM   966  H  HA   . PHE A 1 64  ? 18.195  6.290   30.098 1.00 35.72  ? 61  PHE A HA   1 
ATOM   967  H  HB2  . PHE A 1 64  ? 19.177  8.003   28.847 1.00 37.69  ? 61  PHE A HB2  1 
ATOM   968  H  HB3  . PHE A 1 64  ? 20.472  7.106   28.636 1.00 37.69  ? 61  PHE A HB3  1 
ATOM   969  H  HD1  . PHE A 1 64  ? 20.236  5.050   27.185 1.00 39.26  ? 61  PHE A HD1  1 
ATOM   970  H  HD2  . PHE A 1 64  ? 17.469  7.944   27.276 1.00 41.78  ? 61  PHE A HD2  1 
ATOM   971  H  HE1  . PHE A 1 64  ? 19.349  4.264   25.199 1.00 42.05  ? 61  PHE A HE1  1 
ATOM   972  H  HE2  . PHE A 1 64  ? 16.631  7.193   25.250 1.00 35.13  ? 61  PHE A HE2  1 
ATOM   973  H  HZ   . PHE A 1 64  ? 17.597  5.378   24.218 1.00 36.90  ? 61  PHE A HZ   1 
ATOM   974  N  N    . MET A 1 65  ? 20.887  4.574   30.051 1.00 30.17  ? 62  MET A N    1 
ATOM   975  C  CA   . MET A 1 65  ? 21.411  3.239   29.813 1.00 32.70  ? 62  MET A CA   1 
ATOM   976  C  C    . MET A 1 65  ? 21.205  2.292   30.966 1.00 36.05  ? 62  MET A C    1 
ATOM   977  O  O    . MET A 1 65  ? 21.703  1.154   30.916 1.00 35.41  ? 62  MET A O    1 
ATOM   978  C  CB   . MET A 1 65  ? 22.886  3.302   29.437 1.00 42.53  ? 62  MET A CB   1 
ATOM   979  C  CG   . MET A 1 65  ? 23.110  4.105   28.154 1.00 45.96  ? 62  MET A CG   1 
ATOM   980  S  SD   . MET A 1 65  ? 24.829  4.093   27.590 1.00 47.64  ? 62  MET A SD   1 
ATOM   981  C  CE   . MET A 1 65  ? 25.622  5.012   28.920 1.00 46.97  ? 62  MET A CE   1 
ATOM   982  H  H    . MET A 1 65  ? 21.469  5.145   30.323 1.00 36.24  ? 62  MET A H    1 
ATOM   983  H  HA   . MET A 1 65  ? 20.936  2.874   29.050 1.00 39.28  ? 62  MET A HA   1 
ATOM   984  H  HB2  . MET A 1 65  ? 23.380  3.730   30.154 1.00 51.07  ? 62  MET A HB2  1 
ATOM   985  H  HB3  . MET A 1 65  ? 23.219  2.402   29.295 1.00 51.07  ? 62  MET A HB3  1 
ATOM   986  H  HG2  . MET A 1 65  ? 22.563  3.726   27.448 1.00 55.19  ? 62  MET A HG2  1 
ATOM   987  H  HG3  . MET A 1 65  ? 22.855  5.027   28.312 1.00 55.19  ? 62  MET A HG3  1 
ATOM   988  H  HE1  . MET A 1 65  ? 26.565  5.112   28.716 1.00 56.40  ? 62  MET A HE1  1 
ATOM   989  H  HE2  . MET A 1 65  ? 25.204  5.884   28.994 1.00 56.40  ? 62  MET A HE2  1 
ATOM   990  H  HE3  . MET A 1 65  ? 25.514  4.521   29.750 1.00 56.40  ? 62  MET A HE3  1 
ATOM   991  N  N    . THR A 1 66  ? 20.470  2.688   31.995 1.00 29.45  ? 63  THR A N    1 
ATOM   992  C  CA   . THR A 1 66  ? 20.035  1.722   32.999 1.00 28.58  ? 63  THR A CA   1 
ATOM   993  C  C    . THR A 1 66  ? 18.685  1.118   32.637 1.00 27.96  ? 63  THR A C    1 
ATOM   994  O  O    . THR A 1 66  ? 18.135  0.330   33.412 1.00 32.13  ? 63  THR A O    1 
ATOM   995  C  CB   . THR A 1 66  ? 19.988  2.353   34.402 1.00 30.93  ? 63  THR A CB   1 
ATOM   996  O  OG1  . THR A 1 66  ? 18.959  3.352   34.455 1.00 30.28  ? 63  THR A OG1  1 
ATOM   997  C  CG2  . THR A 1 66  ? 21.331  2.940   34.770 1.00 32.86  ? 63  THR A CG2  1 
ATOM   998  H  H    . THR A 1 66  ? 20.215  3.498   32.133 1.00 35.37  ? 63  THR A H    1 
ATOM   999  H  HA   . THR A 1 66  ? 20.688  1.007   33.056 1.00 34.33  ? 63  THR A HA   1 
ATOM   1000 H  HB   . THR A 1 66  ? 19.783  1.671   35.060 1.00 37.15  ? 63  THR A HB   1 
ATOM   1001 H  HG1  . THR A 1 66  ? 19.146  3.985   33.936 1.00 36.37  ? 63  THR A HG1  1 
ATOM   1002 H  HG21 . THR A 1 66  ? 21.337  3.193   35.707 1.00 39.46  ? 63  THR A HG21 1 
ATOM   1003 H  HG22 . THR A 1 66  ? 22.032  2.288   34.616 1.00 39.46  ? 63  THR A HG22 1 
ATOM   1004 H  HG23 . THR A 1 66  ? 21.508  3.727   34.231 1.00 39.46  ? 63  THR A HG23 1 
ATOM   1005 N  N    . TYR A 1 67  ? 18.142  1.465   31.477 1.00 27.15  ? 64  TYR A N    1 
ATOM   1006 C  CA   . TYR A 1 67  ? 16.930  0.868   30.951 1.00 26.41  ? 64  TYR A CA   1 
ATOM   1007 C  C    . TYR A 1 67  ? 17.289  0.182   29.644 1.00 30.01  ? 64  TYR A C    1 
ATOM   1008 O  O    . TYR A 1 67  ? 18.266  0.541   28.996 1.00 32.52  ? 64  TYR A O    1 
ATOM   1009 C  CB   . TYR A 1 67  ? 15.844  1.893   30.685 1.00 27.29  ? 64  TYR A CB   1 
ATOM   1010 C  CG   . TYR A 1 67  ? 15.410  2.676   31.902 1.00 26.46  ? 64  TYR A CG   1 
ATOM   1011 C  CD1  . TYR A 1 67  ? 16.087  3.822   32.307 1.00 26.84  ? 64  TYR A CD1  1 
ATOM   1012 C  CD2  . TYR A 1 67  ? 14.313  2.254   32.637 1.00 28.09  ? 64  TYR A CD2  1 
ATOM   1013 C  CE1  . TYR A 1 67  ? 15.654  4.555   33.437 1.00 30.55  ? 64  TYR A CE1  1 
ATOM   1014 C  CE2  . TYR A 1 67  ? 13.888  2.972   33.775 1.00 27.70  ? 64  TYR A CE2  1 
ATOM   1015 C  CZ   . TYR A 1 67  ? 14.552  4.122   34.129 1.00 30.58  ? 64  TYR A CZ   1 
ATOM   1016 O  OH   . TYR A 1 67  ? 14.131  4.832   35.224 1.00 31.75  ? 64  TYR A OH   1 
ATOM   1017 H  H    . TYR A 1 67  ? 18.473  2.067   30.959 1.00 32.61  ? 64  TYR A H    1 
ATOM   1018 H  HA   . TYR A 1 67  ? 16.574  0.232   31.591 1.00 31.73  ? 64  TYR A HA   1 
ATOM   1019 H  HB2  . TYR A 1 67  ? 16.173  2.528   30.030 1.00 32.78  ? 64  TYR A HB2  1 
ATOM   1020 H  HB3  . TYR A 1 67  ? 15.063  1.433   30.339 1.00 32.78  ? 64  TYR A HB3  1 
ATOM   1021 H  HD1  . TYR A 1 67  ? 16.831  4.109   31.829 1.00 32.25  ? 64  TYR A HD1  1 
ATOM   1022 H  HD2  . TYR A 1 67  ? 13.851  1.490   32.376 1.00 33.75  ? 64  TYR A HD2  1 
ATOM   1023 H  HE1  . TYR A 1 67  ? 16.111  5.319   33.706 1.00 36.69  ? 64  TYR A HE1  1 
ATOM   1024 H  HE2  . TYR A 1 67  ? 13.168  2.670   34.280 1.00 33.27  ? 64  TYR A HE2  1 
ATOM   1025 H  HH   . TYR A 1 67  ? 13.526  4.410   35.625 1.00 38.13  ? 64  TYR A HH   1 
ATOM   1026 N  N    . ASN A 1 68  ? 16.506  -0.819  29.260 1.00 30.36  ? 65  ASN A N    1 
ATOM   1027 C  CA   . ASN A 1 68  ? 16.830  -1.557  28.032 1.00 28.39  ? 65  ASN A CA   1 
ATOM   1028 C  C    . ASN A 1 68  ? 15.543  -1.894  27.281 1.00 29.64  ? 65  ASN A C    1 
ATOM   1029 O  O    . ASN A 1 68  ? 14.443  -1.509  27.668 1.00 26.96  ? 65  ASN A O    1 
ATOM   1030 C  CB   . ASN A 1 68  ? 17.647  -2.820  28.351 1.00 29.96  ? 65  ASN A CB   1 
ATOM   1031 C  CG   . ASN A 1 68  ? 16.931  -3.777  29.261 1.00 36.78  ? 65  ASN A CG   1 
ATOM   1032 O  OD1  . ASN A 1 68  ? 15.760  -4.092  29.055 1.00 39.15  ? 65  ASN A OD1  1 
ATOM   1033 N  ND2  . ASN A 1 68  ? 17.629  -4.248  30.292 1.00 54.33  ? 65  ASN A ND2  1 
ATOM   1034 H  H    . ASN A 1 68  ? 15.802  -1.084  29.677 1.00 36.46  ? 65  ASN A H    1 
ATOM   1035 H  HA   . ASN A 1 68  ? 17.359  -0.985  27.455 1.00 34.10  ? 65  ASN A HA   1 
ATOM   1036 H  HB2  . ASN A 1 68  ? 17.842  -3.286  27.523 1.00 35.99  ? 65  ASN A HB2  1 
ATOM   1037 H  HB3  . ASN A 1 68  ? 18.474  -2.557  28.786 1.00 35.99  ? 65  ASN A HB3  1 
ATOM   1038 H  HD21 . ASN A 1 68  ? 17.265  -4.799  30.842 1.00 65.24  ? 65  ASN A HD21 1 
ATOM   1039 H  HD22 . ASN A 1 68  ? 18.445  -4.002  30.407 1.00 65.24  ? 65  ASN A HD22 1 
ATOM   1040 N  N    . VAL A 1 69  ? 15.698  -2.623  26.178 1.00 26.29  ? 66  VAL A N    1 
ATOM   1041 C  CA   . VAL A 1 69  ? 14.583  -2.839  25.275 1.00 25.25  ? 66  VAL A CA   1 
ATOM   1042 C  C    . VAL A 1 69  ? 13.457  -3.582  25.969 1.00 25.57  ? 66  VAL A C    1 
ATOM   1043 O  O    . VAL A 1 69  ? 12.279  -3.365  25.644 1.00 25.46  ? 66  VAL A O    1 
ATOM   1044 C  CB   . VAL A 1 69  ? 15.093  -3.567  24.005 1.00 27.36  ? 66  VAL A CB   1 
ATOM   1045 C  CG1  . VAL A 1 69  ? 15.497  -5.000  24.282 1.00 29.69  ? 66  VAL A CG1  1 
ATOM   1046 C  CG2  . VAL A 1 69  ? 14.034  -3.463  22.934 1.00 33.96  ? 66  VAL A CG2  1 
ATOM   1047 H  H    . VAL A 1 69  ? 16.433  -2.998  25.935 1.00 31.59  ? 66  VAL A H    1 
ATOM   1048 H  HA   . VAL A 1 69  ? 14.217  -1.984  25.000 1.00 30.33  ? 66  VAL A HA   1 
ATOM   1049 H  HB   . VAL A 1 69  ? 15.904  -3.139  23.689 1.00 32.87  ? 66  VAL A HB   1 
ATOM   1050 H  HG11 . VAL A 1 69  ? 16.006  -5.336  23.527 1.00 35.67  ? 66  VAL A HG11 1 
ATOM   1051 H  HG12 . VAL A 1 69  ? 16.041  -5.025  25.085 1.00 35.67  ? 66  VAL A HG12 1 
ATOM   1052 H  HG13 . VAL A 1 69  ? 14.698  -5.535  24.407 1.00 35.67  ? 66  VAL A HG13 1 
ATOM   1053 H  HG21 . VAL A 1 69  ? 14.319  -3.970  22.157 1.00 40.79  ? 66  VAL A HG21 1 
ATOM   1054 H  HG22 . VAL A 1 69  ? 13.201  -3.824  23.277 1.00 40.79  ? 66  VAL A HG22 1 
ATOM   1055 H  HG23 . VAL A 1 69  ? 13.917  -2.530  22.695 1.00 40.79  ? 66  VAL A HG23 1 
ATOM   1056 N  N    . ASP A 1 70  ? 13.776  -4.417  26.965 1.00 26.86  ? 67  ASP A N    1 
ATOM   1057 C  CA   . ASP A 1 70  ? 12.704  -5.060  27.724 1.00 31.19  ? 67  ASP A CA   1 
ATOM   1058 C  C    . ASP A 1 70  ? 11.850  -4.040  28.468 1.00 28.53  ? 67  ASP A C    1 
ATOM   1059 O  O    . ASP A 1 70  ? 10.623  -4.176  28.506 1.00 26.57  ? 67  ASP A O    1 
ATOM   1060 C  CB   . ASP A 1 70  ? 13.235  -6.102  28.709 1.00 34.31  ? 67  ASP A CB   1 
ATOM   1061 C  CG   . ASP A 1 70  ? 13.943  -7.229  28.026 1.00 47.52  ? 67  ASP A CG   1 
ATOM   1062 O  OD1  . ASP A 1 70  ? 13.382  -7.762  27.067 1.00 41.81  ? 67  ASP A OD1  1 
ATOM   1063 O  OD2  . ASP A 1 70  ? 15.019  -7.638  28.497 1.00 55.63  ? 67  ASP A OD2  1 
ATOM   1064 H  H    . ASP A 1 70  ? 14.575  -4.619  27.210 1.00 32.26  ? 67  ASP A H    1 
ATOM   1065 H  HA   . ASP A 1 70  ? 12.150  -5.528  27.079 1.00 37.46  ? 67  ASP A HA   1 
ATOM   1066 H  HB2  . ASP A 1 70  ? 13.863  -5.675  29.313 1.00 41.20  ? 67  ASP A HB2  1 
ATOM   1067 H  HB3  . ASP A 1 70  ? 12.492  -6.472  29.209 1.00 41.20  ? 67  ASP A HB3  1 
ATOM   1068 N  N    . ASP A 1 71  ? 12.478  -3.027  29.089 1.00 25.36  ? 68  ASP A N    1 
ATOM   1069 C  CA   . ASP A 1 71  ? 11.713  -1.956  29.717 1.00 24.72  ? 68  ASP A CA   1 
ATOM   1070 C  C    . ASP A 1 71  ? 10.846  -1.202  28.705 1.00 22.30  ? 68  ASP A C    1 
ATOM   1071 O  O    . ASP A 1 71  ? 9.685   -0.853  29.003 1.00 24.90  ? 68  ASP A O    1 
ATOM   1072 C  CB   . ASP A 1 71  ? 12.668  -0.980  30.421 1.00 28.84  ? 68  ASP A CB   1 
ATOM   1073 C  CG   . ASP A 1 71  ? 13.533  -1.657  31.467 1.00 35.55  ? 68  ASP A CG   1 
ATOM   1074 O  OD1  . ASP A 1 71  ? 12.920  -2.282  32.328 1.00 32.46  ? 68  ASP A OD1  1 
ATOM   1075 O  OD2  . ASP A 1 71  ? 14.784  -1.608  31.402 1.00 29.87  ? 68  ASP A OD2  1 
ATOM   1076 H  H    . ASP A 1 71  ? 13.331  -2.944  29.156 1.00 30.47  ? 68  ASP A H    1 
ATOM   1077 H  HA   . ASP A 1 71  ? 11.123  -2.349  30.378 1.00 29.70  ? 68  ASP A HA   1 
ATOM   1078 H  HB2  . ASP A 1 71  ? 13.254  -0.579  29.761 1.00 34.65  ? 68  ASP A HB2  1 
ATOM   1079 H  HB3  . ASP A 1 71  ? 12.147  -0.292  30.863 1.00 34.65  ? 68  ASP A HB3  1 
ATOM   1080 N  N    . TRP A 1 72  ? 11.392  -0.915  27.516 1.00 22.68  ? 69  TRP A N    1 
ATOM   1081 C  CA   . TRP A 1 72  ? 10.638  -0.143  26.544 1.00 25.72  ? 69  TRP A CA   1 
ATOM   1082 C  C    . TRP A 1 72  ? 9.428   -0.933  26.046 1.00 22.64  ? 69  TRP A C    1 
ATOM   1083 O  O    . TRP A 1 72  ? 8.321   -0.393  25.949 1.00 24.31  ? 69  TRP A O    1 
ATOM   1084 C  CB   . TRP A 1 72  ? 11.532  0.309   25.384 1.00 24.76  ? 69  TRP A CB   1 
ATOM   1085 C  CG   . TRP A 1 72  ? 12.832  0.905   25.809 1.00 23.90  ? 69  TRP A CG   1 
ATOM   1086 C  CD1  . TRP A 1 72  ? 13.069  1.638   26.963 1.00 25.47  ? 69  TRP A CD1  1 
ATOM   1087 C  CD2  . TRP A 1 72  ? 14.080  0.844   25.107 1.00 25.53  ? 69  TRP A CD2  1 
ATOM   1088 N  NE1  . TRP A 1 72  ? 14.391  2.027   26.992 1.00 27.54  ? 69  TRP A NE1  1 
ATOM   1089 C  CE2  . TRP A 1 72  ? 15.032  1.540   25.884 1.00 28.80  ? 69  TRP A CE2  1 
ATOM   1090 C  CE3  . TRP A 1 72  ? 14.485  0.259   23.905 1.00 30.20  ? 69  TRP A CE3  1 
ATOM   1091 C  CZ2  . TRP A 1 72  ? 16.363  1.663   25.498 1.00 33.25  ? 69  TRP A CZ2  1 
ATOM   1092 C  CZ3  . TRP A 1 72  ? 15.819  0.386   23.524 1.00 31.29  ? 69  TRP A CZ3  1 
ATOM   1093 C  CH2  . TRP A 1 72  ? 16.733  1.080   24.324 1.00 32.46  ? 69  TRP A CH2  1 
ATOM   1094 H  H    . TRP A 1 72  ? 12.178  -1.153  27.261 1.00 27.25  ? 69  TRP A H    1 
ATOM   1095 H  HA   . TRP A 1 72  ? 10.314  0.666   26.970 1.00 30.90  ? 69  TRP A HA   1 
ATOM   1096 H  HB2  . TRP A 1 72  ? 11.730  -0.460  24.827 1.00 29.75  ? 69  TRP A HB2  1 
ATOM   1097 H  HB3  . TRP A 1 72  ? 11.057  0.978   24.868 1.00 29.75  ? 69  TRP A HB3  1 
ATOM   1098 H  HD1  . TRP A 1 72  ? 12.436  1.835   27.615 1.00 30.60  ? 69  TRP A HD1  1 
ATOM   1099 H  HE1  . TRP A 1 72  ? 14.756  2.501   27.610 1.00 33.08  ? 69  TRP A HE1  1 
ATOM   1100 H  HE3  . TRP A 1 72  ? 13.880  -0.204  23.372 1.00 36.28  ? 69  TRP A HE3  1 
ATOM   1101 H  HZ2  . TRP A 1 72  ? 16.976  2.125   26.022 1.00 39.93  ? 69  TRP A HZ2  1 
ATOM   1102 H  HZ3  . TRP A 1 72  ? 16.106  0.003   22.727 1.00 37.58  ? 69  TRP A HZ3  1 
ATOM   1103 H  HH2  . TRP A 1 72  ? 17.618  1.145   24.046 1.00 38.99  ? 69  TRP A HH2  1 
ATOM   1104 N  N    . TRP A 1 73  ? 9.614   -2.219  25.768 1.00 22.71  ? 70  TRP A N    1 
ATOM   1105 C  CA   . TRP A 1 73  ? 8.504   -3.059  25.343 1.00 25.88  ? 70  TRP A CA   1 
ATOM   1106 C  C    . TRP A 1 73  ? 7.455   -3.210  26.441 1.00 24.15  ? 70  TRP A C    1 
ATOM   1107 O  O    . TRP A 1 73  ? 6.256   -3.177  26.156 1.00 26.09  ? 70  TRP A O    1 
ATOM   1108 C  CB   . TRP A 1 73  ? 9.052   -4.415  24.884 1.00 23.70  ? 70  TRP A CB   1 
ATOM   1109 C  CG   . TRP A 1 73  ? 7.994   -5.455  24.679 1.00 24.82  ? 70  TRP A CG   1 
ATOM   1110 C  CD1  . TRP A 1 73  ? 7.902   -6.652  25.316 1.00 27.64  ? 70  TRP A CD1  1 
ATOM   1111 C  CD2  . TRP A 1 73  ? 6.917   -5.426  23.729 1.00 24.01  ? 70  TRP A CD2  1 
ATOM   1112 N  NE1  . TRP A 1 73  ? 6.816   -7.351  24.857 1.00 32.31  ? 70  TRP A NE1  1 
ATOM   1113 C  CE2  . TRP A 1 73  ? 6.184   -6.613  23.894 1.00 25.97  ? 70  TRP A CE2  1 
ATOM   1114 C  CE3  . TRP A 1 73  ? 6.489   -4.497  22.779 1.00 27.72  ? 70  TRP A CE3  1 
ATOM   1115 C  CZ2  . TRP A 1 73  ? 5.073   -6.911  23.130 1.00 30.46  ? 70  TRP A CZ2  1 
ATOM   1116 C  CZ3  . TRP A 1 73  ? 5.351   -4.797  22.036 1.00 27.68  ? 70  TRP A CZ3  1 
ATOM   1117 C  CH2  . TRP A 1 73  ? 4.673   -5.978  22.220 1.00 29.54  ? 70  TRP A CH2  1 
ATOM   1118 H  H    . TRP A 1 73  ? 10.370  -2.627  25.818 1.00 27.29  ? 70  TRP A H    1 
ATOM   1119 H  HA   . TRP A 1 73  ? 8.053   -2.646  24.590 1.00 31.10  ? 70  TRP A HA   1 
ATOM   1120 H  HB2  . TRP A 1 73  ? 9.516   -4.294  24.041 1.00 28.48  ? 70  TRP A HB2  1 
ATOM   1121 H  HB3  . TRP A 1 73  ? 9.666   -4.747  25.557 1.00 28.48  ? 70  TRP A HB3  1 
ATOM   1122 H  HD1  . TRP A 1 73  ? 8.490   -6.954  25.970 1.00 33.20  ? 70  TRP A HD1  1 
ATOM   1123 H  HE1  . TRP A 1 73  ? 6.571   -8.129  25.130 1.00 38.81  ? 70  TRP A HE1  1 
ATOM   1124 H  HE3  . TRP A 1 73  ? 6.951   -3.701  22.647 1.00 33.29  ? 70  TRP A HE3  1 
ATOM   1125 H  HZ2  . TRP A 1 73  ? 4.617   -7.715  23.232 1.00 36.59  ? 70  TRP A HZ2  1 
ATOM   1126 H  HZ3  . TRP A 1 73  ? 5.044   -4.187  21.404 1.00 33.26  ? 70  TRP A HZ3  1 
ATOM   1127 H  HH2  . TRP A 1 73  ? 3.915   -6.147  21.707 1.00 35.48  ? 70  TRP A HH2  1 
ATOM   1128 N  N    . GLU A 1 74  ? 7.865   -3.347  27.712 1.00 21.80  ? 71  GLU A N    1 
ATOM   1129 C  CA   . GLU A 1 74  ? 6.871   -3.470  28.764 1.00 23.07  ? 71  GLU A CA   1 
ATOM   1130 C  C    . GLU A 1 74  ? 5.983   -2.250  28.843 1.00 26.14  ? 71  GLU A C    1 
ATOM   1131 O  O    . GLU A 1 74  ? 4.781   -2.369  29.134 1.00 24.73  ? 71  GLU A O    1 
ATOM   1132 C  CB   . GLU A 1 74  ? 7.556   -3.754  30.104 1.00 28.01  ? 71  GLU A CB   1 
ATOM   1133 C  CG   . GLU A 1 74  ? 7.996   -5.212  30.174 1.00 41.82  ? 71  GLU A CG   1 
ATOM   1134 C  CD   . GLU A 1 74  ? 8.841   -5.508  31.389 1.00 64.29  ? 71  GLU A CD   1 
ATOM   1135 O  OE1  . GLU A 1 74  ? 8.854   -4.667  32.311 1.00 53.11  ? 71  GLU A OE1  1 
ATOM   1136 O  OE2  . GLU A 1 74  ? 9.498   -6.578  31.392 1.00 53.72  ? 71  GLU A OE2  1 
ATOM   1137 H  H    . GLU A 1 74  ? 8.684   -3.371  27.973 1.00 26.19  ? 71  GLU A H    1 
ATOM   1138 H  HA   . GLU A 1 74  ? 6.296   -4.225  28.563 1.00 27.72  ? 71  GLU A HA   1 
ATOM   1139 H  HB2  . GLU A 1 74  ? 8.339   -3.188  30.196 1.00 33.64  ? 71  GLU A HB2  1 
ATOM   1140 H  HB3  . GLU A 1 74  ? 6.935   -3.582  30.829 1.00 33.64  ? 71  GLU A HB3  1 
ATOM   1141 H  HG2  . GLU A 1 74  ? 7.210   -5.778  30.210 1.00 50.22  ? 71  GLU A HG2  1 
ATOM   1142 H  HG3  . GLU A 1 74  ? 8.521   -5.422  29.385 1.00 50.22  ? 71  GLU A HG3  1 
ATOM   1143 N  N    . GLU A 1 75  ? 6.556   -1.064  28.619 1.00 26.37  ? 72  GLU A N    1 
ATOM   1144 C  CA   . GLU A 1 75  ? 5.760   0.157   28.618 1.00 22.61  ? 72  GLU A CA   1 
ATOM   1145 C  C    . GLU A 1 75  ? 4.753   0.173   27.479 1.00 24.72  ? 72  GLU A C    1 
ATOM   1146 O  O    . GLU A 1 75  ? 3.608   0.614   27.662 1.00 24.16  ? 72  GLU A O    1 
ATOM   1147 C  CB   . GLU A 1 75  ? 6.679   1.362   28.535 1.00 27.57  ? 72  GLU A CB   1 
ATOM   1148 C  CG   . GLU A 1 75  ? 5.991   2.729   28.651 1.00 28.33  ? 72  GLU A CG   1 
ATOM   1149 C  CD   . GLU A 1 75  ? 5.469   3.028   30.051 1.00 34.55  ? 72  GLU A CD   1 
ATOM   1150 O  OE1  . GLU A 1 75  ? 5.986   2.444   31.016 1.00 35.17  ? 72  GLU A OE1  1 
ATOM   1151 O  OE2  . GLU A 1 75  ? 4.559   3.866   30.178 1.00 37.14  ? 72  GLU A OE2  1 
ATOM   1152 H  H    A GLU A 1 75  ? 7.394   -0.943  28.467 0.71 31.68  ? 72  GLU A H    1 
ATOM   1153 H  H    B GLU A 1 75  ? 7.394   -0.943  28.467 0.29 31.68  ? 72  GLU A H    1 
ATOM   1154 H  HA   . GLU A 1 75  ? 5.262   0.206   29.449 1.00 27.17  ? 72  GLU A HA   1 
ATOM   1155 H  HB2  . GLU A 1 75  ? 7.325   1.303   29.256 1.00 33.12  ? 72  GLU A HB2  1 
ATOM   1156 H  HB3  . GLU A 1 75  ? 7.134   1.340   27.679 1.00 33.12  ? 72  GLU A HB3  1 
ATOM   1157 H  HG2  . GLU A 1 75  ? 6.628   3.422   28.418 1.00 34.03  ? 72  GLU A HG2  1 
ATOM   1158 H  HG3  . GLU A 1 75  ? 5.237   2.753   28.042 1.00 34.03  ? 72  GLU A HG3  1 
ATOM   1159 N  N    . VAL A 1 76  ? 5.146   -0.340  26.311 1.00 24.76  ? 73  VAL A N    1 
ATOM   1160 C  CA   . VAL A 1 76  ? 4.221   -0.415  25.179 1.00 23.73  ? 73  VAL A CA   1 
ATOM   1161 C  C    . VAL A 1 76  ? 3.097   -1.401  25.474 1.00 23.79  ? 73  VAL A C    1 
ATOM   1162 O  O    . VAL A 1 76  ? 1.924   -1.122  25.205 1.00 26.00  ? 73  VAL A O    1 
ATOM   1163 C  CB   . VAL A 1 76  ? 4.981   -0.800  23.895 1.00 24.48  ? 73  VAL A CB   1 
ATOM   1164 C  CG1  . VAL A 1 76  ? 3.987   -1.035  22.738 1.00 25.89  ? 73  VAL A CG1  1 
ATOM   1165 C  CG2  . VAL A 1 76  ? 5.989   0.298   23.524 1.00 26.65  ? 73  VAL A CG2  1 
ATOM   1166 H  H    . VAL A 1 76  ? 5.932   -0.647  26.149 1.00 29.75  ? 73  VAL A H    1 
ATOM   1167 H  HA   . VAL A 1 76  ? 3.826   0.461   25.047 1.00 28.51  ? 73  VAL A HA   1 
ATOM   1168 H  HB   . VAL A 1 76  ? 5.471   -1.623  24.049 1.00 29.41  ? 73  VAL A HB   1 
ATOM   1169 H  HG11 . VAL A 1 76  ? 4.480   -1.099  21.905 1.00 31.10  ? 73  VAL A HG11 1 
ATOM   1170 H  HG12 . VAL A 1 76  ? 3.503   -1.860  22.900 1.00 31.10  ? 73  VAL A HG12 1 
ATOM   1171 H  HG13 . VAL A 1 76  ? 3.367   -0.290  22.698 1.00 31.10  ? 73  VAL A HG13 1 
ATOM   1172 H  HG21 . VAL A 1 76  ? 6.418   0.064   22.686 1.00 32.01  ? 73  VAL A HG21 1 
ATOM   1173 H  HG22 . VAL A 1 76  ? 5.517   1.141   23.430 1.00 32.01  ? 73  VAL A HG22 1 
ATOM   1174 H  HG23 . VAL A 1 76  ? 6.653   0.368   24.228 1.00 32.01  ? 73  VAL A HG23 1 
ATOM   1175 N  N    . GLU A 1 77  ? 3.423   -2.543  26.097 1.00 24.40  ? 74  GLU A N    1 
ATOM   1176 C  CA   . GLU A 1 77  ? 2.384   -3.472  26.510 1.00 26.12  ? 74  GLU A CA   1 
ATOM   1177 C  C    . GLU A 1 77  ? 1.428   -2.803  27.477 1.00 28.85  ? 74  GLU A C    1 
ATOM   1178 O  O    . GLU A 1 77  ? 0.204   -2.986  27.399 1.00 28.15  ? 74  GLU A O    1 
ATOM   1179 C  CB   . GLU A 1 77  ? 2.977   -4.724  27.146 1.00 27.93  ? 74  GLU A CB   1 
ATOM   1180 C  CG   . GLU A 1 77  ? 3.397   -5.775  26.160 1.00 35.30  ? 74  GLU A CG   1 
ATOM   1181 C  CD   . GLU A 1 77  ? 4.069   -6.956  26.832 1.00 40.61  ? 74  GLU A CD   1 
ATOM   1182 O  OE1  . GLU A 1 77  ? 4.786   -6.778  27.832 1.00 47.50  ? 74  GLU A OE1  1 
ATOM   1183 O  OE2  . GLU A 1 77  ? 3.842   -8.059  26.380 1.00 40.63  ? 74  GLU A OE2  1 
ATOM   1184 H  H    . GLU A 1 77  ? 4.225   -2.792  26.285 1.00 29.32  ? 74  GLU A H    1 
ATOM   1185 H  HA   . GLU A 1 77  ? 1.899   -3.753  25.719 1.00 31.38  ? 74  GLU A HA   1 
ATOM   1186 H  HB2  . GLU A 1 77  ? 3.761   -4.470  27.658 1.00 33.55  ? 74  GLU A HB2  1 
ATOM   1187 H  HB3  . GLU A 1 77  ? 2.312   -5.119  27.732 1.00 33.55  ? 74  GLU A HB3  1 
ATOM   1188 H  HG2  . GLU A 1 77  ? 2.614   -6.101  25.689 1.00 42.39  ? 74  GLU A HG2  1 
ATOM   1189 H  HG3  . GLU A 1 77  ? 4.026   -5.388  25.531 1.00 42.39  ? 74  GLU A HG3  1 
ATOM   1190 N  N    A LYS A 1 78  ? 1.964   -2.032  28.419 0.49 24.89  ? 75  LYS A N    1 
ATOM   1191 N  N    B LYS A 1 78  ? 1.979   -2.041  28.423 0.51 24.89  ? 75  LYS A N    1 
ATOM   1192 C  CA   A LYS A 1 78  ? 1.100   -1.402  29.406 0.49 26.97  ? 75  LYS A CA   1 
ATOM   1193 C  CA   B LYS A 1 78  ? 1.159   -1.360  29.415 0.51 26.99  ? 75  LYS A CA   1 
ATOM   1194 C  C    A LYS A 1 78  ? 0.206   -0.346  28.771 0.49 27.18  ? 75  LYS A C    1 
ATOM   1195 C  C    B LYS A 1 78  ? 0.215   -0.366  28.757 0.51 27.18  ? 75  LYS A C    1 
ATOM   1196 O  O    A LYS A 1 78  ? -0.939  -0.166  29.214 0.49 28.70  ? 75  LYS A O    1 
ATOM   1197 O  O    B LYS A 1 78  ? -0.950  -0.241  29.168 0.51 28.66  ? 75  LYS A O    1 
ATOM   1198 C  CB   A LYS A 1 78  ? 1.934   -0.788  30.529 0.49 30.83  ? 75  LYS A CB   1 
ATOM   1199 C  CB   B LYS A 1 78  ? 2.063   -0.651  30.429 0.51 30.84  ? 75  LYS A CB   1 
ATOM   1200 C  CG   A LYS A 1 78  ? 2.500   -1.803  31.512 0.49 31.99  ? 75  LYS A CG   1 
ATOM   1201 C  CG   B LYS A 1 78  ? 1.325   0.092   31.522 0.51 35.22  ? 75  LYS A CG   1 
ATOM   1202 C  CD   A LYS A 1 78  ? 3.697   -1.234  32.243 0.49 42.59  ? 75  LYS A CD   1 
ATOM   1203 C  CD   B LYS A 1 78  ? 2.296   0.888   32.417 0.51 40.50  ? 75  LYS A CD   1 
ATOM   1204 C  CE   A LYS A 1 78  ? 3.321   -0.002  33.036 0.49 45.99  ? 75  LYS A CE   1 
ATOM   1205 C  CE   B LYS A 1 78  ? 1.560   1.595   33.537 0.51 48.30  ? 75  LYS A CE   1 
ATOM   1206 N  NZ   A LYS A 1 78  ? 4.449   0.460   33.894 0.49 58.04  ? 75  LYS A NZ   1 
ATOM   1207 N  NZ   B LYS A 1 78  ? 2.516   2.320   34.415 0.51 62.53  ? 75  LYS A NZ   1 
ATOM   1208 H  H    A LYS A 1 78  ? 2.803   -1.863  28.505 0.49 29.90  ? 75  LYS A H    1 
ATOM   1209 H  H    B LYS A 1 78  ? 2.824   -1.905  28.510 0.51 29.91  ? 75  LYS A H    1 
ATOM   1210 H  HA   A LYS A 1 78  ? 0.530   -2.081  29.800 0.49 32.40  ? 75  LYS A HA   1 
ATOM   1211 H  HA   B LYS A 1 78  ? 0.622   -2.014  29.889 0.51 32.43  ? 75  LYS A HA   1 
ATOM   1212 H  HB2  A LYS A 1 78  ? 2.682   -0.311  30.135 0.49 37.03  ? 75  LYS A HB2  1 
ATOM   1213 H  HB2  B LYS A 1 78  ? 2.627   -1.315  30.855 0.51 37.04  ? 75  LYS A HB2  1 
ATOM   1214 H  HB3  A LYS A 1 78  ? 1.376   -0.173  31.030 0.49 37.03  ? 75  LYS A HB3  1 
ATOM   1215 H  HB3  B LYS A 1 78  ? 2.611   -0.006  29.955 0.51 37.04  ? 75  LYS A HB3  1 
ATOM   1216 H  HG2  A LYS A 1 78  ? 1.821   -2.034  32.165 0.49 38.43  ? 75  LYS A HG2  1 
ATOM   1217 H  HG2  B LYS A 1 78  ? 0.699   0.715   31.122 0.51 42.30  ? 75  LYS A HG2  1 
ATOM   1218 H  HG3  A LYS A 1 78  ? 2.782   -2.597  31.031 0.49 38.43  ? 75  LYS A HG3  1 
ATOM   1219 H  HG3  B LYS A 1 78  ? 0.849   -0.544  32.079 0.51 42.30  ? 75  LYS A HG3  1 
ATOM   1220 H  HD2  A LYS A 1 78  ? 4.044   -1.899  32.858 0.49 51.15  ? 75  LYS A HD2  1 
ATOM   1221 H  HD2  B LYS A 1 78  ? 2.941   0.281   32.811 0.51 48.64  ? 75  LYS A HD2  1 
ATOM   1222 H  HD3  A LYS A 1 78  ? 4.380   -0.988  31.600 0.49 51.15  ? 75  LYS A HD3  1 
ATOM   1223 H  HD3  B LYS A 1 78  ? 2.752   1.556   31.882 0.51 48.64  ? 75  LYS A HD3  1 
ATOM   1224 H  HE2  A LYS A 1 78  ? 3.089   0.715   32.425 0.49 55.22  ? 75  LYS A HE2  1 
ATOM   1225 H  HE2  B LYS A 1 78  ? 0.937   2.237   33.162 0.51 57.99  ? 75  LYS A HE2  1 
ATOM   1226 H  HE3  A LYS A 1 78  ? 2.565   -0.206  33.609 0.49 55.22  ? 75  LYS A HE3  1 
ATOM   1227 H  HE3  B LYS A 1 78  ? 1.082   0.943   34.074 0.51 57.99  ? 75  LYS A HE3  1 
ATOM   1228 H  HZ1  A LYS A 1 78  ? 4.195   1.162   34.379 0.49 69.68  ? 75  LYS A HZ1  1 
ATOM   1229 H  HZ1  B LYS A 1 78  ? 2.076   2.737   35.066 0.51 75.08  ? 75  LYS A HZ1  1 
ATOM   1230 H  HZ2  A LYS A 1 78  ? 4.702   -0.194  34.442 0.49 69.68  ? 75  LYS A HZ2  1 
ATOM   1231 H  HZ2  B LYS A 1 78  ? 3.092   1.746   34.777 0.51 75.08  ? 75  LYS A HZ2  1 
ATOM   1232 H  HZ3  A LYS A 1 78  ? 5.141   0.696   33.386 0.49 69.68  ? 75  LYS A HZ3  1 
ATOM   1233 H  HZ3  B LYS A 1 78  ? 2.968   2.922   33.941 0.51 75.08  ? 75  LYS A HZ3  1 
ATOM   1234 N  N    . ALA A 1 79  ? 0.706   0.338   27.730 1.00 25.58  ? 76  ALA A N    1 
ATOM   1235 C  CA   . ALA A 1 79  ? -0.095  1.333   27.018 1.00 27.17  ? 76  ALA A CA   1 
ATOM   1236 C  C    . ALA A 1 79  ? -1.245  0.673   26.257 1.00 26.75  ? 76  ALA A C    1 
ATOM   1237 O  O    . ALA A 1 79  ? -2.376  1.170   26.244 1.00 25.75  ? 76  ALA A O    1 
ATOM   1238 C  CB   . ALA A 1 79  ? 0.802   2.109   26.059 1.00 25.87  ? 76  ALA A CB   1 
ATOM   1239 H  H    A ALA A 1 79  ? 1.502   0.244   27.421 0.49 30.74  ? 76  ALA A H    1 
ATOM   1240 H  H    B ALA A 1 79  ? 1.506   0.258   27.425 0.51 30.74  ? 76  ALA A H    1 
ATOM   1241 H  HA   . ALA A 1 79  ? -0.478  1.955   27.657 1.00 32.64  ? 76  ALA A HA   1 
ATOM   1242 H  HB1  . ALA A 1 79  ? 0.269   2.772   25.593 1.00 31.08  ? 76  ALA A HB1  1 
ATOM   1243 H  HB2  . ALA A 1 79  ? 1.503   2.547   26.568 1.00 31.08  ? 76  ALA A HB2  1 
ATOM   1244 H  HB3  . ALA A 1 79  ? 1.193   1.491   25.422 1.00 31.08  ? 76  ALA A HB3  1 
ATOM   1245 N  N    . TYR A 1 80  ? -0.975  -0.452  25.608 1.00 25.89  ? 77  TYR A N    1 
ATOM   1246 C  CA   . TYR A 1 80  ? -2.056  -1.223  24.994 1.00 24.89  ? 77  TYR A CA   1 
ATOM   1247 C  C    . TYR A 1 80  ? -3.115  -1.621  26.007 1.00 28.32  ? 77  TYR A C    1 
ATOM   1248 O  O    . TYR A 1 80  ? -4.325  -1.469  25.750 1.00 28.25  ? 77  TYR A O    1 
ATOM   1249 C  CB   . TYR A 1 80  ? -1.461  -2.455  24.292 1.00 25.19  ? 77  TYR A CB   1 
ATOM   1250 C  CG   . TYR A 1 80  ? -2.533  -3.303  23.651 1.00 28.09  ? 77  TYR A CG   1 
ATOM   1251 C  CD1  . TYR A 1 80  ? -2.970  -3.025  22.359 1.00 26.13  ? 77  TYR A CD1  1 
ATOM   1252 C  CD2  . TYR A 1 80  ? -3.123  -4.329  24.313 1.00 30.45  ? 77  TYR A CD2  1 
ATOM   1253 C  CE1  . TYR A 1 80  ? -3.992  -3.788  21.793 1.00 26.23  ? 77  TYR A CE1  1 
ATOM   1254 C  CE2  . TYR A 1 80  ? -4.141  -5.070  23.735 1.00 29.77  ? 77  TYR A CE2  1 
ATOM   1255 C  CZ   . TYR A 1 80  ? -4.549  -4.800  22.473 1.00 30.89  ? 77  TYR A CZ   1 
ATOM   1256 O  OH   . TYR A 1 80  ? -5.570  -5.576  21.924 1.00 34.60  ? 77  TYR A OH   1 
ATOM   1257 H  H    . TYR A 1 80  ? -0.190  -0.788  25.507 1.00 31.10  ? 77  TYR A H    1 
ATOM   1258 H  HA   . TYR A 1 80  ? -2.500  -0.674  24.329 1.00 29.90  ? 77  TYR A HA   1 
ATOM   1259 H  HB2  . TYR A 1 80  ? -0.847  -2.164  23.600 1.00 30.26  ? 77  TYR A HB2  1 
ATOM   1260 H  HB3  . TYR A 1 80  ? -0.991  -2.999  24.944 1.00 30.26  ? 77  TYR A HB3  1 
ATOM   1261 H  HD1  . TYR A 1 80  ? -2.582  -2.332  21.875 1.00 31.39  ? 77  TYR A HD1  1 
ATOM   1262 H  HD2  . TYR A 1 80  ? -2.838  -4.539  25.173 1.00 36.58  ? 77  TYR A HD2  1 
ATOM   1263 H  HE1  . TYR A 1 80  ? -4.290  -3.591  20.934 1.00 31.51  ? 77  TYR A HE1  1 
ATOM   1264 H  HE2  . TYR A 1 80  ? -4.546  -5.756  24.215 1.00 35.76  ? 77  TYR A HE2  1 
ATOM   1265 H  HH   . TYR A 1 80  ? -5.860  -6.117  22.497 1.00 41.55  ? 77  TYR A HH   1 
ATOM   1266 N  N    A GLN A 1 81  ? -2.688  -2.124  27.176 0.44 26.55  ? 78  GLN A N    1 
ATOM   1267 N  N    B GLN A 1 81  ? -2.688  -2.144  27.175 0.56 26.53  ? 78  GLN A N    1 
ATOM   1268 C  CA   A GLN A 1 81  ? -3.643  -2.595  28.166 0.44 29.56  ? 78  GLN A CA   1 
ATOM   1269 C  CA   B GLN A 1 81  ? -3.642  -2.586  28.186 0.56 29.55  ? 78  GLN A CA   1 
ATOM   1270 C  C    A GLN A 1 81  ? -4.422  -1.432  28.775 0.44 30.21  ? 78  GLN A C    1 
ATOM   1271 C  C    B GLN A 1 81  ? -4.449  -1.406  28.713 0.56 30.14  ? 78  GLN A C    1 
ATOM   1272 O  O    A GLN A 1 81  ? -5.580  -1.605  29.169 0.44 31.72  ? 78  GLN A O    1 
ATOM   1273 O  O    B GLN A 1 81  ? -5.647  -1.532  28.984 0.56 31.32  ? 78  GLN A O    1 
ATOM   1274 C  CB   A GLN A 1 81  ? -2.919  -3.375  29.261 0.44 30.85  ? 78  GLN A CB   1 
ATOM   1275 C  CB   B GLN A 1 81  ? -2.913  -3.276  29.341 0.56 30.78  ? 78  GLN A CB   1 
ATOM   1276 C  CG   A GLN A 1 81  ? -2.397  -4.760  28.868 0.44 34.09  ? 78  GLN A CG   1 
ATOM   1277 C  CG   B GLN A 1 81  ? -3.805  -4.013  30.393 0.56 36.04  ? 78  GLN A CG   1 
ATOM   1278 C  CD   A GLN A 1 81  ? -3.467  -5.708  28.342 0.44 37.25  ? 78  GLN A CD   1 
ATOM   1279 C  CD   B GLN A 1 81  ? -4.783  -5.018  29.780 0.56 43.33  ? 78  GLN A CD   1 
ATOM   1280 O  OE1  A GLN A 1 81  ? -3.204  -6.527  27.468 0.44 37.43  ? 78  GLN A OE1  1 
ATOM   1281 O  OE1  B GLN A 1 81  ? -4.429  -5.757  28.859 0.56 50.04  ? 78  GLN A OE1  1 
ATOM   1282 N  NE2  A GLN A 1 81  ? -4.673  -5.616  28.900 0.44 48.95  ? 78  GLN A NE2  1 
ATOM   1283 N  NE2  B GLN A 1 81  ? -6.003  -5.075  30.316 0.56 41.78  ? 78  GLN A NE2  1 
ATOM   1284 H  H    A GLN A 1 81  ? -1.864  -2.199  27.409 0.44 31.90  ? 78  GLN A H    1 
ATOM   1285 H  H    B GLN A 1 81  ? -1.863  -2.248  27.395 0.56 31.88  ? 78  GLN A H    1 
ATOM   1286 H  HA   A GLN A 1 81  ? -4.273  -3.196  27.739 0.44 35.50  ? 78  GLN A HA   1 
ATOM   1287 H  HA   B GLN A 1 81  ? -4.247  -3.229  27.785 0.56 35.49  ? 78  GLN A HA   1 
ATOM   1288 H  HB2  A GLN A 1 81  ? -2.154  -2.852  29.549 0.44 37.06  ? 78  GLN A HB2  1 
ATOM   1289 H  HB2  B GLN A 1 81  ? -2.312  -3.938  28.965 0.56 36.97  ? 78  GLN A HB2  1 
ATOM   1290 H  HB3  A GLN A 1 81  ? -3.533  -3.500  30.001 0.44 37.06  ? 78  GLN A HB3  1 
ATOM   1291 H  HB3  B GLN A 1 81  ? -2.406  -2.603  29.822 0.56 36.97  ? 78  GLN A HB3  1 
ATOM   1292 H  HG2  A GLN A 1 81  ? -1.731  -4.654  28.171 0.44 40.95  ? 78  GLN A HG2  1 
ATOM   1293 H  HG2  B GLN A 1 81  ? -3.229  -4.498  31.005 0.56 43.28  ? 78  GLN A HG2  1 
ATOM   1294 H  HG3  A GLN A 1 81  ? -1.998  -5.173  29.649 0.44 40.95  ? 78  GLN A HG3  1 
ATOM   1295 H  HG3  B GLN A 1 81  ? -4.324  -3.354  30.879 0.56 43.28  ? 78  GLN A HG3  1 
ATOM   1296 H  HE21 A GLN A 1 81  ? -4.815  -5.042  29.525 0.44 58.78  ? 78  GLN A HE21 1 
ATOM   1297 H  HE21 B GLN A 1 81  ? -6.207  -4.562  30.976 0.56 50.17  ? 78  GLN A HE21 1 
ATOM   1298 H  HE22 A GLN A 1 81  ? -5.309  -6.131  28.636 0.44 58.78  ? 78  GLN A HE22 1 
ATOM   1299 H  HE22 B GLN A 1 81  ? -6.585  -5.625  30.003 0.56 50.17  ? 78  GLN A HE22 1 
ATOM   1300 N  N    . PHE A 1 82  ? -3.804  -0.253  28.867 1.00 29.73  ? 79  PHE A N    1 
ATOM   1301 C  CA   . PHE A 1 82  ? -4.530  0.947   29.277 1.00 30.67  ? 79  PHE A CA   1 
ATOM   1302 C  C    . PHE A 1 82  ? -5.729  1.210   28.359 1.00 28.50  ? 79  PHE A C    1 
ATOM   1303 O  O    . PHE A 1 82  ? -6.845  1.449   28.830 1.00 30.48  ? 79  PHE A O    1 
ATOM   1304 C  CB   . PHE A 1 82  ? -3.582  2.158   29.295 1.00 31.86  ? 79  PHE A CB   1 
ATOM   1305 C  CG   . PHE A 1 82  ? -4.302  3.462   29.550 1.00 31.95  ? 79  PHE A CG   1 
ATOM   1306 C  CD1  . PHE A 1 82  ? -4.691  3.798   30.832 1.00 38.51  ? 79  PHE A CD1  1 
ATOM   1307 C  CD2  . PHE A 1 82  ? -4.581  4.333   28.516 1.00 31.10  ? 79  PHE A CD2  1 
ATOM   1308 C  CE1  . PHE A 1 82  ? -5.371  4.972   31.071 1.00 37.64  ? 79  PHE A CE1  1 
ATOM   1309 C  CE2  . PHE A 1 82  ? -5.253  5.514   28.743 1.00 36.43  ? 79  PHE A CE2  1 
ATOM   1310 C  CZ   . PHE A 1 82  ? -5.639  5.838   30.014 1.00 36.71  ? 79  PHE A CZ   1 
ATOM   1311 H  H    A PHE A 1 82  ? -2.970  -0.123  28.698 0.44 35.71  ? 79  PHE A H    1 
ATOM   1312 H  H    B PHE A 1 82  ? -2.960  -0.140  28.742 0.56 35.71  ? 79  PHE A H    1 
ATOM   1313 H  HA   . PHE A 1 82  ? -4.865  0.815   30.177 1.00 36.83  ? 79  PHE A HA   1 
ATOM   1314 H  HB2  . PHE A 1 82  ? -2.926  2.034   29.999 1.00 38.26  ? 79  PHE A HB2  1 
ATOM   1315 H  HB3  . PHE A 1 82  ? -3.138  2.223   28.435 1.00 38.26  ? 79  PHE A HB3  1 
ATOM   1316 H  HD1  . PHE A 1 82  ? -4.493  3.227   31.539 1.00 46.24  ? 79  PHE A HD1  1 
ATOM   1317 H  HD2  . PHE A 1 82  ? -4.311  4.120   27.652 1.00 37.36  ? 79  PHE A HD2  1 
ATOM   1318 H  HE1  . PHE A 1 82  ? -5.649  5.185   31.933 1.00 45.20  ? 79  PHE A HE1  1 
ATOM   1319 H  HE2  . PHE A 1 82  ? -5.443  6.087   28.036 1.00 43.75  ? 79  PHE A HE2  1 
ATOM   1320 H  HZ   . PHE A 1 82  ? -6.083  6.640   30.174 1.00 44.08  ? 79  PHE A HZ   1 
ATOM   1321 N  N    . LEU A 1 83  ? -5.525  1.108   27.037 1.00 27.17  ? 80  LEU A N    1 
ATOM   1322 C  CA   . LEU A 1 83  ? -6.615  1.350   26.098 1.00 27.04  ? 80  LEU A CA   1 
ATOM   1323 C  C    . LEU A 1 83  ? -7.676  0.278   26.190 1.00 28.97  ? 80  LEU A C    1 
ATOM   1324 O  O    . LEU A 1 83  ? -8.865  0.574   26.098 1.00 29.18  ? 80  LEU A O    1 
ATOM   1325 C  CB   . LEU A 1 83  ? -6.075  1.463   24.671 1.00 26.70  ? 80  LEU A CB   1 
ATOM   1326 C  CG   . LEU A 1 83  ? -5.205  2.699   24.406 1.00 26.24  ? 80  LEU A CG   1 
ATOM   1327 C  CD1  . LEU A 1 83  ? -4.631  2.600   23.001 1.00 26.26  ? 80  LEU A CD1  1 
ATOM   1328 C  CD2  . LEU A 1 83  ? -5.992  4.003   24.624 1.00 30.20  ? 80  LEU A CD2  1 
ATOM   1329 H  H    . LEU A 1 83  ? -4.776  0.902   26.669 1.00 32.64  ? 80  LEU A H    1 
ATOM   1330 H  HA   . LEU A 1 83  ? -7.030  2.198   26.322 1.00 32.49  ? 80  LEU A HA   1 
ATOM   1331 H  HB2  . LEU A 1 83  ? -5.534  0.679   24.485 1.00 32.07  ? 80  LEU A HB2  1 
ATOM   1332 H  HB3  . LEU A 1 83  ? -6.828  1.499   24.060 1.00 32.07  ? 80  LEU A HB3  1 
ATOM   1333 H  HG   . LEU A 1 83  ? -4.470  2.731   25.039 1.00 31.52  ? 80  LEU A HG   1 
ATOM   1334 H  HD11 . LEU A 1 83  ? -4.065  3.371   22.836 1.00 31.54  ? 80  LEU A HD11 1 
ATOM   1335 H  HD12 . LEU A 1 83  ? -4.110  1.786   22.929 1.00 31.54  ? 80  LEU A HD12 1 
ATOM   1336 H  HD13 . LEU A 1 83  ? -5.361  2.583   22.362 1.00 31.54  ? 80  LEU A HD13 1 
ATOM   1337 H  HD21 . LEU A 1 83  ? -5.485  4.743   24.254 1.00 36.28  ? 80  LEU A HD21 1 
ATOM   1338 H  HD22 . LEU A 1 83  ? -6.849  3.933   24.176 1.00 36.28  ? 80  LEU A HD22 1 
ATOM   1339 H  HD23 . LEU A 1 83  ? -6.125  4.137   25.575 1.00 36.28  ? 80  LEU A HD23 1 
ATOM   1340 N  N    . VAL A 1 84  ? -7.275  -0.985  26.356 1.00 26.76  ? 81  VAL A N    1 
ATOM   1341 C  CA   . VAL A 1 84  ? -8.257  -2.033  26.584 1.00 28.97  ? 81  VAL A CA   1 
ATOM   1342 C  C    . VAL A 1 84  ? -9.094  -1.722  27.814 1.00 31.48  ? 81  VAL A C    1 
ATOM   1343 O  O    . VAL A 1 84  ? -10.324 -1.870  27.816 1.00 33.48  ? 81  VAL A O    1 
ATOM   1344 C  CB   . VAL A 1 84  ? -7.561  -3.401  26.709 1.00 31.49  ? 81  VAL A CB   1 
ATOM   1345 C  CG1  . VAL A 1 84  ? -8.591  -4.433  27.162 1.00 37.43  ? 81  VAL A CG1  1 
ATOM   1346 C  CG2  . VAL A 1 84  ? -6.960  -3.809  25.396 1.00 34.03  ? 81  VAL A CG2  1 
ATOM   1347 H  H    . VAL A 1 84  ? -6.457  -1.250  26.342 1.00 32.15  ? 81  VAL A H    1 
ATOM   1348 H  HA   . VAL A 1 84  ? -8.853  -2.066  25.819 1.00 34.80  ? 81  VAL A HA   1 
ATOM   1349 H  HB   . VAL A 1 84  ? -6.844  -3.348  27.360 1.00 37.82  ? 81  VAL A HB   1 
ATOM   1350 H  HG11 . VAL A 1 84  ? -8.238  -5.323  27.004 1.00 44.96  ? 81  VAL A HG11 1 
ATOM   1351 H  HG12 . VAL A 1 84  ? -8.767  -4.311  28.108 1.00 44.96  ? 81  VAL A HG12 1 
ATOM   1352 H  HG13 . VAL A 1 84  ? -9.409  -4.307  26.655 1.00 44.96  ? 81  VAL A HG13 1 
ATOM   1353 H  HG21 . VAL A 1 84  ? -6.545  -4.680  25.496 1.00 40.86  ? 81  VAL A HG21 1 
ATOM   1354 H  HG22 . VAL A 1 84  ? -7.661  -3.852  24.728 1.00 40.86  ? 81  VAL A HG22 1 
ATOM   1355 H  HG23 . VAL A 1 84  ? -6.294  -3.153  25.136 1.00 40.86  ? 81  VAL A HG23 1 
ATOM   1356 N  N    . ASN A 1 85  ? -8.436  -1.316  28.896 1.00 34.14  ? 82  ASN A N    1 
ATOM   1357 C  CA   . ASN A 1 85  ? -9.159  -1.056  30.128 1.00 34.92  ? 82  ASN A CA   1 
ATOM   1358 C  C    . ASN A 1 85  ? -10.064 0.166   30.008 1.00 36.83  ? 82  ASN A C    1 
ATOM   1359 O  O    . ASN A 1 85  ? -11.058 0.249   30.720 1.00 40.38  ? 82  ASN A O    1 
ATOM   1360 C  CB   . ASN A 1 85  ? -8.172  -0.880  31.285 1.00 37.66  ? 82  ASN A CB   1 
ATOM   1361 C  CG   . ASN A 1 85  ? -7.499  -2.203  31.697 1.00 50.96  ? 82  ASN A CG   1 
ATOM   1362 O  OD1  . ASN A 1 85  ? -7.991  -3.292  31.395 1.00 49.95  ? 82  ASN A OD1  1 
ATOM   1363 N  ND2  . ASN A 1 85  ? -6.384  -2.097  32.407 1.00 54.09  ? 82  ASN A ND2  1 
ATOM   1364 H  H    . ASN A 1 85  ? -7.587  -1.188  28.939 1.00 41.00  ? 82  ASN A H    1 
ATOM   1365 H  HA   . ASN A 1 85  ? -9.722  -1.820  30.326 1.00 41.94  ? 82  ASN A HA   1 
ATOM   1366 H  HB2  . ASN A 1 85  ? -7.476  -0.261  31.016 1.00 45.23  ? 82  ASN A HB2  1 
ATOM   1367 H  HB3  . ASN A 1 85  ? -8.647  -0.532  32.056 1.00 45.23  ? 82  ASN A HB3  1 
ATOM   1368 H  HD21 . ASN A 1 85  ? -5.968  -2.805  32.663 1.00 64.95  ? 82  ASN A HD21 1 
ATOM   1369 H  HD22 . ASN A 1 85  ? -6.076  -1.320  32.611 1.00 64.95  ? 82  ASN A HD22 1 
ATOM   1370 N  N    . GLU A 1 86  ? -9.733  1.126   29.141 1.00 35.13  ? 83  GLU A N    1 
ATOM   1371 C  CA   . GLU A 1 86  ? -10.603 2.273   28.891 1.00 36.63  ? 83  GLU A CA   1 
ATOM   1372 C  C    . GLU A 1 86  ? -11.844 1.890   28.104 1.00 38.23  ? 83  GLU A C    1 
ATOM   1373 O  O    . GLU A 1 86  ? -12.765 2.701   28.009 1.00 42.77  ? 83  GLU A O    1 
ATOM   1374 C  CB   . GLU A 1 86  ? -9.824  3.351   28.142 1.00 38.31  ? 83  GLU A CB   1 
ATOM   1375 C  CG   . GLU A 1 86  ? -8.855  4.164   29.002 1.00 39.79  ? 83  GLU A CG   1 
ATOM   1376 C  CD   . GLU A 1 86  ? -9.569  4.912   30.092 1.00 48.45  ? 83  GLU A CD   1 
ATOM   1377 O  OE1  . GLU A 1 86  ? -10.269 5.864   29.729 1.00 58.44  ? 83  GLU A OE1  1 
ATOM   1378 O  OE2  . GLU A 1 86  ? -9.440  4.551   31.279 1.00 50.80  ? 83  GLU A OE2  1 
ATOM   1379 H  H    . GLU A 1 86  ? -9.005  1.136   28.683 1.00 42.19  ? 83  GLU A H    1 
ATOM   1380 H  HA   . GLU A 1 86  ? -10.892 2.648   29.738 1.00 43.99  ? 83  GLU A HA   1 
ATOM   1381 H  HB2  . GLU A 1 86  ? -9.305  2.924   27.443 1.00 46.00  ? 83  GLU A HB2  1 
ATOM   1382 H  HB3  . GLU A 1 86  ? -10.459 3.973   27.752 1.00 46.00  ? 83  GLU A HB3  1 
ATOM   1383 H  HG2  . GLU A 1 86  ? -8.213  3.564   29.414 1.00 47.78  ? 83  GLU A HG2  1 
ATOM   1384 H  HG3  . GLU A 1 86  ? -8.394  4.808   28.442 1.00 47.78  ? 83  GLU A HG3  1 
ATOM   1385 N  N    . GLY A 1 87  ? -11.915 0.680   27.557 1.00 36.69  ? 84  GLY A N    1 
ATOM   1386 C  CA   . GLY A 1 87  ? -13.113 0.214   26.895 1.00 36.13  ? 84  GLY A CA   1 
ATOM   1387 C  C    . GLY A 1 87  ? -13.069 0.223   25.395 1.00 33.72  ? 84  GLY A C    1 
ATOM   1388 O  O    . GLY A 1 87  ? -14.098 -0.046  24.765 1.00 37.34  ? 84  GLY A O    1 
ATOM   1389 H  H    . GLY A 1 87  ? -11.272 0.109   27.560 1.00 44.07  ? 84  GLY A H    1 
ATOM   1390 H  HA2  . GLY A 1 87  ? -13.286 -0.697  27.178 1.00 43.40  ? 84  GLY A HA2  1 
ATOM   1391 H  HA3  . GLY A 1 87  ? -13.854 0.776   27.170 1.00 43.40  ? 84  GLY A HA3  1 
ATOM   1392 N  N    . TYR A 1 88  ? -11.919 0.509   24.800 1.00 33.25  ? 85  TYR A N    1 
ATOM   1393 C  CA   . TYR A 1 88  ? -11.830 0.544   23.356 1.00 28.68  ? 85  TYR A CA   1 
ATOM   1394 C  C    . TYR A 1 88  ? -11.796 -0.878  22.805 1.00 41.13  ? 85  TYR A C    1 
ATOM   1395 O  O    . TYR A 1 88  ? -10.962 -1.700  23.212 1.00 38.29  ? 85  TYR A O    1 
ATOM   1396 C  CB   . TYR A 1 88  ? -10.587 1.291   22.873 1.00 32.88  ? 85  TYR A CB   1 
ATOM   1397 C  CG   . TYR A 1 88  ? -10.642 2.757   23.236 1.00 29.16  ? 85  TYR A CG   1 
ATOM   1398 C  CD1  . TYR A 1 88  ? -11.424 3.641   22.506 1.00 33.96  ? 85  TYR A CD1  1 
ATOM   1399 C  CD2  . TYR A 1 88  ? -9.936  3.242   24.322 1.00 33.30  ? 85  TYR A CD2  1 
ATOM   1400 C  CE1  . TYR A 1 88  ? -11.500 4.967   22.848 1.00 32.99  ? 85  TYR A CE1  1 
ATOM   1401 C  CE2  . TYR A 1 88  ? -9.986  4.562   24.651 1.00 31.11  ? 85  TYR A CE2  1 
ATOM   1402 C  CZ   . TYR A 1 88  ? -10.772 5.422   23.916 1.00 32.92  ? 85  TYR A CZ   1 
ATOM   1403 O  OH   . TYR A 1 88  ? -10.806 6.747   24.286 1.00 33.93  ? 85  TYR A OH   1 
ATOM   1404 H  H    . TYR A 1 88  ? -11.184 0.684   25.210 1.00 39.93  ? 85  TYR A H    1 
ATOM   1405 H  HA   . TYR A 1 88  ? -12.610 1.014   23.021 1.00 34.45  ? 85  TYR A HA   1 
ATOM   1406 H  HB2  . TYR A 1 88  ? -9.800  0.904   23.287 1.00 39.49  ? 85  TYR A HB2  1 
ATOM   1407 H  HB3  . TYR A 1 88  ? -10.525 1.218   21.908 1.00 39.49  ? 85  TYR A HB3  1 
ATOM   1408 H  HD1  . TYR A 1 88  ? -11.904 3.330   21.774 1.00 40.79  ? 85  TYR A HD1  1 
ATOM   1409 H  HD2  . TYR A 1 88  ? -9.421  2.659   24.832 1.00 39.99  ? 85  TYR A HD2  1 
ATOM   1410 H  HE1  . TYR A 1 88  ? -12.037 5.549   22.362 1.00 39.62  ? 85  TYR A HE1  1 
ATOM   1411 H  HE2  . TYR A 1 88  ? -9.492  4.882   25.371 1.00 37.37  ? 85  TYR A HE2  1 
ATOM   1412 H  HH   . TYR A 1 88  ? -10.290 6.877   24.936 1.00 40.75  ? 85  TYR A HH   1 
ATOM   1413 N  N    . GLU A 1 89  ? -12.721 -1.158  21.891 1.00 37.75  ? 86  GLU A N    1 
ATOM   1414 C  CA   . GLU A 1 89  ? -12.764 -2.424  21.160 1.00 36.84  ? 86  GLU A CA   1 
ATOM   1415 C  C    . GLU A 1 89  ? -11.990 -2.353  19.853 1.00 38.51  ? 86  GLU A C    1 
ATOM   1416 O  O    . GLU A 1 89  ? -11.651 -3.397  19.282 1.00 42.77  ? 86  GLU A O    1 
ATOM   1417 C  CB   . GLU A 1 89  ? -14.237 -2.793  20.905 1.00 46.28  ? 86  GLU A CB   1 
ATOM   1418 C  CG   . GLU A 1 89  ? -14.908 -3.352  22.183 1.00 63.20  ? 86  GLU A CG   1 
ATOM   1419 C  CD   . GLU A 1 89  ? -16.285 -2.758  22.485 1.00 87.36  ? 86  GLU A CD   1 
ATOM   1420 O  OE1  . GLU A 1 89  ? -17.211 -2.920  21.661 1.00 90.31  ? 86  GLU A OE1  1 
ATOM   1421 O  OE2  . GLU A 1 89  ? -16.438 -2.138  23.568 1.00 86.17  ? 86  GLU A OE2  1 
ATOM   1422 H  H    . GLU A 1 89  ? -13.352 -0.618  21.669 1.00 45.34  ? 86  GLU A H    1 
ATOM   1423 H  HA   . GLU A 1 89  ? -12.369 -3.140  21.683 1.00 44.24  ? 86  GLU A HA   1 
ATOM   1424 H  HB2  . GLU A 1 89  ? -14.722 -2.001  20.626 1.00 55.58  ? 86  GLU A HB2  1 
ATOM   1425 H  HB3  . GLU A 1 89  ? -14.283 -3.471  20.213 1.00 55.58  ? 86  GLU A HB3  1 
ATOM   1426 H  HG2  . GLU A 1 89  ? -15.018 -4.311  22.081 1.00 75.87  ? 86  GLU A HG2  1 
ATOM   1427 H  HG3  . GLU A 1 89  ? -14.334 -3.163  22.942 1.00 75.87  ? 86  GLU A HG3  1 
ATOM   1428 N  N    . SER A 1 90  ? -11.657 -1.158  19.399 1.00 32.47  ? 87  SER A N    1 
ATOM   1429 C  CA   . SER A 1 90  ? -10.900 -0.963  18.167 1.00 29.61  ? 87  SER A CA   1 
ATOM   1430 C  C    . SER A 1 90  ? -9.623  -0.223  18.517 1.00 29.65  ? 87  SER A C    1 
ATOM   1431 O  O    . SER A 1 90  ? -9.677  0.955   18.876 1.00 28.39  ? 87  SER A O    1 
ATOM   1432 C  CB   . SER A 1 90  ? -11.720 -0.186  17.147 1.00 36.50  ? 87  SER A CB   1 
ATOM   1433 O  OG   . SER A 1 90  ? -10.902 0.228   16.062 1.00 34.57  ? 87  SER A OG   1 
ATOM   1434 H  H    . SER A 1 90  ? -11.862 -0.423  19.796 1.00 39.00  ? 87  SER A H    1 
ATOM   1435 H  HA   . SER A 1 90  ? -10.666 -1.823  17.783 1.00 35.57  ? 87  SER A HA   1 
ATOM   1436 H  HB2  . SER A 1 90  ? -12.430 -0.755  16.810 1.00 43.84  ? 87  SER A HB2  1 
ATOM   1437 H  HB3  . SER A 1 90  ? -12.099 0.597   17.575 1.00 43.84  ? 87  SER A HB3  1 
ATOM   1438 H  HG   . SER A 1 90  ? -10.336 0.790   16.326 1.00 41.52  ? 87  SER A HG   1 
ATOM   1439 N  N    . ILE A 1 91  ? -8.480  -0.911  18.420 1.00 22.59  ? 88  ILE A N    1 
ATOM   1440 C  CA   . ILE A 1 91  ? -7.181  -0.336  18.732 1.00 21.32  ? 88  ILE A CA   1 
ATOM   1441 C  C    . ILE A 1 91  ? -6.245  -0.578  17.551 1.00 21.99  ? 88  ILE A C    1 
ATOM   1442 O  O    . ILE A 1 91  ? -6.136  -1.715  17.047 1.00 24.68  ? 88  ILE A O    1 
ATOM   1443 C  CB   . ILE A 1 91  ? -6.584  -0.951  20.008 1.00 25.15  ? 88  ILE A CB   1 
ATOM   1444 C  CG1  . ILE A 1 91  ? -7.509  -0.692  21.207 1.00 28.52  ? 88  ILE A CG1  1 
ATOM   1445 C  CG2  . ILE A 1 91  ? -5.181  -0.438  20.266 1.00 25.61  ? 88  ILE A CG2  1 
ATOM   1446 C  CD1  . ILE A 1 91  ? -7.165  -1.554  22.438 1.00 29.61  ? 88  ILE A CD1  1 
ATOM   1447 H  H    . ILE A 1 91  ? -8.438  -1.733  18.168 1.00 27.15  ? 88  ILE A H    1 
ATOM   1448 H  HA   . ILE A 1 91  ? -7.278  0.620   18.857 1.00 25.62  ? 88  ILE A HA   1 
ATOM   1449 H  HB   . ILE A 1 91  ? -6.518  -1.910  19.879 1.00 30.21  ? 88  ILE A HB   1 
ATOM   1450 H  HG12 . ILE A 1 91  ? -7.436  0.240   21.464 1.00 34.26  ? 88  ILE A HG12 1 
ATOM   1451 H  HG13 . ILE A 1 91  ? -8.422  -0.893  20.948 1.00 34.26  ? 88  ILE A HG13 1 
ATOM   1452 H  HG21 . ILE A 1 91  ? -4.913  -0.688  21.164 1.00 30.77  ? 88  ILE A HG21 1 
ATOM   1453 H  HG22 . ILE A 1 91  ? -4.576  -0.833  19.619 1.00 30.77  ? 88  ILE A HG22 1 
ATOM   1454 H  HG23 . ILE A 1 91  ? -5.177  0.528   20.177 1.00 30.77  ? 88  ILE A HG23 1 
ATOM   1455 H  HD11 . ILE A 1 91  ? -7.866  -1.452  23.101 1.00 35.56  ? 88  ILE A HD11 1 
ATOM   1456 H  HD12 . ILE A 1 91  ? -7.099  -2.482  22.166 1.00 35.56  ? 88  ILE A HD12 1 
ATOM   1457 H  HD13 . ILE A 1 91  ? -6.317  -1.255  22.805 1.00 35.56  ? 88  ILE A HD13 1 
ATOM   1458 N  N    . SER A 1 92  ? -5.553  0.485   17.136 1.00 21.64  ? 89  SER A N    1 
ATOM   1459 C  CA   . SER A 1 92  ? -4.599  0.472   16.022 1.00 23.70  ? 89  SER A CA   1 
ATOM   1460 C  C    . SER A 1 92  ? -3.323  1.105   16.539 1.00 25.26  ? 89  SER A C    1 
ATOM   1461 O  O    . SER A 1 92  ? -3.287  1.629   17.646 1.00 23.09  ? 89  SER A O    1 
ATOM   1462 C  CB   . SER A 1 92  ? -5.125  1.224   14.786 1.00 22.87  ? 89  SER A CB   1 
ATOM   1463 O  OG   . SER A 1 92  ? -6.304  0.607   14.337 1.00 25.30  ? 89  SER A OG   1 
ATOM   1464 H  H    . SER A 1 92  ? -5.622  1.262   17.499 1.00 26.01  ? 89  SER A H    1 
ATOM   1465 H  HA   . SER A 1 92  ? -4.427  -0.437  15.730 1.00 28.47  ? 89  SER A HA   1 
ATOM   1466 H  HB2  . SER A 1 92  ? -5.315  2.145   15.026 1.00 27.47  ? 89  SER A HB2  1 
ATOM   1467 H  HB3  . SER A 1 92  ? -4.458  1.194   14.083 1.00 27.47  ? 89  SER A HB3  1 
ATOM   1468 H  HG   . SER A 1 92  ? -6.491  0.873   13.562 1.00 30.39  ? 89  SER A HG   1 
ATOM   1469 N  N    . ALA A 1 93  ? -2.258  1.027   15.764 1.00 21.04  ? 90  ALA A N    1 
ATOM   1470 C  CA   . ALA A 1 93  ? -0.986  1.553   16.216 1.00 21.21  ? 90  ALA A CA   1 
ATOM   1471 C  C    . ALA A 1 93  ? -0.174  2.097   15.047 1.00 23.21  ? 90  ALA A C    1 
ATOM   1472 O  O    . ALA A 1 93  ? -0.256  1.605   13.910 1.00 21.68  ? 90  ALA A O    1 
ATOM   1473 C  CB   . ALA A 1 93  ? -0.140  0.499   16.918 1.00 21.99  ? 90  ALA A CB   1 
ATOM   1474 H  H    . ALA A 1 93  ? -2.246  0.676   14.979 1.00 25.29  ? 90  ALA A H    1 
ATOM   1475 H  HA   . ALA A 1 93  ? -1.184  2.281   16.826 1.00 25.49  ? 90  ALA A HA   1 
ATOM   1476 H  HB1  . ALA A 1 93  ? 0.701   0.898   17.190 1.00 26.42  ? 90  ALA A HB1  1 
ATOM   1477 H  HB2  . ALA A 1 93  ? -0.620  0.176   17.697 1.00 26.42  ? 90  ALA A HB2  1 
ATOM   1478 H  HB3  . ALA A 1 93  ? 0.025   -0.234  16.304 1.00 26.42  ? 90  ALA A HB3  1 
ATOM   1479 N  N    . THR A 1 94  ? 0.660   3.078   15.365 1.00 20.92  ? 91  THR A N    1 
ATOM   1480 C  CA   . THR A 1 94  ? 1.590   3.661   14.397 1.00 21.60  ? 91  THR A CA   1 
ATOM   1481 C  C    . THR A 1 94  ? 2.826   4.090   15.152 1.00 25.25  ? 91  THR A C    1 
ATOM   1482 O  O    . THR A 1 94  ? 2.759   4.444   16.336 1.00 22.23  ? 91  THR A O    1 
ATOM   1483 C  CB   . THR A 1 94  ? 0.984   4.813   13.596 1.00 25.15  ? 91  THR A CB   1 
ATOM   1484 O  OG1  . THR A 1 94  ? 1.959   5.264   12.645 1.00 25.47  ? 91  THR A OG1  1 
ATOM   1485 C  CG2  . THR A 1 94  ? 0.623   5.979   14.457 1.00 24.00  ? 91  THR A CG2  1 
ATOM   1486 H  H    . THR A 1 94  ? 0.711   3.432   16.147 1.00 25.14  ? 91  THR A H    1 
ATOM   1487 H  HA   . THR A 1 94  ? 1.842   2.994   13.739 1.00 25.95  ? 91  THR A HA   1 
ATOM   1488 H  HB   . THR A 1 94  ? 0.174   4.496   13.168 1.00 30.21  ? 91  THR A HB   1 
ATOM   1489 H  HG1  . THR A 1 94  ? 2.201   4.624   12.157 1.00 30.60  ? 91  THR A HG1  1 
ATOM   1490 H  HG21 . THR A 1 94  ? 0.069   6.600   13.959 1.00 28.83  ? 91  THR A HG21 1 
ATOM   1491 H  HG22 . THR A 1 94  ? 0.133   5.676   15.238 1.00 28.83  ? 91  THR A HG22 1 
ATOM   1492 H  HG23 . THR A 1 94  ? 1.427   6.438   14.749 1.00 28.83  ? 91  THR A HG23 1 
ATOM   1493 N  N    . GLY A 1 95  ? 3.966   4.050   14.486 1.00 21.20  ? 92  GLY A N    1 
ATOM   1494 C  CA   . GLY A 1 95  ? 5.177   4.493   15.160 1.00 22.13  ? 92  GLY A CA   1 
ATOM   1495 C  C    . GLY A 1 95  ? 6.290   4.732   14.176 1.00 22.73  ? 92  GLY A C    1 
ATOM   1496 O  O    . GLY A 1 95  ? 6.242   4.260   13.042 1.00 21.88  ? 92  GLY A O    1 
ATOM   1497 H  H    . GLY A 1 95  ? 4.064   3.781   13.675 1.00 25.47  ? 92  GLY A H    1 
ATOM   1498 H  HA2  . GLY A 1 95  ? 5.002   5.319   15.637 1.00 26.59  ? 92  GLY A HA2  1 
ATOM   1499 H  HA3  . GLY A 1 95  ? 5.464   3.817   15.793 1.00 26.59  ? 92  GLY A HA3  1 
ATOM   1500 N  N    A VAL A 1 96  ? 7.300   5.465   14.621 0.70 22.74  ? 93  VAL A N    1 
ATOM   1501 N  N    B VAL A 1 96  ? 7.292   5.478   14.635 0.30 22.73  ? 93  VAL A N    1 
ATOM   1502 C  CA   A VAL A 1 96  ? 8.440   5.830   13.781 0.70 21.51  ? 93  VAL A CA   1 
ATOM   1503 C  CA   B VAL A 1 96  ? 8.456   5.855   13.842 0.30 21.63  ? 93  VAL A CA   1 
ATOM   1504 C  C    A VAL A 1 96  ? 9.709   5.242   14.384 0.70 23.60  ? 93  VAL A C    1 
ATOM   1505 C  C    B VAL A 1 96  ? 9.681   5.152   14.413 0.30 23.56  ? 93  VAL A C    1 
ATOM   1506 O  O    A VAL A 1 96  ? 9.949   5.372   15.588 0.70 23.28  ? 93  VAL A O    1 
ATOM   1507 O  O    B VAL A 1 96  ? 9.868   5.110   15.634 0.30 24.05  ? 93  VAL A O    1 
ATOM   1508 C  CB   A VAL A 1 96  ? 8.536   7.362   13.615 0.70 25.81  ? 93  VAL A CB   1 
ATOM   1509 C  CB   B VAL A 1 96  ? 8.665   7.383   13.850 0.30 24.81  ? 93  VAL A CB   1 
ATOM   1510 C  CG1  A VAL A 1 96  ? 8.621   8.071   14.952 0.70 22.51  ? 93  VAL A CG1  1 
ATOM   1511 C  CG1  B VAL A 1 96  ? 9.819   7.782   12.933 0.30 27.24  ? 93  VAL A CG1  1 
ATOM   1512 C  CG2  A VAL A 1 96  ? 9.691   7.790   12.674 0.70 26.99  ? 93  VAL A CG2  1 
ATOM   1513 C  CG2  B VAL A 1 96  ? 7.378   8.120   13.437 0.30 27.78  ? 93  VAL A CG2  1 
ATOM   1514 H  H    A VAL A 1 96  ? 7.352   5.772   15.423 0.70 27.33  ? 93  VAL A H    1 
ATOM   1515 H  H    B VAL A 1 96  ? 7.319   5.789   15.437 0.30 27.31  ? 93  VAL A H    1 
ATOM   1516 H  HA   A VAL A 1 96  ? 8.337   5.435   12.901 0.70 25.85  ? 93  VAL A HA   1 
ATOM   1517 H  HA   B VAL A 1 96  ? 8.326   5.561   12.927 0.30 25.99  ? 93  VAL A HA   1 
ATOM   1518 H  HB   A VAL A 1 96  ? 7.713   7.646   13.189 0.70 31.01  ? 93  VAL A HB   1 
ATOM   1519 H  HB   B VAL A 1 96  ? 8.890   7.650   14.755 0.30 29.80  ? 93  VAL A HB   1 
ATOM   1520 H  HG11 A VAL A 1 96  ? 8.610   9.029   14.803 0.70 27.04  ? 93  VAL A HG11 1 
ATOM   1521 H  HG11 B VAL A 1 96  ? 9.808   8.745   12.812 0.30 32.72  ? 93  VAL A HG11 1 
ATOM   1522 H  HG12 A VAL A 1 96  ? 7.860   7.813   15.496 0.70 27.04  ? 93  VAL A HG12 1 
ATOM   1523 H  HG12 B VAL A 1 96  ? 10.656  7.510   13.342 0.30 32.72  ? 93  VAL A HG12 1 
ATOM   1524 H  HG13 A VAL A 1 96  ? 9.445   7.814   15.394 0.70 27.04  ? 93  VAL A HG13 1 
ATOM   1525 H  HG13 B VAL A 1 96  ? 9.710   7.340   12.077 0.30 32.72  ? 93  VAL A HG13 1 
ATOM   1526 H  HG21 A VAL A 1 96  ? 9.661   8.753   12.556 0.70 32.42  ? 93  VAL A HG21 1 
ATOM   1527 H  HG21 B VAL A 1 96  ? 7.566   9.069   13.365 0.30 33.37  ? 93  VAL A HG21 1 
ATOM   1528 H  HG22 A VAL A 1 96  ? 10.536  7.532   13.072 0.70 32.42  ? 93  VAL A HG22 1 
ATOM   1529 H  HG22 B VAL A 1 96  ? 7.077   7.776   12.582 0.30 33.37  ? 93  VAL A HG22 1 
ATOM   1530 H  HG23 A VAL A 1 96  ? 9.580   7.349   11.817 0.70 32.42  ? 93  VAL A HG23 1 
ATOM   1531 H  HG23 B VAL A 1 96  ? 6.697   7.968   14.112 0.30 33.37  ? 93  VAL A HG23 1 
ATOM   1532 N  N    . SER A 1 97  ? 10.528  4.623   13.527 1.00 23.59  ? 94  SER A N    1 
ATOM   1533 C  CA   . SER A 1 97  ? 11.835  4.067   13.886 1.00 26.90  ? 94  SER A CA   1 
ATOM   1534 C  C    . SER A 1 97  ? 11.617  2.985   14.935 1.00 24.43  ? 94  SER A C    1 
ATOM   1535 O  O    . SER A 1 97  ? 10.894  2.020   14.632 1.00 24.55  ? 94  SER A O    1 
ATOM   1536 C  CB   . SER A 1 97  ? 12.729  5.247   14.274 1.00 35.70  ? 94  SER A CB   1 
ATOM   1537 O  OG   . SER A 1 97  ? 14.076  4.936   13.983 1.00 57.36  ? 94  SER A OG   1 
ATOM   1538 H  H    A SER A 1 97  ? 10.339  4.509   12.695 0.70 28.34  ? 94  SER A H    1 
ATOM   1539 H  H    B SER A 1 97  ? 10.362  4.574   12.684 0.30 28.34  ? 94  SER A H    1 
ATOM   1540 H  HA   . SER A 1 97  ? 12.230  3.614   13.125 1.00 32.32  ? 94  SER A HA   1 
ATOM   1541 H  HB2  . SER A 1 97  ? 12.464  6.031   13.768 1.00 42.87  ? 94  SER A HB2  1 
ATOM   1542 H  HB3  . SER A 1 97  ? 12.638  5.420   15.224 1.00 42.87  ? 94  SER A HB3  1 
ATOM   1543 H  HG   . SER A 1 97  ? 14.584  5.516   14.316 1.00 68.87  ? 94  SER A HG   1 
ATOM   1544 N  N    . LEU A 1 98  ? 12.175  3.082   16.138 1.00 25.22  ? 95  LEU A N    1 
ATOM   1545 C  CA   . LEU A 1 98  ? 11.903  2.053   17.141 1.00 24.07  ? 95  LEU A CA   1 
ATOM   1546 C  C    . LEU A 1 98  ? 10.410  1.886   17.368 1.00 23.15  ? 95  LEU A C    1 
ATOM   1547 O  O    . LEU A 1 98  ? 9.929   0.759   17.577 1.00 23.22  ? 95  LEU A O    1 
ATOM   1548 C  CB   . LEU A 1 98  ? 12.602  2.383   18.458 1.00 27.01  ? 95  LEU A CB   1 
ATOM   1549 C  CG   . LEU A 1 98  ? 12.310  1.503   19.682 1.00 28.06  ? 95  LEU A CG   1 
ATOM   1550 C  CD1  . LEU A 1 98  ? 12.646  0.065   19.350 1.00 30.49  ? 95  LEU A CD1  1 
ATOM   1551 C  CD2  . LEU A 1 98  ? 13.116  2.027   20.887 1.00 33.05  ? 95  LEU A CD2  1 
ATOM   1552 H  H    . LEU A 1 98  ? 12.699  3.713   16.394 1.00 30.30  ? 95  LEU A H    1 
ATOM   1553 H  HA   . LEU A 1 98  ? 12.263  1.211   16.821 1.00 28.91  ? 95  LEU A HA   1 
ATOM   1554 H  HB2  . LEU A 1 98  ? 13.558  2.332   18.302 1.00 32.45  ? 95  LEU A HB2  1 
ATOM   1555 H  HB3  . LEU A 1 98  ? 12.353  3.288   18.702 1.00 32.45  ? 95  LEU A HB3  1 
ATOM   1556 H  HG   . LEU A 1 98  ? 11.371  1.534   19.926 1.00 33.70  ? 95  LEU A HG   1 
ATOM   1557 H  HD11 . LEU A 1 98  ? 12.623  -0.461  20.164 1.00 36.63  ? 95  LEU A HD11 1 
ATOM   1558 H  HD12 . LEU A 1 98  ? 11.992  -0.275  18.719 1.00 36.63  ? 95  LEU A HD12 1 
ATOM   1559 H  HD13 . LEU A 1 98  ? 13.533  0.030   18.958 1.00 36.63  ? 95  LEU A HD13 1 
ATOM   1560 H  HD21 . LEU A 1 98  ? 12.921  1.476   21.661 1.00 39.70  ? 95  LEU A HD21 1 
ATOM   1561 H  HD22 . LEU A 1 98  ? 14.062  1.980   20.678 1.00 39.70  ? 95  LEU A HD22 1 
ATOM   1562 H  HD23 . LEU A 1 98  ? 12.861  2.946   21.062 1.00 39.70  ? 95  LEU A HD23 1 
ATOM   1563 N  N    . GLY A 1 99  ? 9.648   2.975   17.255 1.00 21.02  ? 96  GLY A N    1 
ATOM   1564 C  CA   . GLY A 1 99  ? 8.210   2.863   17.428 1.00 20.75  ? 96  GLY A CA   1 
ATOM   1565 C  C    . GLY A 1 99  ? 7.559   2.057   16.318 1.00 23.38  ? 96  GLY A C    1 
ATOM   1566 O  O    . GLY A 1 99  ? 6.538   1.400   16.531 1.00 20.99  ? 96  GLY A O    1 
ATOM   1567 H  H    . GLY A 1 99  ? 9.935   3.767   17.083 1.00 25.26  ? 96  GLY A H    1 
ATOM   1568 H  HA2  . GLY A 1 99  ? 8.022   2.427   18.274 1.00 24.93  ? 96  GLY A HA2  1 
ATOM   1569 H  HA3  . GLY A 1 99  ? 7.817   3.749   17.435 1.00 24.93  ? 96  GLY A HA3  1 
ATOM   1570 N  N    . GLY A 1 100 ? 8.160   2.077   15.136 1.00 24.13  ? 97  GLY A N    1 
ATOM   1571 C  CA   . GLY A 1 100 ? 7.684   1.223   14.061 1.00 22.08  ? 97  GLY A CA   1 
ATOM   1572 C  C    . GLY A 1 100 ? 7.953   -0.242  14.346 1.00 18.87  ? 97  GLY A C    1 
ATOM   1573 O  O    . GLY A 1 100 ? 7.088   -1.085  14.111 1.00 20.68  ? 97  GLY A O    1 
ATOM   1574 H  H    . GLY A 1 100 ? 8.835   2.569   14.933 1.00 28.99  ? 97  GLY A H    1 
ATOM   1575 H  HA2  . GLY A 1 100 ? 6.728   1.346   13.949 1.00 26.53  ? 97  GLY A HA2  1 
ATOM   1576 H  HA3  . GLY A 1 100 ? 8.132   1.464   13.235 1.00 26.53  ? 97  GLY A HA3  1 
ATOM   1577 N  N    . LEU A 1 101 ? 9.103   -0.543  14.944 1.00 22.15  ? 98  LEU A N    1 
ATOM   1578 C  CA   . LEU A 1 101 ? 9.372   -1.908  15.397 1.00 21.55  ? 98  LEU A CA   1 
ATOM   1579 C  C    . LEU A 1 101 ? 8.398   -2.343  16.475 1.00 21.04  ? 98  LEU A C    1 
ATOM   1580 O  O    . LEU A 1 101 ? 7.918   -3.475  16.450 1.00 22.15  ? 98  LEU A O    1 
ATOM   1581 C  CB   . LEU A 1 101 ? 10.803  -2.024  15.902 1.00 23.16  ? 98  LEU A CB   1 
ATOM   1582 C  CG   . LEU A 1 101 ? 11.884  -1.823  14.883 1.00 24.58  ? 98  LEU A CG   1 
ATOM   1583 C  CD1  . LEU A 1 101 ? 13.247  -1.706  15.541 1.00 32.17  ? 98  LEU A CD1  1 
ATOM   1584 C  CD2  . LEU A 1 101 ? 11.919  -2.906  13.850 1.00 29.66  ? 98  LEU A CD2  1 
ATOM   1585 H  H    . LEU A 1 101 ? 9.737   0.016   15.099 1.00 26.62  ? 98  LEU A H    1 
ATOM   1586 H  HA   . LEU A 1 101 ? 9.268   -2.506  14.640 1.00 25.89  ? 98  LEU A HA   1 
ATOM   1587 H  HB2  . LEU A 1 101 ? 10.933  -1.357  16.593 1.00 27.82  ? 98  LEU A HB2  1 
ATOM   1588 H  HB3  . LEU A 1 101 ? 10.921  -2.913  16.272 1.00 27.82  ? 98  LEU A HB3  1 
ATOM   1589 H  HG   . LEU A 1 101 ? 11.680  -0.992  14.425 1.00 29.53  ? 98  LEU A HG   1 
ATOM   1590 H  HD11 . LEU A 1 101 ? 13.923  -1.601  14.853 1.00 38.64  ? 98  LEU A HD11 1 
ATOM   1591 H  HD12 . LEU A 1 101 ? 13.250  -0.934  16.128 1.00 38.64  ? 98  LEU A HD12 1 
ATOM   1592 H  HD13 . LEU A 1 101 ? 13.420  -2.511  16.054 1.00 38.64  ? 98  LEU A HD13 1 
ATOM   1593 H  HD21 . LEU A 1 101 ? 12.720  -2.805  13.312 1.00 35.63  ? 98  LEU A HD21 1 
ATOM   1594 H  HD22 . LEU A 1 101 ? 11.927  -3.768  14.296 1.00 35.63  ? 98  LEU A HD22 1 
ATOM   1595 H  HD23 . LEU A 1 101 ? 11.131  -2.832  13.288 1.00 35.63  ? 98  LEU A HD23 1 
ATOM   1596 N  N    . MET A 1 102 ? 8.108   -1.466  17.439 1.00 19.11  ? 99  MET A N    1 
ATOM   1597 C  CA   . MET A 1 102 ? 7.168   -1.782  18.513 1.00 21.75  ? 99  MET A CA   1 
ATOM   1598 C  C    . MET A 1 102 ? 5.778   -2.027  17.941 1.00 24.04  ? 99  MET A C    1 
ATOM   1599 O  O    . MET A 1 102 ? 5.035   -2.856  18.451 1.00 22.52  ? 99  MET A O    1 
ATOM   1600 C  CB   . MET A 1 102 ? 7.135   -0.589  19.477 1.00 19.97  ? 99  MET A CB   1 
ATOM   1601 C  CG   . MET A 1 102 ? 8.360   -0.405  20.343 1.00 22.90  ? 99  MET A CG   1 
ATOM   1602 S  SD   . MET A 1 102 ? 8.800   -1.797  21.307 1.00 28.95  ? 99  MET A SD   1 
ATOM   1603 C  CE   . MET A 1 102 ? 10.121  -1.190  22.312 1.00 29.43  ? 99  MET A CE   1 
ATOM   1604 H  H    . MET A 1 102 ? 8.444   -0.677  17.495 1.00 22.97  ? 99  MET A H    1 
ATOM   1605 H  HA   . MET A 1 102 ? 7.457   -2.574  18.994 1.00 26.14  ? 99  MET A HA   1 
ATOM   1606 H  HB2  . MET A 1 102 ? 7.030   0.221   18.953 1.00 24.00  ? 99  MET A HB2  1 
ATOM   1607 H  HB3  . MET A 1 102 ? 6.377   -0.700  20.072 1.00 24.00  ? 99  MET A HB3  1 
ATOM   1608 H  HG2  . MET A 1 102 ? 9.115   -0.200  19.768 1.00 27.52  ? 99  MET A HG2  1 
ATOM   1609 H  HG3  . MET A 1 102 ? 8.198   0.331   20.953 1.00 27.52  ? 99  MET A HG3  1 
ATOM   1610 H  HE1  . MET A 1 102 ? 10.455  -1.914  22.865 1.00 35.36  ? 99  MET A HE1  1 
ATOM   1611 H  HE2  . MET A 1 102 ? 10.828  -0.858  21.737 1.00 35.36  ? 99  MET A HE2  1 
ATOM   1612 H  HE3  . MET A 1 102 ? 9.787   -0.472  22.873 1.00 35.36  ? 99  MET A HE3  1 
ATOM   1613 N  N    . THR A 1 103 ? 5.390   -1.275  16.916 1.00 22.61  ? 100 THR A N    1 
ATOM   1614 C  CA   . THR A 1 103 ? 4.103   -1.493  16.257 1.00 18.89  ? 100 THR A CA   1 
ATOM   1615 C  C    . THR A 1 103 ? 4.034   -2.882  15.628 1.00 18.54  ? 100 THR A C    1 
ATOM   1616 O  O    . THR A 1 103 ? 3.003   -3.583  15.719 1.00 20.88  ? 100 THR A O    1 
ATOM   1617 C  CB   . THR A 1 103 ? 3.903   -0.387  15.196 1.00 24.23  ? 100 THR A CB   1 
ATOM   1618 O  OG1  . THR A 1 103 ? 3.707   0.906   15.811 1.00 24.24  ? 100 THR A OG1  1 
ATOM   1619 C  CG2  . THR A 1 103 ? 2.699   -0.652  14.318 1.00 23.48  ? 100 THR A CG2  1 
ATOM   1620 H  H    . THR A 1 103 ? 5.851   -0.631  16.581 1.00 27.17  ? 100 THR A H    1 
ATOM   1621 H  HA   . THR A 1 103 ? 3.384   -1.439  16.905 1.00 22.70  ? 100 THR A HA   1 
ATOM   1622 H  HB   . THR A 1 103 ? 4.705   -0.380  14.652 1.00 29.11  ? 100 THR A HB   1 
ATOM   1623 H  HG1  . THR A 1 103 ? 4.430   1.179   16.141 1.00 29.13  ? 100 THR A HG1  1 
ATOM   1624 H  HG21 . THR A 1 103 ? 2.512   0.125   13.768 1.00 28.21  ? 100 THR A HG21 1 
ATOM   1625 H  HG22 . THR A 1 103 ? 2.870   -1.412  13.741 1.00 28.21  ? 100 THR A HG22 1 
ATOM   1626 H  HG23 . THR A 1 103 ? 1.923   -0.842  14.868 1.00 28.21  ? 100 THR A HG23 1 
ATOM   1627 N  N    . LEU A 1 104 ? 5.098   -3.280  14.912 1.00 19.65  ? 101 LEU A N    1 
ATOM   1628 C  CA   . LEU A 1 104 ? 5.143   -4.614  14.330 1.00 21.65  ? 101 LEU A CA   1 
ATOM   1629 C  C    . LEU A 1 104 ? 5.049   -5.686  15.415 1.00 21.09  ? 101 LEU A C    1 
ATOM   1630 O  O    . LEU A 1 104 ? 4.323   -6.687  15.259 1.00 21.14  ? 101 LEU A O    1 
ATOM   1631 C  CB   . LEU A 1 104 ? 6.429   -4.808  13.516 1.00 23.03  ? 101 LEU A CB   1 
ATOM   1632 C  CG   . LEU A 1 104 ? 6.545   -3.946  12.217 1.00 23.26  ? 101 LEU A CG   1 
ATOM   1633 C  CD1  . LEU A 1 104 ? 7.950   -3.975  11.710 1.00 27.73  ? 101 LEU A CD1  1 
ATOM   1634 C  CD2  . LEU A 1 104 ? 5.544   -4.445  11.157 1.00 22.32  ? 101 LEU A CD2  1 
ATOM   1635 H  H    . LEU A 1 104 ? 5.793   -2.798  14.755 1.00 23.62  ? 101 LEU A H    1 
ATOM   1636 H  HA   . LEU A 1 104 ? 4.389   -4.709  13.726 1.00 26.02  ? 101 LEU A HA   1 
ATOM   1637 H  HB2  . LEU A 1 104 ? 7.183   -4.580  14.082 1.00 27.68  ? 101 LEU A HB2  1 
ATOM   1638 H  HB3  . LEU A 1 104 ? 6.483   -5.739  13.251 1.00 27.68  ? 101 LEU A HB3  1 
ATOM   1639 H  HG   . LEU A 1 104 ? 6.323   -3.022  12.409 1.00 27.95  ? 101 LEU A HG   1 
ATOM   1640 H  HD11 . LEU A 1 104 ? 8.012   -3.416  10.919 1.00 33.32  ? 101 LEU A HD11 1 
ATOM   1641 H  HD12 . LEU A 1 104 ? 8.542   -3.637  12.401 1.00 33.32  ? 101 LEU A HD12 1 
ATOM   1642 H  HD13 . LEU A 1 104 ? 8.188   -4.889  11.489 1.00 33.32  ? 101 LEU A HD13 1 
ATOM   1643 H  HD21 . LEU A 1 104 ? 5.644   -3.912  10.353 1.00 26.82  ? 101 LEU A HD21 1 
ATOM   1644 H  HD22 . LEU A 1 104 ? 5.728   -5.377  10.962 1.00 26.82  ? 101 LEU A HD22 1 
ATOM   1645 H  HD23 . LEU A 1 104 ? 4.643   -4.352  11.505 1.00 26.82  ? 101 LEU A HD23 1 
ATOM   1646 N  N    . LYS A 1 105 ? 5.768   -5.489  16.536 1.00 20.70  ? 102 LYS A N    1 
ATOM   1647 C  CA   . LYS A 1 105 ? 5.722   -6.489  17.613 1.00 22.61  ? 102 LYS A CA   1 
ATOM   1648 C  C    . LYS A 1 105 ? 4.332   -6.552  18.235 1.00 21.81  ? 102 LYS A C    1 
ATOM   1649 O  O    . LYS A 1 105 ? 3.819   -7.641  18.536 1.00 21.64  ? 102 LYS A O    1 
ATOM   1650 C  CB   . LYS A 1 105 ? 6.762   -6.177  18.690 1.00 21.74  ? 102 LYS A CB   1 
ATOM   1651 C  CG   . LYS A 1 105 ? 6.921   -7.377  19.627 1.00 24.51  ? 102 LYS A CG   1 
ATOM   1652 C  CD   . LYS A 1 105 ? 8.054   -7.167  20.615 1.00 28.21  ? 102 LYS A CD   1 
ATOM   1653 C  CE   . LYS A 1 105 ? 8.191   -8.365  21.565 1.00 26.12  ? 102 LYS A CE   1 
ATOM   1654 N  NZ   . LYS A 1 105 ? 8.800   -9.552  20.986 1.00 28.19  ? 102 LYS A NZ   1 
ATOM   1655 H  H    . LYS A 1 105 ? 6.271   -4.809  16.690 1.00 24.87  ? 102 LYS A H    1 
ATOM   1656 H  HA   . LYS A 1 105 ? 5.939   -7.355  17.234 1.00 27.17  ? 102 LYS A HA   1 
ATOM   1657 H  HB2  . LYS A 1 105 ? 7.618   -5.992  18.272 1.00 26.13  ? 102 LYS A HB2  1 
ATOM   1658 H  HB3  . LYS A 1 105 ? 6.474   -5.411  19.210 1.00 26.13  ? 102 LYS A HB3  1 
ATOM   1659 H  HG2  . LYS A 1 105 ? 6.100   -7.505  20.128 1.00 29.45  ? 102 LYS A HG2  1 
ATOM   1660 H  HG3  . LYS A 1 105 ? 7.117   -8.170  19.104 1.00 29.45  ? 102 LYS A HG3  1 
ATOM   1661 H  HD2  . LYS A 1 105 ? 8.888   -7.062  20.131 1.00 33.89  ? 102 LYS A HD2  1 
ATOM   1662 H  HD3  . LYS A 1 105 ? 7.876   -6.374  21.145 1.00 33.89  ? 102 LYS A HD3  1 
ATOM   1663 H  HE2  . LYS A 1 105 ? 8.740   -8.097  22.319 1.00 31.38  ? 102 LYS A HE2  1 
ATOM   1664 H  HE3  . LYS A 1 105 ? 7.306   -8.616  21.873 1.00 31.38  ? 102 LYS A HE3  1 
ATOM   1665 H  HZ1  . LYS A 1 105 ? 8.833   -10.204 21.591 1.00 33.86  ? 102 LYS A HZ1  1 
ATOM   1666 H  HZ2  . LYS A 1 105 ? 8.323   -9.829  20.288 1.00 33.86  ? 102 LYS A HZ2  1 
ATOM   1667 H  HZ3  . LYS A 1 105 ? 9.628   -9.368  20.715 1.00 33.86  ? 102 LYS A HZ3  1 
ATOM   1668 N  N    A LEU A 1 106 ? 3.694   -5.397  18.429 0.31 20.66  ? 103 LEU A N    1 
ATOM   1669 N  N    B LEU A 1 106 ? 3.703   -5.391  18.443 0.69 20.58  ? 103 LEU A N    1 
ATOM   1670 C  CA   A LEU A 1 106 ? 2.343   -5.388  18.975 0.31 20.88  ? 103 LEU A CA   1 
ATOM   1671 C  CA   B LEU A 1 106 ? 2.338   -5.385  18.950 0.69 20.76  ? 103 LEU A CA   1 
ATOM   1672 C  C    A LEU A 1 106 ? 1.365   -6.112  18.060 0.31 22.48  ? 103 LEU A C    1 
ATOM   1673 C  C    B LEU A 1 106 ? 1.427   -6.201  18.054 0.69 22.49  ? 103 LEU A C    1 
ATOM   1674 O  O    A LEU A 1 106 ? 0.425   -6.750  18.536 0.31 22.48  ? 103 LEU A O    1 
ATOM   1675 O  O    B LEU A 1 106 ? 0.592   -6.972  18.526 0.69 21.91  ? 103 LEU A O    1 
ATOM   1676 C  CB   A LEU A 1 106 ? 1.906   -3.947  19.210 0.31 22.95  ? 103 LEU A CB   1 
ATOM   1677 C  CB   B LEU A 1 106 ? 1.819   -3.957  19.057 0.69 23.02  ? 103 LEU A CB   1 
ATOM   1678 C  CG   A LEU A 1 106 ? 0.797   -3.690  20.225 0.31 24.30  ? 103 LEU A CG   1 
ATOM   1679 C  CG   B LEU A 1 106 ? 2.144   -3.177  20.332 0.69 21.72  ? 103 LEU A CG   1 
ATOM   1680 C  CD1  A LEU A 1 106 ? 1.231   -4.038  21.647 0.31 25.84  ? 103 LEU A CD1  1 
ATOM   1681 C  CD1  B LEU A 1 106 ? 1.749   -1.698  20.118 0.69 27.51  ? 103 LEU A CD1  1 
ATOM   1682 C  CD2  A LEU A 1 106 ? 0.380   -2.232  20.139 0.31 22.26  ? 103 LEU A CD2  1 
ATOM   1683 C  CD2  B LEU A 1 106 ? 1.480   -3.748  21.578 0.69 27.06  ? 103 LEU A CD2  1 
ATOM   1684 H  H    A LEU A 1 106 ? 4.018   -4.620  18.256 0.31 24.83  ? 103 LEU A H    1 
ATOM   1685 H  H    B LEU A 1 106 ? 4.040   -4.613  18.299 0.69 24.73  ? 103 LEU A H    1 
ATOM   1686 H  HA   A LEU A 1 106 ? 2.333   -5.849  19.828 0.31 25.09  ? 103 LEU A HA   1 
ATOM   1687 H  HA   B LEU A 1 106 ? 2.334   -5.774  19.838 0.69 24.95  ? 103 LEU A HA   1 
ATOM   1688 H  HB2  A LEU A 1 106 ? 2.682   -3.450  19.514 0.31 27.58  ? 103 LEU A HB2  1 
ATOM   1689 H  HB2  B LEU A 1 106 ? 2.191   -3.451  18.317 0.69 27.66  ? 103 LEU A HB2  1 
ATOM   1690 H  HB3  A LEU A 1 106 ? 1.596   -3.591  18.363 0.31 27.58  ? 103 LEU A HB3  1 
ATOM   1691 H  HB3  B LEU A 1 106 ? 0.852   -3.987  18.986 0.69 27.66  ? 103 LEU A HB3  1 
ATOM   1692 H  HG   A LEU A 1 106 ? 0.041   -4.262  20.020 0.31 29.20  ? 103 LEU A HG   1 
ATOM   1693 H  HG   B LEU A 1 106 ? 3.096   -3.247  20.503 0.69 26.10  ? 103 LEU A HG   1 
ATOM   1694 H  HD11 A LEU A 1 106 ? 0.500   -3.848  22.256 0.31 31.04  ? 103 LEU A HD11 1 
ATOM   1695 H  HD11 B LEU A 1 106 ? 1.894   -1.210  20.944 0.69 33.05  ? 103 LEU A HD11 1 
ATOM   1696 H  HD12 A LEU A 1 106 ? 1.459   -4.980  21.687 0.31 31.04  ? 103 LEU A HD12 1 
ATOM   1697 H  HD12 B LEU A 1 106 ? 2.298   -1.324  19.412 0.69 33.05  ? 103 LEU A HD12 1 
ATOM   1698 H  HD13 A LEU A 1 106 ? 2.004   -3.500  21.882 0.31 31.04  ? 103 LEU A HD13 1 
ATOM   1699 H  HD13 B LEU A 1 106 ? 0.813   -1.654  19.868 0.69 33.05  ? 103 LEU A HD13 1 
ATOM   1700 H  HD21 A LEU A 1 106 ? -0.439  -2.107  20.645 0.31 26.75  ? 103 LEU A HD21 1 
ATOM   1701 H  HD21 B LEU A 1 106 ? 1.618   -3.136  22.318 0.69 32.51  ? 103 LEU A HD21 1 
ATOM   1702 H  HD22 A LEU A 1 106 ? 1.085   -1.679  20.510 0.31 26.75  ? 103 LEU A HD22 1 
ATOM   1703 H  HD22 B LEU A 1 106 ? 0.531   -3.854  21.409 0.69 32.51  ? 103 LEU A HD22 1 
ATOM   1704 H  HD23 A LEU A 1 106 ? 0.232   -2.000  19.209 0.31 26.75  ? 103 LEU A HD23 1 
ATOM   1705 H  HD23 B LEU A 1 106 ? 1.878   -4.608  21.781 0.69 32.51  ? 103 LEU A HD23 1 
ATOM   1706 N  N    . ALA A 1 107 ? 1.563   -6.024  16.746 1.00 22.09  ? 104 ALA A N    1 
ATOM   1707 C  CA   . ALA A 1 107 ? 0.735   -6.743  15.810 1.00 22.87  ? 104 ALA A CA   1 
ATOM   1708 C  C    . ALA A 1 107 ? 0.947   -8.254  15.822 1.00 22.53  ? 104 ALA A C    1 
ATOM   1709 O  O    . ALA A 1 107 ? 0.027   -8.991  15.438 1.00 24.25  ? 104 ALA A O    1 
ATOM   1710 C  CB   . ALA A 1 107 ? 1.044   -6.154  14.410 1.00 23.31  ? 104 ALA A CB   1 
ATOM   1711 H  H    A ALA A 1 107 ? 2.178   -5.549  16.377 0.31 26.54  ? 104 ALA A H    1 
ATOM   1712 H  H    B ALA A 1 107 ? 2.130   -5.491  16.380 0.69 26.54  ? 104 ALA A H    1 
ATOM   1713 H  HA   . ALA A 1 107 ? -0.202  -6.624  16.031 1.00 27.48  ? 104 ALA A HA   1 
ATOM   1714 H  HB1  . ALA A 1 107 ? 0.544   -6.648  13.742 1.00 28.01  ? 104 ALA A HB1  1 
ATOM   1715 H  HB2  . ALA A 1 107 ? 0.782   -5.220  14.396 1.00 28.01  ? 104 ALA A HB2  1 
ATOM   1716 H  HB3  . ALA A 1 107 ? 1.995   -6.234  14.237 1.00 28.01  ? 104 ALA A HB3  1 
ATOM   1717 N  N    . GLN A 1 108 ? 2.114   -8.740  16.259 1.00 22.78  ? 105 GLN A N    1 
ATOM   1718 C  CA   . GLN A 1 108 ? 2.350   -10.160 16.420 1.00 23.53  ? 105 GLN A CA   1 
ATOM   1719 C  C    . GLN A 1 108 ? 1.688   -10.737 17.670 1.00 22.99  ? 105 GLN A C    1 
ATOM   1720 O  O    . GLN A 1 108 ? 1.437   -11.959 17.737 1.00 24.55  ? 105 GLN A O    1 
ATOM   1721 C  CB   . GLN A 1 108 ? 3.850   -10.438 16.474 1.00 23.94  ? 105 GLN A CB   1 
ATOM   1722 C  CG   . GLN A 1 108 ? 4.566   -10.054 15.137 1.00 22.21  ? 105 GLN A CG   1 
ATOM   1723 C  CD   . GLN A 1 108 ? 6.049   -10.132 15.203 1.00 27.81  ? 105 GLN A CD   1 
ATOM   1724 O  OE1  . GLN A 1 108 ? 6.650   -10.064 16.252 1.00 29.82  ? 105 GLN A OE1  1 
ATOM   1725 N  NE2  . GLN A 1 108 ? 6.662   -10.273 14.048 1.00 28.42  ? 105 GLN A NE2  1 
ATOM   1726 H  H    . GLN A 1 108 ? 2.791   -8.253  16.471 1.00 27.37  ? 105 GLN A H    1 
ATOM   1727 H  HA   . GLN A 1 108 ? 1.981   -10.620 15.649 1.00 28.27  ? 105 GLN A HA   1 
ATOM   1728 H  HB2  . GLN A 1 108 ? 4.245   -9.917  17.191 1.00 28.76  ? 105 GLN A HB2  1 
ATOM   1729 H  HB3  . GLN A 1 108 ? 3.993   -11.384 16.634 1.00 28.76  ? 105 GLN A HB3  1 
ATOM   1730 H  HG2  . GLN A 1 108 ? 4.269   -10.659 14.440 1.00 26.48  ? 105 GLN A HG2  1 
ATOM   1731 H  HG3  . GLN A 1 108 ? 4.329   -9.142  14.908 1.00 26.48  ? 105 GLN A HG3  1 
ATOM   1732 H  HE21 . GLN A 1 108 ? 6.204   -10.313 13.321 1.00 34.14  ? 105 GLN A HE21 1 
ATOM   1733 H  HE22 . GLN A 1 108 ? 7.520   -10.324 14.020 1.00 34.14  ? 105 GLN A HE22 1 
ATOM   1734 N  N    . HIS A 1 109 ? 1.394   -9.870  18.639 1.00 22.72  ? 106 HIS A N    1 
ATOM   1735 C  CA   . HIS A 1 109 ? 0.826   -10.281 19.921 1.00 23.10  ? 106 HIS A CA   1 
ATOM   1736 C  C    . HIS A 1 109 ? -0.682  -10.040 20.059 1.00 23.59  ? 106 HIS A C    1 
ATOM   1737 O  O    . HIS A 1 109 ? -1.348  -10.795 20.781 1.00 27.43  ? 106 HIS A O    1 
ATOM   1738 C  CB   . HIS A 1 109 ? 1.521   -9.487  21.046 1.00 23.16  ? 106 HIS A CB   1 
ATOM   1739 C  CG   . HIS A 1 109 ? 2.886   -9.981  21.387 1.00 26.30  ? 106 HIS A CG   1 
ATOM   1740 N  ND1  . HIS A 1 109 ? 3.930   -9.959  20.491 1.00 30.01  ? 106 HIS A ND1  1 
ATOM   1741 C  CD2  . HIS A 1 109 ? 3.391   -10.496 22.534 1.00 26.29  ? 106 HIS A CD2  1 
ATOM   1742 C  CE1  . HIS A 1 109 ? 5.020   -10.435 21.065 1.00 29.32  ? 106 HIS A CE1  1 
ATOM   1743 N  NE2  . HIS A 1 109 ? 4.715   -10.775 22.302 1.00 30.55  ? 106 HIS A NE2  1 
ATOM   1744 H  H    . HIS A 1 109 ? 1.517   -9.021  18.576 1.00 27.30  ? 106 HIS A H    1 
ATOM   1745 H  HA   . HIS A 1 109 ? 0.979   -11.233 20.028 1.00 27.54  ? 106 HIS A HA   1 
ATOM   1746 H  HB2  . HIS A 1 109 ? 1.604   -8.562  20.767 1.00 27.82  ? 106 HIS A HB2  1 
ATOM   1747 H  HB3  . HIS A 1 109 ? 0.978   -9.544  21.848 1.00 27.82  ? 106 HIS A HB3  1 
ATOM   1748 H  HD1  . HIS A 1 109 ? 3.881   -9.678  19.680 1.00 36.05  ? 106 HIS A HD1  1 
ATOM   1749 H  HD2  . HIS A 1 109 ? 2.928   -10.634 23.329 1.00 31.59  ? 106 HIS A HD2  1 
ATOM   1750 H  HE1  . HIS A 1 109 ? 5.856   -10.515 20.667 1.00 35.22  ? 106 HIS A HE1  1 
ATOM   1751 N  N    . TYR A 1 110 ? -1.233  -8.990  19.443 1.00 25.02  ? 107 TYR A N    1 
ATOM   1752 C  CA   . TYR A 1 110 ? -2.575  -8.491  19.715 1.00 23.89  ? 107 TYR A CA   1 
ATOM   1753 C  C    . TYR A 1 110 ? -3.372  -8.290  18.435 1.00 27.20  ? 107 TYR A C    1 
ATOM   1754 O  O    . TYR A 1 110 ? -2.792  -8.091  17.360 1.00 26.75  ? 107 TYR A O    1 
ATOM   1755 C  CB   . TYR A 1 110 ? -2.506  -7.145  20.458 1.00 24.45  ? 107 TYR A CB   1 
ATOM   1756 C  CG   . TYR A 1 110 ? -1.895  -7.257  21.834 1.00 26.87  ? 107 TYR A CG   1 
ATOM   1757 C  CD1  . TYR A 1 110 ? -2.562  -7.909  22.862 1.00 32.44  ? 107 TYR A CD1  1 
ATOM   1758 C  CD2  . TYR A 1 110 ? -0.631  -6.735  22.087 1.00 28.34  ? 107 TYR A CD2  1 
ATOM   1759 C  CE1  . TYR A 1 110 ? -2.011  -8.010  24.121 1.00 35.99  ? 107 TYR A CE1  1 
ATOM   1760 C  CE2  . TYR A 1 110 ? -0.046  -6.884  23.366 1.00 30.94  ? 107 TYR A CE2  1 
ATOM   1761 C  CZ   . TYR A 1 110 ? -0.763  -7.517  24.357 1.00 34.30  ? 107 TYR A CZ   1 
ATOM   1762 O  OH   . TYR A 1 110 ? -0.201  -7.668  25.621 1.00 41.05  ? 107 TYR A OH   1 
ATOM   1763 H  H    . TYR A 1 110 ? -0.827  -8.534  18.837 1.00 30.06  ? 107 TYR A H    1 
ATOM   1764 H  HA   . TYR A 1 110 ? -3.040  -9.154  20.250 1.00 28.71  ? 107 TYR A HA   1 
ATOM   1765 H  HB2  . TYR A 1 110 ? -1.965  -6.528  19.940 1.00 29.38  ? 107 TYR A HB2  1 
ATOM   1766 H  HB3  . TYR A 1 110 ? -3.405  -6.795  20.558 1.00 29.38  ? 107 TYR A HB3  1 
ATOM   1767 H  HD1  . TYR A 1 110 ? -3.397  -8.285  22.698 1.00 38.96  ? 107 TYR A HD1  1 
ATOM   1768 H  HD2  . TYR A 1 110 ? -0.170  -6.288  21.414 1.00 34.04  ? 107 TYR A HD2  1 
ATOM   1769 H  HE1  . TYR A 1 110 ? -2.489  -8.415  24.808 1.00 43.22  ? 107 TYR A HE1  1 
ATOM   1770 H  HE2  . TYR A 1 110 ? 0.808   -6.559  23.536 1.00 37.16  ? 107 TYR A HE2  1 
ATOM   1771 H  HH   . TYR A 1 110 ? -0.017  -6.915  25.946 1.00 49.30  ? 107 TYR A HH   1 
ATOM   1772 N  N    . PRO A 1 111 ? -4.731  -8.269  18.533 1.00 28.04  ? 108 PRO A N    1 
ATOM   1773 C  CA   . PRO A 1 111 ? -5.624  -8.061  17.369 1.00 26.06  ? 108 PRO A CA   1 
ATOM   1774 C  C    . PRO A 1 111 ? -5.832  -6.588  17.037 1.00 25.94  ? 108 PRO A C    1 
ATOM   1775 O  O    . PRO A 1 111 ? -6.938  -6.050  17.103 1.00 32.42  ? 108 PRO A O    1 
ATOM   1776 C  CB   . PRO A 1 111 ? -6.917  -8.755  17.824 1.00 34.55  ? 108 PRO A CB   1 
ATOM   1777 C  CG   . PRO A 1 111 ? -6.949  -8.487  19.324 1.00 36.52  ? 108 PRO A CG   1 
ATOM   1778 C  CD   . PRO A 1 111 ? -5.498  -8.612  19.760 1.00 33.21  ? 108 PRO A CD   1 
ATOM   1779 H  HA   . PRO A 1 111 ? -5.267  -8.516  16.590 1.00 31.31  ? 108 PRO A HA   1 
ATOM   1780 H  HB2  . PRO A 1 111 ? -7.684  -8.363  17.379 1.00 41.49  ? 108 PRO A HB2  1 
ATOM   1781 H  HB3  . PRO A 1 111 ? -6.873  -9.705  17.636 1.00 41.49  ? 108 PRO A HB3  1 
ATOM   1782 H  HG2  . PRO A 1 111 ? -7.290  -7.596  19.497 1.00 43.86  ? 108 PRO A HG2  1 
ATOM   1783 H  HG3  . PRO A 1 111 ? -7.504  -9.147  19.769 1.00 43.86  ? 108 PRO A HG3  1 
ATOM   1784 H  HD2  . PRO A 1 111 ? -5.299  -7.987  20.475 1.00 39.89  ? 108 PRO A HD2  1 
ATOM   1785 H  HD3  . PRO A 1 111 ? -5.302  -9.517  20.046 1.00 39.89  ? 108 PRO A HD3  1 
ATOM   1786 N  N    . LEU A 1 112 ? -4.748  -5.926  16.688 1.00 24.43  ? 109 LEU A N    1 
ATOM   1787 C  CA   . LEU A 1 112 ? -4.809  -4.564  16.186 1.00 22.41  ? 109 LEU A CA   1 
ATOM   1788 C  C    . LEU A 1 112 ? -5.632  -4.499  14.903 1.00 27.19  ? 109 LEU A C    1 
ATOM   1789 O  O    . LEU A 1 112 ? -5.634  -5.434  14.097 1.00 25.76  ? 109 LEU A O    1 
ATOM   1790 C  CB   . LEU A 1 112 ? -3.396  -4.046  15.919 1.00 24.35  ? 109 LEU A CB   1 
ATOM   1791 C  CG   . LEU A 1 112 ? -2.426  -4.033  17.101 1.00 27.63  ? 109 LEU A CG   1 
ATOM   1792 C  CD1  . LEU A 1 112 ? -1.110  -3.451  16.680 1.00 27.02  ? 109 LEU A CD1  1 
ATOM   1793 C  CD2  . LEU A 1 112 ? -3.016  -3.201  18.232 1.00 30.69  ? 109 LEU A CD2  1 
ATOM   1794 H  H    . LEU A 1 112 ? -3.950  -6.244  16.732 1.00 29.35  ? 109 LEU A H    1 
ATOM   1795 H  HA   . LEU A 1 112 ? -5.232  -3.994  16.847 1.00 26.93  ? 109 LEU A HA   1 
ATOM   1796 H  HB2  . LEU A 1 112 ? -2.998  -4.604  15.233 1.00 29.26  ? 109 LEU A HB2  1 
ATOM   1797 H  HB3  . LEU A 1 112 ? -3.468  -3.132  15.603 1.00 29.26  ? 109 LEU A HB3  1 
ATOM   1798 H  HG   . LEU A 1 112 ? -2.279  -4.939  17.413 1.00 33.19  ? 109 LEU A HG   1 
ATOM   1799 H  HD11 . LEU A 1 112 ? -0.668  -3.074  17.457 1.00 32.45  ? 109 LEU A HD11 1 
ATOM   1800 H  HD12 . LEU A 1 112 ? -0.562  -4.154  16.297 1.00 32.45  ? 109 LEU A HD12 1 
ATOM   1801 H  HD13 . LEU A 1 112 ? -1.268  -2.758  16.020 1.00 32.45  ? 109 LEU A HD13 1 
ATOM   1802 H  HD21 . LEU A 1 112 ? -2.373  -3.152  18.957 1.00 36.86  ? 109 LEU A HD21 1 
ATOM   1803 H  HD22 . LEU A 1 112 ? -3.209  -2.309  17.902 1.00 36.86  ? 109 LEU A HD22 1 
ATOM   1804 H  HD23 . LEU A 1 112 ? -3.833  -3.622  18.542 1.00 36.86  ? 109 LEU A HD23 1 
ATOM   1805 N  N    A LYS A 1 113 ? -6.310  -3.364  14.704 0.55 24.06  ? 110 LYS A N    1 
ATOM   1806 N  N    B LYS A 1 113 ? -6.321  -3.373  14.707 0.45 24.09  ? 110 LYS A N    1 
ATOM   1807 C  CA   A LYS A 1 113 ? -7.172  -3.213  13.534 0.55 25.15  ? 110 LYS A CA   1 
ATOM   1808 C  CA   B LYS A 1 113 ? -7.171  -3.229  13.528 0.45 25.22  ? 110 LYS A CA   1 
ATOM   1809 C  C    A LYS A 1 113 ? -6.370  -2.900  12.279 0.55 25.45  ? 110 LYS A C    1 
ATOM   1810 C  C    B LYS A 1 113 ? -6.352  -2.922  12.281 0.45 25.52  ? 110 LYS A C    1 
ATOM   1811 O  O    A LYS A 1 113 ? -6.655  -3.446  11.210 0.55 26.61  ? 110 LYS A O    1 
ATOM   1812 O  O    B LYS A 1 113 ? -6.602  -3.499  11.219 0.45 26.62  ? 110 LYS A O    1 
ATOM   1813 C  CB   A LYS A 1 113 ? -8.221  -2.121  13.750 0.55 27.61  ? 110 LYS A CB   1 
ATOM   1814 C  CB   B LYS A 1 113 ? -8.229  -2.145  13.737 0.45 27.66  ? 110 LYS A CB   1 
ATOM   1815 C  CG   A LYS A 1 113 ? -9.277  -2.481  14.766 0.55 33.06  ? 110 LYS A CG   1 
ATOM   1816 C  CG   B LYS A 1 113 ? -9.225  -2.469  14.830 0.45 33.03  ? 110 LYS A CG   1 
ATOM   1817 C  CD   A LYS A 1 113 ? -10.217 -3.559  14.230 0.55 38.33  ? 110 LYS A CD   1 
ATOM   1818 C  CD   B LYS A 1 113 ? -10.053 -3.702  14.467 0.45 38.76  ? 110 LYS A CD   1 
ATOM   1819 C  CE   A LYS A 1 113 ? -11.252 -3.984  15.278 0.55 46.11  ? 110 LYS A CE   1 
ATOM   1820 C  CE   B LYS A 1 113 ? -11.150 -3.986  15.493 0.45 45.78  ? 110 LYS A CE   1 
ATOM   1821 N  NZ   A LYS A 1 113 ? -10.683 -4.897  16.326 0.55 53.38  ? 110 LYS A NZ   1 
ATOM   1822 N  NZ   B LYS A 1 113 ? -11.722 -5.365  15.339 0.45 45.41  ? 110 LYS A NZ   1 
ATOM   1823 H  H    A LYS A 1 113 ? -6.287  -2.679  15.224 0.55 28.91  ? 110 LYS A H    1 
ATOM   1824 H  H    B LYS A 1 113 ? -6.314  -2.692  15.232 0.45 28.95  ? 110 LYS A H    1 
ATOM   1825 H  HA   A LYS A 1 113 ? -7.640  -4.054  13.409 0.55 30.21  ? 110 LYS A HA   1 
ATOM   1826 H  HA   B LYS A 1 113 ? -7.637  -4.069  13.394 0.45 30.30  ? 110 LYS A HA   1 
ATOM   1827 H  HB2  A LYS A 1 113 ? -7.775  -1.318  14.060 0.55 33.17  ? 110 LYS A HB2  1 
ATOM   1828 H  HB2  B LYS A 1 113 ? -7.784  -1.317  13.978 0.45 33.22  ? 110 LYS A HB2  1 
ATOM   1829 H  HB3  A LYS A 1 113 ? -8.669  -1.949  12.907 0.55 33.17  ? 110 LYS A HB3  1 
ATOM   1830 H  HB3  B LYS A 1 113 ? -8.723  -2.028  12.911 0.45 33.22  ? 110 LYS A HB3  1 
ATOM   1831 H  HG2  A LYS A 1 113 ? -8.850  -2.820  15.569 0.55 39.70  ? 110 LYS A HG2  1 
ATOM   1832 H  HG2  B LYS A 1 113 ? -8.751  -2.650  15.657 0.45 39.67  ? 110 LYS A HG2  1 
ATOM   1833 H  HG3  A LYS A 1 113 ? -9.803  -1.694  14.977 0.55 39.70  ? 110 LYS A HG3  1 
ATOM   1834 H  HG3  B LYS A 1 113 ? -9.828  -1.719  14.951 0.45 39.67  ? 110 LYS A HG3  1 
ATOM   1835 H  HD2  A LYS A 1 113 ? -10.692 -3.214  13.457 0.55 46.04  ? 110 LYS A HD2  1 
ATOM   1836 H  HD2  B LYS A 1 113 ? -10.476 -3.559  13.606 0.45 46.55  ? 110 LYS A HD2  1 
ATOM   1837 H  HD3  A LYS A 1 113 ? -9.699  -4.340  13.980 0.55 46.04  ? 110 LYS A HD3  1 
ATOM   1838 H  HD3  B LYS A 1 113 ? -9.471  -4.476  14.426 0.45 46.55  ? 110 LYS A HD3  1 
ATOM   1839 H  HE2  A LYS A 1 113 ? -11.593 -3.193  15.724 0.55 55.37  ? 110 LYS A HE2  1 
ATOM   1840 H  HE2  B LYS A 1 113 ? -10.779 -3.910  16.386 0.45 54.97  ? 110 LYS A HE2  1 
ATOM   1841 H  HE3  A LYS A 1 113 ? -11.976 -4.453  14.835 0.55 55.37  ? 110 LYS A HE3  1 
ATOM   1842 H  HE3  B LYS A 1 113 ? -11.869 -3.345  15.377 0.45 54.97  ? 110 LYS A HE3  1 
ATOM   1843 H  HZ1  A LYS A 1 113 ? -11.313 -5.115  16.915 0.55 64.09  ? 110 LYS A HZ1  1 
ATOM   1844 H  HZ1  B LYS A 1 113 ? -12.358 -5.500  15.947 0.45 54.52  ? 110 LYS A HZ1  1 
ATOM   1845 H  HZ2  A LYS A 1 113 ? -10.372 -5.640  15.947 0.55 64.09  ? 110 LYS A HZ2  1 
ATOM   1846 H  HZ2  B LYS A 1 113 ? -12.073 -5.460  14.527 0.45 54.52  ? 110 LYS A HZ2  1 
ATOM   1847 H  HZ3  A LYS A 1 113 ? -10.016 -4.491  16.754 0.55 64.09  ? 110 LYS A HZ3  1 
ATOM   1848 H  HZ3  B LYS A 1 113 ? -11.082 -5.974  15.450 0.45 54.52  ? 110 LYS A HZ3  1 
ATOM   1849 N  N    . ARG A 1 114 ? -5.373  -2.032  12.397 1.00 25.66  ? 111 ARG A N    1 
ATOM   1850 C  CA   . ARG A 1 114 ? -4.468  -1.732  11.294 1.00 25.79  ? 111 ARG A CA   1 
ATOM   1851 C  C    . ARG A 1 114 ? -3.243  -1.059  11.863 1.00 24.74  ? 111 ARG A C    1 
ATOM   1852 O  O    . ARG A 1 114 ? -3.244  -0.565  13.012 1.00 24.32  ? 111 ARG A O    1 
ATOM   1853 C  CB   . ARG A 1 114 ? -5.144  -0.893  10.194 1.00 31.92  ? 111 ARG A CB   1 
ATOM   1854 C  CG   . ARG A 1 114 ? -5.838  0.312   10.598 1.00 33.92  ? 111 ARG A CG   1 
ATOM   1855 C  CD   . ARG A 1 114 ? -6.511  1.045   9.345  1.00 34.98  ? 111 ARG A CD   1 
ATOM   1856 N  NE   . ARG A 1 114 ? -7.440  0.212   8.582  1.00 40.25  ? 111 ARG A NE   1 
ATOM   1857 C  CZ   . ARG A 1 114 ? -7.510  0.150   7.252  1.00 38.42  ? 111 ARG A CZ   1 
ATOM   1858 N  NH1  . ARG A 1 114 ? -6.809  0.964   6.468  1.00 37.06  ? 111 ARG A NH1  1 
ATOM   1859 N  NH2  . ARG A 1 114 ? -8.297  -0.757  6.683  1.00 44.56  ? 111 ARG A NH2  1 
ATOM   1860 H  H    A ARG A 1 114 ? -5.196  -1.596  13.117 0.55 30.83  ? 111 ARG A H    1 
ATOM   1861 H  H    B ARG A 1 114 ? -5.209  -1.584  13.112 0.45 30.83  ? 111 ARG A H    1 
ATOM   1862 H  HA   . ARG A 1 114 ? -4.181  -2.555  10.868 1.00 30.98  ? 111 ARG A HA   1 
ATOM   1863 H  HB2  . ARG A 1 114 ? -4.458  -0.622  9.563  1.00 38.34  ? 111 ARG A HB2  1 
ATOM   1864 H  HB3  . ARG A 1 114 ? -5.797  -1.457  9.751  1.00 38.34  ? 111 ARG A HB3  1 
ATOM   1865 H  HG2  . ARG A 1 114 ? -6.538  0.084   11.230 1.00 40.74  ? 111 ARG A HG2  1 
ATOM   1866 H  HG3  . ARG A 1 114 ? -5.208  0.925   11.008 1.00 40.74  ? 111 ARG A HG3  1 
ATOM   1867 H  HD2  . ARG A 1 114 ? -7.005  1.816   9.665  1.00 42.01  ? 111 ARG A HD2  1 
ATOM   1868 H  HD3  . ARG A 1 114 ? -5.809  1.330   8.739  1.00 42.01  ? 111 ARG A HD3  1 
ATOM   1869 H  HE   . ARG A 1 114 ? -7.986  -0.280  9.029  1.00 48.34  ? 111 ARG A HE   1 
ATOM   1870 H  HH11 . ARG A 1 114 ? -6.289  1.555   6.816  1.00 44.51  ? 111 ARG A HH11 1 
ATOM   1871 H  HH12 . ARG A 1 114 ? -6.875  0.900   5.613  1.00 44.51  ? 111 ARG A HH12 1 
ATOM   1872 H  HH21 . ARG A 1 114 ? -8.755  -1.296  7.172  1.00 53.51  ? 111 ARG A HH21 1 
ATOM   1873 H  HH22 . ARG A 1 114 ? -8.349  -0.804  5.826  1.00 53.51  ? 111 ARG A HH22 1 
ATOM   1874 N  N    . ILE A 1 115 ? -2.168  -1.088  11.083 1.00 21.33  ? 112 ILE A N    1 
ATOM   1875 C  CA   . ILE A 1 115 ? -0.887  -0.571  11.564 1.00 20.30  ? 112 ILE A CA   1 
ATOM   1876 C  C    . ILE A 1 115 ? -0.235  0.285   10.476 1.00 21.72  ? 112 ILE A C    1 
ATOM   1877 O  O    . ILE A 1 115 ? -0.358  -0.005  9.283  1.00 21.55  ? 112 ILE A O    1 
ATOM   1878 C  CB   . ILE A 1 115 ? 0.095   -1.694  11.969 1.00 23.33  ? 112 ILE A CB   1 
ATOM   1879 C  CG1  . ILE A 1 115 ? 0.413   -2.592  10.758 1.00 27.37  ? 112 ILE A CG1  1 
ATOM   1880 C  CG2  . ILE A 1 115 ? -0.418  -2.429  13.170 1.00 23.39  ? 112 ILE A CG2  1 
ATOM   1881 C  CD1  . ILE A 1 115 ? 1.518   -3.604  11.075 1.00 28.19  ? 112 ILE A CD1  1 
ATOM   1882 H  H    . ILE A 1 115 ? -2.153  -1.399  10.281 1.00 25.63  ? 112 ILE A H    1 
ATOM   1883 H  HA   . ILE A 1 115 ? -1.077  -0.016  12.336 1.00 24.39  ? 112 ILE A HA   1 
ATOM   1884 H  HB   . ILE A 1 115 ? 0.944   -1.309  12.239 1.00 28.03  ? 112 ILE A HB   1 
ATOM   1885 H  HG12 . ILE A 1 115 ? -0.386  -3.082  10.506 1.00 32.88  ? 112 ILE A HG12 1 
ATOM   1886 H  HG13 . ILE A 1 115 ? 0.710   -2.038  10.019 1.00 32.88  ? 112 ILE A HG13 1 
ATOM   1887 H  HG21 . ILE A 1 115 ? 0.237   -3.092  13.439 1.00 28.10  ? 112 ILE A HG21 1 
ATOM   1888 H  HG22 . ILE A 1 115 ? -0.561  -1.795  13.891 1.00 28.10  ? 112 ILE A HG22 1 
ATOM   1889 H  HG23 . ILE A 1 115 ? -1.254  -2.864  12.941 1.00 28.10  ? 112 ILE A HG23 1 
ATOM   1890 H  HD11 . ILE A 1 115 ? 1.759   -4.075  10.261 1.00 33.87  ? 112 ILE A HD11 1 
ATOM   1891 H  HD12 . ILE A 1 115 ? 2.290   -3.131  11.424 1.00 33.87  ? 112 ILE A HD12 1 
ATOM   1892 H  HD13 . ILE A 1 115 ? 1.190   -4.234  11.736 1.00 33.87  ? 112 ILE A HD13 1 
ATOM   1893 N  N    . ALA A 1 116 ? 0.479   1.326   10.896 1.00 22.60  ? 113 ALA A N    1 
ATOM   1894 C  CA   . ALA A 1 116 ? 1.259   2.166   9.985  1.00 25.11  ? 113 ALA A CA   1 
ATOM   1895 C  C    . ALA A 1 116 ? 2.652   2.295   10.571 1.00 23.90  ? 113 ALA A C    1 
ATOM   1896 O  O    . ALA A 1 116 ? 2.823   2.705   11.717 1.00 23.49  ? 113 ALA A O    1 
ATOM   1897 C  CB   . ALA A 1 116 ? 0.594   3.527   9.790  1.00 23.23  ? 113 ALA A CB   1 
ATOM   1898 H  H    . ALA A 1 116 ? 0.529   1.571   11.718 1.00 27.15  ? 113 ALA A H    1 
ATOM   1899 H  HA   . ALA A 1 116 ? 1.331   1.755   9.110  1.00 30.17  ? 113 ALA A HA   1 
ATOM   1900 H  HB1  . ALA A 1 116 ? 1.145   4.066   9.200  1.00 27.91  ? 113 ALA A HB1  1 
ATOM   1901 H  HB2  . ALA A 1 116 ? -0.283  3.397   9.396  1.00 27.91  ? 113 ALA A HB2  1 
ATOM   1902 H  HB3  . ALA A 1 116 ? 0.508   3.964   10.652 1.00 27.91  ? 113 ALA A HB3  1 
ATOM   1903 N  N    . VAL A 1 117 ? 3.642   1.907   9.800  1.00 20.60  ? 114 VAL A N    1 
ATOM   1904 C  CA   . VAL A 1 117 ? 5.018   1.756   10.262 1.00 19.10  ? 114 VAL A CA   1 
ATOM   1905 C  C    . VAL A 1 117 ? 5.892   2.732   9.476  1.00 22.26  ? 114 VAL A C    1 
ATOM   1906 O  O    . VAL A 1 117 ? 5.953   2.655   8.242  1.00 24.37  ? 114 VAL A O    1 
ATOM   1907 C  CB   . VAL A 1 117 ? 5.488   0.309   10.063 1.00 24.77  ? 114 VAL A CB   1 
ATOM   1908 C  CG1  . VAL A 1 117 ? 6.953   0.176   10.415 1.00 28.02  ? 114 VAL A CG1  1 
ATOM   1909 C  CG2  . VAL A 1 117 ? 4.588   -0.629  10.911 1.00 29.28  ? 114 VAL A CG2  1 
ATOM   1910 H  H    . VAL A 1 117 ? 3.546   1.714   8.968  1.00 24.75  ? 114 VAL A H    1 
ATOM   1911 H  HA   . VAL A 1 117 ? 5.087   1.992   11.200 1.00 22.95  ? 114 VAL A HA   1 
ATOM   1912 H  HB   . VAL A 1 117 ? 5.407   0.047   9.133  1.00 29.76  ? 114 VAL A HB   1 
ATOM   1913 H  HG11 . VAL A 1 117 ? 7.172   -0.764  10.506 1.00 33.66  ? 114 VAL A HG11 1 
ATOM   1914 H  HG12 . VAL A 1 117 ? 7.485   0.573   9.708  1.00 33.66  ? 114 VAL A HG12 1 
ATOM   1915 H  HG13 . VAL A 1 117 ? 7.120   0.637   11.253 1.00 33.66  ? 114 VAL A HG13 1 
ATOM   1916 H  HG21 . VAL A 1 117 ? 4.902   -1.542  10.813 1.00 35.17  ? 114 VAL A HG21 1 
ATOM   1917 H  HG22 . VAL A 1 117 ? 4.639   -0.360  11.842 1.00 35.17  ? 114 VAL A HG22 1 
ATOM   1918 H  HG23 . VAL A 1 117 ? 3.673   -0.559  10.596 1.00 35.17  ? 114 VAL A HG23 1 
ATOM   1919 N  N    . MET A 1 118 ? 6.627   3.592   10.180 1.00 21.69  ? 115 MET A N    1 
ATOM   1920 C  CA   . MET A 1 118 ? 7.466   4.616   9.552  1.00 23.41  ? 115 MET A CA   1 
ATOM   1921 C  C    . MET A 1 118 ? 8.929   4.372   9.902  1.00 26.94  ? 115 MET A C    1 
ATOM   1922 O  O    . MET A 1 118 ? 9.282   4.305   11.078 1.00 24.97  ? 115 MET A O    1 
ATOM   1923 C  CB   . MET A 1 118 ? 7.036   6.000   10.109 1.00 24.24  ? 115 MET A CB   1 
ATOM   1924 C  CG   . MET A 1 118 ? 5.669   6.464   9.650  1.00 26.37  ? 115 MET A CG   1 
ATOM   1925 S  SD   . MET A 1 118 ? 5.242   8.022   10.498 1.00 28.78  ? 115 MET A SD   1 
ATOM   1926 C  CE   . MET A 1 118 ? 4.227   7.458   11.814 1.00 33.16  ? 115 MET A CE   1 
ATOM   1927 H  H    . MET A 1 118 ? 6.658   3.603   11.039 1.00 26.06  ? 115 MET A H    1 
ATOM   1928 H  HA   . MET A 1 118 ? 7.371   4.586   8.587  1.00 28.13  ? 115 MET A HA   1 
ATOM   1929 H  HB2  . MET A 1 118 ? 7.019   5.951   11.077 1.00 29.12  ? 115 MET A HB2  1 
ATOM   1930 H  HB3  . MET A 1 118 ? 7.683   6.663   9.821  1.00 29.12  ? 115 MET A HB3  1 
ATOM   1931 H  HG2  . MET A 1 118 ? 5.679   6.620   8.693  1.00 31.68  ? 115 MET A HG2  1 
ATOM   1932 H  HG3  . MET A 1 118 ? 5.004   5.794   9.870  1.00 31.68  ? 115 MET A HG3  1 
ATOM   1933 H  HE1  . MET A 1 118 ? 3.949   8.220   12.347 1.00 39.83  ? 115 MET A HE1  1 
ATOM   1934 H  HE2  . MET A 1 118 ? 3.450   7.011   11.445 1.00 39.83  ? 115 MET A HE2  1 
ATOM   1935 H  HE3  . MET A 1 118 ? 4.735   6.839   12.362 1.00 39.83  ? 115 MET A HE3  1 
ATOM   1936 N  N    . SER A 1 119 ? 9.783   4.307   8.878  1.00 23.04  ? 116 SER A N    1 
ATOM   1937 C  CA   . SER A 1 119 ? 11.249  4.291   9.070  1.00 24.79  ? 116 SER A CA   1 
ATOM   1938 C  C    . SER A 1 119 ? 11.731  3.163   9.976  1.00 24.74  ? 116 SER A C    1 
ATOM   1939 O  O    . SER A 1 119 ? 12.626  3.340   10.804 1.00 27.13  ? 116 SER A O    1 
ATOM   1940 C  CB   . SER A 1 119 ? 11.736  5.642   9.609  1.00 30.85  ? 116 SER A CB   1 
ATOM   1941 O  OG   . SER A 1 119 ? 11.283  6.673   8.750  1.00 30.73  ? 116 SER A OG   1 
ATOM   1942 H  H    . SER A 1 119 ? 9.542   4.270   8.053  1.00 27.68  ? 116 SER A H    1 
ATOM   1943 H  HA   . SER A 1 119 ? 11.644  4.125   8.199  1.00 29.78  ? 116 SER A HA   1 
ATOM   1944 H  HB2  . SER A 1 119 ? 11.377  5.782   10.499 1.00 37.06  ? 116 SER A HB2  1 
ATOM   1945 H  HB3  . SER A 1 119 ? 12.705  5.647   9.637  1.00 37.06  ? 116 SER A HB3  1 
ATOM   1946 H  HG   . SER A 1 119 ? 11.674  7.393   8.935  1.00 36.91  ? 116 SER A HG   1 
ATOM   1947 N  N    . ALA A 1 120 ? 11.120  1.999   9.838  1.00 24.99  ? 117 ALA A N    1 
ATOM   1948 C  CA   . ALA A 1 120 ? 11.575  0.840   10.614 1.00 23.21  ? 117 ALA A CA   1 
ATOM   1949 C  C    . ALA A 1 120 ? 12.809  0.213   9.967  1.00 25.52  ? 117 ALA A C    1 
ATOM   1950 O  O    . ALA A 1 120 ? 12.819  -0.011  8.749  1.00 27.40  ? 117 ALA A O    1 
ATOM   1951 C  CB   . ALA A 1 120 ? 10.468  -0.191  10.684 1.00 26.68  ? 117 ALA A CB   1 
ATOM   1952 H  H    . ALA A 1 120 ? 10.454  1.848   9.316  1.00 30.02  ? 117 ALA A H    1 
ATOM   1953 H  HA   . ALA A 1 120 ? 11.812  1.123   11.511 1.00 27.89  ? 117 ALA A HA   1 
ATOM   1954 H  HB1  . ALA A 1 120 ? 10.769  -0.942  11.219 1.00 32.04  ? 117 ALA A HB1  1 
ATOM   1955 H  HB2  . ALA A 1 120 ? 9.686   0.213   11.092 1.00 32.04  ? 117 ALA A HB2  1 
ATOM   1956 H  HB3  . ALA A 1 120 ? 10.256  -0.489  9.786  1.00 32.04  ? 117 ALA A HB3  1 
ATOM   1957 N  N    . PRO A 1 121 ? 13.836  -0.120  10.739 1.00 25.36  ? 118 PRO A N    1 
ATOM   1958 C  CA   . PRO A 1 121 ? 14.997  -0.840  10.203 1.00 27.54  ? 118 PRO A CA   1 
ATOM   1959 C  C    . PRO A 1 121 ? 14.785  -2.345  10.283 1.00 30.90  ? 118 PRO A C    1 
ATOM   1960 O  O    . PRO A 1 121 ? 14.098  -2.856  11.170 1.00 31.06  ? 118 PRO A O    1 
ATOM   1961 C  CB   . PRO A 1 121 ? 16.132  -0.411  11.146 1.00 29.75  ? 118 PRO A CB   1 
ATOM   1962 C  CG   . PRO A 1 121 ? 15.435  -0.268  12.486 1.00 31.78  ? 118 PRO A CG   1 
ATOM   1963 C  CD   . PRO A 1 121 ? 14.030  0.256   12.162 1.00 27.57  ? 118 PRO A CD   1 
ATOM   1964 H  HA   . PRO A 1 121 ? 15.207  -0.567  9.296  1.00 33.08  ? 118 PRO A HA   1 
ATOM   1965 H  HB2  . PRO A 1 121 ? 16.820  -1.094  11.178 1.00 35.74  ? 118 PRO A HB2  1 
ATOM   1966 H  HB3  . PRO A 1 121 ? 16.513  0.432   10.854 1.00 35.74  ? 118 PRO A HB3  1 
ATOM   1967 H  HG2  . PRO A 1 121 ? 15.388  -1.131  12.926 1.00 38.17  ? 118 PRO A HG2  1 
ATOM   1968 H  HG3  . PRO A 1 121 ? 15.918  0.362   13.043 1.00 38.17  ? 118 PRO A HG3  1 
ATOM   1969 H  HD2  . PRO A 1 121 ? 13.365  -0.170  12.725 1.00 33.12  ? 118 PRO A HD2  1 
ATOM   1970 H  HD3  . PRO A 1 121 ? 13.989  1.219   12.272 1.00 33.12  ? 118 PRO A HD3  1 
ATOM   1971 N  N    . LYS A 1 122 ? 15.404  -3.063  9.350  1.00 29.95  ? 119 LYS A N    1 
ATOM   1972 C  CA   . LYS A 1 122 ? 15.329  -4.521  9.406  1.00 30.52  ? 119 LYS A CA   1 
ATOM   1973 C  C    . LYS A 1 122 ? 16.481  -5.099  10.222 1.00 34.44  ? 119 LYS A C    1 
ATOM   1974 O  O    . LYS A 1 122 ? 16.413  -6.268  10.621 1.00 39.64  ? 119 LYS A O    1 
ATOM   1975 C  CB   . LYS A 1 122 ? 15.289  -5.142  8.007  1.00 35.37  ? 119 LYS A CB   1 
ATOM   1976 C  CG   . LYS A 1 122 ? 16.551  -5.269  7.250  1.00 42.12  ? 119 LYS A CG   1 
ATOM   1977 C  CD   . LYS A 1 122 ? 16.238  -5.869  5.841  1.00 46.52  ? 119 LYS A CD   1 
ATOM   1978 C  CE   . LYS A 1 122 ? 17.410  -6.653  5.283  1.00 56.25  ? 119 LYS A CE   1 
ATOM   1979 N  NZ   . LYS A 1 122 ? 17.735  -7.839  6.127  1.00 84.83  ? 119 LYS A NZ   1 
ATOM   1980 H  H    . LYS A 1 122 ? 15.860  -2.741  8.695  1.00 35.97  ? 119 LYS A H    1 
ATOM   1981 H  HA   . LYS A 1 122 ? 14.493  -4.786  9.820  1.00 36.66  ? 119 LYS A HA   1 
ATOM   1982 H  HB2  . LYS A 1 122 ? 14.930  -6.039  8.096  1.00 42.48  ? 119 LYS A HB2  1 
ATOM   1983 H  HB3  . LYS A 1 122 ? 14.696  -4.599  7.464  1.00 42.48  ? 119 LYS A HB3  1 
ATOM   1984 H  HG2  . LYS A 1 122 ? 16.960  -4.397  7.137  1.00 50.57  ? 119 LYS A HG2  1 
ATOM   1985 H  HG3  . LYS A 1 122 ? 17.160  -5.863  7.717  1.00 50.57  ? 119 LYS A HG3  1 
ATOM   1986 H  HD2  . LYS A 1 122 ? 15.479  -6.469  5.911  1.00 55.86  ? 119 LYS A HD2  1 
ATOM   1987 H  HD3  . LYS A 1 122 ? 16.036  -5.148  5.225  1.00 55.86  ? 119 LYS A HD3  1 
ATOM   1988 H  HE2  . LYS A 1 122 ? 17.190  -6.966  4.392  1.00 67.53  ? 119 LYS A HE2  1 
ATOM   1989 H  HE3  . LYS A 1 122 ? 18.192  -6.080  5.250  1.00 67.53  ? 119 LYS A HE3  1 
ATOM   1990 H  HZ1  . LYS A 1 122 ? 18.420  -8.285  5.774  1.00 101.82 ? 119 LYS A HZ1  1 
ATOM   1991 H  HZ2  . LYS A 1 122 ? 17.954  -7.576  6.949  1.00 101.82 ? 119 LYS A HZ2  1 
ATOM   1992 H  HZ3  . LYS A 1 122 ? 17.031  -8.381  6.175  1.00 101.82 ? 119 LYS A HZ3  1 
ATOM   1993 N  N    . GLU A 1 123 ? 17.532  -4.308  10.455 1.00 33.16  ? 120 GLU A N    1 
ATOM   1994 C  CA   . GLU A 1 123 ? 18.635  -4.674  11.326 1.00 42.22  ? 120 GLU A CA   1 
ATOM   1995 C  C    . GLU A 1 123 ? 19.359  -3.394  11.741 1.00 44.33  ? 120 GLU A C    1 
ATOM   1996 O  O    . GLU A 1 123 ? 19.233  -2.354  11.096 1.00 40.06  ? 120 GLU A O    1 
ATOM   1997 C  CB   . GLU A 1 123 ? 19.638  -5.633  10.668 1.00 44.03  ? 120 GLU A CB   1 
ATOM   1998 C  CG   . GLU A 1 123 ? 20.499  -5.034  9.557  1.00 60.57  ? 120 GLU A CG   1 
ATOM   1999 C  CD   . GLU A 1 123 ? 20.212  -5.606  8.186  1.00 72.60  ? 120 GLU A CD   1 
ATOM   2000 O  OE1  . GLU A 1 123 ? 19.247  -6.381  8.037  1.00 81.60  ? 120 GLU A OE1  1 
ATOM   2001 O  OE2  . GLU A 1 123 ? 20.962  -5.282  7.245  1.00 90.17  ? 120 GLU A OE2  1 
ATOM   2002 H  H    . GLU A 1 123 ? 17.628  -3.529  10.104 1.00 39.82  ? 120 GLU A H    1 
ATOM   2003 H  HA   . GLU A 1 123 ? 18.266  -5.120  12.105 1.00 50.70  ? 120 GLU A HA   1 
ATOM   2004 H  HB2  . GLU A 1 123 ? 20.240  -5.960  11.353 1.00 52.87  ? 120 GLU A HB2  1 
ATOM   2005 H  HB3  . GLU A 1 123 ? 19.143  -6.371  10.280 1.00 52.87  ? 120 GLU A HB3  1 
ATOM   2006 H  HG2  . GLU A 1 123 ? 20.337  -4.078  9.517  1.00 72.71  ? 120 GLU A HG2  1 
ATOM   2007 H  HG3  . GLU A 1 123 ? 21.432  -5.204  9.759  1.00 72.71  ? 120 GLU A HG3  1 
ATOM   2008 N  N    . LYS A 1 124 ? 20.146  -3.491  12.807 1.00 42.23  ? 121 LYS A N    1 
ATOM   2009 C  CA   . LYS A 1 124 ? 20.969  -2.375  13.259 1.00 48.98  ? 121 LYS A CA   1 
ATOM   2010 C  C    . LYS A 1 124 ? 22.306  -2.936  13.716 1.00 55.25  ? 121 LYS A C    1 
ATOM   2011 O  O    . LYS A 1 124 ? 22.353  -3.974  14.379 1.00 47.35  ? 121 LYS A O    1 
ATOM   2012 C  CB   . LYS A 1 124 ? 20.299  -1.607  14.411 1.00 48.50  ? 121 LYS A CB   1 
ATOM   2013 C  CG   . LYS A 1 124 ? 19.131  -0.694  13.986 1.00 49.65  ? 121 LYS A CG   1 
ATOM   2014 C  CD   . LYS A 1 124 ? 19.517  0.367   12.946 1.00 71.23  ? 121 LYS A CD   1 
ATOM   2015 C  CE   . LYS A 1 124 ? 19.763  1.736   13.583 1.00 70.65  ? 121 LYS A CE   1 
ATOM   2016 N  NZ   . LYS A 1 124 ? 20.064  2.756   12.534 1.00 74.70  ? 121 LYS A NZ   1 
ATOM   2017 H  H    . LYS A 1 124 ? 20.222  -4.199  13.289 1.00 50.71  ? 121 LYS A H    1 
ATOM   2018 H  HA   . LYS A 1 124 ? 21.115  -1.748  12.534 1.00 58.81  ? 121 LYS A HA   1 
ATOM   2019 H  HB2  . LYS A 1 124 ? 19.950  -2.250  15.048 1.00 58.24  ? 121 LYS A HB2  1 
ATOM   2020 H  HB3  . LYS A 1 124 ? 20.967  -1.047  14.837 1.00 58.24  ? 121 LYS A HB3  1 
ATOM   2021 H  HG2  . LYS A 1 124 ? 18.431  -1.243  13.601 1.00 59.61  ? 121 LYS A HG2  1 
ATOM   2022 H  HG3  . LYS A 1 124 ? 18.797  -0.230  14.769 1.00 59.61  ? 121 LYS A HG3  1 
ATOM   2023 H  HD2  . LYS A 1 124 ? 20.332  0.092   12.497 1.00 85.51  ? 121 LYS A HD2  1 
ATOM   2024 H  HD3  . LYS A 1 124 ? 18.798  0.458   12.302 1.00 85.51  ? 121 LYS A HD3  1 
ATOM   2025 H  HE2  . LYS A 1 124 ? 18.971  2.015   14.068 1.00 84.81  ? 121 LYS A HE2  1 
ATOM   2026 H  HE3  . LYS A 1 124 ? 20.520  1.681   14.187 1.00 84.81  ? 121 LYS A HE3  1 
ATOM   2027 H  HZ1  . LYS A 1 124 ? 20.213  3.548   12.913 1.00 89.67  ? 121 LYS A HZ1  1 
ATOM   2028 H  HZ2  . LYS A 1 124 ? 20.787  2.516   12.074 1.00 89.67  ? 121 LYS A HZ2  1 
ATOM   2029 H  HZ3  . LYS A 1 124 ? 19.376  2.829   11.974 1.00 89.67  ? 121 LYS A HZ3  1 
ATOM   2030 N  N    . SER A 1 125 ? 23.384  -2.256  13.354 1.00 46.62  ? 122 SER A N    1 
ATOM   2031 C  CA   . SER A 1 125 ? 24.720  -2.625  13.797 1.00 53.70  ? 122 SER A CA   1 
ATOM   2032 C  C    . SER A 1 125 ? 25.036  -2.003  15.158 1.00 51.91  ? 122 SER A C    1 
ATOM   2033 O  O    . SER A 1 125 ? 24.346  -1.096  15.639 1.00 50.70  ? 122 SER A O    1 
ATOM   2034 C  CB   . SER A 1 125 ? 25.765  -2.177  12.773 1.00 53.63  ? 122 SER A CB   1 
ATOM   2035 O  OG   . SER A 1 125 ? 25.840  -0.760  12.736 1.00 51.61  ? 122 SER A OG   1 
ATOM   2036 H  H    . SER A 1 125 ? 23.369  -1.565  12.843 1.00 55.98  ? 122 SER A H    1 
ATOM   2037 H  HA   . SER A 1 125 ? 24.759  -3.591  13.884 1.00 64.48  ? 122 SER A HA   1 
ATOM   2038 H  HB2  . SER A 1 125 ? 26.631  -2.536  13.024 1.00 64.39  ? 122 SER A HB2  1 
ATOM   2039 H  HB3  . SER A 1 125 ? 25.512  -2.505  11.896 1.00 64.39  ? 122 SER A HB3  1 
ATOM   2040 H  HG   . SER A 1 125 ? 26.335  -0.515  12.103 1.00 61.96  ? 122 SER A HG   1 
ATOM   2041 N  N    A ASP A 1 126 ? 26.098  -2.518  15.789 0.42 58.02  ? 123 ASP A N    1 
ATOM   2042 N  N    B ASP A 1 126 ? 26.121  -2.482  15.771 0.58 58.06  ? 123 ASP A N    1 
ATOM   2043 C  CA   A ASP A 1 126 ? 26.591  -1.905  17.019 0.42 59.29  ? 123 ASP A CA   1 
ATOM   2044 C  CA   B ASP A 1 126 ? 26.558  -1.896  17.034 0.58 59.24  ? 123 ASP A CA   1 
ATOM   2045 C  C    A ASP A 1 126 ? 26.971  -0.448  16.783 0.42 61.34  ? 123 ASP A C    1 
ATOM   2046 C  C    B ASP A 1 126 ? 27.053  -0.462  16.846 0.58 61.42  ? 123 ASP A C    1 
ATOM   2047 O  O    A ASP A 1 126 ? 26.523  0.454   17.502 0.42 57.60  ? 123 ASP A O    1 
ATOM   2048 O  O    B ASP A 1 126 ? 26.746  0.415   17.664 0.58 57.37  ? 123 ASP A O    1 
ATOM   2049 C  CB   A ASP A 1 126 ? 27.805  -2.667  17.562 0.42 66.66  ? 123 ASP A CB   1 
ATOM   2050 C  CB   B ASP A 1 126 ? 27.640  -2.774  17.663 0.58 66.84  ? 123 ASP A CB   1 
ATOM   2051 C  CG   A ASP A 1 126 ? 27.509  -4.116  17.869 0.42 63.60  ? 123 ASP A CG   1 
ATOM   2052 C  CG   B ASP A 1 126 ? 28.638  -3.296  16.643 0.58 62.28  ? 123 ASP A CG   1 
ATOM   2053 O  OD1  A ASP A 1 126 ? 26.338  -4.441  18.143 0.42 57.63  ? 123 ASP A OD1  1 
ATOM   2054 O  OD1  B ASP A 1 126 ? 28.800  -2.663  15.579 0.58 62.91  ? 123 ASP A OD1  1 
ATOM   2055 O  OD2  A ASP A 1 126 ? 28.464  -4.929  17.858 0.42 59.74  ? 123 ASP A OD2  1 
ATOM   2056 O  OD2  B ASP A 1 126 ? 29.245  -4.354  16.908 0.58 72.19  ? 123 ASP A OD2  1 
ATOM   2057 H  H    A ASP A 1 126 ? 26.539  -3.209  15.528 0.42 69.66  ? 123 ASP A H    1 
ATOM   2058 H  H    B ASP A 1 126 ? 26.608  -3.130  15.483 0.58 69.71  ? 123 ASP A H    1 
ATOM   2059 H  HA   A ASP A 1 126 ? 25.883  -1.951  17.681 0.42 71.18  ? 123 ASP A HA   1 
ATOM   2060 H  HA   B ASP A 1 126 ? 25.805  -1.863  17.646 0.58 71.13  ? 123 ASP A HA   1 
ATOM   2061 H  HB2  A ASP A 1 126 ? 28.514  -2.641  16.901 0.42 80.03  ? 123 ASP A HB2  1 
ATOM   2062 H  HB2  B ASP A 1 126 ? 28.128  -2.254  18.320 0.58 80.25  ? 123 ASP A HB2  1 
ATOM   2063 H  HB3  A ASP A 1 126 ? 28.101  -2.242  18.383 0.42 80.03  ? 123 ASP A HB3  1 
ATOM   2064 H  HB3  B ASP A 1 126 ? 27.220  -3.537  18.089 0.58 80.25  ? 123 ASP A HB3  1 
ATOM   2065 N  N    . ASP A 1 127 ? 27.822  -0.205  15.782 1.00 59.25  ? 124 ASP A N    1 
ATOM   2066 C  CA   . ASP A 1 127 ? 28.246  1.160   15.478 1.00 64.85  ? 124 ASP A CA   1 
ATOM   2067 C  C    . ASP A 1 127 ? 27.051  2.074   15.244 1.00 61.29  ? 124 ASP A C    1 
ATOM   2068 O  O    . ASP A 1 127 ? 27.022  3.214   15.727 1.00 57.78  ? 124 ASP A O    1 
ATOM   2069 C  CB   . ASP A 1 127 ? 29.153  1.178   14.240 1.00 71.58  ? 124 ASP A CB   1 
ATOM   2070 C  CG   . ASP A 1 127 ? 30.366  0.278   14.380 1.00 76.40  ? 124 ASP A CG   1 
ATOM   2071 O  OD1  . ASP A 1 127 ? 30.775  -0.001  15.523 1.00 89.01  ? 124 ASP A OD1  1 
ATOM   2072 O  OD2  . ASP A 1 127 ? 30.920  -0.135  13.342 1.00 88.81  ? 124 ASP A OD2  1 
ATOM   2073 H  H    A ASP A 1 127 ? 28.164  -0.806  15.271 0.42 71.13  ? 124 ASP A H    1 
ATOM   2074 H  H    B ASP A 1 127 ? 28.108  -0.797  15.228 0.58 71.13  ? 124 ASP A H    1 
ATOM   2075 H  HA   . ASP A 1 127 ? 28.752  1.491   16.237 1.00 77.85  ? 124 ASP A HA   1 
ATOM   2076 H  HB2  . ASP A 1 127 ? 28.644  0.876   13.472 1.00 85.93  ? 124 ASP A HB2  1 
ATOM   2077 H  HB3  . ASP A 1 127 ? 29.468  2.084   14.094 1.00 85.93  ? 124 ASP A HB3  1 
ATOM   2078 N  N    . GLY A 1 128 ? 26.065  1.603   14.478 1.00 56.89  ? 125 GLY A N    1 
ATOM   2079 C  CA   . GLY A 1 128 ? 24.899  2.427   14.219 1.00 51.97  ? 125 GLY A CA   1 
ATOM   2080 C  C    . GLY A 1 128 ? 24.147  2.795   15.488 1.00 53.23  ? 125 GLY A C    1 
ATOM   2081 O  O    . GLY A 1 128 ? 23.661  3.918   15.633 1.00 56.63  ? 125 GLY A O    1 
ATOM   2082 H  H    . GLY A 1 128 ? 26.052  0.827   14.108 1.00 68.30  ? 125 GLY A H    1 
ATOM   2083 H  HA2  . GLY A 1 128 ? 25.177  3.246   13.782 1.00 62.19  ? 125 GLY A HA2  1 
ATOM   2084 H  HA3  . GLY A 1 128 ? 24.292  1.947   13.634 1.00 62.19  ? 125 GLY A HA3  1 
ATOM   2085 N  N    . LEU A 1 129 ? 24.027  1.856   16.420 1.00 48.35  ? 126 LEU A N    1 
ATOM   2086 C  CA   . LEU A 1 129 ? 23.288  2.186   17.635 1.00 47.81  ? 126 LEU A CA   1 
ATOM   2087 C  C    . LEU A 1 129 ? 24.109  3.071   18.563 1.00 51.76  ? 126 LEU A C    1 
ATOM   2088 O  O    . LEU A 1 129 ? 23.581  4.032   19.131 1.00 48.94  ? 126 LEU A O    1 
ATOM   2089 C  CB   . LEU A 1 129 ? 22.844  0.931   18.366 1.00 53.39  ? 126 LEU A CB   1 
ATOM   2090 C  CG   . LEU A 1 129 ? 21.733  0.152   17.658 1.00 58.49  ? 126 LEU A CG   1 
ATOM   2091 C  CD1  . LEU A 1 129 ? 21.762  -1.290  18.171 1.00 54.67  ? 126 LEU A CD1  1 
ATOM   2092 C  CD2  . LEU A 1 129 ? 20.372  0.793   17.843 1.00 57.00  ? 126 LEU A CD2  1 
ATOM   2093 H  H    . LEU A 1 129 ? 24.348  1.060   16.377 1.00 58.05  ? 126 LEU A H    1 
ATOM   2094 H  HA   . LEU A 1 129 ? 22.486  2.667   17.376 1.00 57.41  ? 126 LEU A HA   1 
ATOM   2095 H  HB2  . LEU A 1 129 ? 23.608  0.340   18.456 1.00 64.10  ? 126 LEU A HB2  1 
ATOM   2096 H  HB3  . LEU A 1 129 ? 22.515  1.184   19.242 1.00 64.10  ? 126 LEU A HB3  1 
ATOM   2097 H  HG   . LEU A 1 129 ? 21.885  0.157   16.700 1.00 70.22  ? 126 LEU A HG   1 
ATOM   2098 H  HD11 . LEU A 1 129 ? 21.034  -1.784  17.763 1.00 65.64  ? 126 LEU A HD11 1 
ATOM   2099 H  HD12 . LEU A 1 129 ? 22.611  -1.693  17.932 1.00 65.64  ? 126 LEU A HD12 1 
ATOM   2100 H  HD13 . LEU A 1 129 ? 21.658  -1.284  19.135 1.00 65.64  ? 126 LEU A HD13 1 
ATOM   2101 H  HD21 . LEU A 1 129 ? 19.709  0.270   17.366 1.00 68.43  ? 126 LEU A HD21 1 
ATOM   2102 H  HD22 . LEU A 1 129 ? 20.159  0.814   18.789 1.00 68.43  ? 126 LEU A HD22 1 
ATOM   2103 H  HD23 . LEU A 1 129 ? 20.397  1.696   17.489 1.00 68.43  ? 126 LEU A HD23 1 
ATOM   2104 N  N    . ILE A 1 130 ? 25.401  2.772   18.716 1.00 50.90  ? 127 ILE A N    1 
ATOM   2105 C  CA   . ILE A 1 130 ? 26.264  3.642   19.513 1.00 57.75  ? 127 ILE A CA   1 
ATOM   2106 C  C    . ILE A 1 130 ? 26.200  5.060   18.971 1.00 54.43  ? 127 ILE A C    1 
ATOM   2107 O  O    . ILE A 1 130 ? 26.141  6.031   19.726 1.00 55.45  ? 127 ILE A O    1 
ATOM   2108 C  CB   . ILE A 1 130 ? 27.705  3.101   19.518 1.00 60.57  ? 127 ILE A CB   1 
ATOM   2109 C  CG1  . ILE A 1 130 ? 27.805  1.930   20.495 1.00 68.37  ? 127 ILE A CG1  1 
ATOM   2110 C  CG2  . ILE A 1 130 ? 28.715  4.174   19.885 1.00 61.72  ? 127 ILE A CG2  1 
ATOM   2111 C  CD1  . ILE A 1 130 ? 28.827  0.907   20.096 1.00 66.81  ? 127 ILE A CD1  1 
ATOM   2112 H  H    . ILE A 1 130 ? 25.794  2.086   18.376 1.00 61.11  ? 127 ILE A H    1 
ATOM   2113 H  HA   . ILE A 1 130 ? 25.947  3.649   20.429 1.00 69.33  ? 127 ILE A HA   1 
ATOM   2114 H  HB   . ILE A 1 130 ? 27.912  2.803   18.618 1.00 72.72  ? 127 ILE A HB   1 
ATOM   2115 H  HG12 . ILE A 1 130 ? 28.050  2.271   21.369 1.00 82.08  ? 127 ILE A HG12 1 
ATOM   2116 H  HG13 . ILE A 1 130 ? 26.943  1.487   20.542 1.00 82.08  ? 127 ILE A HG13 1 
ATOM   2117 H  HG21 . ILE A 1 130 ? 29.603  3.784   19.889 1.00 74.10  ? 127 ILE A HG21 1 
ATOM   2118 H  HG22 . ILE A 1 130 ? 28.670  4.887   19.229 1.00 74.10  ? 127 ILE A HG22 1 
ATOM   2119 H  HG23 . ILE A 1 130 ? 28.501  4.520   20.765 1.00 74.10  ? 127 ILE A HG23 1 
ATOM   2120 H  HD11 . ILE A 1 130 ? 28.834  0.194   20.755 1.00 80.21  ? 127 ILE A HD11 1 
ATOM   2121 H  HD12 . ILE A 1 130 ? 28.594  0.549   19.225 1.00 80.21  ? 127 ILE A HD12 1 
ATOM   2122 H  HD13 . ILE A 1 130 ? 29.699  1.330   20.057 1.00 80.21  ? 127 ILE A HD13 1 
ATOM   2123 N  N    . GLU A 1 131 ? 26.183  5.201   17.652 1.00 55.36  ? 128 GLU A N    1 
ATOM   2124 C  CA   . GLU A 1 131 ? 26.168  6.534   17.061 1.00 53.33  ? 128 GLU A CA   1 
ATOM   2125 C  C    . GLU A 1 131 ? 24.902  7.292   17.442 1.00 57.57  ? 128 GLU A C    1 
ATOM   2126 O  O    . GLU A 1 131 ? 24.958  8.501   17.694 1.00 55.05  ? 128 GLU A O    1 
ATOM   2127 C  CB   . GLU A 1 131 ? 26.354  6.400   15.542 1.00 62.91  ? 128 GLU A CB   1 
ATOM   2128 C  CG   . GLU A 1 131 ? 26.120  7.636   14.722 1.00 90.79  ? 128 GLU A CG   1 
ATOM   2129 C  CD   . GLU A 1 131 ? 26.013  7.310   13.235 1.00 103.70 ? 128 GLU A CD   1 
ATOM   2130 O  OE1  . GLU A 1 131 ? 26.577  6.275   12.808 1.00 80.00  ? 128 GLU A OE1  1 
ATOM   2131 O  OE2  . GLU A 1 131 ? 25.354  8.077   12.499 1.00 104.98 ? 128 GLU A OE2  1 
ATOM   2132 H  H    . GLU A 1 131 ? 26.181  4.554   17.086 1.00 66.47  ? 128 GLU A H    1 
ATOM   2133 H  HA   . GLU A 1 131 ? 26.907  7.066   17.396 1.00 64.03  ? 128 GLU A HA   1 
ATOM   2134 H  HB2  . GLU A 1 131 ? 27.266  6.117   15.375 1.00 75.53  ? 128 GLU A HB2  1 
ATOM   2135 H  HB3  . GLU A 1 131 ? 25.734  5.726   15.222 1.00 75.53  ? 128 GLU A HB3  1 
ATOM   2136 H  HG2  . GLU A 1 131 ? 25.292  8.056   15.003 1.00 108.99 ? 128 GLU A HG2  1 
ATOM   2137 H  HG3  . GLU A 1 131 ? 26.862  8.249   14.848 1.00 108.99 ? 128 GLU A HG3  1 
ATOM   2138 N  N    . HIS A 1 132 ? 23.759  6.598   17.529 1.00 53.46  ? 129 HIS A N    1 
ATOM   2139 C  CA   . HIS A 1 132 ? 22.544  7.242   18.024 1.00 49.48  ? 129 HIS A CA   1 
ATOM   2140 C  C    . HIS A 1 132 ? 22.742  7.766   19.446 1.00 51.54  ? 129 HIS A C    1 
ATOM   2141 O  O    . HIS A 1 132 ? 22.238  8.835   19.808 1.00 46.99  ? 129 HIS A O    1 
ATOM   2142 C  CB   . HIS A 1 132 ? 21.348  6.268   18.038 1.00 58.11  ? 129 HIS A CB   1 
ATOM   2143 C  CG   . HIS A 1 132 ? 20.772  5.946   16.693 1.00 67.35  ? 129 HIS A CG   1 
ATOM   2144 N  ND1  . HIS A 1 132 ? 20.218  6.900   15.866 1.00 72.29  ? 129 HIS A ND1  1 
ATOM   2145 C  CD2  . HIS A 1 132 ? 20.637  4.763   16.044 1.00 76.69  ? 129 HIS A CD2  1 
ATOM   2146 C  CE1  . HIS A 1 132 ? 19.790  6.321   14.756 1.00 80.48  ? 129 HIS A CE1  1 
ATOM   2147 N  NE2  . HIS A 1 132 ? 20.032  5.025   14.839 1.00 73.07  ? 129 HIS A NE2  1 
ATOM   2148 H  H    . HIS A 1 132 ? 23.666  5.771   17.312 1.00 64.19  ? 129 HIS A H    1 
ATOM   2149 H  HA   . HIS A 1 132 ? 22.343  7.971   17.418 1.00 59.41  ? 129 HIS A HA   1 
ATOM   2150 H  HB2  . HIS A 1 132 ? 21.638  5.432   18.436 1.00 69.77  ? 129 HIS A HB2  1 
ATOM   2151 H  HB3  . HIS A 1 132 ? 20.639  6.661   18.571 1.00 69.77  ? 129 HIS A HB3  1 
ATOM   2152 H  HD1  . HIS A 1 132 ? 20.160  7.740   16.044 1.00 86.78  ? 129 HIS A HD1  1 
ATOM   2153 H  HD2  . HIS A 1 132 ? 20.905  3.929   16.357 1.00 92.06  ? 129 HIS A HD2  1 
ATOM   2154 H  HE1  . HIS A 1 132 ? 19.386  6.754   14.038 1.00 96.61  ? 129 HIS A HE1  1 
ATOM   2155 N  N    . LEU A 1 133 ? 23.407  6.985   20.292 1.00 51.34  ? 130 LEU A N    1 
ATOM   2156 C  CA   . LEU A 1 133 ? 23.541  7.374   21.690 1.00 46.89  ? 130 LEU A CA   1 
ATOM   2157 C  C    . LEU A 1 133 ? 24.471  8.577   21.827 1.00 47.52  ? 130 LEU A C    1 
ATOM   2158 O  O    . LEU A 1 133 ? 24.231  9.466   22.654 1.00 51.04  ? 130 LEU A O    1 
ATOM   2159 C  CB   . LEU A 1 133 ? 24.052  6.181   22.502 1.00 48.02  ? 130 LEU A CB   1 
ATOM   2160 C  CG   . LEU A 1 133 ? 23.061  5.021   22.616 1.00 48.51  ? 130 LEU A CG   1 
ATOM   2161 C  CD1  . LEU A 1 133 ? 23.729  3.779   23.199 1.00 52.80  ? 130 LEU A CD1  1 
ATOM   2162 C  CD2  . LEU A 1 133 ? 21.868  5.380   23.462 1.00 49.50  ? 130 LEU A CD2  1 
ATOM   2163 H  H    . LEU A 1 133 ? 23.783  6.239   20.086 1.00 61.64  ? 130 LEU A H    1 
ATOM   2164 H  HA   . LEU A 1 133 ? 22.676  7.629   22.047 1.00 56.31  ? 130 LEU A HA   1 
ATOM   2165 H  HB2  . LEU A 1 133 ? 24.855  5.840   22.078 1.00 57.66  ? 130 LEU A HB2  1 
ATOM   2166 H  HB3  . LEU A 1 133 ? 24.254  6.484   23.401 1.00 57.66  ? 130 LEU A HB3  1 
ATOM   2167 H  HG   . LEU A 1 133 ? 22.750  4.823   21.719 1.00 58.25  ? 130 LEU A HG   1 
ATOM   2168 H  HD11 . LEU A 1 133 ? 23.050  3.111   23.382 1.00 63.39  ? 130 LEU A HD11 1 
ATOM   2169 H  HD12 . LEU A 1 133 ? 24.368  3.434   22.556 1.00 63.39  ? 130 LEU A HD12 1 
ATOM   2170 H  HD13 . LEU A 1 133 ? 24.185  4.022   24.020 1.00 63.39  ? 130 LEU A HD13 1 
ATOM   2171 H  HD21 . LEU A 1 133 ? 21.352  4.577   23.637 1.00 59.43  ? 130 LEU A HD21 1 
ATOM   2172 H  HD22 . LEU A 1 133 ? 22.177  5.764   24.297 1.00 59.43  ? 130 LEU A HD22 1 
ATOM   2173 H  HD23 . LEU A 1 133 ? 21.324  6.024   22.983 1.00 59.43  ? 130 LEU A HD23 1 
ATOM   2174 N  N    . VAL A 1 134 ? 25.523  8.628   21.013 1.00 53.10  ? 131 VAL A N    1 
ATOM   2175 C  CA   . VAL A 1 134 ? 26.442  9.769   21.030 1.00 56.12  ? 131 VAL A CA   1 
ATOM   2176 C  C    . VAL A 1 134 ? 25.716  11.064  20.670 1.00 56.60  ? 131 VAL A C    1 
ATOM   2177 O  O    . VAL A 1 134 ? 25.851  12.078  21.366 1.00 57.87  ? 131 VAL A O    1 
ATOM   2178 C  CB   . VAL A 1 134 ? 27.628  9.513   20.086 1.00 70.49  ? 131 VAL A CB   1 
ATOM   2179 C  CG1  . VAL A 1 134 ? 28.643  10.620  20.204 1.00 62.50  ? 131 VAL A CG1  1 
ATOM   2180 C  CG2  . VAL A 1 134 ? 28.313  8.200   20.407 1.00 67.52  ? 131 VAL A CG2  1 
ATOM   2181 H  H    . VAL A 1 134 ? 25.729  8.019   20.442 1.00 63.75  ? 131 VAL A H    1 
ATOM   2182 H  HA   . VAL A 1 134 ? 26.784  9.866   21.933 1.00 67.38  ? 131 VAL A HA   1 
ATOM   2183 H  HB   . VAL A 1 134 ? 27.281  9.476   19.181 1.00 84.62  ? 131 VAL A HB   1 
ATOM   2184 H  HG11 . VAL A 1 134 ? 29.382  10.437  19.602 1.00 75.04  ? 131 VAL A HG11 1 
ATOM   2185 H  HG12 . VAL A 1 134 ? 28.222  11.461  19.965 1.00 75.04  ? 131 VAL A HG12 1 
ATOM   2186 H  HG13 . VAL A 1 134 ? 28.963  10.658  21.119 1.00 75.04  ? 131 VAL A HG13 1 
ATOM   2187 H  HG21 . VAL A 1 134 ? 29.059  8.076   19.800 1.00 81.06  ? 131 VAL A HG21 1 
ATOM   2188 H  HG22 . VAL A 1 134 ? 28.632  8.227   21.323 1.00 81.06  ? 131 VAL A HG22 1 
ATOM   2189 H  HG23 . VAL A 1 134 ? 27.676  7.477   20.300 1.00 81.06  ? 131 VAL A HG23 1 
ATOM   2190 N  N    . TYR A 1 135 ? 24.963  11.065  19.561 1.00 52.67  ? 132 TYR A N    1 
ATOM   2191 C  CA   . TYR A 1 135 ? 24.228  12.269  19.178 1.00 56.94  ? 132 TYR A CA   1 
ATOM   2192 C  C    . TYR A 1 135 ? 23.254  12.692  20.264 1.00 52.38  ? 132 TYR A C    1 
ATOM   2193 O  O    . TYR A 1 135 ? 23.076  13.890  20.523 1.00 54.11  ? 132 TYR A O    1 
ATOM   2194 C  CB   . TYR A 1 135 ? 23.444  12.058  17.879 1.00 54.30  ? 132 TYR A CB   1 
ATOM   2195 C  CG   . TYR A 1 135 ? 22.837  13.342  17.333 1.00 84.62  ? 132 TYR A CG   1 
ATOM   2196 C  CD1  . TYR A 1 135 ? 23.603  14.489  17.158 1.00 96.91  ? 132 TYR A CD1  1 
ATOM   2197 C  CD2  . TYR A 1 135 ? 21.475  13.417  17.044 1.00 89.86  ? 132 TYR A CD2  1 
ATOM   2198 C  CE1  . TYR A 1 135 ? 23.043  15.661  16.661 1.00 118.98 ? 132 TYR A CE1  1 
ATOM   2199 C  CE2  . TYR A 1 135 ? 20.905  14.585  16.555 1.00 94.10  ? 132 TYR A CE2  1 
ATOM   2200 C  CZ   . TYR A 1 135 ? 21.691  15.703  16.366 1.00 113.53 ? 132 TYR A CZ   1 
ATOM   2201 O  OH   . TYR A 1 135 ? 21.126  16.862  15.878 1.00 100.41 ? 132 TYR A OH   1 
ATOM   2202 H  H    . TYR A 1 135 ? 24.866  10.397  19.028 1.00 63.03  ? 132 TYR A H    1 
ATOM   2203 H  HA   . TYR A 1 135 ? 24.884  12.967  19.033 1.00 68.37  ? 132 TYR A HA   1 
ATOM   2204 H  HB2  . TYR A 1 135 ? 24.042  11.701  17.205 1.00 65.19  ? 132 TYR A HB2  1 
ATOM   2205 H  HB3  . TYR A 1 135 ? 22.721  11.434  18.046 1.00 65.19  ? 132 TYR A HB3  1 
ATOM   2206 H  HD1  . TYR A 1 135 ? 24.507  14.472  17.378 1.00 116.33 ? 132 TYR A HD1  1 
ATOM   2207 H  HD2  . TYR A 1 135 ? 20.937  12.670  17.182 1.00 107.87 ? 132 TYR A HD2  1 
ATOM   2208 H  HE1  . TYR A 1 135 ? 23.574  16.413  16.528 1.00 142.81 ? 132 TYR A HE1  1 
ATOM   2209 H  HE2  . TYR A 1 135 ? 19.997  14.614  16.356 1.00 112.96 ? 132 TYR A HE2  1 
ATOM   2210 H  HH   . TYR A 1 135 ? 20.367  16.698  15.556 1.00 120.53 ? 132 TYR A HH   1 
ATOM   2211 N  N    . TYR A 1 136 ? 22.581  11.714  20.881 1.00 49.59  ? 133 TYR A N    1 
ATOM   2212 C  CA   . TYR A 1 136 ? 21.639  12.011  21.952 1.00 48.42  ? 133 TYR A CA   1 
ATOM   2213 C  C    . TYR A 1 136 ? 22.326  12.759  23.088 1.00 49.77  ? 133 TYR A C    1 
ATOM   2214 O  O    . TYR A 1 136 ? 21.817  13.766  23.586 1.00 51.71  ? 133 TYR A O    1 
ATOM   2215 C  CB   . TYR A 1 136 ? 21.016  10.710  22.461 1.00 45.76  ? 133 TYR A CB   1 
ATOM   2216 C  CG   . TYR A 1 136 ? 20.069  10.908  23.620 1.00 44.85  ? 133 TYR A CG   1 
ATOM   2217 C  CD1  . TYR A 1 136 ? 18.875  11.589  23.464 1.00 45.02  ? 133 TYR A CD1  1 
ATOM   2218 C  CD2  . TYR A 1 136 ? 20.407  10.451  24.883 1.00 44.31  ? 133 TYR A CD2  1 
ATOM   2219 C  CE1  . TYR A 1 136 ? 18.018  11.778  24.530 1.00 44.60  ? 133 TYR A CE1  1 
ATOM   2220 C  CE2  . TYR A 1 136 ? 19.570  10.629  25.944 1.00 45.33  ? 133 TYR A CE2  1 
ATOM   2221 C  CZ   . TYR A 1 136 ? 18.383  11.286  25.779 1.00 44.04  ? 133 TYR A CZ   1 
ATOM   2222 O  OH   . TYR A 1 136 ? 17.571  11.468  26.860 1.00 44.30  ? 133 TYR A OH   1 
ATOM   2223 H  H    . TYR A 1 136 ? 22.655  10.877  20.697 1.00 59.33  ? 133 TYR A H    1 
ATOM   2224 H  HA   . TYR A 1 136 ? 20.930  12.576  21.607 1.00 57.93  ? 133 TYR A HA   1 
ATOM   2225 H  HB2  . TYR A 1 136 ? 20.518  10.298  21.737 1.00 54.74  ? 133 TYR A HB2  1 
ATOM   2226 H  HB3  . TYR A 1 136 ? 21.726  10.117  22.755 1.00 54.74  ? 133 TYR A HB3  1 
ATOM   2227 H  HD1  . TYR A 1 136 ? 18.646  11.925  22.627 1.00 53.85  ? 133 TYR A HD1  1 
ATOM   2228 H  HD2  . TYR A 1 136 ? 21.219  10.016  25.009 1.00 53.00  ? 133 TYR A HD2  1 
ATOM   2229 H  HE1  . TYR A 1 136 ? 17.212  12.227  24.416 1.00 53.35  ? 133 TYR A HE1  1 
ATOM   2230 H  HE2  . TYR A 1 136 ? 19.807  10.302  26.782 1.00 54.43  ? 133 TYR A HE2  1 
ATOM   2231 H  HH   . TYR A 1 136 ? 17.927  11.139  27.546 1.00 53.19  ? 133 TYR A HH   1 
ATOM   2232 N  N    . SER A 1 137 ? 23.500  12.290  23.494 1.00 53.03  ? 134 SER A N    1 
ATOM   2233 C  CA   . SER A 1 137 ? 24.190  12.906  24.622 1.00 57.02  ? 134 SER A CA   1 
ATOM   2234 C  C    . SER A 1 137 ? 24.688  14.314  24.290 1.00 54.89  ? 134 SER A C    1 
ATOM   2235 O  O    . SER A 1 137 ? 24.727  15.179  25.176 1.00 59.72  ? 134 SER A O    1 
ATOM   2236 C  CB   . SER A 1 137 ? 25.344  12.002  25.058 1.00 59.85  ? 134 SER A CB   1 
ATOM   2237 O  OG   . SER A 1 137 ? 26.348  12.739  25.736 1.00 92.61  ? 134 SER A OG   1 
ATOM   2238 H  H    . SER A 1 137 ? 23.915  11.626  23.139 1.00 63.67  ? 134 SER A H    1 
ATOM   2239 H  HA   . SER A 1 137 ? 23.576  12.993  25.367 1.00 68.45  ? 134 SER A HA   1 
ATOM   2240 H  HB2  . SER A 1 137 ? 24.999  11.319  25.654 1.00 71.85  ? 134 SER A HB2  1 
ATOM   2241 H  HB3  . SER A 1 137 ? 25.734  11.590  24.271 1.00 71.85  ? 134 SER A HB3  1 
ATOM   2242 H  HG   . SER A 1 137 ? 26.944  12.220  26.019 1.00 111.17 ? 134 SER A HG   1 
ATOM   2243 N  N    . GLN A 1 138 ? 25.042  14.574  23.028 1.00 56.90  ? 135 GLN A N    1 
ATOM   2244 C  CA   . GLN A 1 138 ? 25.540  15.899  22.664 1.00 62.56  ? 135 GLN A CA   1 
ATOM   2245 C  C    . GLN A 1 138 ? 24.417  16.927  22.637 1.00 75.90  ? 135 GLN A C    1 
ATOM   2246 O  O    . GLN A 1 138 ? 24.557  18.026  23.187 1.00 79.39  ? 135 GLN A O    1 
ATOM   2247 C  CB   . GLN A 1 138 ? 26.225  15.856  21.302 1.00 66.91  ? 135 GLN A CB   1 
ATOM   2248 C  CG   . GLN A 1 138 ? 27.316  14.835  21.182 1.00 71.57  ? 135 GLN A CG   1 
ATOM   2249 C  CD   . GLN A 1 138 ? 27.827  14.752  19.760 1.00 94.48  ? 135 GLN A CD   1 
ATOM   2250 O  OE1  . GLN A 1 138 ? 27.800  15.728  19.017 1.00 87.97  ? 135 GLN A OE1  1 
ATOM   2251 N  NE2  . GLN A 1 138 ? 28.330  13.601  19.385 1.00 97.24  ? 135 GLN A NE2  1 
ATOM   2252 H  H    . GLN A 1 138 ? 25.004  14.012  22.378 1.00 68.32  ? 135 GLN A H    1 
ATOM   2253 H  HA   . GLN A 1 138 ? 26.191  16.166  23.331 1.00 75.11  ? 135 GLN A HA   1 
ATOM   2254 H  HB2  . GLN A 1 138 ? 25.559  15.652  20.628 1.00 80.33  ? 135 GLN A HB2  1 
ATOM   2255 H  HB3  . GLN A 1 138 ? 26.618  16.725  21.127 1.00 80.33  ? 135 GLN A HB3  1 
ATOM   2256 H  HG2  . GLN A 1 138 ? 28.055  15.082  21.760 1.00 85.92  ? 135 GLN A HG2  1 
ATOM   2257 H  HG3  . GLN A 1 138 ? 26.973  13.964  21.436 1.00 85.92  ? 135 GLN A HG3  1 
ATOM   2258 H  HE21 . GLN A 1 138 ? 28.356  12.943  19.938 1.00 116.72 ? 135 GLN A HE21 1 
ATOM   2259 H  HE22 . GLN A 1 138 ? 28.633  13.504  18.586 1.00 116.72 ? 135 GLN A HE22 1 
ATOM   2260 N  N    A ARG A 1 139 ? 23.308  16.612  21.958 0.40 68.36  ? 136 ARG A N    1 
ATOM   2261 N  N    B ARG A 1 139 ? 23.309  16.596  21.966 0.60 68.26  ? 136 ARG A N    1 
ATOM   2262 C  CA   A ARG A 1 139 ? 22.165  17.522  21.964 0.40 75.63  ? 136 ARG A CA   1 
ATOM   2263 C  CA   B ARG A 1 139 ? 22.138  17.470  21.943 0.60 75.62  ? 136 ARG A CA   1 
ATOM   2264 C  C    A ARG A 1 139 ? 21.788  17.876  23.392 0.40 77.69  ? 136 ARG A C    1 
ATOM   2265 C  C    B ARG A 1 139 ? 21.727  17.844  23.357 0.60 77.67  ? 136 ARG A C    1 
ATOM   2266 O  O    A ARG A 1 139 ? 21.567  19.046  23.723 0.40 81.77  ? 136 ARG A O    1 
ATOM   2267 O  O    B ARG A 1 139 ? 21.440  19.010  23.648 0.60 81.79  ? 136 ARG A O    1 
ATOM   2268 C  CB   A ARG A 1 139 ? 20.971  16.883  21.244 0.40 75.73  ? 136 ARG A CB   1 
ATOM   2269 C  CB   B ARG A 1 139 ? 21.007  16.759  21.186 0.60 75.65  ? 136 ARG A CB   1 
ATOM   2270 C  CG   A ARG A 1 139 ? 19.642  17.630  21.421 0.40 86.00  ? 136 ARG A CG   1 
ATOM   2271 C  CG   B ARG A 1 139 ? 19.585  17.023  21.658 0.60 85.93  ? 136 ARG A CG   1 
ATOM   2272 C  CD   A ARG A 1 139 ? 18.524  17.076  20.515 0.40 88.88  ? 136 ARG A CD   1 
ATOM   2273 C  CD   B ARG A 1 139 ? 18.530  16.612  20.596 0.60 89.07  ? 136 ARG A CD   1 
ATOM   2274 N  NE   A ARG A 1 139 ? 17.243  16.899  21.199 0.40 84.30  ? 136 ARG A NE   1 
ATOM   2275 N  NE   B ARG A 1 139 ? 18.694  15.270  20.035 0.60 84.13  ? 136 ARG A NE   1 
ATOM   2276 C  CZ   A ARG A 1 139 ? 16.829  15.772  21.761 0.40 79.99  ? 136 ARG A CZ   1 
ATOM   2277 C  CZ   B ARG A 1 139 ? 18.026  14.192  20.436 0.60 83.34  ? 136 ARG A CZ   1 
ATOM   2278 N  NH1  A ARG A 1 139 ? 17.571  14.677  21.745 0.40 85.19  ? 136 ARG A NH1  1 
ATOM   2279 N  NH1  B ARG A 1 139 ? 17.152  14.247  21.429 0.60 85.50  ? 136 ARG A NH1  1 
ATOM   2280 N  NH2  A ARG A 1 139 ? 15.634  15.738  22.346 0.40 77.06  ? 136 ARG A NH2  1 
ATOM   2281 N  NH2  B ARG A 1 139 ? 18.230  13.030  19.816 0.60 69.13  ? 136 ARG A NH2  1 
ATOM   2282 H  H    A ARG A 1 139 ? 23.197  15.893  21.499 0.40 82.06  ? 136 ARG A H    1 
ATOM   2283 H  H    B ARG A 1 139 ? 23.211  15.870  21.515 0.60 81.95  ? 136 ARG A H    1 
ATOM   2284 H  HA   A ARG A 1 139 ? 22.397  18.332  21.484 0.40 90.79  ? 136 ARG A HA   1 
ATOM   2285 H  HA   B ARG A 1 139 ? 22.333  18.295  21.473 0.60 90.78  ? 136 ARG A HA   1 
ATOM   2286 H  HB2  A ARG A 1 139 ? 21.165  16.851  20.294 0.40 90.91  ? 136 ARG A HB2  1 
ATOM   2287 H  HB2  B ARG A 1 139 ? 21.052  17.033  20.257 0.60 90.82  ? 136 ARG A HB2  1 
ATOM   2288 H  HB3  A ARG A 1 139 ? 20.849  15.984  21.588 0.40 90.91  ? 136 ARG A HB3  1 
ATOM   2289 H  HB3  B ARG A 1 139 ? 21.155  15.803  21.257 0.60 90.82  ? 136 ARG A HB3  1 
ATOM   2290 H  HG2  A ARG A 1 139 ? 19.351  17.546  22.342 0.40 103.23 ? 136 ARG A HG2  1 
ATOM   2291 H  HG2  B ARG A 1 139 ? 19.417  16.511  22.465 0.60 103.15 ? 136 ARG A HG2  1 
ATOM   2292 H  HG3  A ARG A 1 139 ? 19.772  18.565  21.198 0.40 103.23 ? 136 ARG A HG3  1 
ATOM   2293 H  HG3  B ARG A 1 139 ? 19.480  17.970  21.838 0.60 103.15 ? 136 ARG A HG3  1 
ATOM   2294 H  HD2  A ARG A 1 139 ? 18.384  17.693  19.779 0.40 106.69 ? 136 ARG A HD2  1 
ATOM   2295 H  HD2  B ARG A 1 139 ? 17.652  16.648  21.006 0.60 106.92 ? 136 ARG A HD2  1 
ATOM   2296 H  HD3  A ARG A 1 139 ? 18.799  16.211  20.174 0.40 106.69 ? 136 ARG A HD3  1 
ATOM   2297 H  HD3  B ARG A 1 139 ? 18.577  17.240  19.858 0.60 106.92 ? 136 ARG A HD3  1 
ATOM   2298 H  HE   A ARG A 1 139 ? 16.718  17.579  21.239 0.40 101.20 ? 136 ARG A HE   1 
ATOM   2299 H  HE   B ARG A 1 139 ? 19.264  15.171  19.399 0.60 100.99 ? 136 ARG A HE   1 
ATOM   2300 H  HH11 A ARG A 1 139 ? 18.341  14.685  21.363 0.40 102.26 ? 136 ARG A HH11 1 
ATOM   2301 H  HH11 B ARG A 1 139 ? 17.005  14.992  21.832 0.60 102.64 ? 136 ARG A HH11 1 
ATOM   2302 H  HH12 A ARG A 1 139 ? 17.282  13.957  22.116 0.40 102.26 ? 136 ARG A HH12 1 
ATOM   2303 H  HH12 B ARG A 1 139 ? 16.731  13.537  21.672 0.60 102.64 ? 136 ARG A HH12 1 
ATOM   2304 H  HH21 A ARG A 1 139 ? 15.140  16.442  22.356 0.40 92.51  ? 136 ARG A HH21 1 
ATOM   2305 H  HH21 B ARG A 1 139 ? 18.790  12.983  19.164 0.60 82.99  ? 136 ARG A HH21 1 
ATOM   2306 H  HH22 A ARG A 1 139 ? 15.356  15.012  22.714 0.40 92.51  ? 136 ARG A HH22 1 
ATOM   2307 H  HH22 B ARG A 1 139 ? 17.803  12.327  20.068 0.60 82.99  ? 136 ARG A HH22 1 
ATOM   2308 N  N    . MET A 1 140 ? 21.769  16.871  24.263 1.00 64.29  ? 137 MET A N    1 
ATOM   2309 C  CA   . MET A 1 140 ? 21.333  17.060  25.637 1.00 74.18  ? 137 MET A CA   1 
ATOM   2310 C  C    . MET A 1 140 ? 22.291  17.956  26.408 1.00 79.42  ? 137 MET A C    1 
ATOM   2311 O  O    . MET A 1 140 ? 21.858  18.697  27.295 1.00 87.15  ? 137 MET A O    1 
ATOM   2312 C  CB   . MET A 1 140 ? 21.279  15.667  26.258 1.00 65.09  ? 137 MET A CB   1 
ATOM   2313 C  CG   . MET A 1 140 ? 20.067  14.853  25.821 1.00 69.43  ? 137 MET A CG   1 
ATOM   2314 S  SD   . MET A 1 140 ? 18.525  15.298  26.581 1.00 64.18  ? 137 MET A SD   1 
ATOM   2315 C  CE   . MET A 1 140 ? 18.910  14.596  28.196 1.00 66.60  ? 137 MET A CE   1 
ATOM   2316 H  H    A MET A 1 140 ? 22.005  16.064  24.081 0.40 77.19  ? 137 MET A H    1 
ATOM   2317 H  H    B MET A 1 140 ? 22.052  16.074  24.103 0.60 77.19  ? 137 MET A H    1 
ATOM   2318 H  HA   . MET A 1 140 ? 20.459  17.479  25.675 1.00 89.05  ? 137 MET A HA   1 
ATOM   2319 H  HB2  . MET A 1 140 ? 22.075  15.178  25.998 1.00 78.15  ? 137 MET A HB2  1 
ATOM   2320 H  HB3  . MET A 1 140 ? 21.244  15.756  27.224 1.00 78.15  ? 137 MET A HB3  1 
ATOM   2321 H  HG2  . MET A 1 140 ? 19.957  14.962  24.863 1.00 83.35  ? 137 MET A HG2  1 
ATOM   2322 H  HG3  . MET A 1 140 ? 20.234  13.922  26.033 1.00 83.35  ? 137 MET A HG3  1 
ATOM   2323 H  HE1  . MET A 1 140 ? 19.588  13.911  28.090 1.00 79.96  ? 137 MET A HE1  1 
ATOM   2324 H  HE2  . MET A 1 140 ? 19.240  15.300  28.776 1.00 79.96  ? 137 MET A HE2  1 
ATOM   2325 H  HE3  . MET A 1 140 ? 18.104  14.208  28.572 1.00 79.96  ? 137 MET A HE3  1 
ATOM   2326 N  N    . SER A 1 141 ? 23.584  17.894  26.088 1.00 72.79  ? 138 SER A N    1 
ATOM   2327 C  CA   . SER A 1 141 ? 24.563  18.721  26.782 1.00 86.33  ? 138 SER A CA   1 
ATOM   2328 C  C    . SER A 1 141 ? 24.455  20.183  26.366 1.00 87.83  ? 138 SER A C    1 
ATOM   2329 O  O    . SER A 1 141 ? 24.666  21.080  27.192 1.00 93.56  ? 138 SER A O    1 
ATOM   2330 C  CB   . SER A 1 141 ? 25.970  18.186  26.514 1.00 84.34  ? 138 SER A CB   1 
ATOM   2331 O  OG   . SER A 1 141 ? 26.169  16.933  27.157 1.00 78.17  ? 138 SER A OG   1 
ATOM   2332 H  H    . SER A 1 141 ? 23.915  17.386  25.477 1.00 87.38  ? 138 SER A H    1 
ATOM   2333 H  HA   . SER A 1 141 ? 24.401  18.673  27.738 1.00 103.63 ? 138 SER A HA   1 
ATOM   2334 H  HB2  . SER A 1 141 ? 26.087  18.072  25.558 1.00 101.25 ? 138 SER A HB2  1 
ATOM   2335 H  HB3  . SER A 1 141 ? 26.619  18.822  26.854 1.00 101.25 ? 138 SER A HB3  1 
ATOM   2336 H  HG   . SER A 1 141 ? 25.599  16.378  26.886 1.00 93.83  ? 138 SER A HG   1 
ATOM   2337 N  N    . ASN A 1 142 ? 24.127  20.446  25.099 1.00 88.01  ? 139 ASN A N    1 
ATOM   2338 C  CA   . ASN A 1 142 ? 23.937  21.815  24.629 1.00 103.17 ? 139 ASN A CA   1 
ATOM   2339 C  C    . ASN A 1 142 ? 22.609  22.404  25.076 1.00 101.95 ? 139 ASN A C    1 
ATOM   2340 O  O    . ASN A 1 142 ? 22.484  23.635  25.149 1.00 90.68  ? 139 ASN A O    1 
ATOM   2341 C  CB   . ASN A 1 142 ? 24.041  21.854  23.103 1.00 97.42  ? 139 ASN A CB   1 
ATOM   2342 C  CG   . ASN A 1 142 ? 25.331  21.241  22.595 1.00 104.41 ? 139 ASN A CG   1 
ATOM   2343 O  OD1  . ASN A 1 142 ? 26.388  21.389  23.217 1.00 95.91  ? 139 ASN A OD1  1 
ATOM   2344 N  ND2  . ASN A 1 142 ? 25.250  20.530  21.473 1.00 106.96 ? 139 ASN A ND2  1 
ATOM   2345 H  H    . ASN A 1 142 ? 24.009  19.847  24.493 1.00 105.64 ? 139 ASN A H    1 
ATOM   2346 H  HA   . ASN A 1 142 ? 24.641  22.377  24.989 1.00 123.84 ? 139 ASN A HA   1 
ATOM   2347 H  HB2  . ASN A 1 142 ? 23.300  21.357  22.722 1.00 116.94 ? 139 ASN A HB2  1 
ATOM   2348 H  HB3  . ASN A 1 142 ? 24.009  22.777  22.806 1.00 116.94 ? 139 ASN A HB3  1 
ATOM   2349 H  HD21 . ASN A 1 142 ? 24.493  20.438  21.076 1.00 128.39 ? 139 ASN A HD21 1 
ATOM   2350 H  HD22 . ASN A 1 142 ? 25.955  20.162  21.145 1.00 128.39 ? 139 ASN A HD22 1 
ATOM   2351 N  N    . ILE A 1 143 ? 21.623  21.553  25.370 1.00 88.49  ? 140 ILE A N    1 
ATOM   2352 C  CA   . ILE A 1 143 ? 20.361  21.974  25.964 1.00 97.31  ? 140 ILE A CA   1 
ATOM   2353 C  C    . ILE A 1 143 ? 20.606  22.298  27.429 1.00 94.30  ? 140 ILE A C    1 
ATOM   2354 O  O    . ILE A 1 143 ? 20.520  23.458  27.851 1.00 98.80  ? 140 ILE A O    1 
ATOM   2355 C  CB   . ILE A 1 143 ? 19.285  20.882  25.825 1.00 94.31  ? 140 ILE A CB   1 
ATOM   2356 C  CG1  . ILE A 1 143 ? 18.726  20.862  24.405 1.00 90.08  ? 140 ILE A CG1  1 
ATOM   2357 C  CG2  . ILE A 1 143 ? 18.174  21.079  26.855 1.00 92.51  ? 140 ILE A CG2  1 
ATOM   2358 C  CD1  . ILE A 1 143 ? 18.332  19.477  23.948 1.00 95.34  ? 140 ILE A CD1  1 
ATOM   2359 H  H    . ILE A 1 143 ? 21.666  20.705  25.230 1.00 106.22 ? 140 ILE A H    1 
ATOM   2360 H  HA   . ILE A 1 143 ? 20.043  22.770  25.509 1.00 116.80 ? 140 ILE A HA   1 
ATOM   2361 H  HB   . ILE A 1 143 ? 19.699  20.022  25.998 1.00 113.20 ? 140 ILE A HB   1 
ATOM   2362 H  HG12 . ILE A 1 143 ? 17.937  21.425  24.369 1.00 108.13 ? 140 ILE A HG12 1 
ATOM   2363 H  HG13 . ILE A 1 143 ? 19.402  21.198  23.796 1.00 108.13 ? 140 ILE A HG13 1 
ATOM   2364 H  HG21 . ILE A 1 143 ? 17.383  20.601  26.562 1.00 111.05 ? 140 ILE A HG21 1 
ATOM   2365 H  HG22 . ILE A 1 143 ? 18.472  20.732  27.711 1.00 111.05 ? 140 ILE A HG22 1 
ATOM   2366 H  HG23 . ILE A 1 143 ? 17.979  22.026  26.932 1.00 111.05 ? 140 ILE A HG23 1 
ATOM   2367 H  HD11 . ILE A 1 143 ? 18.110  19.507  23.004 1.00 114.44 ? 140 ILE A HD11 1 
ATOM   2368 H  HD12 . ILE A 1 143 ? 19.077  18.873  24.093 1.00 114.44 ? 140 ILE A HD12 1 
ATOM   2369 H  HD13 . ILE A 1 143 ? 17.563  19.182  24.460 1.00 114.44 ? 140 ILE A HD13 1 
ATOM   2370 N  N    . LEU A 1 144 ? 20.914  21.261  28.210 1.00 93.21  ? 141 LEU A N    1 
ATOM   2371 C  CA   . LEU A 1 144 ? 21.194  21.401  29.629 1.00 95.43  ? 141 LEU A CA   1 
ATOM   2372 C  C    . LEU A 1 144 ? 22.461  22.185  29.898 1.00 103.28 ? 141 LEU A C    1 
ATOM   2373 O  O    . LEU A 1 144 ? 22.804  22.388  31.071 1.00 103.57 ? 141 LEU A O    1 
ATOM   2374 C  CB   . LEU A 1 144 ? 21.304  20.022  30.260 1.00 83.79  ? 141 LEU A CB   1 
ATOM   2375 C  CG   . LEU A 1 144 ? 19.974  19.275  30.287 1.00 91.19  ? 141 LEU A CG   1 
ATOM   2376 C  CD1  . LEU A 1 144 ? 20.217  17.844  30.729 1.00 97.50  ? 141 LEU A CD1  1 
ATOM   2377 C  CD2  . LEU A 1 144 ? 18.969  19.972  31.178 1.00 102.33 ? 141 LEU A CD2  1 
ATOM   2378 H  H    . LEU A 1 144 ? 20.968  20.450  27.931 1.00 111.89 ? 141 LEU A H    1 
ATOM   2379 H  HA   . LEU A 1 144 ? 20.458  21.872  30.051 1.00 114.55 ? 141 LEU A HA   1 
ATOM   2380 H  HB2  . LEU A 1 144 ? 21.936  19.492  29.749 1.00 100.58 ? 141 LEU A HB2  1 
ATOM   2381 H  HB3  . LEU A 1 144 ? 21.614  20.118  31.174 1.00 100.58 ? 141 LEU A HB3  1 
ATOM   2382 H  HG   . LEU A 1 144 ? 19.585  19.263  29.398 1.00 109.46 ? 141 LEU A HG   1 
ATOM   2383 H  HD11 . LEU A 1 144 ? 19.368  17.438  30.966 1.00 117.03 ? 141 LEU A HD11 1 
ATOM   2384 H  HD12 . LEU A 1 144 ? 20.625  17.353  29.999 1.00 117.03 ? 141 LEU A HD12 1 
ATOM   2385 H  HD13 . LEU A 1 144 ? 20.809  17.847  31.497 1.00 117.03 ? 141 LEU A HD13 1 
ATOM   2386 H  HD21 . LEU A 1 144 ? 18.210  19.384  31.319 1.00 122.83 ? 141 LEU A HD21 1 
ATOM   2387 H  HD22 . LEU A 1 144 ? 19.389  20.179  32.027 1.00 122.83 ? 141 LEU A HD22 1 
ATOM   2388 H  HD23 . LEU A 1 144 ? 18.677  20.790  30.745 1.00 122.83 ? 141 LEU A HD23 1 
ATOM   2389 N  N    . ASN A 1 145 ? 23.162  22.609  28.846 1.00 107.60 ? 142 ASN A N    1 
ATOM   2390 C  CA   . ASN A 1 145 ? 24.353  23.445  28.976 1.00 110.45 ? 142 ASN A CA   1 
ATOM   2391 C  C    . ASN A 1 145 ? 25.287  22.874  30.040 1.00 105.05 ? 142 ASN A C    1 
ATOM   2392 O  O    . ASN A 1 145 ? 25.915  23.602  30.813 1.00 93.96  ? 142 ASN A O    1 
ATOM   2393 C  CB   . ASN A 1 145 ? 23.949  24.886  29.281 1.00 116.14 ? 142 ASN A CB   1 
ATOM   2394 C  CG   . ASN A 1 145 ? 24.102  25.803  28.073 1.00 108.15 ? 142 ASN A CG   1 
ATOM   2395 O  OD1  . ASN A 1 145 ? 25.211  26.194  27.715 1.00 103.71 ? 142 ASN A OD1  1 
ATOM   2396 N  ND2  . ASN A 1 145 ? 22.983  26.127  27.425 1.00 105.64 ? 142 ASN A ND2  1 
ATOM   2397 H  H    . ASN A 1 145 ? 22.962  22.422  28.031 1.00 129.15 ? 142 ASN A H    1 
ATOM   2398 H  HA   . ASN A 1 145 ? 24.845  23.449  28.140 1.00 132.57 ? 142 ASN A HA   1 
ATOM   2399 H  HB2  . ASN A 1 145 ? 23.019  24.903  29.556 1.00 139.40 ? 142 ASN A HB2  1 
ATOM   2400 H  HB3  . ASN A 1 145 ? 24.512  25.228  29.993 1.00 139.40 ? 142 ASN A HB3  1 
ATOM   2401 H  HD21 . ASN A 1 145 ? 23.019  26.642  26.737 1.00 126.81 ? 142 ASN A HD21 1 
ATOM   2402 H  HD22 . ASN A 1 145 ? 22.226  25.821  27.694 1.00 126.81 ? 142 ASN A HD22 1 
ATOM   2403 N  N    . LEU A 1 146 ? 25.372  21.546  30.073 1.00 104.00 ? 143 LEU A N    1 
ATOM   2404 C  CA   . LEU A 1 146 ? 26.248  20.869  31.014 1.00 98.75  ? 143 LEU A CA   1 
ATOM   2405 C  C    . LEU A 1 146 ? 27.696  21.253  30.763 1.00 101.51 ? 143 LEU A C    1 
ATOM   2406 O  O    . LEU A 1 146 ? 28.089  21.581  29.641 1.00 109.05 ? 143 LEU A O    1 
ATOM   2407 C  CB   . LEU A 1 146 ? 26.102  19.360  30.885 1.00 98.29  ? 143 LEU A CB   1 
ATOM   2408 C  CG   . LEU A 1 146 ? 24.745  18.748  31.209 1.00 102.15 ? 143 LEU A CG   1 
ATOM   2409 C  CD1  . LEU A 1 146 ? 24.967  17.239  31.330 1.00 93.24  ? 143 LEU A CD1  1 
ATOM   2410 C  CD2  . LEU A 1 146 ? 24.124  19.321  32.463 1.00 103.72 ? 143 LEU A CD2  1 
ATOM   2411 H  H    . LEU A 1 146 ? 24.931  21.016  29.559 1.00 124.83 ? 143 LEU A H    1 
ATOM   2412 H  HA   . LEU A 1 146 ? 26.005  21.130  31.916 1.00 118.53 ? 143 LEU A HA   1 
ATOM   2413 H  HB2  . LEU A 1 146 ? 26.305  19.121  29.967 1.00 117.98 ? 143 LEU A HB2  1 
ATOM   2414 H  HB3  . LEU A 1 146 ? 26.745  18.949  31.484 1.00 117.98 ? 143 LEU A HB3  1 
ATOM   2415 H  HG   . LEU A 1 146 ? 24.105  18.952  30.509 1.00 122.61 ? 143 LEU A HG   1 
ATOM   2416 H  HD11 . LEU A 1 146 ? 24.142  16.821  31.623 1.00 111.92 ? 143 LEU A HD11 1 
ATOM   2417 H  HD12 . LEU A 1 146 ? 25.227  16.888  30.464 1.00 111.92 ? 143 LEU A HD12 1 
ATOM   2418 H  HD13 . LEU A 1 146 ? 25.670  17.075  31.978 1.00 111.92 ? 143 LEU A HD13 1 
ATOM   2419 H  HD21 . LEU A 1 146 ? 23.341  18.798  32.695 1.00 124.50 ? 143 LEU A HD21 1 
ATOM   2420 H  HD22 . LEU A 1 146 ? 24.773  19.282  33.183 1.00 124.50 ? 143 LEU A HD22 1 
ATOM   2421 H  HD23 . LEU A 1 146 ? 23.870  20.242  32.297 1.00 124.50 ? 143 LEU A HD23 1 
ATOM   2422 N  N    . ASP A 1 147 ? 28.504  21.188  31.816 1.00 111.63 ? 144 ASP A N    1 
ATOM   2423 C  CA   . ASP A 1 147 ? 29.916  21.506  31.672 1.00 118.71 ? 144 ASP A CA   1 
ATOM   2424 C  C    . ASP A 1 147 ? 30.580  20.482  30.751 1.00 108.72 ? 144 ASP A C    1 
ATOM   2425 O  O    . ASP A 1 147 ? 29.957  19.523  30.278 1.00 98.23  ? 144 ASP A O    1 
ATOM   2426 C  CB   . ASP A 1 147 ? 30.594  21.583  33.043 1.00 115.49 ? 144 ASP A CB   1 
ATOM   2427 C  CG   . ASP A 1 147 ? 30.872  20.218  33.661 1.00 124.52 ? 144 ASP A CG   1 
ATOM   2428 O  OD1  . ASP A 1 147 ? 30.669  19.176  33.004 1.00 129.48 ? 144 ASP A OD1  1 
ATOM   2429 O  OD2  . ASP A 1 147 ? 31.308  20.190  34.831 1.00 125.34 ? 144 ASP A OD2  1 
ATOM   2430 H  H    . ASP A 1 147 ? 28.262  20.965  32.611 1.00 133.99 ? 144 ASP A H    1 
ATOM   2431 H  HA   . ASP A 1 147 ? 30.012  22.381  31.264 1.00 142.49 ? 144 ASP A HA   1 
ATOM   2432 H  HB2  . ASP A 1 147 ? 31.443  22.044  32.948 1.00 138.62 ? 144 ASP A HB2  1 
ATOM   2433 H  HB3  . ASP A 1 147 ? 30.018  22.072  33.651 1.00 138.62 ? 144 ASP A HB3  1 
ATOM   2434 N  N    . GLN A 1 148 ? 31.867  20.697  30.485 1.00 106.23 ? 145 GLN A N    1 
ATOM   2435 C  CA   . GLN A 1 148 ? 32.600  19.814  29.583 1.00 104.78 ? 145 GLN A CA   1 
ATOM   2436 C  C    . GLN A 1 148 ? 32.940  18.494  30.258 1.00 88.04  ? 145 GLN A C    1 
ATOM   2437 O  O    . GLN A 1 148 ? 32.910  17.443  29.605 1.00 91.07  ? 145 GLN A O    1 
ATOM   2438 C  CB   . GLN A 1 148 ? 33.857  20.545  29.094 1.00 103.71 ? 145 GLN A CB   1 
ATOM   2439 C  CG   . GLN A 1 148 ? 35.110  19.702  28.883 1.00 106.82 ? 145 GLN A CG   1 
ATOM   2440 C  CD   . GLN A 1 148 ? 34.984  18.681  27.753 1.00 103.66 ? 145 GLN A CD   1 
ATOM   2441 O  OE1  . GLN A 1 148 ? 33.882  18.344  27.304 1.00 100.00 ? 145 GLN A OE1  1 
ATOM   2442 N  NE2  . GLN A 1 148 ? 36.127  18.191  27.282 1.00 89.83  ? 145 GLN A NE2  1 
ATOM   2443 H  H    . GLN A 1 148 ? 32.335  21.341  30.811 1.00 127.51 ? 145 GLN A H    1 
ATOM   2444 H  HA   . GLN A 1 148 ? 32.065  19.599  28.803 1.00 125.77 ? 145 GLN A HA   1 
ATOM   2445 H  HB2  . GLN A 1 148 ? 33.649  20.960  28.242 1.00 124.48 ? 145 GLN A HB2  1 
ATOM   2446 H  HB3  . GLN A 1 148 ? 34.081  21.225  29.748 1.00 124.48 ? 145 GLN A HB3  1 
ATOM   2447 H  HG2  . GLN A 1 148 ? 35.850  20.291  28.668 1.00 128.22 ? 145 GLN A HG2  1 
ATOM   2448 H  HG3  . GLN A 1 148 ? 35.300  19.216  29.701 1.00 128.22 ? 145 GLN A HG3  1 
ATOM   2449 H  HE21 . GLN A 1 148 ? 36.876  18.453  27.614 1.00 107.83 ? 145 GLN A HE21 1 
ATOM   2450 H  HE22 . GLN A 1 148 ? 36.118  17.613  26.645 1.00 107.83 ? 145 GLN A HE22 1 
ATOM   2451 N  N    . GLN A 1 149 ? 33.216  18.534  31.563 1.00 98.56  ? 146 GLN A N    1 
ATOM   2452 C  CA   . GLN A 1 149 ? 33.641  17.339  32.285 1.00 87.89  ? 146 GLN A CA   1 
ATOM   2453 C  C    . GLN A 1 149 ? 32.548  16.280  32.285 1.00 78.62  ? 146 GLN A C    1 
ATOM   2454 O  O    . GLN A 1 149 ? 32.808  15.102  32.009 1.00 77.79  ? 146 GLN A O    1 
ATOM   2455 C  CB   . GLN A 1 149 ? 34.009  17.727  33.714 1.00 95.15  ? 146 GLN A CB   1 
ATOM   2456 C  CG   . GLN A 1 149 ? 35.247  18.603  33.808 1.00 104.48 ? 146 GLN A CG   1 
ATOM   2457 C  CD   . GLN A 1 149 ? 34.909  20.033  34.196 1.00 103.98 ? 146 GLN A CD   1 
ATOM   2458 O  OE1  . GLN A 1 149 ? 34.265  20.758  33.433 1.00 105.43 ? 146 GLN A OE1  1 
ATOM   2459 N  NE2  . GLN A 1 149 ? 35.346  20.447  35.386 1.00 102.63 ? 146 GLN A NE2  1 
ATOM   2460 H  H    . GLN A 1 149 ? 33.166  19.240  32.051 1.00 118.30 ? 146 GLN A H    1 
ATOM   2461 H  HA   . GLN A 1 149 ? 34.421  16.961  31.850 1.00 105.50 ? 146 GLN A HA   1 
ATOM   2462 H  HB2  . GLN A 1 149 ? 33.269  18.217  34.105 1.00 114.21 ? 146 GLN A HB2  1 
ATOM   2463 H  HB3  . GLN A 1 149 ? 34.178  16.919  34.223 1.00 114.21 ? 146 GLN A HB3  1 
ATOM   2464 H  HG2  . GLN A 1 149 ? 35.844  18.239  34.480 1.00 125.41 ? 146 GLN A HG2  1 
ATOM   2465 H  HG3  . GLN A 1 149 ? 35.690  18.620  32.945 1.00 125.41 ? 146 GLN A HG3  1 
ATOM   2466 H  HE21 . GLN A 1 149 ? 35.794  19.913  35.890 1.00 123.19 ? 146 GLN A HE21 1 
ATOM   2467 H  HE22 . GLN A 1 149 ? 35.180  21.249  35.650 1.00 123.19 ? 146 GLN A HE22 1 
ATOM   2468 N  N    . ALA A 1 150 ? 31.317  16.689  32.600 1.00 91.72  ? 147 ALA A N    1 
ATOM   2469 C  CA   . ALA A 1 150 ? 30.184  15.771  32.583 1.00 87.42  ? 147 ALA A CA   1 
ATOM   2470 C  C    . ALA A 1 150 ? 30.034  15.091  31.229 1.00 76.82  ? 147 ALA A C    1 
ATOM   2471 O  O    . ALA A 1 150 ? 29.946  13.860  31.149 1.00 87.09  ? 147 ALA A O    1 
ATOM   2472 C  CB   . ALA A 1 150 ? 28.902  16.526  32.941 1.00 89.22  ? 147 ALA A CB   1 
ATOM   2473 H  H    . ALA A 1 150 ? 31.113  17.493  32.827 1.00 110.10 ? 147 ALA A H    1 
ATOM   2474 H  HA   . ALA A 1 150 ? 30.336  15.082  33.248 1.00 104.93 ? 147 ALA A HA   1 
ATOM   2475 H  HB1  . ALA A 1 150 ? 28.152  15.911  32.901 1.00 107.10 ? 147 ALA A HB1  1 
ATOM   2476 H  HB2  . ALA A 1 150 ? 28.987  16.885  33.838 1.00 107.10 ? 147 ALA A HB2  1 
ATOM   2477 H  HB3  . ALA A 1 150 ? 28.772  17.247  32.306 1.00 107.10 ? 147 ALA A HB3  1 
ATOM   2478 N  N    . SER A 1 151 ? 29.991  15.880  30.149 1.00 83.27  ? 148 SER A N    1 
ATOM   2479 C  CA   . SER A 1 151 ? 29.735  15.314  28.824 1.00 72.16  ? 148 SER A CA   1 
ATOM   2480 C  C    . SER A 1 151 ? 30.595  14.081  28.565 1.00 79.40  ? 148 SER A C    1 
ATOM   2481 O  O    . SER A 1 151 ? 30.099  13.057  28.074 1.00 76.26  ? 148 SER A O    1 
ATOM   2482 C  CB   . SER A 1 151 ? 29.978  16.370  27.740 1.00 75.69  ? 148 SER A CB   1 
ATOM   2483 O  OG   . SER A 1 151 ? 29.440  17.632  28.108 1.00 91.12  ? 148 SER A OG   1 
ATOM   2484 H  H    . SER A 1 151 ? 30.105  16.733  30.158 1.00 99.96  ? 148 SER A H    1 
ATOM   2485 H  HA   . SER A 1 151 ? 28.804  15.046  28.781 1.00 86.63  ? 148 SER A HA   1 
ATOM   2486 H  HB2  . SER A 1 151 ? 30.933  16.466  27.605 1.00 90.86  ? 148 SER A HB2  1 
ATOM   2487 H  HB3  . SER A 1 151 ? 29.554  16.077  26.918 1.00 90.86  ? 148 SER A HB3  1 
ATOM   2488 H  HG   . SER A 1 151 ? 29.977  18.038  28.609 1.00 109.38 ? 148 SER A HG   1 
ATOM   2489 N  N    . SER A 1 152 ? 31.882  14.149  28.919 1.00 86.20  ? 149 SER A N    1 
ATOM   2490 C  CA   . SER A 1 152 ? 32.792  13.052  28.602 1.00 82.59  ? 149 SER A CA   1 
ATOM   2491 C  C    . SER A 1 152 ? 32.487  11.808  29.429 1.00 77.90  ? 149 SER A C    1 
ATOM   2492 O  O    . SER A 1 152 ? 32.573  10.683  28.920 1.00 77.51  ? 149 SER A O    1 
ATOM   2493 C  CB   . SER A 1 152 ? 34.240  13.493  28.826 1.00 90.29  ? 149 SER A CB   1 
ATOM   2494 O  OG   . SER A 1 152 ? 35.117  12.384  28.702 1.00 99.11  ? 149 SER A OG   1 
ATOM   2495 H  H    . SER A 1 152 ? 32.245  14.808  29.335 1.00 103.47 ? 149 SER A H    1 
ATOM   2496 H  HA   . SER A 1 152 ? 32.681  12.824  27.666 1.00 99.14  ? 149 SER A HA   1 
ATOM   2497 H  HB2  . SER A 1 152 ? 34.476  14.160  28.163 1.00 108.39 ? 149 SER A HB2  1 
ATOM   2498 H  HB3  . SER A 1 152 ? 34.325  13.866  29.717 1.00 108.39 ? 149 SER A HB3  1 
ATOM   2499 H  HG   . SER A 1 152 ? 35.865  12.570  29.035 1.00 118.97 ? 149 SER A HG   1 
ATOM   2500 N  N    . ALA A 1 153 ? 32.151  11.986  30.710 1.00 74.70  ? 150 ALA A N    1 
ATOM   2501 C  CA   . ALA A 1 153 ? 31.814  10.842  31.551 1.00 73.81  ? 150 ALA A CA   1 
ATOM   2502 C  C    . ALA A 1 153 ? 30.559  10.150  31.038 1.00 78.21  ? 150 ALA A C    1 
ATOM   2503 O  O    . ALA A 1 153 ? 30.451  8.918   31.085 1.00 82.30  ? 150 ALA A O    1 
ATOM   2504 C  CB   . ALA A 1 153 ? 31.621  11.290  33.001 1.00 71.33  ? 150 ALA A CB   1 
ATOM   2505 H  H    . ALA A 1 153 ? 32.112  12.748  31.108 1.00 89.67  ? 150 ALA A H    1 
ATOM   2506 H  HA   . ALA A 1 153 ? 32.547  10.208  31.530 1.00 88.61  ? 150 ALA A HA   1 
ATOM   2507 H  HB1  . ALA A 1 153 ? 31.770  10.532  33.588 1.00 85.63  ? 150 ALA A HB1  1 
ATOM   2508 H  HB2  . ALA A 1 153 ? 32.257  11.994  33.201 1.00 85.63  ? 150 ALA A HB2  1 
ATOM   2509 H  HB3  . ALA A 1 153 ? 30.716  11.621  33.111 1.00 85.63  ? 150 ALA A HB3  1 
ATOM   2510 N  N    . GLN A 1 154 ? 29.601  10.929  30.537 1.00 82.99  ? 151 GLN A N    1 
ATOM   2511 C  CA   . GLN A 1 154 ? 28.378  10.348  29.987 1.00 84.69  ? 151 GLN A CA   1 
ATOM   2512 C  C    . GLN A 1 154 ? 28.709  9.387   28.852 1.00 80.51  ? 151 GLN A C    1 
ATOM   2513 O  O    . GLN A 1 154 ? 28.195  8.260   28.801 1.00 75.74  ? 151 GLN A O    1 
ATOM   2514 C  CB   . GLN A 1 154 ? 27.459  11.471  29.501 1.00 69.25  ? 151 GLN A CB   1 
ATOM   2515 C  CG   . GLN A 1 154 ? 26.925  12.344  30.640 1.00 71.78  ? 151 GLN A CG   1 
ATOM   2516 C  CD   . GLN A 1 154 ? 25.798  11.710  31.437 1.00 57.93  ? 151 GLN A CD   1 
ATOM   2517 O  OE1  . GLN A 1 154 ? 25.169  10.758  31.001 1.00 62.88  ? 151 GLN A OE1  1 
ATOM   2518 N  NE2  . GLN A 1 154 ? 25.582  12.218  32.652 1.00 69.51  ? 151 GLN A NE2  1 
ATOM   2519 H  H    . GLN A 1 154 ? 29.633  11.788  30.503 1.00 99.62  ? 151 GLN A H    1 
ATOM   2520 H  HA   . GLN A 1 154 ? 27.911  9.850   30.676 1.00 101.67 ? 151 GLN A HA   1 
ATOM   2521 H  HB2  . GLN A 1 154 ? 27.955  12.042  28.893 1.00 83.13  ? 151 GLN A HB2  1 
ATOM   2522 H  HB3  . GLN A 1 154 ? 26.699  11.080  29.043 1.00 83.13  ? 151 GLN A HB3  1 
ATOM   2523 H  HG2  . GLN A 1 154 ? 27.652  12.529  31.256 1.00 86.17  ? 151 GLN A HG2  1 
ATOM   2524 H  HG3  . GLN A 1 154 ? 26.590  13.173  30.265 1.00 86.17  ? 151 GLN A HG3  1 
ATOM   2525 H  HE21 . GLN A 1 154 ? 26.068  12.867  32.939 1.00 83.45  ? 151 GLN A HE21 1 
ATOM   2526 H  HE22 . GLN A 1 154 ? 24.956  11.898  33.147 1.00 83.45  ? 151 GLN A HE22 1 
ATOM   2527 N  N    . LEU A 1 155 ? 29.597  9.813   27.945 1.00 82.29  ? 152 LEU A N    1 
ATOM   2528 C  CA   . LEU A 1 155 ? 29.929  9.009   26.769 1.00 79.85  ? 152 LEU A CA   1 
ATOM   2529 C  C    . LEU A 1 155 ? 30.796  7.807   27.142 1.00 75.67  ? 152 LEU A C    1 
ATOM   2530 O  O    . LEU A 1 155 ? 30.756  6.776   26.459 1.00 70.92  ? 152 LEU A O    1 
ATOM   2531 C  CB   . LEU A 1 155 ? 30.621  9.902   25.735 1.00 79.23  ? 152 LEU A CB   1 
ATOM   2532 C  CG   . LEU A 1 155 ? 29.664  10.955  25.156 1.00 87.41  ? 152 LEU A CG   1 
ATOM   2533 C  CD1  . LEU A 1 155 ? 30.377  12.061  24.375 1.00 78.29  ? 152 LEU A CD1  1 
ATOM   2534 C  CD2  . LEU A 1 155 ? 28.592  10.301  24.275 1.00 81.34  ? 152 LEU A CD2  1 
ATOM   2535 H  H    . LEU A 1 155 ? 30.018  10.562  27.989 1.00 98.78  ? 152 LEU A H    1 
ATOM   2536 H  HA   . LEU A 1 155 ? 29.119  8.659   26.366 1.00 95.85  ? 152 LEU A HA   1 
ATOM   2537 H  HB2  . LEU A 1 155 ? 31.362  10.363  26.158 1.00 95.12  ? 152 LEU A HB2  1 
ATOM   2538 H  HB3  . LEU A 1 155 ? 30.946  9.351   25.005 1.00 95.12  ? 152 LEU A HB3  1 
ATOM   2539 H  HG   . LEU A 1 155 ? 29.236  11.382  25.915 1.00 104.93 ? 152 LEU A HG   1 
ATOM   2540 H  HD11 . LEU A 1 155 ? 29.732  12.742  24.131 1.00 93.98  ? 152 LEU A HD11 1 
ATOM   2541 H  HD12 . LEU A 1 155 ? 31.070  12.446  24.934 1.00 93.98  ? 152 LEU A HD12 1 
ATOM   2542 H  HD13 . LEU A 1 155 ? 30.772  11.678  23.576 1.00 93.98  ? 152 LEU A HD13 1 
ATOM   2543 H  HD21 . LEU A 1 155 ? 28.232  10.967  23.668 1.00 97.64  ? 152 LEU A HD21 1 
ATOM   2544 H  HD22 . LEU A 1 155 ? 28.996  9.578   23.770 1.00 97.64  ? 152 LEU A HD22 1 
ATOM   2545 H  HD23 . LEU A 1 155 ? 27.885  9.954   24.842 1.00 97.64  ? 152 LEU A HD23 1 
ATOM   2546 N  N    . ALA A 1 156 ? 31.549  7.902   28.243 1.00 79.94  ? 153 ALA A N    1 
ATOM   2547 C  CA   . ALA A 1 156 ? 32.401  6.796   28.677 1.00 71.28  ? 153 ALA A CA   1 
ATOM   2548 C  C    . ALA A 1 156 ? 31.595  5.621   29.224 1.00 81.20  ? 153 ALA A C    1 
ATOM   2549 O  O    . ALA A 1 156 ? 32.064  4.477   29.180 1.00 82.08  ? 153 ALA A O    1 
ATOM   2550 C  CB   . ALA A 1 156 ? 33.395  7.302   29.725 1.00 79.52  ? 153 ALA A CB   1 
ATOM   2551 H  H    . ALA A 1 156 ? 31.583  8.593   28.754 1.00 95.96  ? 153 ALA A H    1 
ATOM   2552 H  HA   . ALA A 1 156 ? 32.900  6.466   27.913 1.00 85.58  ? 153 ALA A HA   1 
ATOM   2553 H  HB1  . ALA A 1 156 ? 33.798  6.541   30.171 1.00 95.45  ? 153 ALA A HB1  1 
ATOM   2554 H  HB2  . ALA A 1 156 ? 34.080  7.827   29.282 1.00 95.45  ? 153 ALA A HB2  1 
ATOM   2555 H  HB3  . ALA A 1 156 ? 32.921  7.851   30.369 1.00 95.45  ? 153 ALA A HB3  1 
ATOM   2556 N  N    . ALA A 1 157 ? 30.384  5.876   29.723 1.00 77.78  ? 154 ALA A N    1 
ATOM   2557 C  CA   . ALA A 1 157 ? 29.503  4.814   30.201 1.00 69.09  ? 154 ALA A CA   1 
ATOM   2558 C  C    . ALA A 1 157 ? 28.940  3.954   29.077 1.00 71.39  ? 154 ALA A C    1 
ATOM   2559 O  O    . ALA A 1 157 ? 28.301  2.930   29.353 1.00 61.75  ? 154 ALA A O    1 
ATOM   2560 C  CB   . ALA A 1 157 ? 28.336  5.417   30.997 1.00 68.29  ? 154 ALA A CB   1 
ATOM   2561 H  H    . ALA A 1 157 ? 30.047  6.663   29.795 1.00 93.38  ? 154 ALA A H    1 
ATOM   2562 H  HA   . ALA A 1 157 ? 30.017  4.240   30.791 1.00 82.94  ? 154 ALA A HA   1 
ATOM   2563 H  HB1  . ALA A 1 157 ? 27.765  4.699   31.313 1.00 81.98  ? 154 ALA A HB1  1 
ATOM   2564 H  HB2  . ALA A 1 157 ? 28.692  5.913   31.751 1.00 81.98  ? 154 ALA A HB2  1 
ATOM   2565 H  HB3  . ALA A 1 157 ? 27.833  6.010   30.418 1.00 81.98  ? 154 ALA A HB3  1 
ATOM   2566 N  N    . ILE A 1 158 ? 29.145  4.349   27.821 1.00 70.55  ? 155 ILE A N    1 
ATOM   2567 C  CA   . ILE A 1 158 ? 28.589  3.594   26.698 1.00 70.25  ? 155 ILE A CA   1 
ATOM   2568 C  C    . ILE A 1 158 ? 29.139  2.168   26.694 1.00 65.66  ? 155 ILE A C    1 
ATOM   2569 O  O    . ILE A 1 158 ? 28.416  1.206   26.403 1.00 61.62  ? 155 ILE A O    1 
ATOM   2570 C  CB   . ILE A 1 158 ? 28.897  4.344   25.384 1.00 74.63  ? 155 ILE A CB   1 
ATOM   2571 C  CG1  . ILE A 1 158 ? 27.868  5.467   25.190 1.00 70.81  ? 155 ILE A CG1  1 
ATOM   2572 C  CG2  . ILE A 1 158 ? 28.902  3.391   24.198 1.00 73.22  ? 155 ILE A CG2  1 
ATOM   2573 C  CD1  . ILE A 1 158 ? 27.875  6.118   23.827 1.00 68.04  ? 155 ILE A CD1  1 
ATOM   2574 H  H    . ILE A 1 158 ? 29.597  5.044   27.593 1.00 84.70  ? 155 ILE A H    1 
ATOM   2575 H  HA   . ILE A 1 158 ? 27.626  3.529   26.792 1.00 84.33  ? 155 ILE A HA   1 
ATOM   2576 H  HB   . ILE A 1 158 ? 29.784  4.733   25.443 1.00 89.59  ? 155 ILE A HB   1 
ATOM   2577 H  HG12 . ILE A 1 158 ? 26.982  5.098   25.331 1.00 85.00  ? 155 ILE A HG12 1 
ATOM   2578 H  HG13 . ILE A 1 158 ? 28.046  6.162   25.844 1.00 85.00  ? 155 ILE A HG13 1 
ATOM   2579 H  HG21 . ILE A 1 158 ? 29.076  3.895   23.388 1.00 87.90  ? 155 ILE A HG21 1 
ATOM   2580 H  HG22 . ILE A 1 158 ? 29.596  2.726   24.330 1.00 87.90  ? 155 ILE A HG22 1 
ATOM   2581 H  HG23 . ILE A 1 158 ? 28.036  2.957   24.138 1.00 87.90  ? 155 ILE A HG23 1 
ATOM   2582 H  HD11 . ILE A 1 158 ? 27.215  6.828   23.813 1.00 81.68  ? 155 ILE A HD11 1 
ATOM   2583 H  HD12 . ILE A 1 158 ? 28.758  6.483   23.656 1.00 81.68  ? 155 ILE A HD12 1 
ATOM   2584 H  HD13 . ILE A 1 158 ? 27.658  5.450   23.158 1.00 81.68  ? 155 ILE A HD13 1 
ATOM   2585 N  N    . ASP A 1 159 ? 30.415  2.009   27.052 1.00 73.97  ? 156 ASP A N    1 
ATOM   2586 C  CA   . ASP A 1 159 ? 31.063  0.701   27.000 1.00 75.37  ? 156 ASP A CA   1 
ATOM   2587 C  C    . ASP A 1 159 ? 30.315  -0.350  27.821 1.00 68.49  ? 156 ASP A C    1 
ATOM   2588 O  O    . ASP A 1 159 ? 30.312  -1.528  27.447 1.00 72.54  ? 156 ASP A O    1 
ATOM   2589 C  CB   . ASP A 1 159 ? 32.518  0.840   27.482 1.00 78.46  ? 156 ASP A CB   1 
ATOM   2590 C  CG   . ASP A 1 159 ? 33.475  1.290   26.367 1.00 94.60  ? 156 ASP A CG   1 
ATOM   2591 O  OD1  . ASP A 1 159 ? 32.993  1.678   25.279 1.00 98.03  ? 156 ASP A OD1  1 
ATOM   2592 O  OD2  . ASP A 1 159 ? 34.710  1.271   26.582 1.00 100.12 ? 156 ASP A OD2  1 
ATOM   2593 H  H    . ASP A 1 159 ? 30.927  2.642   27.329 1.00 88.80  ? 156 ASP A H    1 
ATOM   2594 H  HA   . ASP A 1 159 ? 31.069  0.386   26.083 1.00 90.47  ? 156 ASP A HA   1 
ATOM   2595 H  HB2  . ASP A 1 159 ? 32.554  1.499   28.192 1.00 94.18  ? 156 ASP A HB2  1 
ATOM   2596 H  HB3  . ASP A 1 159 ? 32.825  -0.020  27.811 1.00 94.18  ? 156 ASP A HB3  1 
ATOM   2597 N  N    . ASP A 1 160 ? 29.670  0.042   28.924 1.00 66.69  ? 157 ASP A N    1 
ATOM   2598 C  CA   . ASP A 1 160 ? 28.945  -0.901  29.778 1.00 60.93  ? 157 ASP A CA   1 
ATOM   2599 C  C    . ASP A 1 160 ? 27.564  -1.274  29.246 1.00 63.44  ? 157 ASP A C    1 
ATOM   2600 O  O    . ASP A 1 160 ? 26.862  -2.085  29.876 1.00 56.87  ? 157 ASP A O    1 
ATOM   2601 C  CB   . ASP A 1 160 ? 28.768  -0.309  31.175 1.00 64.28  ? 157 ASP A CB   1 
ATOM   2602 C  CG   . ASP A 1 160 ? 30.054  -0.265  31.955 1.00 74.78  ? 157 ASP A CG   1 
ATOM   2603 O  OD1  . ASP A 1 160 ? 30.914  -1.148  31.744 1.00 85.02  ? 157 ASP A OD1  1 
ATOM   2604 O  OD2  . ASP A 1 160 ? 30.206  0.672   32.770 1.00 80.77  ? 157 ASP A OD2  1 
ATOM   2605 H  H    . ASP A 1 160 ? 29.638  0.855   29.200 1.00 80.06  ? 157 ASP A H    1 
ATOM   2606 H  HA   . ASP A 1 160 ? 29.478  -1.709  29.837 1.00 73.16  ? 157 ASP A HA   1 
ATOM   2607 H  HB2  . ASP A 1 160 ? 28.434  0.598   31.094 1.00 77.17  ? 157 ASP A HB2  1 
ATOM   2608 H  HB3  . ASP A 1 160 ? 28.135  -0.852  31.670 1.00 77.17  ? 157 ASP A HB3  1 
ATOM   2609 N  N    . TYR A 1 161 ? 27.143  -0.685  28.138 1.00 53.69  ? 158 TYR A N    1 
ATOM   2610 C  CA   . TYR A 1 161 ? 25.847  -0.954  27.532 1.00 54.24  ? 158 TYR A CA   1 
ATOM   2611 C  C    . TYR A 1 161 ? 25.930  -2.040  26.458 1.00 50.41  ? 158 TYR A C    1 
ATOM   2612 O  O    . TYR A 1 161 ? 24.914  -2.367  25.843 1.00 46.42  ? 158 TYR A O    1 
ATOM   2613 C  CB   . TYR A 1 161 ? 25.295  0.358   26.947 1.00 54.15  ? 158 TYR A CB   1 
ATOM   2614 C  CG   . TYR A 1 161 ? 23.786  0.432   26.823 1.00 49.29  ? 158 TYR A CG   1 
ATOM   2615 C  CD1  . TYR A 1 161 ? 22.956  0.224   27.930 1.00 47.78  ? 158 TYR A CD1  1 
ATOM   2616 C  CD2  . TYR A 1 161 ? 23.192  0.703   25.594 1.00 48.41  ? 158 TYR A CD2  1 
ATOM   2617 C  CE1  . TYR A 1 161 ? 21.552  0.278   27.799 1.00 48.36  ? 158 TYR A CE1  1 
ATOM   2618 C  CE2  . TYR A 1 161 ? 21.805  0.755   25.447 1.00 40.60  ? 158 TYR A CE2  1 
ATOM   2619 C  CZ   . TYR A 1 161 ? 20.992  0.548   26.565 1.00 43.20  ? 158 TYR A CZ   1 
ATOM   2620 O  OH   . TYR A 1 161 ? 19.610  0.609   26.403 1.00 39.92  ? 158 TYR A OH   1 
ATOM   2621 H  H    . TYR A 1 161 ? 27.605  -0.105  27.703 1.00 64.47  ? 158 TYR A H    1 
ATOM   2622 H  HA   . TYR A 1 161 ? 25.217  -1.265  28.200 1.00 65.13  ? 158 TYR A HA   1 
ATOM   2623 H  HB2  . TYR A 1 161 ? 25.574  1.090   27.520 1.00 65.02  ? 158 TYR A HB2  1 
ATOM   2624 H  HB3  . TYR A 1 161 ? 25.664  0.475   26.057 1.00 65.02  ? 158 TYR A HB3  1 
ATOM   2625 H  HD1  . TYR A 1 161 ? 23.334  0.047   28.761 1.00 57.37  ? 158 TYR A HD1  1 
ATOM   2626 H  HD2  . TYR A 1 161 ? 23.733  0.853   24.852 1.00 58.13  ? 158 TYR A HD2  1 
ATOM   2627 H  HE1  . TYR A 1 161 ? 21.007  0.132   28.539 1.00 58.07  ? 158 TYR A HE1  1 
ATOM   2628 H  HE2  . TYR A 1 161 ? 21.426  0.926   24.615 1.00 48.75  ? 158 TYR A HE2  1 
ATOM   2629 H  HH   . TYR A 1 161 ? 19.228  0.472   27.139 1.00 47.94  ? 158 TYR A HH   1 
ATOM   2630 N  N    . GLU A 1 162 ? 27.109  -2.641  26.260 1.00 53.99  ? 159 GLU A N    1 
ATOM   2631 C  CA   . GLU A 1 162 ? 27.300  -3.543  25.130 1.00 53.32  ? 159 GLU A CA   1 
ATOM   2632 C  C    . GLU A 1 162 ? 26.316  -4.703  25.170 1.00 48.64  ? 159 GLU A C    1 
ATOM   2633 O  O    . GLU A 1 162 ? 25.764  -5.087  24.135 1.00 48.95  ? 159 GLU A O    1 
ATOM   2634 C  CB   . GLU A 1 162 ? 28.743  -4.046  25.116 1.00 56.58  ? 159 GLU A CB   1 
ATOM   2635 C  CG   . GLU A 1 162 ? 29.051  -5.152  24.121 1.00 70.68  ? 159 GLU A CG   1 
ATOM   2636 C  CD   . GLU A 1 162 ? 30.440  -5.759  24.358 1.00 88.69  ? 159 GLU A CD   1 
ATOM   2637 O  OE1  . GLU A 1 162 ? 30.782  -6.758  23.690 1.00 95.79  ? 159 GLU A OE1  1 
ATOM   2638 O  OE2  . GLU A 1 162 ? 31.188  -5.230  25.214 1.00 85.41  ? 159 GLU A OE2  1 
ATOM   2639 H  H    . GLU A 1 162 ? 27.802  -2.543  26.761 1.00 64.82  ? 159 GLU A H    1 
ATOM   2640 H  HA   . GLU A 1 162 ? 27.141  -3.058  24.304 1.00 64.02  ? 159 GLU A HA   1 
ATOM   2641 H  HB2  . GLU A 1 162 ? 29.323  -3.298  24.903 1.00 67.93  ? 159 GLU A HB2  1 
ATOM   2642 H  HB3  . GLU A 1 162 ? 28.953  -4.388  25.999 1.00 67.93  ? 159 GLU A HB3  1 
ATOM   2643 H  HG2  . GLU A 1 162 ? 28.391  -5.857  24.211 1.00 84.85  ? 159 GLU A HG2  1 
ATOM   2644 H  HG3  . GLU A 1 162 ? 29.027  -4.789  23.221 1.00 84.85  ? 159 GLU A HG3  1 
ATOM   2645 N  N    . GLY A 1 163 ? 26.090  -5.287  26.346 1.00 48.71  ? 160 GLY A N    1 
ATOM   2646 C  CA   . GLY A 1 163 ? 25.143  -6.388  26.418 1.00 45.20  ? 160 GLY A CA   1 
ATOM   2647 C  C    . GLY A 1 163 ? 23.733  -5.967  26.059 1.00 45.31  ? 160 GLY A C    1 
ATOM   2648 O  O    . GLY A 1 163 ? 22.969  -6.737  25.462 1.00 46.77  ? 160 GLY A O    1 
ATOM   2649 H  H    . GLY A 1 163 ? 26.461  -5.070  27.091 1.00 58.49  ? 160 GLY A H    1 
ATOM   2650 H  HA2  . GLY A 1 163 ? 25.418  -7.087  25.805 1.00 54.28  ? 160 GLY A HA2  1 
ATOM   2651 H  HA3  . GLY A 1 163 ? 25.134  -6.744  27.321 1.00 54.28  ? 160 GLY A HA3  1 
ATOM   2652 N  N    A GLU A 1 164 ? 23.358  -4.739  26.423 0.52 44.55  ? 161 GLU A N    1 
ATOM   2653 N  N    B GLU A 1 164 ? 23.358  -4.745  26.413 0.48 44.55  ? 161 GLU A N    1 
ATOM   2654 C  CA   A GLU A 1 164 ? 22.018  -4.258  26.100 0.52 39.19  ? 161 GLU A CA   1 
ATOM   2655 C  CA   B GLU A 1 164 ? 22.019  -4.277  26.089 0.48 39.22  ? 161 GLU A CA   1 
ATOM   2656 C  C    A GLU A 1 164 ? 21.890  -3.922  24.617 0.52 39.83  ? 161 GLU A C    1 
ATOM   2657 C  C    B GLU A 1 164 ? 21.889  -3.918  24.617 0.48 39.83  ? 161 GLU A C    1 
ATOM   2658 O  O    A GLU A 1 164 ? 20.785  -3.977  24.067 0.52 37.62  ? 161 GLU A O    1 
ATOM   2659 O  O    B GLU A 1 164 ? 20.778  -3.965  24.081 0.48 37.64  ? 161 GLU A O    1 
ATOM   2660 C  CB   A GLU A 1 164 ? 21.684  -3.053  26.976 0.52 44.10  ? 161 GLU A CB   1 
ATOM   2661 C  CB   B GLU A 1 164 ? 21.669  -3.091  26.980 0.48 44.09  ? 161 GLU A CB   1 
ATOM   2662 C  CG   A GLU A 1 164 ? 21.446  -3.447  28.450 0.52 44.76  ? 161 GLU A CG   1 
ATOM   2663 C  CG   B GLU A 1 164 ? 21.655  -3.463  28.475 0.48 44.55  ? 161 GLU A CG   1 
ATOM   2664 C  CD   A GLU A 1 164 ? 22.639  -3.189  29.359 0.52 45.04  ? 161 GLU A CD   1 
ATOM   2665 C  CD   B GLU A 1 164 ? 20.736  -4.645  28.810 0.48 46.15  ? 161 GLU A CD   1 
ATOM   2666 O  OE1  A GLU A 1 164 ? 23.793  -3.322  28.902 0.52 44.07  ? 161 GLU A OE1  1 
ATOM   2667 O  OE1  B GLU A 1 164 ? 19.633  -4.741  28.226 0.48 51.00  ? 161 GLU A OE1  1 
ATOM   2668 O  OE2  A GLU A 1 164 ? 22.430  -2.875  30.549 0.52 56.86  ? 161 GLU A OE2  1 
ATOM   2669 O  OE2  B GLU A 1 164 ? 21.121  -5.474  29.660 0.48 56.89  ? 161 GLU A OE2  1 
ATOM   2670 H  H    A GLU A 1 164 ? 23.851  -4.178  26.848 0.52 53.49  ? 161 GLU A H    1 
ATOM   2671 H  H    B GLU A 1 164 ? 23.850  -4.179  26.833 0.48 53.49  ? 161 GLU A H    1 
ATOM   2672 H  HA   A GLU A 1 164 ? 21.368  -4.951  26.294 0.52 47.06  ? 161 GLU A HA   1 
ATOM   2673 H  HA   B GLU A 1 164 ? 21.365  -4.969  26.272 0.48 47.10  ? 161 GLU A HA   1 
ATOM   2674 H  HB2  A GLU A 1 164 ? 22.422  -2.425  26.947 0.52 52.96  ? 161 GLU A HB2  1 
ATOM   2675 H  HB2  B GLU A 1 164 ? 22.328  -2.391  26.849 0.48 52.95  ? 161 GLU A HB2  1 
ATOM   2676 H  HB3  A GLU A 1 164 ? 20.876  -2.633  26.642 0.52 52.96  ? 161 GLU A HB3  1 
ATOM   2677 H  HB3  B GLU A 1 164 ? 20.787  -2.765  26.742 0.48 52.95  ? 161 GLU A HB3  1 
ATOM   2678 H  HG2  A GLU A 1 164 ? 20.698  -2.934  28.793 0.52 53.75  ? 161 GLU A HG2  1 
ATOM   2679 H  HG2  B GLU A 1 164 ? 22.555  -3.702  28.745 0.48 53.50  ? 161 GLU A HG2  1 
ATOM   2680 H  HG3  A GLU A 1 164 ? 21.245  -4.395  28.491 0.52 53.75  ? 161 GLU A HG3  1 
ATOM   2681 H  HG3  B GLU A 1 164 ? 21.348  -2.696  28.984 0.48 53.50  ? 161 GLU A HG3  1 
ATOM   2682 N  N    . ILE A 1 165 ? 23.000  -3.591  23.956 1.00 44.08  ? 162 ILE A N    1 
ATOM   2683 C  CA   . ILE A 1 165 ? 22.974  -3.394  22.508 1.00 38.05  ? 162 ILE A CA   1 
ATOM   2684 C  C    . ILE A 1 165 ? 22.700  -4.724  21.817 1.00 39.97  ? 162 ILE A C    1 
ATOM   2685 O  O    . ILE A 1 165 ? 21.871  -4.812  20.909 1.00 37.54  ? 162 ILE A O    1 
ATOM   2686 C  CB   . ILE A 1 165 ? 24.299  -2.765  22.024 1.00 43.02  ? 162 ILE A CB   1 
ATOM   2687 C  CG1  . ILE A 1 165 ? 24.391  -1.322  22.531 1.00 46.16  ? 162 ILE A CG1  1 
ATOM   2688 C  CG2  . ILE A 1 165 ? 24.399  -2.864  20.485 1.00 47.98  ? 162 ILE A CG2  1 
ATOM   2689 C  CD1  . ILE A 1 165 ? 25.318  -0.415  21.757 1.00 60.01  ? 162 ILE A CD1  1 
ATOM   2690 H  H    . ILE A 1 165 ? 23.770  -3.475  24.321 1.00 52.93  ? 162 ILE A H    1 
ATOM   2691 H  HA   . ILE A 1 165 ? 22.258  -2.777  22.285 1.00 45.70  ? 162 ILE A HA   1 
ATOM   2692 H  HB   . ILE A 1 165 ? 25.054  -3.253  22.388 1.00 51.66  ? 162 ILE A HB   1 
ATOM   2693 H  HG12 . ILE A 1 165 ? 23.505  -0.928  22.493 1.00 55.42  ? 162 ILE A HG12 1 
ATOM   2694 H  HG13 . ILE A 1 165 ? 24.707  -1.341  23.448 1.00 55.42  ? 162 ILE A HG13 1 
ATOM   2695 H  HG21 . ILE A 1 165 ? 25.230  -2.455  20.196 1.00 57.61  ? 162 ILE A HG21 1 
ATOM   2696 H  HG22 . ILE A 1 165 ? 24.383  -3.799  20.227 1.00 57.61  ? 162 ILE A HG22 1 
ATOM   2697 H  HG23 . ILE A 1 165 ? 23.646  -2.398  20.089 1.00 57.61  ? 162 ILE A HG23 1 
ATOM   2698 H  HD11 . ILE A 1 165 ? 25.313  0.465   22.166 1.00 72.04  ? 162 ILE A HD11 1 
ATOM   2699 H  HD12 . ILE A 1 165 ? 26.214  -0.785  21.781 1.00 72.04  ? 162 ILE A HD12 1 
ATOM   2700 H  HD13 . ILE A 1 165 ? 25.008  -0.355  20.840 1.00 72.04  ? 162 ILE A HD13 1 
ATOM   2701 N  N    . THR A 1 166 ? 23.392  -5.780  22.248 1.00 40.58  ? 163 THR A N    1 
ATOM   2702 C  CA   . THR A 1 166 ? 23.141  -7.116  21.722 1.00 43.35  ? 163 THR A CA   1 
ATOM   2703 C  C    . THR A 1 166 ? 21.681  -7.525  21.919 1.00 37.77  ? 163 THR A C    1 
ATOM   2704 O  O    . THR A 1 166 ? 21.033  -8.021  20.989 1.00 39.31  ? 163 THR A O    1 
ATOM   2705 C  CB   . THR A 1 166 ? 24.104  -8.102  22.394 1.00 46.08  ? 163 THR A CB   1 
ATOM   2706 O  OG1  . THR A 1 166 ? 25.453  -7.722  22.097 1.00 50.69  ? 163 THR A OG1  1 
ATOM   2707 C  CG2  . THR A 1 166 ? 23.867  -9.517  21.902 1.00 51.19  ? 163 THR A CG2  1 
ATOM   2708 H  H    . THR A 1 166 ? 24.012  -5.747  22.844 1.00 48.73  ? 163 THR A H    1 
ATOM   2709 H  HA   . THR A 1 166 ? 23.309  -7.131  20.766 1.00 52.05  ? 163 THR A HA   1 
ATOM   2710 H  HB   . THR A 1 166 ? 23.958  -8.089  23.352 1.00 55.33  ? 163 THR A HB   1 
ATOM   2711 H  HG1  . THR A 1 166 ? 25.553  -6.897  22.220 1.00 60.86  ? 163 THR A HG1  1 
ATOM   2712 H  HG21 . THR A 1 166 ? 24.584  -10.097 22.201 1.00 61.46  ? 163 THR A HG21 1 
ATOM   2713 H  HG22 . THR A 1 166 ? 23.026  -9.852  22.249 1.00 61.46  ? 163 THR A HG22 1 
ATOM   2714 H  HG23 . THR A 1 166 ? 23.835  -9.530  20.933 1.00 61.46  ? 163 THR A HG23 1 
ATOM   2715 N  N    . LYS A 1 167 ? 21.127  -7.290  23.115 1.00 36.02  ? 164 LYS A N    1 
ATOM   2716 C  CA   . LYS A 1 167 ? 19.717  -7.603  23.346 1.00 34.78  ? 164 LYS A CA   1 
ATOM   2717 C  C    . LYS A 1 167 ? 18.801  -6.876  22.360 1.00 37.40  ? 164 LYS A C    1 
ATOM   2718 O  O    . LYS A 1 167 ? 17.825  -7.452  21.852 1.00 35.20  ? 164 LYS A O    1 
ATOM   2719 C  CB   . LYS A 1 167 ? 19.357  -7.236  24.790 1.00 39.63  ? 164 LYS A CB   1 
ATOM   2720 C  CG   . LYS A 1 167 ? 17.947  -7.581  25.204 1.00 51.33  ? 164 LYS A CG   1 
ATOM   2721 C  CD   . LYS A 1 167 ? 17.668  -7.111  26.641 1.00 61.56  ? 164 LYS A CD   1 
ATOM   2722 C  CE   . LYS A 1 167 ? 18.238  -8.072  27.688 1.00 70.91  ? 164 LYS A CE   1 
ATOM   2723 N  NZ   . LYS A 1 167 ? 17.268  -9.170  27.994 1.00 74.03  ? 164 LYS A NZ   1 
ATOM   2724 H  H    . LYS A 1 167 ? 21.539  -6.958  23.793 1.00 43.25  ? 164 LYS A H    1 
ATOM   2725 H  HA   . LYS A 1 167 ? 19.577  -8.554  23.216 1.00 41.78  ? 164 LYS A HA   1 
ATOM   2726 H  HB2  . LYS A 1 167 ? 19.959  -7.710  25.385 1.00 47.59  ? 164 LYS A HB2  1 
ATOM   2727 H  HB3  . LYS A 1 167 ? 19.466  -6.279  24.900 1.00 47.59  ? 164 LYS A HB3  1 
ATOM   2728 H  HG2  . LYS A 1 167 ? 17.319  -7.143  24.609 1.00 61.63  ? 164 LYS A HG2  1 
ATOM   2729 H  HG3  . LYS A 1 167 ? 17.825  -8.543  25.166 1.00 61.63  ? 164 LYS A HG3  1 
ATOM   2730 H  HD2  . LYS A 1 167 ? 18.076  -6.241  26.776 1.00 73.90  ? 164 LYS A HD2  1 
ATOM   2731 H  HD3  . LYS A 1 167 ? 16.709  -7.052  26.776 1.00 73.90  ? 164 LYS A HD3  1 
ATOM   2732 H  HE2  . LYS A 1 167 ? 19.056  -8.469  27.350 1.00 85.13  ? 164 LYS A HE2  1 
ATOM   2733 H  HE3  . LYS A 1 167 ? 18.419  -7.585  28.508 1.00 85.13  ? 164 LYS A HE3  1 
ATOM   2734 H  HZ1  . LYS A 1 167 ? 17.620  -9.729  28.591 1.00 88.87  ? 164 LYS A HZ1  1 
ATOM   2735 H  HZ2  . LYS A 1 167 ? 16.516  -8.829  28.325 1.00 88.87  ? 164 LYS A HZ2  1 
ATOM   2736 H  HZ3  . LYS A 1 167 ? 17.078  -9.624  27.252 1.00 88.87  ? 164 LYS A HZ3  1 
ATOM   2737 N  N    . PHE A 1 168 ? 19.087  -5.605  22.094 1.00 33.22  ? 165 PHE A N    1 
ATOM   2738 C  CA   . PHE A 1 168 ? 18.301  -4.824  21.144 1.00 28.91  ? 165 PHE A CA   1 
ATOM   2739 C  C    . PHE A 1 168 ? 18.405  -5.424  19.749 1.00 29.27  ? 165 PHE A C    1 
ATOM   2740 O  O    . PHE A 1 168 ? 17.395  -5.558  19.045 1.00 32.39  ? 165 PHE A O    1 
ATOM   2741 C  CB   . PHE A 1 168 ? 18.797  -3.371  21.228 1.00 29.59  ? 165 PHE A CB   1 
ATOM   2742 C  CG   . PHE A 1 168 ? 17.928  -2.338  20.528 1.00 35.68  ? 165 PHE A CG   1 
ATOM   2743 C  CD1  . PHE A 1 168 ? 16.744  -2.674  19.889 1.00 46.02  ? 165 PHE A CD1  1 
ATOM   2744 C  CD2  . PHE A 1 168 ? 18.319  -0.999  20.532 1.00 44.53  ? 165 PHE A CD2  1 
ATOM   2745 C  CE1  . PHE A 1 168 ? 15.989  -1.693  19.233 1.00 45.68  ? 165 PHE A CE1  1 
ATOM   2746 C  CE2  . PHE A 1 168 ? 17.559  -0.016  19.886 1.00 43.48  ? 165 PHE A CE2  1 
ATOM   2747 C  CZ   . PHE A 1 168 ? 16.406  -0.370  19.228 1.00 41.85  ? 165 PHE A CZ   1 
ATOM   2748 H  H    . PHE A 1 168 ? 19.735  -5.167  22.451 1.00 39.90  ? 165 PHE A H    1 
ATOM   2749 H  HA   . PHE A 1 168 ? 17.355  -4.825  21.359 1.00 34.73  ? 165 PHE A HA   1 
ATOM   2750 H  HB2  . PHE A 1 168 ? 18.846  -3.119  22.163 1.00 35.54  ? 165 PHE A HB2  1 
ATOM   2751 H  HB3  . PHE A 1 168 ? 19.678  -3.327  20.825 1.00 35.54  ? 165 PHE A HB3  1 
ATOM   2752 H  HD1  . PHE A 1 168 ? 16.449  -3.556  19.896 1.00 55.26  ? 165 PHE A HD1  1 
ATOM   2753 H  HD2  . PHE A 1 168 ? 19.101  -0.755  20.972 1.00 53.47  ? 165 PHE A HD2  1 
ATOM   2754 H  HE1  . PHE A 1 168 ? 15.202  -1.930  18.797 1.00 54.85  ? 165 PHE A HE1  1 
ATOM   2755 H  HE2  . PHE A 1 168 ? 17.833  0.872   19.902 1.00 52.21  ? 165 PHE A HE2  1 
ATOM   2756 H  HZ   . PHE A 1 168 ? 15.906  0.275   18.782 1.00 50.25  ? 165 PHE A HZ   1 
ATOM   2757 N  N    . GLN A 1 169 ? 19.606  -5.851  19.354 1.00 31.35  ? 166 GLN A N    1 
ATOM   2758 C  CA   . GLN A 1 169 ? 19.767  -6.476  18.047 1.00 29.41  ? 166 GLN A CA   1 
ATOM   2759 C  C    . GLN A 1 169 ? 18.934  -7.747  17.930 1.00 36.31  ? 166 GLN A C    1 
ATOM   2760 O  O    . GLN A 1 169 ? 18.299  -7.976  16.895 1.00 33.28  ? 166 GLN A O    1 
ATOM   2761 C  CB   . GLN A 1 169 ? 21.247  -6.774  17.807 1.00 39.05  ? 166 GLN A CB   1 
ATOM   2762 C  CG   . GLN A 1 169 ? 22.051  -5.505  17.523 1.00 45.13  ? 166 GLN A CG   1 
ATOM   2763 C  CD   . GLN A 1 169 ? 23.526  -5.754  17.381 1.00 57.40  ? 166 GLN A CD   1 
ATOM   2764 O  OE1  . GLN A 1 169 ? 24.117  -6.514  18.148 1.00 54.93  ? 166 GLN A OE1  1 
ATOM   2765 N  NE2  . GLN A 1 169 ? 24.137  -5.118  16.386 1.00 61.69  ? 166 GLN A NE2  1 
ATOM   2766 H  H    . GLN A 1 169 ? 20.328  -5.790  19.816 1.00 37.65  ? 166 GLN A H    1 
ATOM   2767 H  HA   . GLN A 1 169 ? 19.460  -5.863  17.361 1.00 35.32  ? 166 GLN A HA   1 
ATOM   2768 H  HB2  . GLN A 1 169 ? 21.618  -7.198  18.596 1.00 46.90  ? 166 GLN A HB2  1 
ATOM   2769 H  HB3  . GLN A 1 169 ? 21.332  -7.364  17.042 1.00 46.90  ? 166 GLN A HB3  1 
ATOM   2770 H  HG2  . GLN A 1 169 ? 21.735  -5.112  16.694 1.00 54.19  ? 166 GLN A HG2  1 
ATOM   2771 H  HG3  . GLN A 1 169 ? 21.924  -4.882  18.255 1.00 54.19  ? 166 GLN A HG3  1 
ATOM   2772 H  HE21 . GLN A 1 169 ? 23.688  -4.599  15.867 1.00 74.06  ? 166 GLN A HE21 1 
ATOM   2773 H  HE22 . GLN A 1 169 ? 24.981  -5.225  16.261 1.00 74.06  ? 166 GLN A HE22 1 
ATOM   2774 N  N    . HIS A 1 170 ? 18.950  -8.595  18.962 1.00 36.14  ? 167 HIS A N    1 
ATOM   2775 C  CA   . HIS A 1 170 ? 18.140  -9.810  18.937 1.00 34.15  ? 167 HIS A CA   1 
ATOM   2776 C  C    . HIS A 1 170 ? 16.655  -9.492  18.952 1.00 30.75  ? 167 HIS A C    1 
ATOM   2777 O  O    . HIS A 1 170 ? 15.876  -10.207 18.329 1.00 33.31  ? 167 HIS A O    1 
ATOM   2778 C  CB   . HIS A 1 170 ? 18.496  -10.715 20.114 1.00 37.74  ? 167 HIS A CB   1 
ATOM   2779 C  CG   . HIS A 1 170 ? 19.815  -11.416 19.964 1.00 57.46  ? 167 HIS A CG   1 
ATOM   2780 N  ND1  . HIS A 1 170 ? 21.022  -10.768 20.099 1.00 69.63  ? 167 HIS A ND1  1 
ATOM   2781 C  CD2  . HIS A 1 170 ? 20.113  -12.710 19.696 1.00 73.83  ? 167 HIS A CD2  1 
ATOM   2782 C  CE1  . HIS A 1 170 ? 22.008  -11.631 19.928 1.00 67.83  ? 167 HIS A CE1  1 
ATOM   2783 N  NE2  . HIS A 1 170 ? 21.484  -12.816 19.680 1.00 77.37  ? 167 HIS A NE2  1 
ATOM   2784 H  H    . HIS A 1 170 ? 19.415  -8.491  19.678 1.00 43.40  ? 167 HIS A H    1 
ATOM   2785 H  HA   . HIS A 1 170 ? 18.338  -10.295 18.121 1.00 41.02  ? 167 HIS A HA   1 
ATOM   2786 H  HB2  . HIS A 1 170 ? 18.537  -10.177 20.919 1.00 45.33  ? 167 HIS A HB2  1 
ATOM   2787 H  HB3  . HIS A 1 170 ? 17.809  -11.395 20.203 1.00 45.33  ? 167 HIS A HB3  1 
ATOM   2788 H  HD1  . HIS A 1 170 ? 21.120  -9.931  20.268 1.00 83.59  ? 167 HIS A HD1  1 
ATOM   2789 H  HD2  . HIS A 1 170 ? 19.505  -13.398 19.550 1.00 88.63  ? 167 HIS A HD2  1 
ATOM   2790 H  HE1  . HIS A 1 170 ? 22.916  -11.436 19.974 1.00 81.43  ? 167 HIS A HE1  1 
ATOM   2791 N  N    . PHE A 1 171 ? 16.249  -8.420  19.641 1.00 28.20  ? 168 PHE A N    1 
ATOM   2792 C  CA   . PHE A 1 171 ? 14.857  -7.972  19.633 1.00 27.18  ? 168 PHE A CA   1 
ATOM   2793 C  C    . PHE A 1 171 ? 14.384  -7.677  18.215 1.00 31.45  ? 168 PHE A C    1 
ATOM   2794 O  O    . PHE A 1 171 ? 13.280  -8.067  17.817 1.00 26.46  ? 168 PHE A O    1 
ATOM   2795 C  CB   . PHE A 1 171 ? 14.760  -6.733  20.531 1.00 29.35  ? 168 PHE A CB   1 
ATOM   2796 C  CG   . PHE A 1 171 ? 13.406  -6.103  20.594 1.00 28.40  ? 168 PHE A CG   1 
ATOM   2797 C  CD1  . PHE A 1 171 ? 12.509  -6.516  21.541 1.00 37.18  ? 168 PHE A CD1  1 
ATOM   2798 C  CD2  . PHE A 1 171 ? 13.088  -5.025  19.800 1.00 34.02  ? 168 PHE A CD2  1 
ATOM   2799 C  CE1  . PHE A 1 171 ? 11.286  -5.911  21.651 1.00 36.49  ? 168 PHE A CE1  1 
ATOM   2800 C  CE2  . PHE A 1 171 ? 11.866  -4.407  19.919 1.00 33.73  ? 168 PHE A CE2  1 
ATOM   2801 C  CZ   . PHE A 1 171 ? 10.965  -4.871  20.829 1.00 30.33  ? 168 PHE A CZ   1 
ATOM   2802 H  H    . PHE A 1 171 ? 16.765  -7.932  20.125 1.00 33.88  ? 168 PHE A H    1 
ATOM   2803 H  HA   . PHE A 1 171 ? 14.273  -8.662  19.983 1.00 32.65  ? 168 PHE A HA   1 
ATOM   2804 H  HB2  . PHE A 1 171 ? 15.003  -6.989  21.434 1.00 35.26  ? 168 PHE A HB2  1 
ATOM   2805 H  HB3  . PHE A 1 171 ? 15.377  -6.063  20.198 1.00 35.26  ? 168 PHE A HB3  1 
ATOM   2806 H  HD1  . PHE A 1 171 ? 12.732  -7.213  22.116 1.00 44.65  ? 168 PHE A HD1  1 
ATOM   2807 H  HD2  . PHE A 1 171 ? 13.705  -4.711  19.179 1.00 40.86  ? 168 PHE A HD2  1 
ATOM   2808 H  HE1  . PHE A 1 171 ? 10.674  -6.209  22.284 1.00 43.83  ? 168 PHE A HE1  1 
ATOM   2809 H  HE2  . PHE A 1 171 ? 11.655  -3.678  19.382 1.00 40.51  ? 168 PHE A HE2  1 
ATOM   2810 H  HZ   . PHE A 1 171 ? 10.126  -4.475  20.891 1.00 36.43  ? 168 PHE A HZ   1 
ATOM   2811 N  N    . ILE A 1 172 ? 15.201  -6.972  17.443 1.00 26.04  ? 169 ILE A N    1 
ATOM   2812 C  CA   . ILE A 1 172 ? 14.855  -6.677  16.046 1.00 23.39  ? 169 ILE A CA   1 
ATOM   2813 C  C    . ILE A 1 172 ? 14.756  -7.964  15.235 1.00 25.71  ? 169 ILE A C    1 
ATOM   2814 O  O    . ILE A 1 172 ? 13.798  -8.176  14.489 1.00 28.75  ? 169 ILE A O    1 
ATOM   2815 C  CB   . ILE A 1 172 ? 15.897  -5.726  15.433 1.00 28.92  ? 169 ILE A CB   1 
ATOM   2816 C  CG1  . ILE A 1 172 ? 15.992  -4.455  16.261 1.00 31.38  ? 169 ILE A CG1  1 
ATOM   2817 C  CG2  . ILE A 1 172 ? 15.545  -5.446  13.984 1.00 34.16  ? 169 ILE A CG2  1 
ATOM   2818 C  CD1  . ILE A 1 172 ? 16.903  -3.418  15.652 1.00 37.01  ? 169 ILE A CD1  1 
ATOM   2819 H  H    . ILE A 1 172 ? 15.958  -6.651  17.695 1.00 31.28  ? 169 ILE A H    1 
ATOM   2820 H  HA   . ILE A 1 172 ? 13.987  -6.243  16.033 1.00 28.11  ? 169 ILE A HA   1 
ATOM   2821 H  HB   . ILE A 1 172 ? 16.771  -6.145  15.447 1.00 34.74  ? 169 ILE A HB   1 
ATOM   2822 H  HG12 . ILE A 1 172 ? 15.107  -4.065  16.341 1.00 37.69  ? 169 ILE A HG12 1 
ATOM   2823 H  HG13 . ILE A 1 172 ? 16.338  -4.677  17.139 1.00 37.69  ? 169 ILE A HG13 1 
ATOM   2824 H  HG21 . ILE A 1 172 ? 16.222  -4.866  13.601 1.00 41.03  ? 169 ILE A HG21 1 
ATOM   2825 H  HG22 . ILE A 1 172 ? 15.516  -6.285  13.498 1.00 41.03  ? 169 ILE A HG22 1 
ATOM   2826 H  HG23 . ILE A 1 172 ? 14.679  -5.011  13.947 1.00 41.03  ? 169 ILE A HG23 1 
ATOM   2827 H  HD11 . ILE A 1 172 ? 17.103  -2.743  16.319 1.00 44.45  ? 169 ILE A HD11 1 
ATOM   2828 H  HD12 . ILE A 1 172 ? 17.722  -3.849  15.361 1.00 44.45  ? 169 ILE A HD12 1 
ATOM   2829 H  HD13 . ILE A 1 172 ? 16.455  -3.011  14.893 1.00 44.45  ? 169 ILE A HD13 1 
ATOM   2830 N  N    . ASP A 1 173 ? 15.751  -8.837  15.383 1.00 27.36  ? 170 ASP A N    1 
ATOM   2831 C  CA   . ASP A 1 173 ? 15.798  -10.093 14.629 1.00 30.41  ? 170 ASP A CA   1 
ATOM   2832 C  C    . ASP A 1 173 ? 14.564  -10.945 14.893 1.00 31.42  ? 170 ASP A C    1 
ATOM   2833 O  O    . ASP A 1 173 ? 13.985  -11.515 13.957 1.00 32.14  ? 170 ASP A O    1 
ATOM   2834 C  CB   . ASP A 1 173 ? 17.055  -10.888 14.990 1.00 31.63  ? 170 ASP A CB   1 
ATOM   2835 C  CG   . ASP A 1 173 ? 18.354  -10.263 14.441 1.00 41.52  ? 170 ASP A CG   1 
ATOM   2836 O  OD1  . ASP A 1 173 ? 18.306  -9.323  13.619 1.00 38.15  ? 170 ASP A OD1  1 
ATOM   2837 O  OD2  . ASP A 1 173 ? 19.431  -10.748 14.819 1.00 47.99  ? 170 ASP A OD2  1 
ATOM   2838 H  H    . ASP A 1 173 ? 16.418  -8.728  15.916 1.00 32.87  ? 170 ASP A H    1 
ATOM   2839 H  HA   . ASP A 1 173 ? 15.831  -9.875  13.685 1.00 36.53  ? 170 ASP A HA   1 
ATOM   2840 H  HB2  . ASP A 1 173 ? 17.131  -10.933 15.956 1.00 37.99  ? 170 ASP A HB2  1 
ATOM   2841 H  HB3  . ASP A 1 173 ? 16.977  -11.782 14.622 1.00 37.99  ? 170 ASP A HB3  1 
ATOM   2842 N  N    A ASP A 1 174 ? 14.133  -11.031 16.152 0.51 27.39  ? 171 ASP A N    1 
ATOM   2843 N  N    B ASP A 1 174 ? 14.156  -11.056 16.171 0.49 27.39  ? 171 ASP A N    1 
ATOM   2844 C  CA   A ASP A 1 174 ? 12.970  -11.848 16.473 0.51 31.78  ? 171 ASP A CA   1 
ATOM   2845 C  CA   B ASP A 1 174 ? 12.953  -11.815 16.520 0.49 31.78  ? 171 ASP A CA   1 
ATOM   2846 C  C    A ASP A 1 174 ? 11.685  -11.273 15.876 0.51 27.67  ? 171 ASP A C    1 
ATOM   2847 C  C    B ASP A 1 174 ? 11.736  -11.276 15.779 0.49 27.76  ? 171 ASP A C    1 
ATOM   2848 O  O    A ASP A 1 174 ? 10.781  -12.037 15.516 0.51 29.86  ? 171 ASP A O    1 
ATOM   2849 O  O    B ASP A 1 174 ? 10.948  -12.052 15.219 0.49 29.32  ? 171 ASP A O    1 
ATOM   2850 C  CB   A ASP A 1 174 ? 12.865  -11.986 17.992 0.51 30.77  ? 171 ASP A CB   1 
ATOM   2851 C  CB   B ASP A 1 174 ? 12.712  -11.770 18.041 0.49 30.58  ? 171 ASP A CB   1 
ATOM   2852 C  CG   A ASP A 1 174 ? 14.022  -12.775 18.594 0.51 36.54  ? 171 ASP A CG   1 
ATOM   2853 C  CG   B ASP A 1 174 ? 11.315  -12.314 18.465 0.49 32.50  ? 171 ASP A CG   1 
ATOM   2854 O  OD1  A ASP A 1 174 ? 14.860  -13.341 17.846 0.51 37.34  ? 171 ASP A OD1  1 
ATOM   2855 O  OD1  B ASP A 1 174 ? 11.070  -13.551 18.442 0.49 33.06  ? 171 ASP A OD1  1 
ATOM   2856 O  OD2  A ASP A 1 174 ? 14.108  -12.799 19.834 0.51 41.83  ? 171 ASP A OD2  1 
ATOM   2857 O  OD2  B ASP A 1 174 ? 10.446  -11.492 18.818 0.49 27.85  ? 171 ASP A OD2  1 
ATOM   2858 H  H    A ASP A 1 174 ? 14.491  -10.632 16.825 0.51 32.91  ? 171 ASP A H    1 
ATOM   2859 H  H    B ASP A 1 174 ? 14.556  -10.703 16.845 0.49 32.90  ? 171 ASP A H    1 
ATOM   2860 H  HA   A ASP A 1 174 ? 13.079  -12.734 16.094 0.51 38.17  ? 171 ASP A HA   1 
ATOM   2861 H  HA   B ASP A 1 174 ? 13.086  -12.742 16.266 0.49 38.17  ? 171 ASP A HA   1 
ATOM   2862 H  HB2  A ASP A 1 174 ? 12.866  -11.102 18.390 0.51 36.96  ? 171 ASP A HB2  1 
ATOM   2863 H  HB2  B ASP A 1 174 ? 13.387  -12.310 18.481 0.49 36.73  ? 171 ASP A HB2  1 
ATOM   2864 H  HB3  A ASP A 1 174 ? 12.041  -12.448 18.211 0.51 36.96  ? 171 ASP A HB3  1 
ATOM   2865 H  HB3  B ASP A 1 174 ? 12.776  -10.850 18.341 0.49 36.73  ? 171 ASP A HB3  1 
ATOM   2866 N  N    . ILE A 1 175 ? 11.582  -9.949  15.733 1.00 26.44  ? 172 ILE A N    1 
ATOM   2867 C  CA   . ILE A 1 175 ? 10.417  -9.358  15.069 1.00 24.67  ? 172 ILE A CA   1 
ATOM   2868 C  C    . ILE A 1 175 ? 10.467  -9.672  13.590 1.00 26.80  ? 172 ILE A C    1 
ATOM   2869 O  O    . ILE A 1 175 ? 9.477   -10.112 12.984 1.00 25.85  ? 172 ILE A O    1 
ATOM   2870 C  CB   . ILE A 1 175 ? 10.350  -7.833  15.299 1.00 23.53  ? 172 ILE A CB   1 
ATOM   2871 C  CG1  . ILE A 1 175 ? 10.145  -7.544  16.788 1.00 25.95  ? 172 ILE A CG1  1 
ATOM   2872 C  CG2  . ILE A 1 175 ? 9.247   -7.203  14.434 1.00 26.77  ? 172 ILE A CG2  1 
ATOM   2873 C  CD1  . ILE A 1 175 ? 10.244  -6.077  17.122 1.00 27.94  ? 172 ILE A CD1  1 
ATOM   2874 H  H    A ILE A 1 175 ? 12.165  -9.379  16.006 0.51 31.77  ? 172 ILE A H    1 
ATOM   2875 H  H    B ILE A 1 175 ? 12.129  -9.379  16.072 0.49 31.77  ? 172 ILE A H    1 
ATOM   2876 H  HA   . ILE A 1 175 ? 9.618   -9.748  15.458 1.00 29.64  ? 172 ILE A HA   1 
ATOM   2877 H  HB   . ILE A 1 175 ? 11.191  -7.432  15.029 1.00 28.27  ? 172 ILE A HB   1 
ATOM   2878 H  HG12 . ILE A 1 175 ? 9.263   -7.852  17.050 1.00 31.17  ? 172 ILE A HG12 1 
ATOM   2879 H  HG13 . ILE A 1 175 ? 10.825  -8.014  17.297 1.00 31.17  ? 172 ILE A HG13 1 
ATOM   2880 H  HG21 . ILE A 1 175 ? 9.134   -6.275  14.692 1.00 32.16  ? 172 ILE A HG21 1 
ATOM   2881 H  HG22 . ILE A 1 175 ? 9.508   -7.257  13.501 1.00 32.16  ? 172 ILE A HG22 1 
ATOM   2882 H  HG23 . ILE A 1 175 ? 8.419   -7.688  14.575 1.00 32.16  ? 172 ILE A HG23 1 
ATOM   2883 H  HD11 . ILE A 1 175 ? 10.334  -5.978  18.083 1.00 33.57  ? 172 ILE A HD11 1 
ATOM   2884 H  HD12 . ILE A 1 175 ? 11.021  -5.704  16.677 1.00 33.57  ? 172 ILE A HD12 1 
ATOM   2885 H  HD13 . ILE A 1 175 ? 9.440   -5.629  16.817 1.00 33.57  ? 172 ILE A HD13 1 
ATOM   2886 N  N    . MET A 1 176 ? 11.644  -9.481  12.994 1.00 25.14  ? 173 MET A N    1 
ATOM   2887 C  CA   . MET A 1 176 ? 11.734  -9.572  11.553 1.00 25.55  ? 173 MET A CA   1 
ATOM   2888 C  C    . MET A 1 176 ? 11.609  -11.012 11.053 1.00 28.38  ? 173 MET A C    1 
ATOM   2889 O  O    . MET A 1 176 ? 11.216  -11.247 9.903  1.00 30.34  ? 173 MET A O    1 
ATOM   2890 C  CB   . MET A 1 176 ? 13.022  -9.006  11.014 1.00 27.54  ? 173 MET A CB   1 
ATOM   2891 C  CG   . MET A 1 176 ? 13.138  -7.548  11.340 1.00 30.27  ? 173 MET A CG   1 
ATOM   2892 S  SD   . MET A 1 176 ? 12.116  -6.659  10.221 1.00 30.28  ? 173 MET A SD   1 
ATOM   2893 C  CE   . MET A 1 176 ? 11.648  -5.303  11.202 1.00 36.09  ? 173 MET A CE   1 
ATOM   2894 H  H    . MET A 1 176 ? 12.382  -9.301  13.397 1.00 30.20  ? 173 MET A H    1 
ATOM   2895 H  HA   . MET A 1 176 ? 11.006  -9.027  11.217 1.00 30.70  ? 173 MET A HA   1 
ATOM   2896 H  HB2  . MET A 1 176 ? 13.773  -9.472  11.413 1.00 33.08  ? 173 MET A HB2  1 
ATOM   2897 H  HB3  . MET A 1 176 ? 13.042  -9.109  10.049 1.00 33.08  ? 173 MET A HB3  1 
ATOM   2898 H  HG2  . MET A 1 176 ? 12.837  -7.384  12.247 1.00 36.36  ? 173 MET A HG2  1 
ATOM   2899 H  HG3  . MET A 1 176 ? 14.057  -7.254  11.236 1.00 36.36  ? 173 MET A HG3  1 
ATOM   2900 H  HE1  . MET A 1 176 ? 11.091  -4.710  10.674 1.00 43.35  ? 173 MET A HE1  1 
ATOM   2901 H  HE2  . MET A 1 176 ? 11.153  -5.626  11.971 1.00 43.35  ? 173 MET A HE2  1 
ATOM   2902 H  HE3  . MET A 1 176 ? 12.445  -4.835  11.494 1.00 43.35  ? 173 MET A HE3  1 
ATOM   2903 N  N    . THR A 1 177 ? 11.965  -11.975 11.889 1.00 25.61  ? 174 THR A N    1 
ATOM   2904 C  CA   . THR A 1 177 ? 11.828  -13.378 11.532 1.00 28.31  ? 174 THR A CA   1 
ATOM   2905 C  C    . THR A 1 177 ? 10.375  -13.794 11.336 1.00 28.36  ? 174 THR A C    1 
ATOM   2906 O  O    . THR A 1 177 ? 10.101  -14.759 10.598 1.00 29.75  ? 174 THR A O    1 
ATOM   2907 C  CB   . THR A 1 177 ? 12.474  -14.226 12.627 1.00 35.30  ? 174 THR A CB   1 
ATOM   2908 O  OG1  . THR A 1 177 ? 13.876  -13.957 12.635 1.00 43.02  ? 174 THR A OG1  1 
ATOM   2909 C  CG2  . THR A 1 177 ? 12.264  -15.715 12.365 1.00 41.13  ? 174 THR A CG2  1 
ATOM   2910 H  H    . THR A 1 177 ? 12.291  -11.844 12.674 1.00 30.76  ? 174 THR A H    1 
ATOM   2911 H  HA   . THR A 1 177 ? 12.282  -13.534 10.689 1.00 34.01  ? 174 THR A HA   1 
ATOM   2912 H  HB   . THR A 1 177 ? 12.075  -14.012 13.484 1.00 42.39  ? 174 THR A HB   1 
ATOM   2913 H  HG1  . THR A 1 177 ? 14.015  -13.164 12.877 1.00 51.66  ? 174 THR A HG1  1 
ATOM   2914 H  HG21 . THR A 1 177 ? 12.892  -16.236 12.889 1.00 49.39  ? 174 THR A HG21 1 
ATOM   2915 H  HG22 . THR A 1 177 ? 11.361  -15.971 12.609 1.00 49.39  ? 174 THR A HG22 1 
ATOM   2916 H  HG23 . THR A 1 177 ? 12.403  -15.910 11.424 1.00 49.39  ? 174 THR A HG23 1 
ATOM   2917 N  N    . ASN A 1 178 ? 9.433   -13.079 11.969 1.00 24.62  ? 175 ASN A N    1 
ATOM   2918 C  CA   . ASN A 1 178 ? 8.053   -13.540 12.084 1.00 27.45  ? 175 ASN A CA   1 
ATOM   2919 C  C    . ASN A 1 178 ? 7.062   -12.542 11.521 1.00 26.35  ? 175 ASN A C    1 
ATOM   2920 O  O    . ASN A 1 178 ? 5.928   -12.443 11.977 1.00 27.18  ? 175 ASN A O    1 
ATOM   2921 C  CB   . ASN A 1 178 ? 7.764   -13.893 13.540 1.00 29.46  ? 175 ASN A CB   1 
ATOM   2922 C  CG   . ASN A 1 178 ? 8.478   -15.182 13.951 1.00 26.32  ? 175 ASN A CG   1 
ATOM   2923 O  OD1  . ASN A 1 178 ? 8.428   -16.204 13.260 1.00 29.92  ? 175 ASN A OD1  1 
ATOM   2924 N  ND2  . ASN A 1 178 ? 9.166   -15.133 15.097 1.00 32.78  ? 175 ASN A ND2  1 
ATOM   2925 H  H    . ASN A 1 178 ? 9.577   -12.318 12.342 1.00 29.58  ? 175 ASN A H    1 
ATOM   2926 H  HA   . ASN A 1 178 ? 7.931   -14.341 11.551 1.00 32.97  ? 175 ASN A HA   1 
ATOM   2927 H  HB2  . ASN A 1 178 ? 8.076   -13.175 14.113 1.00 35.38  ? 175 ASN A HB2  1 
ATOM   2928 H  HB3  . ASN A 1 178 ? 6.810   -14.021 13.657 1.00 35.38  ? 175 ASN A HB3  1 
ATOM   2929 H  HD21 . ASN A 1 178 ? 9.587   -15.829 15.376 1.00 39.37  ? 175 ASN A HD21 1 
ATOM   2930 H  HD22 . ASN A 1 178 ? 9.187   -14.405 15.554 1.00 39.37  ? 175 ASN A HD22 1 
ATOM   2931 N  N    . LEU A 1 179 ? 7.443   -11.854 10.446 1.00 23.57  ? 176 LEU A N    1 
ATOM   2932 C  CA   . LEU A 1 179 ? 6.512   -10.883 9.886  1.00 22.73  ? 176 LEU A CA   1 
ATOM   2933 C  C    . LEU A 1 179 ? 5.305   -11.547 9.251  1.00 24.56  ? 176 LEU A C    1 
ATOM   2934 O  O    . LEU A 1 179 ? 4.255   -10.895 9.109  1.00 25.99  ? 176 LEU A O    1 
ATOM   2935 C  CB   . LEU A 1 179 ? 7.223   -10.002 8.863  1.00 23.75  ? 176 LEU A CB   1 
ATOM   2936 C  CG   . LEU A 1 179 ? 8.311   -9.113  9.437  1.00 26.81  ? 176 LEU A CG   1 
ATOM   2937 C  CD1  . LEU A 1 179 ? 9.070   -8.411  8.302  1.00 30.55  ? 176 LEU A CD1  1 
ATOM   2938 C  CD2  . LEU A 1 179 ? 7.780   -8.071  10.425 1.00 28.83  ? 176 LEU A CD2  1 
ATOM   2939 H  H    . LEU A 1 179 ? 8.198   -11.929 10.042 1.00 28.32  ? 176 LEU A H    1 
ATOM   2940 H  HA   . LEU A 1 179 ? 6.195   -10.309 10.601 1.00 27.31  ? 176 LEU A HA   1 
ATOM   2941 H  HB2  . LEU A 1 179 ? 7.634   -10.575 8.197  1.00 28.53  ? 176 LEU A HB2  1 
ATOM   2942 H  HB3  . LEU A 1 179 ? 6.565   -9.425  8.444  1.00 28.53  ? 176 LEU A HB3  1 
ATOM   2943 H  HG   . LEU A 1 179 ? 8.915   -9.685  9.936  1.00 32.20  ? 176 LEU A HG   1 
ATOM   2944 H  HD11 . LEU A 1 179 ? 9.753   -7.839  8.685  1.00 36.70  ? 176 LEU A HD11 1 
ATOM   2945 H  HD12 . LEU A 1 179 ? 9.481   -9.082  7.734  1.00 36.70  ? 176 LEU A HD12 1 
ATOM   2946 H  HD13 . LEU A 1 179 ? 8.444   -7.879  7.785  1.00 36.70  ? 176 LEU A HD13 1 
ATOM   2947 H  HD21 . LEU A 1 179 ? 8.514   -7.507  10.714 1.00 34.63  ? 176 LEU A HD21 1 
ATOM   2948 H  HD22 . LEU A 1 179 ? 7.104   -7.533  9.983  1.00 34.63  ? 176 LEU A HD22 1 
ATOM   2949 H  HD23 . LEU A 1 179 ? 7.392   -8.527  11.188 1.00 34.63  ? 176 LEU A HD23 1 
ATOM   2950 N  N    . ASN A 1 180 ? 5.433   -12.811 8.864  1.00 25.64  ? 177 ASN A N    1 
ATOM   2951 C  CA   . ASN A 1 180 ? 4.349   -13.529 8.216  1.00 27.96  ? 177 ASN A CA   1 
ATOM   2952 C  C    . ASN A 1 180 ? 3.121   -13.671 9.102  1.00 35.37  ? 177 ASN A C    1 
ATOM   2953 O  O    . ASN A 1 180 ? 2.022   -13.827 8.566  1.00 31.71  ? 177 ASN A O    1 
ATOM   2954 C  CB   . ASN A 1 180 ? 4.833   -14.914 7.806  1.00 30.83  ? 177 ASN A CB   1 
ATOM   2955 C  CG   . ASN A 1 180 ? 5.622   -15.610 8.939  1.00 44.28  ? 177 ASN A CG   1 
ATOM   2956 O  OD1  . ASN A 1 180 ? 6.776   -15.235 9.251  1.00 45.81  ? 177 ASN A OD1  1 
ATOM   2957 N  ND2  . ASN A 1 180 ? 4.982   -16.568 9.589  1.00 45.96  ? 177 ASN A ND2  1 
ATOM   2958 H  H    . ASN A 1 180 ? 6.147   -13.280 8.967  1.00 30.80  ? 177 ASN A H    1 
ATOM   2959 H  HA   . ASN A 1 180 ? 4.085   -13.035 7.423  1.00 33.59  ? 177 ASN A HA   1 
ATOM   2960 H  HB2  . ASN A 1 180 ? 4.068   -15.467 7.585  1.00 37.04  ? 177 ASN A HB2  1 
ATOM   2961 H  HB3  . ASN A 1 180 ? 5.417   -14.833 7.035  1.00 37.04  ? 177 ASN A HB3  1 
ATOM   2962 H  HD21 . ASN A 1 180 ? 4.175   -16.770 9.373  1.00 55.19  ? 177 ASN A HD21 1 
ATOM   2963 H  HD22 . ASN A 1 180 ? 5.374   -16.989 10.229 1.00 55.19  ? 177 ASN A HD22 1 
ATOM   2964 N  N    . VAL A 1 181 ? 3.260   -13.546 10.436 1.00 26.92  ? 178 VAL A N    1 
ATOM   2965 C  CA   . VAL A 1 181 ? 2.085   -13.685 11.294 1.00 26.04  ? 178 VAL A CA   1 
ATOM   2966 C  C    . VAL A 1 181 ? 1.263   -12.419 11.402 1.00 30.56  ? 178 VAL A C    1 
ATOM   2967 O  O    . VAL A 1 181 ? 0.140   -12.467 11.908 1.00 30.00  ? 178 VAL A O    1 
ATOM   2968 C  CB   . VAL A 1 181 ? 2.430   -14.202 12.702 1.00 30.76  ? 178 VAL A CB   1 
ATOM   2969 C  CG1  . VAL A 1 181 ? 3.365   -15.419 12.619 1.00 32.94  ? 178 VAL A CG1  1 
ATOM   2970 C  CG2  . VAL A 1 181 ? 3.044   -13.153 13.553 1.00 31.72  ? 178 VAL A CG2  1 
ATOM   2971 H  H    . VAL A 1 181 ? 3.999   -13.387 10.846 1.00 32.34  ? 178 VAL A H    1 
ATOM   2972 H  HA   . VAL A 1 181 ? 1.528   -14.360 10.877 1.00 31.28  ? 178 VAL A HA   1 
ATOM   2973 H  HB   . VAL A 1 181 ? 1.597   -14.468 13.123 1.00 36.95  ? 178 VAL A HB   1 
ATOM   2974 H  HG11 . VAL A 1 181 ? 3.492   -15.781 13.510 1.00 39.56  ? 178 VAL A HG11 1 
ATOM   2975 H  HG12 . VAL A 1 181 ? 2.961   -16.089 12.045 1.00 39.56  ? 178 VAL A HG12 1 
ATOM   2976 H  HG13 . VAL A 1 181 ? 4.217   -15.138 12.251 1.00 39.56  ? 178 VAL A HG13 1 
ATOM   2977 H  HG21 . VAL A 1 181 ? 3.490   -13.576 14.304 1.00 38.10  ? 178 VAL A HG21 1 
ATOM   2978 H  HG22 . VAL A 1 181 ? 3.687   -12.654 13.025 1.00 38.10  ? 178 VAL A HG22 1 
ATOM   2979 H  HG23 . VAL A 1 181 ? 2.348   -12.559 13.874 1.00 38.10  ? 178 VAL A HG23 1 
ATOM   2980 N  N    . ILE A 1 182 ? 1.748   -11.314 10.859 1.00 24.96  ? 179 ILE A N    1 
ATOM   2981 C  CA   . ILE A 1 182 ? 1.018   -10.064 10.833 1.00 25.03  ? 179 ILE A CA   1 
ATOM   2982 C  C    . ILE A 1 182 ? 0.103   -10.076 9.636  1.00 25.30  ? 179 ILE A C    1 
ATOM   2983 O  O    . ILE A 1 182 ? 0.582   -10.138 8.508  1.00 28.17  ? 179 ILE A O    1 
ATOM   2984 C  CB   . ILE A 1 182 ? 1.973   -8.869  10.761 1.00 22.98  ? 179 ILE A CB   1 
ATOM   2985 C  CG1  . ILE A 1 182 ? 2.808   -8.814  12.031 1.00 23.84  ? 179 ILE A CG1  1 
ATOM   2986 C  CG2  . ILE A 1 182 ? 1.192   -7.595  10.525 1.00 26.00  ? 179 ILE A CG2  1 
ATOM   2987 C  CD1  . ILE A 1 182 ? 4.081   -7.970  11.844 1.00 25.61  ? 179 ILE A CD1  1 
ATOM   2988 H  H    . ILE A 1 182 ? 2.522   -11.264 10.487 1.00 29.98  ? 179 ILE A H    1 
ATOM   2989 H  HA   . ILE A 1 182 ? 0.483   -9.990  11.639 1.00 30.07  ? 179 ILE A HA   1 
ATOM   2990 H  HB   . ILE A 1 182 ? 2.581   -8.973  10.013 1.00 27.62  ? 179 ILE A HB   1 
ATOM   2991 H  HG12 . ILE A 1 182 ? 2.282   -8.416  12.742 1.00 28.65  ? 179 ILE A HG12 1 
ATOM   2992 H  HG13 . ILE A 1 182 ? 3.074   -9.714  12.277 1.00 28.65  ? 179 ILE A HG13 1 
ATOM   2993 H  HG21 . ILE A 1 182 ? 1.636   -6.863  10.982 1.00 31.24  ? 179 ILE A HG21 1 
ATOM   2994 H  HG22 . ILE A 1 182 ? 1.158   -7.417  9.572  1.00 31.24  ? 179 ILE A HG22 1 
ATOM   2995 H  HG23 . ILE A 1 182 ? 0.293   -7.706  10.873 1.00 31.24  ? 179 ILE A HG23 1 
ATOM   2996 H  HD11 . ILE A 1 182 ? 4.727   -8.220  12.522 1.00 30.77  ? 179 ILE A HD11 1 
ATOM   2997 H  HD12 . ILE A 1 182 ? 4.445   -8.140  10.961 1.00 30.77  ? 179 ILE A HD12 1 
ATOM   2998 H  HD13 . ILE A 1 182 ? 3.853   -7.032  11.933 1.00 30.77  ? 179 ILE A HD13 1 
ATOM   2999 N  N    . LYS A 1 183 ? -1.201  -9.958  9.880  1.00 21.65  ? 180 LYS A N    1 
ATOM   3000 C  CA   . LYS A 1 183 ? -2.176  -10.136 8.828  1.00 24.73  ? 180 LYS A CA   1 
ATOM   3001 C  C    . LYS A 1 183 ? -3.174  -8.994  8.655  1.00 25.75  ? 180 LYS A C    1 
ATOM   3002 O  O    . LYS A 1 183 ? -3.985  -9.041  7.706  1.00 28.38  ? 180 LYS A O    1 
ATOM   3003 C  CB   . LYS A 1 183 ? -2.956  -11.428 9.079  1.00 29.64  ? 180 LYS A CB   1 
ATOM   3004 C  CG   . LYS A 1 183 ? -2.099  -12.682 8.842  1.00 35.30  ? 180 LYS A CG   1 
ATOM   3005 C  CD   . LYS A 1 183 ? -2.625  -13.874 9.621  1.00 41.67  ? 180 LYS A CD   1 
ATOM   3006 C  CE   . LYS A 1 183 ? -1.603  -15.008 9.704  1.00 41.15  ? 180 LYS A CE   1 
ATOM   3007 N  NZ   . LYS A 1 183 ? -2.285  -16.276 10.179 1.00 45.41  ? 180 LYS A NZ   1 
ATOM   3008 H  H    . LYS A 1 183 ? -1.539  -9.774  10.649 1.00 26.02  ? 180 LYS A H    1 
ATOM   3009 H  HA   . LYS A 1 183 ? -1.693  -10.201 7.989  1.00 29.71  ? 180 LYS A HA   1 
ATOM   3010 H  HB2  . LYS A 1 183 ? -3.262  -11.440 10.000 1.00 35.61  ? 180 LYS A HB2  1 
ATOM   3011 H  HB3  . LYS A 1 183 ? -3.716  -11.463 8.477  1.00 35.61  ? 180 LYS A HB3  1 
ATOM   3012 H  HG2  . LYS A 1 183 ? -2.112  -12.905 7.898  1.00 42.40  ? 180 LYS A HG2  1 
ATOM   3013 H  HG3  . LYS A 1 183 ? -1.189  -12.507 9.130  1.00 42.40  ? 180 LYS A HG3  1 
ATOM   3014 H  HD2  . LYS A 1 183 ? -2.838  -13.594 10.525 1.00 50.04  ? 180 LYS A HD2  1 
ATOM   3015 H  HD3  . LYS A 1 183 ? -3.420  -14.215 9.183  1.00 50.04  ? 180 LYS A HD3  1 
ATOM   3016 H  HE2  . LYS A 1 183 ? -1.220  -15.169 8.827  1.00 49.41  ? 180 LYS A HE2  1 
ATOM   3017 H  HE3  . LYS A 1 183 ? -0.904  -14.775 10.334 1.00 49.41  ? 180 LYS A HE3  1 
ATOM   3018 H  HZ1  . LYS A 1 183 ? -1.699  -16.945 10.206 1.00 54.52  ? 180 LYS A HZ1  1 
ATOM   3019 H  HZ2  . LYS A 1 183 ? -2.622  -16.153 10.994 1.00 54.52  ? 180 LYS A HZ2  1 
ATOM   3020 H  HZ3  . LYS A 1 183 ? -2.945  -16.493 9.623  1.00 54.52  ? 180 LYS A HZ3  1 
ATOM   3021 N  N    . MET A 1 184 ? -3.158  -7.992  9.511  1.00 26.01  ? 181 MET A N    1 
ATOM   3022 C  CA   . MET A 1 184 ? -4.151  -6.934  9.374  1.00 25.02  ? 181 MET A CA   1 
ATOM   3023 C  C    . MET A 1 184 ? -3.642  -5.891  8.390  1.00 24.65  ? 181 MET A C    1 
ATOM   3024 O  O    . MET A 1 184 ? -2.458  -5.873  8.033  1.00 24.05  ? 181 MET A O    1 
ATOM   3025 C  CB   . MET A 1 184 ? -4.452  -6.267  10.729 1.00 24.85  ? 181 MET A CB   1 
ATOM   3026 C  CG   . MET A 1 184 ? -3.347  -5.551  11.485 1.00 26.80  ? 181 MET A CG   1 
ATOM   3027 S  SD   . MET A 1 184 ? -1.933  -6.425  12.040 1.00 27.98  ? 181 MET A SD   1 
ATOM   3028 C  CE   . MET A 1 184 ? -2.653  -7.329  13.425 1.00 29.56  ? 181 MET A CE   1 
ATOM   3029 H  H    . MET A 1 184 ? -2.602  -7.901  10.161 1.00 31.25  ? 181 MET A H    1 
ATOM   3030 H  HA   . MET A 1 184 ? -4.978  -7.333  9.061  1.00 30.06  ? 181 MET A HA   1 
ATOM   3031 H  HB2  . MET A 1 184 ? -5.145  -5.605  10.576 1.00 29.86  ? 181 MET A HB2  1 
ATOM   3032 H  HB3  . MET A 1 184 ? -4.780  -6.959  11.324 1.00 29.86  ? 181 MET A HB3  1 
ATOM   3033 H  HG2  . MET A 1 184 ? -3.014  -4.848  10.905 1.00 32.20  ? 181 MET A HG2  1 
ATOM   3034 H  HG3  . MET A 1 184 ? -3.749  -5.164  12.279 1.00 32.20  ? 181 MET A HG3  1 
ATOM   3035 H  HE1  . MET A 1 184 ? -1.966  -7.874  13.838 1.00 35.50  ? 181 MET A HE1  1 
ATOM   3036 H  HE2  . MET A 1 184 ? -3.004  -6.694  14.068 1.00 35.50  ? 181 MET A HE2  1 
ATOM   3037 H  HE3  . MET A 1 184 ? -3.369  -7.895  13.094 1.00 35.50  ? 181 MET A HE3  1 
ATOM   3038 N  N    . PRO A 1 185 ? -4.496  -4.977  7.950  1.00 24.62  ? 182 PRO A N    1 
ATOM   3039 C  CA   . PRO A 1 185 ? -4.039  -3.986  6.965  1.00 25.36  ? 182 PRO A CA   1 
ATOM   3040 C  C    . PRO A 1 185 ? -2.870  -3.162  7.477  1.00 28.13  ? 182 PRO A C    1 
ATOM   3041 O  O    . PRO A 1 185 ? -2.832  -2.752  8.646  1.00 26.31  ? 182 PRO A O    1 
ATOM   3042 C  CB   . PRO A 1 185 ? -5.274  -3.137  6.721  1.00 25.65  ? 182 PRO A CB   1 
ATOM   3043 C  CG   . PRO A 1 185 ? -6.418  -4.079  7.056  1.00 26.68  ? 182 PRO A CG   1 
ATOM   3044 C  CD   . PRO A 1 185 ? -5.944  -4.846  8.208  1.00 25.92  ? 182 PRO A CD   1 
ATOM   3045 H  HA   . PRO A 1 185 ? -3.775  -4.425  6.141  1.00 30.47  ? 182 PRO A HA   1 
ATOM   3046 H  HB2  . PRO A 1 185 ? -5.271  -2.363  7.306  1.00 30.81  ? 182 PRO A HB2  1 
ATOM   3047 H  HB3  . PRO A 1 185 ? -5.310  -2.853  5.795  1.00 30.81  ? 182 PRO A HB3  1 
ATOM   3048 H  HG2  . PRO A 1 185 ? -7.212  -3.570  7.281  1.00 32.05  ? 182 PRO A HG2  1 
ATOM   3049 H  HG3  . PRO A 1 185 ? -6.599  -4.662  6.302  1.00 32.05  ? 182 PRO A HG3  1 
ATOM   3050 H  HD2  . PRO A 1 185 ? -6.106  -4.365  9.035  1.00 31.14  ? 182 PRO A HD2  1 
ATOM   3051 H  HD3  . PRO A 1 185 ? -6.369  -5.717  8.243  1.00 31.14  ? 182 PRO A HD3  1 
ATOM   3052 N  N    . ALA A 1 186 ? -1.898  -2.934  6.574  1.00 24.30  ? 183 ALA A N    1 
ATOM   3053 C  CA   . ALA A 1 186 ? -0.633  -2.318  6.940  1.00 23.91  ? 183 ALA A CA   1 
ATOM   3054 C  C    . ALA A 1 186 ? -0.188  -1.283  5.915  1.00 25.35  ? 183 ALA A C    1 
ATOM   3055 O  O    . ALA A 1 186 ? -0.309  -1.480  4.708  1.00 28.21  ? 183 ALA A O    1 
ATOM   3056 C  CB   . ALA A 1 186 ? 0.454   -3.397  7.120  1.00 27.03  ? 183 ALA A CB   1 
ATOM   3057 H  H    . ALA A 1 186 ? -1.959  -3.133  5.740  1.00 29.19  ? 183 ALA A H    1 
ATOM   3058 H  HA   . ALA A 1 186 ? -0.751  -1.831  7.771  1.00 28.73  ? 183 ALA A HA   1 
ATOM   3059 H  HB1  . ALA A 1 186 ? 1.311   -2.963  7.260  1.00 32.47  ? 183 ALA A HB1  1 
ATOM   3060 H  HB2  . ALA A 1 186 ? 0.232   -3.944  7.890  1.00 32.47  ? 183 ALA A HB2  1 
ATOM   3061 H  HB3  . ALA A 1 186 ? 0.489   -3.947  6.322  1.00 32.47  ? 183 ALA A HB3  1 
ATOM   3062 N  N    . ASN A 1 187 ? 0.344   -0.177  6.414  1.00 22.21  ? 184 ASN A N    1 
ATOM   3063 C  CA   . ASN A 1 187 ? 0.912   0.900   5.598  1.00 25.58  ? 184 ASN A CA   1 
ATOM   3064 C  C    . ASN A 1 187 ? 2.375   1.026   6.019  1.00 25.69  ? 184 ASN A C    1 
ATOM   3065 O  O    . ASN A 1 187 ? 2.668   1.356   7.181  1.00 24.33  ? 184 ASN A O    1 
ATOM   3066 C  CB   . ASN A 1 187 ? 0.114   2.175   5.840  1.00 24.87  ? 184 ASN A CB   1 
ATOM   3067 C  CG   . ASN A 1 187 ? 0.542   3.321   4.987  1.00 30.21  ? 184 ASN A CG   1 
ATOM   3068 O  OD1  . ASN A 1 187 ? 1.522   3.250   4.255  1.00 29.78  ? 184 ASN A OD1  1 
ATOM   3069 N  ND2  . ASN A 1 187 ? -0.192  4.410   5.085  1.00 32.78  ? 184 ASN A ND2  1 
ATOM   3070 H  H    . ASN A 1 187 ? 0.393   -0.016  7.258  1.00 26.69  ? 184 ASN A H    1 
ATOM   3071 H  HA   . ASN A 1 187 ? 0.888   0.707   4.647  1.00 30.73  ? 184 ASN A HA   1 
ATOM   3072 H  HB2  . ASN A 1 187 ? -0.821  1.999   5.652  1.00 29.88  ? 184 ASN A HB2  1 
ATOM   3073 H  HB3  . ASN A 1 187 ? 0.222   2.440   6.767  1.00 29.88  ? 184 ASN A HB3  1 
ATOM   3074 H  HD21 . ASN A 1 187 ? 0.005   5.104   4.618  1.00 39.37  ? 184 ASN A HD21 1 
ATOM   3075 H  HD22 . ASN A 1 187 ? -0.868  4.426   5.617  1.00 39.37  ? 184 ASN A HD22 1 
ATOM   3076 N  N    . ILE A 1 188 ? 3.289   0.705   5.101  1.00 22.68  ? 185 ILE A N    1 
ATOM   3077 C  CA   . ILE A 1 188 ? 4.727   0.748   5.369  1.00 22.13  ? 185 ILE A CA   1 
ATOM   3078 C  C    . ILE A 1 188 ? 5.289   1.988   4.695  1.00 24.35  ? 185 ILE A C    1 
ATOM   3079 O  O    . ILE A 1 188 ? 5.209   2.115   3.472  1.00 25.77  ? 185 ILE A O    1 
ATOM   3080 C  CB   . ILE A 1 188 ? 5.437   -0.521  4.881  1.00 27.94  ? 185 ILE A CB   1 
ATOM   3081 C  CG1  . ILE A 1 188 ? 4.753   -1.791  5.417  1.00 24.54  ? 185 ILE A CG1  1 
ATOM   3082 C  CG2  . ILE A 1 188 ? 6.920   -0.498  5.216  1.00 29.86  ? 185 ILE A CG2  1 
ATOM   3083 C  CD1  . ILE A 1 188 ? 4.547   -1.885  6.879  1.00 29.22  ? 185 ILE A CD1  1 
ATOM   3084 H  H    . ILE A 1 188 ? 3.096   0.455   4.301  1.00 27.25  ? 185 ILE A H    1 
ATOM   3085 H  HA   . ILE A 1 188 ? 4.873   0.821   6.325  1.00 26.59  ? 185 ILE A HA   1 
ATOM   3086 H  HB   . ILE A 1 188 ? 5.360   -0.539  3.914  1.00 33.56  ? 185 ILE A HB   1 
ATOM   3087 H  HG12 . ILE A 1 188 ? 3.877   -1.854  5.006  1.00 29.49  ? 185 ILE A HG12 1 
ATOM   3088 H  HG13 . ILE A 1 188 ? 5.296   -2.553  5.161  1.00 29.49  ? 185 ILE A HG13 1 
ATOM   3089 H  HG21 . ILE A 1 188 ? 7.298   -1.373  5.037  1.00 35.87  ? 185 ILE A HG21 1 
ATOM   3090 H  HG22 . ILE A 1 188 ? 7.358   0.170   4.666  1.00 35.87  ? 185 ILE A HG22 1 
ATOM   3091 H  HG23 . ILE A 1 188 ? 7.028   -0.276  6.154  1.00 35.87  ? 185 ILE A HG23 1 
ATOM   3092 H  HD11 . ILE A 1 188 ? 4.002   -2.665  7.071  1.00 35.10  ? 185 ILE A HD11 1 
ATOM   3093 H  HD12 . ILE A 1 188 ? 5.409   -1.969  7.315  1.00 35.10  ? 185 ILE A HD12 1 
ATOM   3094 H  HD13 . ILE A 1 188 ? 4.097   -1.083  7.187  1.00 35.10  ? 185 ILE A HD13 1 
ATOM   3095 N  N    . LEU A 1 189 ? 5.866   2.909   5.482  1.00 22.51  ? 186 LEU A N    1 
ATOM   3096 C  CA   . LEU A 1 189 ? 6.316   4.188   4.960  1.00 23.37  ? 186 LEU A CA   1 
ATOM   3097 C  C    . LEU A 1 189 ? 7.812   4.376   5.194  1.00 28.78  ? 186 LEU A C    1 
ATOM   3098 O  O    . LEU A 1 189 ? 8.359   3.958   6.220  1.00 27.26  ? 186 LEU A O    1 
ATOM   3099 C  CB   . LEU A 1 189 ? 5.558   5.361   5.629  1.00 26.25  ? 186 LEU A CB   1 
ATOM   3100 C  CG   . LEU A 1 189 ? 4.039   5.364   5.473  1.00 28.51  ? 186 LEU A CG   1 
ATOM   3101 C  CD1  . LEU A 1 189 ? 3.282   5.173   6.765  1.00 29.90  ? 186 LEU A CD1  1 
ATOM   3102 C  CD2  . LEU A 1 189 ? 3.604   6.647   4.752  1.00 34.40  ? 186 LEU A CD2  1 
ATOM   3103 H  H    . LEU A 1 189 ? 6.003   2.807   6.325  1.00 27.04  ? 186 LEU A H    1 
ATOM   3104 H  HA   . LEU A 1 189 ? 6.156   4.203   4.004  1.00 28.08  ? 186 LEU A HA   1 
ATOM   3105 H  HB2  . LEU A 1 189 ? 5.747   5.339   6.580  1.00 31.54  ? 186 LEU A HB2  1 
ATOM   3106 H  HB3  . LEU A 1 189 ? 5.886   6.189   5.244  1.00 31.54  ? 186 LEU A HB3  1 
ATOM   3107 H  HG   . LEU A 1 189 ? 3.799   4.590   4.939  1.00 34.24  ? 186 LEU A HG   1 
ATOM   3108 H  HD11 . LEU A 1 189 ? 2.331   5.189   6.579  1.00 35.92  ? 186 LEU A HD11 1 
ATOM   3109 H  HD12 . LEU A 1 189 ? 3.529   4.319   7.152  1.00 35.92  ? 186 LEU A HD12 1 
ATOM   3110 H  HD13 . LEU A 1 189 ? 3.512   5.891   7.375  1.00 35.92  ? 186 LEU A HD13 1 
ATOM   3111 H  HD21 . LEU A 1 189 ? 2.641   6.633   4.634  1.00 41.32  ? 186 LEU A HD21 1 
ATOM   3112 H  HD22 . LEU A 1 189 ? 3.860   7.414   5.289  1.00 41.32  ? 186 LEU A HD22 1 
ATOM   3113 H  HD23 . LEU A 1 189 ? 4.042   6.688   3.887  1.00 41.32  ? 186 LEU A HD23 1 
ATOM   3114 N  N    . PHE A 1 190 ? 8.473   5.032   4.243  1.00 25.77  ? 187 PHE A N    1 
ATOM   3115 C  CA   . PHE A 1 190 ? 9.862   5.424   4.453  1.00 27.91  ? 187 PHE A CA   1 
ATOM   3116 C  C    . PHE A 1 190 ? 10.104  6.754   3.762  1.00 29.89  ? 187 PHE A C    1 
ATOM   3117 O  O    . PHE A 1 190 ? 9.339   7.175   2.885  1.00 29.68  ? 187 PHE A O    1 
ATOM   3118 C  CB   . PHE A 1 190 ? 10.834  4.338   3.944  1.00 28.47  ? 187 PHE A CB   1 
ATOM   3119 C  CG   . PHE A 1 190 ? 10.823  4.170   2.453  1.00 30.53  ? 187 PHE A CG   1 
ATOM   3120 C  CD1  . PHE A 1 190 ? 9.871   3.380   1.829  1.00 31.90  ? 187 PHE A CD1  1 
ATOM   3121 C  CD2  . PHE A 1 190 ? 11.780  4.805   1.688  1.00 29.53  ? 187 PHE A CD2  1 
ATOM   3122 C  CE1  . PHE A 1 190 ? 9.893   3.224   0.407  1.00 32.60  ? 187 PHE A CE1  1 
ATOM   3123 C  CE2  . PHE A 1 190 ? 11.804  4.682   0.279  1.00 35.97  ? 187 PHE A CE2  1 
ATOM   3124 C  CZ   . PHE A 1 190 ? 10.856  3.882   -0.351 1.00 34.58  ? 187 PHE A CZ   1 
ATOM   3125 H  H    . PHE A 1 190 ? 8.144   5.258   3.482  1.00 30.95  ? 187 PHE A H    1 
ATOM   3126 H  HA   . PHE A 1 190 ? 10.032  5.549   5.400  1.00 33.52  ? 187 PHE A HA   1 
ATOM   3127 H  HB2  . PHE A 1 190 ? 11.736  4.578   4.208  1.00 34.20  ? 187 PHE A HB2  1 
ATOM   3128 H  HB3  . PHE A 1 190 ? 10.588  3.487   4.340  1.00 34.20  ? 187 PHE A HB3  1 
ATOM   3129 H  HD1  . PHE A 1 190 ? 9.219   2.951   2.333  1.00 38.31  ? 187 PHE A HD1  1 
ATOM   3130 H  HD2  . PHE A 1 190 ? 12.425  5.325   2.108  1.00 35.47  ? 187 PHE A HD2  1 
ATOM   3131 H  HE1  . PHE A 1 190 ? 9.264   2.683   -0.011 1.00 39.16  ? 187 PHE A HE1  1 
ATOM   3132 H  HE2  . PHE A 1 190 ? 12.446  5.132   -0.221 1.00 43.19  ? 187 PHE A HE2  1 
ATOM   3133 H  HZ   . PHE A 1 190 ? 10.866  3.788   -1.276 1.00 41.54  ? 187 PHE A HZ   1 
ATOM   3134 N  N    . GLY A 1 191 ? 11.182  7.420   4.152  1.00 29.18  ? 188 GLY A N    1 
ATOM   3135 C  CA   . GLY A 1 191 ? 11.520  8.712   3.581  1.00 30.07  ? 188 GLY A CA   1 
ATOM   3136 C  C    . GLY A 1 191 ? 12.606  8.616   2.528  1.00 37.84  ? 188 GLY A C    1 
ATOM   3137 O  O    . GLY A 1 191 ? 13.603  7.926   2.719  1.00 35.31  ? 188 GLY A O    1 
ATOM   3138 H  H    . GLY A 1 191 ? 11.735  7.141   4.749  1.00 35.05  ? 188 GLY A H    1 
ATOM   3139 H  HA2  . GLY A 1 191 ? 10.730  9.097   3.170  1.00 36.12  ? 188 GLY A HA2  1 
ATOM   3140 H  HA3  . GLY A 1 191 ? 11.829  9.302   4.286  1.00 36.12  ? 188 GLY A HA3  1 
ATOM   3141 N  N    . GLY A 1 192 ? 12.404  9.341   1.421  1.00 36.35  ? 189 GLY A N    1 
ATOM   3142 C  CA   . GLY A 1 192 ? 13.380  9.329   0.339  1.00 37.34  ? 189 GLY A CA   1 
ATOM   3143 C  C    . GLY A 1 192 ? 14.632  10.121  0.623  1.00 43.43  ? 189 GLY A C    1 
ATOM   3144 O  O    . GLY A 1 192 ? 15.589  10.021  -0.150 1.00 48.30  ? 189 GLY A O    1 
ATOM   3145 H  H    . GLY A 1 192 ? 11.717  9.840   1.279  1.00 43.65  ? 189 GLY A H    1 
ATOM   3146 H  HA2  . GLY A 1 192 ? 13.641  8.412   0.163  1.00 44.85  ? 189 GLY A HA2  1 
ATOM   3147 H  HA3  . GLY A 1 192 ? 12.968  9.699   -0.458 1.00 44.85  ? 189 GLY A HA3  1 
ATOM   3148 N  N    . LYS A 1 193 ? 14.639  10.926  1.683  1.00 42.63  ? 190 LYS A N    1 
ATOM   3149 C  CA   . LYS A 1 193 ? 15.828  11.627  2.139  1.00 42.53  ? 190 LYS A CA   1 
ATOM   3150 C  C    . LYS A 1 193 ? 16.415  10.981  3.390  1.00 47.35  ? 190 LYS A C    1 
ATOM   3151 O  O    . LYS A 1 193 ? 17.289  11.568  4.033  1.00 50.62  ? 190 LYS A O    1 
ATOM   3152 C  CB   . LYS A 1 193 ? 15.487  13.094  2.384  1.00 43.98  ? 190 LYS A CB   1 
ATOM   3153 C  CG   . LYS A 1 193 ? 15.168  13.824  1.076  1.00 55.44  ? 190 LYS A CG   1 
ATOM   3154 C  CD   . LYS A 1 193 ? 15.169  15.317  1.230  1.00 66.80  ? 190 LYS A CD   1 
ATOM   3155 C  CE   . LYS A 1 193 ? 14.578  15.993  -0.000 1.00 64.85  ? 190 LYS A CE   1 
ATOM   3156 N  NZ   . LYS A 1 193 ? 14.337  17.437  0.264  1.00 83.82  ? 190 LYS A NZ   1 
ATOM   3157 H  H    . LYS A 1 193 ? 13.946  11.084  2.166  1.00 51.19  ? 190 LYS A H    1 
ATOM   3158 H  HA   . LYS A 1 193 ? 16.513  11.601  1.453  1.00 51.07  ? 190 LYS A HA   1 
ATOM   3159 H  HB2  . LYS A 1 193 ? 14.710  13.149  2.962  1.00 52.81  ? 190 LYS A HB2  1 
ATOM   3160 H  HB3  . LYS A 1 193 ? 16.244  13.533  2.802  1.00 52.81  ? 190 LYS A HB3  1 
ATOM   3161 H  HG2  . LYS A 1 193 ? 15.835  13.591  0.413  1.00 66.57  ? 190 LYS A HG2  1 
ATOM   3162 H  HG3  . LYS A 1 193 ? 14.287  13.556  0.771  1.00 66.57  ? 190 LYS A HG3  1 
ATOM   3163 H  HD2  . LYS A 1 193 ? 14.635  15.563  2.001  1.00 80.19  ? 190 LYS A HD2  1 
ATOM   3164 H  HD3  . LYS A 1 193 ? 16.080  15.629  1.343  1.00 80.19  ? 190 LYS A HD3  1 
ATOM   3165 H  HE2  . LYS A 1 193 ? 15.196  15.913  -0.744 1.00 77.86  ? 190 LYS A HE2  1 
ATOM   3166 H  HE3  . LYS A 1 193 ? 13.732  15.575  -0.226 1.00 77.86  ? 190 LYS A HE3  1 
ATOM   3167 H  HZ1  . LYS A 1 193 ? 13.998  17.827  -0.461 1.00 100.61 ? 190 LYS A HZ1  1 
ATOM   3168 H  HZ2  . LYS A 1 193 ? 13.764  17.532  0.938  1.00 100.61 ? 190 LYS A HZ2  1 
ATOM   3169 H  HZ3  . LYS A 1 193 ? 15.102  17.839  0.477  1.00 100.61 ? 190 LYS A HZ3  1 
ATOM   3170 N  N    . ASP A 1 194 ? 15.931  9.795   3.761  1.00 40.91  ? 191 ASP A N    1 
ATOM   3171 C  CA   . ASP A 1 194 ? 16.558  8.937   4.768  1.00 38.82  ? 191 ASP A CA   1 
ATOM   3172 C  C    . ASP A 1 194 ? 17.677  8.123   4.099  1.00 45.34  ? 191 ASP A C    1 
ATOM   3173 O  O    . ASP A 1 194 ? 17.832  8.127   2.874  1.00 42.34  ? 191 ASP A O    1 
ATOM   3174 C  CB   . ASP A 1 194 ? 15.505  8.023   5.391  1.00 34.48  ? 191 ASP A CB   1 
ATOM   3175 C  CG   . ASP A 1 194 ? 15.882  7.510   6.781  1.00 34.31  ? 191 ASP A CG   1 
ATOM   3176 O  OD1  . ASP A 1 194 ? 17.019  7.739   7.255  1.00 39.14  ? 191 ASP A OD1  1 
ATOM   3177 O  OD2  . ASP A 1 194 ? 15.018  6.858   7.399  1.00 34.05  ? 191 ASP A OD2  1 
ATOM   3178 H  H    . ASP A 1 194 ? 15.215  9.451   3.433  1.00 49.13  ? 191 ASP A H    1 
ATOM   3179 H  HA   . ASP A 1 194 ? 16.946  9.465   5.483  1.00 46.62  ? 191 ASP A HA   1 
ATOM   3180 H  HB2  . ASP A 1 194 ? 14.673  8.515   5.473  1.00 41.41  ? 191 ASP A HB2  1 
ATOM   3181 H  HB3  . ASP A 1 194 ? 15.380  7.253   4.815  1.00 41.41  ? 191 ASP A HB3  1 
ATOM   3182 N  N    . ALA A 1 195 ? 18.464  7.422   4.915  1.00 40.87  ? 192 ALA A N    1 
ATOM   3183 C  CA   . ALA A 1 195 ? 19.496  6.535   4.388  1.00 48.49  ? 192 ALA A CA   1 
ATOM   3184 C  C    . ALA A 1 195 ? 18.875  5.462   3.491  1.00 40.94  ? 192 ALA A C    1 
ATOM   3185 O  O    . ALA A 1 195 ? 17.753  5.013   3.729  1.00 37.62  ? 192 ALA A O    1 
ATOM   3186 C  CB   . ALA A 1 195 ? 20.258  5.869   5.533  1.00 47.94  ? 192 ALA A CB   1 
ATOM   3187 H  H    . ALA A 1 195 ? 18.420  7.441   5.774  1.00 49.07  ? 192 ALA A H    1 
ATOM   3188 H  HA   . ALA A 1 195 ? 20.122  7.053   3.857  1.00 58.22  ? 192 ALA A HA   1 
ATOM   3189 H  HB1  . ALA A 1 195 ? 20.953  5.302   5.162  1.00 57.56  ? 192 ALA A HB1  1 
ATOM   3190 H  HB2  . ALA A 1 195 ? 20.655  6.556   6.090  1.00 57.56  ? 192 ALA A HB2  1 
ATOM   3191 H  HB3  . ALA A 1 195 ? 19.640  5.336   6.056  1.00 57.56  ? 192 ALA A HB3  1 
ATOM   3192 N  N    . PRO A 1 196 ? 19.600  5.014   2.460  1.00 42.84  ? 193 PRO A N    1 
ATOM   3193 C  CA   . PRO A 1 196 ? 19.023  4.002   1.557  1.00 37.53  ? 193 PRO A CA   1 
ATOM   3194 C  C    . PRO A 1 196 ? 18.705  2.689   2.248  1.00 34.78  ? 193 PRO A C    1 
ATOM   3195 O  O    . PRO A 1 196 ? 17.824  1.962   1.785  1.00 37.77  ? 193 PRO A O    1 
ATOM   3196 C  CB   . PRO A 1 196 ? 20.092  3.814   0.467  1.00 47.24  ? 193 PRO A CB   1 
ATOM   3197 C  CG   . PRO A 1 196 ? 21.288  4.617   0.894  1.00 55.97  ? 193 PRO A CG   1 
ATOM   3198 C  CD   . PRO A 1 196 ? 20.850  5.599   1.935  1.00 46.09  ? 193 PRO A CD   1 
ATOM   3199 H  HA   . PRO A 1 196 ? 18.220  4.358   1.145  1.00 45.07  ? 193 PRO A HA   1 
ATOM   3200 H  HB2  . PRO A 1 196 ? 20.320  2.874   0.397  1.00 56.72  ? 193 PRO A HB2  1 
ATOM   3201 H  HB3  . PRO A 1 196 ? 19.750  4.137   -0.381 1.00 56.72  ? 193 PRO A HB3  1 
ATOM   3202 H  HG2  . PRO A 1 196 ? 21.958  4.018   1.260  1.00 67.20  ? 193 PRO A HG2  1 
ATOM   3203 H  HG3  . PRO A 1 196 ? 21.647  5.084   0.123  1.00 67.20  ? 193 PRO A HG3  1 
ATOM   3204 H  HD2  . PRO A 1 196 ? 21.515  5.676   2.637  1.00 55.35  ? 193 PRO A HD2  1 
ATOM   3205 H  HD3  . PRO A 1 196 ? 20.682  6.468   1.539  1.00 55.35  ? 193 PRO A HD3  1 
ATOM   3206 N  N    . SER A 1 197 ? 19.371  2.371   3.356  1.00 41.22  ? 194 SER A N    1 
ATOM   3207 C  CA   . SER A 1 197 ? 19.028  1.160   4.083  1.00 37.00  ? 194 SER A CA   1 
ATOM   3208 C  C    . SER A 1 197 ? 17.572  1.152   4.532  1.00 36.12  ? 194 SER A C    1 
ATOM   3209 O  O    . SER A 1 197 ? 17.009  0.078   4.746  1.00 33.18  ? 194 SER A O    1 
ATOM   3210 C  CB   . SER A 1 197 ? 19.951  1.013   5.294  1.00 42.22  ? 194 SER A CB   1 
ATOM   3211 O  OG   . SER A 1 197 ? 19.742  2.079   6.196  1.00 43.09  ? 194 SER A OG   1 
ATOM   3212 H  H    . SER A 1 197 ? 20.012  2.831   3.698  1.00 49.50  ? 194 SER A H    1 
ATOM   3213 H  HA   . SER A 1 197 ? 19.157  0.399   3.496  1.00 44.43  ? 194 SER A HA   1 
ATOM   3214 H  HB2  . SER A 1 197 ? 19.759  0.174   5.741  1.00 50.70  ? 194 SER A HB2  1 
ATOM   3215 H  HB3  . SER A 1 197 ? 20.874  1.026   4.994  1.00 50.70  ? 194 SER A HB3  1 
ATOM   3216 H  HG   . SER A 1 197 ? 20.271  2.014   6.845  1.00 51.74  ? 194 SER A HG   1 
ATOM   3217 N  N    . TYR A 1 198 ? 16.954  2.323   4.738  1.00 30.47  ? 195 TYR A N    1 
ATOM   3218 C  CA   . TYR A 1 198 ? 15.560  2.332   5.169  1.00 32.51  ? 195 TYR A CA   1 
ATOM   3219 C  C    . TYR A 1 198 ? 14.601  2.059   4.010  1.00 27.34  ? 195 TYR A C    1 
ATOM   3220 O  O    . TYR A 1 198 ? 13.489  1.527   4.250  1.00 28.83  ? 195 TYR A O    1 
ATOM   3221 C  CB   . TYR A 1 198 ? 15.214  3.652   5.864  1.00 30.43  ? 195 TYR A CB   1 
ATOM   3222 C  CG   . TYR A 1 198 ? 15.830  3.684   7.248  1.00 30.40  ? 195 TYR A CG   1 
ATOM   3223 C  CD1  . TYR A 1 198 ? 15.164  3.121   8.317  1.00 30.81  ? 195 TYR A CD1  1 
ATOM   3224 C  CD2  . TYR A 1 198 ? 17.092  4.207   7.448  1.00 34.64  ? 195 TYR A CD2  1 
ATOM   3225 C  CE1  . TYR A 1 198 ? 15.743  3.102   9.603  1.00 33.34  ? 195 TYR A CE1  1 
ATOM   3226 C  CE2  . TYR A 1 198 ? 17.683  4.196   8.714  1.00 37.87  ? 195 TYR A CE2  1 
ATOM   3227 C  CZ   . TYR A 1 198 ? 17.001  3.657   9.775  1.00 40.62  ? 195 TYR A CZ   1 
ATOM   3228 O  OH   . TYR A 1 198 ? 17.580  3.657   11.014 1.00 42.17  ? 195 TYR A OH   1 
ATOM   3229 H  H    . TYR A 1 198 ? 17.311  3.098   4.636  1.00 36.59  ? 195 TYR A H    1 
ATOM   3230 H  HA   . TYR A 1 198 ? 15.436  1.628   5.826  1.00 39.05  ? 195 TYR A HA   1 
ATOM   3231 H  HB2  . TYR A 1 198 ? 15.565  4.394   5.349  1.00 36.55  ? 195 TYR A HB2  1 
ATOM   3232 H  HB3  . TYR A 1 198 ? 14.251  3.733   5.950  1.00 36.55  ? 195 TYR A HB3  1 
ATOM   3233 H  HD1  . TYR A 1 198 ? 14.322  2.748   8.188  1.00 37.01  ? 195 TYR A HD1  1 
ATOM   3234 H  HD2  . TYR A 1 198 ? 17.556  4.572   6.730  1.00 41.61  ? 195 TYR A HD2  1 
ATOM   3235 H  HE1  . TYR A 1 198 ? 15.289  2.725   10.322 1.00 40.04  ? 195 TYR A HE1  1 
ATOM   3236 H  HE2  . TYR A 1 198 ? 18.534  4.552   8.836  1.00 45.48  ? 195 TYR A HE2  1 
ATOM   3237 H  HH   . TYR A 1 198 ? 17.062  3.304   11.573 1.00 50.64  ? 195 TYR A HH   1 
ATOM   3238 N  N    . GLU A 1 199 ? 15.014  2.364   2.772  1.00 31.13  ? 196 GLU A N    1 
ATOM   3239 C  CA   . GLU A 1 199 ? 14.203  1.950   1.636  1.00 33.15  ? 196 GLU A CA   1 
ATOM   3240 C  C    . GLU A 1 199 ? 14.281  0.429   1.489  1.00 28.73  ? 196 GLU A C    1 
ATOM   3241 O  O    . GLU A 1 199 ? 13.255  -0.240  1.336  1.00 28.49  ? 196 GLU A O    1 
ATOM   3242 C  CB   . GLU A 1 199 ? 14.659  2.681   0.366  1.00 32.50  ? 196 GLU A CB   1 
ATOM   3243 C  CG   . GLU A 1 199 ? 14.284  1.954   -0.910 1.00 33.26  ? 196 GLU A CG   1 
ATOM   3244 C  CD   . GLU A 1 199 ? 14.234  2.807   -2.188 1.00 48.34  ? 196 GLU A CD   1 
ATOM   3245 O  OE1  . GLU A 1 199 ? 14.902  3.841   -2.264 1.00 39.98  ? 196 GLU A OE1  1 
ATOM   3246 O  OE2  . GLU A 1 199 ? 13.572  2.365   -3.151 1.00 50.64  ? 196 GLU A OE2  1 
ATOM   3247 H  H    . GLU A 1 199 ? 15.733  2.793   2.577  1.00 37.39  ? 196 GLU A H    1 
ATOM   3248 H  HA   . GLU A 1 199 ? 13.274  2.196   1.769  1.00 39.81  ? 196 GLU A HA   1 
ATOM   3249 H  HB2  . GLU A 1 199 ? 14.244  3.558   0.342  1.00 39.03  ? 196 GLU A HB2  1 
ATOM   3250 H  HB3  . GLU A 1 199 ? 15.624  2.772   0.385  1.00 39.03  ? 196 GLU A HB3  1 
ATOM   3251 H  HG2  . GLU A 1 199 ? 14.937  1.252   -1.061 1.00 39.95  ? 196 GLU A HG2  1 
ATOM   3252 H  HG3  . GLU A 1 199 ? 13.403  1.567   -0.790 1.00 39.95  ? 196 GLU A HG3  1 
ATOM   3253 N  N    . THR A 1 200 ? 15.491  -0.135  1.583  1.00 31.11  ? 197 THR A N    1 
ATOM   3254 C  CA   . THR A 1 200 ? 15.631  -1.586  1.534  1.00 30.00  ? 197 THR A CA   1 
ATOM   3255 C  C    . THR A 1 200 ? 14.855  -2.256  2.650  1.00 32.10  ? 197 THR A C    1 
ATOM   3256 O  O    . THR A 1 200 ? 14.203  -3.290  2.428  1.00 28.87  ? 197 THR A O    1 
ATOM   3257 C  CB   . THR A 1 200 ? 17.100  -1.987  1.617  1.00 34.17  ? 197 THR A CB   1 
ATOM   3258 O  OG1  . THR A 1 200 ? 17.795  -1.370  0.537  1.00 40.79  ? 197 THR A OG1  1 
ATOM   3259 C  CG2  . THR A 1 200 ? 17.218  -3.511  1.542  1.00 41.01  ? 197 THR A CG2  1 
ATOM   3260 H  H    . THR A 1 200 ? 16.230  0.294   1.674  1.00 37.36  ? 197 THR A H    1 
ATOM   3261 H  HA   . THR A 1 200 ? 15.278  -1.891  0.683  1.00 36.04  ? 197 THR A HA   1 
ATOM   3262 H  HB   . THR A 1 200 ? 17.500  -1.702  2.453  1.00 41.03  ? 197 THR A HB   1 
ATOM   3263 H  HG1  . THR A 1 200 ? 18.624  -1.432  0.657  1.00 48.98  ? 197 THR A HG1  1 
ATOM   3264 H  HG21 . THR A 1 200 ? 18.140  -3.765  1.379  1.00 49.25  ? 197 THR A HG21 1 
ATOM   3265 H  HG22 . THR A 1 200 ? 16.925  -3.908  2.378  1.00 49.25  ? 197 THR A HG22 1 
ATOM   3266 H  HG23 . THR A 1 200 ? 16.666  -3.852  0.821  1.00 49.25  ? 197 THR A HG23 1 
ATOM   3267 N  N    . SER A 1 201 ? 14.922  -1.688  3.863  1.00 29.27  ? 198 SER A N    1 
ATOM   3268 C  CA   . SER A 1 201 ? 14.165  -2.249  4.977  1.00 27.16  ? 198 SER A CA   1 
ATOM   3269 C  C    . SER A 1 201 ? 12.672  -2.249  4.698  1.00 25.09  ? 198 SER A C    1 
ATOM   3270 O  O    . SER A 1 201 ? 11.965  -3.208  5.031  1.00 24.86  ? 198 SER A O    1 
ATOM   3271 C  CB   . SER A 1 201 ? 14.444  -1.469  6.281  1.00 26.51  ? 198 SER A CB   1 
ATOM   3272 O  OG   . SER A 1 201 ? 15.788  -1.686  6.715  1.00 30.92  ? 198 SER A OG   1 
ATOM   3273 H  H    . SER A 1 201 ? 15.388  -0.992  4.057  1.00 35.16  ? 198 SER A H    1 
ATOM   3274 H  HA   . SER A 1 201 ? 14.461  -3.165  5.100  1.00 32.63  ? 198 SER A HA   1 
ATOM   3275 H  HB2  . SER A 1 201 ? 14.312  -0.521  6.118  1.00 31.85  ? 198 SER A HB2  1 
ATOM   3276 H  HB3  . SER A 1 201 ? 13.835  -1.774  6.971  1.00 31.85  ? 198 SER A HB3  1 
ATOM   3277 H  HG   . SER A 1 201 ? 16.324  -1.298  6.197  1.00 37.14  ? 198 SER A HG   1 
ATOM   3278 N  N    . ALA A 1 202 ? 12.159  -1.154  4.144  1.00 25.08  ? 199 ALA A N    1 
ATOM   3279 C  CA   . ALA A 1 202 ? 10.720  -1.054  3.933  1.00 23.58  ? 199 ALA A CA   1 
ATOM   3280 C  C    . ALA A 1 202 ? 10.233  -2.090  2.932  1.00 25.51  ? 199 ALA A C    1 
ATOM   3281 O  O    . ALA A 1 202 ? 9.185   -2.730  3.150  1.00 25.90  ? 199 ALA A O    1 
ATOM   3282 C  CB   . ALA A 1 202 ? 10.350  0.340   3.452  1.00 28.35  ? 199 ALA A CB   1 
ATOM   3283 H  H    . ALA A 1 202 ? 12.611  -0.470  3.888  1.00 30.13  ? 199 ALA A H    1 
ATOM   3284 H  HA   . ALA A 1 202 ? 10.278  -1.213  4.782  1.00 28.33  ? 199 ALA A HA   1 
ATOM   3285 H  HB1  . ALA A 1 202 ? 9.385   0.401   3.373  1.00 34.05  ? 199 ALA A HB1  1 
ATOM   3286 H  HB2  . ALA A 1 202 ? 10.671  0.991   4.095  1.00 34.05  ? 199 ALA A HB2  1 
ATOM   3287 H  HB3  . ALA A 1 202 ? 10.763  0.496   2.588  1.00 34.05  ? 199 ALA A HB3  1 
ATOM   3288 N  N    . HIS A 1 203 ? 10.983  -2.279  1.846  1.00 27.22  ? 200 HIS A N    1 
ATOM   3289 C  CA   . HIS A 1 203 ? 10.668  -3.344  0.897  1.00 25.68  ? 200 HIS A CA   1 
ATOM   3290 C  C    . HIS A 1 203 ? 10.694  -4.715  1.565  1.00 29.09  ? 200 HIS A C    1 
ATOM   3291 O  O    . HIS A 1 203 ? 9.823   -5.555  1.308  1.00 27.64  ? 200 HIS A O    1 
ATOM   3292 C  CB   . HIS A 1 203 ? 11.669  -3.307  -0.250 1.00 28.17  ? 200 HIS A CB   1 
ATOM   3293 C  CG   . HIS A 1 203 ? 11.401  -2.229  -1.260 1.00 28.84  ? 200 HIS A CG   1 
ATOM   3294 N  ND1  . HIS A 1 203 ? 10.359  -2.294  -2.160 1.00 30.71  ? 200 HIS A ND1  1 
ATOM   3295 C  CD2  . HIS A 1 203 ? 12.065  -1.082  -1.537 1.00 32.09  ? 200 HIS A CD2  1 
ATOM   3296 C  CE1  . HIS A 1 203 ? 10.380  -1.224  -2.935 1.00 34.37  ? 200 HIS A CE1  1 
ATOM   3297 N  NE2  . HIS A 1 203 ? 11.403  -0.466  -2.576 1.00 32.60  ? 200 HIS A NE2  1 
ATOM   3298 H  H    . HIS A 1 203 ? 11.673  -1.809  1.638  1.00 32.70  ? 200 HIS A H    1 
ATOM   3299 H  HA   . HIS A 1 203 ? 9.775   -3.198  0.546  1.00 30.85  ? 200 HIS A HA   1 
ATOM   3300 H  HB2  . HIS A 1 203 ? 12.555  -3.155  0.115  1.00 33.84  ? 200 HIS A HB2  1 
ATOM   3301 H  HB3  . HIS A 1 203 ? 11.642  -4.158  -0.714 1.00 33.84  ? 200 HIS A HB3  1 
ATOM   3302 H  HD2  . HIS A 1 203 ? 12.827  -0.769  -1.106 1.00 38.54  ? 200 HIS A HD2  1 
ATOM   3303 H  HE1  . HIS A 1 203 ? 9.778   -1.035  -3.618 1.00 41.27  ? 200 HIS A HE1  1 
ATOM   3304 H  HE2  . HIS A 1 203 ? 11.619  0.286   -2.932 1.00 39.16  ? 200 HIS A HE2  1 
ATOM   3305 N  N    . PHE A 1 204 ? 11.714  -4.978  2.382  1.00 26.40  ? 201 PHE A N    1 
ATOM   3306 C  CA   . PHE A 1 204 ? 11.793  -6.258  3.073  1.00 28.12  ? 201 PHE A CA   1 
ATOM   3307 C  C    . PHE A 1 204 ? 10.556  -6.476  3.926  1.00 26.61  ? 201 PHE A C    1 
ATOM   3308 O  O    . PHE A 1 204 ? 9.951   -7.564  3.924  1.00 25.71  ? 201 PHE A O    1 
ATOM   3309 C  CB   . PHE A 1 204 ? 13.063  -6.331  3.933  1.00 28.45  ? 201 PHE A CB   1 
ATOM   3310 C  CG   . PHE A 1 204 ? 13.148  -7.596  4.739  1.00 26.97  ? 201 PHE A CG   1 
ATOM   3311 C  CD1  . PHE A 1 204 ? 12.565  -7.666  6.003  1.00 30.71  ? 201 PHE A CD1  1 
ATOM   3312 C  CD2  . PHE A 1 204 ? 13.791  -8.711  4.226  1.00 31.16  ? 201 PHE A CD2  1 
ATOM   3313 C  CE1  . PHE A 1 204 ? 12.621  -8.830  6.736  1.00 34.10  ? 201 PHE A CE1  1 
ATOM   3314 C  CE2  . PHE A 1 204 ? 13.829  -9.900  4.967  1.00 34.44  ? 201 PHE A CE2  1 
ATOM   3315 C  CZ   . PHE A 1 204 ? 13.248  -9.940  6.219  1.00 32.69  ? 201 PHE A CZ   1 
ATOM   3316 H  H    . PHE A 1 204 ? 12.363  -4.439  2.549  1.00 31.71  ? 201 PHE A H    1 
ATOM   3317 H  HA   . PHE A 1 204 ? 11.847  -6.968  2.414  1.00 33.77  ? 201 PHE A HA   1 
ATOM   3318 H  HB2  . PHE A 1 204 ? 13.840  -6.291  3.354  1.00 34.18  ? 201 PHE A HB2  1 
ATOM   3319 H  HB3  . PHE A 1 204 ? 13.070  -5.581  4.549  1.00 34.18  ? 201 PHE A HB3  1 
ATOM   3320 H  HD1  . PHE A 1 204 ? 12.134  -6.921  6.354  1.00 36.89  ? 201 PHE A HD1  1 
ATOM   3321 H  HD2  . PHE A 1 204 ? 14.198  -8.670  3.390  1.00 37.42  ? 201 PHE A HD2  1 
ATOM   3322 H  HE1  . PHE A 1 204 ? 12.234  -8.866  7.581  1.00 40.95  ? 201 PHE A HE1  1 
ATOM   3323 H  HE2  . PHE A 1 204 ? 14.242  -10.657 4.618  1.00 41.37  ? 201 PHE A HE2  1 
ATOM   3324 H  HZ   . PHE A 1 204 ? 13.281  -10.725 6.717  1.00 39.27  ? 201 PHE A HZ   1 
ATOM   3325 N  N    . ILE A 1 205 ? 10.201  -5.467  4.726  1.00 24.99  ? 202 ILE A N    1 
ATOM   3326 C  CA   . ILE A 1 205 ? 9.058   -5.603  5.614  1.00 22.23  ? 202 ILE A CA   1 
ATOM   3327 C  C    . ILE A 1 205 ? 7.791   -5.830  4.796  1.00 27.72  ? 202 ILE A C    1 
ATOM   3328 O  O    . ILE A 1 205 ? 7.014   -6.751  5.055  1.00 26.79  ? 202 ILE A O    1 
ATOM   3329 C  CB   . ILE A 1 205 ? 8.949   -4.363  6.523  1.00 22.66  ? 202 ILE A CB   1 
ATOM   3330 C  CG1  . ILE A 1 205 ? 10.125  -4.355  7.471  1.00 25.99  ? 202 ILE A CG1  1 
ATOM   3331 C  CG2  . ILE A 1 205 ? 7.617   -4.347  7.276  1.00 27.47  ? 202 ILE A CG2  1 
ATOM   3332 C  CD1  . ILE A 1 205 ? 10.297  -3.011  8.183  1.00 27.86  ? 202 ILE A CD1  1 
ATOM   3333 H  H    . ILE A 1 205 ? 10.602  -4.707  4.770  1.00 30.02  ? 202 ILE A H    1 
ATOM   3334 H  HA   . ILE A 1 205 ? 9.184   -6.378  6.184  1.00 26.71  ? 202 ILE A HA   1 
ATOM   3335 H  HB   . ILE A 1 205 ? 8.971   -3.559  5.980  1.00 27.23  ? 202 ILE A HB   1 
ATOM   3336 H  HG12 . ILE A 1 205 ? 9.991   -5.039  8.146  1.00 31.22  ? 202 ILE A HG12 1 
ATOM   3337 H  HG13 . ILE A 1 205 ? 10.936  -4.537  6.970  1.00 31.22  ? 202 ILE A HG13 1 
ATOM   3338 H  HG21 . ILE A 1 205 ? 7.660   -3.681  7.980  1.00 33.00  ? 202 ILE A HG21 1 
ATOM   3339 H  HG22 . ILE A 1 205 ? 6.906   -4.126  6.654  1.00 33.00  ? 202 ILE A HG22 1 
ATOM   3340 H  HG23 . ILE A 1 205 ? 7.461   -5.224  7.659  1.00 33.00  ? 202 ILE A HG23 1 
ATOM   3341 H  HD11 . ILE A 1 205 ? 11.154  -3.001  8.637  1.00 33.47  ? 202 ILE A HD11 1 
ATOM   3342 H  HD12 . ILE A 1 205 ? 10.262  -2.298  7.525  1.00 33.47  ? 202 ILE A HD12 1 
ATOM   3343 H  HD13 . ILE A 1 205 ? 9.580   -2.901  8.827  1.00 33.47  ? 202 ILE A HD13 1 
ATOM   3344 N  N    . TYR A 1 206 ? 7.579   -5.014  3.768  1.00 24.82  ? 203 TYR A N    1 
ATOM   3345 C  CA   . TYR A 1 206 ? 6.389   -5.152  2.946  1.00 25.31  ? 203 TYR A CA   1 
ATOM   3346 C  C    . TYR A 1 206 ? 6.278   -6.547  2.362  1.00 28.62  ? 203 TYR A C    1 
ATOM   3347 O  O    . TYR A 1 206 ? 5.203   -7.163  2.388  1.00 29.35  ? 203 TYR A O    1 
ATOM   3348 C  CB   . TYR A 1 206 ? 6.427   -4.115  1.821  1.00 32.15  ? 203 TYR A CB   1 
ATOM   3349 C  CG   . TYR A 1 206 ? 5.339   -4.276  0.797  1.00 26.55  ? 203 TYR A CG   1 
ATOM   3350 C  CD1  . TYR A 1 206 ? 5.466   -5.159  -0.262 1.00 28.13  ? 203 TYR A CD1  1 
ATOM   3351 C  CD2  . TYR A 1 206 ? 4.137   -3.576  0.923  1.00 29.89  ? 203 TYR A CD2  1 
ATOM   3352 C  CE1  . TYR A 1 206 ? 4.469   -5.319  -1.185 1.00 30.79  ? 203 TYR A CE1  1 
ATOM   3353 C  CE2  . TYR A 1 206 ? 3.127   -3.744  -0.012 1.00 33.12  ? 203 TYR A CE2  1 
ATOM   3354 C  CZ   . TYR A 1 206 ? 3.295   -4.613  -1.039 1.00 31.89  ? 203 TYR A CZ   1 
ATOM   3355 O  OH   . TYR A 1 206 ? 2.299   -4.788  -1.996 1.00 36.21  ? 203 TYR A OH   1 
ATOM   3356 H  H    . TYR A 1 206 ? 8.106   -4.378  3.528  1.00 29.82  ? 203 TYR A H    1 
ATOM   3357 H  HA   . TYR A 1 206 ? 5.607   -4.994  3.498  1.00 30.40  ? 203 TYR A HA   1 
ATOM   3358 H  HB2  . TYR A 1 206 ? 6.336   -3.232  2.211  1.00 38.61  ? 203 TYR A HB2  1 
ATOM   3359 H  HB3  . TYR A 1 206 ? 7.277   -4.189  1.360  1.00 38.61  ? 203 TYR A HB3  1 
ATOM   3360 H  HD1  . TYR A 1 206 ? 6.248   -5.655  -0.348 1.00 33.79  ? 203 TYR A HD1  1 
ATOM   3361 H  HD2  . TYR A 1 206 ? 4.013   -2.994  1.637  1.00 35.91  ? 203 TYR A HD2  1 
ATOM   3362 H  HE1  . TYR A 1 206 ? 4.582   -5.899  -1.904 1.00 36.99  ? 203 TYR A HE1  1 
ATOM   3363 H  HE2  . TYR A 1 206 ? 2.335   -3.261  0.066  1.00 39.78  ? 203 TYR A HE2  1 
ATOM   3364 H  HH   . TYR A 1 206 ? 1.755   -4.149  -1.965 1.00 43.48  ? 203 TYR A HH   1 
ATOM   3365 N  N    . GLU A 1 207 ? 7.382   -7.057  1.818  1.00 28.80  ? 204 GLU A N    1 
ATOM   3366 C  CA   . GLU A 1 207 ? 7.359   -8.331  1.108  1.00 26.29  ? 204 GLU A CA   1 
ATOM   3367 C  C    . GLU A 1 207 ? 7.148   -9.508  2.034  1.00 27.54  ? 204 GLU A C    1 
ATOM   3368 O  O    . GLU A 1 207 ? 6.717   -10.564 1.571  1.00 32.55  ? 204 GLU A O    1 
ATOM   3369 C  CB   . GLU A 1 207 ? 8.655   -8.492  0.320  1.00 28.58  ? 204 GLU A CB   1 
ATOM   3370 C  CG   . GLU A 1 207 ? 8.659   -7.563  -0.883 1.00 28.78  ? 204 GLU A CG   1 
ATOM   3371 C  CD   . GLU A 1 207 ? 10.026  -7.387  -1.573 1.00 32.37  ? 204 GLU A CD   1 
ATOM   3372 O  OE1  . GLU A 1 207 ? 10.918  -8.248  -1.450 1.00 32.43  ? 204 GLU A OE1  1 
ATOM   3373 O  OE2  . GLU A 1 207 ? 10.197  -6.358  -2.306 1.00 35.96  ? 204 GLU A OE2  1 
ATOM   3374 H  H    . GLU A 1 207 ? 8.157   -6.685  1.847  1.00 34.60  ? 204 GLU A H    1 
ATOM   3375 H  HA   . GLU A 1 207 ? 6.621   -8.332  0.478  1.00 31.58  ? 204 GLU A HA   1 
ATOM   3376 H  HB2  . GLU A 1 207 ? 9.410   -8.269  0.888  1.00 34.33  ? 204 GLU A HB2  1 
ATOM   3377 H  HB3  . GLU A 1 207 ? 8.734   -9.406  0.007  1.00 34.33  ? 204 GLU A HB3  1 
ATOM   3378 H  HG2  . GLU A 1 207 ? 8.044   -7.916  -1.545 1.00 34.57  ? 204 GLU A HG2  1 
ATOM   3379 H  HG3  . GLU A 1 207 ? 8.367   -6.684  -0.593 1.00 34.57  ? 204 GLU A HG3  1 
ATOM   3380 N  N    . HIS A 1 208 ? 7.457   -9.365  3.318  1.00 25.20  ? 205 HIS A N    1 
ATOM   3381 C  CA   . HIS A 1 208 ? 7.373   -10.498 4.240  1.00 25.48  ? 205 HIS A CA   1 
ATOM   3382 C  C    . HIS A 1 208 ? 6.166   -10.434 5.147  1.00 27.81  ? 205 HIS A C    1 
ATOM   3383 O  O    . HIS A 1 208 ? 5.891   -11.413 5.846  1.00 27.12  ? 205 HIS A O    1 
ATOM   3384 C  CB   . HIS A 1 208 ? 8.647   -10.623 5.076  1.00 26.00  ? 205 HIS A CB   1 
ATOM   3385 C  CG   . HIS A 1 208 ? 9.806   -11.100 4.278  1.00 28.20  ? 205 HIS A CG   1 
ATOM   3386 N  ND1  . HIS A 1 208 ? 10.532  -10.261 3.460  1.00 30.79  ? 205 HIS A ND1  1 
ATOM   3387 C  CD2  . HIS A 1 208 ? 10.288  -12.348 4.071  1.00 36.01  ? 205 HIS A CD2  1 
ATOM   3388 C  CE1  . HIS A 1 208 ? 11.432  -10.974 2.798  1.00 35.18  ? 205 HIS A CE1  1 
ATOM   3389 N  NE2  . HIS A 1 208 ? 11.315  -12.239 3.166  1.00 39.27  ? 205 HIS A NE2  1 
ATOM   3390 H  H    . HIS A 1 208 ? 7.716   -8.629  3.679  1.00 30.28  ? 205 HIS A H    1 
ATOM   3391 H  HA   . HIS A 1 208 ? 7.304   -11.312 3.716  1.00 30.61  ? 205 HIS A HA   1 
ATOM   3392 H  HB2  . HIS A 1 208 ? 8.871   -9.753  5.443  1.00 31.24  ? 205 HIS A HB2  1 
ATOM   3393 H  HB3  . HIS A 1 208 ? 8.494   -11.256 5.794  1.00 31.24  ? 205 HIS A HB3  1 
ATOM   3394 H  HD1  . HIS A 1 208 ? 10.420  -9.411  3.391  1.00 36.99  ? 205 HIS A HD1  1 
ATOM   3395 H  HD2  . HIS A 1 208 ? 9.982   -13.131 4.468  1.00 43.25  ? 205 HIS A HD2  1 
ATOM   3396 H  HE1  . HIS A 1 208 ? 12.041  -10.641 2.179  1.00 42.25  ? 205 HIS A HE1  1 
ATOM   3397 N  N    . LEU A 1 209 ? 5.402   -9.357  5.104  1.00 25.68  ? 206 LEU A N    1 
ATOM   3398 C  CA   . LEU A 1 209 ? 4.164   -9.305  5.857  1.00 22.57  ? 206 LEU A CA   1 
ATOM   3399 C  C    . LEU A 1 209 ? 3.150   -10.307 5.320  1.00 29.66  ? 206 LEU A C    1 
ATOM   3400 O  O    . LEU A 1 209 ? 3.037   -10.510 4.109  1.00 29.25  ? 206 LEU A O    1 
ATOM   3401 C  CB   . LEU A 1 209 ? 3.506   -7.927  5.797  1.00 28.53  ? 206 LEU A CB   1 
ATOM   3402 C  CG   . LEU A 1 209 ? 4.137   -6.742  6.488  1.00 32.85  ? 206 LEU A CG   1 
ATOM   3403 C  CD1  . LEU A 1 209 ? 3.299   -5.508  6.254  1.00 39.84  ? 206 LEU A CD1  1 
ATOM   3404 C  CD2  . LEU A 1 209 ? 4.236   -7.067  7.942  1.00 26.84  ? 206 LEU A CD2  1 
ATOM   3405 H  H    . LEU A 1 209 ? 5.576   -8.647  4.650  1.00 30.85  ? 206 LEU A H    1 
ATOM   3406 H  HA   . LEU A 1 209 ? 4.388   -9.509  6.778  1.00 27.11  ? 206 LEU A HA   1 
ATOM   3407 H  HB2  . LEU A 1 209 ? 3.439   -7.685  4.860  1.00 34.27  ? 206 LEU A HB2  1 
ATOM   3408 H  HB3  . LEU A 1 209 ? 2.619   -8.019  6.180  1.00 34.27  ? 206 LEU A HB3  1 
ATOM   3409 H  HG   . LEU A 1 209 ? 5.024   -6.555  6.142  1.00 39.46  ? 206 LEU A HG   1 
ATOM   3410 H  HD11 . LEU A 1 209 ? 3.755   -4.740  6.632  1.00 47.85  ? 206 LEU A HD11 1 
ATOM   3411 H  HD12 . LEU A 1 209 ? 3.178   -5.385  5.300  1.00 47.85  ? 206 LEU A HD12 1 
ATOM   3412 H  HD13 . LEU A 1 209 ? 2.437   -5.625  6.684  1.00 47.85  ? 206 LEU A HD13 1 
ATOM   3413 H  HD21 . LEU A 1 209 ? 4.511   -6.272  8.425  1.00 32.25  ? 206 LEU A HD21 1 
ATOM   3414 H  HD22 . LEU A 1 209 ? 3.369   -7.363  8.259  1.00 32.25  ? 206 LEU A HD22 1 
ATOM   3415 H  HD23 . LEU A 1 209 ? 4.891   -7.771  8.064  1.00 32.25  ? 206 LEU A HD23 1 
ATOM   3416 N  N    . GLY A 1 210 ? 2.365   -10.886 6.233  1.00 29.30  ? 207 GLY A N    1 
ATOM   3417 C  CA   . GLY A 1 210 ? 1.266   -11.747 5.839  1.00 30.88  ? 207 GLY A CA   1 
ATOM   3418 C  C    . GLY A 1 210 ? 0.035   -11.042 5.339  1.00 31.22  ? 207 GLY A C    1 
ATOM   3419 O  O    . GLY A 1 210 ? -0.835  -11.680 4.747  1.00 32.21  ? 207 GLY A O    1 
ATOM   3420 H  H    . GLY A 1 210 ? 2.453   -10.791 7.083  1.00 35.19  ? 207 GLY A H    1 
ATOM   3421 H  HA2  . GLY A 1 210 ? 1.574   -12.335 5.132  1.00 37.09  ? 207 GLY A HA2  1 
ATOM   3422 H  HA3  . GLY A 1 210 ? 1.005   -12.283 6.605  1.00 37.09  ? 207 GLY A HA3  1 
ATOM   3423 N  N    . SER A 1 211 ? -0.061  -9.745  5.577  1.00 26.82  ? 208 SER A N    1 
ATOM   3424 C  CA   . SER A 1 211 ? -1.264  -8.984  5.263  1.00 28.39  ? 208 SER A CA   1 
ATOM   3425 C  C    . SER A 1 211 ? -1.588  -9.038  3.783  1.00 31.66  ? 208 SER A C    1 
ATOM   3426 O  O    . SER A 1 211 ? -0.703  -8.863  2.943  1.00 32.71  ? 208 SER A O    1 
ATOM   3427 C  CB   . SER A 1 211 ? -1.077  -7.522  5.666  1.00 31.70  ? 208 SER A CB   1 
ATOM   3428 O  OG   . SER A 1 211 ? -0.585  -7.436  7.003  1.00 30.88  ? 208 SER A OG   1 
ATOM   3429 H  H    . SER A 1 211 ? 0.565   -9.269  5.927  1.00 32.22  ? 208 SER A H    1 
ATOM   3430 H  HA   . SER A 1 211 ? -2.006  -9.370  5.755  1.00 34.11  ? 208 SER A HA   1 
ATOM   3431 H  HB2  . SER A 1 211 ? -0.439  -7.106  5.066  1.00 38.08  ? 208 SER A HB2  1 
ATOM   3432 H  HB3  . SER A 1 211 ? -1.930  -7.064  5.611  1.00 38.08  ? 208 SER A HB3  1 
ATOM   3433 H  HG   . SER A 1 211 ? -0.476  -6.632  7.218  1.00 37.09  ? 208 SER A HG   1 
ATOM   3434 N  N    . VAL A 1 212 ? -2.871  -9.235  3.470  1.00 31.79  ? 209 VAL A N    1 
ATOM   3435 C  CA   . VAL A 1 212 ? -3.297  -9.147  2.083  1.00 30.94  ? 209 VAL A CA   1 
ATOM   3436 C  C    . VAL A 1 212 ? -3.510  -7.694  1.689  1.00 32.62  ? 209 VAL A C    1 
ATOM   3437 O  O    . VAL A 1 212 ? -3.280  -7.326  0.538  1.00 38.78  ? 209 VAL A O    1 
ATOM   3438 C  CB   . VAL A 1 212 ? -4.556  -9.995  1.828  1.00 41.04  ? 209 VAL A CB   1 
ATOM   3439 C  CG1  . VAL A 1 212 ? -4.227  -11.475 2.002  1.00 47.92  ? 209 VAL A CG1  1 
ATOM   3440 C  CG2  . VAL A 1 212 ? -5.686  -9.592  2.739  1.00 48.20  ? 209 VAL A CG2  1 
ATOM   3441 H  H    . VAL A 1 212 ? -3.496  -9.416  4.032  1.00 38.19  ? 209 VAL A H    1 
ATOM   3442 H  HA   . VAL A 1 212 ? -2.593  -9.516  1.527  1.00 37.17  ? 209 VAL A HA   1 
ATOM   3443 H  HB   . VAL A 1 212 ? -4.854  -9.844  0.917  1.00 49.28  ? 209 VAL A HB   1 
ATOM   3444 H  HG11 . VAL A 1 212 ? -5.027  -11.998 1.837  1.00 57.54  ? 209 VAL A HG11 1 
ATOM   3445 H  HG12 . VAL A 1 212 ? -3.535  -11.721 1.368  1.00 57.54  ? 209 VAL A HG12 1 
ATOM   3446 H  HG13 . VAL A 1 212 ? -3.914  -11.624 2.908  1.00 57.54  ? 209 VAL A HG13 1 
ATOM   3447 H  HG21 . VAL A 1 212 ? -6.462  -10.138 2.540  1.00 57.88  ? 209 VAL A HG21 1 
ATOM   3448 H  HG22 . VAL A 1 212 ? -5.413  -9.728  3.660  1.00 57.88  ? 209 VAL A HG22 1 
ATOM   3449 H  HG23 . VAL A 1 212 ? -5.892  -8.656  2.590  1.00 57.88  ? 209 VAL A HG23 1 
ATOM   3450 N  N    A ASP A 1 213 ? -4.019  -6.878  2.609  0.46 31.41  ? 210 ASP A N    1 
ATOM   3451 N  N    B ASP A 1 213 ? -3.852  -6.824  2.643  0.54 30.96  ? 210 ASP A N    1 
ATOM   3452 C  CA   A ASP A 1 213 ? -4.131  -5.443  2.403  0.46 31.02  ? 210 ASP A CA   1 
ATOM   3453 C  CA   B ASP A 1 213 ? -4.161  -5.414  2.384  0.54 30.98  ? 210 ASP A CA   1 
ATOM   3454 C  C    A ASP A 1 213 ? -2.865  -4.816  2.975  0.46 29.79  ? 210 ASP A C    1 
ATOM   3455 C  C    B ASP A 1 213 ? -3.018  -4.546  2.910  0.54 30.55  ? 210 ASP A C    1 
ATOM   3456 O  O    A ASP A 1 213 ? -2.665  -4.764  4.200  0.46 27.23  ? 210 ASP A O    1 
ATOM   3457 O  O    B ASP A 1 213 ? -3.083  -4.009  4.020  0.54 30.17  ? 210 ASP A O    1 
ATOM   3458 C  CB   A ASP A 1 213 ? -5.398  -4.870  3.031  0.46 34.08  ? 210 ASP A CB   1 
ATOM   3459 C  CB   B ASP A 1 213 ? -5.491  -5.040  3.032  0.54 34.19  ? 210 ASP A CB   1 
ATOM   3460 C  CG   A ASP A 1 213 ? -6.669  -5.467  2.435  0.46 36.72  ? 210 ASP A CG   1 
ATOM   3461 C  CG   B ASP A 1 213 ? -5.945  -3.632  2.700  0.54 42.21  ? 210 ASP A CG   1 
ATOM   3462 O  OD1  A ASP A 1 213 ? -6.712  -5.687  1.199  0.46 43.24  ? 210 ASP A OD1  1 
ATOM   3463 O  OD1  B ASP A 1 213 ? -5.188  -2.877  2.055  0.54 36.34  ? 210 ASP A OD1  1 
ATOM   3464 O  OD2  A ASP A 1 213 ? -7.639  -5.683  3.193  0.46 44.52  ? 210 ASP A OD2  1 
ATOM   3465 O  OD2  B ASP A 1 213 ? -7.073  -3.279  3.101  0.54 47.47  ? 210 ASP A OD2  1 
ATOM   3466 H  H    A ASP A 1 213 ? -4.311  -7.140  3.374  0.46 37.73  ? 210 ASP A H    1 
ATOM   3467 H  H    B ASP A 1 213 ? -3.913  -7.034  3.475  0.54 37.19  ? 210 ASP A H    1 
ATOM   3468 H  HA   A ASP A 1 213 ? -4.191  -5.245  1.456  0.46 37.25  ? 210 ASP A HA   1 
ATOM   3469 H  HA   B ASP A 1 213 ? -4.216  -5.275  1.425  0.54 37.22  ? 210 ASP A HA   1 
ATOM   3470 H  HB2  A ASP A 1 213 ? -5.394  -5.060  3.983  0.46 40.94  ? 210 ASP A HB2  1 
ATOM   3471 H  HB2  B ASP A 1 213 ? -6.175  -5.654  2.723  0.54 41.06  ? 210 ASP A HB2  1 
ATOM   3472 H  HB3  A ASP A 1 213 ? -5.418  -3.911  2.885  0.46 40.94  ? 210 ASP A HB3  1 
ATOM   3473 H  HB3  B ASP A 1 213 ? -5.399  -5.103  3.996  0.54 41.06  ? 210 ASP A HB3  1 
ATOM   3474 N  N    . LYS A 1 214 ? -1.994  -4.364  2.081  1.00 31.38  ? 211 LYS A N    1 
ATOM   3475 C  CA   . LYS A 1 214 ? -0.776  -3.699  2.497  1.00 29.76  ? 211 LYS A CA   1 
ATOM   3476 C  C    . LYS A 1 214 ? -0.348  -2.753  1.398  1.00 31.61  ? 211 LYS A C    1 
ATOM   3477 O  O    . LYS A 1 214 ? -0.598  -3.003  0.212  1.00 32.14  ? 211 LYS A O    1 
ATOM   3478 C  CB   . LYS A 1 214 ? 0.336   -4.692  2.813  1.00 27.92  ? 211 LYS A CB   1 
ATOM   3479 C  CG   . LYS A 1 214 ? 0.622   -5.689  1.702  1.00 28.84  ? 211 LYS A CG   1 
ATOM   3480 C  CD   . LYS A 1 214 ? 1.730   -6.667  2.093  1.00 32.53  ? 211 LYS A CD   1 
ATOM   3481 C  CE   . LYS A 1 214 ? 2.014   -7.717  1.024  1.00 34.88  ? 211 LYS A CE   1 
ATOM   3482 N  NZ   . LYS A 1 214 ? 3.043   -8.684  1.529  1.00 32.51  ? 211 LYS A NZ   1 
ATOM   3483 H  H    A LYS A 1 214 ? -2.088  -4.433  1.229  0.46 37.69  ? 211 LYS A H    1 
ATOM   3484 H  H    B LYS A 1 214 ? -1.985  -4.624  1.261  0.54 37.69  ? 211 LYS A H    1 
ATOM   3485 H  HA   . LYS A 1 214 ? -0.938  -3.181  3.301  1.00 35.75  ? 211 LYS A HA   1 
ATOM   3486 H  HB2  . LYS A 1 214 ? 1.153   -4.198  2.982  1.00 33.54  ? 211 LYS A HB2  1 
ATOM   3487 H  HB3  . LYS A 1 214 ? 0.084   -5.197  3.603  1.00 33.54  ? 211 LYS A HB3  1 
ATOM   3488 H  HG2  . LYS A 1 214 ? -0.181  -6.199  1.515  1.00 34.64  ? 211 LYS A HG2  1 
ATOM   3489 H  HG3  . LYS A 1 214 ? 0.905   -5.211  0.907  1.00 34.64  ? 211 LYS A HG3  1 
ATOM   3490 H  HD2  . LYS A 1 214 ? 2.549   -6.169  2.246  1.00 39.07  ? 211 LYS A HD2  1 
ATOM   3491 H  HD3  . LYS A 1 214 ? 1.468   -7.131  2.904  1.00 39.07  ? 211 LYS A HD3  1 
ATOM   3492 H  HE2  . LYS A 1 214 ? 1.200   -8.204  0.819  1.00 41.89  ? 211 LYS A HE2  1 
ATOM   3493 H  HE3  . LYS A 1 214 ? 2.354   -7.287  0.224  1.00 41.89  ? 211 LYS A HE3  1 
ATOM   3494 H  HZ1  . LYS A 1 214 ? 3.256   -9.264  0.889  1.00 39.05  ? 211 LYS A HZ1  1 
ATOM   3495 H  HZ2  . LYS A 1 214 ? 3.777   -8.245  1.777  1.00 39.05  ? 211 LYS A HZ2  1 
ATOM   3496 H  HZ3  . LYS A 1 214 ? 2.723   -9.131  2.229  1.00 39.05  ? 211 LYS A HZ3  1 
ATOM   3497 N  N    . GLU A 1 215 ? 0.288   -1.651  1.804  1.00 28.80  ? 212 GLU A N    1 
ATOM   3498 C  CA   . GLU A 1 215 ? 0.803   -0.675  0.844  1.00 31.41  ? 212 GLU A CA   1 
ATOM   3499 C  C    . GLU A 1 215 ? 2.190   -0.233  1.266  1.00 31.07  ? 212 GLU A C    1 
ATOM   3500 O  O    . GLU A 1 215 ? 2.561   -0.319  2.445  1.00 29.81  ? 212 GLU A O    1 
ATOM   3501 C  CB   . GLU A 1 215 ? -0.170  0.499   0.676  1.00 39.61  ? 212 GLU A CB   1 
ATOM   3502 C  CG   . GLU A 1 215 ? -0.462  1.288   1.897  1.00 40.93  ? 212 GLU A CG   1 
ATOM   3503 C  CD   . GLU A 1 215 ? -1.571  2.325   1.651  1.00 47.51  ? 212 GLU A CD   1 
ATOM   3504 O  OE1  . GLU A 1 215 ? -1.273  3.374   1.055  1.00 49.85  ? 212 GLU A OE1  1 
ATOM   3505 O  OE2  . GLU A 1 215 ? -2.739  2.079   2.028  1.00 54.76  ? 212 GLU A OE2  1 
ATOM   3506 H  H    . GLU A 1 215 ? 0.432   -1.448  2.627  1.00 34.59  ? 212 GLU A H    1 
ATOM   3507 H  HA   . GLU A 1 215 ? 0.910   -1.077  -0.033 1.00 37.73  ? 212 GLU A HA   1 
ATOM   3508 H  HB2  . GLU A 1 215 ? 0.205   1.111   0.023  1.00 47.57  ? 212 GLU A HB2  1 
ATOM   3509 H  HB3  . GLU A 1 215 ? -1.015  0.147   0.354  1.00 47.57  ? 212 GLU A HB3  1 
ATOM   3510 H  HG2  . GLU A 1 215 ? -0.754  0.691   2.603  1.00 49.15  ? 212 GLU A HG2  1 
ATOM   3511 H  HG3  . GLU A 1 215 ? 0.340   1.760   2.173  1.00 49.15  ? 212 GLU A HG3  1 
ATOM   3512 N  N    . LEU A 1 216 ? 2.975   0.173   0.267  1.00 30.97  ? 213 LEU A N    1 
ATOM   3513 C  CA   . LEU A 1 216 ? 4.324   0.677   0.479  1.00 28.59  ? 213 LEU A CA   1 
ATOM   3514 C  C    . LEU A 1 216 ? 4.346   2.098   -0.065 1.00 26.52  ? 213 LEU A C    1 
ATOM   3515 O  O    . LEU A 1 216 ? 4.013   2.322   -1.232 1.00 31.05  ? 213 LEU A O    1 
ATOM   3516 C  CB   . LEU A 1 216 ? 5.350   -0.214  -0.230 1.00 28.63  ? 213 LEU A CB   1 
ATOM   3517 C  CG   . LEU A 1 216 ? 6.815   0.181   -0.099 1.00 38.11  ? 213 LEU A CG   1 
ATOM   3518 C  CD1  . LEU A 1 216 ? 7.296   0.077   1.298  1.00 33.44  ? 213 LEU A CD1  1 
ATOM   3519 C  CD2  . LEU A 1 216 ? 7.686   -0.688  -0.993 1.00 42.93  ? 213 LEU A CD2  1 
ATOM   3520 H  H    . LEU A 1 216 ? 2.739   0.164   -0.560 1.00 37.19  ? 213 LEU A H    1 
ATOM   3521 H  HA   . LEU A 1 216 ? 4.555   0.692   1.420  1.00 34.34  ? 213 LEU A HA   1 
ATOM   3522 H  HB2  . LEU A 1 216 ? 5.265   -1.111  0.129  1.00 34.39  ? 213 LEU A HB2  1 
ATOM   3523 H  HB3  . LEU A 1 216 ? 5.141   -0.215  -1.177 1.00 34.39  ? 213 LEU A HB3  1 
ATOM   3524 H  HG   . LEU A 1 216 ? 6.892   1.107   -0.375 1.00 45.77  ? 213 LEU A HG   1 
ATOM   3525 H  HD11 . LEU A 1 216 ? 8.239   0.302   1.325  1.00 40.16  ? 213 LEU A HD11 1 
ATOM   3526 H  HD12 . LEU A 1 216 ? 6.793   0.694   1.852  1.00 40.16  ? 213 LEU A HD12 1 
ATOM   3527 H  HD13 . LEU A 1 216 ? 7.164   -0.831  1.611  1.00 40.16  ? 213 LEU A HD13 1 
ATOM   3528 H  HD21 . LEU A 1 216 ? 8.619   -0.511  -0.794 1.00 51.55  ? 213 LEU A HD21 1 
ATOM   3529 H  HD22 . LEU A 1 216 ? 7.483   -1.621  -0.822 1.00 51.55  ? 213 LEU A HD22 1 
ATOM   3530 H  HD23 . LEU A 1 216 ? 7.500   -0.474  -1.921 1.00 51.55  ? 213 LEU A HD23 1 
ATOM   3531 N  N    . ASN A 1 217 ? 4.704   3.052   0.788  1.00 27.89  ? 214 ASN A N    1 
ATOM   3532 C  CA   . ASN A 1 217 ? 4.708   4.465   0.426  1.00 31.96  ? 214 ASN A CA   1 
ATOM   3533 C  C    . ASN A 1 217 ? 6.077   5.057   0.717  1.00 32.08  ? 214 ASN A C    1 
ATOM   3534 O  O    . ASN A 1 217 ? 6.408   5.303   1.874  1.00 32.68  ? 214 ASN A O    1 
ATOM   3535 C  CB   . ASN A 1 217 ? 3.621   5.232   1.168  1.00 30.86  ? 214 ASN A CB   1 
ATOM   3536 C  CG   . ASN A 1 217 ? 2.236   4.889   0.672  1.00 34.30  ? 214 ASN A CG   1 
ATOM   3537 O  OD1  . ASN A 1 217 ? 1.899   5.204   -0.452 1.00 36.36  ? 214 ASN A OD1  1 
ATOM   3538 N  ND2  . ASN A 1 217 ? 1.423   4.257   1.515  1.00 35.36  ? 214 ASN A ND2  1 
ATOM   3539 H  H    . ASN A 1 217 ? 4.953   2.903   1.598  1.00 33.51  ? 214 ASN A H    1 
ATOM   3540 H  HA   . ASN A 1 217 ? 4.551   4.531   -0.529 1.00 38.39  ? 214 ASN A HA   1 
ATOM   3541 H  HB2  . ASN A 1 217 ? 3.665   5.012   2.112  1.00 37.07  ? 214 ASN A HB2  1 
ATOM   3542 H  HB3  . ASN A 1 217 ? 3.759   6.183   1.042  1.00 37.07  ? 214 ASN A HB3  1 
ATOM   3543 H  HD21 . ASN A 1 217 ? 0.627   4.045   1.268  1.00 42.46  ? 214 ASN A HD21 1 
ATOM   3544 H  HD22 . ASN A 1 217 ? 1.694   4.060   2.307  1.00 42.46  ? 214 ASN A HD22 1 
ATOM   3545 N  N    . GLY A 1 218 ? 6.862   5.278   -0.339 1.00 29.14  ? 215 GLY A N    1 
ATOM   3546 C  CA   . GLY A 1 218 ? 8.061   6.086   -0.209 1.00 32.96  ? 215 GLY A CA   1 
ATOM   3547 C  C    . GLY A 1 218 ? 7.745   7.541   -0.477 1.00 36.11  ? 215 GLY A C    1 
ATOM   3548 O  O    . GLY A 1 218 ? 7.278   7.911   -1.566 1.00 36.14  ? 215 GLY A O    1 
ATOM   3549 H  H    . GLY A 1 218 ? 6.719   4.972   -1.129 1.00 35.00  ? 215 GLY A H    1 
ATOM   3550 H  HA2  . GLY A 1 218 ? 8.418   6.002   0.689  1.00 39.58  ? 215 GLY A HA2  1 
ATOM   3551 H  HA3  . GLY A 1 218 ? 8.729   5.787   -0.845 1.00 39.58  ? 215 GLY A HA3  1 
ATOM   3552 N  N    . LEU A 1 219 ? 7.989   8.391   0.523  1.00 32.27  ? 216 LEU A N    1 
ATOM   3553 C  CA   . LEU A 1 219 ? 7.701   9.816   0.404  1.00 30.60  ? 216 LEU A CA   1 
ATOM   3554 C  C    . LEU A 1 219 ? 9.004   10.545  0.119  1.00 34.57  ? 216 LEU A C    1 
ATOM   3555 O  O    . LEU A 1 219 ? 9.914   10.560  0.955  1.00 35.61  ? 216 LEU A O    1 
ATOM   3556 C  CB   . LEU A 1 219 ? 7.031   10.312  1.693  1.00 31.28  ? 216 LEU A CB   1 
ATOM   3557 C  CG   . LEU A 1 219 ? 5.772   9.523   2.092  1.00 39.53  ? 216 LEU A CG   1 
ATOM   3558 C  CD1  . LEU A 1 219 ? 5.133   10.180  3.342  1.00 40.76  ? 216 LEU A CD1  1 
ATOM   3559 C  CD2  . LEU A 1 219 ? 4.768   9.431   0.956  1.00 43.85  ? 216 LEU A CD2  1 
ATOM   3560 H  H    . LEU A 1 219 ? 8.322   8.162   1.282  1.00 38.76  ? 216 LEU A H    1 
ATOM   3561 H  HA   . LEU A 1 219 ? 7.099   9.996   -0.335 1.00 36.54  ? 216 LEU A HA   1 
ATOM   3562 H  HB2  . LEU A 1 219 ? 7.668   10.239  2.421  1.00 37.57  ? 216 LEU A HB2  1 
ATOM   3563 H  HB3  . LEU A 1 219 ? 6.772   11.239  1.571  1.00 37.57  ? 216 LEU A HB3  1 
ATOM   3564 H  HG   . LEU A 1 219 ? 6.027   8.611   2.301  1.00 47.47  ? 216 LEU A HG   1 
ATOM   3565 H  HD11 . LEU A 1 219 ? 4.333   9.688   3.585  1.00 48.94  ? 216 LEU A HD11 1 
ATOM   3566 H  HD12 . LEU A 1 219 ? 5.771   10.156  4.073  1.00 48.94  ? 216 LEU A HD12 1 
ATOM   3567 H  HD13 . LEU A 1 219 ? 4.905   11.100  3.134  1.00 48.94  ? 216 LEU A HD13 1 
ATOM   3568 H  HD21 . LEU A 1 219 ? 3.962   9.000   1.282  1.00 52.66  ? 216 LEU A HD21 1 
ATOM   3569 H  HD22 . LEU A 1 219 ? 4.561   10.326  0.645  1.00 52.66  ? 216 LEU A HD22 1 
ATOM   3570 H  HD23 . LEU A 1 219 ? 5.154   8.910   0.235  1.00 52.66  ? 216 LEU A HD23 1 
ATOM   3571 N  N    . LYS A 1 220 ? 9.086   11.162  -1.057 1.00 37.00  ? 217 LYS A N    1 
ATOM   3572 C  CA   . LYS A 1 220 ? 10.378  11.616  -1.564 1.00 44.16  ? 217 LYS A CA   1 
ATOM   3573 C  C    . LYS A 1 220 ? 10.997  12.695  -0.698 1.00 42.88  ? 217 LYS A C    1 
ATOM   3574 O  O    . LYS A 1 220 ? 12.226  12.773  -0.610 1.00 44.23  ? 217 LYS A O    1 
ATOM   3575 C  CB   . LYS A 1 220 ? 10.215  12.086  -3.012 1.00 46.42  ? 217 LYS A CB   1 
ATOM   3576 C  CG   . LYS A 1 220 ? 9.132   13.141  -3.213 1.00 50.81  ? 217 LYS A CG   1 
ATOM   3577 C  CD   . LYS A 1 220 ? 9.245   13.796  -4.596 1.00 63.15  ? 217 LYS A CD   1 
ATOM   3578 C  CE   . LYS A 1 220 ? 8.910   15.284  -4.548 1.00 76.28  ? 217 LYS A CE   1 
ATOM   3579 N  NZ   . LYS A 1 220 ? 10.085  16.100  -4.118 1.00 85.86  ? 217 LYS A NZ   1 
ATOM   3580 H  H    . LYS A 1 220 ? 8.420   11.328  -1.575 1.00 44.43  ? 217 LYS A H    1 
ATOM   3581 H  HA   . LYS A 1 220 ? 11.000  10.872  -1.555 1.00 53.03  ? 217 LYS A HA   1 
ATOM   3582 H  HB2  . LYS A 1 220 ? 11.056  12.468  -3.310 1.00 55.74  ? 217 LYS A HB2  1 
ATOM   3583 H  HB3  . LYS A 1 220 ? 9.986   11.321  -3.562 1.00 55.74  ? 217 LYS A HB3  1 
ATOM   3584 H  HG2  . LYS A 1 220 ? 8.259   12.723  -3.142 1.00 61.00  ? 217 LYS A HG2  1 
ATOM   3585 H  HG3  . LYS A 1 220 ? 9.225   13.831  -2.539 1.00 61.00  ? 217 LYS A HG3  1 
ATOM   3586 H  HD2  . LYS A 1 220 ? 10.153  13.699  -4.923 1.00 75.82  ? 217 LYS A HD2  1 
ATOM   3587 H  HD3  . LYS A 1 220 ? 8.625   13.365  -5.206 1.00 75.82  ? 217 LYS A HD3  1 
ATOM   3588 H  HE2  . LYS A 1 220 ? 8.640   15.581  -5.431 1.00 91.58  ? 217 LYS A HE2  1 
ATOM   3589 H  HE3  . LYS A 1 220 ? 8.190   15.430  -3.915 1.00 91.58  ? 217 LYS A HE3  1 
ATOM   3590 H  HZ1  . LYS A 1 220 ? 9.857   16.958  -4.064 1.00 103.07 ? 217 LYS A HZ1  1 
ATOM   3591 H  HZ2  . LYS A 1 220 ? 10.370  15.826  -3.320 1.00 103.07 ? 217 LYS A HZ2  1 
ATOM   3592 H  HZ3  . LYS A 1 220 ? 10.747  16.013  -4.706 1.00 103.07 ? 217 LYS A HZ3  1 
ATOM   3593 N  N    . ASP A 1 221 ? 10.189  13.529  -0.039 1.00 38.76  ? 218 ASP A N    1 
ATOM   3594 C  CA   . ASP A 1 221 ? 10.734  14.660  0.697  1.00 43.17  ? 218 ASP A CA   1 
ATOM   3595 C  C    . ASP A 1 221 ? 10.923  14.386  2.180  1.00 40.56  ? 218 ASP A C    1 
ATOM   3596 O  O    . ASP A 1 221 ? 11.455  15.255  2.885  1.00 45.82  ? 218 ASP A O    1 
ATOM   3597 C  CB   . ASP A 1 221 ? 9.825   15.881  0.498  1.00 48.32  ? 218 ASP A CB   1 
ATOM   3598 C  CG   . ASP A 1 221 ? 9.969   16.484  -0.872 1.00 60.10  ? 218 ASP A CG   1 
ATOM   3599 O  OD1  . ASP A 1 221 ? 11.098  16.521  -1.410 1.00 56.48  ? 218 ASP A OD1  1 
ATOM   3600 O  OD2  . ASP A 1 221 ? 8.928   16.865  -1.427 1.00 72.90  ? 218 ASP A OD2  1 
ATOM   3601 H  H    . ASP A 1 221 ? 9.332   13.456  -0.007 1.00 46.54  ? 218 ASP A H    1 
ATOM   3602 H  HA   . ASP A 1 221 ? 11.610  14.871  0.340  1.00 51.84  ? 218 ASP A HA   1 
ATOM   3603 H  HB2  . ASP A 1 221 ? 8.900   15.611  0.613  1.00 58.02  ? 218 ASP A HB2  1 
ATOM   3604 H  HB3  . ASP A 1 221 ? 10.056  16.559  1.152  1.00 58.02  ? 218 ASP A HB3  1 
ATOM   3605 N  N    . SER A 1 222 ? 10.522  13.213  2.663  1.00 39.04  ? 219 SER A N    1 
ATOM   3606 C  CA   . SER A 1 222 ? 10.566  12.933  4.096  1.00 37.90  ? 219 SER A CA   1 
ATOM   3607 C  C    . SER A 1 222 ? 11.951  12.481  4.527  1.00 40.26  ? 219 SER A C    1 
ATOM   3608 O  O    . SER A 1 222 ? 12.642  11.776  3.789  1.00 38.46  ? 219 SER A O    1 
ATOM   3609 C  CB   . SER A 1 222 ? 9.534   11.878  4.451  1.00 33.13  ? 219 SER A CB   1 
ATOM   3610 O  OG   . SER A 1 222 ? 8.233   12.416  4.397  1.00 36.55  ? 219 SER A OG   1 
ATOM   3611 H  H    . SER A 1 222 ? 10.221  12.565  2.184  1.00 46.88  ? 219 SER A H    1 
ATOM   3612 H  HA   . SER A 1 222 ? 10.361  13.744  4.587  1.00 45.51  ? 219 SER A HA   1 
ATOM   3613 H  HB2  . SER A 1 222 ? 9.600   11.146  3.819  1.00 39.79  ? 219 SER A HB2  1 
ATOM   3614 H  HB3  . SER A 1 222 ? 9.707   11.557  5.350  1.00 39.79  ? 219 SER A HB3  1 
ATOM   3615 H  HG   . SER A 1 222 ? 7.670   11.825  4.593  1.00 43.89  ? 219 SER A HG   1 
ATOM   3616 N  N    . HIS A 1 223 ? 12.361  12.924  5.714  1.00 36.70  ? 220 HIS A N    1 
ATOM   3617 C  CA   . HIS A 1 223 ? 13.586  12.481  6.362  1.00 39.78  ? 220 HIS A CA   1 
ATOM   3618 C  C    . HIS A 1 223 ? 13.278  11.306  7.300  1.00 33.32  ? 220 HIS A C    1 
ATOM   3619 O  O    . HIS A 1 223 ? 12.157  10.817  7.367  1.00 37.71  ? 220 HIS A O    1 
ATOM   3620 C  CB   . HIS A 1 223 ? 14.217  13.653  7.109  1.00 45.47  ? 220 HIS A CB   1 
ATOM   3621 C  CG   . HIS A 1 223 ? 14.614  14.788  6.215  1.00 48.29  ? 220 HIS A CG   1 
ATOM   3622 N  ND1  . HIS A 1 223 ? 15.927  15.119  5.972  1.00 59.02  ? 220 HIS A ND1  1 
ATOM   3623 C  CD2  . HIS A 1 223 ? 13.866  15.664  5.501  1.00 53.42  ? 220 HIS A CD2  1 
ATOM   3624 C  CE1  . HIS A 1 223 ? 15.974  16.153  5.147  1.00 62.62  ? 220 HIS A CE1  1 
ATOM   3625 N  NE2  . HIS A 1 223 ? 14.735  16.502  4.845  1.00 59.82  ? 220 HIS A NE2  1 
ATOM   3626 H  H    . HIS A 1 223 ? 11.929  13.503  6.179  1.00 44.08  ? 220 HIS A H    1 
ATOM   3627 H  HA   . HIS A 1 223 ? 14.219  12.172  5.695  1.00 47.77  ? 220 HIS A HA   1 
ATOM   3628 H  HB2  . HIS A 1 223 ? 13.578  13.993  7.755  1.00 54.60  ? 220 HIS A HB2  1 
ATOM   3629 H  HB3  . HIS A 1 223 ? 15.015  13.341  7.565  1.00 54.60  ? 220 HIS A HB3  1 
ATOM   3630 H  HD2  . HIS A 1 223 ? 12.937  15.692  5.461  1.00 64.13  ? 220 HIS A HD2  1 
ATOM   3631 H  HE1  . HIS A 1 223 ? 16.746  16.564  4.832  1.00 75.18  ? 220 HIS A HE1  1 
ATOM   3632 H  HE2  . HIS A 1 223 ? 14.510  17.148  4.324  1.00 71.82  ? 220 HIS A HE2  1 
ATOM   3633 N  N    . HIS A 1 224 ? 14.290  10.851  8.039  1.00 34.41  ? 221 HIS A N    1 
ATOM   3634 C  CA   . HIS A 1 224 ? 14.119  9.678   8.896  1.00 33.55  ? 221 HIS A CA   1 
ATOM   3635 C  C    . HIS A 1 224 ? 12.959  9.857   9.877  1.00 30.87  ? 221 HIS A C    1 
ATOM   3636 O  O    . HIS A 1 224 ? 12.072  8.993   9.987  1.00 32.85  ? 221 HIS A O    1 
ATOM   3637 C  CB   . HIS A 1 224 ? 15.426  9.405   9.653  1.00 36.92  ? 221 HIS A CB   1 
ATOM   3638 C  CG   . HIS A 1 224 ? 15.347  8.224   10.569 1.00 35.98  ? 221 HIS A CG   1 
ATOM   3639 N  ND1  . HIS A 1 224 ? 15.237  6.931   10.102 1.00 35.81  ? 221 HIS A ND1  1 
ATOM   3640 C  CD2  . HIS A 1 224 ? 15.340  8.141   11.927 1.00 34.77  ? 221 HIS A CD2  1 
ATOM   3641 C  CE1  . HIS A 1 224 ? 15.158  6.102   11.130 1.00 36.95  ? 221 HIS A CE1  1 
ATOM   3642 N  NE2  . HIS A 1 224 ? 15.233  6.810   12.247 1.00 34.87  ? 221 HIS A NE2  1 
ATOM   3643 H  H    . HIS A 1 224 ? 15.076  11.198  8.063  1.00 41.33  ? 221 HIS A H    1 
ATOM   3644 H  HA   . HIS A 1 224 ? 13.914  8.911   8.339  1.00 40.29  ? 221 HIS A HA   1 
ATOM   3645 H  HB2  . HIS A 1 224 ? 16.132  9.236   9.009  1.00 44.34  ? 221 HIS A HB2  1 
ATOM   3646 H  HB3  . HIS A 1 224 ? 15.647  10.184  10.188 1.00 44.34  ? 221 HIS A HB3  1 
ATOM   3647 H  HD1  . HIS A 1 224 ? 15.221  6.701   9.273  1.00 43.00  ? 221 HIS A HD1  1 
ATOM   3648 H  HD2  . HIS A 1 224 ? 15.397  8.851   12.525 1.00 41.76  ? 221 HIS A HD2  1 
ATOM   3649 H  HE1  . HIS A 1 224 ? 15.066  5.178   11.078 1.00 44.37  ? 221 HIS A HE1  1 
ATOM   3650 N  N    . LEU A 1 225 ? 12.977  10.955  10.633 1.00 33.61  ? 222 LEU A N    1 
ATOM   3651 C  CA   . LEU A 1 225 ? 11.886  11.266  11.563 1.00 32.59  ? 222 LEU A CA   1 
ATOM   3652 C  C    . LEU A 1 225 ? 10.771  11.886  10.713 1.00 31.39  ? 222 LEU A C    1 
ATOM   3653 O  O    . LEU A 1 225 ? 10.628  13.112  10.614 1.00 33.66  ? 222 LEU A O    1 
ATOM   3654 C  CB   . LEU A 1 225 ? 12.379  12.184  12.673 1.00 35.74  ? 222 LEU A CB   1 
ATOM   3655 C  CG   . LEU A 1 225 ? 11.341  12.483  13.776 1.00 41.74  ? 222 LEU A CG   1 
ATOM   3656 C  CD1  . LEU A 1 225 ? 10.969  11.184  14.504 1.00 43.54  ? 222 LEU A CD1  1 
ATOM   3657 C  CD2  . LEU A 1 225 ? 11.816  13.566  14.777 1.00 50.62  ? 222 LEU A CD2  1 
ATOM   3658 H  H    . LEU A 1 225 ? 13.609  11.538  10.626 1.00 40.36  ? 222 LEU A H    1 
ATOM   3659 H  HA   . LEU A 1 225 ? 11.547  10.466  11.996 1.00 39.14  ? 222 LEU A HA   1 
ATOM   3660 H  HB2  . LEU A 1 225 ? 13.146  11.768  13.098 1.00 42.92  ? 222 LEU A HB2  1 
ATOM   3661 H  HB3  . LEU A 1 225 ? 12.638  13.031  12.278 1.00 42.92  ? 222 LEU A HB3  1 
ATOM   3662 H  HG   . LEU A 1 225 ? 10.549  12.849  13.351 1.00 50.12  ? 222 LEU A HG   1 
ATOM   3663 H  HD11 . LEU A 1 225 ? 10.333  11.387  15.207 1.00 52.29  ? 222 LEU A HD11 1 
ATOM   3664 H  HD12 . LEU A 1 225 ? 10.574  10.567  13.868 1.00 52.29  ? 222 LEU A HD12 1 
ATOM   3665 H  HD13 . LEU A 1 225 ? 11.772  10.795  14.887 1.00 52.29  ? 222 LEU A HD13 1 
ATOM   3666 H  HD21 . LEU A 1 225 ? 11.118  13.715  15.434 1.00 60.77  ? 222 LEU A HD21 1 
ATOM   3667 H  HD22 . LEU A 1 225 ? 12.624  13.258  15.216 1.00 60.77  ? 222 LEU A HD22 1 
ATOM   3668 H  HD23 . LEU A 1 225 ? 11.995  14.387  14.292 1.00 60.77  ? 222 LEU A HD23 1 
ATOM   3669 N  N    . MET A 1 226 ? 9.969   11.001  10.104 1.00 30.81  ? 223 MET A N    1 
ATOM   3670 C  CA   . MET A 1 226 ? 8.999   11.431  9.096  1.00 32.19  ? 223 MET A CA   1 
ATOM   3671 C  C    . MET A 1 226 ? 7.910   12.324  9.651  1.00 33.77  ? 223 MET A C    1 
ATOM   3672 O  O    . MET A 1 226 ? 7.269   13.062  8.896  1.00 34.56  ? 223 MET A O    1 
ATOM   3673 C  CB   . MET A 1 226 ? 8.334   10.244  8.382  1.00 33.93  ? 223 MET A CB   1 
ATOM   3674 C  CG   . MET A 1 226 ? 9.283   9.192   7.854  1.00 33.57  ? 223 MET A CG   1 
ATOM   3675 S  SD   . MET A 1 226 ? 8.381   7.918   6.953  1.00 31.37  ? 223 MET A SD   1 
ATOM   3676 C  CE   . MET A 1 226 ? 7.895   8.765   5.462  1.00 29.59  ? 223 MET A CE   1 
ATOM   3677 H  H    . MET A 1 226 ? 9.969   10.154  10.257 1.00 37.01  ? 223 MET A H    1 
ATOM   3678 H  HA   . MET A 1 226 ? 9.515   11.920  8.436  1.00 38.66  ? 223 MET A HA   1 
ATOM   3679 H  HB2  . MET A 1 226 ? 7.736   9.807   9.008  1.00 40.75  ? 223 MET A HB2  1 
ATOM   3680 H  HB3  . MET A 1 226 ? 7.831   10.585  7.625  1.00 40.75  ? 223 MET A HB3  1 
ATOM   3681 H  HG2  . MET A 1 226 ? 9.921   9.604   7.251  1.00 40.32  ? 223 MET A HG2  1 
ATOM   3682 H  HG3  . MET A 1 226 ? 9.748   8.774   8.596  1.00 40.32  ? 223 MET A HG3  1 
ATOM   3683 H  HE1  . MET A 1 226 ? 7.408   8.148   4.893  1.00 35.55  ? 223 MET A HE1  1 
ATOM   3684 H  HE2  . MET A 1 226 ? 7.328   9.516   5.696  1.00 35.55  ? 223 MET A HE2  1 
ATOM   3685 H  HE3  . MET A 1 226 ? 8.690   9.081   5.004  1.00 35.55  ? 223 MET A HE3  1 
ATOM   3686 N  N    . THR A 1 227 ? 7.713   12.308  10.967 1.00 29.98  ? 224 THR A N    1 
ATOM   3687 C  CA   . THR A 1 227 ? 6.688   13.146  11.585 1.00 30.82  ? 224 THR A CA   1 
ATOM   3688 C  C    . THR A 1 227 ? 7.107   14.603  11.704 1.00 34.24  ? 224 THR A C    1 
ATOM   3689 O  O    . THR A 1 227 ? 6.278   15.459  12.075 1.00 37.62  ? 224 THR A O    1 
ATOM   3690 C  CB   . THR A 1 227 ? 6.380   12.601  12.983 1.00 34.10  ? 224 THR A CB   1 
ATOM   3691 O  OG1  . THR A 1 227 ? 7.628   12.338  13.624 1.00 34.40  ? 224 THR A OG1  1 
ATOM   3692 C  CG2  . THR A 1 227 ? 5.624   11.318  12.890 1.00 34.10  ? 224 THR A CG2  1 
ATOM   3693 H  H    . THR A 1 227 ? 8.157   11.823  11.521 1.00 36.01  ? 224 THR A H    1 
ATOM   3694 H  HA   . THR A 1 227 ? 5.882   13.113  11.047 1.00 37.02  ? 224 THR A HA   1 
ATOM   3695 H  HB   . THR A 1 227 ? 5.846   13.236  13.485 1.00 40.95  ? 224 THR A HB   1 
ATOM   3696 H  HG1  . THR A 1 227 ? 7.497   12.075  14.411 1.00 41.31  ? 224 THR A HG1  1 
ATOM   3697 H  HG21 . THR A 1 227 ? 5.429   10.983  13.779 1.00 40.95  ? 224 THR A HG21 1 
ATOM   3698 H  HG22 . THR A 1 227 ? 4.790   11.458  12.416 1.00 40.95  ? 224 THR A HG22 1 
ATOM   3699 H  HG23 . THR A 1 227 ? 6.150   10.657  12.413 1.00 40.95  ? 224 THR A HG23 1 
ATOM   3700 N  N    . HIS A 1 228 ? 8.373   14.925  11.422 1.00 36.30  ? 225 HIS A N    1 
ATOM   3701 C  CA   . HIS A 1 228 ? 8.907   16.254  11.623 1.00 39.45  ? 225 HIS A CA   1 
ATOM   3702 C  C    . HIS A 1 228 ? 9.538   16.779  10.342 1.00 38.12  ? 225 HIS A C    1 
ATOM   3703 O  O    . HIS A 1 228 ? 10.077  16.012  9.537  1.00 39.84  ? 225 HIS A O    1 
ATOM   3704 C  CB   . HIS A 1 228 ? 9.968   16.277  12.727 1.00 39.98  ? 225 HIS A CB   1 
ATOM   3705 C  CG   . HIS A 1 228 ? 9.397   16.241  14.108 1.00 67.58  ? 225 HIS A CG   1 
ATOM   3706 N  ND1  . HIS A 1 228 ? 9.985   16.895  15.171 1.00 82.80  ? 225 HIS A ND1  1 
ATOM   3707 C  CD2  . HIS A 1 228 ? 8.287   15.638  14.601 1.00 63.87  ? 225 HIS A CD2  1 
ATOM   3708 C  CE1  . HIS A 1 228 ? 9.259   16.701  16.258 1.00 72.90  ? 225 HIS A CE1  1 
ATOM   3709 N  NE2  . HIS A 1 228 ? 8.220   15.948  15.939 1.00 67.89  ? 225 HIS A NE2  1 
ATOM   3710 H  H    . HIS A 1 228 ? 8.948   14.369  11.106 1.00 43.59  ? 225 HIS A H    1 
ATOM   3711 H  HA   . HIS A 1 228 ? 8.175   16.839  11.872 1.00 47.37  ? 225 HIS A HA   1 
ATOM   3712 H  HB2  . HIS A 1 228 ? 10.543  15.503  12.624 1.00 48.01  ? 225 HIS A HB2  1 
ATOM   3713 H  HB3  . HIS A 1 228 ? 10.488  17.091  12.643 1.00 48.01  ? 225 HIS A HB3  1 
ATOM   3714 H  HD2  . HIS A 1 228 ? 7.685   15.113  14.125 1.00 76.68  ? 225 HIS A HD2  1 
ATOM   3715 H  HE1  . HIS A 1 228 ? 9.448   17.036  17.105 1.00 87.51  ? 225 HIS A HE1  1 
ATOM   3716 H  HE2  . HIS A 1 228 ? 7.602   15.694  16.481 1.00 81.51  ? 225 HIS A HE2  1 
ATOM   3717 N  N    . GLY A 1 229 ? 9.436   18.092  10.176 1.00 40.49  ? 226 GLY A N    1 
ATOM   3718 C  CA   . GLY A 1 229 ? 10.200  18.790  9.164  1.00 45.95  ? 226 GLY A CA   1 
ATOM   3719 C  C    . GLY A 1 229 ? 9.601   18.682  7.772  1.00 45.36  ? 226 GLY A C    1 
ATOM   3720 O  O    . GLY A 1 229 ? 8.404   18.494  7.580  1.00 45.37  ? 226 GLY A O    1 
ATOM   3721 H  H    . GLY A 1 229 ? 8.926   18.603  10.643 1.00 48.41  ? 226 GLY A H    1 
ATOM   3722 H  HA2  . GLY A 1 229 ? 10.251  19.730  9.397  1.00 55.18  ? 226 GLY A HA2  1 
ATOM   3723 H  HA3  . GLY A 1 229 ? 11.098  18.423  9.135  1.00 55.18  ? 226 GLY A HA3  1 
ATOM   3724 N  N    . GLU A 1 230 ? 10.483  18.805  6.788  1.00 55.30  ? 227 GLU A N    1 
ATOM   3725 C  CA   . GLU A 1 230 ? 10.105  18.759  5.386  1.00 51.46  ? 227 GLU A CA   1 
ATOM   3726 C  C    . GLU A 1 230 ? 9.209   17.574  5.080  1.00 45.13  ? 227 GLU A C    1 
ATOM   3727 O  O    . GLU A 1 230 ? 9.453   16.449  5.533  1.00 43.78  ? 227 GLU A O    1 
ATOM   3728 C  CB   . GLU A 1 230 ? 11.382  18.688  4.545  1.00 62.51  ? 227 GLU A CB   1 
ATOM   3729 C  CG   . GLU A 1 230 ? 11.180  18.948  3.094  1.00 75.34  ? 227 GLU A CG   1 
ATOM   3730 C  CD   . GLU A 1 230 ? 12.490  18.948  2.327  1.00 82.06  ? 227 GLU A CD   1 
ATOM   3731 O  OE1  . GLU A 1 230 ? 12.472  19.373  1.152  1.00 78.62  ? 227 GLU A OE1  1 
ATOM   3732 O  OE2  . GLU A 1 230 ? 13.525  18.517  2.894  1.00 70.90  ? 227 GLU A OE2  1 
ATOM   3733 H  H    . GLU A 1 230 ? 11.326  18.920  6.909  1.00 66.40  ? 227 GLU A H    1 
ATOM   3734 H  HA   . GLU A 1 230 ? 9.605   19.558  5.159  1.00 61.79  ? 227 GLU A HA   1 
ATOM   3735 H  HB2  . GLU A 1 230 ? 12.008  19.351  4.877  1.00 75.05  ? 227 GLU A HB2  1 
ATOM   3736 H  HB3  . GLU A 1 230 ? 11.762  17.800  4.634  1.00 75.05  ? 227 GLU A HB3  1 
ATOM   3737 H  HG2  . GLU A 1 230 ? 10.612  18.255  2.722  1.00 90.45  ? 227 GLU A HG2  1 
ATOM   3738 H  HG3  . GLU A 1 230 ? 10.763  19.816  2.981  1.00 90.45  ? 227 GLU A HG3  1 
ATOM   3739 N  N    . GLY A 1 231 ? 8.136   17.838  4.341  1.00 40.85  ? 228 GLY A N    1 
ATOM   3740 C  CA   . GLY A 1 231 ? 7.271   16.759  3.903  1.00 42.46  ? 228 GLY A CA   1 
ATOM   3741 C  C    . GLY A 1 231 ? 6.222   16.301  4.884  1.00 36.37  ? 228 GLY A C    1 
ATOM   3742 O  O    . GLY A 1 231 ? 5.463   15.361  4.569  1.00 37.34  ? 228 GLY A O    1 
ATOM   3743 H  H    . GLY A 1 231 ? 7.894   18.624  4.087  1.00 49.06  ? 228 GLY A H    1 
ATOM   3744 H  HA2  . GLY A 1 231 ? 6.810   17.045  3.099  1.00 50.99  ? 228 GLY A HA2  1 
ATOM   3745 H  HA3  . GLY A 1 231 ? 7.826   15.991  3.693  1.00 50.99  ? 228 GLY A HA3  1 
ATOM   3746 N  N    . ARG A 1 232 ? 6.170   16.887  6.080  1.00 38.08  ? 229 ARG A N    1 
ATOM   3747 C  CA   . ARG A 1 232 ? 5.324   16.348  7.126  1.00 35.91  ? 229 ARG A CA   1 
ATOM   3748 C  C    . ARG A 1 232 ? 3.856   16.386  6.731  1.00 33.35  ? 229 ARG A C    1 
ATOM   3749 O  O    . ARG A 1 232 ? 3.079   15.518  7.152  1.00 33.71  ? 229 ARG A O    1 
ATOM   3750 C  CB   . ARG A 1 232 ? 5.524   17.136  8.420  1.00 39.28  ? 229 ARG A CB   1 
ATOM   3751 C  CG   . ARG A 1 232 ? 4.338   17.042  9.359  1.00 42.17  ? 229 ARG A CG   1 
ATOM   3752 C  CD   . ARG A 1 232 ? 4.641   17.859  10.581 1.00 51.24  ? 229 ARG A CD   1 
ATOM   3753 N  NE   . ARG A 1 232 ? 3.865   19.082  10.513 1.00 43.47  ? 229 ARG A NE   1 
ATOM   3754 C  CZ   . ARG A 1 232 ? 3.932   20.063  11.407 1.00 51.57  ? 229 ARG A CZ   1 
ATOM   3755 N  NH1  . ARG A 1 232 ? 4.613   19.928  12.529 1.00 55.71  ? 229 ARG A NH1  1 
ATOM   3756 N  NH2  . ARG A 1 232 ? 3.330   21.217  11.150 1.00 61.17  ? 229 ARG A NH2  1 
ATOM   3757 H  H    . ARG A 1 232 ? 6.612   17.590  6.304  1.00 45.73  ? 229 ARG A H    1 
ATOM   3758 H  HA   . ARG A 1 232 ? 5.579   15.424  7.277  1.00 43.13  ? 229 ARG A HA   1 
ATOM   3759 H  HB2  . ARG A 1 232 ? 6.302   16.788  8.884  1.00 47.17  ? 229 ARG A HB2  1 
ATOM   3760 H  HB3  . ARG A 1 232 ? 5.660   18.071  8.201  1.00 47.17  ? 229 ARG A HB3  1 
ATOM   3761 H  HG2  . ARG A 1 232 ? 3.543   17.395  8.929  1.00 50.64  ? 229 ARG A HG2  1 
ATOM   3762 H  HG3  . ARG A 1 232 ? 4.192   16.119  9.621  1.00 50.64  ? 229 ARG A HG3  1 
ATOM   3763 H  HD2  . ARG A 1 232 ? 4.393   17.368  11.380 1.00 61.52  ? 229 ARG A HD2  1 
ATOM   3764 H  HD3  . ARG A 1 232 ? 5.585   18.081  10.608 1.00 61.52  ? 229 ARG A HD3  1 
ATOM   3765 H  HE   . ARG A 1 232 ? 3.326   19.180  9.851  1.00 52.20  ? 229 ARG A HE   1 
ATOM   3766 H  HH11 . ARG A 1 232 ? 5.026   19.192  12.695 1.00 66.89  ? 229 ARG A HH11 1 
ATOM   3767 H  HH12 . ARG A 1 232 ? 4.643   20.575  13.094 1.00 66.89  ? 229 ARG A HH12 1 
ATOM   3768 H  HH21 . ARG A 1 232 ? 2.902   21.324  10.412 1.00 73.44  ? 229 ARG A HH21 1 
ATOM   3769 H  HH22 . ARG A 1 232 ? 3.367   21.858  11.722 1.00 73.44  ? 229 ARG A HH22 1 
ATOM   3770 N  N    . ASP A 1 233 ? 3.441   17.426  5.991  1.00 37.58  ? 230 ASP A N    1 
ATOM   3771 C  CA   . ASP A 1 233 ? 2.040   17.528  5.598  1.00 36.49  ? 230 ASP A CA   1 
ATOM   3772 C  C    . ASP A 1 233 ? 1.640   16.341  4.731  1.00 34.73  ? 230 ASP A C    1 
ATOM   3773 O  O    . ASP A 1 233 ? 0.540   15.796  4.872  1.00 37.05  ? 230 ASP A O    1 
ATOM   3774 C  CB   . ASP A 1 233 ? 1.804   18.848  4.865  1.00 43.61  ? 230 ASP A CB   1 
ATOM   3775 C  CG   . ASP A 1 233 ? 1.707   20.026  5.821  1.00 74.81  ? 230 ASP A CG   1 
ATOM   3776 O  OD1  . ASP A 1 233 ? 1.671   21.177  5.345  1.00 83.88  ? 230 ASP A OD1  1 
ATOM   3777 O  OD2  . ASP A 1 233 ? 1.664   19.796  7.055  1.00 83.26  ? 230 ASP A OD2  1 
ATOM   3778 H  H    . ASP A 1 233 ? 3.942   18.067  5.713  1.00 45.13  ? 230 ASP A H    1 
ATOM   3779 H  HA   . ASP A 1 233 ? 1.478   17.526  6.388  1.00 43.82  ? 230 ASP A HA   1 
ATOM   3780 H  HB2  . ASP A 1 233 ? 2.542   19.012  4.257  1.00 52.37  ? 230 ASP A HB2  1 
ATOM   3781 H  HB3  . ASP A 1 233 ? 0.972   18.792  4.368  1.00 52.37  ? 230 ASP A HB3  1 
ATOM   3782 N  N    . ILE A 1 234 ? 2.518   15.937  3.816  1.00 34.61  ? 231 ILE A N    1 
ATOM   3783 C  CA   . ILE A 1 234 ? 2.241   14.775  2.969  1.00 34.41  ? 231 ILE A CA   1 
ATOM   3784 C  C    . ILE A 1 234 ? 2.166   13.490  3.797  1.00 31.62  ? 231 ILE A C    1 
ATOM   3785 O  O    . ILE A 1 234 ? 1.282   12.645  3.598  1.00 31.44  ? 231 ILE A O    1 
ATOM   3786 C  CB   . ILE A 1 234 ? 3.310   14.679  1.853  1.00 35.96  ? 231 ILE A CB   1 
ATOM   3787 C  CG1  . ILE A 1 234 ? 3.376   15.975  1.068  1.00 51.46  ? 231 ILE A CG1  1 
ATOM   3788 C  CG2  . ILE A 1 234 ? 3.038   13.441  1.007  1.00 38.17  ? 231 ILE A CG2  1 
ATOM   3789 C  CD1  . ILE A 1 234 ? 2.102   16.349  0.409  1.00 63.26  ? 231 ILE A CD1  1 
ATOM   3790 H  H    . ILE A 1 234 ? 3.276   16.313  3.666  1.00 41.57  ? 231 ILE A H    1 
ATOM   3791 H  HA   . ILE A 1 234 ? 1.372   14.895  2.554  1.00 41.33  ? 231 ILE A HA   1 
ATOM   3792 H  HB   . ILE A 1 234 ? 4.195   14.569  2.234  1.00 43.19  ? 231 ILE A HB   1 
ATOM   3793 H  HG12 . ILE A 1 234 ? 3.616   16.693  1.675  1.00 61.79  ? 231 ILE A HG12 1 
ATOM   3794 H  HG13 . ILE A 1 234 ? 4.050   15.885  0.377  1.00 61.79  ? 231 ILE A HG13 1 
ATOM   3795 H  HG21 . ILE A 1 234 ? 3.706   13.385  0.306  1.00 45.83  ? 231 ILE A HG21 1 
ATOM   3796 H  HG22 . ILE A 1 234 ? 3.085   12.655  1.573  1.00 45.83  ? 231 ILE A HG22 1 
ATOM   3797 H  HG23 . ILE A 1 234 ? 2.154   13.514  0.615  1.00 45.83  ? 231 ILE A HG23 1 
ATOM   3798 H  HD11 . ILE A 1 234 ? 2.231   17.177  -0.081 1.00 75.95  ? 231 ILE A HD11 1 
ATOM   3799 H  HD12 . ILE A 1 234 ? 1.842   15.641  -0.201 1.00 75.95  ? 231 ILE A HD12 1 
ATOM   3800 H  HD13 . ILE A 1 234 ? 1.419   16.469  1.087  1.00 75.95  ? 231 ILE A HD13 1 
ATOM   3801 N  N    . LEU A 1 235 ? 3.115   13.305  4.713  1.00 31.78  ? 232 LEU A N    1 
ATOM   3802 C  CA   . LEU A 1 235 ? 3.069   12.152  5.614  1.00 29.02  ? 232 LEU A CA   1 
ATOM   3803 C  C    . LEU A 1 235 ? 1.758   12.101  6.399  1.00 28.58  ? 232 LEU A C    1 
ATOM   3804 O  O    . LEU A 1 235 ? 1.093   11.058  6.450  1.00 28.24  ? 232 LEU A O    1 
ATOM   3805 C  CB   . LEU A 1 235 ? 4.278   12.217  6.548  1.00 31.02  ? 232 LEU A CB   1 
ATOM   3806 C  CG   . LEU A 1 235 ? 4.489   11.161  7.633  1.00 31.14  ? 232 LEU A CG   1 
ATOM   3807 C  CD1  . LEU A 1 235 ? 3.648   11.422  8.834  1.00 29.43  ? 232 LEU A CD1  1 
ATOM   3808 C  CD2  . LEU A 1 235 ? 4.259   9.756   7.088  1.00 29.14  ? 232 LEU A CD2  1 
ATOM   3809 H  H    . LEU A 1 235 ? 3.789   13.825  4.835  1.00 38.17  ? 232 LEU A H    1 
ATOM   3810 H  HA   . LEU A 1 235 ? 3.115   11.332  5.098  1.00 34.86  ? 232 LEU A HA   1 
ATOM   3811 H  HB2  . LEU A 1 235 ? 5.069   12.186  5.988  1.00 37.26  ? 232 LEU A HB2  1 
ATOM   3812 H  HB3  . LEU A 1 235 ? 4.232   13.068  7.011  1.00 37.26  ? 232 LEU A HB3  1 
ATOM   3813 H  HG   . LEU A 1 235 ? 5.413   11.213  7.922  1.00 37.40  ? 232 LEU A HG   1 
ATOM   3814 H  HD11 . LEU A 1 235 ? 4.020   10.942  9.590  1.00 35.35  ? 232 LEU A HD11 1 
ATOM   3815 H  HD12 . LEU A 1 235 ? 3.645   12.375  9.016  1.00 35.35  ? 232 LEU A HD12 1 
ATOM   3816 H  HD13 . LEU A 1 235 ? 2.744   11.116  8.659  1.00 35.35  ? 232 LEU A HD13 1 
ATOM   3817 H  HD21 . LEU A 1 235 ? 4.453   9.111   7.786  1.00 35.01  ? 232 LEU A HD21 1 
ATOM   3818 H  HD22 . LEU A 1 235 ? 3.333   9.674   6.810  1.00 35.01  ? 232 LEU A HD22 1 
ATOM   3819 H  HD23 . LEU A 1 235 ? 4.847   9.611   6.331  1.00 35.01  ? 232 LEU A HD23 1 
ATOM   3820 N  N    . GLU A 1 236 ? 1.358   13.221  7.011  1.00 26.41  ? 233 GLU A N    1 
ATOM   3821 C  CA   . GLU A 1 236 ? 0.140   13.223  7.815  1.00 28.18  ? 233 GLU A CA   1 
ATOM   3822 C  C    . GLU A 1 236 ? -1.102  12.921  6.979  1.00 32.71  ? 233 GLU A C    1 
ATOM   3823 O  O    . GLU A 1 236 ? -1.964  12.150  7.416  1.00 32.61  ? 233 GLU A O    1 
ATOM   3824 C  CB   . GLU A 1 236 ? -0.003  14.557  8.549  1.00 31.08  ? 233 GLU A CB   1 
ATOM   3825 C  CG   . GLU A 1 236 ? 1.054   14.690  9.661  1.00 30.91  ? 233 GLU A CG   1 
ATOM   3826 C  CD   . GLU A 1 236 ? 0.922   15.928  10.498 1.00 37.65  ? 233 GLU A CD   1 
ATOM   3827 O  OE1  . GLU A 1 236 ? 0.175   16.858  10.124 1.00 36.01  ? 233 GLU A OE1  1 
ATOM   3828 O  OE2  . GLU A 1 236 ? 1.599   15.983  11.544 1.00 34.48  ? 233 GLU A OE2  1 
ATOM   3829 H  H    . GLU A 1 236 ? 1.768   13.977  6.976  1.00 31.73  ? 233 GLU A H    1 
ATOM   3830 H  HA   . GLU A 1 236 ? 0.214   12.521  8.481  1.00 33.85  ? 233 GLU A HA   1 
ATOM   3831 H  HB2  . GLU A 1 236 ? 0.118   15.285  7.920  1.00 37.33  ? 233 GLU A HB2  1 
ATOM   3832 H  HB3  . GLU A 1 236 ? -0.883  14.610  8.952  1.00 37.33  ? 233 GLU A HB3  1 
ATOM   3833 H  HG2  . GLU A 1 236 ? 0.978   13.926  10.254 1.00 37.13  ? 233 GLU A HG2  1 
ATOM   3834 H  HG3  . GLU A 1 236 ? 1.934   14.705  9.252  1.00 37.13  ? 233 GLU A HG3  1 
ATOM   3835 N  N    . GLU A 1 237 ? -1.224  13.517  5.790  1.00 29.60  ? 234 GLU A N    1 
ATOM   3836 C  CA   . GLU A 1 237 ? -2.382  13.220  4.941  1.00 30.58  ? 234 GLU A CA   1 
ATOM   3837 C  C    . GLU A 1 237 ? -2.443  11.729  4.650  1.00 30.52  ? 234 GLU A C    1 
ATOM   3838 O  O    . GLU A 1 237 ? -3.520  11.124  4.644  1.00 34.13  ? 234 GLU A O    1 
ATOM   3839 C  CB   . GLU A 1 237 ? -2.312  14.032  3.636  1.00 34.84  ? 234 GLU A CB   1 
ATOM   3840 C  CG   . GLU A 1 237 ? -3.277  13.559  2.577  1.00 46.66  ? 234 GLU A CG   1 
ATOM   3841 C  CD   . GLU A 1 237 ? -3.214  14.413  1.305  1.00 79.15  ? 234 GLU A CD   1 
ATOM   3842 O  OE1  . GLU A 1 237 ? -3.453  13.872  0.206  1.00 83.89  ? 234 GLU A OE1  1 
ATOM   3843 O  OE2  . GLU A 1 237 ? -2.938  15.630  1.413  1.00 76.00  ? 234 GLU A OE2  1 
ATOM   3844 H  H    . GLU A 1 237 ? -0.667  14.082  5.459  1.00 35.55  ? 234 GLU A H    1 
ATOM   3845 H  HA   . GLU A 1 237 ? -3.196  13.483  5.399  1.00 36.53  ? 234 GLU A HA   1 
ATOM   3846 H  HB2  . GLU A 1 237 ? -2.520  14.959  3.834  1.00 41.85  ? 234 GLU A HB2  1 
ATOM   3847 H  HB3  . GLU A 1 237 ? -1.416  13.963  3.273  1.00 41.85  ? 234 GLU A HB3  1 
ATOM   3848 H  HG2  . GLU A 1 237 ? -3.061  12.645  2.337  1.00 56.03  ? 234 GLU A HG2  1 
ATOM   3849 H  HG3  . GLU A 1 237 ? -4.180  13.607  2.927  1.00 56.03  ? 234 GLU A HG3  1 
ATOM   3850 N  N    . ASN A 1 238 ? -1.285  11.117  4.410  1.00 29.81  ? 235 ASN A N    1 
ATOM   3851 C  CA   . ASN A 1 238 ? -1.252  9.699   4.065  1.00 30.92  ? 235 ASN A CA   1 
ATOM   3852 C  C    . ASN A 1 238 ? -1.708  8.830   5.227  1.00 27.78  ? 235 ASN A C    1 
ATOM   3853 O  O    . ASN A 1 238 ? -2.547  7.944   5.057  1.00 28.12  ? 235 ASN A O    1 
ATOM   3854 C  CB   . ASN A 1 238 ? 0.147   9.332   3.617  1.00 29.85  ? 235 ASN A CB   1 
ATOM   3855 C  CG   . ASN A 1 238 ? 0.230   7.916   3.078  1.00 35.15  ? 235 ASN A CG   1 
ATOM   3856 O  OD1  . ASN A 1 238 ? 0.028   6.976   3.820  1.00 36.96  ? 235 ASN A OD1  1 
ATOM   3857 N  ND2  . ASN A 1 238 ? 0.443   7.776   1.776  1.00 35.68  ? 235 ASN A ND2  1 
ATOM   3858 H  H    . ASN A 1 238 ? -0.514  11.495  4.441  1.00 35.81  ? 235 ASN A H    1 
ATOM   3859 H  HA   . ASN A 1 238 ? -1.862  9.532   3.330  1.00 37.14  ? 235 ASN A HA   1 
ATOM   3860 H  HB2  . ASN A 1 238 ? 0.425   9.939   2.913  1.00 35.86  ? 235 ASN A HB2  1 
ATOM   3861 H  HB3  . ASN A 1 238 ? 0.751   9.403   4.372  1.00 35.86  ? 235 ASN A HB3  1 
ATOM   3862 H  HD21 . ASN A 1 238 ? 0.528   8.472   1.277  1.00 42.85  ? 235 ASN A HD21 1 
ATOM   3863 H  HD22 . ASN A 1 238 ? 0.497   6.990   1.431  1.00 42.85  ? 235 ASN A HD22 1 
ATOM   3864 N  N    . VAL A 1 239 ? -1.173  9.090   6.419  1.00 25.99  ? 236 VAL A N    1 
ATOM   3865 C  CA   . VAL A 1 239 ? -1.499  8.301   7.599  1.00 23.60  ? 236 VAL A CA   1 
ATOM   3866 C  C    . VAL A 1 239 ? -2.950  8.518   8.001  1.00 27.58  ? 236 VAL A C    1 
ATOM   3867 O  O    . VAL A 1 239 ? -3.654  7.574   8.370  1.00 27.09  ? 236 VAL A O    1 
ATOM   3868 C  CB   . VAL A 1 239 ? -0.537  8.661   8.738  1.00 26.75  ? 236 VAL A CB   1 
ATOM   3869 C  CG1  . VAL A 1 239 ? -1.049  8.057   10.087 1.00 29.82  ? 236 VAL A CG1  1 
ATOM   3870 C  CG2  . VAL A 1 239 ? 0.836   8.197   8.418  1.00 28.85  ? 236 VAL A CG2  1 
ATOM   3871 H  H    . VAL A 1 239 ? -0.614  9.725   6.571  1.00 31.22  ? 236 VAL A H    1 
ATOM   3872 H  HA   . VAL A 1 239 ? -1.390  7.360   7.389  1.00 28.36  ? 236 VAL A HA   1 
ATOM   3873 H  HB   . VAL A 1 239 ? -0.503  9.625   8.842  1.00 32.13  ? 236 VAL A HB   1 
ATOM   3874 H  HG11 . VAL A 1 239 ? -0.336  8.098   10.743 1.00 35.82  ? 236 VAL A HG11 1 
ATOM   3875 H  HG12 . VAL A 1 239 ? -1.811  8.572   10.395 1.00 35.82  ? 236 VAL A HG12 1 
ATOM   3876 H  HG13 . VAL A 1 239 ? -1.311  7.134   9.941  1.00 35.82  ? 236 VAL A HG13 1 
ATOM   3877 H  HG21 . VAL A 1 239 ? 1.434   8.461   9.135  1.00 34.65  ? 236 VAL A HG21 1 
ATOM   3878 H  HG22 . VAL A 1 239 ? 0.831   7.231   8.331  1.00 34.65  ? 236 VAL A HG22 1 
ATOM   3879 H  HG23 . VAL A 1 239 ? 1.120   8.603   7.584  1.00 34.65  ? 236 VAL A HG23 1 
ATOM   3880 N  N    . ILE A 1 240 ? -3.430  9.752   7.914  1.00 28.73  ? 237 ILE A N    1 
ATOM   3881 C  CA   . ILE A 1 240 ? -4.813  10.033  8.292  1.00 25.70  ? 237 ILE A CA   1 
ATOM   3882 C  C    . ILE A 1 240 ? -5.782  9.359   7.336  1.00 30.71  ? 237 ILE A C    1 
ATOM   3883 O  O    . ILE A 1 240 ? -6.785  8.774   7.756  1.00 29.73  ? 237 ILE A O    1 
ATOM   3884 C  CB   . ILE A 1 240 ? -5.018  11.554  8.354  1.00 30.60  ? 237 ILE A CB   1 
ATOM   3885 C  CG1  . ILE A 1 240 ? -4.329  12.137  9.588  1.00 32.33  ? 237 ILE A CG1  1 
ATOM   3886 C  CG2  . ILE A 1 240 ? -6.498  11.885  8.307  1.00 36.01  ? 237 ILE A CG2  1 
ATOM   3887 C  CD1  . ILE A 1 240 ? -4.309  13.640  9.565  1.00 41.48  ? 237 ILE A CD1  1 
ATOM   3888 H  H    . ILE A 1 240 ? -2.985  10.436  7.644  1.00 34.52  ? 237 ILE A H    1 
ATOM   3889 H  HA   . ILE A 1 240 ? -4.986  9.665   9.172  1.00 30.87  ? 237 ILE A HA   1 
ATOM   3890 H  HB   . ILE A 1 240 ? -4.605  11.964  7.578  1.00 36.76  ? 237 ILE A HB   1 
ATOM   3891 H  HG12 . ILE A 1 240 ? -4.805  11.852  10.384 1.00 38.83  ? 237 ILE A HG12 1 
ATOM   3892 H  HG13 . ILE A 1 240 ? -3.412  11.821  9.619  1.00 38.83  ? 237 ILE A HG13 1 
ATOM   3893 H  HG21 . ILE A 1 240 ? -6.625  12.804  8.589  1.00 43.24  ? 237 ILE A HG21 1 
ATOM   3894 H  HG22 . ILE A 1 240 ? -6.819  11.769  7.399  1.00 43.24  ? 237 ILE A HG22 1 
ATOM   3895 H  HG23 . ILE A 1 240 ? -6.974  11.287  8.905  1.00 43.24  ? 237 ILE A HG23 1 
ATOM   3896 H  HD11 . ILE A 1 240 ? -3.629  13.956  10.180 1.00 49.82  ? 237 ILE A HD11 1 
ATOM   3897 H  HD12 . ILE A 1 240 ? -4.106  13.939  8.665  1.00 49.82  ? 237 ILE A HD12 1 
ATOM   3898 H  HD13 . ILE A 1 240 ? -5.179  13.972  9.835  1.00 49.82  ? 237 ILE A HD13 1 
ATOM   3899 N  N    . ARG A 1 241 ? -5.506  9.436   6.038  1.00 28.13  ? 238 ARG A N    1 
ATOM   3900 C  CA   . ARG A 1 241 ? -6.326  8.728   5.056  1.00 30.69  ? 238 ARG A CA   1 
ATOM   3901 C  C    . ARG A 1 241 ? -6.375  7.234   5.359  1.00 28.09  ? 238 ARG A C    1 
ATOM   3902 O  O    . ARG A 1 241 ? -7.434  6.593   5.255  1.00 31.54  ? 238 ARG A O    1 
ATOM   3903 C  CB   . ARG A 1 241 ? -5.744  8.940   3.665  1.00 36.49  ? 238 ARG A CB   1 
ATOM   3904 C  CG   . ARG A 1 241 ? -6.395  8.099   2.568  1.00 46.45  ? 238 ARG A CG   1 
ATOM   3905 C  CD   . ARG A 1 241 ? -5.923  8.590   1.203  1.00 64.45  ? 238 ARG A CD   1 
ATOM   3906 N  NE   . ARG A 1 241 ? -4.541  8.203   0.928  1.00 85.99  ? 238 ARG A NE   1 
ATOM   3907 C  CZ   . ARG A 1 241 ? -3.545  9.056   0.704  1.00 72.57  ? 238 ARG A CZ   1 
ATOM   3908 N  NH1  . ARG A 1 241 ? -3.730  10.368  0.741  1.00 75.23  ? 238 ARG A NH1  1 
ATOM   3909 N  NH2  . ARG A 1 241 ? -2.331  8.581   0.439  1.00 67.41  ? 238 ARG A NH2  1 
ATOM   3910 H  H    . ARG A 1 241 ? -4.855  9.886   5.700  1.00 33.79  ? 238 ARG A H    1 
ATOM   3911 H  HA   . ARG A 1 241 ? -7.228  9.083   5.085  1.00 36.86  ? 238 ARG A HA   1 
ATOM   3912 H  HB2  . ARG A 1 241 ? -5.855  9.873   3.424  1.00 43.82  ? 238 ARG A HB2  1 
ATOM   3913 H  HB3  . ARG A 1 241 ? -4.801  8.713   3.687  1.00 43.82  ? 238 ARG A HB3  1 
ATOM   3914 H  HG2  . ARG A 1 241 ? -6.140  7.169   2.672  1.00 55.77  ? 238 ARG A HG2  1 
ATOM   3915 H  HG3  . ARG A 1 241 ? -7.360  8.187   2.616  1.00 55.77  ? 238 ARG A HG3  1 
ATOM   3916 H  HD2  . ARG A 1 241 ? -6.488  8.206   0.514  1.00 77.38  ? 238 ARG A HD2  1 
ATOM   3917 H  HD3  . ARG A 1 241 ? -5.978  9.558   1.176  1.00 77.38  ? 238 ARG A HD3  1 
ATOM   3918 H  HE   . ARG A 1 241 ? -4.357  7.363   0.909  1.00 103.22 ? 238 ARG A HE   1 
ATOM   3919 H  HH11 . ARG A 1 241 ? -4.509  10.688  0.913  1.00 90.31  ? 238 ARG A HH11 1 
ATOM   3920 H  HH12 . ARG A 1 241 ? -3.070  10.899  0.593  1.00 90.31  ? 238 ARG A HH12 1 
ATOM   3921 H  HH21 . ARG A 1 241 ? -2.197  7.732   0.415  1.00 80.93  ? 238 ARG A HH21 1 
ATOM   3922 H  HH22 . ARG A 1 241 ? -1.679  9.123   0.293  1.00 80.93  ? 238 ARG A HH22 1 
ATOM   3923 N  N    . PHE A 1 242 ? -5.227  6.662   5.722  1.00 28.57  ? 239 PHE A N    1 
ATOM   3924 C  CA   . PHE A 1 242 ? -5.148  5.242   6.021  1.00 29.55  ? 239 PHE A CA   1 
ATOM   3925 C  C    . PHE A 1 242 ? -6.008  4.879   7.230  1.00 28.78  ? 239 PHE A C    1 
ATOM   3926 O  O    . PHE A 1 242 ? -6.722  3.870   7.212  1.00 29.16  ? 239 PHE A O    1 
ATOM   3927 C  CB   . PHE A 1 242 ? -3.680  4.867   6.247  1.00 26.94  ? 239 PHE A CB   1 
ATOM   3928 C  CG   . PHE A 1 242 ? -3.471  3.422   6.631  1.00 25.10  ? 239 PHE A CG   1 
ATOM   3929 C  CD1  . PHE A 1 242 ? -3.569  2.420   5.699  1.00 28.94  ? 239 PHE A CD1  1 
ATOM   3930 C  CD2  . PHE A 1 242 ? -3.123  3.098   7.937  1.00 28.33  ? 239 PHE A CD2  1 
ATOM   3931 C  CE1  . PHE A 1 242 ? -3.368  1.087   6.049  1.00 31.44  ? 239 PHE A CE1  1 
ATOM   3932 C  CE2  . PHE A 1 242 ? -2.926  1.794   8.286  1.00 29.31  ? 239 PHE A CE2  1 
ATOM   3933 C  CZ   . PHE A 1 242 ? -3.043  0.801   7.357  1.00 26.26  ? 239 PHE A CZ   1 
ATOM   3934 H  H    . PHE A 1 242 ? -4.478  7.078   5.802  1.00 34.31  ? 239 PHE A H    1 
ATOM   3935 H  HA   . PHE A 1 242 ? -5.484  4.727   5.270  1.00 35.50  ? 239 PHE A HA   1 
ATOM   3936 H  HB2  . PHE A 1 242 ? -3.187  5.030   5.427  1.00 32.37  ? 239 PHE A HB2  1 
ATOM   3937 H  HB3  . PHE A 1 242 ? -3.325  5.417   6.962  1.00 32.37  ? 239 PHE A HB3  1 
ATOM   3938 H  HD1  . PHE A 1 242 ? -3.773  2.636   4.818  1.00 34.77  ? 239 PHE A HD1  1 
ATOM   3939 H  HD2  . PHE A 1 242 ? -3.025  3.770   8.572  1.00 34.03  ? 239 PHE A HD2  1 
ATOM   3940 H  HE1  . PHE A 1 242 ? -3.452  0.410   5.417  1.00 37.77  ? 239 PHE A HE1  1 
ATOM   3941 H  HE2  . PHE A 1 242 ? -2.711  1.579   9.165  1.00 35.20  ? 239 PHE A HE2  1 
ATOM   3942 H  HZ   . PHE A 1 242 ? -2.900  -0.082  7.610  1.00 31.55  ? 239 PHE A HZ   1 
ATOM   3943 N  N    . PHE A 1 243 ? -5.954  5.679   8.294  1.00 27.46  ? 240 PHE A N    1 
ATOM   3944 C  CA   . PHE A 1 243 ? -6.750  5.328   9.461  1.00 25.49  ? 240 PHE A CA   1 
ATOM   3945 C  C    . PHE A 1 243 ? -8.208  5.702   9.285  1.00 32.67  ? 240 PHE A C    1 
ATOM   3946 O  O    . PHE A 1 243 ? -9.077  5.046   9.871  1.00 30.00  ? 240 PHE A O    1 
ATOM   3947 C  CB   . PHE A 1 243 ? -6.186  5.964   10.738 1.00 27.56  ? 240 PHE A CB   1 
ATOM   3948 C  CG   . PHE A 1 243 ? -4.962  5.260   11.215 1.00 25.90  ? 240 PHE A CG   1 
ATOM   3949 C  CD1  . PHE A 1 243 ? -5.020  3.893   11.566 1.00 29.56  ? 240 PHE A CD1  1 
ATOM   3950 C  CD2  . PHE A 1 243 ? -3.761  5.909   11.284 1.00 25.35  ? 240 PHE A CD2  1 
ATOM   3951 C  CE1  . PHE A 1 243 ? -3.881  3.230   11.950 1.00 27.64  ? 240 PHE A CE1  1 
ATOM   3952 C  CE2  . PHE A 1 243 ? -2.611  5.237   11.704 1.00 30.92  ? 240 PHE A CE2  1 
ATOM   3953 C  CZ   . PHE A 1 243 ? -2.694  3.894   12.055 1.00 27.45  ? 240 PHE A CZ   1 
ATOM   3954 H  H    . PHE A 1 243 ? -5.484  6.396   8.359  1.00 32.99  ? 240 PHE A H    1 
ATOM   3955 H  HA   . PHE A 1 243 ? -6.696  4.369   9.592  1.00 30.62  ? 240 PHE A HA   1 
ATOM   3956 H  HB2  . PHE A 1 243 ? -5.954  6.888   10.558 1.00 33.11  ? 240 PHE A HB2  1 
ATOM   3957 H  HB3  . PHE A 1 243 ? -6.855  5.919   11.439 1.00 33.11  ? 240 PHE A HB3  1 
ATOM   3958 H  HD1  . PHE A 1 243 ? -5.832  3.441   11.537 1.00 35.51  ? 240 PHE A HD1  1 
ATOM   3959 H  HD2  . PHE A 1 243 ? -3.709  6.807   11.050 1.00 30.45  ? 240 PHE A HD2  1 
ATOM   3960 H  HE1  . PHE A 1 243 ? -3.919  2.321   12.140 1.00 33.20  ? 240 PHE A HE1  1 
ATOM   3961 H  HE2  . PHE A 1 243 ? -1.797  5.685   11.749 1.00 37.13  ? 240 PHE A HE2  1 
ATOM   3962 H  HZ   . PHE A 1 243 ? -1.939  3.447   12.362 1.00 32.98  ? 240 PHE A HZ   1 
ATOM   3963 N  N    . ASN A 1 244 ? -8.509  6.681   8.434  1.00 29.52  ? 241 ASN A N    1 
ATOM   3964 C  CA   . ASN A 1 244 ? -9.911  7.016   8.230  1.00 29.78  ? 241 ASN A CA   1 
ATOM   3965 C  C    . ASN A 1 244 ? -10.678 5.908   7.526  1.00 34.03  ? 241 ASN A C    1 
ATOM   3966 O  O    . ASN A 1 244 ? -11.907 5.988   7.451  1.00 39.92  ? 241 ASN A O    1 
ATOM   3967 C  CB   . ASN A 1 244 ? -10.074 8.326   7.444  1.00 34.86  ? 241 ASN A CB   1 
ATOM   3968 C  CG   . ASN A 1 244 ? -10.090 9.529   8.366  1.00 41.51  ? 241 ASN A CG   1 
ATOM   3969 O  OD1  . ASN A 1 244 ? -10.342 9.406   9.563  1.00 42.27  ? 241 ASN A OD1  1 
ATOM   3970 N  ND2  . ASN A 1 244 ? -9.872  10.708  7.798  1.00 41.79  ? 241 ASN A ND2  1 
ATOM   3971 H  H    . ASN A 1 244 ? -7.943  7.145   7.983  1.00 35.46  ? 241 ASN A H    1 
ATOM   3972 H  HA   . ASN A 1 244 ? -10.305 7.162   9.104  1.00 35.70  ? 241 ASN A HA   1 
ATOM   3973 H  HB2  . ASN A 1 244 ? -9.332  8.424   6.827  1.00 41.86  ? 241 ASN A HB2  1 
ATOM   3974 H  HB3  . ASN A 1 244 ? -10.911 8.305   6.955  1.00 41.86  ? 241 ASN A HB3  1 
ATOM   3975 H  HD21 . ASN A 1 244 ? -9.871  11.423  8.276  1.00 50.18  ? 241 ASN A HD21 1 
ATOM   3976 H  HD22 . ASN A 1 244 ? -9.732  10.758  6.951  1.00 50.18  ? 241 ASN A HD22 1 
ATOM   3977 N  N    . ALA A 1 245 ? -10.001 4.880   7.018  1.00 31.69  ? 242 ALA A N    1 
ATOM   3978 C  CA   . ALA A 1 245 ? -10.719 3.734   6.460  1.00 38.86  ? 242 ALA A CA   1 
ATOM   3979 C  C    . ALA A 1 245 ? -11.476 2.964   7.537  1.00 43.29  ? 242 ALA A C    1 
ATOM   3980 O  O    . ALA A 1 245 ? -12.380 2.189   7.219  1.00 44.76  ? 242 ALA A O    1 
ATOM   3981 C  CB   . ALA A 1 245 ? -9.751  2.805   5.737  1.00 46.66  ? 242 ALA A CB   1 
ATOM   3982 H  H    . ALA A 1 245 ? -9.144  4.822   6.984  1.00 38.06  ? 242 ALA A H    1 
ATOM   3983 H  HA   . ALA A 1 245 ? -11.361 4.053   5.806  1.00 46.66  ? 242 ALA A HA   1 
ATOM   3984 H  HB1  . ALA A 1 245 ? -10.244 2.048   5.384  1.00 56.03  ? 242 ALA A HB1  1 
ATOM   3985 H  HB2  . ALA A 1 245 ? -9.328  3.291   5.011  1.00 56.03  ? 242 ALA A HB2  1 
ATOM   3986 H  HB3  . ALA A 1 245 ? -9.079  2.499   6.365  1.00 56.03  ? 242 ALA A HB3  1 
ATOM   3987 N  N    . LEU A 1 246 ? -11.130 3.173   8.803  1.00 37.41  ? 243 LEU A N    1 
ATOM   3988 C  CA   . LEU A 1 246 ? -11.856 2.562   9.910  1.00 43.21  ? 243 LEU A CA   1 
ATOM   3989 C  C    . LEU A 1 246 ? -13.251 3.136   10.082 1.00 52.42  ? 243 LEU A C    1 
ATOM   3990 O  O    . LEU A 1 246 ? -14.103 2.490   10.702 1.00 53.58  ? 243 LEU A O    1 
ATOM   3991 C  CB   . LEU A 1 246 ? -11.088 2.768   11.209 1.00 38.11  ? 243 LEU A CB   1 
ATOM   3992 C  CG   . LEU A 1 246 ? -9.773  2.003   11.325 1.00 36.10  ? 243 LEU A CG   1 
ATOM   3993 C  CD1  . LEU A 1 246 ? -8.998  2.446   12.530 1.00 38.69  ? 243 LEU A CD1  1 
ATOM   3994 C  CD2  . LEU A 1 246 ? -10.088 0.501   11.379 1.00 46.15  ? 243 LEU A CD2  1 
ATOM   3995 H  H    . LEU A 1 246 ? -10.472 3.668   9.051  1.00 44.93  ? 243 LEU A H    1 
ATOM   3996 H  HA   . LEU A 1 246 ? -11.933 1.612   9.731  1.00 51.89  ? 243 LEU A HA   1 
ATOM   3997 H  HB2  . LEU A 1 246 ? -10.882 3.712   11.294 1.00 45.77  ? 243 LEU A HB2  1 
ATOM   3998 H  HB3  . LEU A 1 246 ? -11.653 2.485   11.945 1.00 45.77  ? 243 LEU A HB3  1 
ATOM   3999 H  HG   . LEU A 1 246 ? -9.210  2.181   10.555 1.00 43.35  ? 243 LEU A HG   1 
ATOM   4000 H  HD11 . LEU A 1 246 ? -8.140  1.993   12.538 1.00 46.47  ? 243 LEU A HD11 1 
ATOM   4001 H  HD12 . LEU A 1 246 ? -8.864  3.406   12.485 1.00 46.47  ? 243 LEU A HD12 1 
ATOM   4002 H  HD13 . LEU A 1 246 ? -9.499  2.219   13.329 1.00 46.47  ? 243 LEU A HD13 1 
ATOM   4003 H  HD21 . LEU A 1 246 ? -9.269  0.013   11.554 1.00 55.41  ? 243 LEU A HD21 1 
ATOM   4004 H  HD22 . LEU A 1 246 ? -10.728 0.338   12.090 1.00 55.41  ? 243 LEU A HD22 1 
ATOM   4005 H  HD23 . LEU A 1 246 ? -10.462 0.225   10.528 1.00 55.41  ? 243 LEU A HD23 1 
ATOM   4006 N  N    . THR A 1 247 ? -13.500 4.330   9.557  1.00 51.65  ? 244 THR A N    1 
ATOM   4007 C  CA   . THR A 1 247 ? -14.743 5.032   9.820  1.00 62.74  ? 244 THR A CA   1 
ATOM   4008 C  C    . THR A 1 247 ? -15.654 4.918   8.606  1.00 73.02  ? 244 THR A C    1 
ATOM   4009 O  O    . THR A 1 247 ? -16.855 5.155   8.734  1.00 70.86  ? 244 THR A O    1 
ATOM   4010 C  CB   . THR A 1 247 ? -14.482 6.501   10.155 1.00 62.53  ? 244 THR A CB   1 
ATOM   4011 O  OG1  . THR A 1 247 ? -13.979 7.177   8.996  1.00 62.59  ? 244 THR A OG1  1 
ATOM   4012 C  CG2  . THR A 1 247 ? -13.449 6.601   11.292 1.00 61.50  ? 244 THR A CG2  1 
ATOM   4013 O  OXT  . THR A 1 247 ? -15.214 4.585   7.493  1.00 65.87  ? 244 THR A OXT  1 
ATOM   4014 H  H    . THR A 1 247 ? -12.959 4.755   9.041  1.00 62.01  ? 244 THR A H    1 
ATOM   4015 H  HA   . THR A 1 247 ? -15.204 4.645   10.581 1.00 75.32  ? 244 THR A HA   1 
ATOM   4016 H  HB   . THR A 1 247 ? -15.305 6.926   10.440 1.00 75.07  ? 244 THR A HB   1 
ATOM   4017 H  HG1  . THR A 1 247 ? -13.280 6.799   8.724  1.00 75.14  ? 244 THR A HG1  1 
ATOM   4018 H  HG21 . THR A 1 247 ? -13.309 7.530   11.531 1.00 73.83  ? 244 THR A HG21 1 
ATOM   4019 H  HG22 . THR A 1 247 ? -13.766 6.119   12.071 1.00 73.83  ? 244 THR A HG22 1 
ATOM   4020 H  HG23 . THR A 1 247 ? -12.604 6.218   11.007 1.00 73.83  ? 244 THR A HG23 1 
HETATM 4021 CA CA   . CA  B 2 .   ? -8.509  17.852  19.373 0.57 29.85  ? 301 CA  A CA   1 
HETATM 4022 CA CA   . CA  C 2 .   ? -4.984  20.702  11.106 0.65 35.08  ? 302 CA  A CA   1 
HETATM 4023 CA CA   . CA  D 2 .   ? 14.461  3.952   -4.836 0.63 45.00  ? 303 CA  A CA   1 
HETATM 4024 CA CA   . CA  E 2 .   ? 24.874  -3.393  30.969 0.99 79.07  ? 304 CA  A CA   1 
HETATM 4025 O  O    . HOH F 3 .   ? 14.491  4.845   16.213 1.00 36.89  ? 401 HOH A O    1 
HETATM 4026 O  O    . HOH F 3 .   ? 9.726   -2.825  33.397 1.00 51.25  ? 402 HOH A O    1 
HETATM 4027 O  O    . HOH F 3 .   ? 11.455  1.762   -3.999 1.00 43.69  ? 403 HOH A O    1 
HETATM 4028 O  O    . HOH F 3 .   ? 6.588   0.611   32.423 1.00 51.25  ? 404 HOH A O    1 
HETATM 4029 O  O    . HOH F 3 .   ? 14.264  -4.041  33.464 1.00 67.00  ? 405 HOH A O    1 
HETATM 4030 O  O    . HOH F 3 .   ? -14.031 0.881   20.608 1.00 52.70  ? 406 HOH A O    1 
HETATM 4031 O  O    . HOH F 3 .   ? 12.266  -15.478 17.296 1.00 53.87  ? 407 HOH A O    1 
HETATM 4032 O  O    . HOH F 3 .   ? 7.983   13.915  6.454  1.00 31.77  ? 408 HOH A O    1 
HETATM 4033 O  O    . HOH F 3 .   ? 6.536   -8.559  28.408 1.00 46.87  ? 409 HOH A O    1 
HETATM 4034 O  O    . HOH F 3 .   ? 8.653   -4.314  -1.906 1.00 29.87  ? 410 HOH A O    1 
HETATM 4035 O  O    . HOH F 3 .   ? 15.050  10.524  17.695 1.00 49.44  ? 411 HOH A O    1 
HETATM 4036 O  O    . HOH F 3 .   ? 10.770  14.887  7.299  1.00 42.39  ? 412 HOH A O    1 
HETATM 4037 O  O    . HOH F 3 .   ? 2.396   2.897   29.100 1.00 41.38  ? 413 HOH A O    1 
HETATM 4038 O  O    . HOH F 3 .   ? 22.863  26.161  24.588 1.00 50.23  ? 414 HOH A O    1 
HETATM 4039 O  O    . HOH F 3 .   ? 5.143   7.808   21.890 1.00 25.95  ? 415 HOH A O    1 
HETATM 4040 O  O    . HOH F 3 .   ? -5.532  19.408  9.166  1.00 47.65  ? 416 HOH A O    1 
HETATM 4041 O  O    . HOH F 3 .   ? 15.983  3.121   13.600 1.00 40.34  ? 417 HOH A O    1 
HETATM 4042 O  O    . HOH F 3 .   ? -0.126  13.904  22.213 1.00 40.38  ? 418 HOH A O    1 
HETATM 4043 O  O    . HOH F 3 .   ? 18.967  12.206  33.983 1.00 39.53  ? 419 HOH A O    1 
HETATM 4044 O  O    . HOH F 3 .   ? 12.634  6.376   6.304  1.00 31.36  ? 420 HOH A O    1 
HETATM 4045 O  O    . HOH F 3 .   ? 0.734   -2.740  -2.691 1.00 49.09  ? 421 HOH A O    1 
HETATM 4046 O  O    . HOH F 3 .   ? -4.753  -10.734 5.785  1.00 44.96  ? 422 HOH A O    1 
HETATM 4047 O  O    . HOH F 3 .   ? 3.698   14.524  12.328 1.00 30.09  ? 423 HOH A O    1 
HETATM 4048 O  O    . HOH F 3 .   ? 12.277  6.961   32.939 1.00 34.24  ? 424 HOH A O    1 
HETATM 4049 O  O    . HOH F 3 .   ? 22.239  9.986   37.828 1.00 45.32  ? 425 HOH A O    1 
HETATM 4050 O  O    . HOH F 3 .   ? 9.609   -12.431 8.092  1.00 44.91  ? 426 HOH A O    1 
HETATM 4051 O  O    . HOH F 3 .   ? -6.488  -7.989  13.971 1.00 45.83  ? 427 HOH A O    1 
HETATM 4052 O  O    . HOH F 3 .   ? -7.717  -7.337  5.340  1.00 50.02  ? 428 HOH A O    1 
HETATM 4053 O  O    . HOH F 3 .   ? 4.649   14.910  26.499 1.00 41.47  ? 429 HOH A O    1 
HETATM 4054 O  O    . HOH F 3 .   ? 11.380  -9.180  19.908 1.00 30.35  ? 430 HOH A O    1 
HETATM 4055 O  O    . HOH F 3 .   ? -9.791  6.963   3.939  1.00 50.58  ? 431 HOH A O    1 
HETATM 4056 O  O    . HOH F 3 .   ? -11.687 -3.040  25.760 1.00 46.21  ? 432 HOH A O    1 
HETATM 4057 O  O    . HOH F 3 .   ? -14.123 9.947   12.558 1.00 51.57  ? 433 HOH A O    1 
HETATM 4058 O  O    . HOH F 3 .   ? 11.282  -16.068 8.491  1.00 50.49  ? 434 HOH A O    1 
HETATM 4059 O  O    . HOH F 3 .   ? 13.395  13.001  18.443 1.00 43.35  ? 435 HOH A O    1 
HETATM 4060 O  O    . HOH F 3 .   ? 24.025  -0.160  31.595 1.00 58.46  ? 436 HOH A O    1 
HETATM 4061 O  O    . HOH F 3 .   ? 0.990   -10.741 1.845  1.00 52.40  ? 437 HOH A O    1 
HETATM 4062 O  O    . HOH F 3 .   ? -8.531  -5.437  10.855 1.00 45.28  ? 438 HOH A O    1 
HETATM 4063 O  O    . HOH F 3 .   ? -1.859  -0.366  31.809 1.00 39.98  ? 439 HOH A O    1 
HETATM 4064 O  O    . HOH F 3 .   ? 6.618   13.660  2.533  1.00 33.96  ? 440 HOH A O    1 
HETATM 4065 O  O    . HOH F 3 .   ? -6.638  -7.615  23.462 1.00 43.71  ? 441 HOH A O    1 
HETATM 4066 O  O    . HOH F 3 .   ? -14.038 -0.169  11.477 1.00 55.13  ? 442 HOH A O    1 
HETATM 4067 O  O    . HOH F 3 .   ? 11.968  14.619  21.844 1.00 46.56  ? 443 HOH A O    1 
HETATM 4068 O  O    . HOH F 3 .   ? 2.707   13.623  22.540 1.00 35.79  ? 444 HOH A O    1 
HETATM 4069 O  O    . HOH F 3 .   ? 2.519   -17.855 9.514  1.00 41.29  ? 445 HOH A O    1 
HETATM 4070 O  O    . HOH F 3 .   ? 7.863   6.003   30.995 1.00 37.74  ? 446 HOH A O    1 
HETATM 4071 O  O    . HOH F 3 .   ? 15.907  5.641   -4.133 1.00 53.28  ? 447 HOH A O    1 
HETATM 4072 O  O    . HOH F 3 .   ? 0.348   3.494   30.224 1.00 46.12  ? 448 HOH A O    1 
HETATM 4073 O  O    . HOH F 3 .   ? 8.421   -12.704 16.839 1.00 33.53  ? 449 HOH A O    1 
HETATM 4074 O  O    . HOH F 3 .   ? -8.409  1.666   15.832 1.00 29.26  ? 450 HOH A O    1 
HETATM 4075 O  O    . HOH F 3 .   ? 11.931  1.557   6.602  1.00 28.29  ? 451 HOH A O    1 
HETATM 4076 O  O    . HOH F 3 .   ? 13.044  -8.151  0.375  1.00 46.57  ? 452 HOH A O    1 
HETATM 4077 O  O    . HOH F 3 .   ? 24.673  3.531   32.934 1.00 51.67  ? 453 HOH A O    1 
HETATM 4078 O  O    . HOH F 3 .   ? -6.894  16.642  11.277 1.00 38.13  ? 454 HOH A O    1 
HETATM 4079 O  O    . HOH F 3 .   ? -8.480  -3.917  18.091 1.00 34.10  ? 455 HOH A O    1 
HETATM 4080 O  O    . HOH F 3 .   ? -7.982  -4.764  20.729 1.00 46.05  ? 456 HOH A O    1 
HETATM 4081 O  O    . HOH F 3 .   ? 18.739  7.561   9.474  1.00 46.42  ? 457 HOH A O    1 
HETATM 4082 O  O    . HOH F 3 .   ? -2.246  17.469  8.800  1.00 44.51  ? 458 HOH A O    1 
HETATM 4083 O  O    . HOH F 3 .   ? 18.385  -1.668  8.485  1.00 45.38  ? 459 HOH A O    1 
HETATM 4084 O  O    . HOH F 3 .   ? 4.609   6.541   29.228 1.00 30.34  ? 460 HOH A O    1 
HETATM 4085 O  O    . HOH F 3 .   ? 14.593  -5.439  0.602  1.00 43.54  ? 461 HOH A O    1 
HETATM 4086 O  O    . HOH F 3 .   ? -12.239 14.183  18.725 1.00 46.46  ? 462 HOH A O    1 
HETATM 4087 O  O    . HOH F 3 .   ? 15.488  5.863   2.151  1.00 46.00  ? 463 HOH A O    1 
HETATM 4088 O  O    . HOH F 3 .   ? 7.174   -10.905 18.929 1.00 27.95  ? 464 HOH A O    1 
HETATM 4089 O  O    . HOH F 3 .   ? 5.120   20.232  23.633 1.00 39.26  ? 465 HOH A O    1 
HETATM 4090 O  O    . HOH F 3 .   ? 15.404  10.131  24.939 1.00 45.33  ? 466 HOH A O    1 
HETATM 4091 O  O    . HOH F 3 .   ? 1.067   -14.801 17.794 1.00 32.91  ? 467 HOH A O    1 
HETATM 4092 O  O    . HOH F 3 .   ? 13.292  -7.993  -3.037 1.00 37.36  ? 468 HOH A O    1 
HETATM 4093 O  O    . HOH F 3 .   ? 7.195   -13.901 5.270  1.00 46.41  ? 469 HOH A O    1 
HETATM 4094 O  O    . HOH F 3 .   ? -12.470 7.702   19.953 1.00 38.59  ? 470 HOH A O    1 
HETATM 4095 O  O    . HOH F 3 .   ? 16.935  11.773  7.407  1.00 48.70  ? 471 HOH A O    1 
HETATM 4096 O  O    . HOH F 3 .   ? 17.863  0.851   7.991  1.00 41.43  ? 472 HOH A O    1 
HETATM 4097 O  O    . HOH F 3 .   ? 5.832   8.326   31.192 1.00 40.42  ? 473 HOH A O    1 
HETATM 4098 O  O    . HOH F 3 .   ? -2.062  -10.767 12.669 1.00 32.42  ? 474 HOH A O    1 
HETATM 4099 O  O    . HOH F 3 .   ? 18.531  -2.296  24.889 1.00 37.45  ? 475 HOH A O    1 
HETATM 4100 O  O    . HOH F 3 .   ? 3.894   14.362  15.022 1.00 27.51  ? 476 HOH A O    1 
HETATM 4101 O  O    . HOH F 3 .   ? -6.685  20.489  12.886 1.00 40.44  ? 477 HOH A O    1 
HETATM 4102 O  O    . HOH F 3 .   ? 1.972   -0.312  -2.439 1.00 37.78  ? 478 HOH A O    1 
HETATM 4103 O  O    . HOH F 3 .   ? -6.386  17.467  18.842 1.00 30.17  ? 479 HOH A O    1 
HETATM 4104 O  O    . HOH F 3 .   ? -4.807  -7.348  5.458  1.00 34.04  ? 480 HOH A O    1 
HETATM 4105 O  O    . HOH F 3 .   ? 8.943   -0.693  31.840 1.00 38.60  ? 481 HOH A O    1 
HETATM 4106 O  O    . HOH F 3 .   ? 8.006   19.805  12.098 1.00 48.98  ? 482 HOH A O    1 
HETATM 4107 O  O    . HOH F 3 .   ? -9.805  -4.372  22.769 1.00 47.88  ? 483 HOH A O    1 
HETATM 4108 O  O    . HOH F 3 .   ? -4.189  -11.578 20.995 1.00 34.66  ? 484 HOH A O    1 
HETATM 4109 O  O    . HOH F 3 .   ? 6.933   10.488  -3.007 1.00 44.08  ? 485 HOH A O    1 
HETATM 4110 O  O    . HOH F 3 .   ? -5.639  -7.725  26.246 1.00 45.07  ? 486 HOH A O    1 
HETATM 4111 O  O    . HOH F 3 .   ? 16.070  -9.558  23.017 1.00 43.03  ? 487 HOH A O    1 
HETATM 4112 O  O    . HOH F 3 .   ? 4.298   0.987   -3.893 1.00 48.52  ? 488 HOH A O    1 
HETATM 4113 O  O    . HOH F 3 .   ? -0.371  12.243  1.138  1.00 48.35  ? 489 HOH A O    1 
HETATM 4114 O  O    . HOH F 3 .   ? 6.211   4.398   -3.133 1.00 45.22  ? 490 HOH A O    1 
HETATM 4115 O  O    . HOH F 3 .   ? 16.333  4.161   27.839 1.00 33.65  ? 491 HOH A O    1 
HETATM 4116 O  O    . HOH F 3 .   ? 9.167   1.384   7.573  1.00 27.55  ? 492 HOH A O    1 
HETATM 4117 O  O    . HOH F 3 .   ? -9.125  -2.162  9.386  1.00 43.81  ? 493 HOH A O    1 
HETATM 4118 O  O    . HOH F 3 .   ? 7.170   13.670  -0.082 1.00 40.87  ? 494 HOH A O    1 
HETATM 4119 O  O    . HOH F 3 .   ? 18.092  8.163   -0.148 1.00 58.78  ? 495 HOH A O    1 
HETATM 4120 O  O    . HOH F 3 .   ? 13.112  -5.303  32.099 1.00 56.52  ? 496 HOH A O    1 
HETATM 4121 O  O    . HOH F 3 .   ? -3.112  6.119   2.675  1.00 46.54  ? 497 HOH A O    1 
HETATM 4122 O  O    . HOH F 3 .   ? -1.682  11.294  22.137 1.00 38.26  ? 498 HOH A O    1 
HETATM 4123 O  O    . HOH F 3 .   ? 11.485  4.067   36.605 1.00 40.88  ? 499 HOH A O    1 
HETATM 4124 O  O    . HOH F 3 .   ? 12.947  15.192  10.327 1.00 44.14  ? 500 HOH A O    1 
HETATM 4125 O  O    . HOH F 3 .   ? 23.792  -3.269  33.294 1.00 65.01  ? 501 HOH A O    1 
HETATM 4126 O  O    . HOH F 3 .   ? 5.531   20.373  15.453 1.00 44.86  ? 502 HOH A O    1 
HETATM 4127 O  O    . HOH F 3 .   ? 15.076  13.233  10.650 1.00 38.76  ? 503 HOH A O    1 
HETATM 4128 O  O    . HOH F 3 .   ? 5.213   16.657  16.699 1.00 35.11  ? 504 HOH A O    1 
HETATM 4129 O  O    . HOH F 3 .   ? 5.582   15.710  31.056 1.00 45.74  ? 505 HOH A O    1 
HETATM 4130 O  O    . HOH F 3 .   ? 26.459  -5.162  29.562 1.00 63.42  ? 506 HOH A O    1 
HETATM 4131 O  O    . HOH F 3 .   ? 12.220  10.595  35.289 1.00 45.88  ? 507 HOH A O    1 
HETATM 4132 O  O    . HOH F 3 .   ? 11.290  0.095   33.586 1.00 49.21  ? 508 HOH A O    1 
HETATM 4133 O  O    . HOH F 3 .   ? 22.926  0.268   11.511 1.00 52.00  ? 509 HOH A O    1 
HETATM 4134 O  O    . HOH F 3 .   ? 19.622  -6.493  14.126 1.00 44.16  ? 510 HOH A O    1 
HETATM 4135 O  O    . HOH F 3 .   ? 17.678  2.522   -3.047 1.00 60.02  ? 511 HOH A O    1 
HETATM 4136 O  O    . HOH F 3 .   ? -3.480  20.738  9.475  1.00 55.92  ? 512 HOH A O    1 
HETATM 4137 O  O    . HOH F 3 .   ? 3.345   15.775  24.207 1.00 46.05  ? 513 HOH A O    1 
HETATM 4138 O  O    . HOH F 3 .   ? 24.661  -6.562  30.222 1.00 65.10  ? 514 HOH A O    1 
HETATM 4139 O  O    . HOH F 3 .   ? 5.670   12.027  -1.898 1.00 50.43  ? 515 HOH A O    1 
HETATM 4140 O  O    . HOH F 3 .   ? 15.557  -1.150  -2.379 1.00 51.58  ? 516 HOH A O    1 
HETATM 4141 O  O    . HOH F 3 .   ? 15.914  2.190   15.786 1.00 50.96  ? 517 HOH A O    1 
HETATM 4142 O  O    . HOH F 3 .   ? 4.476   18.366  25.637 1.00 47.31  ? 518 HOH A O    1 
HETATM 4143 O  O    . HOH F 3 .   ? 9.492   5.935   33.223 1.00 45.88  ? 519 HOH A 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   . ILE A 6   ? 0.8380 0.9296 0.9293 -0.0312 -0.2237 -0.2595 3   ILE A N   
2    C CA  . ILE A 6   ? 0.9346 1.0387 1.0358 -0.0357 -0.2116 -0.2349 3   ILE A CA  
3    C C   . ILE A 6   ? 0.7858 0.9014 0.8365 -0.0141 -0.2041 -0.2247 3   ILE A C   
4    O O   . ILE A 6   ? 0.7600 0.8999 0.7818 0.0027  -0.2119 -0.2257 3   ILE A O   
5    C CB  . ILE A 6   ? 0.8232 0.9588 0.9625 -0.0458 -0.2198 -0.2271 3   ILE A CB  
6    C CG1 . ILE A 6   ? 1.0655 1.1897 1.2625 -0.0711 -0.2178 -0.2250 3   ILE A CG1 
7    C CG2 . ILE A 6   ? 0.6621 0.8198 0.7984 -0.0410 -0.2102 -0.2041 3   ILE A CG2 
8    C CD1 . ILE A 6   ? 1.1462 1.2452 1.3604 -0.0831 -0.1975 -0.2067 3   ILE A CD1 
19   N N   . LYS A 7   ? 0.8554 0.9498 0.8941 -0.0139 -0.1792 -0.2022 4   LYS A N   
20   C CA  . LYS A 7   ? 0.7795 0.8800 0.7741 0.0046  -0.1637 -0.1830 4   LYS A CA  
21   C C   . LYS A 7   ? 0.6912 0.7786 0.6964 -0.0033 -0.1394 -0.1537 4   LYS A C   
22   O O   . LYS A 7   ? 0.6794 0.7490 0.7154 -0.0193 -0.1330 -0.1498 4   LYS A O   
23   C CB  . LYS A 7   ? 0.8400 0.9288 0.7907 0.0219  -0.1617 -0.1959 4   LYS A CB  
24   C CG  . LYS A 7   ? 1.1880 1.2943 1.0930 0.0439  -0.1534 -0.1811 4   LYS A CG  
25   C CD  . LYS A 7   ? 1.2980 1.3907 1.1655 0.0583  -0.1375 -0.1785 4   LYS A CD  
26   C CE  . LYS A 7   ? 1.3753 1.4759 1.2198 0.0689  -0.1169 -0.1474 4   LYS A CE  
27   N NZ  . LYS A 7   ? 0.9592 1.0484 0.8339 0.0530  -0.1011 -0.1236 4   LYS A NZ  
41   N N   . THR A 8   ? 0.5645 0.6610 0.5444 0.0087  -0.1264 -0.1329 5   THR A N   
42   C CA  . THR A 8   ? 0.5565 0.6388 0.5398 0.0043  -0.1043 -0.1088 5   THR A CA  
43   C C   . THR A 8   ? 0.4955 0.5530 0.4659 0.0053  -0.0938 -0.1120 5   THR A C   
44   O O   . THR A 8   ? 0.5252 0.5821 0.4646 0.0191  -0.0944 -0.1212 5   THR A O   
45   C CB  . THR A 8   ? 0.5680 0.6622 0.5282 0.0173  -0.0939 -0.0881 5   THR A CB  
46   O OG1 . THR A 8   ? 0.5472 0.6642 0.5229 0.0172  -0.1030 -0.0839 5   THR A OG1 
47   C CG2 . THR A 8   ? 0.5547 0.6331 0.5174 0.0134  -0.0731 -0.0675 5   THR A CG2 
55   N N   . PRO A 9   ? 0.4640 0.5030 0.4562 -0.0069 -0.0838 -0.1045 6   PRO A N   
56   C CA  . PRO A 9   ? 0.4077 0.4254 0.3889 -0.0041 -0.0741 -0.1065 6   PRO A CA  
57   C C   . PRO A 9   ? 0.4593 0.4804 0.4104 0.0094  -0.0600 -0.0938 6   PRO A C   
58   O O   . PRO A 9   ? 0.4511 0.4828 0.3971 0.0121  -0.0525 -0.0768 6   PRO A O   
59   C CB  . PRO A 9   ? 0.5050 0.5076 0.5143 -0.0180 -0.0650 -0.0939 6   PRO A CB  
60   C CG  . PRO A 9   ? 0.4953 0.5110 0.5310 -0.0286 -0.0699 -0.0880 6   PRO A CG  
61   C CD  . PRO A 9   ? 0.4880 0.5264 0.5177 -0.0232 -0.0832 -0.0966 6   PRO A CD  
69   N N   . SER A 10  ? 0.4615 0.4720 0.3975 0.0169  -0.0549 -0.1010 7   SER A N   
70   C CA  . SER A 10  ? 0.4622 0.4758 0.3771 0.0276  -0.0393 -0.0883 7   SER A CA  
71   C C   . SER A 10  ? 0.4097 0.4137 0.3418 0.0193  -0.0258 -0.0710 7   SER A C   
72   O O   . SER A 10  ? 0.3905 0.3822 0.3451 0.0082  -0.0276 -0.0712 7   SER A O   
73   C CB  . SER A 10  ? 0.5143 0.5225 0.4101 0.0395  -0.0379 -0.1033 7   SER A CB  
74   O OG  . SER A 10  ? 0.5731 0.5607 0.4891 0.0316  -0.0402 -0.1128 7   SER A OG  
80   N N   . PRO A 11  ? 0.3852 0.3950 0.3077 0.0248  -0.0123 -0.0558 8   PRO A N   
81   C CA  . PRO A 11  ? 0.3321 0.3340 0.2711 0.0178  -0.0020 -0.0432 8   PRO A CA  
82   C C   . PRO A 11  ? 0.3894 0.3794 0.3351 0.0180  0.0006  -0.0507 8   PRO A C   
83   O O   . PRO A 11  ? 0.3970 0.3848 0.3315 0.0261  -0.0015 -0.0638 8   PRO A O   
84   C CB  . PRO A 11  ? 0.4435 0.4547 0.3733 0.0238  0.0108  -0.0278 8   PRO A CB  
85   C CG  . PRO A 11  ? 0.5178 0.5402 0.4214 0.0372  0.0110  -0.0317 8   PRO A CG  
86   C CD  . PRO A 11  ? 0.4587 0.4827 0.3568 0.0375  -0.0059 -0.0481 8   PRO A CD  
94   N N   A SER A 12  ? 0.3354 0.3183 0.2985 0.0108  0.0047  -0.0424 9   SER A N   
95   N N   B SER A 12  ? 0.3344 0.3168 0.2978 0.0106  0.0043  -0.0429 9   SER A N   
96   C CA  A SER A 12  ? 0.3705 0.3425 0.3426 0.0116  0.0066  -0.0462 9   SER A CA  
97   C CA  B SER A 12  ? 0.3710 0.3431 0.3426 0.0121  0.0067  -0.0468 9   SER A CA  
98   C C   A SER A 12  ? 0.3489 0.3275 0.3269 0.0134  0.0171  -0.0355 9   SER A C   
99   C C   B SER A 12  ? 0.3481 0.3266 0.3259 0.0134  0.0170  -0.0357 9   SER A C   
100  O O   A SER A 12  ? 0.3309 0.3120 0.3177 0.0072  0.0189  -0.0254 9   SER A O   
101  O O   B SER A 12  ? 0.3317 0.3126 0.3184 0.0072  0.0187  -0.0256 9   SER A O   
102  C CB  A SER A 12  ? 0.3745 0.3330 0.3631 0.0024  0.0002  -0.0461 9   SER A CB  
103  C CB  B SER A 12  ? 0.3674 0.3248 0.3552 0.0035  0.0000  -0.0479 9   SER A CB  
104  O OG  A SER A 12  ? 0.4273 0.3733 0.4228 0.0054  0.0009  -0.0497 9   SER A OG  
105  O OG  B SER A 12  ? 0.4191 0.3690 0.4068 0.0021  -0.0097 -0.0613 9   SER A OG  
116  N N   . TYR A 13  ? 0.3362 0.3185 0.3114 0.0221  0.0234  -0.0392 10  TYR A N   
117  C CA  . TYR A 13  ? 0.2993 0.2921 0.2853 0.0236  0.0332  -0.0301 10  TYR A CA  
118  C C   . TYR A 13  ? 0.3414 0.3296 0.3383 0.0283  0.0329  -0.0352 10  TYR A C   
119  O O   . TYR A 13  ? 0.3483 0.3344 0.3381 0.0380  0.0342  -0.0450 10  TYR A O   
120  C CB  . TYR A 13  ? 0.3395 0.3476 0.3151 0.0312  0.0443  -0.0259 10  TYR A CB  
121  C CG  . TYR A 13  ? 0.3154 0.3372 0.3084 0.0310  0.0559  -0.0155 10  TYR A CG  
122  C CD1 . TYR A 13  ? 0.3484 0.3700 0.3629 0.0217  0.0539  -0.0093 10  TYR A CD1 
123  C CD2 . TYR A 13  ? 0.3766 0.4137 0.3652 0.0406  0.0689  -0.0124 10  TYR A CD2 
124  C CE1 . TYR A 13  ? 0.3309 0.3665 0.3668 0.0200  0.0626  -0.0019 10  TYR A CE1 
125  C CE2 . TYR A 13  ? 0.4524 0.5047 0.4635 0.0388  0.0804  -0.0019 10  TYR A CE2 
126  C CZ  . TYR A 13  ? 0.4692 0.5203 0.5059 0.0274  0.0762  0.0025  10  TYR A CZ  
127  O OH  . TYR A 13  ? 0.4192 0.4863 0.4834 0.0240  0.0854  0.0108  10  TYR A OH  
138  N N   . LEU A 14  ? 0.2892 0.2759 0.3017 0.0233  0.0305  -0.0293 11  LEU A N   
139  C CA  . LEU A 14  ? 0.3149 0.3002 0.3390 0.0293  0.0297  -0.0315 11  LEU A CA  
140  C C   . LEU A 14  ? 0.3074 0.3127 0.3479 0.0305  0.0364  -0.0256 11  LEU A C   
141  O O   . LEU A 14  ? 0.3302 0.3416 0.3802 0.0227  0.0352  -0.0191 11  LEU A O   
142  C CB  . LEU A 14  ? 0.3108 0.2826 0.3398 0.0249  0.0213  -0.0283 11  LEU A CB  
143  C CG  . LEU A 14  ? 0.3429 0.2945 0.3649 0.0226  0.0154  -0.0327 11  LEU A CG  
144  C CD1 . LEU A 14  ? 0.4743 0.4183 0.5009 0.0163  0.0109  -0.0235 11  LEU A CD1 
145  C CD2 . LEU A 14  ? 0.4705 0.4087 0.4937 0.0316  0.0140  -0.0411 11  LEU A CD2 
157  N N   . LYS A 15  ? 0.2874 0.3038 0.3329 0.0403  0.0437  -0.0289 12  LYS A N   
158  C CA  . LYS A 15  ? 0.2901 0.3290 0.3581 0.0411  0.0506  -0.0234 12  LYS A CA  
159  C C   . LYS A 15  ? 0.3373 0.3783 0.4225 0.0439  0.0425  -0.0244 12  LYS A C   
160  O O   . LYS A 15  ? 0.3177 0.3483 0.3989 0.0534  0.0385  -0.0296 12  LYS A O   
161  C CB  . LYS A 15  ? 0.3089 0.3639 0.3770 0.0520  0.0640  -0.0249 12  LYS A CB  
162  C CG  . LYS A 15  ? 0.4841 0.5415 0.5331 0.0514  0.0729  -0.0212 12  LYS A CG  
163  C CD  . LYS A 15  ? 0.6739 0.7345 0.7021 0.0669  0.0810  -0.0293 12  LYS A CD  
164  C CE  . LYS A 15  ? 0.8264 0.8633 0.8368 0.0734  0.0691  -0.0454 12  LYS A CE  
165  N NZ  . LYS A 15  ? 0.5365 0.5534 0.5296 0.0649  0.0574  -0.0494 12  LYS A NZ  
179  N N   . GLY A 16  ? 0.3043 0.3581 0.4085 0.0366  0.0392  -0.0198 13  GLY A N   
180  C CA  . GLY A 16  ? 0.3500 0.4115 0.4705 0.0404  0.0299  -0.0209 13  GLY A CA  
181  C C   . GLY A 16  ? 0.3370 0.4279 0.4890 0.0421  0.0346  -0.0204 13  GLY A C   
182  O O   . GLY A 16  ? 0.3542 0.4586 0.5150 0.0422  0.0479  -0.0179 13  GLY A O   
186  N N   . THR A 17  ? 0.3356 0.4383 0.5053 0.0443  0.0238  -0.0223 14  THR A N   
187  C CA  . THR A 17  ? 0.3121 0.4459 0.5172 0.0473  0.0256  -0.0233 14  THR A CA  
188  C C   . THR A 17  ? 0.3264 0.4776 0.5590 0.0357  0.0168  -0.0251 14  THR A C   
189  O O   . THR A 17  ? 0.3350 0.5151 0.6046 0.0345  0.0194  -0.0257 14  THR A O   
190  C CB  . THR A 17  ? 0.3812 0.5208 0.5907 0.0639  0.0183  -0.0263 14  THR A CB  
191  O OG1 . THR A 17  ? 0.3776 0.5016 0.5703 0.0664  0.0030  -0.0266 14  THR A OG1 
192  C CG2 . THR A 17  ? 0.4463 0.5722 0.6383 0.0766  0.0283  -0.0272 14  THR A CG2 
200  N N   . ASN A 18  ? 0.3185 0.4546 0.5371 0.0277  0.0064  -0.0271 15  ASN A N   
201  C CA  . ASN A 18  ? 0.3267 0.4778 0.5695 0.0202  -0.0066 -0.0336 15  ASN A CA  
202  C C   . ASN A 18  ? 0.3291 0.4809 0.5905 0.0036  -0.0001 -0.0325 15  ASN A C   
203  O O   . ASN A 18  ? 0.3536 0.5156 0.6389 -0.0044 -0.0111 -0.0402 15  ASN A O   
204  C CB  . ASN A 18  ? 0.2783 0.4162 0.4961 0.0247  -0.0234 -0.0384 15  ASN A CB  
205  C CG  . ASN A 18  ? 0.2822 0.3917 0.4671 0.0188  -0.0205 -0.0352 15  ASN A CG  
206  O OD1 . ASN A 18  ? 0.3016 0.4014 0.4845 0.0097  -0.0090 -0.0311 15  ASN A OD1 
207  N ND2 . ASN A 18  ? 0.3443 0.4422 0.5033 0.0257  -0.0304 -0.0358 15  ASN A ND2 
214  N N   . GLY A 19  ? 0.3028 0.4436 0.5539 -0.0007 0.0169  -0.0235 16  GLY A N   
215  C CA  . GLY A 19  ? 0.2840 0.4243 0.5534 -0.0146 0.0262  -0.0182 16  GLY A CA  
216  C C   . GLY A 19  ? 0.3284 0.4436 0.5771 -0.0219 0.0212  -0.0193 16  GLY A C   
217  O O   . GLY A 19  ? 0.3684 0.4785 0.6306 -0.0325 0.0292  -0.0137 16  GLY A O   
221  N N   . HIS A 20  ? 0.2818 0.3817 0.5000 -0.0159 0.0094  -0.0250 17  HIS A N   
222  C CA  . HIS A 20  ? 0.2568 0.3352 0.4536 -0.0202 0.0053  -0.0263 17  HIS A CA  
223  C C   . HIS A 20  ? 0.3261 0.3871 0.4882 -0.0155 0.0135  -0.0187 17  HIS A C   
224  O O   . HIS A 20  ? 0.3369 0.3970 0.4833 -0.0067 0.0139  -0.0178 17  HIS A O   
225  C CB  . HIS A 20  ? 0.2668 0.3434 0.4530 -0.0156 -0.0123 -0.0372 17  HIS A CB  
226  C CG  . HIS A 20  ? 0.3297 0.4248 0.5483 -0.0189 -0.0250 -0.0488 17  HIS A CG  
227  N ND1 . HIS A 20  ? 0.3468 0.4399 0.5887 -0.0301 -0.0293 -0.0562 17  HIS A ND1 
228  C CD2 . HIS A 20  ? 0.3440 0.4609 0.5788 -0.0125 -0.0353 -0.0551 17  HIS A CD2 
229  C CE1 . HIS A 20  ? 0.3372 0.4506 0.6090 -0.0315 -0.0431 -0.0685 17  HIS A CE1 
230  N NE2 . HIS A 20  ? 0.3638 0.4938 0.6315 -0.0204 -0.0471 -0.0676 17  HIS A NE2 
238  N N   . ALA A 21  ? 0.2688 0.3156 0.4208 -0.0209 0.0187  -0.0141 18  ALA A N   
239  C CA  . ALA A 21  ? 0.2250 0.2580 0.3472 -0.0172 0.0243  -0.0083 18  ALA A CA  
240  C C   . ALA A 21  ? 0.2615 0.2800 0.3658 -0.0180 0.0173  -0.0108 18  ALA A C   
241  O O   . ALA A 21  ? 0.2724 0.2873 0.3861 -0.0226 0.0129  -0.0147 18  ALA A O   
242  C CB  . ALA A 21  ? 0.2669 0.2997 0.3902 -0.0197 0.0384  0.0017  18  ALA A CB  
248  N N   . ILE A 22  ? 0.2374 0.2478 0.3181 -0.0132 0.0166  -0.0092 19  ILE A N   
249  C CA  . ILE A 22  ? 0.2309 0.2312 0.2952 -0.0128 0.0123  -0.0094 19  ILE A CA  
250  C C   . ILE A 22  ? 0.2658 0.2595 0.3158 -0.0129 0.0182  -0.0036 19  ILE A C   
251  O O   . ILE A 22  ? 0.2867 0.2805 0.3295 -0.0103 0.0206  -0.0027 19  ILE A O   
252  C CB  . ILE A 22  ? 0.2615 0.2612 0.3150 -0.0072 0.0049  -0.0119 19  ILE A CB  
253  C CG1 . ILE A 22  ? 0.3309 0.3407 0.3969 -0.0047 -0.0033 -0.0188 19  ILE A CG1 
254  C CG2 . ILE A 22  ? 0.2992 0.2920 0.3377 -0.0063 0.0034  -0.0105 19  ILE A CG2 
255  C CD1 . ILE A 22  ? 0.3966 0.4076 0.4502 0.0037  -0.0100 -0.0186 19  ILE A CD1 
267  N N   A LEU A 23  ? 0.2631 0.2513 0.3087 -0.0147 0.0191  -0.0013 20  LEU A N   
268  N N   B LEU A 23  ? 0.2629 0.2513 0.3096 -0.0149 0.0197  -0.0010 20  LEU A N   
269  C CA  A LEU A 23  ? 0.2756 0.2605 0.3086 -0.0137 0.0220  0.0035  20  LEU A CA  
270  C CA  B LEU A 23  ? 0.2759 0.2608 0.3088 -0.0137 0.0217  0.0032  20  LEU A CA  
271  C C   A LEU A 23  ? 0.2772 0.2600 0.3008 -0.0124 0.0174  0.0025  20  LEU A C   
272  C C   B LEU A 23  ? 0.2799 0.2630 0.3041 -0.0123 0.0168  0.0017  20  LEU A C   
273  O O   A LEU A 23  ? 0.2752 0.2565 0.2989 -0.0114 0.0150  0.0009  20  LEU A O   
274  O O   B LEU A 23  ? 0.2866 0.2692 0.3110 -0.0110 0.0134  -0.0008 20  LEU A O   
275  C CB  A LEU A 23  ? 0.2755 0.2571 0.3119 -0.0147 0.0265  0.0087  20  LEU A CB  
276  C CB  B LEU A 23  ? 0.2790 0.2600 0.3131 -0.0143 0.0251  0.0080  20  LEU A CB  
277  C CG  A LEU A 23  ? 0.2884 0.2698 0.3123 -0.0116 0.0287  0.0146  20  LEU A CG  
278  C CG  B LEU A 23  ? 0.2816 0.2636 0.3235 -0.0154 0.0331  0.0146  20  LEU A CG  
279  C CD1 A LEU A 23  ? 0.2402 0.2274 0.2559 -0.0091 0.0322  0.0163  20  LEU A CD1 
280  C CD1 B LEU A 23  ? 0.3220 0.2956 0.3718 -0.0165 0.0358  0.0195  20  LEU A CD1 
281  C CD2 A LEU A 23  ? 0.3408 0.3163 0.3692 -0.0108 0.0328  0.0214  20  LEU A CD2 
282  C CD2 B LEU A 23  ? 0.3509 0.3378 0.3777 -0.0110 0.0367  0.0189  20  LEU A CD2 
305  N N   . LEU A 24  ? 0.2520 0.2348 0.2692 -0.0122 0.0165  0.0030  21  LEU A N   
306  C CA  . LEU A 24  ? 0.2615 0.2438 0.2753 -0.0125 0.0141  0.0045  21  LEU A CA  
307  C C   . LEU A 24  ? 0.2985 0.2841 0.3104 -0.0137 0.0141  0.0066  21  LEU A C   
308  O O   . LEU A 24  ? 0.2789 0.2655 0.2884 -0.0141 0.0131  0.0046  21  LEU A O   
309  C CB  . LEU A 24  ? 0.2734 0.2516 0.2878 -0.0126 0.0124  0.0040  21  LEU A CB  
310  C CG  . LEU A 24  ? 0.2964 0.2737 0.3125 -0.0090 0.0109  0.0029  21  LEU A CG  
311  C CD1 . LEU A 24  ? 0.3291 0.3068 0.3496 -0.0077 0.0119  -0.0012 21  LEU A CD1 
312  C CD2 . LEU A 24  ? 0.3478 0.3206 0.3619 -0.0070 0.0098  0.0077  21  LEU A CD2 
325  N N   . LEU A 25  ? 0.2538 0.2433 0.2665 -0.0128 0.0145  0.0096  22  LEU A N   
326  C CA  . LEU A 25  ? 0.2801 0.2765 0.2939 -0.0122 0.0140  0.0119  22  LEU A CA  
327  C C   . LEU A 25  ? 0.2546 0.2586 0.2756 -0.0145 0.0138  0.0148  22  LEU A C   
328  O O   . LEU A 25  ? 0.2580 0.2633 0.2792 -0.0128 0.0171  0.0180  22  LEU A O   
329  C CB  . LEU A 25  ? 0.2711 0.2669 0.2836 -0.0074 0.0164  0.0137  22  LEU A CB  
330  C CG  . LEU A 25  ? 0.2924 0.2802 0.3039 -0.0070 0.0184  0.0132  22  LEU A CG  
331  C CD1 . LEU A 25  ? 0.3575 0.3391 0.3721 -0.0037 0.0205  0.0143  22  LEU A CD1 
332  C CD2 . LEU A 25  ? 0.3071 0.2975 0.3138 -0.0065 0.0188  0.0156  22  LEU A CD2 
344  N N   . HIS A 26  ? 0.2192 0.2299 0.2468 -0.0179 0.0099  0.0137  23  HIS A N   
345  C CA  . HIS A 26  ? 0.2446 0.2631 0.2866 -0.0232 0.0094  0.0164  23  HIS A CA  
346  C C   . HIS A 26  ? 0.2384 0.2732 0.2891 -0.0205 0.0114  0.0212  23  HIS A C   
347  O O   . HIS A 26  ? 0.2424 0.2802 0.2865 -0.0133 0.0126  0.0219  23  HIS A O   
348  C CB  . HIS A 26  ? 0.2496 0.2670 0.2991 -0.0294 0.0019  0.0094  23  HIS A CB  
349  C CG  . HIS A 26  ? 0.2437 0.2713 0.2907 -0.0269 -0.0056 0.0035  23  HIS A CG  
350  N ND1 . HIS A 26  ? 0.2673 0.3125 0.3280 -0.0279 -0.0099 0.0041  23  HIS A ND1 
351  C CD2 . HIS A 26  ? 0.2786 0.3035 0.3105 -0.0220 -0.0095 -0.0026 23  HIS A CD2 
352  C CE1 . HIS A 26  ? 0.2694 0.3218 0.3218 -0.0230 -0.0178 -0.0018 23  HIS A CE1 
353  N NE2 . HIS A 26  ? 0.2648 0.3047 0.2978 -0.0189 -0.0168 -0.0052 23  HIS A NE2 
361  N N   . SER A 27  ? 0.2408 0.2859 0.3095 -0.0262 0.0127  0.0254  24  SER A N   
362  C CA  . SER A 27  ? 0.2473 0.3118 0.3291 -0.0237 0.0168  0.0315  24  SER A CA  
363  C C   . SER A 27  ? 0.2823 0.3630 0.3759 -0.0237 0.0084  0.0273  24  SER A C   
364  O O   . SER A 27  ? 0.2788 0.3570 0.3719 -0.0273 -0.0014 0.0193  24  SER A O   
365  C CB  . SER A 27  ? 0.2567 0.3283 0.3578 -0.0307 0.0236  0.0404  24  SER A CB  
366  O OG  . SER A 27  ? 0.2859 0.3602 0.4103 -0.0429 0.0169  0.0374  24  SER A OG  
372  N N   . PHE A 28  ? 0.2825 0.3820 0.3861 -0.0178 0.0121  0.0324  25  PHE A N   
373  C CA  . PHE A 28  ? 0.3443 0.4655 0.4637 -0.0162 0.0041  0.0302  25  PHE A CA  
374  C C   . PHE A 28  ? 0.2937 0.4281 0.4423 -0.0296 -0.0022 0.0276  25  PHE A C   
375  O O   . PHE A 28  ? 0.2583 0.3983 0.4269 -0.0372 0.0059  0.0349  25  PHE A O   
376  C CB  . PHE A 28  ? 0.3128 0.4521 0.4396 -0.0058 0.0113  0.0370  25  PHE A CB  
377  C CG  . PHE A 28  ? 0.3245 0.4899 0.4697 -0.0017 0.0030  0.0360  25  PHE A CG  
378  C CD1 . PHE A 28  ? 0.3407 0.5043 0.4738 0.0037  -0.0089 0.0303  25  PHE A CD1 
379  C CD2 . PHE A 28  ? 0.3559 0.5503 0.5304 -0.0016 0.0076  0.0418  25  PHE A CD2 
380  C CE1 . PHE A 28  ? 0.3099 0.4996 0.4580 0.0100  -0.0182 0.0295  25  PHE A CE1 
381  C CE2 . PHE A 28  ? 0.3735 0.5954 0.5675 0.0034  -0.0015 0.0403  25  PHE A CE2 
382  C CZ  . PHE A 28  ? 0.3640 0.5832 0.5437 0.0096  -0.0155 0.0337  25  PHE A CZ  
392  N N   . THR A 29  ? 0.2231 0.3622 0.3745 -0.0320 -0.0166 0.0173  26  THR A N   
393  C CA  . THR A 29  ? 0.2093 0.3569 0.3875 -0.0451 -0.0275 0.0088  26  THR A CA  
394  C C   . THR A 29  ? 0.2776 0.3997 0.4540 -0.0556 -0.0263 0.0051  26  THR A C   
395  O O   . THR A 29  ? 0.3081 0.4314 0.5094 -0.0678 -0.0347 -0.0027 26  THR A O   
396  C CB  . THR A 29  ? 0.2790 0.4549 0.4994 -0.0530 -0.0255 0.0146  26  THR A CB  
397  O OG1 . THR A 29  ? 0.2957 0.4648 0.5280 -0.0600 -0.0097 0.0274  26  THR A OG1 
398  C CG2 . THR A 29  ? 0.3035 0.5070 0.5289 -0.0407 -0.0252 0.0195  26  THR A CG2 
406  N N   . GLY A 30  ? 0.2457 0.3446 0.3952 -0.0508 -0.0175 0.0091  27  GLY A N   
407  C CA  . GLY A 30  ? 0.2526 0.3269 0.3968 -0.0572 -0.0171 0.0055  27  GLY A CA  
408  C C   . GLY A 30  ? 0.2955 0.3583 0.4173 -0.0525 -0.0274 -0.0086 27  GLY A C   
409  O O   . GLY A 30  ? 0.2794 0.3549 0.3930 -0.0462 -0.0363 -0.0155 27  GLY A O   
413  N N   . THR A 31  ? 0.2737 0.3135 0.3838 -0.0535 -0.0251 -0.0116 28  THR A N   
414  C CA  . THR A 31  ? 0.2725 0.3012 0.3584 -0.0468 -0.0308 -0.0231 28  THR A CA  
415  C C   . THR A 31  ? 0.3189 0.3287 0.3900 -0.0434 -0.0209 -0.0173 28  THR A C   
416  O O   . THR A 31  ? 0.2619 0.2672 0.3404 -0.0462 -0.0124 -0.0063 28  THR A O   
417  C CB  . THR A 31  ? 0.2859 0.3086 0.3803 -0.0518 -0.0436 -0.0402 28  THR A CB  
418  O OG1 . THR A 31  ? 0.3359 0.3391 0.4464 -0.0605 -0.0402 -0.0391 28  THR A OG1 
419  C CG2 . THR A 31  ? 0.3312 0.3752 0.4470 -0.0570 -0.0567 -0.0487 28  THR A CG2 
427  N N   A ASN A 32  ? 0.3082 0.3087 0.3592 -0.0367 -0.0221 -0.0247 29  ASN A N   
428  N N   B ASN A 32  ? 0.3084 0.3089 0.3595 -0.0368 -0.0222 -0.0248 29  ASN A N   
429  C CA  A ASN A 32  ? 0.3346 0.3213 0.3757 -0.0333 -0.0138 -0.0198 29  ASN A CA  
430  C CA  B ASN A 32  ? 0.3340 0.3201 0.3757 -0.0336 -0.0140 -0.0200 29  ASN A CA  
431  C C   A ASN A 32  ? 0.3457 0.3156 0.3991 -0.0385 -0.0133 -0.0202 29  ASN A C   
432  C C   B ASN A 32  ? 0.3467 0.3162 0.4015 -0.0391 -0.0138 -0.0208 29  ASN A C   
433  O O   A ASN A 32  ? 0.3565 0.3167 0.4039 -0.0348 -0.0073 -0.0149 29  ASN A O   
434  O O   B ASN A 32  ? 0.3567 0.3157 0.4056 -0.0355 -0.0080 -0.0159 29  ASN A O   
435  C CB  A ASN A 32  ? 0.3582 0.3432 0.3782 -0.0242 -0.0128 -0.0253 29  ASN A CB  
436  C CB  B ASN A 32  ? 0.3587 0.3428 0.3795 -0.0245 -0.0130 -0.0257 29  ASN A CB  
437  C CG  A ASN A 32  ? 0.3780 0.3563 0.3928 -0.0218 -0.0198 -0.0403 29  ASN A CG  
438  C CG  B ASN A 32  ? 0.3303 0.3155 0.3436 -0.0214 -0.0219 -0.0406 29  ASN A CG  
439  O OD1 A ASN A 32  ? 0.3504 0.3236 0.3787 -0.0279 -0.0279 -0.0492 29  ASN A OD1 
440  O OD1 B ASN A 32  ? 0.3254 0.3088 0.3518 -0.0273 -0.0312 -0.0501 29  ASN A OD1 
441  N ND2 A ASN A 32  ? 0.3756 0.3538 0.3722 -0.0126 -0.0160 -0.0434 29  ASN A ND2 
442  N ND2 B ASN A 32  ? 0.3389 0.3278 0.3316 -0.0116 -0.0191 -0.0430 29  ASN A ND2 
455  N N   A ARG A 33  ? 0.3489 0.3153 0.4225 -0.0471 -0.0195 -0.0252 30  ARG A N   
456  N N   B ARG A 33  ? 0.3470 0.3139 0.4224 -0.0479 -0.0201 -0.0256 30  ARG A N   
457  C CA  A ARG A 33  ? 0.3765 0.3254 0.4665 -0.0531 -0.0164 -0.0198 30  ARG A CA  
458  C CA  B ARG A 33  ? 0.3782 0.3282 0.4712 -0.0544 -0.0170 -0.0200 30  ARG A CA  
459  C C   A ARG A 33  ? 0.3864 0.3396 0.4820 -0.0544 -0.0056 -0.0005 30  ARG A C   
460  C C   B ARG A 33  ? 0.3861 0.3392 0.4809 -0.0541 -0.0056 -0.0007 30  ARG A C   
461  O O   A ARG A 33  ? 0.4281 0.3667 0.5291 -0.0549 -0.0002 0.0086  30  ARG A O   
462  O O   B ARG A 33  ? 0.4263 0.3648 0.5230 -0.0531 -0.0002 0.0078  30  ARG A O   
463  C CB  A ARG A 33  ? 0.3987 0.3427 0.5146 -0.0639 -0.0257 -0.0297 30  ARG A CB  
464  C CB  B ARG A 33  ? 0.4002 0.3490 0.5220 -0.0664 -0.0252 -0.0268 30  ARG A CB  
465  C CG  A ARG A 33  ? 0.4041 0.3423 0.5114 -0.0603 -0.0379 -0.0521 30  ARG A CG  
466  C CG  B ARG A 33  ? 0.5065 0.4351 0.6523 -0.0747 -0.0208 -0.0183 30  ARG A CG  
467  C CD  A ARG A 33  ? 0.5345 0.4622 0.6712 -0.0719 -0.0489 -0.0648 30  ARG A CD  
468  C CD  B ARG A 33  ? 0.5617 0.4888 0.7412 -0.0885 -0.0308 -0.0284 30  ARG A CD  
469  N NE  A ARG A 33  ? 0.5574 0.5080 0.7142 -0.0805 -0.0565 -0.0672 30  ARG A NE  
470  N NE  B ARG A 33  ? 0.5299 0.4386 0.7398 -0.0990 -0.0249 -0.0165 30  ARG A NE  
471  C CZ  A ARG A 33  ? 0.6378 0.6070 0.7834 -0.0757 -0.0683 -0.0817 30  ARG A CZ  
472  C CZ  B ARG A 33  ? 0.5433 0.4393 0.7866 -0.1118 -0.0337 -0.0269 30  ARG A CZ  
473  N NH1 A ARG A 33  ? 0.6347 0.6025 0.7475 -0.0624 -0.0723 -0.0942 30  ARG A NH1 
474  N NH1 B ARG A 33  ? 0.6642 0.5647 0.9120 -0.1144 -0.0508 -0.0525 30  ARG A NH1 
475  N NH2 A ARG A 33  ? 0.6338 0.6259 0.8020 -0.0833 -0.0757 -0.0826 30  ARG A NH2 
476  N NH2 B ARG A 33  ? 0.5778 0.4561 0.8512 -0.1219 -0.0254 -0.0112 30  ARG A NH2 
503  N N   . ASP A 34  ? 0.3425 0.3150 0.4350 -0.0529 -0.0021 0.0060  31  ASP A N   
504  C CA  . ASP A 34  ? 0.3823 0.3606 0.4733 -0.0504 0.0084  0.0220  31  ASP A CA  
505  C C   . ASP A 34  ? 0.4098 0.3771 0.4814 -0.0416 0.0127  0.0260  31  ASP A C   
506  O O   . ASP A 34  ? 0.3869 0.3539 0.4561 -0.0384 0.0201  0.0386  31  ASP A O   
507  C CB  . ASP A 34  ? 0.3447 0.3429 0.4289 -0.0458 0.0107  0.0244  31  ASP A CB  
508  C CG  . ASP A 34  ? 0.3841 0.4003 0.4894 -0.0520 0.0083  0.0246  31  ASP A CG  
509  O OD1 . ASP A 34  ? 0.3625 0.3779 0.4915 -0.0620 0.0044  0.0228  31  ASP A OD1 
510  O OD2 . ASP A 34  ? 0.2988 0.3304 0.3982 -0.0461 0.0100  0.0263  31  ASP A OD2 
516  N N   . VAL A 35  ? 0.3033 0.2658 0.3604 -0.0362 0.0085  0.0159  32  VAL A N   
517  C CA  . VAL A 35  ? 0.3081 0.2668 0.3503 -0.0279 0.0110  0.0178  32  VAL A CA  
518  C C   . VAL A 35  ? 0.3532 0.2973 0.3942 -0.0250 0.0084  0.0122  32  VAL A C   
519  O O   . VAL A 35  ? 0.3311 0.2751 0.3634 -0.0180 0.0091  0.0119  32  VAL A O   
520  C CB  . VAL A 35  ? 0.2986 0.2678 0.3289 -0.0233 0.0109  0.0134  32  VAL A CB  
521  C CG1 . VAL A 35  ? 0.3306 0.3121 0.3612 -0.0231 0.0144  0.0197  32  VAL A CG1 
522  C CG2 . VAL A 35  ? 0.3441 0.3147 0.3719 -0.0239 0.0069  0.0038  32  VAL A CG2 
532  N N   . LYS A 36  ? 0.3090 0.2413 0.3612 -0.0299 0.0047  0.0066  33  LYS A N   
533  C CA  . LYS A 36  ? 0.3340 0.2517 0.3846 -0.0250 0.0020  -0.0015 33  LYS A CA  
534  C C   . LYS A 36  ? 0.3254 0.2340 0.3742 -0.0181 0.0058  0.0086  33  LYS A C   
535  O O   . LYS A 36  ? 0.3360 0.2439 0.3777 -0.0096 0.0053  0.0043  33  LYS A O   
536  C CB  . LYS A 36  ? 0.3063 0.2102 0.3713 -0.0317 -0.0037 -0.0107 33  LYS A CB  
537  C CG  . LYS A 36  ? 0.3075 0.1925 0.3716 -0.0253 -0.0066 -0.0211 33  LYS A CG  
538  C CD  . LYS A 36  ? 0.3878 0.2572 0.4666 -0.0316 -0.0143 -0.0343 33  LYS A CD  
539  C CE  . LYS A 36  ? 0.3875 0.2399 0.4603 -0.0217 -0.0175 -0.0490 33  LYS A CE  
540  N NZ  . LYS A 36  ? 0.4029 0.2375 0.4890 -0.0265 -0.0268 -0.0663 33  LYS A NZ  
554  N N   . HIS A 37  ? 0.3345 0.2376 0.3908 -0.0207 0.0098  0.0228  34  HIS A N   
555  C CA  . HIS A 37  ? 0.3080 0.2019 0.3604 -0.0118 0.0126  0.0340  34  HIS A CA  
556  C C   . HIS A 37  ? 0.3247 0.2350 0.3608 -0.0024 0.0127  0.0358  34  HIS A C   
557  O O   . HIS A 37  ? 0.3446 0.2530 0.3761 0.0072  0.0105  0.0352  34  HIS A O   
558  C CB  . HIS A 37  ? 0.3266 0.2123 0.3885 -0.0151 0.0191  0.0526  34  HIS A CB  
559  C CG  . HIS A 37  ? 0.3869 0.2588 0.4451 -0.0045 0.0215  0.0653  34  HIS A CG  
560  N ND1 . HIS A 37  ? 0.3989 0.2811 0.4412 0.0060  0.0253  0.0798  34  HIS A ND1 
561  C CD2 . HIS A 37  ? 0.4006 0.2499 0.4666 -0.0001 0.0194  0.0643  34  HIS A CD2 
562  C CE1 . HIS A 37  ? 0.4214 0.2888 0.4623 0.0162  0.0257  0.0895  34  HIS A CE1 
563  N NE2 . HIS A 37  ? 0.4314 0.2773 0.4881 0.0124  0.0227  0.0810  34  HIS A NE2 
571  N N   . LEU A 38  ? 0.3065 0.2332 0.3359 -0.0047 0.0143  0.0370  35  LEU A N   
572  C CA  . LEU A 38  ? 0.2901 0.2310 0.3067 0.0030  0.0124  0.0353  35  LEU A CA  
573  C C   . LEU A 38  ? 0.2866 0.2322 0.3043 0.0047  0.0082  0.0222  35  LEU A C   
574  O O   . LEU A 38  ? 0.3247 0.2764 0.3401 0.0122  0.0050  0.0203  35  LEU A O   
575  C CB  . LEU A 38  ? 0.3277 0.2819 0.3389 0.0004  0.0150  0.0368  35  LEU A CB  
576  C CG  . LEU A 38  ? 0.3575 0.3241 0.3577 0.0070  0.0115  0.0313  35  LEU A CG  
577  C CD1 . LEU A 38  ? 0.3879 0.3571 0.3776 0.0183  0.0089  0.0367  35  LEU A CD1 
578  C CD2 . LEU A 38  ? 0.3936 0.3695 0.3893 0.0053  0.0144  0.0310  35  LEU A CD2 
590  N N   . ALA A 39  ? 0.3123 0.2564 0.3347 -0.0014 0.0083  0.0137  36  ALA A N   
591  C CA  . ALA A 39  ? 0.2896 0.2390 0.3130 0.0013  0.0073  0.0042  36  ALA A CA  
592  C C   . ALA A 39  ? 0.2844 0.2269 0.3119 0.0091  0.0061  0.0025  36  ALA A C   
593  O O   . ALA A 39  ? 0.3103 0.2628 0.3408 0.0148  0.0054  -0.0009 36  ALA A O   
594  C CB  . ALA A 39  ? 0.3182 0.2672 0.3413 -0.0038 0.0080  -0.0033 36  ALA A CB  
600  N N   . ALA A 40  ? 0.2913 0.2166 0.3220 0.0095  0.0058  0.0042  37  ALA A N   
601  C CA  . ALA A 40  ? 0.3203 0.2356 0.3553 0.0188  0.0047  0.0027  37  ALA A CA  
602  C C   . ALA A 40  ? 0.3221 0.2441 0.3556 0.0280  0.0029  0.0118  37  ALA A C   
603  O O   . ALA A 40  ? 0.3294 0.2573 0.3671 0.0375  0.0011  0.0084  37  ALA A O   
604  C CB  . ALA A 40  ? 0.3288 0.2199 0.3702 0.0163  0.0043  0.0036  37  ALA A CB  
610  N N   . GLU A 41  ? 0.3251 0.2485 0.3523 0.0270  0.0031  0.0232  38  GLU A N   
611  C CA  . GLU A 41  ? 0.3318 0.2633 0.3531 0.0382  -0.0003 0.0310  38  GLU A CA  
612  C C   . GLU A 41  ? 0.3061 0.2607 0.3281 0.0406  -0.0052 0.0220  38  GLU A C   
613  O O   . GLU A 41  ? 0.3392 0.3040 0.3642 0.0511  -0.0108 0.0212  38  GLU A O   
614  C CB  . GLU A 41  ? 0.3391 0.2683 0.3498 0.0383  0.0026  0.0457  38  GLU A CB  
615  C CG  . GLU A 41  ? 0.3870 0.2928 0.4025 0.0376  0.0081  0.0596  38  GLU A CG  
616  C CD  . GLU A 41  ? 0.4928 0.3860 0.5099 0.0509  0.0063  0.0674  38  GLU A CD  
617  O OE1 . GLU A 41  ? 0.4829 0.3890 0.4895 0.0640  0.0017  0.0720  38  GLU A OE1 
618  O OE2 . GLU A 41  ? 0.5858 0.4554 0.6147 0.0492  0.0087  0.0693  38  GLU A OE2 
625  N N   . LEU A 42  ? 0.3212 0.2846 0.3433 0.0312  -0.0039 0.0153  39  LEU A N   
626  C CA  . LEU A 42  ? 0.3211 0.3032 0.3500 0.0309  -0.0078 0.0064  39  LEU A CA  
627  C C   . LEU A 42  ? 0.2916 0.2799 0.3354 0.0333  -0.0069 -0.0004 39  LEU A C   
628  O O   . LEU A 42  ? 0.2942 0.2990 0.3495 0.0378  -0.0116 -0.0046 39  LEU A O   
629  C CB  . LEU A 42  ? 0.3175 0.3028 0.3450 0.0207  -0.0051 0.0025  39  LEU A CB  
630  C CG  . LEU A 42  ? 0.3229 0.3104 0.3379 0.0213  -0.0072 0.0057  39  LEU A CG  
631  C CD1 . LEU A 42  ? 0.3668 0.3520 0.3796 0.0128  -0.0027 0.0046  39  LEU A CD1 
632  C CD2 . LEU A 42  ? 0.3799 0.3822 0.3953 0.0273  -0.0162 -0.0010 39  LEU A CD2 
644  N N   . ASN A 43  ? 0.3032 0.2807 0.3481 0.0309  -0.0009 -0.0025 40  ASN A N   
645  C CA  . ASN A 43  ? 0.2842 0.2691 0.3407 0.0359  0.0020  -0.0087 40  ASN A CA  
646  C C   . ASN A 43  ? 0.3449 0.3314 0.4081 0.0489  -0.0022 -0.0070 40  ASN A C   
647  O O   . ASN A 43  ? 0.3355 0.3392 0.4136 0.0549  -0.0021 -0.0112 40  ASN A O   
648  C CB  . ASN A 43  ? 0.2835 0.2553 0.3343 0.0336  0.0079  -0.0133 40  ASN A CB  
649  C CG  . ASN A 43  ? 0.3234 0.3024 0.3820 0.0420  0.0125  -0.0200 40  ASN A CG  
650  O OD1 . ASN A 43  ? 0.3260 0.2911 0.3831 0.0501  0.0123  -0.0233 40  ASN A OD1 
651  N ND2 . ASN A 43  ? 0.3241 0.3232 0.3915 0.0402  0.0180  -0.0219 40  ASN A ND2 
658  N N   . ASP A 44  ? 0.3394 0.3088 0.3937 0.0542  -0.0050 0.0008  41  ASP A N   
659  C CA  . ASP A 44  ? 0.3773 0.3469 0.4364 0.0688  -0.0094 0.0049  41  ASP A CA  
660  C C   . ASP A 44  ? 0.3994 0.3936 0.4635 0.0748  -0.0179 0.0056  41  ASP A C   
661  O O   . ASP A 44  ? 0.4183 0.4213 0.4908 0.0882  -0.0229 0.0067  41  ASP A O   
662  C CB  . ASP A 44  ? 0.3830 0.3262 0.4319 0.0726  -0.0091 0.0164  41  ASP A CB  
663  C CG  . ASP A 44  ? 0.5227 0.4417 0.5753 0.0721  -0.0041 0.0118  41  ASP A CG  
664  O OD1 . ASP A 44  ? 0.5614 0.4869 0.6206 0.0729  -0.0013 -0.0006 41  ASP A OD1 
665  O OD2 . ASP A 44  ? 0.6121 0.5065 0.6615 0.0708  -0.0027 0.0201  41  ASP A OD2 
670  N N   . GLN A 45  ? 0.3801 0.3858 0.4404 0.0662  -0.0209 0.0033  42  GLN A N   
671  C CA  . GLN A 45  ? 0.3931 0.4238 0.4615 0.0702  -0.0311 -0.0014 42  GLN A CA  
672  C C   . GLN A 45  ? 0.3939 0.4462 0.4878 0.0633  -0.0303 -0.0122 42  GLN A C   
673  O O   . GLN A 45  ? 0.4109 0.4851 0.5184 0.0638  -0.0399 -0.0187 42  GLN A O   
674  C CB  . GLN A 45  ? 0.4243 0.4554 0.4758 0.0661  -0.0357 -0.0003 42  GLN A CB  
675  C CG  . GLN A 45  ? 0.4712 0.4864 0.4991 0.0738  -0.0349 0.0132  42  GLN A CG  
676  C CD  . GLN A 45  ? 0.5480 0.5742 0.5686 0.0913  -0.0452 0.0184  42  GLN A CD  
677  O OE1 . GLN A 45  ? 0.5158 0.5629 0.5354 0.0957  -0.0566 0.0104  42  GLN A OE1 
678  N NE2 . GLN A 45  ? 0.6757 0.6877 0.6922 0.1021  -0.0425 0.0309  42  GLN A NE2 
687  N N   . GLY A 46  ? 0.3456 0.3550 0.4327 0.0707  -0.0447 -0.0463 43  GLY A N   
688  C CA  . GLY A 46  ? 0.3771 0.4198 0.4934 0.0706  -0.0328 -0.0512 43  GLY A CA  
689  C C   . GLY A 46  ? 0.3616 0.4108 0.4806 0.0561  -0.0177 -0.0458 43  GLY A C   
690  O O   . GLY A 46  ? 0.3241 0.3970 0.4622 0.0552  -0.0062 -0.0484 43  GLY A O   
694  N N   . PHE A 47  ? 0.2820 0.3117 0.3822 0.0451  -0.0173 -0.0383 44  PHE A N   
695  C CA  . PHE A 47  ? 0.2831 0.3177 0.3856 0.0325  -0.0052 -0.0333 44  PHE A CA  
696  C C   . PHE A 47  ? 0.3311 0.3602 0.4228 0.0338  0.0044  -0.0318 44  PHE A C   
697  O O   . PHE A 47  ? 0.2897 0.3014 0.3633 0.0413  0.0003  -0.0327 44  PHE A O   
698  C CB  . PHE A 47  ? 0.3088 0.3274 0.3963 0.0222  -0.0085 -0.0269 44  PHE A CB  
699  C CG  . PHE A 47  ? 0.3092 0.3339 0.4060 0.0194  -0.0160 -0.0284 44  PHE A CG  
700  C CD1 . PHE A 47  ? 0.3443 0.3862 0.4608 0.0120  -0.0110 -0.0295 44  PHE A CD1 
701  C CD2 . PHE A 47  ? 0.3120 0.3236 0.3961 0.0237  -0.0287 -0.0287 44  PHE A CD2 
702  C CE1 . PHE A 47  ? 0.3329 0.3796 0.4573 0.0095  -0.0191 -0.0321 44  PHE A CE1 
703  C CE2 . PHE A 47  ? 0.3749 0.3924 0.4660 0.0218  -0.0361 -0.0307 44  PHE A CE2 
704  C CZ  . PHE A 47  ? 0.3451 0.3803 0.4565 0.0150  -0.0315 -0.0330 44  PHE A CZ  
714  N N   . SER A 48  ? 0.2864 0.3287 0.3877 0.0264  0.0167  -0.0295 45  SER A N   
715  C CA  . SER A 48  ? 0.2902 0.3236 0.3764 0.0246  0.0254  -0.0262 45  SER A CA  
716  C C   . SER A 48  ? 0.3097 0.3252 0.3795 0.0150  0.0234  -0.0192 45  SER A C   
717  O O   . SER A 48  ? 0.3046 0.3229 0.3811 0.0070  0.0224  -0.0165 45  SER A O   
718  C CB  . SER A 48  ? 0.2515 0.3055 0.3524 0.0210  0.0394  -0.0259 45  SER A CB  
719  O OG  . SER A 48  ? 0.2939 0.3680 0.4104 0.0308  0.0423  -0.0332 45  SER A OG  
725  N N   . CYS A 49  ? 0.2615 0.2593 0.3102 0.0161  0.0222  -0.0171 46  CYS A N   
726  C CA  . CYS A 49  ? 0.2763 0.2600 0.3104 0.0079  0.0197  -0.0113 46  CYS A CA  
727  C C   . CYS A 49  ? 0.3434 0.3214 0.3652 0.0060  0.0263  -0.0086 46  CYS A C   
728  O O   . CYS A 49  ? 0.3501 0.3238 0.3634 0.0126  0.0280  -0.0116 46  CYS A O   
729  C CB  . CYS A 49  ? 0.3185 0.2842 0.3370 0.0094  0.0086  -0.0111 46  CYS A CB  
730  S SG  . CYS A 49  ? 0.3388 0.3078 0.3664 0.0115  -0.0005 -0.0132 46  CYS A SG  
736  N N   . TYR A 50  ? 0.2982 0.2757 0.3179 -0.0019 0.0293  -0.0035 47  TYR A N   
737  C CA  . TYR A 50  ? 0.2943 0.2656 0.3010 -0.0036 0.0337  -0.0005 47  TYR A CA  
738  C C   . TYR A 50  ? 0.3272 0.2905 0.3247 -0.0096 0.0282  0.0033  47  TYR A C   
739  O O   . TYR A 50  ? 0.2933 0.2614 0.2985 -0.0141 0.0272  0.0052  47  TYR A O   
740  C CB  . TYR A 50  ? 0.2802 0.2616 0.2948 -0.0060 0.0438  0.0020  47  TYR A CB  
741  C CG  . TYR A 50  ? 0.3026 0.2770 0.3013 -0.0057 0.0484  0.0048  47  TYR A CG  
742  C CD1 . TYR A 50  ? 0.3821 0.3546 0.3711 0.0007  0.0520  0.0016  47  TYR A CD1 
743  C CD2 . TYR A 50  ? 0.3773 0.3474 0.3705 -0.0107 0.0492  0.0101  47  TYR A CD2 
744  C CE1 . TYR A 50  ? 0.4129 0.3786 0.3854 0.0013  0.0559  0.0039  47  TYR A CE1 
745  C CE2 . TYR A 50  ? 0.4379 0.4012 0.4154 -0.0097 0.0525  0.0128  47  TYR A CE2 
746  C CZ  . TYR A 50  ? 0.3907 0.3516 0.3571 -0.0042 0.0557  0.0099  47  TYR A CZ  
747  O OH  . TYR A 50  ? 0.4128 0.3660 0.3605 -0.0026 0.0585  0.0121  47  TYR A OH  
757  N N   . ALA A 51  ? 0.3019 0.2539 0.2834 -0.0096 0.0244  0.0036  48  ALA A N   
758  C CA  . ALA A 51  ? 0.2877 0.2352 0.2618 -0.0159 0.0188  0.0066  48  ALA A CA  
759  C C   . ALA A 51  ? 0.3483 0.2925 0.3118 -0.0162 0.0204  0.0083  48  ALA A C   
760  O O   . ALA A 51  ? 0.3558 0.2895 0.3057 -0.0145 0.0172  0.0064  48  ALA A O   
761  C CB  . ALA A 51  ? 0.3502 0.2866 0.3150 -0.0178 0.0103  0.0057  48  ALA A CB  
767  N N   . PRO A 52  ? 0.3335 0.2842 0.3010 -0.0178 0.0242  0.0114  49  PRO A N   
768  C CA  . PRO A 52  ? 0.3135 0.2605 0.2695 -0.0176 0.0238  0.0133  49  PRO A CA  
769  C C   . PRO A 52  ? 0.3448 0.2916 0.2961 -0.0224 0.0157  0.0137  49  PRO A C   
770  O O   . PRO A 52  ? 0.3478 0.2987 0.3052 -0.0269 0.0120  0.0136  49  PRO A O   
771  C CB  . PRO A 52  ? 0.3390 0.2912 0.3014 -0.0172 0.0292  0.0168  49  PRO A CB  
772  C CG  . PRO A 52  ? 0.3535 0.3132 0.3307 -0.0198 0.0285  0.0164  49  PRO A CG  
773  C CD  . PRO A 52  ? 0.3450 0.3047 0.3265 -0.0193 0.0276  0.0130  49  PRO A CD  
781  N N   . ASN A 53  ? 0.3440 0.2876 0.2846 -0.0219 0.0130  0.0145  50  ASN A N   
782  C CA  . ASN A 53  ? 0.3324 0.2801 0.2712 -0.0270 0.0054  0.0148  50  ASN A CA  
783  C C   . ASN A 53  ? 0.3423 0.2973 0.2826 -0.0244 0.0053  0.0171  50  ASN A C   
784  O O   . ASN A 53  ? 0.3552 0.3035 0.2861 -0.0193 0.0079  0.0185  50  ASN A O   
785  C CB  . ASN A 53  ? 0.4070 0.3427 0.3306 -0.0287 -0.0009 0.0122  50  ASN A CB  
786  C CG  . ASN A 53  ? 0.4928 0.4327 0.4177 -0.0376 -0.0090 0.0122  50  ASN A CG  
787  O OD1 . ASN A 53  ? 0.4890 0.4233 0.4134 -0.0433 -0.0119 0.0117  50  ASN A OD1 
788  N ND2 . ASN A 53  ? 0.5965 0.5458 0.5222 -0.0394 -0.0134 0.0128  50  ASN A ND2 
795  N N   . TYR A 54  ? 0.3210 0.2895 0.2719 -0.0270 0.0022  0.0175  51  TYR A N   
796  C CA  . TYR A 54  ? 0.3192 0.2943 0.2722 -0.0223 0.0008  0.0189  51  TYR A CA  
797  C C   . TYR A 54  ? 0.3360 0.3080 0.2768 -0.0214 -0.0059 0.0186  51  TYR A C   
798  O O   . TYR A 54  ? 0.3586 0.3317 0.2961 -0.0274 -0.0117 0.0165  51  TYR A O   
799  C CB  . TYR A 54  ? 0.3136 0.3071 0.2811 -0.0236 -0.0015 0.0178  51  TYR A CB  
800  C CG  . TYR A 54  ? 0.2751 0.2729 0.2531 -0.0252 0.0034  0.0171  51  TYR A CG  
801  C CD1 . TYR A 54  ? 0.3452 0.3332 0.3240 -0.0220 0.0092  0.0180  51  TYR A CD1 
802  C CD2 . TYR A 54  ? 0.3540 0.3665 0.3406 -0.0306 0.0020  0.0156  51  TYR A CD2 
803  C CE1 . TYR A 54  ? 0.3030 0.2949 0.2910 -0.0234 0.0121  0.0166  51  TYR A CE1 
804  C CE2 . TYR A 54  ? 0.3227 0.3381 0.3160 -0.0315 0.0059  0.0147  51  TYR A CE2 
805  C CZ  . TYR A 54  ? 0.3059 0.3101 0.2994 -0.0276 0.0101  0.0149  51  TYR A CZ  
806  O OH  . TYR A 54  ? 0.2993 0.3064 0.2990 -0.0286 0.0125  0.0134  51  TYR A OH  
817  N N   . PRO A 55  ? 0.3410 0.3071 0.2732 -0.0145 -0.0061 0.0208  52  PRO A N   
818  C CA  . PRO A 55  ? 0.3336 0.2968 0.2526 -0.0127 -0.0140 0.0203  52  PRO A CA  
819  C C   . PRO A 55  ? 0.3713 0.3532 0.3015 -0.0166 -0.0231 0.0176  52  PRO A C   
820  O O   . PRO A 55  ? 0.3876 0.3860 0.3342 -0.0167 -0.0227 0.0170  52  PRO A O   
821  C CB  . PRO A 55  ? 0.4328 0.3875 0.3423 -0.0041 -0.0127 0.0243  52  PRO A CB  
822  C CG  . PRO A 55  ? 0.4244 0.3725 0.3382 -0.0032 -0.0025 0.0272  52  PRO A CG  
823  C CD  . PRO A 55  ? 0.3442 0.3016 0.2745 -0.0092 0.0011  0.0244  52  PRO A CD  
831  N N   . GLY A 56  ? 0.3549 0.3351 0.2761 -0.0204 -0.0312 0.0152  53  GLY A N   
832  C CA  . GLY A 56  ? 0.4109 0.4104 0.3430 -0.0265 -0.0404 0.0124  53  GLY A CA  
833  C C   . GLY A 56  ? 0.3770 0.3833 0.3185 -0.0390 -0.0400 0.0111  53  GLY A C   
834  O O   . GLY A 56  ? 0.4020 0.4197 0.3484 -0.0478 -0.0478 0.0090  53  GLY A O   
838  N N   . HIS A 57  ? 0.3662 0.3652 0.3098 -0.0407 -0.0316 0.0125  54  HIS A N   
839  C CA  . HIS A 57  ? 0.3592 0.3626 0.3096 -0.0522 -0.0314 0.0123  54  HIS A CA  
840  C C   . HIS A 57  ? 0.4192 0.4022 0.3538 -0.0586 -0.0366 0.0108  54  HIS A C   
841  O O   . HIS A 57  ? 0.5089 0.4716 0.4286 -0.0522 -0.0346 0.0100  54  HIS A O   
842  C CB  . HIS A 57  ? 0.3551 0.3570 0.3119 -0.0503 -0.0222 0.0140  54  HIS A CB  
843  C CG  . HIS A 57  ? 0.3453 0.3687 0.3186 -0.0473 -0.0187 0.0143  54  HIS A CG  
844  N ND1 . HIS A 57  ? 0.3604 0.3910 0.3377 -0.0371 -0.0187 0.0139  54  HIS A ND1 
845  C CD2 . HIS A 57  ? 0.3355 0.3743 0.3205 -0.0528 -0.0156 0.0144  54  HIS A CD2 
846  C CE1 . HIS A 57  ? 0.3640 0.4123 0.3554 -0.0352 -0.0158 0.0129  54  HIS A CE1 
847  N NE2 . HIS A 57  ? 0.3237 0.3788 0.3201 -0.0448 -0.0133 0.0131  54  HIS A NE2 
855  N N   . GLY A 58  ? 0.4003 0.3889 0.3375 -0.0714 -0.0434 0.0102  55  GLY A N   
856  C CA  . GLY A 58  ? 0.4540 0.4215 0.3750 -0.0782 -0.0512 0.0081  55  GLY A CA  
857  C C   . GLY A 58  ? 0.4965 0.4680 0.4132 -0.0813 -0.0621 0.0050  55  GLY A C   
858  O O   . GLY A 58  ? 0.5259 0.4806 0.4297 -0.0891 -0.0706 0.0025  55  GLY A O   
862  N N   . LEU A 59  ? 0.4256 0.4172 0.3516 -0.0747 -0.0634 0.0047  56  LEU A N   
863  C CA  . LEU A 59  ? 0.4063 0.4039 0.3289 -0.0758 -0.0749 0.0015  56  LEU A CA  
864  C C   . LEU A 59  ? 0.4417 0.4711 0.3863 -0.0875 -0.0806 0.0010  56  LEU A C   
865  O O   . LEU A 59  ? 0.4422 0.4924 0.4051 -0.0916 -0.0738 0.0034  56  LEU A O   
866  C CB  . LEU A 59  ? 0.5152 0.5135 0.4318 -0.0596 -0.0743 0.0015  56  LEU A CB  
867  C CG  . LEU A 59  ? 0.5062 0.4783 0.4028 -0.0483 -0.0667 0.0027  56  LEU A CG  
868  C CD1 . LEU A 59  ? 0.5010 0.4742 0.3903 -0.0350 -0.0676 0.0040  56  LEU A CD1 
869  C CD2 . LEU A 59  ? 0.6396 0.5852 0.5139 -0.0510 -0.0708 -0.0009 56  LEU A CD2 
881  N N   . LEU A 60  ? 0.4975 0.5325 0.4403 -0.0926 -0.0933 -0.0026 57  LEU A N   
882  C CA  . LEU A 60  ? 0.5108 0.5818 0.4774 -0.1027 -0.0995 -0.0039 57  LEU A CA  
883  C C   . LEU A 60  ? 0.5054 0.6056 0.4909 -0.0898 -0.0944 -0.0034 57  LEU A C   
884  O O   . LEU A 60  ? 0.4203 0.5094 0.3966 -0.0730 -0.0909 -0.0027 57  LEU A O   
885  C CB  . LEU A 60  ? 0.5398 0.6114 0.5007 -0.1079 -0.1156 -0.0088 57  LEU A CB  
886  C CG  . LEU A 60  ? 0.6805 0.7226 0.6230 -0.1223 -0.1226 -0.0103 57  LEU A CG  
887  C CD1 . LEU A 60  ? 0.6737 0.7138 0.6080 -0.1261 -0.1398 -0.0162 57  LEU A CD1 
888  C CD2 . LEU A 60  ? 0.7168 0.7672 0.6723 -0.1430 -0.1195 -0.0070 57  LEU A CD2 
900  N N   . LEU A 61  ? 0.4897 0.6272 0.5012 -0.0979 -0.0941 -0.0041 58  LEU A N   
901  C CA  . LEU A 61  ? 0.4239 0.5892 0.4542 -0.0853 -0.0879 -0.0045 58  LEU A CA  
902  C C   . LEU A 61  ? 0.3789 0.5451 0.4052 -0.0665 -0.0951 -0.0070 58  LEU A C   
903  O O   . LEU A 61  ? 0.4273 0.5908 0.4533 -0.0508 -0.0890 -0.0059 58  LEU A O   
904  C CB  . LEU A 61  ? 0.4942 0.7043 0.5536 -0.0966 -0.0876 -0.0063 58  LEU A CB  
905  C CG  . LEU A 61  ? 0.5158 0.7525 0.5934 -0.0848 -0.0778 -0.0070 58  LEU A CG  
906  C CD1 . LEU A 61  ? 0.4516 0.6705 0.5214 -0.0838 -0.0642 -0.0029 58  LEU A CD1 
907  C CD2 . LEU A 61  ? 0.5822 0.8688 0.6895 -0.0950 -0.0782 -0.0101 58  LEU A CD2 
919  N N   . LYS A 62  ? 0.3980 0.5675 0.4209 -0.0679 -0.1092 -0.0105 59  LYS A N   
920  C CA  . LYS A 62  ? 0.4744 0.6456 0.4925 -0.0497 -0.1177 -0.0125 59  LYS A CA  
921  C C   . LYS A 62  ? 0.5010 0.6321 0.4903 -0.0362 -0.1127 -0.0086 59  LYS A C   
922  O O   . LYS A 62  ? 0.5070 0.6360 0.4933 -0.0195 -0.1123 -0.0074 59  LYS A O   
923  C CB  . LYS A 62  ? 0.5549 0.7358 0.5727 -0.0545 -0.1350 -0.0173 59  LYS A CB  
924  C CG  . LYS A 62  ? 0.8702 1.0599 0.8868 -0.0355 -0.1462 -0.0198 59  LYS A CG  
925  C CD  . LYS A 62  ? 1.0971 1.2952 1.1118 -0.0409 -0.1649 -0.0251 59  LYS A CD  
926  C CE  . LYS A 62  ? 0.9313 1.1233 0.9322 -0.0205 -0.1773 -0.0264 59  LYS A CE  
927  N NZ  . LYS A 62  ? 1.1404 1.3698 1.1680 -0.0071 -0.1808 -0.0291 59  LYS A NZ  
941  N N   . ASP A 63  ? 0.4014 0.5005 0.3694 -0.0431 -0.1084 -0.0065 60  ASP A N   
942  C CA  . ASP A 63  ? 0.3904 0.4561 0.3343 -0.0319 -0.1006 -0.0026 60  ASP A CA  
943  C C   . ASP A 63  ? 0.3912 0.4571 0.3443 -0.0278 -0.0861 0.0011  60  ASP A C   
944  O O   . ASP A 63  ? 0.3862 0.4394 0.3305 -0.0150 -0.0811 0.0042  60  ASP A O   
945  C CB  . ASP A 63  ? 0.4034 0.4389 0.3240 -0.0392 -0.1004 -0.0031 60  ASP A CB  
946  C CG  . ASP A 63  ? 0.5449 0.5753 0.4521 -0.0423 -0.1159 -0.0077 60  ASP A CG  
947  O OD1 . ASP A 63  ? 0.4700 0.5089 0.3748 -0.0331 -0.1257 -0.0090 60  ASP A OD1 
948  O OD2 . ASP A 63  ? 0.5363 0.5530 0.4345 -0.0538 -0.1193 -0.0103 60  ASP A OD2 
954  N N   . PHE A 64  ? 0.3702 0.4490 0.3393 -0.0391 -0.0796 0.0012  61  PHE A N   
955  C CA  . PHE A 64  ? 0.3568 0.4379 0.3352 -0.0360 -0.0671 0.0037  61  PHE A CA  
956  C C   . PHE A 64  ? 0.3479 0.4438 0.3369 -0.0216 -0.0668 0.0033  61  PHE A C   
957  O O   . PHE A 64  ? 0.3151 0.3975 0.2994 -0.0128 -0.0591 0.0059  61  PHE A O   
958  C CB  . PHE A 64  ? 0.3660 0.4655 0.3609 -0.0509 -0.0633 0.0033  61  PHE A CB  
959  C CG  . PHE A 64  ? 0.3641 0.4677 0.3680 -0.0491 -0.0515 0.0052  61  PHE A CG  
960  C CD1 . PHE A 64  ? 0.3646 0.4922 0.3854 -0.0405 -0.0488 0.0034  61  PHE A CD1 
961  C CD2 . PHE A 64  ? 0.4143 0.4981 0.4095 -0.0556 -0.0442 0.0078  61  PHE A CD2 
962  C CE1 . PHE A 64  ? 0.3910 0.5213 0.4182 -0.0390 -0.0388 0.0042  61  PHE A CE1 
963  C CE2 . PHE A 64  ? 0.3401 0.4281 0.3429 -0.0544 -0.0348 0.0091  61  PHE A CE2 
964  C CZ  . PHE A 64  ? 0.3460 0.4570 0.3642 -0.0466 -0.0321 0.0072  61  PHE A CZ  
974  N N   . MET A 65  ? 0.3401 0.4631 0.3432 -0.0185 -0.0762 -0.0004 62  MET A N   
975  C CA  . MET A 65  ? 0.3629 0.5018 0.3778 -0.0034 -0.0771 -0.0021 62  MET A CA  
976  C C   . MET A 65  ? 0.4188 0.5359 0.4151 0.0123  -0.0833 0.0000  62  MET A C   
977  O O   . MET A 65  ? 0.4055 0.5315 0.4084 0.0266  -0.0868 -0.0015 62  MET A O   
978  C CB  . MET A 65  ? 0.4644 0.6462 0.5054 -0.0052 -0.0840 -0.0077 62  MET A CB  
979  C CG  . MET A 65  ? 0.4940 0.6990 0.5532 -0.0214 -0.0759 -0.0086 62  MET A CG  
980  S SD  . MET A 65  ? 0.4848 0.7473 0.5782 -0.0243 -0.0808 -0.0153 62  MET A SD  
981  C CE  . MET A 65  ? 0.4757 0.7426 0.5665 -0.0331 -0.0975 -0.0172 62  MET A CE  
991  N N   . THR A 66  ? 0.3534 0.4407 0.3247 0.0109  -0.0845 0.0034  63  THR A N   
992  C CA  . THR A 66  ? 0.3584 0.4199 0.3076 0.0246  -0.0871 0.0074  63  THR A CA  
993  C C   . THR A 66  ? 0.3623 0.3988 0.3013 0.0267  -0.0738 0.0127  63  THR A C   
994  O O   . THR A 66  ? 0.4299 0.4418 0.3489 0.0353  -0.0733 0.0176  63  THR A O   
995  C CB  . THR A 66  ? 0.4023 0.4457 0.3273 0.0235  -0.0954 0.0082  63  THR A CB  
996  O OG1 . THR A 66  ? 0.4045 0.4291 0.3168 0.0126  -0.0872 0.0096  63  THR A OG1 
997  C CG2 . THR A 66  ? 0.4146 0.4832 0.3506 0.0205  -0.1101 0.0024  63  THR A CG2 
1005 N N   . TYR A 67  ? 0.3457 0.3881 0.2977 0.0182  -0.0634 0.0122  64  TYR A N   
1006 C CA  . TYR A 67  ? 0.3438 0.3681 0.2916 0.0195  -0.0517 0.0160  64  TYR A CA  
1007 C C   . TYR A 67  ? 0.3760 0.4192 0.3451 0.0226  -0.0485 0.0130  64  TYR A C   
1008 O O   . TYR A 67  ? 0.3921 0.4638 0.3797 0.0197  -0.0517 0.0083  64  TYR A O   
1009 C CB  . TYR A 67  ? 0.3603 0.3734 0.3031 0.0080  -0.0429 0.0172  64  TYR A CB  
1010 C CG  . TYR A 67  ? 0.3632 0.3577 0.2843 0.0054  -0.0450 0.0186  64  TYR A CG  
1011 C CD1 . TYR A 67  ? 0.3662 0.3680 0.2857 -0.0014 -0.0532 0.0150  64  TYR A CD1 
1012 C CD2 . TYR A 67  ? 0.3985 0.3686 0.3003 0.0095  -0.0386 0.0233  64  TYR A CD2 
1013 C CE1 . TYR A 67  ? 0.4271 0.4095 0.3240 -0.0026 -0.0555 0.0150  64  TYR A CE1 
1014 C CE2 . TYR A 67  ? 0.4062 0.3601 0.2861 0.0083  -0.0395 0.0237  64  TYR A CE2 
1015 C CZ  . TYR A 67  ? 0.4417 0.4012 0.3190 0.0030  -0.0481 0.0191  64  TYR A CZ  
1016 O OH  . TYR A 67  ? 0.4700 0.4122 0.3241 0.0030  -0.0494 0.0183  64  TYR A OH  
1026 N N   . ASN A 68  ? 0.3866 0.4143 0.3526 0.0283  -0.0420 0.0156  65  ASN A N   
1027 C CA  . ASN A 68  ? 0.3508 0.3937 0.3342 0.0331  -0.0396 0.0117  65  ASN A CA  
1028 C C   . ASN A 68  ? 0.3728 0.3990 0.3544 0.0296  -0.0292 0.0139  65  ASN A C   
1029 O O   . ASN A 68  ? 0.3491 0.3563 0.3191 0.0231  -0.0235 0.0182  65  ASN A O   
1030 C CB  . ASN A 68  ? 0.3703 0.4143 0.3539 0.0493  -0.0481 0.0100  65  ASN A CB  
1031 C CG  . ASN A 68  ? 0.4755 0.4848 0.4371 0.0565  -0.0491 0.0164  65  ASN A CG  
1032 O OD1 . ASN A 68  ? 0.5151 0.5032 0.4691 0.0524  -0.0407 0.0204  65  ASN A OD1 
1033 N ND2 . ASN A 68  ? 0.7034 0.7069 0.6541 0.0669  -0.0598 0.0177  65  ASN A ND2 
1040 N N   . VAL A 69  ? 0.3234 0.3586 0.3171 0.0344  -0.0270 0.0101  66  VAL A N   
1041 C CA  . VAL A 69  ? 0.3134 0.3376 0.3084 0.0300  -0.0184 0.0106  66  VAL A CA  
1042 C C   . VAL A 69  ? 0.3331 0.3258 0.3127 0.0314  -0.0158 0.0165  66  VAL A C   
1043 O O   . VAL A 69  ? 0.3357 0.3178 0.3139 0.0238  -0.0084 0.0187  66  VAL A O   
1044 C CB  . VAL A 69  ? 0.3304 0.3701 0.3392 0.0367  -0.0180 0.0042  66  VAL A CB  
1045 C CG1 . VAL A 69  ? 0.3649 0.3936 0.3697 0.0520  -0.0241 0.0027  66  VAL A CG1 
1046 C CG2 . VAL A 69  ? 0.4151 0.4488 0.4265 0.0296  -0.0100 0.0038  66  VAL A CG2 
1056 N N   . ASP A 70  ? 0.3584 0.3362 0.3258 0.0404  -0.0218 0.0196  67  ASP A N   
1057 C CA  . ASP A 70  ? 0.4291 0.3764 0.3795 0.0393  -0.0183 0.0268  67  ASP A CA  
1058 C C   . ASP A 70  ? 0.4006 0.3420 0.3416 0.0291  -0.0122 0.0313  67  ASP A C   
1059 O O   . ASP A 70  ? 0.3821 0.3091 0.3185 0.0229  -0.0042 0.0351  67  ASP A O   
1060 C CB  . ASP A 70  ? 0.4798 0.4090 0.4147 0.0505  -0.0266 0.0306  67  ASP A CB  
1061 C CG  . ASP A 70  ? 0.6446 0.5746 0.5865 0.0629  -0.0330 0.0258  67  ASP A CG  
1062 O OD1 . ASP A 70  ? 0.5717 0.4964 0.5204 0.0615  -0.0287 0.0235  67  ASP A OD1 
1063 O OD2 . ASP A 70  ? 0.7469 0.6807 0.6860 0.0750  -0.0432 0.0241  67  ASP A OD2 
1068 N N   . ASP A 71  ? 0.3577 0.3103 0.2957 0.0275  -0.0162 0.0302  68  ASP A N   
1069 C CA  . ASP A 71  ? 0.3544 0.3017 0.2831 0.0192  -0.0110 0.0325  68  ASP A CA  
1070 C C   . ASP A 71  ? 0.3172 0.2718 0.2582 0.0103  -0.0031 0.0300  68  ASP A C   
1071 O O   . ASP A 71  ? 0.3557 0.2999 0.2905 0.0054  0.0043  0.0325  68  ASP A O   
1072 C CB  . ASP A 71  ? 0.4046 0.3625 0.3288 0.0190  -0.0189 0.0301  68  ASP A CB  
1073 C CG  . ASP A 71  ? 0.4960 0.4475 0.4073 0.0287  -0.0284 0.0322  68  ASP A CG  
1074 O OD1 . ASP A 71  ? 0.4706 0.3997 0.3630 0.0316  -0.0261 0.0382  68  ASP A OD1 
1075 O OD2 . ASP A 71  ? 0.4152 0.3844 0.3352 0.0334  -0.0381 0.0280  68  ASP A OD2 
1080 N N   . TRP A 72  ? 0.3103 0.2835 0.2680 0.0086  -0.0045 0.0250  69  TRP A N   
1081 C CA  . TRP A 72  ? 0.3440 0.3226 0.3107 0.0007  0.0013  0.0230  69  TRP A CA  
1082 C C   . TRP A 72  ? 0.3079 0.2750 0.2772 0.0001  0.0081  0.0246  69  TRP A C   
1083 O O   . TRP A 72  ? 0.3306 0.2932 0.3000 -0.0052 0.0139  0.0253  69  TRP A O   
1084 C CB  . TRP A 72  ? 0.3197 0.3202 0.3008 -0.0018 -0.0013 0.0183  69  TRP A CB  
1085 C CG  . TRP A 72  ? 0.3034 0.3189 0.2857 -0.0023 -0.0085 0.0165  69  TRP A CG  
1086 C CD1 . TRP A 72  ? 0.3288 0.3390 0.2999 -0.0043 -0.0130 0.0179  69  TRP A CD1 
1087 C CD2 . TRP A 72  ? 0.3113 0.3514 0.3072 -0.0013 -0.0125 0.0125  69  TRP A CD2 
1088 N NE1 . TRP A 72  ? 0.3461 0.3759 0.3244 -0.0055 -0.0203 0.0150  69  TRP A NE1 
1089 C CE2 . TRP A 72  ? 0.3499 0.3998 0.3444 -0.0038 -0.0196 0.0118  69  TRP A CE2 
1090 C CE3 . TRP A 72  ? 0.3608 0.4169 0.3700 0.0016  -0.0105 0.0087  69  TRP A CE3 
1091 C CZ2 . TRP A 72  ? 0.3923 0.4701 0.4008 -0.0043 -0.0244 0.0080  69  TRP A CZ2 
1092 C CZ3 . TRP A 72  ? 0.3610 0.4450 0.3827 0.0023  -0.0143 0.0047  69  TRP A CZ3 
1093 C CH2 . TRP A 72  ? 0.3717 0.4675 0.3943 -0.0012 -0.0210 0.0046  69  TRP A CH2 
1104 N N   . TRP A 73  ? 0.3098 0.2719 0.2813 0.0060  0.0067  0.0247  70  TRP A N   
1105 C CA  . TRP A 73  ? 0.3534 0.3029 0.3272 0.0043  0.0118  0.0261  70  TRP A CA  
1106 C C   . TRP A 73  ? 0.3410 0.2735 0.3030 0.0008  0.0174  0.0323  70  TRP A C   
1107 O O   . TRP A 73  ? 0.3650 0.2944 0.3318 -0.0052 0.0239  0.0331  70  TRP A O   
1108 C CB  . TRP A 73  ? 0.3269 0.2709 0.3027 0.0121  0.0073  0.0243  70  TRP A CB  
1109 C CG  . TRP A 73  ? 0.3476 0.2731 0.3224 0.0098  0.0107  0.0265  70  TRP A CG  
1110 C CD1 . TRP A 73  ? 0.3942 0.2977 0.3582 0.0133  0.0087  0.0310  70  TRP A CD1 
1111 C CD2 . TRP A 73  ? 0.3336 0.2601 0.3186 0.0030  0.0154  0.0243  70  TRP A CD2 
1112 N NE1 . TRP A 73  ? 0.4566 0.3473 0.4239 0.0074  0.0125  0.0320  70  TRP A NE1 
1113 C CE2 . TRP A 73  ? 0.3665 0.2725 0.3477 0.0013  0.0165  0.0275  70  TRP A CE2 
1114 C CE3 . TRP A 73  ? 0.3718 0.3135 0.3677 -0.0021 0.0181  0.0202  70  TRP A CE3 
1115 C CZ2 . TRP A 73  ? 0.4214 0.3244 0.4117 -0.0057 0.0197  0.0259  70  TRP A CZ2 
1116 C CZ3 . TRP A 73  ? 0.3700 0.3081 0.3738 -0.0075 0.0210  0.0187  70  TRP A CZ3 
1117 C CH2 . TRP A 73  ? 0.4000 0.3204 0.4020 -0.0094 0.0218  0.0211  70  TRP A CH2 
1128 N N   . GLU A 74  ? 0.3197 0.2425 0.2660 0.0043  0.0152  0.0368  71  GLU A N   
1129 C CA  . GLU A 74  ? 0.3451 0.2533 0.2783 0.0005  0.0220  0.0430  71  GLU A CA  
1130 C C   . GLU A 74  ? 0.3803 0.2968 0.3163 -0.0055 0.0287  0.0414  71  GLU A C   
1131 O O   . GLU A 74  ? 0.3643 0.2759 0.2994 -0.0103 0.0372  0.0443  71  GLU A O   
1132 C CB  . GLU A 74  ? 0.4185 0.3146 0.3311 0.0061  0.0175  0.0479  71  GLU A CB  
1133 C CG  . GLU A 74  ? 0.6011 0.4808 0.5073 0.0120  0.0123  0.0515  71  GLU A CG  
1134 C CD  . GLU A 74  ? 0.8964 0.7644 0.7818 0.0196  0.0051  0.0558  71  GLU A CD  
1135 O OE1 . GLU A 74  ? 0.7582 0.6281 0.6317 0.0185  0.0061  0.0571  71  GLU A OE1 
1136 O OE2 . GLU A 74  ? 0.7682 0.6243 0.6486 0.0276  -0.0026 0.0572  71  GLU A OE2 
1143 N N   . GLU A 75  ? 0.3780 0.3069 0.3172 -0.0052 0.0248  0.0367  72  GLU A N   
1144 C CA  . GLU A 75  ? 0.3281 0.2622 0.2689 -0.0092 0.0294  0.0342  72  GLU A CA  
1145 C C   . GLU A 75  ? 0.3472 0.2876 0.3044 -0.0133 0.0340  0.0318  72  GLU A C   
1146 O O   . GLU A 75  ? 0.3395 0.2804 0.2982 -0.0156 0.0406  0.0315  72  GLU A O   
1147 C CB  . GLU A 75  ? 0.3886 0.3309 0.3282 -0.0091 0.0225  0.0301  72  GLU A CB  
1148 C CG  . GLU A 75  ? 0.3990 0.3416 0.3359 -0.0116 0.0248  0.0270  72  GLU A CG  
1149 C CD  . GLU A 75  ? 0.4870 0.4197 0.4062 -0.0092 0.0289  0.0286  72  GLU A CD  
1150 O OE1 . GLU A 75  ? 0.5017 0.4272 0.4075 -0.0062 0.0272  0.0321  72  GLU A OE1 
1151 O OE2 . GLU A 75  ? 0.5205 0.4524 0.4382 -0.0093 0.0333  0.0259  72  GLU A OE2 
1159 N N   . VAL A 76  ? 0.3419 0.2878 0.3111 -0.0133 0.0305  0.0294  73  VAL A N   
1160 C CA  . VAL A 76  ? 0.3224 0.2733 0.3058 -0.0168 0.0334  0.0267  73  VAL A CA  
1161 C C   . VAL A 76  ? 0.3250 0.2680 0.3108 -0.0197 0.0397  0.0301  73  VAL A C   
1162 O O   . VAL A 76  ? 0.3485 0.2963 0.3432 -0.0235 0.0447  0.0289  73  VAL A O   
1163 C CB  . VAL A 76  ? 0.3265 0.2844 0.3191 -0.0155 0.0280  0.0230  73  VAL A CB  
1164 C CG1 . VAL A 76  ? 0.3393 0.3000 0.3443 -0.0187 0.0299  0.0201  73  VAL A CG1 
1165 C CG2 . VAL A 76  ? 0.3505 0.3195 0.3425 -0.0155 0.0232  0.0203  73  VAL A CG2 
1175 N N   . GLU A 77  ? 0.3397 0.2703 0.3172 -0.0184 0.0395  0.0347  74  GLU A N   
1176 C CA  . GLU A 77  ? 0.3648 0.2855 0.3420 -0.0236 0.0460  0.0394  74  GLU A CA  
1177 C C   . GLU A 77  ? 0.3999 0.3240 0.3725 -0.0269 0.0548  0.0420  74  GLU A C   
1178 O O   . GLU A 77  ? 0.3863 0.3148 0.3684 -0.0330 0.0619  0.0427  74  GLU A O   
1179 C CB  . GLU A 77  ? 0.3984 0.3004 0.3623 -0.0213 0.0433  0.0451  74  GLU A CB  
1180 C CG  . GLU A 77  ? 0.4919 0.3869 0.4623 -0.0191 0.0369  0.0425  74  GLU A CG  
1181 C CD  . GLU A 77  ? 0.5716 0.4451 0.5264 -0.0145 0.0323  0.0478  74  GLU A CD  
1182 O OE1 . GLU A 77  ? 0.6653 0.5343 0.6052 -0.0093 0.0301  0.0513  74  GLU A OE1 
1183 O OE2 . GLU A 77  ? 0.5760 0.4354 0.5325 -0.0160 0.0301  0.0483  74  GLU A OE2 
1190 N N   A LYS A 78  ? 0.3547 0.2781 0.3128 -0.0227 0.0543  0.0428  75  LYS A N   
1191 N N   B LYS A 78  ? 0.3549 0.2781 0.3128 -0.0226 0.0543  0.0428  75  LYS A N   
1192 C CA  A LYS A 78  ? 0.3825 0.3087 0.3334 -0.0240 0.0630  0.0443  75  LYS A CA  
1193 C CA  B LYS A 78  ? 0.3831 0.3092 0.3334 -0.0237 0.0626  0.0441  75  LYS A CA  
1194 C C   A LYS A 78  ? 0.3751 0.3167 0.3409 -0.0246 0.0658  0.0379  75  LYS A C   
1195 C C   B LYS A 78  ? 0.3751 0.3166 0.3410 -0.0246 0.0657  0.0380  75  LYS A C   
1196 O O   A LYS A 78  ? 0.3910 0.3395 0.3601 -0.0269 0.0749  0.0381  75  LYS A O   
1197 O O   B LYS A 78  ? 0.3902 0.3386 0.3601 -0.0272 0.0749  0.0383  75  LYS A O   
1198 C CB  A LYS A 78  ? 0.4406 0.3605 0.3704 -0.0185 0.0602  0.0453  75  LYS A CB  
1199 C CB  B LYS A 78  ? 0.4400 0.3610 0.3706 -0.0179 0.0588  0.0444  75  LYS A CB  
1200 C CG  A LYS A 78  ? 0.4672 0.3706 0.3778 -0.0173 0.0593  0.0529  75  LYS A CG  
1201 C CG  B LYS A 78  ? 0.4991 0.4215 0.4177 -0.0170 0.0669  0.0445  75  LYS A CG  
1202 C CD  A LYS A 78  ? 0.6085 0.5076 0.5022 -0.0106 0.0511  0.0519  75  LYS A CD  
1203 C CD  B LYS A 78  ? 0.5748 0.4909 0.4732 -0.0111 0.0607  0.0430  75  LYS A CD  
1204 C CE  A LYS A 78  ? 0.6538 0.5568 0.5368 -0.0089 0.0549  0.0487  75  LYS A CE  
1205 C CE  B LYS A 78  ? 0.6785 0.5945 0.5620 -0.0088 0.0688  0.0421  75  LYS A CE  
1206 N NZ  A LYS A 78  ? 0.8150 0.7114 0.6789 -0.0034 0.0462  0.0481  75  LYS A NZ  
1207 N NZ  B LYS A 78  ? 0.8688 0.7764 0.7309 -0.0033 0.0613  0.0401  75  LYS A NZ  
1234 N N   . ALA A 79  ? 0.3500 0.2976 0.3245 -0.0223 0.0581  0.0324  76  ALA A N   
1235 C CA  . ALA A 79  ? 0.3622 0.3211 0.3490 -0.0219 0.0585  0.0266  76  ALA A CA  
1236 C C   . ALA A 79  ? 0.3479 0.3149 0.3535 -0.0266 0.0625  0.0259  76  ALA A C   
1237 O O   . ALA A 79  ? 0.3284 0.3062 0.3438 -0.0266 0.0674  0.0229  76  ALA A O   
1238 C CB  . ALA A 79  ? 0.3449 0.3050 0.3332 -0.0199 0.0490  0.0226  76  ALA A CB  
1245 N N   . TYR A 80  ? 0.3365 0.2990 0.3481 -0.0302 0.0597  0.0276  77  TYR A N   
1246 C CA  . TYR A 80  ? 0.3164 0.2844 0.3447 -0.0363 0.0628  0.0271  77  TYR A CA  
1247 C C   . TYR A 80  ? 0.3584 0.3297 0.3880 -0.0416 0.0736  0.0314  77  TYR A C   
1248 O O   . TYR A 80  ? 0.3471 0.3331 0.3932 -0.0449 0.0783  0.0286  77  TYR A O   
1249 C CB  . TYR A 80  ? 0.3234 0.2807 0.3530 -0.0386 0.0573  0.0282  77  TYR A CB  
1250 C CG  . TYR A 80  ? 0.3537 0.3139 0.3996 -0.0460 0.0588  0.0273  77  TYR A CG  
1251 C CD1 . TYR A 80  ? 0.3206 0.2908 0.3813 -0.0460 0.0536  0.0207  77  TYR A CD1 
1252 C CD2 . TYR A 80  ? 0.3861 0.3390 0.4318 -0.0538 0.0648  0.0329  77  TYR A CD2 
1253 C CE1 . TYR A 80  ? 0.3155 0.2893 0.3920 -0.0534 0.0538  0.0191  77  TYR A CE1 
1254 C CE2 . TYR A 80  ? 0.3709 0.3274 0.4330 -0.0626 0.0657  0.0318  77  TYR A CE2 
1255 C CZ  . TYR A 80  ? 0.3761 0.3434 0.4541 -0.0621 0.0596  0.0244  77  TYR A CZ  
1256 O OH  . TYR A 80  ? 0.4162 0.3872 0.5111 -0.0715 0.0593  0.0228  77  TYR A OH  
1266 N N   A GLN A 81  ? 0.3459 0.3050 0.3579 -0.0424 0.0779  0.0381  78  GLN A N   
1267 N N   B GLN A 81  ? 0.3457 0.3047 0.3578 -0.0425 0.0779  0.0382  78  GLN A N   
1268 C CA  A GLN A 81  ? 0.3837 0.3452 0.3941 -0.0490 0.0896  0.0436  78  GLN A CA  
1269 C CA  B GLN A 81  ? 0.3837 0.3451 0.3938 -0.0489 0.0897  0.0436  78  GLN A CA  
1270 C C   A GLN A 81  ? 0.3858 0.3641 0.3978 -0.0450 0.0973  0.0399  78  GLN A C   
1271 C C   B GLN A 81  ? 0.3844 0.3634 0.3974 -0.0450 0.0970  0.0395  78  GLN A C   
1272 O O   A GLN A 81  ? 0.3973 0.3890 0.4189 -0.0506 0.1077  0.0410  78  GLN A O   
1273 O O   B GLN A 81  ? 0.3904 0.3842 0.4153 -0.0503 0.1069  0.0399  78  GLN A O   
1274 C CB  A GLN A 81  ? 0.4148 0.3561 0.4015 -0.0499 0.0912  0.0522  78  GLN A CB  
1275 C CB  B GLN A 81  ? 0.4140 0.3559 0.3996 -0.0493 0.0916  0.0521  78  GLN A CB  
1276 C CG  A GLN A 81  ? 0.4632 0.3852 0.4470 -0.0540 0.0853  0.0569  78  GLN A CG  
1277 C CG  B GLN A 81  ? 0.4835 0.4231 0.4626 -0.0585 0.1043  0.0605  78  GLN A CG  
1278 C CD  A GLN A 81  ? 0.4970 0.4206 0.4976 -0.0657 0.0892  0.0586  78  GLN A CD  
1279 C CD  B GLN A 81  ? 0.5684 0.5113 0.5666 -0.0709 0.1078  0.0626  78  GLN A CD  
1280 O OE1 A GLN A 81  ? 0.5007 0.4139 0.5074 -0.0677 0.0816  0.0573  78  GLN A OE1 
1281 O OE1 B GLN A 81  ? 0.6546 0.5869 0.6596 -0.0730 0.0990  0.0616  78  GLN A OE1 
1282 N NE2 A GLN A 81  ? 0.6383 0.5755 0.6463 -0.0737 0.1011  0.0610  78  GLN A NE2 
1283 N NE2 B GLN A 81  ? 0.5409 0.4990 0.5474 -0.0796 0.1207  0.0652  78  GLN A NE2 
1300 N N   . PHE A 82  ? 0.3829 0.3609 0.3856 -0.0357 0.0921  0.0351  79  PHE A N   
1301 C CA  . PHE A 82  ? 0.3897 0.3814 0.3940 -0.0296 0.0971  0.0295  79  PHE A CA  
1302 C C   . PHE A 82  ? 0.3469 0.3586 0.3775 -0.0306 0.0983  0.0236  79  PHE A C   
1303 O O   . PHE A 82  ? 0.3632 0.3921 0.4028 -0.0304 0.1079  0.0215  79  PHE A O   
1304 C CB  . PHE A 82  ? 0.4121 0.3957 0.4026 -0.0205 0.0882  0.0249  79  PHE A CB  
1305 C CG  . PHE A 82  ? 0.4097 0.4033 0.4011 -0.0126 0.0905  0.0176  79  PHE A CG  
1306 C CD1 . PHE A 82  ? 0.4967 0.4923 0.4741 -0.0087 0.0996  0.0175  79  PHE A CD1 
1307 C CD2 . PHE A 82  ? 0.3929 0.3922 0.3968 -0.0082 0.0833  0.0108  79  PHE A CD2 
1308 C CE1 . PHE A 82  ? 0.4827 0.4870 0.4605 0.0005  0.1015  0.0095  79  PHE A CE1 
1309 C CE2 . PHE A 82  ? 0.4583 0.4640 0.4620 0.0007  0.0841  0.0037  79  PHE A CE2 
1310 C CZ  . PHE A 82  ? 0.4650 0.4734 0.4563 0.0056  0.0931  0.0025  79  PHE A CZ  
1321 N N   . LEU A 83  ? 0.3259 0.3371 0.3693 -0.0316 0.0886  0.0206  80  LEU A N   
1322 C CA  . LEU A 83  ? 0.3103 0.3395 0.3777 -0.0318 0.0874  0.0146  80  LEU A CA  
1323 C C   . LEU A 83  ? 0.3246 0.3666 0.4095 -0.0421 0.0958  0.0174  80  LEU A C   
1324 O O   . LEU A 83  ? 0.3136 0.3775 0.4175 -0.0420 0.1005  0.0130  80  LEU A O   
1325 C CB  . LEU A 83  ? 0.3061 0.3295 0.3788 -0.0305 0.0748  0.0113  80  LEU A CB  
1326 C CG  . LEU A 83  ? 0.3079 0.3221 0.3669 -0.0220 0.0663  0.0081  80  LEU A CG  
1327 C CD1 . LEU A 83  ? 0.3086 0.3178 0.3712 -0.0231 0.0559  0.0065  80  LEU A CD1 
1328 C CD2 . LEU A 83  ? 0.3542 0.3777 0.4156 -0.0133 0.0670  0.0020  80  LEU A CD2 
1340 N N   . VAL A 84  ? 0.3030 0.3315 0.3823 -0.0514 0.0972  0.0246  81  VAL A N   
1341 C CA  . VAL A 84  ? 0.3234 0.3607 0.4166 -0.0638 0.1057  0.0287  81  VAL A CA  
1342 C C   . VAL A 84  ? 0.3501 0.4035 0.4424 -0.0648 0.1204  0.0307  81  VAL A C   
1343 O O   . VAL A 84  ? 0.3603 0.4375 0.4742 -0.0710 0.1282  0.0290  81  VAL A O   
1344 C CB  . VAL A 84  ? 0.3675 0.3805 0.4483 -0.0725 0.1040  0.0369  81  VAL A CB  
1345 C CG1 . VAL A 84  ? 0.4373 0.4565 0.5285 -0.0874 0.1142  0.0429  81  VAL A CG1 
1346 C CG2 . VAL A 84  ? 0.4016 0.4037 0.4874 -0.0716 0.0909  0.0333  81  VAL A CG2 
1356 N N   . ASN A 85  ? 0.3959 0.4382 0.4632 -0.0589 0.1245  0.0340  82  ASN A N   
1357 C CA  . ASN A 85  ? 0.4028 0.4591 0.4649 -0.0591 0.1392  0.0359  82  ASN A CA  
1358 C C   . ASN A 85  ? 0.4128 0.4958 0.4907 -0.0491 0.1420  0.0256  82  ASN A C   
1359 O O   . ASN A 85  ? 0.4479 0.5530 0.5334 -0.0509 0.1554  0.0250  82  ASN A O   
1360 C CB  . ASN A 85  ? 0.4556 0.4912 0.4841 -0.0539 0.1410  0.0411  82  ASN A CB  
1361 C CG  . ASN A 85  ? 0.6379 0.6489 0.6492 -0.0636 0.1410  0.0525  82  ASN A CG  
1362 O OD1 . ASN A 85  ? 0.6215 0.6319 0.6443 -0.0763 0.1438  0.0578  82  ASN A OD1 
1363 N ND2 . ASN A 85  ? 0.6942 0.6839 0.6773 -0.0575 0.1368  0.0561  82  ASN A ND2 
1370 N N   . GLU A 86  ? 0.3906 0.4717 0.4725 -0.0383 0.1297  0.0175  83  GLU A N   
1371 C CA  . GLU A 86  ? 0.3972 0.5004 0.4942 -0.0274 0.1295  0.0072  83  GLU A CA  
1372 C C   . GLU A 86  ? 0.3972 0.5274 0.5281 -0.0332 0.1310  0.0035  83  GLU A C   
1373 O O   . GLU A 86  ? 0.4414 0.5952 0.5885 -0.0242 0.1327  -0.0050 83  GLU A O   
1374 C CB  . GLU A 86  ? 0.4265 0.5143 0.5147 -0.0158 0.1146  0.0013  83  GLU A CB  
1375 C CG  . GLU A 86  ? 0.4617 0.5299 0.5201 -0.0072 0.1128  0.0014  83  GLU A CG  
1376 C CD  . GLU A 86  ? 0.5690 0.6503 0.6216 0.0018  0.1232  -0.0035 83  GLU A CD  
1377 O OE1 . GLU A 86  ? 0.6874 0.7815 0.7515 0.0124  0.1203  -0.0126 83  GLU A OE1 
1378 O OE2 . GLU A 86  ? 0.6053 0.6838 0.6411 -0.0008 0.1337  0.0014  83  GLU A OE2 
1385 N N   . GLY A 87  ? 0.3747 0.5024 0.5171 -0.0473 0.1298  0.0089  84  GLY A N   
1386 C CA  . GLY A 87  ? 0.3479 0.5020 0.5230 -0.0552 0.1311  0.0055  84  GLY A CA  
1387 C C   . GLY A 87  ? 0.3134 0.4648 0.5029 -0.0540 0.1154  0.0002  84  GLY A C   
1388 O O   . GLY A 87  ? 0.3420 0.5167 0.5599 -0.0591 0.1142  -0.0042 84  GLY A O   
1392 N N   . TYR A 88  ? 0.3223 0.4475 0.4934 -0.0480 0.1035  0.0003  85  TYR A N   
1393 C CA  . TYR A 88  ? 0.2624 0.3841 0.4434 -0.0464 0.0890  -0.0045 85  TYR A CA  
1394 C C   . TYR A 88  ? 0.4199 0.5340 0.6087 -0.0610 0.0866  -0.0004 85  TYR A C   
1395 O O   . TYR A 88  ? 0.3970 0.4892 0.5686 -0.0675 0.0888  0.0070  85  TYR A O   
1396 C CB  . TYR A 88  ? 0.3310 0.4287 0.4894 -0.0367 0.0782  -0.0053 85  TYR A CB  
1397 C CG  . TYR A 88  ? 0.2856 0.3865 0.4359 -0.0225 0.0774  -0.0103 85  TYR A CG  
1398 C CD1 . TYR A 88  ? 0.3370 0.4520 0.5015 -0.0132 0.0702  -0.0185 85  TYR A CD1 
1399 C CD2 . TYR A 88  ? 0.3497 0.4381 0.4773 -0.0179 0.0828  -0.0073 85  TYR A CD2 
1400 C CE1 . TYR A 88  ? 0.3279 0.4421 0.4835 0.0005  0.0684  -0.0234 85  TYR A CE1 
1401 C CE2 . TYR A 88  ? 0.3252 0.4132 0.4438 -0.0051 0.0809  -0.0126 85  TYR A CE2 
1402 C CZ  . TYR A 88  ? 0.3395 0.4394 0.4719 0.0042  0.0738  -0.0207 85  TYR A CZ  
1403 O OH  . TYR A 88  ? 0.3577 0.4530 0.4786 0.0179  0.0711  -0.0262 85  TYR A OH  
1413 N N   . GLU A 89  ? 0.3630 0.4944 0.5771 -0.0654 0.0812  -0.0058 86  GLU A N   
1414 C CA  . GLU A 89  ? 0.3515 0.4745 0.5738 -0.0784 0.0757  -0.0042 86  GLU A CA  
1415 C C   . GLU A 89  ? 0.3816 0.4866 0.5950 -0.0727 0.0604  -0.0082 86  GLU A C   
1416 O O   . GLU A 89  ? 0.4415 0.5310 0.6527 -0.0807 0.0550  -0.0069 86  GLU A O   
1417 C CB  . GLU A 89  ? 0.4497 0.6033 0.7056 -0.0877 0.0777  -0.0085 86  GLU A CB  
1418 C CG  . GLU A 89  ? 0.6564 0.8247 0.9201 -0.1000 0.0948  -0.0019 86  GLU A CG  
1419 C CD  . GLU A 89  ? 0.9386 1.1492 1.2314 -0.0985 0.1025  -0.0079 86  GLU A CD  
1420 O OE1 . GLU A 89  ? 0.9590 1.1919 1.2805 -0.1027 0.0958  -0.0145 86  GLU A OE1 
1421 O OE2 . GLU A 89  ? 0.9215 1.1440 1.2084 -0.0924 0.1151  -0.0064 86  GLU A OE2 
1428 N N   . SER A 90  ? 0.3077 0.4125 0.5134 -0.0590 0.0537  -0.0127 87  SER A N   
1429 C CA  . SER A 90  ? 0.2804 0.3696 0.4751 -0.0535 0.0405  -0.0159 87  SER A CA  
1430 C C   . SER A 90  ? 0.2959 0.3667 0.4641 -0.0451 0.0407  -0.0124 87  SER A C   
1431 O O   . SER A 90  ? 0.2800 0.3554 0.4433 -0.0359 0.0416  -0.0139 87  SER A O   
1432 C CB  . SER A 90  ? 0.3575 0.4625 0.5668 -0.0464 0.0304  -0.0241 87  SER A CB  
1433 O OG  . SER A 90  ? 0.3440 0.4326 0.5370 -0.0399 0.0190  -0.0259 87  SER A OG  
1439 N N   . ILE A 91  ? 0.2188 0.2691 0.3706 -0.0480 0.0393  -0.0084 88  ILE A N   
1440 C CA  . ILE A 91  ? 0.2154 0.2504 0.3442 -0.0417 0.0390  -0.0051 88  ILE A CA  
1441 C C   . ILE A 91  ? 0.2313 0.2540 0.3504 -0.0403 0.0297  -0.0069 88  ILE A C   
1442 O O   . ILE A 91  ? 0.2665 0.2828 0.3884 -0.0456 0.0270  -0.0075 88  ILE A O   
1443 C CB  . ILE A 91  ? 0.2711 0.2960 0.3883 -0.0455 0.0480  0.0020  88  ILE A CB  
1444 C CG1 . ILE A 91  ? 0.3072 0.3453 0.4313 -0.0470 0.0588  0.0038  88  ILE A CG1 
1445 C CG2 . ILE A 91  ? 0.2889 0.2997 0.3844 -0.0396 0.0460  0.0045  88  ILE A CG2 
1446 C CD1 . ILE A 91  ? 0.3280 0.3558 0.4411 -0.0532 0.0681  0.0118  88  ILE A CD1 
1458 N N   . SER A 92  ? 0.2324 0.2510 0.3389 -0.0333 0.0249  -0.0078 89  SER A N   
1459 C CA  . SER A 92  ? 0.2651 0.2750 0.3603 -0.0315 0.0175  -0.0092 89  SER A CA  
1460 C C   . SER A 92  ? 0.2936 0.2953 0.3711 -0.0286 0.0194  -0.0052 89  SER A C   
1461 O O   . SER A 92  ? 0.2675 0.2689 0.3410 -0.0273 0.0246  -0.0023 89  SER A O   
1462 C CB  . SER A 92  ? 0.2522 0.2668 0.3499 -0.0278 0.0086  -0.0140 89  SER A CB  
1463 O OG  . SER A 92  ? 0.2738 0.2979 0.3896 -0.0308 0.0058  -0.0184 89  SER A OG  
1469 N N   . ALA A 93  ? 0.2454 0.2418 0.3124 -0.0279 0.0154  -0.0054 90  ALA A N   
1470 C CA  . ALA A 93  ? 0.2537 0.2455 0.3066 -0.0266 0.0168  -0.0019 90  ALA A CA  
1471 C C   . ALA A 93  ? 0.2823 0.2739 0.3255 -0.0260 0.0114  -0.0030 90  ALA A C   
1472 O O   . ALA A 93  ? 0.2621 0.2552 0.3066 -0.0259 0.0076  -0.0065 90  ALA A O   
1473 C CB  . ALA A 93  ? 0.2661 0.2535 0.3159 -0.0274 0.0205  0.0006  90  ALA A CB  
1479 N N   . THR A 94  ? 0.2578 0.2473 0.2899 -0.0262 0.0114  0.0000  91  THR A N   
1480 C CA  . THR A 94  ? 0.2697 0.2598 0.2910 -0.0279 0.0081  0.0006  91  THR A CA  
1481 C C   . THR A 94  ? 0.3184 0.3090 0.3320 -0.0301 0.0103  0.0042  91  THR A C   
1482 O O   . THR A 94  ? 0.2818 0.2684 0.2944 -0.0297 0.0122  0.0061  91  THR A O   
1483 C CB  . THR A 94  ? 0.3183 0.3038 0.3335 -0.0279 0.0025  0.0006  91  THR A CB  
1484 O OG1 . THR A 94  ? 0.3264 0.3122 0.3291 -0.0314 0.0004  0.0023  91  THR A OG1 
1485 C CG2 . THR A 94  ? 0.3076 0.2856 0.3186 -0.0268 0.0017  0.0026  91  THR A CG2 
1493 N N   . GLY A 95  ? 0.2668 0.2637 0.2749 -0.0325 0.0100  0.0046  92  GLY A N   
1494 C CA  . GLY A 95  ? 0.2790 0.2797 0.2822 -0.0356 0.0112  0.0075  92  GLY A CA  
1495 C C   . GLY A 95  ? 0.2849 0.2960 0.2828 -0.0400 0.0111  0.0080  92  GLY A C   
1496 O O   . GLY A 95  ? 0.2725 0.2886 0.2701 -0.0388 0.0112  0.0054  92  GLY A O   
1500 N N   A VAL A 96  ? 0.2851 0.3005 0.2786 -0.0455 0.0110  0.0111  93  VAL A N   
1501 N N   B VAL A 96  ? 0.2850 0.3001 0.2784 -0.0455 0.0110  0.0112  93  VAL A N   
1502 C CA  A VAL A 96  ? 0.2664 0.2951 0.2558 -0.0521 0.0121  0.0125  93  VAL A CA  
1503 C CA  B VAL A 96  ? 0.2679 0.2964 0.2574 -0.0522 0.0120  0.0126  93  VAL A CA  
1504 C C   A VAL A 96  ? 0.2845 0.3305 0.2818 -0.0511 0.0143  0.0113  93  VAL A C   
1505 C C   B VAL A 96  ? 0.2838 0.3298 0.2817 -0.0504 0.0144  0.0110  93  VAL A C   
1506 O O   A VAL A 96  ? 0.2808 0.3239 0.2800 -0.0507 0.0128  0.0123  93  VAL A O   
1507 O O   B VAL A 96  ? 0.2899 0.3331 0.2907 -0.0487 0.0132  0.0116  93  VAL A O   
1508 C CB  A VAL A 96  ? 0.3282 0.3472 0.3053 -0.0620 0.0088  0.0177  93  VAL A CB  
1509 C CB  B VAL A 96  ? 0.3150 0.3346 0.2929 -0.0622 0.0088  0.0179  93  VAL A CB  
1510 C CG1 A VAL A 96  ? 0.2903 0.2994 0.2656 -0.0641 0.0060  0.0197  93  VAL A CG1 
1511 C CG1 B VAL A 96  ? 0.3423 0.3768 0.3158 -0.0718 0.0110  0.0205  93  VAL A CG1 
1512 C CG2 A VAL A 96  ? 0.3400 0.3735 0.3120 -0.0717 0.0110  0.0205  93  VAL A CG2 
1513 C CG2 B VAL A 96  ? 0.3625 0.3617 0.3314 -0.0613 0.0046  0.0191  93  VAL A CG2 
1532 N N   . SER A 97  ? 0.2768 0.3416 0.2779 -0.0499 0.0175  0.0085  94  SER A N   
1533 C CA  . SER A 97  ? 0.3085 0.3948 0.3188 -0.0477 0.0193  0.0061  94  SER A CA  
1534 C C   . SER A 97  ? 0.2772 0.3571 0.2941 -0.0370 0.0177  0.0034  94  SER A C   
1535 O O   . SER A 97  ? 0.2811 0.3526 0.2991 -0.0293 0.0181  0.0001  94  SER A O   
1536 C CB  . SER A 97  ? 0.4178 0.5122 0.4264 -0.0595 0.0182  0.0107  94  SER A CB  
1537 O OG  . SER A 97  ? 0.6793 0.8029 0.6972 -0.0605 0.0212  0.0083  94  SER A OG  
1544 N N   . LEU A 98  ? 0.2855 0.3673 0.3054 -0.0366 0.0153  0.0048  95  LEU A N   
1545 C CA  . LEU A 98  ? 0.2734 0.3453 0.2956 -0.0267 0.0136  0.0034  95  LEU A CA  
1546 C C   . LEU A 98  ? 0.2712 0.3199 0.2886 -0.0252 0.0141  0.0049  95  LEU A C   
1547 O O   . LEU A 98  ? 0.2742 0.3143 0.2936 -0.0179 0.0144  0.0031  95  LEU A O   
1548 C CB  . LEU A 98  ? 0.3100 0.3841 0.3322 -0.0274 0.0100  0.0055  95  LEU A CB  
1549 C CG  . LEU A 98  ? 0.3287 0.3889 0.3485 -0.0186 0.0077  0.0060  95  LEU A CG  
1550 C CD1 . LEU A 98  ? 0.3562 0.4209 0.3816 -0.0075 0.0076  0.0019  95  LEU A CD1 
1551 C CD2 . LEU A 98  ? 0.3914 0.4555 0.4089 -0.0202 0.0029  0.0078  95  LEU A CD2 
1563 N N   . GLY A 99  ? 0.2495 0.2883 0.2610 -0.0322 0.0140  0.0077  96  GLY A N   
1564 C CA  . GLY A 99  ? 0.2522 0.2741 0.2621 -0.0303 0.0147  0.0082  96  GLY A CA  
1565 C C   . GLY A 99  ? 0.2844 0.3057 0.2982 -0.0272 0.0157  0.0048  96  GLY A C   
1566 O O   . GLY A 99  ? 0.2565 0.2676 0.2733 -0.0242 0.0164  0.0040  96  GLY A O   
1570 N N   . GLY A 100 ? 0.2902 0.3232 0.3036 -0.0284 0.0160  0.0025  97  GLY A N   
1571 C CA  . GLY A 100 ? 0.2638 0.2963 0.2790 -0.0244 0.0161  -0.0020 97  GLY A CA  
1572 C C   . GLY A 100 ? 0.2215 0.2534 0.2420 -0.0161 0.0161  -0.0059 97  GLY A C   
1573 O O   . GLY A 100 ? 0.2473 0.2685 0.2700 -0.0131 0.0151  -0.0086 97  GLY A O   
1577 N N   . LEU A 101 ? 0.2592 0.3007 0.2818 -0.0124 0.0163  -0.0061 98  LEU A N   
1578 C CA  . LEU A 101 ? 0.2522 0.2888 0.2777 -0.0031 0.0149  -0.0091 98  LEU A CA  
1579 C C   . LEU A 101 ? 0.2530 0.2692 0.2774 -0.0033 0.0143  -0.0054 98  LEU A C   
1580 O O   . LEU A 101 ? 0.2711 0.2745 0.2961 0.0010  0.0130  -0.0074 98  LEU A O   
1581 C CB  . LEU A 101 ? 0.2664 0.3187 0.2947 0.0017  0.0140  -0.0099 98  LEU A CB  
1582 C CG  . LEU A 101 ? 0.2750 0.3522 0.3067 0.0026  0.0158  -0.0143 98  LEU A CG  
1583 C CD1 . LEU A 101 ? 0.3626 0.4594 0.4003 0.0054  0.0146  -0.0145 98  LEU A CD1 
1584 C CD2 . LEU A 101 ? 0.3388 0.4174 0.3707 0.0116  0.0160  -0.0220 98  LEU A CD2 
1596 N N   . MET A 102 ? 0.2306 0.2431 0.2525 -0.0085 0.0153  0.0000  99  MET A N   
1597 C CA  . MET A 102 ? 0.2702 0.2662 0.2901 -0.0093 0.0164  0.0040  99  MET A CA  
1598 C C   . MET A 102 ? 0.3006 0.2880 0.3245 -0.0126 0.0178  0.0029  99  MET A C   
1599 O O   . MET A 102 ? 0.2852 0.2602 0.3102 -0.0127 0.0189  0.0044  99  MET A O   
1600 C CB  . MET A 102 ? 0.2492 0.2453 0.2643 -0.0138 0.0174  0.0083  99  MET A CB  
1601 C CG  . MET A 102 ? 0.2857 0.2879 0.2967 -0.0114 0.0150  0.0098  99  MET A CG  
1602 S SD  . MET A 102 ? 0.3668 0.3592 0.3739 -0.0030 0.0128  0.0112  99  MET A SD  
1603 C CE  . MET A 102 ? 0.3712 0.3734 0.3737 -0.0012 0.0084  0.0126  99  MET A CE  
1613 N N   . THR A 103 ? 0.2798 0.2737 0.3057 -0.0160 0.0174  0.0007  100 THR A N   
1614 C CA  . THR A 103 ? 0.2326 0.2212 0.2638 -0.0184 0.0170  -0.0015 100 THR A CA  
1615 C C   . THR A 103 ? 0.2293 0.2119 0.2632 -0.0150 0.0148  -0.0060 100 THR A C   
1616 O O   . THR A 103 ? 0.2604 0.2334 0.2996 -0.0174 0.0146  -0.0064 100 THR A O   
1617 C CB  . THR A 103 ? 0.2984 0.2942 0.3279 -0.0212 0.0152  -0.0029 100 THR A CB  
1618 O OG1 . THR A 103 ? 0.2997 0.2955 0.3259 -0.0244 0.0160  0.0010  100 THR A OG1 
1619 C CG2 . THR A 103 ? 0.2881 0.2809 0.3232 -0.0223 0.0127  -0.0065 100 THR A CG2 
1627 N N   . LEU A 104 ? 0.2423 0.2313 0.2730 -0.0097 0.0130  -0.0102 101 LEU A N   
1628 C CA  . LEU A 104 ? 0.2702 0.2513 0.3012 -0.0045 0.0099  -0.0158 101 LEU A CA  
1629 C C   . LEU A 104 ? 0.2687 0.2334 0.2991 -0.0025 0.0095  -0.0130 101 LEU A C   
1630 O O   . LEU A 104 ? 0.2739 0.2234 0.3058 -0.0036 0.0071  -0.0150 101 LEU A O   
1631 C CB  . LEU A 104 ? 0.2849 0.2784 0.3119 0.0029  0.0090  -0.0214 101 LEU A CB  
1632 C CG  . LEU A 104 ? 0.2839 0.2919 0.3080 0.0005  0.0097  -0.0243 101 LEU A CG  
1633 C CD1 . LEU A 104 ? 0.3356 0.3613 0.3569 0.0064  0.0114  -0.0281 101 LEU A CD1 
1634 C CD2 . LEU A 104 ? 0.2752 0.2743 0.2986 0.0000  0.0060  -0.0298 101 LEU A CD2 
1646 N N   . LYS A 105 ? 0.2646 0.2304 0.2915 -0.0004 0.0111  -0.0081 102 LYS A N   
1647 C CA  . LYS A 105 ? 0.2964 0.2440 0.3189 0.0018  0.0102  -0.0042 102 LYS A CA  
1648 C C   . LYS A 105 ? 0.2893 0.2252 0.3143 -0.0074 0.0136  0.0010  102 LYS A C   
1649 O O   . LYS A 105 ? 0.2939 0.2114 0.3172 -0.0092 0.0125  0.0026  102 LYS A O   
1650 C CB  . LYS A 105 ? 0.2857 0.2378 0.3026 0.0062  0.0103  -0.0001 102 LYS A CB  
1651 C CG  . LYS A 105 ? 0.3306 0.2616 0.3393 0.0111  0.0074  0.0033  102 LYS A CG  
1652 C CD  . LYS A 105 ? 0.3779 0.3137 0.3803 0.0176  0.0053  0.0062  102 LYS A CD  
1653 C CE  . LYS A 105 ? 0.3634 0.2747 0.3543 0.0232  0.0013  0.0105  102 LYS A CE  
1654 N NZ  . LYS A 105 ? 0.3934 0.2952 0.3826 0.0341  -0.0053 0.0047  102 LYS A NZ  
1668 N N   A LEU A 106 ? 0.2699 0.2161 0.2990 -0.0135 0.0177  0.0035  103 LEU A N   
1669 N N   B LEU A 106 ? 0.2690 0.2151 0.2979 -0.0135 0.0177  0.0036  103 LEU A N   
1670 C CA  A LEU A 106 ? 0.2729 0.2136 0.3069 -0.0215 0.0219  0.0074  103 LEU A CA  
1671 C CA  B LEU A 106 ? 0.2712 0.2121 0.3054 -0.0216 0.0219  0.0072  103 LEU A CA  
1672 C C   A LEU A 106 ? 0.2917 0.2277 0.3348 -0.0260 0.0196  0.0032  103 LEU A C   
1673 C C   B LEU A 106 ? 0.2924 0.2273 0.3349 -0.0256 0.0193  0.0031  103 LEU A C   
1674 O O   A LEU A 106 ? 0.2934 0.2202 0.3406 -0.0328 0.0220  0.0063  103 LEU A O   
1675 O O   B LEU A 106 ? 0.2878 0.2114 0.3332 -0.0319 0.0211  0.0061  103 LEU A O   
1676 C CB  A LEU A 106 ? 0.2938 0.2477 0.3305 -0.0244 0.0255  0.0088  103 LEU A CB  
1677 C CB  B LEU A 106 ? 0.2941 0.2486 0.3320 -0.0247 0.0252  0.0081  103 LEU A CB  
1678 C CG  A LEU A 106 ? 0.3103 0.2633 0.3499 -0.0300 0.0319  0.0134  103 LEU A CG  
1679 C CG  B LEU A 106 ? 0.2798 0.2356 0.3098 -0.0241 0.0291  0.0133  103 LEU A CG  
1680 C CD1 A LEU A 106 ? 0.3370 0.2799 0.3648 -0.0291 0.0354  0.0199  103 LEU A CD1 
1681 C CD1 B LEU A 106 ? 0.3485 0.3157 0.3811 -0.0253 0.0299  0.0120  103 LEU A CD1 
1682 C CD2 A LEU A 106 ? 0.2793 0.2449 0.3218 -0.0301 0.0332  0.0121  103 LEU A CD2 
1683 C CD2 B LEU A 106 ? 0.3519 0.2975 0.3787 -0.0276 0.0345  0.0192  103 LEU A CD2 
1706 N N   . ALA A 107 ? 0.2838 0.2262 0.3294 -0.0231 0.0149  -0.0038 104 ALA A N   
1707 C CA  . ALA A 107 ? 0.2932 0.2301 0.3457 -0.0265 0.0108  -0.0090 104 ALA A CA  
1708 C C   . ALA A 107 ? 0.2972 0.2136 0.3451 -0.0250 0.0069  -0.0106 104 ALA A C   
1709 O O   . ALA A 107 ? 0.3200 0.2271 0.3742 -0.0313 0.0039  -0.0131 104 ALA A O   
1710 C CB  . ALA A 107 ? 0.2950 0.2439 0.3469 -0.0224 0.0067  -0.0160 104 ALA A CB  
1717 N N   . GLN A 108 ? 0.3066 0.2150 0.3440 -0.0168 0.0057  -0.0097 105 GLN A N   
1718 C CA  . GLN A 108 ? 0.3264 0.2110 0.3567 -0.0139 0.0011  -0.0106 105 GLN A CA  
1719 C C   . GLN A 108 ? 0.3263 0.1932 0.3542 -0.0222 0.0043  -0.0014 105 GLN A C   
1720 O O   . GLN A 108 ? 0.3557 0.1982 0.3789 -0.0246 0.0001  -0.0011 105 GLN A O   
1721 C CB  . GLN A 108 ? 0.3350 0.2191 0.3554 -0.0002 -0.0020 -0.0132 105 GLN A CB  
1722 C CG  . GLN A 108 ? 0.3068 0.2088 0.3284 0.0079  -0.0044 -0.0228 105 GLN A CG  
1723 C CD  . GLN A 108 ? 0.3767 0.2872 0.3927 0.0208  -0.0058 -0.0257 105 GLN A CD  
1724 O OE1 . GLN A 108 ? 0.4036 0.3134 0.4161 0.0238  -0.0048 -0.0201 105 GLN A OE1 
1725 N NE2 . GLN A 108 ? 0.3814 0.3020 0.3964 0.0289  -0.0082 -0.0350 105 GLN A NE2 
1734 N N   . HIS A 109 ? 0.3188 0.1963 0.3483 -0.0270 0.0116  0.0059  106 HIS A N   
1735 C CA  . HIS A 109 ? 0.3296 0.1936 0.3544 -0.0349 0.0168  0.0155  106 HIS A CA  
1736 C C   . HIS A 109 ? 0.3288 0.2006 0.3670 -0.0487 0.0230  0.0182  106 HIS A C   
1737 O O   . HIS A 109 ? 0.3829 0.2402 0.4191 -0.0582 0.0263  0.0248  106 HIS A O   
1738 C CB  . HIS A 109 ? 0.3310 0.2023 0.3466 -0.0302 0.0213  0.0215  106 HIS A CB  
1739 C CG  . HIS A 109 ? 0.3791 0.2393 0.3808 -0.0185 0.0157  0.0218  106 HIS A CG  
1740 N ND1 . HIS A 109 ? 0.4232 0.2914 0.4258 -0.0076 0.0096  0.0138  106 HIS A ND1 
1741 C CD2 . HIS A 109 ? 0.3898 0.2330 0.3763 -0.0152 0.0150  0.0289  106 HIS A CD2 
1742 C CE1 . HIS A 109 ? 0.4212 0.2804 0.4125 0.0025  0.0052  0.0152  106 HIS A CE1 
1743 N NE2 . HIS A 109 ? 0.4460 0.2882 0.4265 -0.0017 0.0076  0.0244  106 HIS A NE2 
1751 N N   . TYR A 110 ? 0.3348 0.2298 0.3862 -0.0500 0.0247  0.0137  107 TYR A N   
1752 C CA  . TYR A 110 ? 0.3109 0.2203 0.3766 -0.0601 0.0312  0.0157  107 TYR A CA  
1753 C C   . TYR A 110 ? 0.3432 0.2651 0.4251 -0.0629 0.0263  0.0076  107 TYR A C   
1754 O O   . TYR A 110 ? 0.3374 0.2616 0.4173 -0.0555 0.0194  0.0007  107 TYR A O   
1755 C CB  . TYR A 110 ? 0.3128 0.2393 0.3770 -0.0565 0.0379  0.0185  107 TYR A CB  
1756 C CG  . TYR A 110 ? 0.3524 0.2682 0.4003 -0.0546 0.0430  0.0266  107 TYR A CG  
1757 C CD1 . TYR A 110 ? 0.4271 0.3337 0.4718 -0.0635 0.0499  0.0344  107 TYR A CD1 
1758 C CD2 . TYR A 110 ? 0.3755 0.2907 0.4106 -0.0446 0.0403  0.0266  107 TYR A CD2 
1759 C CE1 . TYR A 110 ? 0.4818 0.3771 0.5084 -0.0614 0.0540  0.0421  107 TYR A CE1 
1760 C CE2 . TYR A 110 ? 0.4174 0.3219 0.4363 -0.0423 0.0432  0.0337  107 TYR A CE2 
1761 C CZ  . TYR A 110 ? 0.4653 0.3589 0.4790 -0.0503 0.0498  0.0414  107 TYR A CZ  
1762 O OH  . TYR A 110 ? 0.5613 0.4426 0.5558 -0.0477 0.0522  0.0488  107 TYR A OH  
1772 N N   . PRO A 111 ? 0.3446 0.2777 0.4433 -0.0734 0.0300  0.0081  108 PRO A N   
1773 C CA  . PRO A 111 ? 0.3092 0.2561 0.4250 -0.0763 0.0243  0.0002  108 PRO A CA  
1774 C C   . PRO A 111 ? 0.2980 0.2676 0.4200 -0.0695 0.0247  -0.0032 108 PRO A C   
1775 O O   . PRO A 111 ? 0.3685 0.3566 0.5068 -0.0734 0.0273  -0.0044 108 PRO A O   
1776 C CB  . PRO A 111 ? 0.4103 0.3603 0.5421 -0.0911 0.0285  0.0032  108 PRO A CB  
1777 C CG  . PRO A 111 ? 0.4364 0.3888 0.5624 -0.0937 0.0407  0.0127  108 PRO A CG  
1778 C CD  . PRO A 111 ? 0.4092 0.3417 0.5111 -0.0839 0.0397  0.0164  108 PRO A CD  
1786 N N   . LEU A 112 ? 0.2840 0.2518 0.3925 -0.0592 0.0219  -0.0047 109 LEU A N   
1787 C CA  . LEU A 112 ? 0.2528 0.2359 0.3628 -0.0528 0.0201  -0.0078 109 LEU A CA  
1788 C C   . LEU A 112 ? 0.3065 0.2981 0.4285 -0.0538 0.0119  -0.0153 109 LEU A C   
1789 O O   . LEU A 112 ? 0.2910 0.2739 0.4137 -0.0562 0.0055  -0.0197 109 LEU A O   
1790 C CB  . LEU A 112 ? 0.2849 0.2628 0.3776 -0.0442 0.0179  -0.0078 109 LEU A CB  
1791 C CG  . LEU A 112 ? 0.3331 0.3036 0.4132 -0.0417 0.0236  -0.0014 109 LEU A CG  
1792 C CD1 . LEU A 112 ? 0.3294 0.3002 0.3969 -0.0345 0.0207  -0.0025 109 LEU A CD1 
1793 C CD2 . LEU A 112 ? 0.3682 0.3468 0.4509 -0.0431 0.0309  0.0029  109 LEU A CD2 
1805 N N   A LYS A 113 ? 0.2591 0.2663 0.3888 -0.0509 0.0109  -0.0172 110 LYS A N   
1806 N N   B LYS A 113 ? 0.2594 0.2667 0.3894 -0.0509 0.0109  -0.0172 110 LYS A N   
1807 C CA  A LYS A 113 ? 0.2660 0.2824 0.4071 -0.0508 0.0020  -0.0242 110 LYS A CA  
1808 C CA  B LYS A 113 ? 0.2669 0.2833 0.4081 -0.0509 0.0019  -0.0243 110 LYS A CA  
1809 C C   A LYS A 113 ? 0.2773 0.2866 0.4031 -0.0441 -0.0064 -0.0281 110 LYS A C   
1810 C C   B LYS A 113 ? 0.2783 0.2874 0.4039 -0.0441 -0.0064 -0.0281 110 LYS A C   
1811 O O   A LYS A 113 ? 0.2919 0.2992 0.4199 -0.0451 -0.0147 -0.0342 110 LYS A O   
1812 O O   B LYS A 113 ? 0.2925 0.2990 0.4199 -0.0452 -0.0146 -0.0341 110 LYS A O   
1813 C CB  A LYS A 113 ? 0.2863 0.3217 0.4410 -0.0481 0.0026  -0.0255 110 LYS A CB  
1814 C CB  B LYS A 113 ? 0.2869 0.3222 0.4417 -0.0483 0.0025  -0.0255 110 LYS A CB  
1815 C CG  A LYS A 113 ? 0.3442 0.3933 0.5185 -0.0555 0.0108  -0.0235 110 LYS A CG  
1816 C CG  B LYS A 113 ? 0.3443 0.3928 0.5177 -0.0554 0.0113  -0.0231 110 LYS A CG  
1817 C CD  A LYS A 113 ? 0.4028 0.4576 0.5962 -0.0655 0.0061  -0.0277 110 LYS A CD  
1818 C CD  B LYS A 113 ? 0.4101 0.4617 0.6010 -0.0665 0.0083  -0.0261 110 LYS A CD  
1819 C CE  A LYS A 113 ? 0.4892 0.5597 0.7030 -0.0756 0.0159  -0.0248 110 LYS A CE  
1820 C CE  B LYS A 113 ? 0.4862 0.5552 0.6979 -0.0757 0.0179  -0.0234 110 LYS A CE  
1821 N NZ  A LYS A 113 ? 0.5902 0.6444 0.7934 -0.0834 0.0255  -0.0166 110 LYS A NZ  
1822 N NZ  B LYS A 113 ? 0.4781 0.5441 0.7030 -0.0902 0.0165  -0.0238 110 LYS A NZ  
1849 N N   . ARG A 114 ? 0.2865 0.2924 0.3962 -0.0380 -0.0042 -0.0249 111 ARG A N   
1850 C CA  . ARG A 114 ? 0.2954 0.2958 0.3888 -0.0330 -0.0098 -0.0272 111 ARG A CA  
1851 C C   . ARG A 114 ? 0.2881 0.2851 0.3668 -0.0299 -0.0043 -0.0217 111 ARG A C   
1852 O O   . ARG A 114 ? 0.2817 0.2804 0.3620 -0.0303 0.0018  -0.0170 111 ARG A O   
1853 C CB  . ARG A 114 ? 0.3711 0.3774 0.4645 -0.0297 -0.0185 -0.0312 111 ARG A CB  
1854 C CG  . ARG A 114 ? 0.3920 0.4061 0.4907 -0.0269 -0.0186 -0.0293 111 ARG A CG  
1855 C CD  . ARG A 114 ? 0.4052 0.4221 0.5016 -0.0222 -0.0301 -0.0337 111 ARG A CD  
1856 N NE  . ARG A 114 ? 0.4657 0.4883 0.5755 -0.0246 -0.0377 -0.0406 111 ARG A NE  
1857 C CZ  . ARG A 114 ? 0.4465 0.4656 0.5475 -0.0222 -0.0480 -0.0454 111 ARG A CZ  
1858 N NH1 . ARG A 114 ? 0.4397 0.4505 0.5181 -0.0175 -0.0516 -0.0435 111 ARG A NH1 
1859 N NH2 . ARG A 114 ? 0.5188 0.5420 0.6325 -0.0255 -0.0550 -0.0522 111 ARG A NH2 
1874 N N   . ILE A 115 ? 0.2509 0.2443 0.3154 -0.0271 -0.0063 -0.0229 112 ILE A N   
1875 C CA  . ILE A 115 ? 0.2420 0.2347 0.2944 -0.0255 -0.0015 -0.0183 112 ILE A CA  
1876 C C   . ILE A 115 ? 0.2641 0.2589 0.3023 -0.0238 -0.0048 -0.0186 112 ILE A C   
1877 O O   . ILE A 115 ? 0.2635 0.2582 0.2973 -0.0225 -0.0098 -0.0232 112 ILE A O   
1878 C CB  . ILE A 115 ? 0.2827 0.2711 0.3325 -0.0243 0.0019  -0.0184 112 ILE A CB  
1879 C CG1 . ILE A 115 ? 0.3362 0.3222 0.3815 -0.0215 -0.0026 -0.0251 112 ILE A CG1 
1880 C CG2 . ILE A 115 ? 0.2822 0.2652 0.3413 -0.0270 0.0059  -0.0157 112 ILE A CG2 
1881 C CD1 . ILE A 115 ? 0.3495 0.3313 0.3904 -0.0174 -0.0002 -0.0262 112 ILE A CD1 
1893 N N   . ALA A 116 ? 0.2778 0.2735 0.3074 -0.0246 -0.0021 -0.0135 113 ALA A N   
1894 C CA  . ALA A 116 ? 0.3141 0.3113 0.3287 -0.0255 -0.0038 -0.0119 113 ALA A CA  
1895 C C   . ALA A 116 ? 0.2989 0.3008 0.3083 -0.0272 0.0018  -0.0083 113 ALA A C   
1896 O O   . ALA A 116 ? 0.2934 0.2938 0.3053 -0.0285 0.0045  -0.0046 113 ALA A O   
1897 C CB  . ALA A 116 ? 0.2941 0.2858 0.3028 -0.0263 -0.0083 -0.0089 113 ALA A CB  
1903 N N   . VAL A 117 ? 0.2568 0.2661 0.2596 -0.0267 0.0033  -0.0103 114 VAL A N   
1904 C CA  . VAL A 117 ? 0.2349 0.2539 0.2367 -0.0271 0.0083  -0.0088 114 VAL A CA  
1905 C C   . VAL A 117 ? 0.2765 0.3035 0.2660 -0.0325 0.0095  -0.0056 114 VAL A C   
1906 O O   . VAL A 117 ? 0.3050 0.3353 0.2858 -0.0322 0.0088  -0.0081 114 VAL A O   
1907 C CB  . VAL A 117 ? 0.3036 0.3274 0.3101 -0.0207 0.0096  -0.0149 114 VAL A CB  
1908 C CG1 . VAL A 117 ? 0.3401 0.3777 0.3468 -0.0193 0.0138  -0.0145 114 VAL A CG1 
1909 C CG2 . VAL A 117 ? 0.3610 0.3733 0.3781 -0.0179 0.0083  -0.0164 114 VAL A CG2 
1919 N N   . MET A 118 ? 0.2687 0.2989 0.2564 -0.0380 0.0115  -0.0003 115 MET A N   
1920 C CA  . MET A 118 ? 0.2923 0.3289 0.2684 -0.0462 0.0129  0.0042  115 MET A CA  
1921 C C   . MET A 118 ? 0.3286 0.3851 0.3100 -0.0482 0.0181  0.0041  115 MET A C   
1922 O O   . MET A 118 ? 0.3005 0.3584 0.2900 -0.0475 0.0183  0.0050  115 MET A O   
1923 C CB  . MET A 118 ? 0.3101 0.3315 0.2793 -0.0526 0.0091  0.0105  115 MET A CB  
1924 C CG  . MET A 118 ? 0.3449 0.3490 0.3081 -0.0502 0.0031  0.0107  115 MET A CG  
1925 S SD  . MET A 118 ? 0.3844 0.3693 0.3399 -0.0545 -0.0019 0.0164  115 MET A SD  
1926 C CE  . MET A 118 ? 0.4359 0.4171 0.4070 -0.0459 -0.0018 0.0124  115 MET A CE  
1936 N N   . SER A 119 ? 0.2754 0.3484 0.2516 -0.0506 0.0222  0.0031  116 SER A N   
1937 C CA  . SER A 119 ? 0.2874 0.3848 0.2696 -0.0541 0.0274  0.0032  116 SER A CA  
1938 C C   . SER A 119 ? 0.2785 0.3855 0.2759 -0.0440 0.0280  -0.0023 116 SER A C   
1939 O O   . SER A 119 ? 0.3020 0.4213 0.3074 -0.0464 0.0287  -0.0008 116 SER A O   
1940 C CB  . SER A 119 ? 0.3659 0.4619 0.3444 -0.0673 0.0267  0.0111  116 SER A CB  
1941 O OG  . SER A 119 ? 0.3744 0.4572 0.3360 -0.0762 0.0251  0.0168  116 SER A OG  
1947 N N   . ALA A 120 ? 0.2832 0.3827 0.2837 -0.0329 0.0265  -0.0084 117 ALA A N   
1948 C CA  . ALA A 120 ? 0.2553 0.3598 0.2670 -0.0224 0.0261  -0.0134 117 ALA A CA  
1949 C C   . ALA A 120 ? 0.2743 0.4052 0.2902 -0.0163 0.0303  -0.0196 117 ALA A C   
1950 O O   . ALA A 120 ? 0.2982 0.4358 0.3073 -0.0144 0.0331  -0.0238 117 ALA A O   
1951 C CB  . ALA A 120 ? 0.3057 0.3898 0.3180 -0.0142 0.0224  -0.0174 117 ALA A CB  
1957 N N   . PRO A 121 ? 0.2633 0.4103 0.2899 -0.0119 0.0306  -0.0212 118 PRO A N   
1958 C CA  . PRO A 121 ? 0.2795 0.4541 0.3128 -0.0029 0.0343  -0.0288 118 PRO A CA  
1959 C C   . PRO A 121 ? 0.3251 0.4886 0.3604 0.0140  0.0306  -0.0371 118 PRO A C   
1960 O O   . PRO A 121 ? 0.3352 0.4745 0.3706 0.0178  0.0252  -0.0356 118 PRO A O   
1961 C CB  . PRO A 121 ? 0.2964 0.4923 0.3417 -0.0061 0.0341  -0.0263 118 PRO A CB  
1962 C CG  . PRO A 121 ? 0.3311 0.5009 0.3756 -0.0075 0.0278  -0.0209 118 PRO A CG  
1963 C CD  . PRO A 121 ? 0.2909 0.4333 0.3235 -0.0148 0.0272  -0.0162 118 PRO A CD  
1971 N N   . LYS A 122 ? 0.3072 0.4880 0.3427 0.0240  0.0337  -0.0461 119 LYS A N   
1972 C CA  . LYS A 122 ? 0.3183 0.4870 0.3544 0.0412  0.0291  -0.0550 119 LYS A CA  
1973 C C   . LYS A 122 ? 0.3582 0.5439 0.4065 0.0528  0.0269  -0.0588 119 LYS A C   
1974 O O   . LYS A 122 ? 0.4296 0.5988 0.4777 0.0670  0.0209  -0.0642 119 LYS A O   
1975 C CB  . LYS A 122 ? 0.3812 0.5542 0.4087 0.0492  0.0317  -0.0647 119 LYS A CB  
1976 C CG  . LYS A 122 ? 0.4529 0.6627 0.4846 0.0567  0.0384  -0.0725 119 LYS A CG  
1977 C CD  . LYS A 122 ? 0.5143 0.7210 0.5323 0.0644  0.0404  -0.0822 119 LYS A CD  
1978 C CE  . LYS A 122 ? 0.6263 0.8621 0.6487 0.0815  0.0444  -0.0949 119 LYS A CE  
1979 N NZ  . LYS A 122 ? 0.9891 1.2142 1.0197 0.0993  0.0365  -0.1017 119 LYS A NZ  
1993 N N   . GLU A 123 ? 0.3278 0.5454 0.3865 0.0469  0.0309  -0.0563 120 GLU A N   
1994 C CA  . GLU A 123 ? 0.4316 0.6685 0.5040 0.0564  0.0275  -0.0591 120 GLU A CA  
1995 C C   . GLU A 123 ? 0.4464 0.7097 0.5284 0.0411  0.0307  -0.0521 120 GLU A C   
1996 O O   . GLU A 123 ? 0.3909 0.6626 0.4687 0.0254  0.0369  -0.0470 120 GLU A O   
1997 C CB  . GLU A 123 ? 0.4433 0.7066 0.5228 0.0748  0.0292  -0.0718 120 GLU A CB  
1998 C CG  . GLU A 123 ? 0.6367 0.9426 0.7219 0.0696  0.0398  -0.0754 120 GLU A CG  
1999 C CD  . GLU A 123 ? 0.7932 1.0982 0.8669 0.0774  0.0448  -0.0841 120 GLU A CD  
2000 O OE1 . GLU A 123 ? 0.9234 1.1924 0.9845 0.0847  0.0393  -0.0869 120 GLU A OE1 
2001 O OE2 . GLU A 123 ? 1.0029 1.3438 1.0794 0.0757  0.0543  -0.0882 120 GLU A OE2 
2008 N N   . LYS A 124 ? 0.4119 0.6871 0.5056 0.0459  0.0254  -0.0520 121 LYS A N   
2009 C CA  . LYS A 124 ? 0.4847 0.7870 0.5894 0.0321  0.0267  -0.0469 121 LYS A CA  
2010 C C   . LYS A 124 ? 0.5466 0.8827 0.6698 0.0454  0.0231  -0.0542 121 LYS A C   
2011 O O   . LYS A 124 ? 0.4510 0.7736 0.5745 0.0630  0.0152  -0.0586 121 LYS A O   
2012 C CB  . LYS A 124 ? 0.4902 0.7647 0.5880 0.0202  0.0210  -0.0369 121 LYS A CB  
2013 C CG  . LYS A 124 ? 0.5180 0.7672 0.6010 0.0045  0.0245  -0.0291 121 LYS A CG  
2014 C CD  . LYS A 124 ? 0.7838 1.0558 0.8669 -0.0113 0.0325  -0.0264 121 LYS A CD  
2015 C CE  . LYS A 124 ? 0.7754 1.0495 0.8593 -0.0298 0.0307  -0.0181 121 LYS A CE  
2016 N NZ  . LYS A 124 ? 0.8223 1.1130 0.9029 -0.0468 0.0383  -0.0140 121 LYS A NZ  
2030 N N   . SER A 125 ? 0.4177 0.7976 0.5561 0.0369  0.0286  -0.0554 122 SER A N   
2031 C CA  . SER A 125 ? 0.4870 0.9064 0.6470 0.0477  0.0251  -0.0626 122 SER A CA  
2032 C C   . SER A 125 ? 0.4628 0.8805 0.6292 0.0397  0.0158  -0.0564 122 SER A C   
2033 O O   . SER A 125 ? 0.4597 0.8517 0.6149 0.0229  0.0143  -0.0468 122 SER A O   
2034 C CB  . SER A 125 ? 0.4631 0.9357 0.6389 0.0409  0.0361  -0.0670 122 SER A CB  
2035 O OG  . SER A 125 ? 0.4342 0.9159 0.6107 0.0142  0.0406  -0.0571 122 SER A OG  
2041 N N   A ASP A 126 ? 0.5309 1.1750 0.4985 0.1063  0.0701  -0.0670 123 ASP A N   
2042 N N   B ASP A 126 ? 0.5309 1.1768 0.4983 0.1055  0.0705  -0.0668 123 ASP A N   
2043 C CA  A ASP A 126 ? 0.5324 1.2005 0.5198 0.0921  0.0692  -0.0508 123 ASP A CA  
2044 C CA  B ASP A 126 ? 0.5325 1.1989 0.5197 0.0916  0.0689  -0.0505 123 ASP A CA  
2045 C C   A ASP A 126 ? 0.5483 1.2522 0.5301 0.0550  0.0783  -0.0387 123 ASP A C   
2046 C C   B ASP A 126 ? 0.5474 1.2552 0.5312 0.0556  0.0785  -0.0387 123 ASP A C   
2047 O O   A ASP A 126 ? 0.5077 1.1897 0.4913 0.0293  0.0734  -0.0250 123 ASP A O   
2048 O O   B ASP A 126 ? 0.4994 1.1924 0.4880 0.0308  0.0740  -0.0252 123 ASP A O   
2049 C CB  A ASP A 126 ? 0.5999 1.3207 0.6124 0.1209  0.0704  -0.0576 123 ASP A CB  
2050 C CB  B ASP A 126 ? 0.6062 1.3154 0.6181 0.1226  0.0683  -0.0569 123 ASP A CB  
2051 C CG  A ASP A 126 ? 0.5741 1.2506 0.5916 0.1588  0.0599  -0.0662 123 ASP A CG  
2052 C CG  B ASP A 126 ? 0.5280 1.2948 0.5437 0.1460  0.0790  -0.0770 123 ASP A CG  
2053 O OD1 A ASP A 126 ? 0.5258 1.1307 0.5330 0.1550  0.0511  -0.0614 123 ASP A OD1 
2054 O OD1 B ASP A 126 ? 0.5313 1.3277 0.5312 0.1281  0.0913  -0.0810 123 ASP A OD1 
2055 O OD2 A ASP A 126 ? 0.5075 1.2213 0.5411 0.1922  0.0601  -0.0779 123 ASP A OD2 
2056 O OD2 B ASP A 126 ? 0.6425 1.4246 0.6759 0.1835  0.0747  -0.0887 123 ASP A OD2 
2065 N N   . ASP A 127 ? 0.5056 1.2650 0.4806 0.0509  0.0923  -0.0444 124 ASP A N   
2066 C CA  . ASP A 127 ? 0.5688 1.3589 0.5362 0.0117  0.1027  -0.0302 124 ASP A CA  
2067 C C   . ASP A 127 ? 0.5548 1.2772 0.4966 -0.0139 0.0949  -0.0152 124 ASP A C   
2068 O O   . ASP A 127 ? 0.5123 1.2259 0.4570 -0.0450 0.0940  -0.0004 124 ASP A O   
2069 C CB  . ASP A 127 ? 0.6363 1.4912 0.5921 0.0099  0.1210  -0.0377 124 ASP A CB  
2070 C CG  . ASP A 127 ? 0.6673 1.5826 0.6531 0.0388  0.1235  -0.0561 124 ASP A CG  
2071 O OD1 . ASP A 127 ? 0.8112 1.7442 0.8267 0.0505  0.1166  -0.0571 124 ASP A OD1 
2072 O OD2 . ASP A 127 ? 0.8168 1.7620 0.7955 0.0503  0.1305  -0.0698 124 ASP A OD2 
2078 N N   . GLY A 128 ? 0.5227 1.1980 0.4408 -0.0002 0.0880  -0.0211 125 GLY A N   
2079 C CA  . GLY A 128 ? 0.4877 1.1031 0.3838 -0.0189 0.0776  -0.0088 125 GLY A CA  
2080 C C   . GLY A 128 ? 0.5117 1.0839 0.4270 -0.0268 0.0650  -0.0030 125 GLY A C   
2081 O O   . GLY A 128 ? 0.5666 1.1094 0.4756 -0.0505 0.0597  0.0098  125 GLY A O   
2085 N N   . LEU A 129 ? 0.4443 1.0109 0.3818 -0.0064 0.0601  -0.0124 126 LEU A N   
2086 C CA  . LEU A 129 ? 0.4440 0.9764 0.3964 -0.0150 0.0502  -0.0079 126 LEU A CA  
2087 C C   . LEU A 129 ? 0.4767 1.0436 0.4462 -0.0360 0.0543  0.0003  126 LEU A C   
2088 O O   . LEU A 129 ? 0.4484 0.9902 0.4211 -0.0564 0.0485  0.0054  126 LEU A O   
2089 C CB  . LEU A 129 ? 0.5170 1.0291 0.4824 0.0090  0.0443  -0.0162 126 LEU A CB  
2090 C CG  . LEU A 129 ? 0.6009 1.0668 0.5545 0.0230  0.0374  -0.0270 126 LEU A CG  
2091 C CD1 . LEU A 129 ? 0.5527 1.0065 0.5180 0.0481  0.0357  -0.0347 126 LEU A CD1 
2092 C CD2 . LEU A 129 ? 0.5973 1.0192 0.5492 0.0080  0.0274  -0.0254 126 LEU A CD2 
2104 N N   . ILE A 130 ? 0.4411 1.0688 0.4240 -0.0306 0.0634  -0.0018 127 ILE A N   
2105 C CA  . ILE A 130 ? 0.5078 1.1775 0.5088 -0.0536 0.0669  0.0028  127 ILE A CA  
2106 C C   . ILE A 130 ? 0.4745 1.1304 0.4634 -0.0895 0.0706  0.0128  127 ILE A C   
2107 O O   . ILE A 130 ? 0.4872 1.1336 0.4860 -0.1135 0.0666  0.0157  127 ILE A O   
2108 C CB  . ILE A 130 ? 0.5114 1.2594 0.5305 -0.0412 0.0762  -0.0034 127 ILE A CB  
2109 C CG1 . ILE A 130 ? 0.6028 1.3577 0.6373 -0.0082 0.0676  -0.0089 127 ILE A CG1 
2110 C CG2 . ILE A 130 ? 0.5020 1.3048 0.5382 -0.0733 0.0832  -0.0006 127 ILE A CG2 
2111 C CD1 . ILE A 130 ? 0.5614 1.3700 0.6072 0.0231  0.0728  -0.0189 127 ILE A CD1 
2123 N N   . GLU A 131 ? 0.4962 1.1466 0.4608 -0.0935 0.0773  0.0183  128 GLU A N   
2124 C CA  . GLU A 131 ? 0.4826 1.1139 0.4297 -0.1281 0.0805  0.0335  128 GLU A CA  
2125 C C   . GLU A 131 ? 0.5631 1.1203 0.5039 -0.1361 0.0648  0.0381  128 GLU A C   
2126 O O   . GLU A 131 ? 0.5373 1.0748 0.4797 -0.1652 0.0630  0.0467  128 GLU A O   
2127 C CB  . GLU A 131 ? 0.6109 1.2533 0.5262 -0.1272 0.0904  0.0402  128 GLU A CB  
2128 C CG  . GLU A 131 ? 0.9859 1.5932 0.8706 -0.1582 0.0914  0.0618  128 GLU A CG  
2129 C CD  . GLU A 131 ? 1.1612 1.7730 1.0061 -0.1500 0.0975  0.0677  128 GLU A CD  
2130 O OE1 . GLU A 131 ? 0.8426 1.5074 0.6895 -0.1284 0.1079  0.0527  128 GLU A OE1 
2131 O OE2 . GLU A 131 ? 1.2052 1.7677 1.0159 -0.1628 0.0904  0.0860  128 GLU A OE2 
2138 N N   . HIS A 132 ? 0.5256 1.0427 0.4629 -0.1110 0.0532  0.0302  129 HIS A N   
2139 C CA  . HIS A 132 ? 0.4941 0.9527 0.4333 -0.1149 0.0384  0.0294  129 HIS A CA  
2140 C C   . HIS A 132 ? 0.5081 0.9753 0.4747 -0.1282 0.0363  0.0229  129 HIS A C   
2141 O O   . HIS A 132 ? 0.4616 0.8925 0.4314 -0.1443 0.0283  0.0233  129 HIS A O   
2142 C CB  . HIS A 132 ? 0.6134 1.0423 0.5524 -0.0876 0.0284  0.0180  129 HIS A CB  
2143 C CG  . HIS A 132 ? 0.7464 1.1544 0.6581 -0.0755 0.0242  0.0198  129 HIS A CG  
2144 N ND1 . HIS A 132 ? 0.8288 1.2008 0.7171 -0.0854 0.0156  0.0313  129 HIS A ND1 
2145 C CD2 . HIS A 132 ? 0.8646 1.2814 0.7678 -0.0532 0.0256  0.0101  129 HIS A CD2 
2146 C CE1 . HIS A 132 ? 0.9423 1.3088 0.8068 -0.0700 0.0118  0.0291  129 HIS A CE1 
2147 N NE2 . HIS A 132 ? 0.8362 1.2297 0.7104 -0.0512 0.0183  0.0141  129 HIS A NE2 
2155 N N   . LEU A 133 ? 0.4839 0.9971 0.4695 -0.1182 0.0415  0.0150  130 LEU A N   
2156 C CA  . LEU A 133 ? 0.4157 0.9427 0.4234 -0.1281 0.0381  0.0069  130 LEU A CA  
2157 C C   . LEU A 133 ? 0.4134 0.9626 0.4295 -0.1610 0.0427  0.0094  130 LEU A C   
2158 O O   . LEU A 133 ? 0.4596 0.9925 0.4872 -0.1781 0.0364  0.0018  130 LEU A O   
2159 C CB  . LEU A 133 ? 0.4111 0.9820 0.4316 -0.1066 0.0403  0.0016  130 LEU A CB  
2160 C CG  . LEU A 133 ? 0.4295 0.9695 0.4442 -0.0795 0.0353  -0.0009 130 LEU A CG  
2161 C CD1 . LEU A 133 ? 0.4692 1.0456 0.4913 -0.0564 0.0373  -0.0007 130 LEU A CD1 
2162 C CD2 . LEU A 133 ? 0.4526 0.9562 0.4717 -0.0843 0.0273  -0.0075 130 LEU A CD2 
2174 N N   . VAL A 134 ? 0.4728 1.0603 0.4844 -0.1720 0.0543  0.0180  131 VAL A N   
2175 C CA  . VAL A 134 ? 0.5007 1.1105 0.5211 -0.2095 0.0609  0.0217  131 VAL A CA  
2176 C C   . VAL A 134 ? 0.5357 1.0733 0.5416 -0.2333 0.0538  0.0304  131 VAL A C   
2177 O O   . VAL A 134 ? 0.5512 1.0759 0.5716 -0.2589 0.0497  0.0241  131 VAL A O   
2178 C CB  . VAL A 134 ? 0.6642 1.3331 0.6810 -0.2175 0.0774  0.0298  131 VAL A CB  
2179 C CG1 . VAL A 134 ? 0.5475 1.2484 0.5788 -0.2608 0.0860  0.0324  131 VAL A CG1 
2180 C CG2 . VAL A 134 ? 0.5986 1.3349 0.6318 -0.1869 0.0816  0.0190  131 VAL A CG2 
2190 N N   . TYR A 135 ? 0.5117 1.0010 0.4884 -0.2242 0.0508  0.0441  132 TYR A N   
2191 C CA  . TYR A 135 ? 0.5958 1.0113 0.5565 -0.2408 0.0406  0.0550  132 TYR A CA  
2192 C C   . TYR A 135 ? 0.5457 0.9197 0.5246 -0.2334 0.0250  0.0374  132 TYR A C   
2193 O O   . TYR A 135 ? 0.5811 0.9106 0.5641 -0.2544 0.0174  0.0369  132 TYR A O   
2194 C CB  . TYR A 135 ? 0.5878 0.9625 0.5128 -0.2244 0.0356  0.0708  132 TYR A CB  
2195 C CG  . TYR A 135 ? 1.0043 1.3034 0.9076 -0.2406 0.0237  0.0880  132 TYR A CG  
2196 C CD1 . TYR A 135 ? 1.1668 1.4509 1.0646 -0.2798 0.0298  0.1041  132 TYR A CD1 
2197 C CD2 . TYR A 135 ? 1.0941 1.3351 0.9851 -0.2164 0.0049  0.0873  132 TYR A CD2 
2198 C CE1 . TYR A 135 ? 1.4804 1.6844 1.3559 -0.2930 0.0170  0.1230  132 TYR A CE1 
2199 C CE2 . TYR A 135 ? 1.1785 1.3472 1.0498 -0.2256 -0.0094 0.1038  132 TYR A CE2 
2200 C CZ  . TYR A 135 ? 1.4355 1.5810 1.2973 -0.2630 -0.0038 0.1230  132 TYR A CZ  
2201 O OH  . TYR A 135 ? 1.3040 1.3674 1.1438 -0.2707 -0.0199 0.1424  132 TYR A OH  
2211 N N   . TYR A 136 ? 0.5028 0.8890 0.4923 -0.2037 0.0204  0.0223  133 TYR A N   
2212 C CA  . TYR A 136 ? 0.4909 0.8507 0.4982 -0.1960 0.0086  0.0032  133 TYR A CA  
2213 C C   . TYR A 136 ? 0.4928 0.8752 0.5230 -0.2198 0.0099  -0.0111 133 TYR A C   
2214 O O   . TYR A 136 ? 0.5276 0.8700 0.5670 -0.2298 0.0003  -0.0232 133 TYR A O   
2215 C CB  . TYR A 136 ? 0.4479 0.8293 0.4615 -0.1663 0.0082  -0.0074 133 TYR A CB  
2216 C CG  . TYR A 136 ? 0.4348 0.8029 0.4663 -0.1597 0.0000  -0.0279 133 TYR A CG  
2217 C CD1 . TYR A 136 ? 0.4540 0.7699 0.4866 -0.1539 -0.0124 -0.0355 133 TYR A CD1 
2218 C CD2 . TYR A 136 ? 0.4082 0.8209 0.4547 -0.1589 0.0043  -0.0403 133 TYR A CD2 
2219 C CE1 . TYR A 136 ? 0.4434 0.7565 0.4948 -0.1475 -0.0179 -0.0581 133 TYR A CE1 
2220 C CE2 . TYR A 136 ? 0.4182 0.8265 0.4776 -0.1547 -0.0008 -0.0596 133 TYR A CE2 
2221 C CZ  . TYR A 136 ? 0.4161 0.7774 0.4796 -0.1496 -0.0106 -0.0702 133 TYR A CZ  
2222 O OH  . TYR A 136 ? 0.4126 0.7791 0.4914 -0.1452 -0.0135 -0.0932 133 TYR A OH  
2232 N N   . SER A 137 ? 0.5084 0.9570 0.5493 -0.2279 0.0206  -0.0124 134 SER A N   
2233 C CA  . SER A 137 ? 0.5403 1.0218 0.6042 -0.2499 0.0204  -0.0294 134 SER A CA  
2234 C C   . SER A 137 ? 0.5225 0.9739 0.5890 -0.2882 0.0204  -0.0261 134 SER A C   
2235 O O   . SER A 137 ? 0.5808 1.0235 0.6648 -0.3067 0.0141  -0.0457 134 SER A O   
2236 C CB  . SER A 137 ? 0.5443 1.1099 0.6197 -0.2455 0.0293  -0.0308 134 SER A CB  
2237 O OG  . SER A 137 ? 0.9384 1.5457 1.0347 -0.2753 0.0308  -0.0430 134 SER A OG  
2243 N N   . GLN A 138 ? 0.5607 0.9932 0.6081 -0.3020 0.0273  -0.0020 135 GLN A N   
2244 C CA  . GLN A 138 ? 0.6444 1.0419 0.6907 -0.3429 0.0286  0.0064  135 GLN A CA  
2245 C C   . GLN A 138 ? 0.8476 1.1500 0.8862 -0.3424 0.0121  0.0045  135 GLN A C   
2246 O O   . GLN A 138 ? 0.8974 1.1680 0.9509 -0.3686 0.0061  -0.0082 135 GLN A O   
2247 C CB  . GLN A 138 ? 0.7041 1.1114 0.7268 -0.3590 0.0426  0.0361  135 GLN A CB  
2248 C CG  . GLN A 138 ? 0.7282 1.2312 0.7600 -0.3549 0.0589  0.0361  135 GLN A CG  
2249 C CD  . GLN A 138 ? 1.0238 1.5375 1.0285 -0.3667 0.0738  0.0629  135 GLN A CD  
2250 O OE1 . GLN A 138 ? 0.9658 1.4274 0.9491 -0.3958 0.0754  0.0839  135 GLN A OE1 
2251 N NE2 . GLN A 138 ? 1.0364 1.6177 1.0404 -0.3447 0.0849  0.0623  135 GLN A NE2 
2260 N N   A ARG A 139 ? 0.7749 1.0306 0.7918 -0.3124 0.0034  0.0154  136 ARG A N   
2261 N N   B ARG A 139 ? 0.7733 1.0299 0.7904 -0.3121 0.0035  0.0152  136 ARG A N   
2262 C CA  A ARG A 139 ? 0.8965 1.0673 0.9099 -0.3040 -0.0152 0.0106  136 ARG A CA  
2263 C CA  B ARG A 139 ? 0.8962 1.0680 0.9091 -0.3025 -0.0151 0.0109  136 ARG A CA  
2264 C C   A ARG A 139 ? 0.9110 1.0848 0.9562 -0.3006 -0.0234 -0.0260 136 ARG A C   
2265 C C   B ARG A 139 ? 0.9115 1.0839 0.9558 -0.2986 -0.0238 -0.0255 136 ARG A C   
2266 O O   A ARG A 139 ? 0.9780 1.0961 1.0329 -0.3150 -0.0342 -0.0379 136 ARG A O   
2267 O O   B ARG A 139 ? 0.9803 1.0940 1.0333 -0.3113 -0.0353 -0.0367 136 ARG A O   
2268 C CB  A ARG A 139 ? 0.9133 1.0570 0.9071 -0.2658 -0.0246 0.0193  136 ARG A CB  
2269 C CB  B ARG A 139 ? 0.9109 1.0602 0.9033 -0.2646 -0.0234 0.0206  136 ARG A CB  
2270 C CG  A ARG A 139 ? 1.0655 1.1375 1.0645 -0.2464 -0.0461 0.0068  136 ARG A CG  
2271 C CG  B ARG A 139 ? 1.0523 1.1560 1.0567 -0.2366 -0.0421 0.0001  136 ARG A CG  
2272 C CD  A ARG A 139 ? 1.1163 1.1652 1.0953 -0.2121 -0.0570 0.0177  136 ARG A CD  
2273 C CD  B ARG A 139 ? 1.1104 1.1824 1.0916 -0.2064 -0.0531 0.0148  136 ARG A CD  
2274 N NE  A ARG A 139 ? 1.0531 1.0952 1.0549 -0.1815 -0.0699 -0.0105 136 ARG A NE  
2275 N NE  B ARG A 139 ? 1.0352 1.1586 1.0026 -0.1922 -0.0421 0.0242  136 ARG A NE  
2276 C CZ  A ARG A 139 ? 0.9759 1.0709 0.9925 -0.1623 -0.0637 -0.0278 136 ARG A CZ  
2277 C CZ  B ARG A 139 ? 1.0101 1.1664 0.9901 -0.1663 -0.0418 0.0075  136 ARG A CZ  
2278 N NH1 A ARG A 139 ? 1.0243 1.1772 1.0354 -0.1657 -0.0473 -0.0206 136 ARG A NH1 
2279 N NH1 B ARG A 139 ? 1.0296 1.1832 1.0359 -0.1528 -0.0494 -0.0188 136 ARG A NH1 
2280 N NH2 A ARG A 139 ? 0.9336 1.0228 0.9716 -0.1390 -0.0743 -0.0531 136 ARG A NH2 
2281 N NH2 B ARG A 139 ? 0.8228 1.0151 0.7886 -0.1549 -0.0329 0.0164  136 ARG A NH2 
2308 N N   . MET A 140 ? 0.7145 0.9538 0.7746 -0.2824 -0.0181 -0.0445 137 MET A N   
2309 C CA  . MET A 140 ? 0.8271 1.0798 0.9117 -0.2760 -0.0244 -0.0794 137 MET A CA  
2310 C C   . MET A 140 ? 0.8819 1.1502 0.9856 -0.3113 -0.0230 -0.0972 137 MET A C   
2311 O O   . MET A 140 ? 0.9811 1.2283 1.1020 -0.3137 -0.0325 -0.1273 137 MET A O   
2312 C CB  . MET A 140 ? 0.6877 1.0101 0.7754 -0.2527 -0.0167 -0.0853 137 MET A CB  
2313 C CG  . MET A 140 ? 0.7525 1.0558 0.8296 -0.2188 -0.0205 -0.0795 137 MET A CG  
2314 S SD  . MET A 140 ? 0.6920 0.9614 0.7851 -0.1987 -0.0334 -0.1096 137 MET A SD  
2315 C CE  . MET A 140 ? 0.6918 1.0404 0.7984 -0.1996 -0.0239 -0.1321 137 MET A CE  
2326 N N   . SER A 141 ? 0.7841 1.0941 0.8875 -0.3389 -0.0113 -0.0826 138 SER A N   
2327 C CA  . SER A 141 ? 0.9407 1.2735 1.0658 -0.3767 -0.0098 -0.1011 138 SER A CA  
2328 C C   . SER A 141 ? 0.9892 1.2340 1.1140 -0.4058 -0.0180 -0.0993 138 SER A C   
2329 O O   . SER A 141 ? 1.0587 1.2913 1.2048 -0.4284 -0.0245 -0.1281 138 SER A O   
2330 C CB  . SER A 141 ? 0.8878 1.3000 1.0169 -0.3972 0.0055  -0.0870 138 SER A CB  
2331 O OG  . SER A 141 ? 0.7812 1.2735 0.9153 -0.3702 0.0094  -0.0941 138 SER A OG  
2337 N N   . ASN A 142 ? 1.0217 1.2017 1.1205 -0.4055 -0.0189 -0.0660 139 ASN A N   
2338 C CA  . ASN A 142 ? 1.2485 1.3308 1.3409 -0.4296 -0.0290 -0.0576 139 ASN A CA  
2339 C C   . ASN A 142 ? 1.2552 1.2645 1.3541 -0.4010 -0.0497 -0.0810 139 ASN A C   
2340 O O   . ASN A 142 ? 1.1364 1.0676 1.2416 -0.4194 -0.0615 -0.0893 139 ASN A O   
2341 C CB  . ASN A 142 ? 1.2013 1.2429 1.2572 -0.4372 -0.0237 -0.0101 139 ASN A CB  
2342 C CG  . ASN A 142 ? 1.2650 1.3868 1.3155 -0.4631 -0.0011 0.0104  139 ASN A CG  
2343 O OD1 . ASN A 142 ? 1.1295 1.3093 1.2055 -0.4954 0.0087  -0.0053 139 ASN A OD1 
2344 N ND2 . ASN A 142 ? 1.3041 1.4365 1.3235 -0.4475 0.0067  0.0419  139 ASN A ND2 
2351 N N   . ILE A 143 ? 1.0764 1.1099 1.1759 -0.3570 -0.0541 -0.0929 140 ILE A N   
2352 C CA  . ILE A 143 ? 1.1982 1.1874 1.3116 -0.3270 -0.0713 -0.1230 140 ILE A CA  
2353 C C   . ILE A 143 ? 1.1370 1.1649 1.2812 -0.3377 -0.0715 -0.1694 140 ILE A C   
2354 O O   . ILE A 143 ? 1.2073 1.1798 1.3670 -0.3516 -0.0828 -0.1940 140 ILE A O   
2355 C CB  . ILE A 143 ? 1.1534 1.1697 1.2602 -0.2822 -0.0727 -0.1216 140 ILE A CB  
2356 C CG1 . ILE A 143 ? 1.1284 1.0877 1.2064 -0.2664 -0.0805 -0.0849 140 ILE A CG1 
2357 C CG2 . ILE A 143 ? 1.1233 1.1371 1.2547 -0.2550 -0.0836 -0.1641 140 ILE A CG2 
2358 C CD1 . ILE A 143 ? 1.1824 1.1928 1.2471 -0.2393 -0.0731 -0.0710 140 ILE A CD1 
2370 N N   . LEU A 144 ? 1.0896 1.2114 1.2407 -0.3304 -0.0600 -0.1817 141 LEU A N   
2371 C CA  . LEU A 144 ? 1.0924 1.2673 1.2664 -0.3388 -0.0595 -0.2239 141 LEU A CA  
2372 C C   . LEU A 144 ? 1.1843 1.3686 1.3713 -0.3849 -0.0570 -0.2328 141 LEU A C   
2373 O O   . LEU A 144 ? 1.1660 1.3973 1.3717 -0.3958 -0.0582 -0.2703 141 LEU A O   
2374 C CB  . LEU A 144 ? 0.9143 1.1846 1.0846 -0.3203 -0.0482 -0.2243 141 LEU A CB  
2375 C CG  . LEU A 144 ? 1.0110 1.2790 1.1748 -0.2794 -0.0500 -0.2255 141 LEU A CG  
2376 C CD1 . LEU A 144 ? 1.0662 1.4170 1.2211 -0.2659 -0.0379 -0.2155 141 LEU A CD1 
2377 C CD2 . LEU A 144 ? 1.1532 1.3999 1.3350 -0.2655 -0.0602 -0.2684 141 LEU A CD2 
2389 N N   . ASN A 145 ? 1.2553 1.4012 1.4319 -0.4137 -0.0529 -0.1998 142 ASN A N   
2390 C CA  . ASN A 145 ? 1.2856 1.4341 1.4769 -0.4642 -0.0496 -0.2062 142 ASN A CA  
2391 C C   . ASN A 145 ? 1.1734 1.4345 1.3837 -0.4762 -0.0418 -0.2311 142 ASN A C   
2392 O O   . ASN A 145 ? 1.0198 1.2971 1.2531 -0.5079 -0.0454 -0.2634 142 ASN A O   
2393 C CB  . ASN A 145 ? 1.3840 1.4393 1.5896 -0.4798 -0.0654 -0.2339 142 ASN A CB  
2394 C CG  . ASN A 145 ? 1.3219 1.2758 1.5115 -0.5066 -0.0683 -0.1977 142 ASN A CG  
2395 O OD1 . ASN A 145 ? 1.2627 1.2230 1.4546 -0.5542 -0.0585 -0.1819 142 ASN A OD1 
2396 N ND2 . ASN A 145 ? 1.3260 1.1896 1.4984 -0.4763 -0.0818 -0.1828 142 ASN A ND2 
2403 N N   . LEU A 146 ? 1.1377 1.4759 1.3378 -0.4495 -0.0326 -0.2162 143 LEU A N   
2404 C CA  . LEU A 146 ? 1.0306 1.4773 1.2440 -0.4538 -0.0274 -0.2332 143 LEU A CA  
2405 C C   . LEU A 146 ? 1.0522 1.5292 1.2755 -0.4879 -0.0188 -0.2226 143 LEU A C   
2406 O O   . LEU A 146 ? 1.1600 1.6047 1.3788 -0.5150 -0.0114 -0.1946 143 LEU A O   
2407 C CB  . LEU A 146 ? 1.0107 1.5164 1.2073 -0.4161 -0.0197 -0.2103 143 LEU A CB  
2408 C CG  . LEU A 146 ? 1.0713 1.5560 1.2538 -0.3729 -0.0243 -0.2147 143 LEU A CG  
2409 C CD1 . LEU A 146 ? 0.9381 1.4959 1.1088 -0.3458 -0.0163 -0.1961 143 LEU A CD1 
2410 C CD2 . LEU A 146 ? 1.0877 1.5709 1.2822 -0.3691 -0.0341 -0.2585 143 LEU A CD2 
2422 N N   . ASP A 147 ? 1.1557 1.6965 1.3892 -0.4845 -0.0188 -0.2434 144 ASP A N   
2423 C CA  . ASP A 147 ? 1.2286 1.8077 1.4741 -0.5125 -0.0110 -0.2376 144 ASP A CA  
2424 C C   . ASP A 147 ? 1.0886 1.7193 1.3231 -0.5039 0.0031  -0.2021 144 ASP A C   
2425 O O   . ASP A 147 ? 0.9597 1.5952 1.1776 -0.4762 0.0059  -0.1826 144 ASP A O   
2426 C CB  . ASP A 147 ? 1.1632 1.8047 1.4200 -0.5078 -0.0159 -0.2697 144 ASP A CB  
2427 C CG  . ASP A 147 ? 1.2534 1.9817 1.4960 -0.4693 -0.0129 -0.2651 144 ASP A CG  
2428 O OD1 . ASP A 147 ? 1.3160 2.0599 1.5436 -0.4465 -0.0065 -0.2373 144 ASP A OD1 
2429 O OD2 . ASP A 147 ? 1.2458 2.0252 1.4912 -0.4619 -0.0177 -0.2895 144 ASP A OD2 
2434 N N   . GLN A 148 ? 1.2827 1.4791 1.2744 -0.4719 -0.2042 -0.2186 145 GLN A N   
2435 C CA  . GLN A 148 ? 1.2270 1.4903 1.2639 -0.4631 -0.2038 -0.2027 145 GLN A CA  
2436 C C   . GLN A 148 ? 0.9976 1.3084 1.0391 -0.4427 -0.2196 -0.2015 145 GLN A C   
2437 O O   . GLN A 148 ? 1.0152 1.3626 1.0824 -0.4222 -0.2139 -0.1898 145 GLN A O   
2438 C CB  . GLN A 148 ? 1.1907 1.4885 1.2612 -0.4894 -0.2089 -0.2006 145 GLN A CB  
2439 C CG  . GLN A 148 ? 1.1870 1.5675 1.3044 -0.4860 -0.2202 -0.1944 145 GLN A CG  
2440 C CD  . GLN A 148 ? 1.1243 1.5413 1.2730 -0.4650 -0.2043 -0.1799 145 GLN A CD  
2441 O OE1 . GLN A 148 ? 1.0950 1.4787 1.2259 -0.4483 -0.1887 -0.1739 145 GLN A OE1 
2442 N NE2 . GLN A 148 ? 0.9097 1.3961 1.1073 -0.4661 -0.2078 -0.1755 145 GLN A NE2 
2451 N N   . GLN A 149 ? 1.1417 1.4477 1.1553 -0.4476 -0.2399 -0.2134 146 GLN A N   
2452 C CA  . GLN A 149 ? 0.9920 1.3399 1.0075 -0.4297 -0.2609 -0.2107 146 GLN A CA  
2453 C C   . GLN A 149 ? 0.8872 1.2187 0.8813 -0.4016 -0.2508 -0.2047 146 GLN A C   
2454 O O   . GLN A 149 ? 0.8530 1.2290 0.8735 -0.3800 -0.2571 -0.1936 146 GLN A O   
2455 C CB  . GLN A 149 ? 1.1016 1.4344 1.0792 -0.4434 -0.2845 -0.2247 146 GLN A CB  
2456 C CG  . GLN A 149 ? 1.2020 1.5619 1.2058 -0.4707 -0.3002 -0.2306 146 GLN A CG  
2457 C CD  . GLN A 149 ? 1.2279 1.5276 1.1951 -0.4970 -0.2928 -0.2459 146 GLN A CD  
2458 O OE1 . GLN A 149 ? 1.2595 1.5204 1.2260 -0.5028 -0.2696 -0.2454 146 GLN A OE1 
2459 N NE2 . GLN A 149 ? 1.2244 1.5141 1.1608 -0.5127 -0.3140 -0.2596 146 GLN A NE2 
2468 N N   . ALA A 150 ? 1.0899 1.3568 1.0382 -0.4012 -0.2346 -0.2131 147 ALA A N   
2469 C CA  . ALA A 150 ? 1.0493 1.2960 0.9760 -0.3773 -0.2220 -0.2090 147 ALA A CA  
2470 C C   . ALA A 150 ? 0.8904 1.1677 0.8607 -0.3611 -0.2080 -0.1933 147 ALA A C   
2471 O O   . ALA A 150 ? 1.0079 1.3143 0.9867 -0.3386 -0.2118 -0.1841 147 ALA A O   
2472 C CB  . ALA A 150 ? 1.1116 1.2842 0.9941 -0.3819 -0.2022 -0.2228 147 ALA A CB  
2478 N N   . SER A 151 ? 0.9668 1.2349 0.9622 -0.3724 -0.1919 -0.1896 148 SER A N   
2479 C CA  . SER A 151 ? 0.8081 1.0969 0.8368 -0.3591 -0.1758 -0.1753 148 SER A CA  
2480 C C   . SER A 151 ? 0.8641 1.2229 0.9299 -0.3423 -0.1861 -0.1656 148 SER A C   
2481 O O   . SER A 151 ? 0.8169 1.1888 0.8917 -0.3201 -0.1781 -0.1574 148 SER A O   
2482 C CB  . SER A 151 ? 0.8489 1.1276 0.8994 -0.3783 -0.1634 -0.1704 148 SER A CB  
2483 O OG  . SER A 151 ? 1.0745 1.2911 1.0966 -0.3951 -0.1600 -0.1807 148 SER A OG  
2489 N N   . SER A 152 ? 0.9271 1.3309 1.0172 -0.3515 -0.2048 -0.1674 149 SER A N   
2490 C CA  . SER A 152 ? 0.8433 1.3153 0.9796 -0.3346 -0.2147 -0.1595 149 SER A CA  
2491 C C   . SER A 152 ? 0.7871 1.2658 0.9068 -0.3081 -0.2311 -0.1569 149 SER A C   
2492 O O   . SER A 152 ? 0.7607 1.2748 0.9097 -0.2843 -0.2296 -0.1481 149 SER A O   
2493 C CB  . SER A 152 ? 0.9140 1.4317 1.0851 -0.3518 -0.2325 -0.1634 149 SER A CB  
2494 O OG  . SER A 152 ? 0.9883 1.5704 1.2071 -0.3325 -0.2456 -0.1579 149 SER A OG  
2500 N N   . ALA A 153 ? 0.7750 1.2178 0.8452 -0.3123 -0.2466 -0.1645 150 ALA A N   
2501 C CA  . ALA A 153 ? 0.7736 1.2141 0.8167 -0.2895 -0.2629 -0.1604 150 ALA A CA  
2502 C C   . ALA A 153 ? 0.8432 1.2585 0.8700 -0.2705 -0.2414 -0.1547 150 ALA A C   
2503 O O   . ALA A 153 ? 0.8871 1.3213 0.9186 -0.2454 -0.2493 -0.1454 150 ALA A O   
2504 C CB  . ALA A 153 ? 0.7764 1.1750 0.7587 -0.3020 -0.2790 -0.1708 150 ALA A CB  
2510 N N   . GLN A 154 ? 0.9242 1.2952 0.9337 -0.2816 -0.2156 -0.1600 151 GLN A N   
2511 C CA  . GLN A 154 ? 0.9576 1.3046 0.9559 -0.2656 -0.1952 -0.1559 151 GLN A CA  
2512 C C   . GLN A 154 ? 0.8709 1.2682 0.9199 -0.2458 -0.1899 -0.1432 151 GLN A C   
2513 O O   . GLN A 154 ? 0.8099 1.2130 0.8550 -0.2224 -0.1894 -0.1367 151 GLN A O   
2514 C CB  . GLN A 154 ? 0.7840 1.0784 0.7687 -0.2816 -0.1714 -0.1632 151 GLN A CB  
2515 C CG  . GLN A 154 ? 0.8523 1.0897 0.7853 -0.2967 -0.1714 -0.1791 151 GLN A CG  
2516 C CD  . GLN A 154 ? 0.7059 0.9050 0.5902 -0.2840 -0.1645 -0.1849 151 GLN A CD  
2517 O OE1 . GLN A 154 ? 0.7652 0.9702 0.6536 -0.2654 -0.1564 -0.1773 151 GLN A OE1 
2518 N NE2 . GLN A 154 ? 0.8819 1.0419 0.7173 -0.2949 -0.1672 -0.1990 151 GLN A NE2 
2527 N N   . LEU A 155 ? 0.8661 1.2991 0.9612 -0.2554 -0.1848 -0.1404 152 LEU A N   
2528 C CA  . LEU A 155 ? 0.8047 1.2823 0.9467 -0.2391 -0.1739 -0.1314 152 LEU A CA  
2529 C C   . LEU A 155 ? 0.7244 1.2542 0.8963 -0.2157 -0.1945 -0.1271 152 LEU A C   
2530 O O   . LEU A 155 ? 0.6463 1.2027 0.8456 -0.1923 -0.1872 -0.1209 152 LEU A O   
2531 C CB  . LEU A 155 ? 0.7808 1.2753 0.9544 -0.2601 -0.1599 -0.1311 152 LEU A CB  
2532 C CG  . LEU A 155 ? 0.9121 1.3499 1.0593 -0.2780 -0.1403 -0.1309 152 LEU A CG  
2533 C CD1 . LEU A 155 ? 0.7891 1.2316 0.9538 -0.3041 -0.1317 -0.1299 152 LEU A CD1 
2534 C CD2 . LEU A 155 ? 0.8418 1.2628 0.9859 -0.2618 -0.1220 -0.1236 152 LEU A CD2 
2546 N N   . ALA A 156 ? 0.7769 1.3175 0.9428 -0.2203 -0.2219 -0.1301 153 ALA A N   
2547 C CA  . ALA A 156 ? 0.6426 1.2274 0.8385 -0.1973 -0.2473 -0.1243 153 ALA A CA  
2548 C C   . ALA A 156 ? 0.7860 1.3494 0.9497 -0.1701 -0.2565 -0.1166 153 ALA A C   
2549 O O   . ALA A 156 ? 0.7760 1.3717 0.9711 -0.1433 -0.2703 -0.1085 153 ALA A O   
2550 C CB  . ALA A 156 ? 0.7431 1.3399 0.9382 -0.2124 -0.2775 -0.1290 153 ALA A CB  
2556 N N   . ALA A 157 ? 0.7820 1.2892 0.8842 -0.1762 -0.2482 -0.1190 154 ALA A N   
2557 C CA  . ALA A 157 ? 0.6931 1.1746 0.7572 -0.1537 -0.2529 -0.1114 154 ALA A CA  
2558 C C   . ALA A 157 ? 0.7085 1.2034 0.8007 -0.1304 -0.2323 -0.1054 154 ALA A C   
2559 O O   . ALA A 157 ? 0.5995 1.0788 0.6679 -0.1078 -0.2367 -0.0975 154 ALA A O   
2560 C CB  . ALA A 157 ? 0.7291 1.1456 0.7199 -0.1704 -0.2436 -0.1189 154 ALA A CB  
2566 N N   . ILE A 158 ? 0.6750 1.1939 0.8118 -0.1363 -0.2097 -0.1085 155 ILE A N   
2567 C CA  . ILE A 158 ? 0.6604 1.1883 0.8203 -0.1167 -0.1886 -0.1044 155 ILE A CA  
2568 C C   . ILE A 158 ? 0.5807 1.1419 0.7723 -0.0818 -0.2028 -0.0964 155 ILE A C   
2569 O O   . ILE A 158 ? 0.5380 1.0818 0.7216 -0.0569 -0.1947 -0.0900 155 ILE A O   
2570 C CB  . ILE A 158 ? 0.6981 1.2433 0.8940 -0.1339 -0.1636 -0.1082 155 ILE A CB  
2571 C CG1 . ILE A 158 ? 0.6789 1.1731 0.8385 -0.1591 -0.1464 -0.1121 155 ILE A CG1 
2572 C CG2 . ILE A 158 ? 0.6590 1.2310 0.8920 -0.1118 -0.1463 -0.1047 155 ILE A CG2 
2573 C CD1 . ILE A 158 ? 0.6363 1.1314 0.8174 -0.1746 -0.1222 -0.1110 155 ILE A CD1 
2585 N N   . ASP A 159 ? 0.6615 1.2607 0.8885 -0.0781 -0.2240 -0.0955 156 ASP A N   
2586 C CA  . ASP A 159 ? 0.6558 1.2853 0.9225 -0.0447 -0.2383 -0.0884 156 ASP A CA  
2587 C C   . ASP A 159 ? 0.5954 1.1880 0.8189 -0.0196 -0.2562 -0.0768 156 ASP A C   
2588 O O   . ASP A 159 ? 0.6371 1.2354 0.8836 0.0118  -0.2563 -0.0705 156 ASP A O   
2589 C CB  . ASP A 159 ? 0.6671 1.3384 0.9754 -0.0492 -0.2640 -0.0889 156 ASP A CB  
2590 C CG  . ASP A 159 ? 0.8336 1.5556 1.2051 -0.0600 -0.2434 -0.0984 156 ASP A CG  
2591 O OD1 . ASP A 159 ? 0.8783 1.5959 1.2504 -0.0698 -0.2101 -0.1041 156 ASP A OD1 
2592 O OD2 . ASP A 159 ? 0.8734 1.6385 1.2921 -0.0604 -0.2612 -0.0995 156 ASP A OD2 
2597 N N   . ASP A 160 ? 0.6092 1.1586 0.7660 -0.0337 -0.2694 -0.0742 157 ASP A N   
2598 C CA  . ASP A 160 ? 0.5683 1.0756 0.6713 -0.0146 -0.2853 -0.0617 157 ASP A CA  
2599 C C   . ASP A 160 ? 0.6304 1.0791 0.7011 -0.0050 -0.2504 -0.0571 157 ASP A C   
2600 O O   . ASP A 160 ? 0.5795 0.9786 0.6026 0.0089  -0.2548 -0.0447 157 ASP A O   
2601 C CB  . ASP A 160 ? 0.6465 1.1158 0.6801 -0.0382 -0.3050 -0.0607 157 ASP A CB  
2602 C CG  . ASP A 160 ? 0.7660 1.2576 0.8175 -0.0422 -0.3414 -0.0567 157 ASP A CG  
2603 O OD1 . ASP A 160 ? 0.8671 1.3919 0.9715 -0.0181 -0.3597 -0.0474 157 ASP A OD1 
2604 O OD2 . ASP A 160 ? 0.8599 1.3343 0.8746 -0.0696 -0.3512 -0.0641 157 ASP A OD2 
2609 N N   . TYR A 161 ? 0.4987 0.9501 0.5914 -0.0147 -0.2177 -0.0658 158 TYR A N   
2610 C CA  . TYR A 161 ? 0.5299 0.9315 0.5996 -0.0076 -0.1865 -0.0622 158 TYR A CA  
2611 C C   . TYR A 161 ? 0.4610 0.8814 0.5730 0.0204  -0.1761 -0.0582 158 TYR A C   
2612 O O   . TYR A 161 ? 0.4273 0.8110 0.5254 0.0270  -0.1523 -0.0550 158 TYR A O   
2613 C CB  . TYR A 161 ? 0.5347 0.9225 0.6005 -0.0355 -0.1608 -0.0726 158 TYR A CB  
2614 C CG  . TYR A 161 ? 0.5069 0.8319 0.5340 -0.0362 -0.1351 -0.0700 158 TYR A CG  
2615 C CD1 . TYR A 161 ? 0.5236 0.7976 0.4942 -0.0359 -0.1364 -0.0664 158 TYR A CD1 
2616 C CD2 . TYR A 161 ? 0.4911 0.8094 0.5388 -0.0387 -0.1099 -0.0713 158 TYR A CD2 
2617 C CE1 . TYR A 161 ? 0.5568 0.7795 0.5012 -0.0364 -0.1107 -0.0660 158 TYR A CE1 
2618 C CE2 . TYR A 161 ? 0.4186 0.6842 0.4398 -0.0381 -0.0892 -0.0689 158 TYR A CE2 
2619 C CZ  . TYR A 161 ? 0.4825 0.7030 0.4561 -0.0363 -0.0889 -0.0672 158 TYR A CZ  
2620 O OH  . TYR A 161 ? 0.4619 0.6367 0.4183 -0.0361 -0.0666 -0.0668 158 TYR A OH  
2630 N N   . GLU A 162 ? 0.4701 0.9466 0.6347 0.0377  -0.1945 -0.0596 159 GLU A N   
2631 C CA  . GLU A 162 ? 0.4382 0.9384 0.6494 0.0618  -0.1806 -0.0618 159 GLU A CA  
2632 C C   . GLU A 162 ? 0.4089 0.8523 0.5869 0.0859  -0.1745 -0.0499 159 GLU A C   
2633 O O   . GLU A 162 ? 0.4137 0.8452 0.6010 0.0934  -0.1495 -0.0523 159 GLU A O   
2634 C CB  . GLU A 162 ? 0.4344 1.0042 0.7111 0.0795  -0.2038 -0.0671 159 GLU A CB  
2635 C CG  . GLU A 162 ? 0.5929 1.1771 0.9156 0.1078  -0.1894 -0.0703 159 GLU A CG  
2636 C CD  . GLU A 162 ? 0.7915 1.4112 1.1671 0.1240  -0.2089 -0.0695 159 GLU A CD  
2637 O OE1 . GLU A 162 ? 0.8667 1.4937 1.2792 0.1487  -0.1996 -0.0726 159 GLU A OE1 
2638 O OE2 . GLU A 162 ? 0.7417 1.3811 1.1224 0.1112  -0.2338 -0.0662 159 GLU A OE2 
2645 N N   . GLY A 163 ? 0.4360 0.8425 0.5722 0.0960  -0.1979 -0.0367 160 GLY A N   
2646 C CA  . GLY A 163 ? 0.4219 0.7717 0.5238 0.1152  -0.1918 -0.0245 160 GLY A CA  
2647 C C   . GLY A 163 ? 0.4527 0.7535 0.5154 0.0988  -0.1597 -0.0248 160 GLY A C   
2648 O O   . GLY A 163 ? 0.4831 0.7534 0.5406 0.1117  -0.1431 -0.0208 160 GLY A O   
2652 N N   A GLU A 164 ? 0.4545 0.7464 0.4917 0.0704  -0.1514 -0.0305 161 GLU A N   
2653 N N   B GLU A 164 ? 0.4544 0.7463 0.4919 0.0705  -0.1513 -0.0305 161 GLU A N   
2654 C CA  A GLU A 164 ? 0.4105 0.6591 0.4195 0.0561  -0.1227 -0.0321 161 GLU A CA  
2655 C CA  B GLU A 164 ? 0.4108 0.6594 0.4200 0.0565  -0.1226 -0.0320 161 GLU A CA  
2656 C C   A GLU A 164 ? 0.3987 0.6676 0.4471 0.0528  -0.0998 -0.0398 161 GLU A C   
2657 C C   B GLU A 164 ? 0.3987 0.6676 0.4472 0.0527  -0.0998 -0.0398 161 GLU A C   
2658 O O   A GLU A 164 ? 0.3860 0.6210 0.4223 0.0508  -0.0790 -0.0380 161 GLU A O   
2659 O O   B GLU A 164 ? 0.3866 0.6211 0.4223 0.0506  -0.0790 -0.0380 161 GLU A O   
2660 C CB  A GLU A 164 ? 0.4909 0.7213 0.4636 0.0289  -0.1215 -0.0379 161 GLU A CB  
2661 C CB  B GLU A 164 ? 0.4912 0.7208 0.4634 0.0295  -0.1215 -0.0376 161 GLU A CB  
2662 C CG  A GLU A 164 ? 0.5307 0.7245 0.4454 0.0278  -0.1374 -0.0298 161 GLU A CG  
2663 C CG  B GLU A 164 ? 0.5244 0.7252 0.4432 0.0287  -0.1417 -0.0297 161 GLU A CG  
2664 C CD  A GLU A 164 ? 0.5260 0.7494 0.4361 0.0218  -0.1701 -0.0302 161 GLU A CD  
2665 C CD  B GLU A 164 ? 0.5735 0.7249 0.4552 0.0436  -0.1363 -0.0163 161 GLU A CD  
2666 O OE1 A GLU A 164 ? 0.4789 0.7555 0.4400 0.0317  -0.1871 -0.0318 161 GLU A OE1 
2667 O OE1 B GLU A 164 ? 0.6447 0.7686 0.5244 0.0434  -0.1096 -0.0170 161 GLU A OE1 
2668 O OE2 A GLU A 164 ? 0.7033 0.8981 0.5591 0.0062  -0.1791 -0.0297 161 GLU A OE2 
2669 O OE2 B GLU A 164 ? 0.7225 0.8619 0.5771 0.0539  -0.1606 -0.0040 161 GLU A OE2 
2682 N N   . ILE A 165 ? 0.4184 0.7431 0.5134 0.0505  -0.1037 -0.0482 162 ILE A N   
2683 C CA  . ILE A 165 ? 0.3249 0.6692 0.4518 0.0459  -0.0822 -0.0547 162 ILE A CA  
2684 C C   . ILE A 165 ? 0.3495 0.6831 0.4861 0.0716  -0.0744 -0.0515 162 ILE A C   
2685 O O   . ILE A 165 ? 0.3286 0.6389 0.4589 0.0685  -0.0546 -0.0511 162 ILE A O   
2686 C CB  . ILE A 165 ? 0.3505 0.7603 0.5238 0.0344  -0.0861 -0.0657 162 ILE A CB  
2687 C CG1 . ILE A 165 ? 0.3946 0.8051 0.5540 0.0036  -0.0901 -0.0695 162 ILE A CG1 
2688 C CG2 . ILE A 165 ? 0.3959 0.8280 0.5989 0.0321  -0.0633 -0.0723 162 ILE A CG2 
2689 C CD1 . ILE A 165 ? 0.5404 1.0020 0.7375 -0.0190 -0.0844 -0.0794 162 ILE A CD1 
2701 N N   . THR A 166 ? 0.3473 0.6953 0.4992 0.0971  -0.0922 -0.0491 163 THR A N   
2702 C CA  . THR A 166 ? 0.3860 0.7163 0.5447 0.1233  -0.0870 -0.0466 163 THR A CA  
2703 C C   . THR A 166 ? 0.3539 0.6172 0.4640 0.1228  -0.0769 -0.0356 163 THR A C   
2704 O O   . THR A 166 ? 0.3797 0.6237 0.4902 0.1270  -0.0593 -0.0370 163 THR A O   
2705 C CB  . THR A 166 ? 0.4070 0.7560 0.5878 0.1514  -0.1139 -0.0436 163 THR A CB  
2706 O OG1 . THR A 166 ? 0.4230 0.8426 0.6603 0.1518  -0.1210 -0.0563 163 THR A OG1 
2707 C CG2 . THR A 166 ? 0.4776 0.8019 0.6654 0.1800  -0.1100 -0.0418 163 THR A CG2 
2715 N N   . LYS A 167 ? 0.3575 0.5859 0.4250 0.1148  -0.0864 -0.0260 164 LYS A N   
2716 C CA  . LYS A 167 ? 0.3754 0.5454 0.4008 0.1108  -0.0736 -0.0175 164 LYS A CA  
2717 C C   . LYS A 167 ? 0.4100 0.5713 0.4398 0.0935  -0.0488 -0.0231 164 LYS A C   
2718 O O   . LYS A 167 ? 0.3961 0.5251 0.4162 0.0969  -0.0356 -0.0194 164 LYS A O   
2719 C CB  . LYS A 167 ? 0.4617 0.6031 0.4408 0.0991  -0.0835 -0.0105 164 LYS A CB  
2720 C CG  . LYS A 167 ? 0.6428 0.7281 0.5794 0.0933  -0.0689 -0.0030 164 LYS A CG  
2721 C CD  . LYS A 167 ? 0.7966 0.8576 0.6846 0.0776  -0.0747 0.0001  164 LYS A CD  
2722 C CE  . LYS A 167 ? 0.9310 0.9763 0.7871 0.0899  -0.1011 0.0137  164 LYS A CE  
2723 N NZ  . LYS A 167 ? 1.0006 0.9928 0.8194 0.0952  -0.0938 0.0266  164 LYS A NZ  
2737 N N   . PHE A 168 ? 0.3437 0.5312 0.3875 0.0736  -0.0447 -0.0309 165 PHE A N   
2738 C CA  . PHE A 168 ? 0.2904 0.4686 0.3395 0.0566  -0.0264 -0.0341 165 PHE A CA  
2739 C C   . PHE A 168 ? 0.2831 0.4741 0.3549 0.0638  -0.0165 -0.0367 165 PHE A C   
2740 O O   . PHE A 168 ? 0.3344 0.4978 0.3987 0.0599  -0.0044 -0.0338 165 PHE A O   
2741 C CB  . PHE A 168 ? 0.2879 0.4901 0.3464 0.0340  -0.0284 -0.0409 165 PHE A CB  
2742 C CG  . PHE A 168 ? 0.3713 0.5545 0.4300 0.0142  -0.0150 -0.0419 165 PHE A CG  
2743 C CD1 . PHE A 168 ? 0.5148 0.6657 0.5682 0.0164  -0.0033 -0.0368 165 PHE A CD1 
2744 C CD2 . PHE A 168 ? 0.4765 0.6733 0.5422 -0.0075 -0.0169 -0.0473 165 PHE A CD2 
2745 C CE1 . PHE A 168 ? 0.5144 0.6487 0.5726 -0.0006 0.0038  -0.0361 165 PHE A CE1 
2746 C CE2 . PHE A 168 ? 0.4697 0.6449 0.5373 -0.0247 -0.0085 -0.0465 165 PHE A CE2 
2747 C CZ  . PHE A 168 ? 0.4599 0.6049 0.5252 -0.0202 0.0007  -0.0404 165 PHE A CZ  
2757 N N   . GLN A 169 ? 0.2859 0.5189 0.3863 0.0748  -0.0215 -0.0433 166 GLN A N   
2758 C CA  . GLN A 169 ? 0.2510 0.4964 0.3700 0.0812  -0.0090 -0.0495 166 GLN A CA  
2759 C C   . GLN A 169 ? 0.3581 0.5615 0.4599 0.0992  -0.0056 -0.0442 166 GLN A C   
2760 O O   . GLN A 169 ? 0.3267 0.5140 0.4238 0.0942  0.0077  -0.0457 166 GLN A O   
2761 C CB  . GLN A 169 ? 0.3413 0.6427 0.4998 0.0925  -0.0135 -0.0609 166 GLN A CB  
2762 C CG  . GLN A 169 ? 0.3962 0.7432 0.5752 0.0684  -0.0111 -0.0682 166 GLN A CG  
2763 C CD  . GLN A 169 ? 0.5152 0.9250 0.7408 0.0780  -0.0149 -0.0808 166 GLN A CD  
2764 O OE1 . GLN A 169 ? 0.4739 0.8965 0.7168 0.1023  -0.0319 -0.0809 166 GLN A OE1 
2765 N NE2 . GLN A 169 ? 0.5486 0.9989 0.7963 0.0582  0.0004  -0.0915 166 GLN A NE2 
2774 N N   . HIS A 170 ? 0.3667 0.5501 0.4564 0.1183  -0.0190 -0.0373 167 HIS A N   
2775 C CA  . HIS A 170 ? 0.3631 0.5012 0.4333 0.1329  -0.0165 -0.0309 167 HIS A CA  
2776 C C   . HIS A 170 ? 0.3435 0.4395 0.3853 0.1162  -0.0058 -0.0233 167 HIS A C   
2777 O O   . HIS A 170 ? 0.3882 0.4555 0.4220 0.1187  0.0028  -0.0218 167 HIS A O   
2778 C CB  . HIS A 170 ? 0.4182 0.5394 0.4765 0.1537  -0.0358 -0.0221 167 HIS A CB  
2779 C CG  . HIS A 170 ? 0.6445 0.8000 0.7388 0.1782  -0.0481 -0.0295 167 HIS A CG  
2780 N ND1 . HIS A 170 ? 0.7688 0.9801 0.8968 0.1779  -0.0577 -0.0373 167 HIS A ND1 
2781 C CD2 . HIS A 170 ? 0.8518 0.9947 0.9588 0.2043  -0.0527 -0.0314 167 HIS A CD2 
2782 C CE1 . HIS A 170 ? 0.7257 0.9615 0.8900 0.2040  -0.0674 -0.0443 167 HIS A CE1 
2783 N NE2 . HIS A 170 ? 0.8649 1.0579 1.0170 0.2216  -0.0646 -0.0412 167 HIS A NE2 
2791 N N   . PHE A 171 ? 0.3164 0.4091 0.3460 0.0989  -0.0059 -0.0201 168 PHE A N   
2792 C CA  . PHE A 171 ? 0.3195 0.3794 0.3336 0.0836  0.0054  -0.0159 168 PHE A CA  
2793 C C   . PHE A 171 ? 0.3676 0.4304 0.3968 0.0732  0.0157  -0.0192 168 PHE A C   
2794 O O   . PHE A 171 ? 0.3164 0.3499 0.3388 0.0702  0.0226  -0.0152 168 PHE A O   
2795 C CB  . PHE A 171 ? 0.3484 0.4120 0.3549 0.0680  0.0040  -0.0171 168 PHE A CB  
2796 C CG  . PHE A 171 ? 0.3474 0.3836 0.3481 0.0536  0.0160  -0.0161 168 PHE A CG  
2797 C CD1 . PHE A 171 ? 0.4773 0.4810 0.4544 0.0537  0.0218  -0.0120 168 PHE A CD1 
2798 C CD2 . PHE A 171 ? 0.4095 0.4535 0.4295 0.0389  0.0207  -0.0196 168 PHE A CD2 
2799 C CE1 . PHE A 171 ? 0.4738 0.4584 0.4543 0.0414  0.0347  -0.0142 168 PHE A CE1 
2800 C CE2 . PHE A 171 ? 0.4126 0.4333 0.4357 0.0285  0.0293  -0.0197 168 PHE A CE2 
2801 C CZ  . PHE A 171 ? 0.3837 0.3777 0.3909 0.0308  0.0374  -0.0183 168 PHE A CZ  
2811 N N   . ILE A 172 ? 0.2812 0.3790 0.3292 0.0649  0.0159  -0.0259 169 ILE A N   
2812 C CA  . ILE A 172 ? 0.2451 0.3442 0.2996 0.0517  0.0238  -0.0276 169 ILE A CA  
2813 C C   . ILE A 172 ? 0.2793 0.3673 0.3303 0.0639  0.0289  -0.0304 169 ILE A C   
2814 O O   . ILE A 172 ? 0.3290 0.3920 0.3715 0.0563  0.0332  -0.0273 169 ILE A O   
2815 C CB  . ILE A 172 ? 0.2966 0.4358 0.3665 0.0378  0.0243  -0.0341 169 ILE A CB  
2816 C CG1 . ILE A 172 ? 0.3252 0.4701 0.3968 0.0247  0.0183  -0.0324 169 ILE A CG1 
2817 C CG2 . ILE A 172 ? 0.3651 0.5008 0.4320 0.0208  0.0313  -0.0338 169 ILE A CG2 
2818 C CD1 . ILE A 172 ? 0.3809 0.5599 0.4656 0.0057  0.0188  -0.0370 169 ILE A CD1 
2830 N N   . ASP A 173 ? 0.2914 0.3971 0.3511 0.0833  0.0269  -0.0372 170 ASP A N   
2831 C CA  . ASP A 173 ? 0.3342 0.4285 0.3928 0.0971  0.0326  -0.0436 170 ASP A CA  
2832 C C   . ASP A 173 ? 0.3709 0.4148 0.4080 0.1016  0.0320  -0.0348 170 ASP A C   
2833 O O   . ASP A 173 ? 0.3896 0.4132 0.4183 0.0979  0.0385  -0.0376 170 ASP A O   
2834 C CB  . ASP A 173 ? 0.3347 0.4538 0.4132 0.1219  0.0276  -0.0521 170 ASP A CB  
2835 C CG  . ASP A 173 ? 0.4309 0.6075 0.5391 0.1174  0.0324  -0.0655 170 ASP A CG  
2836 O OD1 . ASP A 173 ? 0.3833 0.5761 0.4900 0.0933  0.0417  -0.0681 170 ASP A OD1 
2837 O OD2 . ASP A 173 ? 0.4945 0.7000 0.6290 0.1375  0.0263  -0.0730 170 ASP A OD2 
2842 N N   A ASP A 174 ? 0.3308 0.3537 0.3563 0.1065  0.0250  -0.0247 171 ASP A N   
2843 N N   B ASP A 174 ? 0.3308 0.3537 0.3562 0.1071  0.0248  -0.0247 171 ASP A N   
2844 C CA  A ASP A 174 ? 0.4085 0.3852 0.4138 0.1077  0.0266  -0.0163 171 ASP A CA  
2845 C CA  B ASP A 174 ? 0.4086 0.3851 0.4136 0.1074  0.0265  -0.0159 171 ASP A CA  
2846 C C   A ASP A 174 ? 0.3619 0.3237 0.3656 0.0867  0.0336  -0.0129 171 ASP A C   
2847 C C   B ASP A 174 ? 0.3622 0.3257 0.3668 0.0867  0.0337  -0.0136 171 ASP A C   
2848 O O   A ASP A 174 ? 0.4029 0.3341 0.3977 0.0847  0.0368  -0.0103 171 ASP A O   
2849 O O   B ASP A 174 ? 0.3938 0.3297 0.3905 0.0849  0.0370  -0.0126 171 ASP A O   
2850 C CB  A ASP A 174 ? 0.4071 0.3667 0.3954 0.1134  0.0195  -0.0065 171 ASP A CB  
2851 C CB  B ASP A 174 ? 0.4046 0.3646 0.3926 0.1096  0.0206  -0.0060 171 ASP A CB  
2852 C CG  A ASP A 174 ? 0.4783 0.4437 0.4665 0.1364  0.0066  -0.0063 171 ASP A CG  
2853 C CG  B ASP A 174 ? 0.4506 0.3662 0.4180 0.1021  0.0269  0.0030  171 ASP A CG  
2854 O OD1 A ASP A 174 ? 0.4764 0.4586 0.4837 0.1512  0.0053  -0.0156 171 ASP A OD1 
2855 O OD1 B ASP A 174 ? 0.4729 0.3567 0.4266 0.1115  0.0260  0.0067  171 ASP A OD1 
2856 O OD2 A ASP A 174 ? 0.5552 0.5093 0.5250 0.1391  -0.0028 0.0026  171 ASP A OD2 
2857 O OD2 B ASP A 174 ? 0.3926 0.3053 0.3603 0.0861  0.0337  0.0052  171 ASP A OD2 
2866 N N   . ILE A 175 ? 0.3360 0.3179 0.3509 0.0710  0.0340  -0.0129 172 ILE A N   
2867 C CA  . ILE A 175 ? 0.3159 0.2853 0.3362 0.0531  0.0363  -0.0091 172 ILE A CA  
2868 C C   . ILE A 175 ? 0.3430 0.3139 0.3615 0.0467  0.0368  -0.0132 172 ILE A C   
2869 O O   . ILE A 175 ? 0.3403 0.2875 0.3545 0.0395  0.0365  -0.0103 172 ILE A O   
2870 C CB  . ILE A 175 ? 0.2916 0.2772 0.3252 0.0394  0.0342  -0.0079 172 ILE A CB  
2871 C CG1 . ILE A 175 ? 0.3256 0.3047 0.3556 0.0430  0.0361  -0.0065 172 ILE A CG1 
2872 C CG2 . ILE A 175 ? 0.3327 0.3066 0.3778 0.0229  0.0317  -0.0032 172 ILE A CG2 
2873 C CD1 . ILE A 175 ? 0.3423 0.3354 0.3841 0.0314  0.0346  -0.0087 172 ILE A CD1 
2886 N N   . MET A 176 ? 0.3115 0.3113 0.3324 0.0477  0.0383  -0.0213 173 MET A N   
2887 C CA  . MET A 176 ? 0.3182 0.3213 0.3314 0.0360  0.0413  -0.0266 173 MET A CA  
2888 C C   . MET A 176 ? 0.3656 0.3468 0.3659 0.0467  0.0460  -0.0337 173 MET A C   
2889 O O   . MET A 176 ? 0.3991 0.3683 0.3853 0.0339  0.0475  -0.0369 173 MET A O   
2890 C CB  . MET A 176 ? 0.3286 0.3704 0.3472 0.0308  0.0461  -0.0356 173 MET A CB  
2891 C CG  . MET A 176 ? 0.3544 0.4130 0.3826 0.0159  0.0408  -0.0288 173 MET A CG  
2892 S SD  . MET A 176 ? 0.3650 0.4035 0.3820 -0.0119 0.0338  -0.0183 173 MET A SD  
2893 C CE  . MET A 176 ? 0.4339 0.4690 0.4684 -0.0177 0.0248  -0.0085 173 MET A CE  
2903 N N   . THR A 177 ? 0.3329 0.3053 0.3347 0.0690  0.0468  -0.0363 174 THR A N   
2904 C CA  . THR A 177 ? 0.3805 0.3247 0.3705 0.0809  0.0501  -0.0429 174 THR A CA  
2905 C C   . THR A 177 ? 0.3989 0.3032 0.3753 0.0690  0.0473  -0.0347 174 THR A C   
2906 O O   . THR A 177 ? 0.4295 0.3091 0.3919 0.0690  0.0500  -0.0416 174 THR A O   
2907 C CB  . THR A 177 ? 0.4694 0.4074 0.4644 0.1074  0.0467  -0.0431 174 THR A CB  
2908 O OG1 . THR A 177 ? 0.5467 0.5266 0.5614 0.1192  0.0481  -0.0533 174 THR A OG1 
2909 C CG2 . THR A 177 ? 0.5603 0.4596 0.5428 0.1208  0.0484  -0.0485 174 THR A CG2 
2917 N N   . ASN A 178 ? 0.3512 0.2500 0.3341 0.0582  0.0427  -0.0220 175 ASN A N   
2918 C CA  . ASN A 178 ? 0.3993 0.2650 0.3784 0.0493  0.0407  -0.0142 175 ASN A CA  
2919 C C   . ASN A 178 ? 0.3796 0.2505 0.3712 0.0277  0.0348  -0.0076 175 ASN A C   
2920 O O   . ASN A 178 ? 0.3904 0.2483 0.3941 0.0205  0.0333  -0.0001 175 ASN A O   
2921 C CB  . ASN A 178 ? 0.4303 0.2804 0.4085 0.0592  0.0426  -0.0064 175 ASN A CB  
2922 C CG  . ASN A 178 ? 0.4028 0.2324 0.3648 0.0797  0.0431  -0.0095 175 ASN A CG  
2923 O OD1 . ASN A 178 ? 0.4599 0.2659 0.4111 0.0831  0.0439  -0.0156 175 ASN A OD1 
2924 N ND2 . ASN A 178 ? 0.4832 0.3193 0.4429 0.0934  0.0406  -0.0055 175 ASN A ND2 
2931 N N   . LEU A 179 ? 0.3394 0.2277 0.3285 0.0161  0.0309  -0.0106 176 LEU A N   
2932 C CA  . LEU A 179 ? 0.3245 0.2135 0.3256 -0.0037 0.0201  -0.0017 176 LEU A CA  
2933 C C   . LEU A 179 ? 0.3573 0.2201 0.3557 -0.0152 0.0127  0.0015  176 LEU A C   
2934 O O   . LEU A 179 ? 0.3690 0.2299 0.3886 -0.0278 0.0015  0.0106  176 LEU A O   
2935 C CB  . LEU A 179 ? 0.3343 0.2425 0.3255 -0.0170 0.0158  -0.0029 176 LEU A CB  
2936 C CG  . LEU A 179 ? 0.3605 0.2979 0.3601 -0.0113 0.0208  -0.0048 176 LEU A CG  
2937 C CD1 . LEU A 179 ? 0.4074 0.3619 0.3916 -0.0284 0.0194  -0.0068 176 LEU A CD1 
2938 C CD2 . LEU A 179 ? 0.3763 0.3173 0.4017 -0.0113 0.0161  0.0037  176 LEU A CD2 
2950 N N   . ASN A 180 ? 0.3851 0.2277 0.3613 -0.0111 0.0175  -0.0065 177 ASN A N   
2951 C CA  . ASN A 180 ? 0.4255 0.2416 0.3955 -0.0244 0.0098  -0.0051 177 ASN A CA  
2952 C C   . ASN A 180 ? 0.5137 0.3193 0.5107 -0.0258 0.0085  0.0035  177 ASN A C   
2953 O O   . ASN A 180 ? 0.4681 0.2623 0.4743 -0.0416 -0.0024 0.0078  177 ASN A O   
2954 C CB  . ASN A 180 ? 0.4796 0.2720 0.4199 -0.0172 0.0178  -0.0181 177 ASN A CB  
2955 C CG  . ASN A 180 ? 0.6513 0.4395 0.5917 0.0083  0.0304  -0.0224 177 ASN A CG  
2956 O OD1 . ASN A 180 ? 0.6620 0.4741 0.6046 0.0223  0.0365  -0.0271 177 ASN A OD1 
2957 N ND2 . ASN A 180 ? 0.6831 0.4413 0.6220 0.0125  0.0323  -0.0193 177 ASN A ND2 
2964 N N   . VAL A 181 ? 0.4002 0.2120 0.4106 -0.0123 0.0189  0.0060  178 VAL A N   
2965 C CA  . VAL A 181 ? 0.3839 0.1875 0.4180 -0.0167 0.0225  0.0120  178 VAL A CA  
2966 C C   . VAL A 181 ? 0.4206 0.2457 0.4948 -0.0259 0.0160  0.0178  178 VAL A C   
2967 O O   . VAL A 181 ? 0.4044 0.2281 0.5072 -0.0325 0.0192  0.0205  178 VAL A O   
2968 C CB  . VAL A 181 ? 0.4500 0.2444 0.4744 -0.0026 0.0372  0.0123  178 VAL A CB  
2969 C CG1 . VAL A 181 ? 0.4970 0.2682 0.4862 0.0109  0.0402  0.0071  178 VAL A CG1 
2970 C CG2 . VAL A 181 ? 0.4511 0.2698 0.4844 0.0060  0.0420  0.0129  178 VAL A CG2 
2980 N N   . ILE A 182 ? 0.3188 0.2970 0.3325 0.0236  0.0056  0.0098  179 ILE A N   
2981 C CA  . ILE A 182 ? 0.3171 0.3053 0.3287 0.0183  0.0017  0.0051  179 ILE A CA  
2982 C C   . ILE A 182 ? 0.3194 0.3033 0.3385 0.0155  -0.0046 -0.0074 179 ILE A C   
2983 O O   . ILE A 182 ? 0.3599 0.3401 0.3705 0.0189  -0.0093 -0.0143 179 ILE A O   
2984 C CB  . ILE A 182 ? 0.2922 0.2922 0.2888 0.0202  -0.0015 0.0062  179 ILE A CB  
2985 C CG1 . ILE A 182 ? 0.3026 0.3108 0.2925 0.0216  0.0014  0.0169  179 ILE A CG1 
2986 C CG2 . ILE A 182 ? 0.3299 0.3339 0.3241 0.0164  -0.0049 0.0007  179 ILE A CG2 
2987 C CD1 . ILE A 182 ? 0.3236 0.3449 0.3048 0.0226  -0.0022 0.0173  179 ILE A CD1 
2999 N N   . LYS A 183 ? 0.2671 0.2537 0.3018 0.0097  -0.0048 -0.0105 180 LYS A N   
3000 C CA  . LYS A 183 ? 0.3022 0.2883 0.3492 0.0065  -0.0135 -0.0226 180 LYS A CA  
3001 C C   . LYS A 183 ? 0.3080 0.3076 0.3627 0.0058  -0.0200 -0.0262 180 LYS A C   
3002 O O   . LYS A 183 ? 0.3367 0.3401 0.4014 0.0045  -0.0309 -0.0362 180 LYS A O   
3003 C CB  . LYS A 183 ? 0.3595 0.3370 0.4298 -0.0006 -0.0090 -0.0253 180 LYS A CB  
3004 C CG  . LYS A 183 ? 0.4397 0.3979 0.5038 0.0018  -0.0047 -0.0252 180 LYS A CG  
3005 C CD  . LYS A 183 ? 0.5182 0.4631 0.6021 -0.0047 0.0061  -0.0204 180 LYS A CD  
3006 C CE  . LYS A 183 ? 0.5216 0.4447 0.5972 0.0014  0.0134  -0.0149 180 LYS A CE  
3007 N NZ  . LYS A 183 ? 0.5753 0.4783 0.6717 -0.0066 0.0237  -0.0127 180 LYS A NZ  
3021 N N   . MET A 184 ? 0.3105 0.3171 0.3608 0.0072  -0.0144 -0.0193 181 MET A N   
3022 C CA  . MET A 184 ? 0.2910 0.3082 0.3515 0.0087  -0.0188 -0.0224 181 MET A CA  
3023 C C   . MET A 184 ? 0.2942 0.3092 0.3333 0.0151  -0.0280 -0.0239 181 MET A C   
3024 O O   . MET A 184 ? 0.2964 0.3038 0.3134 0.0169  -0.0276 -0.0218 181 MET A O   
3025 C CB  . MET A 184 ? 0.2863 0.3080 0.3501 0.0080  -0.0065 -0.0160 181 MET A CB  
3026 C CG  . MET A 184 ? 0.3214 0.3379 0.3591 0.0096  -0.0004 -0.0098 181 MET A CG  
3027 S SD  . MET A 184 ? 0.3442 0.3545 0.3643 0.0084  0.0035  -0.0024 181 MET A SD  
3028 C CE  . MET A 184 ? 0.3607 0.3699 0.3924 0.0042  0.0169  0.0046  181 MET A CE  
3038 N N   . PRO A 185 ? 0.2893 0.3109 0.3354 0.0194  -0.0350 -0.0262 182 PRO A N   
3039 C CA  . PRO A 185 ? 0.3086 0.3238 0.3313 0.0262  -0.0427 -0.0253 182 PRO A CA  
3040 C C   . PRO A 185 ? 0.3541 0.3602 0.3547 0.0260  -0.0332 -0.0186 182 PRO A C   
3041 O O   . PRO A 185 ? 0.3294 0.3365 0.3337 0.0234  -0.0234 -0.0156 182 PRO A O   
3042 C CB  . PRO A 185 ? 0.3039 0.3280 0.3426 0.0325  -0.0501 -0.0263 182 PRO A CB  
3043 C CG  . PRO A 185 ? 0.2999 0.3395 0.3744 0.0275  -0.0518 -0.0321 182 PRO A CG  
3044 C CD  . PRO A 185 ? 0.2906 0.3262 0.3681 0.0195  -0.0367 -0.0292 182 PRO A CD  
3052 N N   . ALA A 186 ? 0.3162 0.3139 0.2931 0.0280  -0.0356 -0.0173 183 ALA A N   
3053 C CA  . ALA A 186 ? 0.3188 0.3106 0.2790 0.0252  -0.0270 -0.0122 183 ALA A CA  
3054 C C   . ALA A 186 ? 0.3479 0.3289 0.2866 0.0290  -0.0285 -0.0089 183 ALA A C   
3055 O O   . ALA A 186 ? 0.3895 0.3663 0.3160 0.0338  -0.0357 -0.0102 183 ALA A O   
3056 C CB  . ALA A 186 ? 0.3579 0.3529 0.3161 0.0219  -0.0226 -0.0118 183 ALA A CB  
3062 N N   . ASN A 187 ? 0.3127 0.2870 0.2444 0.0259  -0.0211 -0.0049 184 ASN A N   
3063 C CA  . ASN A 187 ? 0.3668 0.3268 0.2783 0.0272  -0.0184 0.0002  184 ASN A CA  
3064 C C   . ASN A 187 ? 0.3688 0.3312 0.2763 0.0178  -0.0086 0.0018  184 ASN A C   
3065 O O   . ASN A 187 ? 0.3476 0.3139 0.2631 0.0108  -0.0041 0.0002  184 ASN A O   
3066 C CB  . ASN A 187 ? 0.3616 0.3095 0.2740 0.0312  -0.0178 0.0027  184 ASN A CB  
3067 C CG  . ASN A 187 ? 0.4430 0.3707 0.3341 0.0334  -0.0142 0.0101  184 ASN A CG  
3068 O OD1 . ASN A 187 ? 0.4442 0.3679 0.3193 0.0302  -0.0100 0.0136  184 ASN A OD1 
3069 N ND2 . ASN A 187 ? 0.4803 0.3935 0.3716 0.0395  -0.0138 0.0133  184 ASN A ND2 
3076 N N   . ILE A 188 ? 0.3344 0.2968 0.2303 0.0177  -0.0056 0.0040  185 ILE A N   
3077 C CA  . ILE A 188 ? 0.3241 0.2945 0.2224 0.0093  0.0036  0.0055  185 ILE A CA  
3078 C C   . ILE A 188 ? 0.3622 0.3175 0.2457 0.0055  0.0120  0.0113  185 ILE A C   
3079 O O   . ILE A 188 ? 0.3905 0.3339 0.2548 0.0115  0.0134  0.0156  185 ILE A O   
3080 C CB  . ILE A 188 ? 0.3928 0.3753 0.2935 0.0123  0.0050  0.0040  185 ILE A CB  
3081 C CG1 . ILE A 188 ? 0.3428 0.3333 0.2564 0.0166  -0.0024 -0.0007 185 ILE A CG1 
3082 C CG2 . ILE A 188 ? 0.4089 0.4060 0.3197 0.0051  0.0139  0.0060  185 ILE A CG2 
3083 C CD1 . ILE A 188 ? 0.3938 0.3933 0.3230 0.0122  -0.0039 -0.0010 185 ILE A CD1 
3095 N N   . LEU A 189 ? 0.3370 0.2909 0.2274 -0.0052 0.0180  0.0113  186 LEU A N   
3096 C CA  . LEU A 189 ? 0.3582 0.2929 0.2371 -0.0111 0.0277  0.0169  186 LEU A CA  
3097 C C   . LEU A 189 ? 0.4181 0.3663 0.3091 -0.0250 0.0375  0.0166  186 LEU A C   
3098 O O   . LEU A 189 ? 0.3852 0.3555 0.2952 -0.0320 0.0341  0.0107  186 LEU A O   
3099 C CB  . LEU A 189 ? 0.4018 0.3164 0.2793 -0.0129 0.0273  0.0155  186 LEU A CB  
3100 C CG  . LEU A 189 ? 0.4355 0.3396 0.3080 0.0013  0.0184  0.0162  186 LEU A CG  
3101 C CD1 . LEU A 189 ? 0.4452 0.3578 0.3331 0.0014  0.0136  0.0081  186 LEU A CD1 
3102 C CD2 . LEU A 189 ? 0.5261 0.3992 0.3818 0.0067  0.0227  0.0246  186 LEU A CD2 
3114 N N   . PHE A 190 ? 0.3875 0.3234 0.2681 -0.0292 0.0498  0.0236  187 PHE A N   
3115 C CA  . PHE A 190 ? 0.4045 0.3536 0.3022 -0.0450 0.0608  0.0233  187 PHE A CA  
3116 C C   . PHE A 190 ? 0.4439 0.3639 0.3280 -0.0527 0.0751  0.0312  187 PHE A C   
3117 O O   . PHE A 190 ? 0.4596 0.3513 0.3169 -0.0424 0.0770  0.0396  187 PHE A O   
3118 C CB  . PHE A 190 ? 0.3989 0.3753 0.3077 -0.0424 0.0659  0.0242  187 PHE A CB  
3119 C CG  . PHE A 190 ? 0.4380 0.4000 0.3220 -0.0330 0.0760  0.0321  187 PHE A CG  
3120 C CD1 . PHE A 190 ? 0.4652 0.4188 0.3279 -0.0169 0.0673  0.0317  187 PHE A CD1 
3121 C CD2 . PHE A 190 ? 0.4278 0.3849 0.3092 -0.0413 0.0948  0.0392  187 PHE A CD2 
3122 C CE1 . PHE A 190 ? 0.4886 0.4281 0.3219 -0.0082 0.0758  0.0376  187 PHE A CE1 
3123 C CE2 . PHE A 190 ? 0.5244 0.4660 0.3761 -0.0323 0.1064  0.0473  187 PHE A CE2 
3124 C CZ  . PHE A 190 ? 0.5187 0.4514 0.3439 -0.0152 0.0958  0.0459  187 PHE A CZ  
3134 N N   . GLY A 191 ? 0.4262 0.3531 0.3294 -0.0712 0.0848  0.0292  188 GLY A N   
3135 C CA  . GLY A 191 ? 0.4505 0.3476 0.3446 -0.0819 0.1011  0.0368  188 GLY A CA  
3136 C C   . GLY A 191 ? 0.5456 0.4507 0.4415 -0.0870 0.1195  0.0457  188 GLY A C   
3137 O O   . GLY A 191 ? 0.4923 0.4342 0.4151 -0.0931 0.1219  0.0413  188 GLY A O   
3141 N N   . GLY A 192 ? 0.5481 0.4181 0.4149 -0.0834 0.1337  0.0593  189 GLY A N   
3142 C CA  . GLY A 192 ? 0.5612 0.4339 0.4237 -0.0877 0.1554  0.0694  189 GLY A CA  
3143 C C   . GLY A 192 ? 0.6250 0.5058 0.5192 -0.1131 0.1730  0.0688  189 GLY A C   
3144 O O   . GLY A 192 ? 0.6810 0.5728 0.5813 -0.1189 0.1933  0.0758  189 GLY A O   
3148 N N   . LYS A 193 ? 0.6102 0.4850 0.5245 -0.1291 0.1670  0.0598  190 LYS A N   
3149 C CA  . LYS A 193 ? 0.5923 0.4801 0.5435 -0.1566 0.1793  0.0546  190 LYS A CA  
3150 C C   . LYS A 193 ? 0.6229 0.5607 0.6155 -0.1659 0.1619  0.0372  190 LYS A C   
3151 O O   . LYS A 193 ? 0.6479 0.6010 0.6744 -0.1899 0.1646  0.0285  190 LYS A O   
3152 C CB  . LYS A 193 ? 0.6298 0.4700 0.5713 -0.1701 0.1862  0.0557  190 LYS A CB  
3153 C CG  . LYS A 193 ? 0.8040 0.5952 0.7074 -0.1629 0.2071  0.0767  190 LYS A CG  
3154 C CD  . LYS A 193 ? 0.9644 0.7080 0.8656 -0.1802 0.2206  0.0797  190 LYS A CD  
3155 C CE  . LYS A 193 ? 0.9733 0.6625 0.8283 -0.1663 0.2369  0.1033  190 LYS A CE  
3156 N NZ  . LYS A 193 ? 1.2292 0.8727 1.0827 -0.1744 0.2415  0.1038  190 LYS A NZ  
3170 N N   . ASP A 194 ? 0.5341 0.4965 0.5238 -0.1476 0.1431  0.0323  191 ASP A N   
3171 C CA  . ASP A 194 ? 0.4791 0.4918 0.5042 -0.1510 0.1275  0.0204  191 ASP A CA  
3172 C C   . ASP A 194 ? 0.5402 0.5917 0.5910 -0.1491 0.1396  0.0255  191 ASP A C   
3173 O O   . ASP A 194 ? 0.5120 0.5496 0.5471 -0.1434 0.1595  0.0370  191 ASP A O   
3174 C CB  . ASP A 194 ? 0.4286 0.4444 0.4369 -0.1313 0.1057  0.0156  191 ASP A CB  
3175 C CG  . ASP A 194 ? 0.4050 0.4586 0.4402 -0.1369 0.0863  0.0030  191 ASP A CG  
3176 O OD1 . ASP A 194 ? 0.4442 0.5289 0.5142 -0.1546 0.0864  -0.0029 191 ASP A OD1 
3177 O OD2 . ASP A 194 ? 0.4066 0.4596 0.4277 -0.1232 0.0706  -0.0004 191 ASP A OD2 
3182 N N   . ALA A 195 ? 0.4543 0.5548 0.5436 -0.1526 0.1277  0.0172  192 ALA A N   
3183 C CA  . ALA A 195 ? 0.5275 0.6688 0.6461 -0.1471 0.1379  0.0212  192 ALA A CA  
3184 C C   . ALA A 195 ? 0.4462 0.5758 0.5336 -0.1205 0.1415  0.0283  192 ALA A C   
3185 O O   . ALA A 195 ? 0.4207 0.5303 0.4785 -0.1057 0.1261  0.0266  192 ALA A O   
3186 C CB  . ALA A 195 ? 0.4880 0.6831 0.6503 -0.1501 0.1191  0.0119  192 ALA A CB  
3192 N N   . PRO A 196 ? 0.4634 0.6060 0.5582 -0.1147 0.1624  0.0350  193 PRO A N   
3193 C CA  . PRO A 196 ? 0.4123 0.5403 0.4735 -0.0904 0.1661  0.0391  193 PRO A CA  
3194 C C   . PRO A 196 ? 0.3677 0.5167 0.4369 -0.0733 0.1454  0.0325  193 PRO A C   
3195 O O   . PRO A 196 ? 0.4240 0.5512 0.4598 -0.0556 0.1407  0.0327  193 PRO A O   
3196 C CB  . PRO A 196 ? 0.5256 0.6694 0.5998 -0.0900 0.1951  0.0454  193 PRO A CB  
3197 C CG  . PRO A 196 ? 0.6092 0.7840 0.7336 -0.1141 0.2052  0.0448  193 PRO A CG  
3198 C CD  . PRO A 196 ? 0.4875 0.6492 0.6145 -0.1317 0.1871  0.0393  193 PRO A CD  
3206 N N   . SER A 197 ? 0.4218 0.6111 0.5333 -0.0784 0.1321  0.0270  194 SER A N   
3207 C CA  . SER A 197 ? 0.3619 0.5661 0.4777 -0.0619 0.1127  0.0234  194 SER A CA  
3208 C C   . SER A 197 ? 0.3750 0.5445 0.4530 -0.0560 0.0953  0.0209  194 SER A C   
3209 O O   . SER A 197 ? 0.3414 0.5091 0.4103 -0.0398 0.0848  0.0197  194 SER A O   
3210 C CB  . SER A 197 ? 0.3964 0.6480 0.5597 -0.0695 0.0985  0.0196  194 SER A CB  
3211 O OG  . SER A 197 ? 0.4093 0.6554 0.5725 -0.0888 0.0860  0.0142  194 SER A OG  
3217 N N   . TYR A 198 ? 0.3187 0.4610 0.3778 -0.0689 0.0926  0.0198  195 TYR A N   
3218 C CA  . TYR A 198 ? 0.3647 0.4775 0.3929 -0.0622 0.0778  0.0174  195 TYR A CA  
3219 C C   . TYR A 198 ? 0.3229 0.4024 0.3133 -0.0479 0.0838  0.0216  195 TYR A C   
3220 O O   . TYR A 198 ? 0.3525 0.4178 0.3250 -0.0369 0.0709  0.0192  195 TYR A O   
3221 C CB  . TYR A 198 ? 0.3460 0.4412 0.3690 -0.0788 0.0730  0.0136  195 TYR A CB  
3222 C CG  . TYR A 198 ? 0.3255 0.4522 0.3773 -0.0901 0.0590  0.0060  195 TYR A CG  
3223 C CD1 . TYR A 198 ? 0.3319 0.4620 0.3768 -0.0828 0.0409  0.0016  195 TYR A CD1 
3224 C CD2 . TYR A 198 ? 0.3587 0.5134 0.4442 -0.1075 0.0638  0.0034  195 TYR A CD2 
3225 C CE1 . TYR A 198 ? 0.3475 0.5068 0.4125 -0.0917 0.0263  -0.0048 195 TYR A CE1 
3226 C CE2 . TYR A 198 ? 0.3802 0.5676 0.4911 -0.1174 0.0473  -0.0045 195 TYR A CE2 
3227 C CZ  . TYR A 198 ? 0.4193 0.6075 0.5165 -0.1088 0.0282  -0.0084 195 TYR A CZ  
3228 O OH  . TYR A 198 ? 0.4225 0.6417 0.5382 -0.1178 0.0109  -0.0156 195 TYR A OH  
3238 N N   . GLU A 199 ? 0.3786 0.4473 0.3569 -0.0479 0.1028  0.0275  196 GLU A N   
3239 C CA  . GLU A 199 ? 0.4260 0.4675 0.3660 -0.0329 0.1061  0.0305  196 GLU A CA  
3240 C C   . GLU A 199 ? 0.3630 0.4204 0.3082 -0.0173 0.1027  0.0258  196 GLU A C   
3241 O O   . GLU A 199 ? 0.3723 0.4139 0.2962 -0.0056 0.0915  0.0223  196 GLU A O   
3242 C CB  . GLU A 199 ? 0.4305 0.4542 0.3500 -0.0365 0.1285  0.0390  196 GLU A CB  
3243 C CG  . GLU A 199 ? 0.4578 0.4649 0.3409 -0.0200 0.1349  0.0405  196 GLU A CG  
3244 C CD  . GLU A 199 ? 0.6725 0.6485 0.5160 -0.0204 0.1522  0.0511  196 GLU A CD  
3245 O OE1 . GLU A 199 ? 0.5649 0.5373 0.4170 -0.0345 0.1680  0.0589  196 GLU A OE1 
3246 O OE2 . GLU A 199 ? 0.7218 0.6775 0.5248 -0.0063 0.1505  0.0515  196 GLU A OE2 
3253 N N   . THR A 200 ? 0.3718 0.4612 0.3490 -0.0172 0.1121  0.0252  197 THR A N   
3254 C CA  . THR A 200 ? 0.3507 0.4531 0.3362 -0.0014 0.1100  0.0210  197 THR A CA  
3255 C C   . THR A 200 ? 0.3746 0.4789 0.3662 0.0037  0.0881  0.0171  197 THR A C   
3256 O O   . THR A 200 ? 0.3425 0.4343 0.3203 0.0167  0.0827  0.0132  197 THR A O   
3257 C CB  . THR A 200 ? 0.3769 0.5176 0.4036 -0.0012 0.1229  0.0222  197 THR A CB  
3258 O OG1 . THR A 200 ? 0.4636 0.6018 0.4844 -0.0065 0.1470  0.0264  197 THR A OG1 
3259 C CG2 . THR A 200 ? 0.4584 0.6072 0.4926 0.0179  0.1221  0.0183  197 THR A CG2 
3267 N N   . SER A 201 ? 0.3277 0.4460 0.3385 -0.0073 0.0762  0.0175  198 SER A N   
3268 C CA  . SER A 201 ? 0.3004 0.4188 0.3128 -0.0031 0.0576  0.0152  198 SER A CA  
3269 C C   . SER A 201 ? 0.2963 0.3811 0.2761 0.0014  0.0504  0.0128  198 SER A C   
3270 O O   . SER A 201 ? 0.2962 0.3755 0.2729 0.0106  0.0415  0.0106  198 SER A O   
3271 C CB  . SER A 201 ? 0.2806 0.4160 0.3106 -0.0170 0.0468  0.0147  198 SER A CB  
3272 O OG  . SER A 201 ? 0.3116 0.4855 0.3777 -0.0197 0.0478  0.0162  198 SER A OG  
3278 N N   . ALA A 202 ? 0.3106 0.3735 0.2688 -0.0051 0.0539  0.0139  199 ALA A N   
3279 C CA  . ALA A 202 ? 0.3091 0.3452 0.2417 -0.0002 0.0450  0.0121  199 ALA A CA  
3280 C C   . ALA A 202 ? 0.3432 0.3676 0.2583 0.0128  0.0453  0.0089  199 ALA A C   
3281 O O   . ALA A 202 ? 0.3526 0.3685 0.2629 0.0186  0.0340  0.0048  199 ALA A O   
3282 C CB  . ALA A 202 ? 0.3832 0.3974 0.2965 -0.0070 0.0492  0.0158  199 ALA A CB  
3288 N N   . HIS A 203 ? 0.3681 0.3921 0.2741 0.0166  0.0591  0.0098  200 HIS A N   
3289 C CA  . HIS A 203 ? 0.3585 0.3712 0.2460 0.0286  0.0604  0.0039  200 HIS A CA  
3290 C C   . HIS A 203 ? 0.3910 0.4146 0.2997 0.0356  0.0546  -0.0013 200 HIS A C   
3291 O O   . HIS A 203 ? 0.3812 0.3904 0.2785 0.0422  0.0467  -0.0082 200 HIS A O   
3292 C CB  . HIS A 203 ? 0.3941 0.4068 0.2694 0.0314  0.0801  0.0055  200 HIS A CB  
3293 C CG  . HIS A 203 ? 0.4214 0.4125 0.2618 0.0286  0.0865  0.0110  200 HIS A CG  
3294 N ND1 . HIS A 203 ? 0.4663 0.4326 0.2681 0.0359  0.0784  0.0081  200 HIS A ND1 
3295 C CD2 . HIS A 203 ? 0.4638 0.4537 0.3016 0.0196  0.1006  0.0202  200 HIS A CD2 
3296 C CE1 . HIS A 203 ? 0.5274 0.4771 0.3012 0.0335  0.0865  0.0169  200 HIS A CE1 
3297 N NE2 . HIS A 203 ? 0.4941 0.4556 0.2891 0.0231  0.1015  0.0247  200 HIS A NE2 
3305 N N   . PHE A 204 ? 0.3381 0.3867 0.2782 0.0345  0.0585  0.0022  201 PHE A N   
3306 C CA  . PHE A 204 ? 0.3506 0.4075 0.3102 0.0430  0.0535  0.0004  201 PHE A CA  
3307 C C   . PHE A 204 ? 0.3360 0.3820 0.2931 0.0411  0.0378  -0.0007 201 PHE A C   
3308 O O   . PHE A 204 ? 0.3292 0.3629 0.2848 0.0480  0.0339  -0.0051 201 PHE A O   
3309 C CB  . PHE A 204 ? 0.3324 0.4218 0.3269 0.0425  0.0565  0.0067  201 PHE A CB  
3310 C CG  . PHE A 204 ? 0.3051 0.4013 0.3182 0.0530  0.0504  0.0083  201 PHE A CG  
3311 C CD1 . PHE A 204 ? 0.3502 0.4482 0.3684 0.0498  0.0362  0.0122  201 PHE A CD1 
3312 C CD2 . PHE A 204 ? 0.3544 0.4520 0.3774 0.0670  0.0606  0.0066  201 PHE A CD2 
3313 C CE1 . PHE A 204 ? 0.3879 0.4882 0.4195 0.0601  0.0318  0.0163  201 PHE A CE1 
3314 C CE2 . PHE A 204 ? 0.3904 0.4889 0.4294 0.0782  0.0557  0.0099  201 PHE A CE2 
3315 C CZ  . PHE A 204 ? 0.3667 0.4663 0.4092 0.0744  0.0411  0.0158  201 PHE A CZ  
3325 N N   . ILE A 205 ? 0.3134 0.3636 0.2724 0.0311  0.0305  0.0029  202 ILE A N   
3326 C CA  . ILE A 205 ? 0.2812 0.3236 0.2398 0.0292  0.0187  0.0024  202 ILE A CA  
3327 C C   . ILE A 205 ? 0.3646 0.3844 0.3044 0.0321  0.0143  -0.0041 202 ILE A C   
3328 O O   . ILE A 205 ? 0.3540 0.3661 0.2977 0.0354  0.0088  -0.0074 202 ILE A O   
3329 C CB  . ILE A 205 ? 0.2839 0.3326 0.2445 0.0184  0.0143  0.0054  202 ILE A CB  
3330 C CG1 . ILE A 205 ? 0.3108 0.3849 0.2918 0.0152  0.0142  0.0098  202 ILE A CG1 
3331 C CG2 . ILE A 205 ? 0.3498 0.3876 0.3063 0.0171  0.0056  0.0040  202 ILE A CG2 
3332 C CD1 . ILE A 205 ? 0.3324 0.4125 0.3138 0.0021  0.0115  0.0098  202 ILE A CD1 
3344 N N   . TYR A 206 ? 0.3382 0.3472 0.2575 0.0309  0.0162  -0.0055 203 TYR A N   
3345 C CA  . TYR A 206 ? 0.3565 0.3478 0.2573 0.0342  0.0085  -0.0116 203 TYR A CA  
3346 C C   . TYR A 206 ? 0.4018 0.3855 0.3001 0.0410  0.0084  -0.0202 203 TYR A C   
3347 O O   . TYR A 206 ? 0.4131 0.3887 0.3134 0.0413  -0.0012 -0.0266 203 TYR A O   
3348 C CB  . TYR A 206 ? 0.4556 0.4359 0.3299 0.0344  0.0118  -0.0094 203 TYR A CB  
3349 C CG  . TYR A 206 ? 0.3976 0.3624 0.2488 0.0397  0.0017  -0.0156 203 TYR A CG  
3350 C CD1 . TYR A 206 ? 0.4267 0.3828 0.2592 0.0457  0.0033  -0.0238 203 TYR A CD1 
3351 C CD2 . TYR A 206 ? 0.4422 0.4021 0.2914 0.0392  -0.0105 -0.0143 203 TYR A CD2 
3352 C CE1 . TYR A 206 ? 0.4721 0.4159 0.2819 0.0496  -0.0090 -0.0312 203 TYR A CE1 
3353 C CE2 . TYR A 206 ? 0.4922 0.4428 0.3234 0.0445  -0.0230 -0.0201 203 TYR A CE2 
3354 C CZ  . TYR A 206 ? 0.4858 0.4291 0.2969 0.0489  -0.0235 -0.0288 203 TYR A CZ  
3355 O OH  . TYR A 206 ? 0.5498 0.4854 0.3405 0.0534  -0.0389 -0.0364 203 TYR A OH  
3365 N N   . GLU A 207 ? 0.4042 0.3901 0.3000 0.0462  0.0202  -0.0213 204 GLU A N   
3366 C CA  . GLU A 207 ? 0.3789 0.3524 0.2675 0.0536  0.0227  -0.0315 204 GLU A CA  
3367 C C   . GLU A 207 ? 0.3868 0.3600 0.2996 0.0554  0.0198  -0.0328 204 GLU A C   
3368 O O   . GLU A 207 ? 0.4572 0.4141 0.3656 0.0588  0.0185  -0.0431 204 GLU A O   
3369 C CB  . GLU A 207 ? 0.4096 0.3858 0.2905 0.0600  0.0395  -0.0319 204 GLU A CB  
3370 C CG  . GLU A 207 ? 0.4264 0.3936 0.2734 0.0592  0.0438  -0.0321 204 GLU A CG  
3371 C CD  . GLU A 207 ? 0.4716 0.4455 0.3128 0.0631  0.0648  -0.0291 204 GLU A CD  
3372 O OE1 . GLU A 207 ? 0.4632 0.4459 0.3230 0.0699  0.0763  -0.0312 204 GLU A OE1 
3373 O OE2 . GLU A 207 ? 0.5265 0.4958 0.3438 0.0602  0.0714  -0.0238 204 GLU A OE2 
3380 N N   . HIS A 208 ? 0.3443 0.3330 0.2802 0.0530  0.0192  -0.0226 205 HIS A N   
3381 C CA  . HIS A 208 ? 0.3419 0.3286 0.2977 0.0563  0.0184  -0.0202 205 HIS A CA  
3382 C C   . HIS A 208 ? 0.3700 0.3536 0.3331 0.0490  0.0088  -0.0182 205 HIS A C   
3383 O O   . HIS A 208 ? 0.3592 0.3360 0.3354 0.0506  0.0091  -0.0158 205 HIS A O   
3384 C CB  . HIS A 208 ? 0.3352 0.3420 0.3107 0.0615  0.0245  -0.0093 205 HIS A CB  
3385 C CG  . HIS A 208 ? 0.3613 0.3714 0.3390 0.0714  0.0367  -0.0117 205 HIS A CG  
3386 N ND1 . HIS A 208 ? 0.3935 0.4138 0.3626 0.0702  0.0447  -0.0127 205 HIS A ND1 
3387 C CD2 . HIS A 208 ? 0.4602 0.4613 0.4466 0.0833  0.0447  -0.0141 205 HIS A CD2 
3388 C CE1 . HIS A 208 ? 0.4477 0.4681 0.4209 0.0810  0.0577  -0.0160 205 HIS A CE1 
3389 N NE2 . HIS A 208 ? 0.4997 0.5085 0.4839 0.0899  0.0576  -0.0172 205 HIS A NE2 
3397 N N   . LEU A 209 ? 0.3448 0.3311 0.2998 0.0420  0.0019  -0.0188 206 LEU A N   
3398 C CA  . LEU A 209 ? 0.3031 0.2873 0.2670 0.0360  -0.0051 -0.0183 206 LEU A CA  
3399 C C   . LEU A 209 ? 0.3970 0.3657 0.3643 0.0350  -0.0094 -0.0287 206 LEU A C   
3400 O O   . LEU A 209 ? 0.3996 0.3588 0.3529 0.0369  -0.0123 -0.0391 206 LEU A O   
3401 C CB  . LEU A 209 ? 0.3795 0.3686 0.3359 0.0310  -0.0108 -0.0179 206 LEU A CB  
3402 C CG  . LEU A 209 ? 0.4310 0.4317 0.3857 0.0278  -0.0080 -0.0100 206 LEU A CG  
3403 C CD1 . LEU A 209 ? 0.5231 0.5208 0.4700 0.0248  -0.0129 -0.0110 206 LEU A CD1 
3404 C CD2 . LEU A 209 ? 0.3478 0.3565 0.3157 0.0258  -0.0064 -0.0033 206 LEU A CD2 
3416 N N   . GLY A 210 ? 0.3874 0.3536 0.3722 0.0307  -0.0098 -0.0262 207 GLY A N   
3417 C CA  . GLY A 210 ? 0.4083 0.3621 0.4028 0.0260  -0.0142 -0.0366 207 GLY A CA  
3418 C C   . GLY A 210 ? 0.4100 0.3701 0.4062 0.0205  -0.0256 -0.0441 207 GLY A C   
3419 O O   . GLY A 210 ? 0.4221 0.3756 0.4261 0.0159  -0.0326 -0.0559 207 GLY A O   
3423 N N   . SER A 211 ? 0.3517 0.3247 0.3428 0.0210  -0.0281 -0.0380 208 SER A N   
3424 C CA  . SER A 211 ? 0.3669 0.3480 0.3638 0.0185  -0.0385 -0.0423 208 SER A CA  
3425 C C   . SER A 211 ? 0.4150 0.3912 0.3967 0.0206  -0.0509 -0.0540 208 SER A C   
3426 O O   . SER A 211 ? 0.4395 0.4084 0.3948 0.0260  -0.0496 -0.0551 208 SER A O   
3427 C CB  . SER A 211 ? 0.4087 0.3984 0.3975 0.0210  -0.0370 -0.0335 208 SER A CB  
3428 O OG  . SER A 211 ? 0.3949 0.3883 0.3899 0.0191  -0.0265 -0.0241 208 SER A OG  
3434 N N   . VAL A 212 ? 0.4091 0.3913 0.4075 0.0164  -0.0629 -0.0627 209 VAL A N   
3435 C CA  . VAL A 212 ? 0.4045 0.3853 0.3858 0.0189  -0.0788 -0.0740 209 VAL A CA  
3436 C C   . VAL A 212 ? 0.4279 0.4170 0.3944 0.0264  -0.0863 -0.0666 209 VAL A C   
3437 O O   . VAL A 212 ? 0.5185 0.5012 0.4539 0.0324  -0.0945 -0.0693 209 VAL A O   
3438 C CB  . VAL A 212 ? 0.5217 0.5083 0.5291 0.0105  -0.0916 -0.0880 209 VAL A CB  
3439 C CG1 . VAL A 212 ? 0.6118 0.5816 0.6274 0.0034  -0.0830 -0.0962 209 VAL A CG1 
3440 C CG2 . VAL A 212 ? 0.5931 0.5996 0.6387 0.0063  -0.0928 -0.0830 209 VAL A CG2 
3450 N N   A ASP A 213 ? 0.4019 0.4028 0.3888 0.0267  -0.0832 -0.0576 210 ASP A N   
3451 N N   B ASP A 213 ? 0.3977 0.3971 0.3816 0.0271  -0.0814 -0.0564 210 ASP A N   
3452 C CA  A ASP A 213 ? 0.4002 0.4038 0.3745 0.0347  -0.0866 -0.0488 210 ASP A CA  
3453 C CA  B ASP A 213 ? 0.3997 0.4035 0.3740 0.0349  -0.0871 -0.0487 210 ASP A CA  
3454 C C   A ASP A 213 ? 0.3934 0.3875 0.3508 0.0355  -0.0703 -0.0381 210 ASP A C   
3455 C C   B ASP A 213 ? 0.4030 0.3979 0.3598 0.0369  -0.0720 -0.0371 210 ASP A C   
3456 O O   A ASP A 213 ? 0.3546 0.3522 0.3277 0.0314  -0.0589 -0.0330 210 ASP A O   
3457 O O   B ASP A 213 ? 0.3919 0.3910 0.3636 0.0351  -0.0630 -0.0308 210 ASP A O   
3458 C CB  A ASP A 213 ? 0.4227 0.4429 0.4295 0.0357  -0.0913 -0.0467 210 ASP A CB  
3459 C CB  B ASP A 213 ? 0.4225 0.4439 0.4326 0.0347  -0.0921 -0.0482 210 ASP A CB  
3460 C CG  A ASP A 213 ? 0.4431 0.4788 0.4735 0.0338  -0.1094 -0.0579 210 ASP A CG  
3461 C CG  B ASP A 213 ? 0.5253 0.5497 0.5287 0.0454  -0.0990 -0.0407 210 ASP A CG  
3462 O OD1 A ASP A 213 ? 0.5337 0.5663 0.5429 0.0368  -0.1250 -0.0653 210 ASP A OD1 
3463 O OD1 B ASP A 213 ? 0.4672 0.4771 0.4363 0.0517  -0.0983 -0.0341 210 ASP A OD1 
3464 O OD2 A ASP A 213 ? 0.5230 0.5753 0.5933 0.0292  -0.1081 -0.0598 210 ASP A OD2 
3465 O OD2 B ASP A 213 ? 0.5763 0.6168 0.6107 0.0479  -0.1037 -0.0406 210 ASP A OD2 
3474 N N   . LYS A 214 ? 0.4283 0.4111 0.3529 0.0401  -0.0690 -0.0351 211 LYS A N   
3475 C CA  . LYS A 214 ? 0.4141 0.3907 0.3260 0.0393  -0.0545 -0.0259 211 LYS A CA  
3476 C C   . LYS A 214 ? 0.4523 0.4172 0.3316 0.0453  -0.0552 -0.0204 211 LYS A C   
3477 O O   . LYS A 214 ? 0.4680 0.4274 0.3259 0.0504  -0.0647 -0.0248 211 LYS A O   
3478 C CB  . LYS A 214 ? 0.3907 0.3665 0.3035 0.0353  -0.0437 -0.0277 211 LYS A CB  
3479 C CG  . LYS A 214 ? 0.4105 0.3785 0.3068 0.0379  -0.0464 -0.0368 211 LYS A CG  
3480 C CD  . LYS A 214 ? 0.4556 0.4227 0.3576 0.0366  -0.0340 -0.0375 211 LYS A CD  
3481 C CE  . LYS A 214 ? 0.4945 0.4503 0.3803 0.0400  -0.0340 -0.0486 211 LYS A CE  
3482 N NZ  . LYS A 214 ? 0.4611 0.4159 0.3583 0.0412  -0.0212 -0.0479 211 LYS A NZ  
3497 N N   . GLU A 215 ? 0.4204 0.3797 0.2941 0.0441  -0.0448 -0.0108 212 GLU A N   
3498 C CA  . GLU A 215 ? 0.4687 0.4132 0.3117 0.0484  -0.0412 -0.0028 212 GLU A CA  
3499 C C   . GLU A 215 ? 0.4660 0.4078 0.3067 0.0411  -0.0238 0.0030  212 GLU A C   
3500 O O   . GLU A 215 ? 0.4394 0.3909 0.3023 0.0340  -0.0180 0.0021  212 GLU A O   
3501 C CB  . GLU A 215 ? 0.5763 0.5131 0.4158 0.0557  -0.0492 0.0041  212 GLU A CB  
3502 C CG  . GLU A 215 ? 0.5848 0.5229 0.4474 0.0527  -0.0437 0.0072  212 GLU A CG  
3503 C CD  . GLU A 215 ? 0.6706 0.6011 0.5334 0.0634  -0.0523 0.0131  212 GLU A CD  
3504 O OE1 . GLU A 215 ? 0.7146 0.6253 0.5541 0.0682  -0.0483 0.0233  212 GLU A OE1 
3505 O OE2 . GLU A 215 ? 0.7495 0.6939 0.6373 0.0677  -0.0623 0.0085  212 GLU A OE2 
3512 N N   . LEU A 216 ? 0.4778 0.4079 0.2909 0.0427  -0.0158 0.0086  213 LEU A N   
3513 C CA  . LEU A 216 ? 0.4479 0.3773 0.2611 0.0347  0.0015  0.0143  213 LEU A CA  
3514 C C   . LEU A 216 ? 0.4358 0.3442 0.2276 0.0356  0.0072  0.0257  213 LEU A C   
3515 O O   . LEU A 216 ? 0.5083 0.4020 0.2693 0.0442  0.0040  0.0307  213 LEU A O   
3516 C CB  . LEU A 216 ? 0.4500 0.3845 0.2532 0.0352  0.0111  0.0112  213 LEU A CB  
3517 C CG  . LEU A 216 ? 0.5660 0.5063 0.3757 0.0270  0.0297  0.0165  213 LEU A CG  
3518 C CD1 . LEU A 216 ? 0.4889 0.4483 0.3334 0.0183  0.0306  0.0143  213 LEU A CD1 
3519 C CD2 . LEU A 216 ? 0.6297 0.5739 0.4276 0.0310  0.0407  0.0134  213 LEU A CD2 
3531 N N   . ASN A 217 ? 0.4496 0.3546 0.2557 0.0270  0.0150  0.0296  214 ASN A N   
3532 C CA  . ASN A 217 ? 0.5149 0.3950 0.3044 0.0266  0.0223  0.0406  214 ASN A CA  
3533 C C   . ASN A 217 ? 0.5141 0.3935 0.3113 0.0119  0.0406  0.0438  214 ASN A C   
3534 O O   . ASN A 217 ? 0.5103 0.3991 0.3324 0.0011  0.0425  0.0384  214 ASN A O   
3535 C CB  . ASN A 217 ? 0.5002 0.3712 0.3011 0.0302  0.0141  0.0407  214 ASN A CB  
3536 C CG  . ASN A 217 ? 0.5455 0.4173 0.3403 0.0454  -0.0035 0.0401  214 ASN A CG  
3537 O OD1 . ASN A 217 ? 0.5856 0.4428 0.3530 0.0557  -0.0079 0.0484  214 ASN A OD1 
3538 N ND2 . ASN A 217 ? 0.5443 0.4340 0.3650 0.0467  -0.0137 0.0308  214 ASN A ND2 
3545 N N   . GLY A 218 ? 0.4874 0.3568 0.2629 0.0109  0.0540  0.0520  215 GLY A N   
3546 C CA  . GLY A 218 ? 0.5344 0.3996 0.3182 -0.0041 0.0731  0.0571  215 GLY A CA  
3547 C C   . GLY A 218 ? 0.5919 0.4218 0.3585 -0.0053 0.0799  0.0687  215 GLY A C   
3548 O O   . GLY A 218 ? 0.6119 0.4173 0.3439 0.0062  0.0809  0.0804  215 GLY A O   
3552 N N   . LEU A 219 ? 0.5378 0.3622 0.3261 -0.0186 0.0843  0.0655  216 LEU A N   
3553 C CA  . LEU A 219 ? 0.5337 0.3198 0.3092 -0.0205 0.0923  0.0752  216 LEU A CA  
3554 C C   . LEU A 219 ? 0.5861 0.3623 0.3649 -0.0388 0.1151  0.0817  216 LEU A C   
3555 O O   . LEU A 219 ? 0.5823 0.3787 0.3922 -0.0572 0.1203  0.0718  216 LEU A O   
3556 C CB  . LEU A 219 ? 0.5371 0.3189 0.3326 -0.0233 0.0835  0.0652  216 LEU A CB  
3557 C CG  . LEU A 219 ? 0.6350 0.4321 0.4349 -0.0073 0.0634  0.0581  216 LEU A CG  
3558 C CD1 . LEU A 219 ? 0.6480 0.4362 0.4645 -0.0098 0.0599  0.0492  216 LEU A CD1 
3559 C CD2 . LEU A 219 ? 0.7033 0.4868 0.4761 0.0134  0.0543  0.0690  216 LEU A CD2 
3571 N N   . LYS A 220 ? 0.6377 0.3834 0.3847 -0.0340 0.1286  0.0986  217 LYS A N   
3572 C CA  . LYS A 220 ? 0.7296 0.4701 0.4783 -0.0507 0.1537  0.1065  217 LYS A CA  
3573 C C   . LYS A 220 ? 0.7080 0.4364 0.4847 -0.0737 0.1650  0.1022  217 LYS A C   
3574 O O   . LYS A 220 ? 0.7115 0.4567 0.5123 -0.0936 0.1808  0.0998  217 LYS A O   
3575 C CB  . LYS A 220 ? 0.7857 0.4908 0.4874 -0.0392 0.1665  0.1277  217 LYS A CB  
3576 C CG  . LYS A 220 ? 0.8653 0.5247 0.5405 -0.0264 0.1612  0.1404  217 LYS A CG  
3577 C CD  . LYS A 220 ? 1.0500 0.6709 0.6787 -0.0187 0.1783  0.1645  217 LYS A CD  
3578 C CE  . LYS A 220 ? 1.2306 0.8097 0.8582 -0.0192 0.1836  0.1748  217 LYS A CE  
3579 N NZ  . LYS A 220 ? 1.3439 0.9166 1.0020 -0.0467 0.2065  0.1720  217 LYS A NZ  
3593 N N   . ASP A 221 ? 0.6651 0.3659 0.4417 -0.0720 0.1577  0.0997  218 ASP A N   
3594 C CA  . ASP A 221 ? 0.7208 0.4014 0.5182 -0.0944 0.1697  0.0945  218 ASP A CA  
3595 C C   . ASP A 221 ? 0.6655 0.3765 0.4990 -0.1077 0.1566  0.0716  218 ASP A C   
3596 O O   . ASP A 221 ? 0.7300 0.4286 0.5824 -0.1291 0.1644  0.0630  218 ASP A O   
3597 C CB  . ASP A 221 ? 0.8130 0.4370 0.5860 -0.0848 0.1737  0.1058  218 ASP A CB  
3598 C CG  . ASP A 221 ? 0.9864 0.5726 0.7246 -0.0788 0.1924  0.1307  218 ASP A CG  
3599 O OD1 . ASP A 221 ? 0.9374 0.5291 0.6794 -0.0949 0.2125  0.1370  218 ASP A OD1 
3600 O OD2 . ASP A 221 ? 1.1698 0.7235 0.8765 -0.0565 0.1866  0.1446  218 ASP A OD2 
3605 N N   . SER A 222 ? 0.6311 0.3797 0.4725 -0.0966 0.1373  0.0616  219 SER A N   
3606 C CA  . SER A 222 ? 0.5992 0.3736 0.4671 -0.1060 0.1238  0.0419  219 SER A CA  
3607 C C   . SER A 222 ? 0.6046 0.4202 0.5049 -0.1262 0.1264  0.0330  219 SER A C   
3608 O O   . SER A 222 ? 0.5721 0.4118 0.4773 -0.1247 0.1326  0.0398  219 SER A O   
3609 C CB  . SER A 222 ? 0.5337 0.3283 0.3967 -0.0857 0.1040  0.0369  219 SER A CB  
3610 O OG  . SER A 222 ? 0.5941 0.3564 0.4381 -0.0697 0.0994  0.0409  219 SER A OG  
3616 N N   . HIS A 223 ? 0.5496 0.3731 0.4718 -0.1448 0.1217  0.0172  220 HIS A N   
3617 C CA  . HIS A 223 ? 0.5619 0.4307 0.5188 -0.1632 0.1179  0.0063  220 HIS A CA  
3618 C C   . HIS A 223 ? 0.4653 0.3718 0.4290 -0.1525 0.0962  -0.0037 220 HIS A C   
3619 O O   . HIS A 223 ? 0.5305 0.4282 0.4741 -0.1327 0.0868  -0.0019 220 HIS A O   
3620 C CB  . HIS A 223 ? 0.6326 0.4882 0.6070 -0.1909 0.1231  -0.0062 220 HIS A CB  
3621 C CG  . HIS A 223 ? 0.6822 0.4993 0.6532 -0.2039 0.1470  0.0046  220 HIS A CG  
3622 N ND1 . HIS A 223 ? 0.8022 0.6365 0.8039 -0.2283 0.1609  0.0044  220 HIS A ND1 
3623 C CD2 . HIS A 223 ? 0.7755 0.5372 0.7168 -0.1954 0.1601  0.0173  220 HIS A CD2 
3624 C CE1 . HIS A 223 ? 0.8672 0.6556 0.8564 -0.2356 0.1836  0.0169  220 HIS A CE1 
3625 N NE2 . HIS A 223 ? 0.8599 0.6024 0.8106 -0.2150 0.1829  0.0256  220 HIS A NE2 
3633 N N   . HIS A 224 ? 0.4547 0.4043 0.4485 -0.1657 0.0881  -0.0134 221 HIS A N   
3634 C CA  . HIS A 224 ? 0.4301 0.4153 0.4294 -0.1548 0.0688  -0.0197 221 HIS A CA  
3635 C C   . HIS A 224 ? 0.4103 0.3747 0.3877 -0.1479 0.0571  -0.0287 221 HIS A C   
3636 O O   . HIS A 224 ? 0.4389 0.4065 0.4028 -0.1286 0.0488  -0.0255 221 HIS A O   
3637 C CB  . HIS A 224 ? 0.4451 0.4774 0.4803 -0.1716 0.0604  -0.0289 221 HIS A CB  
3638 C CG  . HIS A 224 ? 0.4201 0.4875 0.4594 -0.1600 0.0406  -0.0329 221 HIS A CG  
3639 N ND1 . HIS A 224 ? 0.4111 0.4981 0.4513 -0.1397 0.0384  -0.0230 221 HIS A ND1 
3640 C CD2 . HIS A 224 ? 0.3997 0.4826 0.4390 -0.1654 0.0229  -0.0452 221 HIS A CD2 
3641 C CE1 . HIS A 224 ? 0.4166 0.5282 0.4590 -0.1328 0.0210  -0.0273 221 HIS A CE1 
3642 N NE2 . HIS A 224 ? 0.3912 0.5021 0.4317 -0.1478 0.0110  -0.0400 221 HIS A NE2 
3650 N N   . LEU A 225 ? 0.4527 0.3963 0.4279 -0.1646 0.0576  -0.0411 222 LEU A N   
3651 C CA  . LEU A 225 ? 0.4551 0.3750 0.4081 -0.1584 0.0507  -0.0510 222 LEU A CA  
3652 C C   . LEU A 225 ? 0.4627 0.3361 0.3938 -0.1441 0.0628  -0.0410 222 LEU A C   
3653 O O   . LEU A 225 ? 0.5071 0.3410 0.4307 -0.1528 0.0738  -0.0437 222 LEU A O   
3654 C CB  . LEU A 225 ? 0.4956 0.4098 0.4525 -0.1815 0.0470  -0.0702 222 LEU A CB  
3655 C CG  . LEU A 225 ? 0.5875 0.4790 0.5194 -0.1759 0.0414  -0.0833 222 LEU A CG  
3656 C CD1 . LEU A 225 ? 0.6010 0.5264 0.5271 -0.1609 0.0263  -0.0826 222 LEU A CD1 
3657 C CD2 . LEU A 225 ? 0.7055 0.5821 0.6356 -0.2004 0.0399  -0.1052 222 LEU A CD2 
3669 N N   . MET A 226 ? 0.4569 0.3354 0.3784 -0.1216 0.0597  -0.0294 223 MET A N   
3670 C CA  . MET A 226 ? 0.4922 0.3353 0.3955 -0.1057 0.0680  -0.0170 223 MET A CA  
3671 C C   . MET A 226 ? 0.5290 0.3357 0.4184 -0.1000 0.0699  -0.0232 223 MET A C   
3672 O O   . MET A 226 ? 0.5552 0.3261 0.4318 -0.0902 0.0784  -0.0136 223 MET A O   
3673 C CB  . MET A 226 ? 0.5108 0.3703 0.4081 -0.0841 0.0611  -0.0065 223 MET A CB  
3674 C CG  . MET A 226 ? 0.4905 0.3850 0.4000 -0.0853 0.0597  -0.0015 223 MET A CG  
3675 S SD  . MET A 226 ? 0.4635 0.3670 0.3614 -0.0610 0.0525  0.0079  223 MET A SD  
3676 C CE  . MET A 226 ? 0.4621 0.3273 0.3350 -0.0518 0.0629  0.0223  223 MET A CE  
3686 N N   . THR A 227 ? 0.4783 0.2921 0.3686 -0.1052 0.0632  -0.0389 224 THR A N   
3687 C CA  . THR A 227 ? 0.5046 0.2843 0.3823 -0.0991 0.0675  -0.0470 224 THR A CA  
3688 C C   . THR A 227 ? 0.5625 0.3020 0.4366 -0.1157 0.0798  -0.0547 224 THR A C   
3689 O O   . THR A 227 ? 0.6211 0.3239 0.4843 -0.1095 0.0869  -0.0608 224 THR A O   
3690 C CB  . THR A 227 ? 0.5401 0.3403 0.4152 -0.0996 0.0583  -0.0618 224 THR A CB  
3691 O OG1 . THR A 227 ? 0.5318 0.3600 0.4153 -0.1197 0.0509  -0.0713 224 THR A OG1 
3692 C CG2 . THR A 227 ? 0.5304 0.3576 0.4076 -0.0808 0.0499  -0.0535 224 THR A CG2 
3700 N N   . HIS A 228 ? 0.5830 0.3276 0.4685 -0.1371 0.0840  -0.0553 225 HIS A N   
3701 C CA  . HIS A 228 ? 0.6347 0.3431 0.5209 -0.1579 0.0957  -0.0649 225 HIS A CA  
3702 C C   . HIS A 228 ? 0.6224 0.3121 0.5138 -0.1646 0.1100  -0.0483 225 HIS A C   
3703 O O   . HIS A 228 ? 0.6314 0.3508 0.5314 -0.1621 0.1089  -0.0352 225 HIS A O   
3704 C CB  . HIS A 228 ? 0.6287 0.3625 0.5278 -0.1845 0.0873  -0.0859 225 HIS A CB  
3705 C CG  . HIS A 228 ? 0.9829 0.7171 0.8678 -0.1831 0.0781  -0.1056 225 HIS A CG  
3706 N ND1 . HIS A 228 ? 1.1781 0.9065 1.0615 -0.2067 0.0749  -0.1291 225 HIS A ND1 
3707 C CD2 . HIS A 228 ? 0.9391 0.6783 0.8093 -0.1616 0.0727  -0.1057 225 HIS A CD2 
3708 C CE1 . HIS A 228 ? 1.0594 0.7873 0.9229 -0.1984 0.0684  -0.1426 225 HIS A CE1 
3709 N NE2 . HIS A 228 ? 0.9961 0.7306 0.8530 -0.1713 0.0684  -0.1280 225 HIS A NE2 
3717 N N   . GLY A 229 ? 0.6724 0.3095 0.5564 -0.1721 0.1253  -0.0490 226 GLY A N   
3718 C CA  . GLY A 229 ? 0.7479 0.3613 0.6368 -0.1851 0.1423  -0.0355 226 GLY A CA  
3719 C C   . GLY A 229 ? 0.7523 0.3475 0.6235 -0.1611 0.1499  -0.0083 226 GLY A C   
3720 O O   . GLY A 229 ? 0.7618 0.3457 0.6162 -0.1344 0.1441  -0.0007 226 GLY A O   
3724 N N   . GLU A 230 ? 0.8771 0.4715 0.7528 -0.1716 0.1630  0.0063  227 GLU A N   
3725 C CA  . GLU A 230 ? 0.8420 0.4177 0.6956 -0.1519 0.1717  0.0328  227 GLU A CA  
3726 C C   . GLU A 230 ? 0.7556 0.3619 0.5971 -0.1233 0.1542  0.0393  227 GLU A C   
3727 O O   . GLU A 230 ? 0.7172 0.3734 0.5730 -0.1239 0.1402  0.0295  227 GLU A O   
3728 C CB  . GLU A 230 ? 0.9739 0.5632 0.8380 -0.1697 0.1870  0.0436  227 GLU A CB  
3729 C CG  . GLU A 230 ? 1.1564 0.7145 0.9919 -0.1550 0.2018  0.0711  227 GLU A CG  
3730 C CD  . GLU A 230 ? 1.2317 0.8061 1.0800 -0.1729 0.2194  0.0800  227 GLU A CD  
3731 O OE1 . GLU A 230 ? 1.2028 0.7554 1.0290 -0.1612 0.2309  0.1006  227 GLU A OE1 
3732 O OE2 . GLU A 230 ? 1.0651 0.6810 0.9477 -0.1957 0.2190  0.0657  227 GLU A OE2 
3739 N N   . GLY A 231 ? 0.7202 0.2956 0.5363 -0.0980 0.1541  0.0555  228 GLY A N   
3740 C CA  . GLY A 231 ? 0.7350 0.3380 0.5404 -0.0724 0.1375  0.0620  228 GLY A CA  
3741 C C   . GLY A 231 ? 0.6494 0.2691 0.4633 -0.0594 0.1206  0.0479  228 GLY A C   
3742 O O   . GLY A 231 ? 0.6549 0.2994 0.4644 -0.0399 0.1063  0.0519  228 GLY A O   
3746 N N   . ARG A 232 ? 0.6936 0.4093 0.3440 -0.1589 0.1042  0.0197  229 ARG A N   
3747 C CA  . ARG A 232 ? 0.6400 0.3770 0.3474 -0.1320 0.1016  0.0121  229 ARG A CA  
3748 C C   . ARG A 232 ? 0.6134 0.3138 0.3400 -0.0962 0.0816  0.0203  229 ARG A C   
3749 O O   . ARG A 232 ? 0.5898 0.3248 0.3663 -0.0717 0.0739  0.0151  229 ARG A O   
3750 C CB  . ARG A 232 ? 0.6894 0.4103 0.3928 -0.1505 0.1199  0.0030  229 ARG A CB  
3751 C CG  . ARG A 232 ? 0.7141 0.4268 0.4614 -0.1241 0.1186  -0.0048 229 ARG A CG  
3752 C CD  . ARG A 232 ? 0.8410 0.5332 0.5727 -0.1508 0.1413  -0.0169 229 ARG A CD  
3753 N NE  . ARG A 232 ? 0.7794 0.3845 0.4878 -0.1400 0.1466  -0.0166 229 ARG A NE  
3754 C CZ  . ARG A 232 ? 0.9066 0.4636 0.5891 -0.1609 0.1698  -0.0289 229 ARG A CZ  
3755 N NH1 . ARG A 232 ? 0.9412 0.5496 0.6260 -0.1883 0.1824  -0.0438 229 ARG A NH1 
3756 N NH2 . ARG A 232 ? 1.0623 0.5394 0.7226 -0.1449 0.1726  -0.0265 229 ARG A NH2 
3770 N N   . ASP A 233 ? 0.7029 0.3338 0.3912 -0.0940 0.0723  0.0349  230 ASP A N   
3771 C CA  . ASP A 233 ? 0.6900 0.2935 0.4030 -0.0580 0.0503  0.0472  230 ASP A CA  
3772 C C   . ASP A 233 ? 0.6464 0.2953 0.3777 -0.0456 0.0298  0.0527  230 ASP A C   
3773 O O   . ASP A 233 ? 0.6533 0.3243 0.4304 -0.0179 0.0157  0.0538  230 ASP A O   
3774 C CB  . ASP A 233 ? 0.8247 0.3431 0.4893 -0.0589 0.0406  0.0673  230 ASP A CB  
3775 C CG  . ASP A 233 ? 1.2423 0.7005 0.8996 -0.0586 0.0601  0.0604  230 ASP A CG  
3776 O OD1 . ASP A 233 ? 1.3999 0.7765 1.0106 -0.0625 0.0565  0.0757  230 ASP A OD1 
3777 O OD2 . ASP A 233 ? 1.3273 0.8150 1.0210 -0.0570 0.0796  0.0394  230 ASP A OD2 
3782 N N   . ILE A 234 ? 0.6529 0.3163 0.3460 -0.0692 0.0302  0.0545  231 ILE A N   
3783 C CA  . ILE A 234 ? 0.6356 0.3358 0.3362 -0.0637 0.0162  0.0555  231 ILE A CA  
3784 C C   . ILE A 234 ? 0.5620 0.3231 0.3164 -0.0503 0.0239  0.0376  231 ILE A C   
3785 O O   . ILE A 234 ? 0.5442 0.3257 0.3246 -0.0334 0.0090  0.0382  231 ILE A O   
3786 C CB  . ILE A 234 ? 0.6740 0.3740 0.3183 -0.0957 0.0226  0.0560  231 ILE A CB  
3787 C CG1 . ILE A 234 ? 0.9130 0.5464 0.4960 -0.1143 0.0130  0.0760  231 ILE A CG1 
3788 C CG2 . ILE A 234 ? 0.6903 0.4224 0.3375 -0.0930 0.0135  0.0522  231 ILE A CG2 
3789 C CD1 . ILE A 234 ? 1.0767 0.6707 0.6562 -0.0950 -0.0191 0.1006  231 ILE A CD1 
3801 N N   . LEU A 235 ? 0.5495 0.3406 0.3174 -0.0614 0.0456  0.0235  232 LEU A N   
3802 C CA  . LEU A 235 ? 0.4812 0.3235 0.2979 -0.0497 0.0507  0.0107  232 LEU A CA  
3803 C C   . LEU A 235 ? 0.4626 0.3034 0.3199 -0.0274 0.0402  0.0101  232 LEU A C   
3804 O O   . LEU A 235 ? 0.4401 0.3075 0.3253 -0.0140 0.0304  0.0065  232 LEU A O   
3805 C CB  . LEU A 235 ? 0.4942 0.3672 0.3175 -0.0678 0.0716  0.0020  232 LEU A CB  
3806 C CG  . LEU A 235 ? 0.4631 0.3878 0.3322 -0.0615 0.0765  -0.0067 232 LEU A CG  
3807 C CD1 . LEU A 235 ? 0.4343 0.3540 0.3300 -0.0557 0.0748  -0.0099 232 LEU A CD1 
3808 C CD2 . LEU A 235 ? 0.4246 0.3716 0.3112 -0.0446 0.0686  -0.0099 232 LEU A CD2 
3820 N N   . GLU A 236 ? 0.4452 0.2536 0.3047 -0.0247 0.0444  0.0117  233 GLU A N   
3821 C CA  . GLU A 236 ? 0.4513 0.2647 0.3545 -0.0038 0.0400  0.0072  233 GLU A CA  
3822 C C   . GLU A 236 ? 0.5032 0.3171 0.4225 0.0191  0.0153  0.0184  233 GLU A C   
3823 O O   . GLU A 236 ? 0.4770 0.3260 0.4359 0.0314  0.0084  0.0124  233 GLU A O   
3824 C CB  . GLU A 236 ? 0.5037 0.2743 0.4029 -0.0048 0.0545  0.0038  233 GLU A CB  
3825 C CG  . GLU A 236 ? 0.5005 0.2843 0.3898 -0.0333 0.0786  -0.0098 233 GLU A CG  
3826 C CD  . GLU A 236 ? 0.6046 0.3426 0.4834 -0.0409 0.0980  -0.0183 233 GLU A CD  
3827 O OE1 . GLU A 236 ? 0.6032 0.2870 0.4778 -0.0216 0.0951  -0.0124 233 GLU A OE1 
3828 O OE2 . GLU A 236 ? 0.5611 0.3152 0.4338 -0.0677 0.1167  -0.0304 233 GLU A OE2 
3835 N N   . GLU A 237 ? 0.4866 0.2647 0.3733 0.0209  0.0000  0.0365  234 GLU A N   
3836 C CA  . GLU A 237 ? 0.4920 0.2780 0.3920 0.0380  -0.0276 0.0514  234 GLU A CA  
3837 C C   . GLU A 237 ? 0.4743 0.3059 0.3794 0.0307  -0.0339 0.0438  234 GLU A C   
3838 O O   . GLU A 237 ? 0.4999 0.3610 0.4360 0.0424  -0.0495 0.0455  234 GLU A O   
3839 C CB  . GLU A 237 ? 0.5773 0.3169 0.4297 0.0327  -0.0454 0.0755  234 GLU A CB  
3840 C CG  . GLU A 237 ? 0.7213 0.4770 0.5747 0.0391  -0.0769 0.0940  234 GLU A CG  
3841 C CD  . GLU A 237 ? 1.1663 0.8736 0.9673 0.0295  -0.0979 0.1221  234 GLU A CD  
3842 O OE1 . GLU A 237 ? 1.2320 0.9507 1.0047 0.0150  -0.1191 0.1348  234 GLU A OE1 
3843 O OE2 . GLU A 237 ? 1.1504 0.8038 0.9333 0.0330  -0.0934 0.1318  234 GLU A OE2 
3850 N N   . ASN A 238 ? 0.4733 0.3109 0.3485 0.0107  -0.0203 0.0345  235 ASN A N   
3851 C CA  . ASN A 238 ? 0.4780 0.3452 0.3517 0.0047  -0.0225 0.0258  235 ASN A CA  
3852 C C   . ASN A 238 ? 0.4116 0.3136 0.3304 0.0136  -0.0181 0.0125  235 ASN A C   
3853 O O   . ASN A 238 ? 0.4059 0.3266 0.3358 0.0160  -0.0310 0.0112  235 ASN A O   
3854 C CB  . ASN A 238 ? 0.4763 0.3420 0.3158 -0.0134 -0.0043 0.0172  235 ASN A CB  
3855 C CG  . ASN A 238 ? 0.5410 0.4230 0.3716 -0.0183 -0.0029 0.0068  235 ASN A CG  
3856 O OD1 . ASN A 238 ? 0.5467 0.4504 0.4071 -0.0103 0.0002  -0.0031 235 ASN A OD1 
3857 N ND2 . ASN A 238 ? 0.5685 0.4340 0.3532 -0.0340 -0.0056 0.0092  235 ASN A ND2 
3864 N N   . VAL A 239 ? 0.3792 0.2894 0.3188 0.0132  -0.0008 0.0033  236 VAL A N   
3865 C CA  . VAL A 239 ? 0.3267 0.2678 0.3022 0.0153  0.0036  -0.0080 236 VAL A CA  
3866 C C   . VAL A 239 ? 0.3618 0.3148 0.3713 0.0278  -0.0078 -0.0076 236 VAL A C   
3867 O O   . VAL A 239 ? 0.3399 0.3200 0.3694 0.0272  -0.0144 -0.0135 236 VAL A O   
3868 C CB  . VAL A 239 ? 0.3619 0.3097 0.3447 0.0053  0.0232  -0.0149 236 VAL A CB  
3869 C CG1 . VAL A 239 ? 0.3798 0.3562 0.3969 0.0030  0.0257  -0.0244 236 VAL A CG1 
3870 C CG2 . VAL A 239 ? 0.3928 0.3477 0.3557 -0.0047 0.0332  -0.0154 236 VAL A CG2 
3880 N N   . ILE A 240 ? 0.3804 0.3136 0.3978 0.0395  -0.0098 -0.0005 237 ILE A N   
3881 C CA  . ILE A 240 ? 0.3214 0.2730 0.3818 0.0566  -0.0181 -0.0007 237 ILE A CA  
3882 C C   . ILE A 240 ? 0.3758 0.3503 0.4407 0.0615  -0.0440 0.0103  237 ILE A C   
3883 O O   . ILE A 240 ? 0.3387 0.3530 0.4378 0.0641  -0.0508 0.0046  237 ILE A O   
3884 C CB  . ILE A 240 ? 0.3929 0.3088 0.4609 0.0728  -0.0124 0.0054  237 ILE A CB  
3885 C CG1 . ILE A 240 ? 0.4202 0.3205 0.4878 0.0620  0.0164  -0.0112 237 ILE A CG1 
3886 C CG2 . ILE A 240 ? 0.4381 0.3751 0.5549 0.0987  -0.0261 0.0112  237 ILE A CG2 
3887 C CD1 . ILE A 240 ? 0.5568 0.4037 0.6157 0.0730  0.0263  -0.0067 237 ILE A CD1 
3899 N N   . ARG A 241 ? 0.3633 0.3156 0.3898 0.0574  -0.0587 0.0261  238 ARG A N   
3900 C CA  . ARG A 241 ? 0.3912 0.3647 0.4102 0.0528  -0.0838 0.0371  238 ARG A CA  
3901 C C   . ARG A 241 ? 0.3508 0.3506 0.3660 0.0361  -0.0805 0.0217  238 ARG A C   
3902 O O   . ARG A 241 ? 0.3777 0.4115 0.4091 0.0323  -0.0962 0.0230  238 ARG A O   
3903 C CB  . ARG A 241 ? 0.4943 0.4342 0.4578 0.0404  -0.0946 0.0525  238 ARG A CB  
3904 C CG  . ARG A 241 ? 0.6229 0.5799 0.5619 0.0245  -0.1181 0.0619  238 ARG A CG  
3905 C CD  . ARG A 241 ? 0.8817 0.8032 0.7640 0.0098  -0.1298 0.0797  238 ARG A CD  
3906 N NE  . ARG A 241 ? 1.1794 1.0730 1.0148 -0.0091 -0.1058 0.0643  238 ARG A NE  
3907 C CZ  . ARG A 241 ? 1.0301 0.8897 0.8376 -0.0132 -0.0937 0.0673  238 ARG A CZ  
3908 N NH1 . ARG A 241 ? 1.0695 0.9053 0.8836 -0.0004 -0.1028 0.0854  238 ARG A NH1 
3909 N NH2 . ARG A 241 ? 0.9802 0.8287 0.7525 -0.0307 -0.0707 0.0514  238 ARG A NH2 
3923 N N   . PHE A 242 ? 0.3693 0.3534 0.3627 0.0254  -0.0608 0.0084  239 PHE A N   
3924 C CA  . PHE A 242 ? 0.3806 0.3758 0.3664 0.0122  -0.0567 -0.0044 239 PHE A CA  
3925 C C   . PHE A 242 ? 0.3457 0.3750 0.3727 0.0128  -0.0565 -0.0133 239 PHE A C   
3926 O O   . PHE A 242 ? 0.3456 0.3922 0.3700 0.0007  -0.0659 -0.0174 239 PHE A O   
3927 C CB  . PHE A 242 ? 0.3612 0.3358 0.3268 0.0078  -0.0358 -0.0132 239 PHE A CB  
3928 C CG  . PHE A 242 ? 0.3394 0.3152 0.2990 -0.0005 -0.0304 -0.0243 239 PHE A CG  
3929 C CD1 . PHE A 242 ? 0.4054 0.3642 0.3300 -0.0110 -0.0344 -0.0279 239 PHE A CD1 
3930 C CD2 . PHE A 242 ? 0.3682 0.3558 0.3523 0.0000  -0.0206 -0.0303 239 PHE A CD2 
3931 C CE1 . PHE A 242 ? 0.4442 0.3912 0.3593 -0.0170 -0.0280 -0.0380 239 PHE A CE1 
3932 C CE2 . PHE A 242 ? 0.3854 0.3662 0.3619 -0.0061 -0.0184 -0.0364 239 PHE A CE2 
3933 C CZ  . PHE A 242 ? 0.3658 0.3230 0.3089 -0.0124 -0.0213 -0.0404 239 PHE A CZ  
3943 N N   . PHE A 243 ? 0.3156 0.3530 0.3750 0.0217  -0.0442 -0.0181 240 PHE A N   
3944 C CA  . PHE A 243 ? 0.2676 0.3391 0.3619 0.0168  -0.0409 -0.0293 240 PHE A CA  
3945 C C   . PHE A 243 ? 0.3340 0.4422 0.4650 0.0265  -0.0549 -0.0257 240 PHE A C   
3946 O O   . PHE A 243 ? 0.2806 0.4263 0.4328 0.0156  -0.0577 -0.0345 240 PHE A O   
3947 C CB  . PHE A 243 ? 0.2889 0.3580 0.4002 0.0159  -0.0196 -0.0391 240 PHE A CB  
3948 C CG  . PHE A 243 ? 0.2805 0.3356 0.3679 0.0020  -0.0099 -0.0418 240 PHE A CG  
3949 C CD1 . PHE A 243 ? 0.3274 0.3902 0.4057 -0.0124 -0.0151 -0.0453 240 PHE A CD1 
3950 C CD2 . PHE A 243 ? 0.2849 0.3196 0.3586 0.0026  0.0027  -0.0389 240 PHE A CD2 
3951 C CE1 . PHE A 243 ? 0.3128 0.3623 0.3749 -0.0194 -0.0089 -0.0435 240 PHE A CE1 
3952 C CE2 . PHE A 243 ? 0.3605 0.3934 0.4208 -0.0077 0.0093  -0.0382 240 PHE A CE2 
3953 C CZ  . PHE A 243 ? 0.3148 0.3554 0.3729 -0.0158 0.0028  -0.0395 240 PHE A CZ  
3963 N N   . ASN A 244 ? 0.2942 0.3951 0.4325 0.0451  -0.0658 -0.0109 241 ASN A N   
3964 C CA  . ASN A 244 ? 0.2681 0.4127 0.4506 0.0586  -0.0822 -0.0035 241 ASN A CA  
3965 C C   . ASN A 244 ? 0.3151 0.4930 0.4848 0.0400  -0.1049 0.0022  241 ASN A C   
3966 O O   . ASN A 244 ? 0.3584 0.5891 0.5693 0.0458  -0.1199 0.0078  241 ASN A O   
3967 C CB  . ASN A 244 ? 0.3351 0.4603 0.5289 0.0852  -0.0933 0.0168  241 ASN A CB  
3968 C CG  . ASN A 244 ? 0.4109 0.5230 0.6431 0.1082  -0.0718 0.0081  241 ASN A CG  
3969 O OD1 . ASN A 244 ? 0.4027 0.5384 0.6651 0.1047  -0.0516 -0.0132 241 ASN A OD1 
3970 N ND2 . ASN A 244 ? 0.4301 0.5006 0.6572 0.1290  -0.0757 0.0243  241 ASN A ND2 
3977 N N   . ALA A 245 ? 0.3130 0.4631 0.4279 0.0171  -0.1063 0.0001  242 ALA A N   
3978 C CA  . ALA A 245 ? 0.4033 0.5766 0.4964 -0.0078 -0.1235 0.0012  242 ALA A CA  
3979 C C   . ALA A 245 ? 0.4374 0.6515 0.5559 -0.0232 -0.1185 -0.0146 242 ALA A C   
3980 O O   . ALA A 245 ? 0.4471 0.6948 0.5590 -0.0450 -0.1341 -0.0135 242 ALA A O   
3981 C CB  . ALA A 245 ? 0.5415 0.6641 0.5674 -0.0277 -0.1192 -0.0023 242 ALA A CB  
3987 N N   . LEU A 246 ? 0.3554 0.5682 0.4978 -0.0177 -0.0974 -0.0289 243 LEU A N   
3988 C CA  . LEU A 246 ? 0.4080 0.6606 0.5732 -0.0360 -0.0912 -0.0442 243 LEU A CA  
3989 C C   . LEU A 246 ? 0.4802 0.8045 0.7071 -0.0266 -0.0986 -0.0442 243 LEU A C   
3990 O O   . LEU A 246 ? 0.4741 0.8452 0.7166 -0.0488 -0.0986 -0.0555 243 LEU A O   
3991 C CB  . LEU A 246 ? 0.3477 0.5810 0.5194 -0.0359 -0.0671 -0.0577 243 LEU A CB  
3992 C CG  . LEU A 246 ? 0.3572 0.5351 0.4793 -0.0470 -0.0600 -0.0579 243 LEU A CG  
3993 C CD1 . LEU A 246 ? 0.3900 0.5575 0.5227 -0.0466 -0.0401 -0.0656 243 LEU A CD1 
3994 C CD2 . LEU A 246 ? 0.4978 0.6705 0.5850 -0.0770 -0.0685 -0.0619 243 LEU A CD2 
4006 N N   . THR A 247 ? 0.4548 0.7893 0.7183 0.0058  -0.1046 -0.0312 244 THR A N   
4007 C CA  . THR A 247 ? 0.5481 0.9513 0.8845 0.0252  -0.1077 -0.0312 244 THR A CA  
4008 C C   . THR A 247 ? 0.6601 1.1076 1.0066 0.0261  -0.1411 -0.0080 244 THR A C   
4009 O O   . THR A 247 ? 0.5864 1.1104 0.9954 0.0354  -0.1496 -0.0060 244 THR A O   
4010 C CB  . THR A 247 ? 0.5391 0.9210 0.9156 0.0644  -0.0910 -0.0313 244 THR A CB  
4011 O OG1 . THR A 247 ? 0.5623 0.8999 0.9160 0.0845  -0.1076 -0.0065 244 THR A OG1 
4012 C CG2 . THR A 247 ? 0.5492 0.8843 0.9032 0.0550  -0.0594 -0.0523 244 THR A CG2 
4013 O OXT . THR A 247 ? 0.5990 1.0114 0.8922 0.0152  -0.1597 0.0088  244 THR A OXT 
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