data_9M7M
# 
_entry.id   9M7M 
# 
_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   9M7M         pdb_00009m7m 10.2210/pdb9m7m/pdb 
WWPDB D_1300057349 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9M7M 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              srheesnu@snu.ac.kr 
_pdbx_contact_author.name_first         Sangkee 
_pdbx_contact_author.name_last          Rhee 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8779-9737 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seo, S.'  1 0009-0006-4578-2968 
'Rhee, S.' 2 0000-0002-8779-9737 
# 
_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            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                110257 
_citation.page_last                 110257 
_citation.title                     
'Structural and functional insights in the substrate specificity of the pseudouridine monophosphate phosphatase HDHD1A.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.110257 
_citation.pdbx_database_id_PubMed   40409548 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Seo, S.'  1 ? 
primary 'Kim, M.'  2 ? 
primary 'Rhee, S.' 3 ? 
# 
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 "Pseudouridine-5'-phosphatase"                                                                            
25074.951 1   3.1.3.96 ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'                                                                                           24.305 
1   ?        ? ? ? 
3 non-polymer syn '5-[(2~{S},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]-1~{H}-pyrimidine-2,4-dione' 
244.201   1   ?        ? ? ? 
4 water       nat water                                                                                                     18.015 
300 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Haloacid dehalogenase-like hydrolase domain-containing protein 1,Haloacid dehalogenase-like hydrolase domain-containing protein 1A,Protein GS1,Pseudouridine-5'-monophosphatase,5'-PsiMPase
;
# 
_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       
;APPQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKL
KEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRF
SPPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;APPQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKL
KEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRF
SPPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE
;
_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 'MAGNESIUM ION'                                                                                           MG  
3 '5-[(2~{S},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]-1~{H}-pyrimidine-2,4-dione' FJF 
4 water                                                                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   PRO n 
1 4   GLN n 
1 5   PRO n 
1 6   VAL n 
1 7   THR n 
1 8   HIS n 
1 9   LEU n 
1 10  ILE n 
1 11  PHE n 
1 12  ASP n 
1 13  MET n 
1 14  ASP n 
1 15  GLY n 
1 16  LEU n 
1 17  LEU n 
1 18  LEU n 
1 19  ASP n 
1 20  THR n 
1 21  GLU n 
1 22  ARG n 
1 23  LEU n 
1 24  TYR n 
1 25  SER n 
1 26  VAL n 
1 27  VAL n 
1 28  PHE n 
1 29  GLN n 
1 30  GLU n 
1 31  ILE n 
1 32  CYS n 
1 33  ASN n 
1 34  ARG n 
1 35  TYR n 
1 36  ASP n 
1 37  LYS n 
1 38  LYS n 
1 39  TYR n 
1 40  SER n 
1 41  TRP n 
1 42  ASP n 
1 43  VAL n 
1 44  LYS n 
1 45  SER n 
1 46  LEU n 
1 47  VAL n 
1 48  MET n 
1 49  GLY n 
1 50  LYS n 
1 51  LYS n 
1 52  ALA n 
1 53  LEU n 
1 54  GLU n 
1 55  ALA n 
1 56  ALA n 
1 57  GLN n 
1 58  ILE n 
1 59  ILE n 
1 60  ILE n 
1 61  ASP n 
1 62  VAL n 
1 63  LEU n 
1 64  GLN n 
1 65  LEU n 
1 66  PRO n 
1 67  MET n 
1 68  SER n 
1 69  LYS n 
1 70  GLU n 
1 71  GLU n 
1 72  LEU n 
1 73  VAL n 
1 74  GLU n 
1 75  GLU n 
1 76  SER n 
1 77  GLN n 
1 78  THR n 
1 79  LYS n 
1 80  LEU n 
1 81  LYS n 
1 82  GLU n 
1 83  VAL n 
1 84  PHE n 
1 85  PRO n 
1 86  THR n 
1 87  ALA n 
1 88  ALA n 
1 89  LEU n 
1 90  MET n 
1 91  PRO n 
1 92  GLY n 
1 93  ALA n 
1 94  GLU n 
1 95  LYS n 
1 96  LEU n 
1 97  ILE n 
1 98  ILE n 
1 99  HIS n 
1 100 LEU n 
1 101 ARG n 
1 102 LYS n 
1 103 HIS n 
1 104 GLY n 
1 105 ILE n 
1 106 PRO n 
1 107 PHE n 
1 108 ALA n 
1 109 LEU n 
1 110 ALA n 
1 111 THR n 
1 112 SER n 
1 113 SER n 
1 114 GLY n 
1 115 SER n 
1 116 ALA n 
1 117 SER n 
1 118 PHE n 
1 119 ASP n 
1 120 MET n 
1 121 LYS n 
1 122 THR n 
1 123 SER n 
1 124 ARG n 
1 125 HIS n 
1 126 LYS n 
1 127 GLU n 
1 128 PHE n 
1 129 PHE n 
1 130 SER n 
1 131 LEU n 
1 132 PHE n 
1 133 SER n 
1 134 HIS n 
1 135 ILE n 
1 136 VAL n 
1 137 LEU n 
1 138 GLY n 
1 139 ASP n 
1 140 ASP n 
1 141 PRO n 
1 142 GLU n 
1 143 VAL n 
1 144 GLN n 
1 145 HIS n 
1 146 GLY n 
1 147 LYS n 
1 148 PRO n 
1 149 ASP n 
1 150 PRO n 
1 151 ASP n 
1 152 ILE n 
1 153 PHE n 
1 154 LEU n 
1 155 ALA n 
1 156 CYS n 
1 157 ALA n 
1 158 LYS n 
1 159 ARG n 
1 160 PHE n 
1 161 SER n 
1 162 PRO n 
1 163 PRO n 
1 164 PRO n 
1 165 ALA n 
1 166 MET n 
1 167 GLU n 
1 168 LYS n 
1 169 CYS n 
1 170 LEU n 
1 171 VAL n 
1 172 PHE n 
1 173 GLU n 
1 174 ASP n 
1 175 ALA n 
1 176 PRO n 
1 177 ASN n 
1 178 GLY n 
1 179 VAL n 
1 180 GLU n 
1 181 ALA n 
1 182 ALA n 
1 183 LEU n 
1 184 ALA n 
1 185 ALA n 
1 186 GLY n 
1 187 MET n 
1 188 GLN n 
1 189 VAL n 
1 190 VAL n 
1 191 MET n 
1 192 VAL n 
1 193 PRO n 
1 194 ASP n 
1 195 GLY n 
1 196 ASN n 
1 197 LEU n 
1 198 SER n 
1 199 ARG n 
1 200 ASP n 
1 201 LEU n 
1 202 THR n 
1 203 THR n 
1 204 LYS n 
1 205 ALA n 
1 206 THR n 
1 207 LEU n 
1 208 VAL n 
1 209 LEU n 
1 210 ASN n 
1 211 SER n 
1 212 LEU n 
1 213 GLN n 
1 214 ASP n 
1 215 PHE n 
1 216 GLN n 
1 217 PRO n 
1 218 GLU n 
1 219 LEU n 
1 220 PHE n 
1 221 GLY n 
1 222 LEU n 
1 223 PRO n 
1 224 SER n 
1 225 TYR n 
1 226 GLU 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                   226 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PUDP, DXF68S1E, FAM16AX, GS1, HDHD1, HDHD1A' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
FJF non-polymer         . 
'5-[(2~{S},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]-1~{H}-pyrimidine-2,4-dione' ? 'C9 H12 N2 O6'   
244.201 
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 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   3   3   ALA ALA A . n 
A 1 2   PRO 2   4   4   PRO PRO A . n 
A 1 3   PRO 3   5   5   PRO PRO A . n 
A 1 4   GLN 4   6   6   GLN GLN A . n 
A 1 5   PRO 5   7   7   PRO PRO A . n 
A 1 6   VAL 6   8   8   VAL VAL A . n 
A 1 7   THR 7   9   9   THR THR A . n 
A 1 8   HIS 8   10  10  HIS HIS A . n 
A 1 9   LEU 9   11  11  LEU LEU A . n 
A 1 10  ILE 10  12  12  ILE ILE A . n 
A 1 11  PHE 11  13  13  PHE PHE A . n 
A 1 12  ASP 12  14  14  ASP ASP A . n 
A 1 13  MET 13  15  15  MET MET A . n 
A 1 14  ASP 14  16  16  ASP ASP A . n 
A 1 15  GLY 15  17  17  GLY GLY A . n 
A 1 16  LEU 16  18  18  LEU LEU A . n 
A 1 17  LEU 17  19  19  LEU LEU A . n 
A 1 18  LEU 18  20  20  LEU LEU A . n 
A 1 19  ASP 19  21  21  ASP ASP A . n 
A 1 20  THR 20  22  22  THR THR A . n 
A 1 21  GLU 21  23  23  GLU GLU A . n 
A 1 22  ARG 22  24  24  ARG ARG A . n 
A 1 23  LEU 23  25  25  LEU LEU A . n 
A 1 24  TYR 24  26  26  TYR TYR A . n 
A 1 25  SER 25  27  27  SER SER A . n 
A 1 26  VAL 26  28  28  VAL VAL A . n 
A 1 27  VAL 27  29  29  VAL VAL A . n 
A 1 28  PHE 28  30  30  PHE PHE A . n 
A 1 29  GLN 29  31  31  GLN GLN A . n 
A 1 30  GLU 30  32  32  GLU GLU A . n 
A 1 31  ILE 31  33  33  ILE ILE A . n 
A 1 32  CYS 32  34  34  CYS CYS A . n 
A 1 33  ASN 33  35  35  ASN ASN A . n 
A 1 34  ARG 34  36  36  ARG ARG A . n 
A 1 35  TYR 35  37  37  TYR TYR A . n 
A 1 36  ASP 36  38  38  ASP ASP A . n 
A 1 37  LYS 37  39  39  LYS LYS A . n 
A 1 38  LYS 38  40  40  LYS LYS A . n 
A 1 39  TYR 39  41  41  TYR TYR A . n 
A 1 40  SER 40  42  42  SER SER A . n 
A 1 41  TRP 41  43  43  TRP TRP A . n 
A 1 42  ASP 42  44  44  ASP ASP A . n 
A 1 43  VAL 43  45  45  VAL VAL A . n 
A 1 44  LYS 44  46  46  LYS LYS A . n 
A 1 45  SER 45  47  47  SER SER A . n 
A 1 46  LEU 46  48  48  LEU LEU A . n 
A 1 47  VAL 47  49  49  VAL VAL A . n 
A 1 48  MET 48  50  50  MET MET A . n 
A 1 49  GLY 49  51  51  GLY GLY A . n 
A 1 50  LYS 50  52  52  LYS LYS A . n 
A 1 51  LYS 51  53  53  LYS LYS A . n 
A 1 52  ALA 52  54  54  ALA ALA A . n 
A 1 53  LEU 53  55  55  LEU LEU A . n 
A 1 54  GLU 54  56  56  GLU GLU A . n 
A 1 55  ALA 55  57  57  ALA ALA A . n 
A 1 56  ALA 56  58  58  ALA ALA A . n 
A 1 57  GLN 57  59  59  GLN GLN A . n 
A 1 58  ILE 58  60  60  ILE ILE A . n 
A 1 59  ILE 59  61  61  ILE ILE A . n 
A 1 60  ILE 60  62  62  ILE ILE A . n 
A 1 61  ASP 61  63  63  ASP ASP A . n 
A 1 62  VAL 62  64  64  VAL VAL A . n 
A 1 63  LEU 63  65  65  LEU LEU A . n 
A 1 64  GLN 64  66  66  GLN GLN A . n 
A 1 65  LEU 65  67  67  LEU LEU A . n 
A 1 66  PRO 66  68  68  PRO PRO A . n 
A 1 67  MET 67  69  69  MET MET A . n 
A 1 68  SER 68  70  70  SER SER A . n 
A 1 69  LYS 69  71  71  LYS LYS A . n 
A 1 70  GLU 70  72  72  GLU GLU A . n 
A 1 71  GLU 71  73  73  GLU GLU A . n 
A 1 72  LEU 72  74  74  LEU LEU A . n 
A 1 73  VAL 73  75  75  VAL VAL A . n 
A 1 74  GLU 74  76  76  GLU GLU A . n 
A 1 75  GLU 75  77  77  GLU GLU A . n 
A 1 76  SER 76  78  78  SER SER A . n 
A 1 77  GLN 77  79  79  GLN GLN A . n 
A 1 78  THR 78  80  80  THR THR A . n 
A 1 79  LYS 79  81  81  LYS LYS A . n 
A 1 80  LEU 80  82  82  LEU LEU A . n 
A 1 81  LYS 81  83  83  LYS LYS A . n 
A 1 82  GLU 82  84  84  GLU GLU A . n 
A 1 83  VAL 83  85  85  VAL VAL A . n 
A 1 84  PHE 84  86  86  PHE PHE A . n 
A 1 85  PRO 85  87  87  PRO PRO A . n 
A 1 86  THR 86  88  88  THR THR A . n 
A 1 87  ALA 87  89  89  ALA ALA A . n 
A 1 88  ALA 88  90  90  ALA ALA A . n 
A 1 89  LEU 89  91  91  LEU LEU A . n 
A 1 90  MET 90  92  92  MET MET A . n 
A 1 91  PRO 91  93  93  PRO PRO A . n 
A 1 92  GLY 92  94  94  GLY GLY A . n 
A 1 93  ALA 93  95  95  ALA ALA A . n 
A 1 94  GLU 94  96  96  GLU GLU A . n 
A 1 95  LYS 95  97  97  LYS LYS A . n 
A 1 96  LEU 96  98  98  LEU LEU A . n 
A 1 97  ILE 97  99  99  ILE ILE A . n 
A 1 98  ILE 98  100 100 ILE ILE A . n 
A 1 99  HIS 99  101 101 HIS HIS A . n 
A 1 100 LEU 100 102 102 LEU LEU A . n 
A 1 101 ARG 101 103 103 ARG ARG A . n 
A 1 102 LYS 102 104 104 LYS LYS A . n 
A 1 103 HIS 103 105 105 HIS HIS A . n 
A 1 104 GLY 104 106 106 GLY GLY A . n 
A 1 105 ILE 105 107 107 ILE ILE A . n 
A 1 106 PRO 106 108 108 PRO PRO A . n 
A 1 107 PHE 107 109 109 PHE PHE A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 LEU 109 111 111 LEU LEU A . n 
A 1 110 ALA 110 112 112 ALA ALA A . n 
A 1 111 THR 111 113 113 THR THR A . n 
A 1 112 SER 112 114 114 SER SER A . n 
A 1 113 SER 113 115 115 SER SER A . n 
A 1 114 GLY 114 116 116 GLY GLY A . n 
A 1 115 SER 115 117 117 SER SER A . n 
A 1 116 ALA 116 118 118 ALA ALA A . n 
A 1 117 SER 117 119 119 SER SER A . n 
A 1 118 PHE 118 120 120 PHE PHE A . n 
A 1 119 ASP 119 121 121 ASP ASP A . n 
A 1 120 MET 120 122 122 MET MET A . n 
A 1 121 LYS 121 123 123 LYS LYS A . n 
A 1 122 THR 122 124 124 THR THR A . n 
A 1 123 SER 123 125 125 SER SER A . n 
A 1 124 ARG 124 126 126 ARG ARG A . n 
A 1 125 HIS 125 127 127 HIS HIS A . n 
A 1 126 LYS 126 128 128 LYS LYS A . n 
A 1 127 GLU 127 129 129 GLU GLU A . n 
A 1 128 PHE 128 130 130 PHE PHE A . n 
A 1 129 PHE 129 131 131 PHE PHE A . n 
A 1 130 SER 130 132 132 SER SER A . n 
A 1 131 LEU 131 133 133 LEU LEU A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 SER 133 135 135 SER SER A . n 
A 1 134 HIS 134 136 136 HIS HIS A . n 
A 1 135 ILE 135 137 137 ILE ILE A . n 
A 1 136 VAL 136 138 138 VAL VAL A . n 
A 1 137 LEU 137 139 139 LEU LEU A . n 
A 1 138 GLY 138 140 140 GLY GLY A . n 
A 1 139 ASP 139 141 141 ASP ASP A . n 
A 1 140 ASP 140 142 142 ASP ASP A . n 
A 1 141 PRO 141 143 143 PRO PRO A . n 
A 1 142 GLU 142 144 144 GLU GLU A . n 
A 1 143 VAL 143 145 145 VAL VAL A . n 
A 1 144 GLN 144 146 146 GLN GLN A . n 
A 1 145 HIS 145 147 147 HIS HIS A . n 
A 1 146 GLY 146 148 148 GLY GLY A . n 
A 1 147 LYS 147 149 149 LYS LYS A . n 
A 1 148 PRO 148 150 150 PRO PRO A . n 
A 1 149 ASP 149 151 151 ASP ASP A . n 
A 1 150 PRO 150 152 152 PRO PRO A . n 
A 1 151 ASP 151 153 153 ASP ASP A . n 
A 1 152 ILE 152 154 154 ILE ILE A . n 
A 1 153 PHE 153 155 155 PHE PHE A . n 
A 1 154 LEU 154 156 156 LEU LEU A . n 
A 1 155 ALA 155 157 157 ALA ALA A . n 
A 1 156 CYS 156 158 158 CYS CYS A . n 
A 1 157 ALA 157 159 159 ALA ALA A . n 
A 1 158 LYS 158 160 160 LYS LYS A . n 
A 1 159 ARG 159 161 161 ARG ARG A . n 
A 1 160 PHE 160 162 162 PHE PHE A . n 
A 1 161 SER 161 163 163 SER SER A . n 
A 1 162 PRO 162 164 164 PRO PRO A . n 
A 1 163 PRO 163 165 165 PRO PRO A . n 
A 1 164 PRO 164 166 166 PRO PRO A . n 
A 1 165 ALA 165 167 167 ALA ALA A . n 
A 1 166 MET 166 168 168 MET MET A . n 
A 1 167 GLU 167 169 169 GLU GLU A . n 
A 1 168 LYS 168 170 170 LYS LYS A . n 
A 1 169 CYS 169 171 171 CYS CYS A . n 
A 1 170 LEU 170 172 172 LEU LEU A . n 
A 1 171 VAL 171 173 173 VAL VAL A . n 
A 1 172 PHE 172 174 174 PHE PHE A . n 
A 1 173 GLU 173 175 175 GLU GLU A . n 
A 1 174 ASP 174 176 176 ASP ASP A . n 
A 1 175 ALA 175 177 177 ALA ALA A . n 
A 1 176 PRO 176 178 178 PRO PRO A . n 
A 1 177 ASN 177 179 179 ASN ASN A . n 
A 1 178 GLY 178 180 180 GLY GLY A . n 
A 1 179 VAL 179 181 181 VAL VAL A . n 
A 1 180 GLU 180 182 182 GLU GLU A . n 
A 1 181 ALA 181 183 183 ALA ALA A . n 
A 1 182 ALA 182 184 184 ALA ALA A . n 
A 1 183 LEU 183 185 185 LEU LEU A . n 
A 1 184 ALA 184 186 186 ALA ALA A . n 
A 1 185 ALA 185 187 187 ALA ALA A . n 
A 1 186 GLY 186 188 188 GLY GLY A . n 
A 1 187 MET 187 189 189 MET MET A . n 
A 1 188 GLN 188 190 190 GLN GLN A . n 
A 1 189 VAL 189 191 191 VAL VAL A . n 
A 1 190 VAL 190 192 192 VAL VAL A . n 
A 1 191 MET 191 193 193 MET MET A . n 
A 1 192 VAL 192 194 194 VAL VAL A . n 
A 1 193 PRO 193 195 195 PRO PRO A . n 
A 1 194 ASP 194 196 196 ASP ASP A . n 
A 1 195 GLY 195 197 197 GLY GLY A . n 
A 1 196 ASN 196 198 198 ASN ASN A . n 
A 1 197 LEU 197 199 199 LEU LEU A . n 
A 1 198 SER 198 200 200 SER SER A . n 
A 1 199 ARG 199 201 201 ARG ARG A . n 
A 1 200 ASP 200 202 202 ASP ASP A . n 
A 1 201 LEU 201 203 203 LEU LEU A . n 
A 1 202 THR 202 204 204 THR THR A . n 
A 1 203 THR 203 205 205 THR THR A . n 
A 1 204 LYS 204 206 206 LYS LYS A . n 
A 1 205 ALA 205 207 207 ALA ALA A . n 
A 1 206 THR 206 208 208 THR THR A . n 
A 1 207 LEU 207 209 209 LEU LEU A . n 
A 1 208 VAL 208 210 210 VAL VAL A . n 
A 1 209 LEU 209 211 211 LEU LEU A . n 
A 1 210 ASN 210 212 212 ASN ASN A . n 
A 1 211 SER 211 213 213 SER SER A . n 
A 1 212 LEU 212 214 214 LEU LEU A . n 
A 1 213 GLN 213 215 215 GLN GLN A . n 
A 1 214 ASP 214 216 216 ASP ASP A . n 
A 1 215 PHE 215 217 217 PHE PHE A . n 
A 1 216 GLN 216 218 218 GLN GLN A . n 
A 1 217 PRO 217 219 219 PRO PRO A . n 
A 1 218 GLU 218 220 220 GLU GLU A . n 
A 1 219 LEU 219 221 221 LEU LEU A . n 
A 1 220 PHE 220 222 222 PHE PHE A . n 
A 1 221 GLY 221 223 223 GLY GLY A . n 
A 1 222 LEU 222 224 224 LEU LEU A . n 
A 1 223 PRO 223 225 225 PRO PRO A . n 
A 1 224 SER 224 226 226 SER SER A . n 
A 1 225 TYR 225 227 227 TYR TYR A . n 
A 1 226 GLU 226 228 228 GLU GLU A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FJF ? ? FJF ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MG  1   301 229 MG  MG  A . 
C 3 FJF 1   302 230 FJF PSU A . 
D 4 HOH 1   401 241 HOH HOH A . 
D 4 HOH 2   402 136 HOH HOH A . 
D 4 HOH 3   403 54  HOH HOH A . 
D 4 HOH 4   404 172 HOH HOH A . 
D 4 HOH 5   405 84  HOH HOH A . 
D 4 HOH 6   406 259 HOH HOH A . 
D 4 HOH 7   407 242 HOH HOH A . 
D 4 HOH 8   408 130 HOH HOH A . 
D 4 HOH 9   409 134 HOH HOH A . 
D 4 HOH 10  410 153 HOH HOH A . 
D 4 HOH 11  411 284 HOH HOH A . 
D 4 HOH 12  412 302 HOH HOH A . 
D 4 HOH 13  413 107 HOH HOH A . 
D 4 HOH 14  414 83  HOH HOH A . 
D 4 HOH 15  415 187 HOH HOH A . 
D 4 HOH 16  416 106 HOH HOH A . 
D 4 HOH 17  417 59  HOH HOH A . 
D 4 HOH 18  418 274 HOH HOH A . 
D 4 HOH 19  419 293 HOH HOH A . 
D 4 HOH 20  420 34  HOH HOH A . 
D 4 HOH 21  421 177 HOH HOH A . 
D 4 HOH 22  422 137 HOH HOH A . 
D 4 HOH 23  423 299 HOH HOH A . 
D 4 HOH 24  424 150 HOH HOH A . 
D 4 HOH 25  425 248 HOH HOH A . 
D 4 HOH 26  426 6   HOH HOH A . 
D 4 HOH 27  427 163 HOH HOH A . 
D 4 HOH 28  428 154 HOH HOH A . 
D 4 HOH 29  429 2   HOH HOH A . 
D 4 HOH 30  430 53  HOH HOH A . 
D 4 HOH 31  431 135 HOH HOH A . 
D 4 HOH 32  432 97  HOH HOH A . 
D 4 HOH 33  433 181 HOH HOH A . 
D 4 HOH 34  434 113 HOH HOH A . 
D 4 HOH 35  435 202 HOH HOH A . 
D 4 HOH 36  436 123 HOH HOH A . 
D 4 HOH 37  437 288 HOH HOH A . 
D 4 HOH 38  438 254 HOH HOH A . 
D 4 HOH 39  439 243 HOH HOH A . 
D 4 HOH 40  440 176 HOH HOH A . 
D 4 HOH 41  441 139 HOH HOH A . 
D 4 HOH 42  442 105 HOH HOH A . 
D 4 HOH 43  443 68  HOH HOH A . 
D 4 HOH 44  444 132 HOH HOH A . 
D 4 HOH 45  445 180 HOH HOH A . 
D 4 HOH 46  446 126 HOH HOH A . 
D 4 HOH 47  447 294 HOH HOH A . 
D 4 HOH 48  448 71  HOH HOH A . 
D 4 HOH 49  449 104 HOH HOH A . 
D 4 HOH 50  450 74  HOH HOH A . 
D 4 HOH 51  451 26  HOH HOH A . 
D 4 HOH 52  452 309 HOH HOH A . 
D 4 HOH 53  453 175 HOH HOH A . 
D 4 HOH 54  454 12  HOH HOH A . 
D 4 HOH 55  455 29  HOH HOH A . 
D 4 HOH 56  456 125 HOH HOH A . 
D 4 HOH 57  457 49  HOH HOH A . 
D 4 HOH 58  458 52  HOH HOH A . 
D 4 HOH 59  459 28  HOH HOH A . 
D 4 HOH 60  460 17  HOH HOH A . 
D 4 HOH 61  461 7   HOH HOH A . 
D 4 HOH 62  462 238 HOH HOH A . 
D 4 HOH 63  463 169 HOH HOH A . 
D 4 HOH 64  464 212 HOH HOH A . 
D 4 HOH 65  465 62  HOH HOH A . 
D 4 HOH 66  466 36  HOH HOH A . 
D 4 HOH 67  467 9   HOH HOH A . 
D 4 HOH 68  468 56  HOH HOH A . 
D 4 HOH 69  469 292 HOH HOH A . 
D 4 HOH 70  470 21  HOH HOH A . 
D 4 HOH 71  471 10  HOH HOH A . 
D 4 HOH 72  472 140 HOH HOH A . 
D 4 HOH 73  473 23  HOH HOH A . 
D 4 HOH 74  474 87  HOH HOH A . 
D 4 HOH 75  475 173 HOH HOH A . 
D 4 HOH 76  476 24  HOH HOH A . 
D 4 HOH 77  477 43  HOH HOH A . 
D 4 HOH 78  478 301 HOH HOH A . 
D 4 HOH 79  479 88  HOH HOH A . 
D 4 HOH 80  480 16  HOH HOH A . 
D 4 HOH 81  481 112 HOH HOH A . 
D 4 HOH 82  482 266 HOH HOH A . 
D 4 HOH 83  483 27  HOH HOH A . 
D 4 HOH 84  484 218 HOH HOH A . 
D 4 HOH 85  485 14  HOH HOH A . 
D 4 HOH 86  486 91  HOH HOH A . 
D 4 HOH 87  487 45  HOH HOH A . 
D 4 HOH 88  488 149 HOH HOH A . 
D 4 HOH 89  489 260 HOH HOH A . 
D 4 HOH 90  490 145 HOH HOH A . 
D 4 HOH 91  491 306 HOH HOH A . 
D 4 HOH 92  492 110 HOH HOH A . 
D 4 HOH 93  493 96  HOH HOH A . 
D 4 HOH 94  494 81  HOH HOH A . 
D 4 HOH 95  495 55  HOH HOH A . 
D 4 HOH 96  496 77  HOH HOH A . 
D 4 HOH 97  497 66  HOH HOH A . 
D 4 HOH 98  498 75  HOH HOH A . 
D 4 HOH 99  499 5   HOH HOH A . 
D 4 HOH 100 500 31  HOH HOH A . 
D 4 HOH 101 501 32  HOH HOH A . 
D 4 HOH 102 502 213 HOH HOH A . 
D 4 HOH 103 503 94  HOH HOH A . 
D 4 HOH 104 504 120 HOH HOH A . 
D 4 HOH 105 505 47  HOH HOH A . 
D 4 HOH 106 506 46  HOH HOH A . 
D 4 HOH 107 507 60  HOH HOH A . 
D 4 HOH 108 508 230 HOH HOH A . 
D 4 HOH 109 509 217 HOH HOH A . 
D 4 HOH 110 510 108 HOH HOH A . 
D 4 HOH 111 511 4   HOH HOH A . 
D 4 HOH 112 512 98  HOH HOH A . 
D 4 HOH 113 513 221 HOH HOH A . 
D 4 HOH 114 514 30  HOH HOH A . 
D 4 HOH 115 515 191 HOH HOH A . 
D 4 HOH 116 516 174 HOH HOH A . 
D 4 HOH 117 517 118 HOH HOH A . 
D 4 HOH 118 518 3   HOH HOH A . 
D 4 HOH 119 519 63  HOH HOH A . 
D 4 HOH 120 520 89  HOH HOH A . 
D 4 HOH 121 521 90  HOH HOH A . 
D 4 HOH 122 522 35  HOH HOH A . 
D 4 HOH 123 523 144 HOH HOH A . 
D 4 HOH 124 524 19  HOH HOH A . 
D 4 HOH 125 525 8   HOH HOH A . 
D 4 HOH 126 526 67  HOH HOH A . 
D 4 HOH 127 527 206 HOH HOH A . 
D 4 HOH 128 528 42  HOH HOH A . 
D 4 HOH 129 529 236 HOH HOH A . 
D 4 HOH 130 530 295 HOH HOH A . 
D 4 HOH 131 531 297 HOH HOH A . 
D 4 HOH 132 532 15  HOH HOH A . 
D 4 HOH 133 533 101 HOH HOH A . 
D 4 HOH 134 534 48  HOH HOH A . 
D 4 HOH 135 535 193 HOH HOH A . 
D 4 HOH 136 536 78  HOH HOH A . 
D 4 HOH 137 537 50  HOH HOH A . 
D 4 HOH 138 538 244 HOH HOH A . 
D 4 HOH 139 539 11  HOH HOH A . 
D 4 HOH 140 540 168 HOH HOH A . 
D 4 HOH 141 541 80  HOH HOH A . 
D 4 HOH 142 542 179 HOH HOH A . 
D 4 HOH 143 543 129 HOH HOH A . 
D 4 HOH 144 544 41  HOH HOH A . 
D 4 HOH 145 545 33  HOH HOH A . 
D 4 HOH 146 546 44  HOH HOH A . 
D 4 HOH 147 547 82  HOH HOH A . 
D 4 HOH 148 548 219 HOH HOH A . 
D 4 HOH 149 549 240 HOH HOH A . 
D 4 HOH 150 550 308 HOH HOH A . 
D 4 HOH 151 551 228 HOH HOH A . 
D 4 HOH 152 552 37  HOH HOH A . 
D 4 HOH 153 553 76  HOH HOH A . 
D 4 HOH 154 554 39  HOH HOH A . 
D 4 HOH 155 555 287 HOH HOH A . 
D 4 HOH 156 556 95  HOH HOH A . 
D 4 HOH 157 557 270 HOH HOH A . 
D 4 HOH 158 558 216 HOH HOH A . 
D 4 HOH 159 559 124 HOH HOH A . 
D 4 HOH 160 560 13  HOH HOH A . 
D 4 HOH 161 561 128 HOH HOH A . 
D 4 HOH 162 562 232 HOH HOH A . 
D 4 HOH 163 563 86  HOH HOH A . 
D 4 HOH 164 564 315 HOH HOH A . 
D 4 HOH 165 565 290 HOH HOH A . 
D 4 HOH 166 566 102 HOH HOH A . 
D 4 HOH 167 567 235 HOH HOH A . 
D 4 HOH 168 568 159 HOH HOH A . 
D 4 HOH 169 569 255 HOH HOH A . 
D 4 HOH 170 570 61  HOH HOH A . 
D 4 HOH 171 571 227 HOH HOH A . 
D 4 HOH 172 572 20  HOH HOH A . 
D 4 HOH 173 573 245 HOH HOH A . 
D 4 HOH 174 574 141 HOH HOH A . 
D 4 HOH 175 575 207 HOH HOH A . 
D 4 HOH 176 576 38  HOH HOH A . 
D 4 HOH 177 577 231 HOH HOH A . 
D 4 HOH 178 578 317 HOH HOH A . 
D 4 HOH 179 579 92  HOH HOH A . 
D 4 HOH 180 580 117 HOH HOH A . 
D 4 HOH 181 581 70  HOH HOH A . 
D 4 HOH 182 582 283 HOH HOH A . 
D 4 HOH 183 583 146 HOH HOH A . 
D 4 HOH 184 584 85  HOH HOH A . 
D 4 HOH 185 585 156 HOH HOH A . 
D 4 HOH 186 586 18  HOH HOH A . 
D 4 HOH 187 587 263 HOH HOH A . 
D 4 HOH 188 588 272 HOH HOH A . 
D 4 HOH 189 589 252 HOH HOH A . 
D 4 HOH 190 590 114 HOH HOH A . 
D 4 HOH 191 591 257 HOH HOH A . 
D 4 HOH 192 592 122 HOH HOH A . 
D 4 HOH 193 593 155 HOH HOH A . 
D 4 HOH 194 594 69  HOH HOH A . 
D 4 HOH 195 595 286 HOH HOH A . 
D 4 HOH 196 596 300 HOH HOH A . 
D 4 HOH 197 597 198 HOH HOH A . 
D 4 HOH 198 598 73  HOH HOH A . 
D 4 HOH 199 599 251 HOH HOH A . 
D 4 HOH 200 600 223 HOH HOH A . 
D 4 HOH 201 601 100 HOH HOH A . 
D 4 HOH 202 602 121 HOH HOH A . 
D 4 HOH 203 603 311 HOH HOH A . 
D 4 HOH 204 604 158 HOH HOH A . 
D 4 HOH 205 605 265 HOH HOH A . 
D 4 HOH 206 606 127 HOH HOH A . 
D 4 HOH 207 607 215 HOH HOH A . 
D 4 HOH 208 608 192 HOH HOH A . 
D 4 HOH 209 609 79  HOH HOH A . 
D 4 HOH 210 610 280 HOH HOH A . 
D 4 HOH 211 611 298 HOH HOH A . 
D 4 HOH 212 612 291 HOH HOH A . 
D 4 HOH 213 613 313 HOH HOH A . 
D 4 HOH 214 614 229 HOH HOH A . 
D 4 HOH 215 615 133 HOH HOH A . 
D 4 HOH 216 616 161 HOH HOH A . 
D 4 HOH 217 617 138 HOH HOH A . 
D 4 HOH 218 618 204 HOH HOH A . 
D 4 HOH 219 619 267 HOH HOH A . 
D 4 HOH 220 620 93  HOH HOH A . 
D 4 HOH 221 621 57  HOH HOH A . 
D 4 HOH 222 622 197 HOH HOH A . 
D 4 HOH 223 623 304 HOH HOH A . 
D 4 HOH 224 624 64  HOH HOH A . 
D 4 HOH 225 625 170 HOH HOH A . 
D 4 HOH 226 626 253 HOH HOH A . 
D 4 HOH 227 627 189 HOH HOH A . 
D 4 HOH 228 628 51  HOH HOH A . 
D 4 HOH 229 629 239 HOH HOH A . 
D 4 HOH 230 630 162 HOH HOH A . 
D 4 HOH 231 631 167 HOH HOH A . 
D 4 HOH 232 632 142 HOH HOH A . 
D 4 HOH 233 633 148 HOH HOH A . 
D 4 HOH 234 634 296 HOH HOH A . 
D 4 HOH 235 635 201 HOH HOH A . 
D 4 HOH 236 636 277 HOH HOH A . 
D 4 HOH 237 637 25  HOH HOH A . 
D 4 HOH 238 638 222 HOH HOH A . 
D 4 HOH 239 639 278 HOH HOH A . 
D 4 HOH 240 640 22  HOH HOH A . 
D 4 HOH 241 641 151 HOH HOH A . 
D 4 HOH 242 642 65  HOH HOH A . 
D 4 HOH 243 643 190 HOH HOH A . 
D 4 HOH 244 644 40  HOH HOH A . 
D 4 HOH 245 645 233 HOH HOH A . 
D 4 HOH 246 646 237 HOH HOH A . 
D 4 HOH 247 647 72  HOH HOH A . 
D 4 HOH 248 648 273 HOH HOH A . 
D 4 HOH 249 649 205 HOH HOH A . 
D 4 HOH 250 650 186 HOH HOH A . 
D 4 HOH 251 651 116 HOH HOH A . 
D 4 HOH 252 652 276 HOH HOH A . 
D 4 HOH 253 653 147 HOH HOH A . 
D 4 HOH 254 654 256 HOH HOH A . 
D 4 HOH 255 655 303 HOH HOH A . 
D 4 HOH 256 656 285 HOH HOH A . 
D 4 HOH 257 657 310 HOH HOH A . 
D 4 HOH 258 658 165 HOH HOH A . 
D 4 HOH 259 659 314 HOH HOH A . 
D 4 HOH 260 660 119 HOH HOH A . 
D 4 HOH 261 661 269 HOH HOH A . 
D 4 HOH 262 662 152 HOH HOH A . 
D 4 HOH 263 663 200 HOH HOH A . 
D 4 HOH 264 664 103 HOH HOH A . 
D 4 HOH 265 665 171 HOH HOH A . 
D 4 HOH 266 666 209 HOH HOH A . 
D 4 HOH 267 667 58  HOH HOH A . 
D 4 HOH 268 668 210 HOH HOH A . 
D 4 HOH 269 669 279 HOH HOH A . 
D 4 HOH 270 670 225 HOH HOH A . 
D 4 HOH 271 671 199 HOH HOH A . 
D 4 HOH 272 672 275 HOH HOH A . 
D 4 HOH 273 673 99  HOH HOH A . 
D 4 HOH 274 674 211 HOH HOH A . 
D 4 HOH 275 675 115 HOH HOH A . 
D 4 HOH 276 676 182 HOH HOH A . 
D 4 HOH 277 677 282 HOH HOH A . 
D 4 HOH 278 678 268 HOH HOH A . 
D 4 HOH 279 679 250 HOH HOH A . 
D 4 HOH 280 680 261 HOH HOH A . 
D 4 HOH 281 681 214 HOH HOH A . 
D 4 HOH 282 682 264 HOH HOH A . 
D 4 HOH 283 683 226 HOH HOH A . 
D 4 HOH 284 684 262 HOH HOH A . 
D 4 HOH 285 685 131 HOH HOH A . 
D 4 HOH 286 686 224 HOH HOH A . 
D 4 HOH 287 687 166 HOH HOH A . 
D 4 HOH 288 688 157 HOH HOH A . 
D 4 HOH 289 689 183 HOH HOH A . 
D 4 HOH 290 690 281 HOH HOH A . 
D 4 HOH 291 691 249 HOH HOH A . 
D 4 HOH 292 692 178 HOH HOH A . 
D 4 HOH 293 693 258 HOH HOH A . 
D 4 HOH 294 694 164 HOH HOH A . 
D 4 HOH 295 695 316 HOH HOH A . 
D 4 HOH 296 696 188 HOH HOH A . 
D 4 HOH 297 697 307 HOH HOH A . 
D 4 HOH 298 698 305 HOH HOH A . 
D 4 HOH 299 699 247 HOH HOH A . 
D 4 HOH 300 700 196 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 201 ? NE  ? A ARG 199 NE  
2 1 Y 1 A ARG 201 ? CZ  ? A ARG 199 CZ  
3 1 Y 1 A ARG 201 ? NH1 ? A ARG 199 NH1 
4 1 Y 1 A ARG 201 ? NH2 ? A ARG 199 NH2 
5 1 Y 1 A GLU 228 ? CG  ? A GLU 226 CG  
6 1 Y 1 A GLU 228 ? CD  ? A GLU 226 CD  
7 1 Y 1 A GLU 228 ? OE1 ? A GLU 226 OE1 
8 1 Y 1 A GLU 228 ? OE2 ? A GLU 226 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.9_1692  ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? v20230630 ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? v20230630 ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.9_1692  ? 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                     9M7M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.620 
_cell.length_a_esd                 ? 
_cell.length_b                     61.090 
_cell.length_b_esd                 ? 
_cell.length_c                     68.250 
_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                         9M7M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 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                   9M7M 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.77 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M magnesium chloride, 0.1 M Tris-HCl (pH 8.5), 30% (w/v) PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-11-25 
_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   0.97933 
_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                        'PAL/PLS BEAMLINE 7A (6B, 6C1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97933 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '7A (6B, 6C1)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M7M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.26 
_reflns.d_resolution_low                               30 
_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                                     107923 
_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                           95.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.53 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.89 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.26 
_reflns_shell.d_res_low                                     1.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6012 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.85 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9M7M 
_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                            1.260 
_refine.ls_d_res_low                             29.792 
_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                     107923 
_refine.ls_number_reflns_R_free                  3836 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.79 
_refine.ls_percent_reflns_R_free                 3.55 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1845 
_refine.ls_R_factor_R_free                       0.2090 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1836 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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               NONE 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.05 
_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                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.260 
_refine_hist.d_res_low                        29.792 
_refine_hist.number_atoms_solvent             300 
_refine_hist.number_atoms_total               2069 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1751 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.016  ? 1819 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.551  ? 2470 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 11.635 ? 675  ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.096  ? 282  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 318  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.2601 1.2760 . . 138 3756 93.00  . . . . 0.3008 . . . . . . . . . . . . . . . 0.3347 
'X-RAY DIFFRACTION' 1.2760 1.2928 . . 139 3759 94.00  . . . . 0.2895 . . . . . . . . . . . . . . . 0.3269 
'X-RAY DIFFRACTION' 1.2928 1.3105 . . 143 3834 95.00  . . . . 0.2916 . . . . . . . . . . . . . . . 0.3221 
'X-RAY DIFFRACTION' 1.3105 1.3292 . . 139 3817 95.00  . . . . 0.2832 . . . . . . . . . . . . . . . 0.3045 
'X-RAY DIFFRACTION' 1.3292 1.3491 . . 140 3851 96.00  . . . . 0.2726 . . . . . . . . . . . . . . . 0.2919 
'X-RAY DIFFRACTION' 1.3491 1.3702 . . 136 3780 95.00  . . . . 0.2701 . . . . . . . . . . . . . . . 0.2852 
'X-RAY DIFFRACTION' 1.3702 1.3926 . . 141 3798 95.00  . . . . 0.2691 . . . . . . . . . . . . . . . 0.3694 
'X-RAY DIFFRACTION' 1.3926 1.4166 . . 140 3854 96.00  . . . . 0.2714 . . . . . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 1.4166 1.4424 . . 142 3821 95.00  . . . . 0.2533 . . . . . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 1.4424 1.4701 . . 139 3762 95.00  . . . . 0.2534 . . . . . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 1.4701 1.5001 . . 144 3825 94.00  . . . . 0.2362 . . . . . . . . . . . . . . . 0.2796 
'X-RAY DIFFRACTION' 1.5001 1.5328 . . 138 3714 93.00  . . . . 0.2340 . . . . . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 1.5328 1.5684 . . 143 3859 94.00  . . . . 0.2235 . . . . . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 1.5684 1.6076 . . 139 3759 94.00  . . . . 0.2165 . . . . . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 1.6076 1.6511 . . 135 3748 94.00  . . . . 0.2293 . . . . . . . . . . . . . . . 0.2863 
'X-RAY DIFFRACTION' 1.6511 1.6997 . . 139 3795 94.00  . . . . 0.2180 . . . . . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 1.6997 1.7545 . . 138 3777 94.00  . . . . 0.2094 . . . . . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 1.7545 1.8172 . . 145 3882 95.00  . . . . 0.1944 . . . . . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 1.8172 1.8900 . . 143 3871 97.00  . . . . 0.1839 . . . . . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 1.8900 1.9760 . . 145 3902 97.00  . . . . 0.1775 . . . . . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 1.9760 2.0801 . . 143 3929 98.00  . . . . 0.1776 . . . . . . . . . . . . . . . 0.2362 
'X-RAY DIFFRACTION' 2.0801 2.2104 . . 144 3958 99.00  . . . . 0.1684 . . . . . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 2.2104 2.3810 . . 148 4001 99.00  . . . . 0.1616 . . . . . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 2.3810 2.6205 . . 149 3992 99.00  . . . . 0.1588 . . . . . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 2.6205 2.9994 . . 152 4009 100.00 . . . . 0.1705 . . . . . . . . . . . . . . . 0.1804 
'X-RAY DIFFRACTION' 2.9994 3.7777 . . 149 4027 100.00 . . . . 0.1527 . . . . . . . . . . . . . . . 0.1728 
'X-RAY DIFFRACTION' 3.7777 29.792 . . 145 4007 99.00  . . . . 0.1391 . . . . . . . . . . . . . . . 0.1505 
# 
_struct.entry_id                     9M7M 
_struct.title                        
;Crystal structure of human pseudouridine 5'-monophosphate phosphatase (hHDHD1A) complexed with pseudouridine
;
_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        9M7M 
_struct_keywords.text            
'pseudouridine monophosphate phosphatase, HAD phosphatase, cofactor, pseudouridine, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDHD1_HUMAN 
_struct_ref.pdbx_db_accession          Q08623 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APPQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKL
KEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRF
SPPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE
;
_struct_ref.pdbx_align_begin           3 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9M7M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 226 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q08623 
_struct_ref_seq.db_align_beg                  3 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  228 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       228 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 110   ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  10080 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 20  ? ARG A 34  ? THR A 22  ARG A 36  1 ? 15 
HELX_P HELX_P2  AA2 SER A 40  ? MET A 48  ? SER A 42  MET A 50  1 ? 9  
HELX_P HELX_P3  AA3 LYS A 51  ? GLN A 64  ? LYS A 53  GLN A 66  1 ? 14 
HELX_P HELX_P4  AA4 SER A 68  ? LYS A 81  ? SER A 70  LYS A 83  1 ? 14 
HELX_P HELX_P5  AA5 GLU A 82  ? ALA A 87  ? GLU A 84  ALA A 89  5 ? 6  
HELX_P HELX_P6  AA6 GLY A 92  ? HIS A 103 ? GLY A 94  HIS A 105 1 ? 12 
HELX_P HELX_P7  AA7 GLY A 114 ? SER A 123 ? GLY A 116 SER A 125 1 ? 10 
HELX_P HELX_P8  AA8 HIS A 125 ? SER A 130 ? HIS A 127 SER A 132 1 ? 6  
HELX_P HELX_P9  AA9 PRO A 150 ? LYS A 158 ? PRO A 152 LYS A 160 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 165 ? GLU A 167 ? ALA A 167 GLU A 169 5 ? 3  
HELX_P HELX_P11 AB2 ALA A 175 ? ALA A 185 ? ALA A 177 ALA A 187 1 ? 11 
HELX_P HELX_P12 AB3 ARG A 199 ? THR A 203 ? ARG A 201 THR A 205 5 ? 5  
HELX_P HELX_P13 AB4 SER A 211 ? PHE A 215 ? SER A 213 PHE A 217 5 ? 5  
HELX_P HELX_P14 AB5 GLN A 216 ? GLY A 221 ? GLN A 218 GLY A 223 5 ? 6  
# 
_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 ASP 12  OD2 ? ? ? 1_555 B MG  . MG ? ? A ASP 14  A MG  301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc2 metalc ? ? A ASP 14  O   ? ? ? 1_555 B MG  . MG ? ? A ASP 16  A MG  301 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc3 metalc ? ? A ASP 174 OD1 ? ? ? 1_555 B MG  . MG ? ? A ASP 176 A MG  301 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc4 metalc ? ? B MG  .   MG  ? ? ? 1_555 D HOH . O  ? ? A MG  301 A HOH 426 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc5 metalc ? ? B MG  .   MG  ? ? ? 1_555 D HOH . O  ? ? A MG  301 A HOH 429 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc6 metalc ? ? B MG  .   MG  ? ? ? 1_555 D HOH . O  ? ? A MG  301 A HOH 511 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
# 
_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  OD2 ? A ASP 12  ? A ASP 14  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? A ASP 14  ? A ASP 16  ? 1_555 88.8  ? 
2  OD2 ? A ASP 12  ? A ASP 14  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 OD1 ? A ASP 174 ? A ASP 176 ? 1_555 88.7  ? 
3  O   ? A ASP 14  ? A ASP 16  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 OD1 ? A ASP 174 ? A ASP 176 ? 1_555 91.5  ? 
4  OD2 ? A ASP 12  ? A ASP 14  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 426 ? 1_555 88.0  ? 
5  O   ? A ASP 14  ? A ASP 16  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 426 ? 1_555 173.7 ? 
6  OD1 ? A ASP 174 ? A ASP 176 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 426 ? 1_555 93.7  ? 
7  OD2 ? A ASP 12  ? A ASP 14  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 429 ? 1_555 171.9 ? 
8  O   ? A ASP 14  ? A ASP 16  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 429 ? 1_555 87.8  ? 
9  OD1 ? A ASP 174 ? A ASP 176 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 429 ? 1_555 84.1  ? 
10 O   ? D HOH .   ? A HOH 426 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 429 ? 1_555 96.1  ? 
11 OD2 ? A ASP 12  ? A ASP 14  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 99.8  ? 
12 O   ? A ASP 14  ? A ASP 16  ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 94.0  ? 
13 OD1 ? A ASP 174 ? A ASP 176 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 170.0 ? 
14 O   ? D HOH .   ? A HOH 426 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 81.2  ? 
15 O   ? D HOH .   ? A HOH 429 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 87.8  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LYS 147 A . ? LYS 149 A PRO 148 A ? PRO 150 A 1 17.66 
2 SER 161 A . ? SER 163 A PRO 162 A ? PRO 164 A 1 -3.17 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? 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 ILE A 135 ? VAL A 136 ? ILE A 137 VAL A 138 
AA1 2 PHE A 107 ? ALA A 110 ? PHE A 109 ALA A 112 
AA1 3 HIS A 8   ? PHE A 11  ? HIS A 10  PHE A 13  
AA1 4 CYS A 169 ? GLU A 173 ? CYS A 171 GLU A 175 
AA1 5 GLN A 188 ? MET A 191 ? GLN A 190 MET A 193 
AA1 6 LEU A 207 ? VAL A 208 ? LEU A 209 VAL A 210 
# 
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 O VAL A 136 ? O VAL A 138 N LEU A 109 ? N LEU A 111 
AA1 2 3 O ALA A 108 ? O ALA A 110 N PHE A 11  ? N PHE A 13  
AA1 3 4 N ILE A 10  ? N ILE A 12  O LEU A 170 ? O LEU A 172 
AA1 4 5 N VAL A 171 ? N VAL A 173 O VAL A 190 ? O VAL A 192 
AA1 5 6 N MET A 191 ? N MET A 193 O LEU A 207 ? O LEU A 209 
# 
_pdbx_entry_details.entry_id                   9M7M 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 555 ? ? O A HOH 556 ? ? 2.00 
2  1 O   A HOH 403 ? ? O A HOH 462 ? ? 2.02 
3  1 OE1 A GLN 66  ? ? O A HOH 401 ? ? 2.02 
4  1 O   A HOH 576 ? ? O A HOH 646 ? ? 2.04 
5  1 O   A HOH 638 ? ? O A HOH 683 ? ? 2.04 
6  1 O   A HOH 446 ? ? O A HOH 612 ? ? 2.04 
7  1 O   A HOH 691 ? ? O A HOH 700 ? ? 2.07 
8  1 O   A HOH 489 ? ? O A HOH 595 ? ? 2.07 
9  1 O   A HOH 404 ? ? O A HOH 619 ? ? 2.07 
10 1 O   A HOH 589 ? ? O A HOH 610 ? ? 2.10 
11 1 O   A HOH 653 ? ? O A HOH 694 ? ? 2.10 
12 1 O   A HOH 403 ? ? O A HOH 581 ? ? 2.10 
13 1 O   A HOH 412 ? ? O A HOH 611 ? ? 2.12 
14 1 O   A HOH 575 ? ? O A HOH 678 ? ? 2.12 
15 1 O   A HOH 587 ? ? O A HOH 597 ? ? 2.16 
16 1 O   A HOH 478 ? ? O A HOH 513 ? ? 2.16 
17 1 N   A ALA 3   ? ? O A HOH 402 ? ? 2.16 
18 1 O   A HOH 437 ? ? O A HOH 548 ? ? 2.16 
19 1 OD1 A ASP 153 ? ? O A HOH 403 ? ? 2.16 
20 1 O   A HOH 421 ? ? O A HOH 583 ? ? 2.17 
21 1 O   A HOH 563 ? ? O A HOH 680 ? ? 2.18 
22 1 O   A HOH 422 ? ? O A HOH 636 ? ? 2.18 
23 1 O   A HOH 440 ? ? O A HOH 568 ? ? 2.18 
24 1 O   A HOH 431 ? ? O A HOH 670 ? ? 2.19 
25 1 O   A HOH 416 ? ? O A HOH 567 ? ? 2.19 
26 1 O   A HOH 410 ? ? O A HOH 425 ? ? 2.19 
27 1 O   A HOH 417 ? ? O A HOH 654 ? ? 2.19 
28 1 O   A HOH 410 ? ? O A HOH 413 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 661 ? ? 1_555 O A HOH 690 ? ? 3_645 2.14 
2 1 O A HOH 646 ? ? 1_555 O A HOH 692 ? ? 2_565 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                87.35 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -12.85 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 MET A 15 ? ? -105.04 -67.81 
2 1 ASP A 21 ? ? -84.86  49.12  
3 1 PRO A 68 ? ? -87.04  46.83  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 409 ? D HOH . 
2 1 A HOH 615 ? D HOH . 
3 1 A HOH 618 ? D HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         24.0030 
_pdbx_refine_tls.origin_y         16.0201 
_pdbx_refine_tls.origin_z         11.5378 
_pdbx_refine_tls.T[1][1]          0.0569 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0169 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0135 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0295 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0166 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0570 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.7028 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0117 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.6489 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.4852 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1282 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.4542 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0752 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0937 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0587 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0475 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0180 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0281 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0783 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0235 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0301 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 695 ? 5.82 . 
2 1 O ? A HOH 696 ? 6.15 . 
3 1 O ? A HOH 697 ? 6.22 . 
4 1 O ? A HOH 698 ? 6.44 . 
5 1 O ? A HOH 699 ? 6.59 . 
6 1 O ? A HOH 700 ? 6.89 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
FJF O01  O  N N 88  
FJF C02  C  N N 89  
FJF N03  N  N N 90  
FJF C04  C  N N 91  
FJF C05  C  N N 92  
FJF C06  C  N N 93  
FJF O07  O  N N 94  
FJF N08  N  N N 95  
FJF C09  C  N S 96  
FJF O10  O  N N 97  
FJF C11  C  N R 98  
FJF C12  C  N N 99  
FJF O13  O  N N 100 
FJF C14  C  N S 101 
FJF O15  O  N N 102 
FJF C16  C  N R 103 
FJF O17  O  N N 104 
FJF H1   H  N N 105 
FJF H3   H  N N 106 
FJF H4   H  N N 107 
FJF H5   H  N N 108 
FJF H6   H  N N 109 
FJF H7   H  N N 110 
FJF H8   H  N N 111 
FJF H9   H  N N 112 
FJF H10  H  N N 113 
FJF H11  H  N N 114 
FJF H12  H  N N 115 
FJF H13  H  N N 116 
GLN N    N  N N 117 
GLN CA   C  N S 118 
GLN C    C  N N 119 
GLN O    O  N N 120 
GLN CB   C  N N 121 
GLN CG   C  N N 122 
GLN CD   C  N N 123 
GLN OE1  O  N N 124 
GLN NE2  N  N N 125 
GLN OXT  O  N N 126 
GLN H    H  N N 127 
GLN H2   H  N N 128 
GLN HA   H  N N 129 
GLN HB2  H  N N 130 
GLN HB3  H  N N 131 
GLN HG2  H  N N 132 
GLN HG3  H  N N 133 
GLN HE21 H  N N 134 
GLN HE22 H  N N 135 
GLN HXT  H  N N 136 
GLU N    N  N N 137 
GLU CA   C  N S 138 
GLU C    C  N N 139 
GLU O    O  N N 140 
GLU CB   C  N N 141 
GLU CG   C  N N 142 
GLU CD   C  N N 143 
GLU OE1  O  N N 144 
GLU OE2  O  N N 145 
GLU OXT  O  N N 146 
GLU H    H  N N 147 
GLU H2   H  N N 148 
GLU HA   H  N N 149 
GLU HB2  H  N N 150 
GLU HB3  H  N N 151 
GLU HG2  H  N N 152 
GLU HG3  H  N N 153 
GLU HE2  H  N N 154 
GLU HXT  H  N N 155 
GLY N    N  N N 156 
GLY CA   C  N N 157 
GLY C    C  N N 158 
GLY O    O  N N 159 
GLY OXT  O  N N 160 
GLY H    H  N N 161 
GLY H2   H  N N 162 
GLY HA2  H  N N 163 
GLY HA3  H  N N 164 
GLY HXT  H  N N 165 
HIS N    N  N N 166 
HIS CA   C  N S 167 
HIS C    C  N N 168 
HIS O    O  N N 169 
HIS CB   C  N N 170 
HIS CG   C  Y N 171 
HIS ND1  N  Y N 172 
HIS CD2  C  Y N 173 
HIS CE1  C  Y N 174 
HIS NE2  N  Y N 175 
HIS OXT  O  N N 176 
HIS H    H  N N 177 
HIS H2   H  N N 178 
HIS HA   H  N N 179 
HIS HB2  H  N N 180 
HIS HB3  H  N N 181 
HIS HD1  H  N N 182 
HIS HD2  H  N N 183 
HIS HE1  H  N N 184 
HIS HE2  H  N N 185 
HIS HXT  H  N N 186 
HOH O    O  N N 187 
HOH H1   H  N N 188 
HOH H2   H  N N 189 
ILE N    N  N N 190 
ILE CA   C  N S 191 
ILE C    C  N N 192 
ILE O    O  N N 193 
ILE CB   C  N S 194 
ILE CG1  C  N N 195 
ILE CG2  C  N N 196 
ILE CD1  C  N N 197 
ILE OXT  O  N N 198 
ILE H    H  N N 199 
ILE H2   H  N N 200 
ILE HA   H  N N 201 
ILE HB   H  N N 202 
ILE HG12 H  N N 203 
ILE HG13 H  N N 204 
ILE HG21 H  N N 205 
ILE HG22 H  N N 206 
ILE HG23 H  N N 207 
ILE HD11 H  N N 208 
ILE HD12 H  N N 209 
ILE HD13 H  N N 210 
ILE HXT  H  N N 211 
LEU N    N  N N 212 
LEU CA   C  N S 213 
LEU C    C  N N 214 
LEU O    O  N N 215 
LEU CB   C  N N 216 
LEU CG   C  N N 217 
LEU CD1  C  N N 218 
LEU CD2  C  N N 219 
LEU OXT  O  N N 220 
LEU H    H  N N 221 
LEU H2   H  N N 222 
LEU HA   H  N N 223 
LEU HB2  H  N N 224 
LEU HB3  H  N N 225 
LEU HG   H  N N 226 
LEU HD11 H  N N 227 
LEU HD12 H  N N 228 
LEU HD13 H  N N 229 
LEU HD21 H  N N 230 
LEU HD22 H  N N 231 
LEU HD23 H  N N 232 
LEU HXT  H  N N 233 
LYS N    N  N N 234 
LYS CA   C  N S 235 
LYS C    C  N N 236 
LYS O    O  N N 237 
LYS CB   C  N N 238 
LYS CG   C  N N 239 
LYS CD   C  N N 240 
LYS CE   C  N N 241 
LYS NZ   N  N N 242 
LYS OXT  O  N N 243 
LYS H    H  N N 244 
LYS H2   H  N N 245 
LYS HA   H  N N 246 
LYS HB2  H  N N 247 
LYS HB3  H  N N 248 
LYS HG2  H  N N 249 
LYS HG3  H  N N 250 
LYS HD2  H  N N 251 
LYS HD3  H  N N 252 
LYS HE2  H  N N 253 
LYS HE3  H  N N 254 
LYS HZ1  H  N N 255 
LYS HZ2  H  N N 256 
LYS HZ3  H  N N 257 
LYS HXT  H  N N 258 
MET N    N  N N 259 
MET CA   C  N S 260 
MET C    C  N N 261 
MET O    O  N N 262 
MET CB   C  N N 263 
MET CG   C  N N 264 
MET SD   S  N N 265 
MET CE   C  N N 266 
MET OXT  O  N N 267 
MET H    H  N N 268 
MET H2   H  N N 269 
MET HA   H  N N 270 
MET HB2  H  N N 271 
MET HB3  H  N N 272 
MET HG2  H  N N 273 
MET HG3  H  N N 274 
MET HE1  H  N N 275 
MET HE2  H  N N 276 
MET HE3  H  N N 277 
MET HXT  H  N N 278 
MG  MG   MG N N 279 
PHE N    N  N N 280 
PHE CA   C  N S 281 
PHE C    C  N N 282 
PHE O    O  N N 283 
PHE CB   C  N N 284 
PHE CG   C  Y N 285 
PHE CD1  C  Y N 286 
PHE CD2  C  Y N 287 
PHE CE1  C  Y N 288 
PHE CE2  C  Y N 289 
PHE CZ   C  Y N 290 
PHE OXT  O  N N 291 
PHE H    H  N N 292 
PHE H2   H  N N 293 
PHE HA   H  N N 294 
PHE HB2  H  N N 295 
PHE HB3  H  N N 296 
PHE HD1  H  N N 297 
PHE HD2  H  N N 298 
PHE HE1  H  N N 299 
PHE HE2  H  N N 300 
PHE HZ   H  N N 301 
PHE HXT  H  N N 302 
PRO N    N  N N 303 
PRO CA   C  N S 304 
PRO C    C  N N 305 
PRO O    O  N N 306 
PRO CB   C  N N 307 
PRO CG   C  N N 308 
PRO CD   C  N N 309 
PRO OXT  O  N N 310 
PRO H    H  N N 311 
PRO HA   H  N N 312 
PRO HB2  H  N N 313 
PRO HB3  H  N N 314 
PRO HG2  H  N N 315 
PRO HG3  H  N N 316 
PRO HD2  H  N N 317 
PRO HD3  H  N N 318 
PRO HXT  H  N N 319 
SER N    N  N N 320 
SER CA   C  N S 321 
SER C    C  N N 322 
SER O    O  N N 323 
SER CB   C  N N 324 
SER OG   O  N N 325 
SER OXT  O  N N 326 
SER H    H  N N 327 
SER H2   H  N N 328 
SER HA   H  N N 329 
SER HB2  H  N N 330 
SER HB3  H  N N 331 
SER HG   H  N N 332 
SER HXT  H  N N 333 
THR N    N  N N 334 
THR CA   C  N S 335 
THR C    C  N N 336 
THR O    O  N N 337 
THR CB   C  N R 338 
THR OG1  O  N N 339 
THR CG2  C  N N 340 
THR OXT  O  N N 341 
THR H    H  N N 342 
THR H2   H  N N 343 
THR HA   H  N N 344 
THR HB   H  N N 345 
THR HG1  H  N N 346 
THR HG21 H  N N 347 
THR HG22 H  N N 348 
THR HG23 H  N N 349 
THR HXT  H  N N 350 
TRP N    N  N N 351 
TRP CA   C  N S 352 
TRP C    C  N N 353 
TRP O    O  N N 354 
TRP CB   C  N N 355 
TRP CG   C  Y N 356 
TRP CD1  C  Y N 357 
TRP CD2  C  Y N 358 
TRP NE1  N  Y N 359 
TRP CE2  C  Y N 360 
TRP CE3  C  Y N 361 
TRP CZ2  C  Y N 362 
TRP CZ3  C  Y N 363 
TRP CH2  C  Y N 364 
TRP OXT  O  N N 365 
TRP H    H  N N 366 
TRP H2   H  N N 367 
TRP HA   H  N N 368 
TRP HB2  H  N N 369 
TRP HB3  H  N N 370 
TRP HD1  H  N N 371 
TRP HE1  H  N N 372 
TRP HE3  H  N N 373 
TRP HZ2  H  N N 374 
TRP HZ3  H  N N 375 
TRP HH2  H  N N 376 
TRP HXT  H  N N 377 
TYR N    N  N N 378 
TYR CA   C  N S 379 
TYR C    C  N N 380 
TYR O    O  N N 381 
TYR CB   C  N N 382 
TYR CG   C  Y N 383 
TYR CD1  C  Y N 384 
TYR CD2  C  Y N 385 
TYR CE1  C  Y N 386 
TYR CE2  C  Y N 387 
TYR CZ   C  Y N 388 
TYR OH   O  N N 389 
TYR OXT  O  N N 390 
TYR H    H  N N 391 
TYR H2   H  N N 392 
TYR HA   H  N N 393 
TYR HB2  H  N N 394 
TYR HB3  H  N N 395 
TYR HD1  H  N N 396 
TYR HD2  H  N N 397 
TYR HE1  H  N N 398 
TYR HE2  H  N N 399 
TYR HH   H  N N 400 
TYR HXT  H  N N 401 
VAL N    N  N N 402 
VAL CA   C  N S 403 
VAL C    C  N N 404 
VAL O    O  N N 405 
VAL CB   C  N N 406 
VAL CG1  C  N N 407 
VAL CG2  C  N N 408 
VAL OXT  O  N N 409 
VAL H    H  N N 410 
VAL H2   H  N N 411 
VAL HA   H  N N 412 
VAL HB   H  N N 413 
VAL HG11 H  N N 414 
VAL HG12 H  N N 415 
VAL HG13 H  N N 416 
VAL HG21 H  N N 417 
VAL HG22 H  N N 418 
VAL HG23 H  N N 419 
VAL HXT  H  N N 420 
# 
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  
FJF O13 C12  sing N N 83  
FJF C12 C11  sing N N 84  
FJF O10 C11  sing N N 85  
FJF O10 C09  sing N N 86  
FJF C11 C14  sing N N 87  
FJF C09 C05  sing N N 88  
FJF C09 C16  sing N N 89  
FJF C14 O15  sing N N 90  
FJF C14 C16  sing N N 91  
FJF C05 C04  doub N N 92  
FJF C05 C06  sing N N 93  
FJF O07 C06  doub N N 94  
FJF C04 N03  sing N N 95  
FJF C06 N08  sing N N 96  
FJF N03 C02  sing N N 97  
FJF N08 C02  sing N N 98  
FJF C02 O01  doub N N 99  
FJF C16 O17  sing N N 100 
FJF C04 H1   sing N N 101 
FJF N08 H3   sing N N 102 
FJF C09 H4   sing N N 103 
FJF C11 H5   sing N N 104 
FJF C12 H6   sing N N 105 
FJF C12 H7   sing N N 106 
FJF O13 H8   sing N N 107 
FJF C14 H9   sing N N 108 
FJF O15 H10  sing N N 109 
FJF C16 H11  sing N N 110 
FJF O17 H12  sing N N 111 
FJF N03 H13  sing N N 112 
GLN N   CA   sing N N 113 
GLN N   H    sing N N 114 
GLN N   H2   sing N N 115 
GLN CA  C    sing N N 116 
GLN CA  CB   sing N N 117 
GLN CA  HA   sing N N 118 
GLN C   O    doub N N 119 
GLN C   OXT  sing N N 120 
GLN CB  CG   sing N N 121 
GLN CB  HB2  sing N N 122 
GLN CB  HB3  sing N N 123 
GLN CG  CD   sing N N 124 
GLN CG  HG2  sing N N 125 
GLN CG  HG3  sing N N 126 
GLN CD  OE1  doub N N 127 
GLN CD  NE2  sing N N 128 
GLN NE2 HE21 sing N N 129 
GLN NE2 HE22 sing N N 130 
GLN OXT HXT  sing N N 131 
GLU N   CA   sing N N 132 
GLU N   H    sing N N 133 
GLU N   H2   sing N N 134 
GLU CA  C    sing N N 135 
GLU CA  CB   sing N N 136 
GLU CA  HA   sing N N 137 
GLU C   O    doub N N 138 
GLU C   OXT  sing N N 139 
GLU CB  CG   sing N N 140 
GLU CB  HB2  sing N N 141 
GLU CB  HB3  sing N N 142 
GLU CG  CD   sing N N 143 
GLU CG  HG2  sing N N 144 
GLU CG  HG3  sing N N 145 
GLU CD  OE1  doub N N 146 
GLU CD  OE2  sing N N 147 
GLU OE2 HE2  sing N N 148 
GLU OXT HXT  sing N N 149 
GLY N   CA   sing N N 150 
GLY N   H    sing N N 151 
GLY N   H2   sing N N 152 
GLY CA  C    sing N N 153 
GLY CA  HA2  sing N N 154 
GLY CA  HA3  sing N N 155 
GLY C   O    doub N N 156 
GLY C   OXT  sing N N 157 
GLY OXT HXT  sing N N 158 
HIS N   CA   sing N N 159 
HIS N   H    sing N N 160 
HIS N   H2   sing N N 161 
HIS CA  C    sing N N 162 
HIS CA  CB   sing N N 163 
HIS CA  HA   sing N N 164 
HIS C   O    doub N N 165 
HIS C   OXT  sing N N 166 
HIS CB  CG   sing N N 167 
HIS CB  HB2  sing N N 168 
HIS CB  HB3  sing N N 169 
HIS CG  ND1  sing Y N 170 
HIS CG  CD2  doub Y N 171 
HIS ND1 CE1  doub Y N 172 
HIS ND1 HD1  sing N N 173 
HIS CD2 NE2  sing Y N 174 
HIS CD2 HD2  sing N N 175 
HIS CE1 NE2  sing Y N 176 
HIS CE1 HE1  sing N N 177 
HIS NE2 HE2  sing N N 178 
HIS OXT HXT  sing N N 179 
HOH O   H1   sing N N 180 
HOH O   H2   sing N N 181 
ILE N   CA   sing N N 182 
ILE N   H    sing N N 183 
ILE N   H2   sing N N 184 
ILE CA  C    sing N N 185 
ILE CA  CB   sing N N 186 
ILE CA  HA   sing N N 187 
ILE C   O    doub N N 188 
ILE C   OXT  sing N N 189 
ILE CB  CG1  sing N N 190 
ILE CB  CG2  sing N N 191 
ILE CB  HB   sing N N 192 
ILE CG1 CD1  sing N N 193 
ILE CG1 HG12 sing N N 194 
ILE CG1 HG13 sing N N 195 
ILE CG2 HG21 sing N N 196 
ILE CG2 HG22 sing N N 197 
ILE CG2 HG23 sing N N 198 
ILE CD1 HD11 sing N N 199 
ILE CD1 HD12 sing N N 200 
ILE CD1 HD13 sing N N 201 
ILE OXT HXT  sing N N 202 
LEU N   CA   sing N N 203 
LEU N   H    sing N N 204 
LEU N   H2   sing N N 205 
LEU CA  C    sing N N 206 
LEU CA  CB   sing N N 207 
LEU CA  HA   sing N N 208 
LEU C   O    doub N N 209 
LEU C   OXT  sing N N 210 
LEU CB  CG   sing N N 211 
LEU CB  HB2  sing N N 212 
LEU CB  HB3  sing N N 213 
LEU CG  CD1  sing N N 214 
LEU CG  CD2  sing N N 215 
LEU CG  HG   sing N N 216 
LEU CD1 HD11 sing N N 217 
LEU CD1 HD12 sing N N 218 
LEU CD1 HD13 sing N N 219 
LEU CD2 HD21 sing N N 220 
LEU CD2 HD22 sing N N 221 
LEU CD2 HD23 sing N N 222 
LEU OXT HXT  sing N N 223 
LYS N   CA   sing N N 224 
LYS N   H    sing N N 225 
LYS N   H2   sing N N 226 
LYS CA  C    sing N N 227 
LYS CA  CB   sing N N 228 
LYS CA  HA   sing N N 229 
LYS C   O    doub N N 230 
LYS C   OXT  sing N N 231 
LYS CB  CG   sing N N 232 
LYS CB  HB2  sing N N 233 
LYS CB  HB3  sing N N 234 
LYS CG  CD   sing N N 235 
LYS CG  HG2  sing N N 236 
LYS CG  HG3  sing N N 237 
LYS CD  CE   sing N N 238 
LYS CD  HD2  sing N N 239 
LYS CD  HD3  sing N N 240 
LYS CE  NZ   sing N N 241 
LYS CE  HE2  sing N N 242 
LYS CE  HE3  sing N N 243 
LYS NZ  HZ1  sing N N 244 
LYS NZ  HZ2  sing N N 245 
LYS NZ  HZ3  sing N N 246 
LYS OXT HXT  sing N N 247 
MET N   CA   sing N N 248 
MET N   H    sing N N 249 
MET N   H2   sing N N 250 
MET CA  C    sing N N 251 
MET CA  CB   sing N N 252 
MET CA  HA   sing N N 253 
MET C   O    doub N N 254 
MET C   OXT  sing N N 255 
MET CB  CG   sing N N 256 
MET CB  HB2  sing N N 257 
MET CB  HB3  sing N N 258 
MET CG  SD   sing N N 259 
MET CG  HG2  sing N N 260 
MET CG  HG3  sing N N 261 
MET SD  CE   sing N N 262 
MET CE  HE1  sing N N 263 
MET CE  HE2  sing N N 264 
MET CE  HE3  sing N N 265 
MET OXT HXT  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9M7M 
_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]   0.019372 
_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]   0.016369 
_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]   0.014652 
_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  
CL 
H  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA A 1 1   ? 6.194  20.706 -2.817  1.00 53.71 ? 3   ALA A N    1 
ATOM   2    C  CA   . ALA A 1 1   ? 5.218  19.754 -2.290  1.00 50.05 ? 3   ALA A CA   1 
ATOM   3    C  C    . ALA A 1 1   ? 4.805  20.154 -0.867  1.00 50.24 ? 3   ALA A C    1 
ATOM   4    O  O    . ALA A 1 1   ? 5.666  20.252 0.022   1.00 47.92 ? 3   ALA A O    1 
ATOM   5    C  CB   . ALA A 1 1   ? 5.790  18.340 -2.300  1.00 43.54 ? 3   ALA A CB   1 
ATOM   6    H  HA   . ALA A 1 1   ? 4.426  19.765 -2.850  1.00 41.33 ? 3   ALA A HA   1 
ATOM   7    H  HB1  . ALA A 1 1   ? 5.125  17.729 -1.947  1.00 35.08 ? 3   ALA A HB1  1 
ATOM   8    H  HB2  . ALA A 1 1   ? 6.012  18.097 -3.212  1.00 35.08 ? 3   ALA A HB2  1 
ATOM   9    H  HB3  . ALA A 1 1   ? 6.587  18.319 -1.748  1.00 35.08 ? 3   ALA A HB3  1 
ATOM   10   N  N    . PRO A 1 2   ? 3.493  20.380 -0.637  1.00 41.08 ? 4   PRO A N    1 
ATOM   11   C  CA   . PRO A 1 2   ? 3.020  20.796 0.687   1.00 38.96 ? 4   PRO A CA   1 
ATOM   12   C  C    . PRO A 1 2   ? 3.383  19.771 1.769   1.00 33.42 ? 4   PRO A C    1 
ATOM   13   O  O    . PRO A 1 2   ? 3.550  18.589 1.478   1.00 31.86 ? 4   PRO A O    1 
ATOM   14   C  CB   . PRO A 1 2   ? 1.496  20.860 0.505   1.00 34.87 ? 4   PRO A CB   1 
ATOM   15   C  CG   . PRO A 1 2   ? 1.278  21.013 -0.933  1.00 42.30 ? 4   PRO A CG   1 
ATOM   16   C  CD   . PRO A 1 2   ? 2.378  20.253 -1.586  1.00 40.08 ? 4   PRO A CD   1 
ATOM   17   H  HA   . PRO A 1 2   ? 3.365  21.671 0.924   1.00 34.84 ? 4   PRO A HA   1 
ATOM   18   H  HB2  . PRO A 1 2   ? 1.095  20.037 0.825   1.00 29.92 ? 4   PRO A HB2  1 
ATOM   19   H  HB3  . PRO A 1 2   ? 1.143  21.623 0.987   1.00 29.92 ? 4   PRO A HB3  1 
ATOM   20   H  HG2  . PRO A 1 2   ? 0.415  20.640 -1.174  1.00 37.40 ? 4   PRO A HG2  1 
ATOM   21   H  HG3  . PRO A 1 2   ? 1.324  21.952 -1.172  1.00 37.40 ? 4   PRO A HG3  1 
ATOM   22   H  HD2  . PRO A 1 2   ? 2.128  19.321 -1.692  1.00 35.90 ? 4   PRO A HD2  1 
ATOM   23   H  HD3  . PRO A 1 2   ? 2.610  20.658 -2.437  1.00 35.90 ? 4   PRO A HD3  1 
ATOM   24   N  N    . PRO A 1 3   ? 3.491  20.213 3.020   1.00 28.20 ? 5   PRO A N    1 
ATOM   25   C  CA   . PRO A 1 3   ? 3.893  19.283 4.069   1.00 25.74 ? 5   PRO A CA   1 
ATOM   26   C  C    . PRO A 1 3   ? 2.763  18.320 4.373   1.00 25.11 ? 5   PRO A C    1 
ATOM   27   O  O    . PRO A 1 3   ? 1.611  18.744 4.464   1.00 25.09 ? 5   PRO A O    1 
ATOM   28   C  CB   . PRO A 1 3   ? 4.194  20.217 5.244   1.00 26.14 ? 5   PRO A CB   1 
ATOM   29   C  CG   . PRO A 1 3   ? 3.386  21.418 4.982   1.00 32.38 ? 5   PRO A CG   1 
ATOM   30   C  CD   . PRO A 1 3   ? 3.353  21.586 3.517   1.00 28.16 ? 5   PRO A CD   1 
ATOM   31   H  HA   . PRO A 1 3   ? 4.692  18.794 3.816   1.00 24.13 ? 5   PRO A HA   1 
ATOM   32   H  HB2  . PRO A 1 3   ? 3.924  19.795 6.075   1.00 24.44 ? 5   PRO A HB2  1 
ATOM   33   H  HB3  . PRO A 1 3   ? 5.139  20.433 5.258   1.00 24.44 ? 5   PRO A HB3  1 
ATOM   34   H  HG2  . PRO A 1 3   ? 2.490  21.287 5.329   1.00 30.21 ? 5   PRO A HG2  1 
ATOM   35   H  HG3  . PRO A 1 3   ? 3.804  22.186 5.402   1.00 30.21 ? 5   PRO A HG3  1 
ATOM   36   H  HD2  . PRO A 1 3   ? 2.504  21.963 3.239   1.00 26.24 ? 5   PRO A HD2  1 
ATOM   37   H  HD3  . PRO A 1 3   ? 4.100  22.130 3.222   1.00 26.24 ? 5   PRO A HD3  1 
ATOM   38   N  N    . GLN A 1 4   ? 3.090  17.052 4.506   1.00 21.79 ? 6   GLN A N    1 
ATOM   39   C  CA   . GLN A 1 4   ? 2.144  15.989 4.817   1.00 22.70 ? 6   GLN A CA   1 
ATOM   40   C  C    . GLN A 1 4   ? 2.396  15.469 6.232   1.00 24.69 ? 6   GLN A C    1 
ATOM   41   O  O    . GLN A 1 4   ? 3.530  15.553 6.734   1.00 18.68 ? 6   GLN A O    1 
ATOM   42   C  CB   . GLN A 1 4   ? 2.306  14.856 3.825   1.00 21.84 ? 6   GLN A CB   1 
ATOM   43   C  CG   . GLN A 1 4   ? 2.273  15.363 2.393   1.00 25.74 ? 6   GLN A CG   1 
ATOM   44   C  CD   . GLN A 1 4   ? 2.475  14.274 1.371   1.00 32.90 ? 6   GLN A CD   1 
ATOM   45   O  OE1  . GLN A 1 4   ? 2.218  13.099 1.629   1.00 38.00 ? 6   GLN A OE1  1 
ATOM   46   N  NE2  . GLN A 1 4   ? 2.951  14.663 0.194   1.00 35.17 ? 6   GLN A NE2  1 
ATOM   47   H  H    . GLN A 1 4   ? 3.895  16.764 4.417   1.00 20.03 ? 6   GLN A H    1 
ATOM   48   H  HA   . GLN A 1 4   ? 1.237  16.327 4.762   1.00 20.22 ? 6   GLN A HA   1 
ATOM   49   H  HB2  . GLN A 1 4   ? 3.160  14.420 3.973   1.00 19.53 ? 6   GLN A HB2  1 
ATOM   50   H  HB3  . GLN A 1 4   ? 1.580  14.223 3.940   1.00 19.53 ? 6   GLN A HB3  1 
ATOM   51   H  HG2  . GLN A 1 4   ? 1.411  15.774 2.225   1.00 23.77 ? 6   GLN A HG2  1 
ATOM   52   H  HG3  . GLN A 1 4   ? 2.980  16.017 2.275   1.00 23.77 ? 6   GLN A HG3  1 
ATOM   53   H  HE21 . GLN A 1 4   ? 3.124  15.494 0.054   1.00 33.83 ? 6   GLN A HE21 1 
ATOM   54   H  HE22 . GLN A 1 4   ? 3.086  14.085 -0.428  1.00 33.83 ? 6   GLN A HE22 1 
ATOM   55   N  N    . PRO A 1 5   ? 1.347  14.938 6.895   1.00 20.21 ? 7   PRO A N    1 
ATOM   56   C  CA   . PRO A 1 5   ? 1.506  14.477 8.264   1.00 20.64 ? 7   PRO A CA   1 
ATOM   57   C  C    . PRO A 1 5   ? 2.521  13.330 8.400   1.00 18.00 ? 7   PRO A C    1 
ATOM   58   O  O    . PRO A 1 5   ? 2.705  12.502 7.512   1.00 19.98 ? 7   PRO A O    1 
ATOM   59   C  CB   . PRO A 1 5   ? 0.077  14.044 8.651   1.00 22.17 ? 7   PRO A CB   1 
ATOM   60   C  CG   . PRO A 1 5   ? -0.781 14.881 7.810   1.00 24.15 ? 7   PRO A CG   1 
ATOM   61   C  CD   . PRO A 1 5   ? -0.086 14.933 6.500   1.00 20.67 ? 7   PRO A CD   1 
ATOM   62   H  HA   . PRO A 1 5   ? 1.780  15.213 8.834   1.00 17.66 ? 7   PRO A HA   1 
ATOM   63   H  HB2  . PRO A 1 5   ? -0.050 13.104 8.448   1.00 18.01 ? 7   PRO A HB2  1 
ATOM   64   H  HB3  . PRO A 1 5   ? -0.080 14.221 9.592   1.00 18.01 ? 7   PRO A HB3  1 
ATOM   65   H  HG2  . PRO A 1 5   ? -1.655 14.471 7.720   1.00 19.79 ? 7   PRO A HG2  1 
ATOM   66   H  HG3  . PRO A 1 5   ? -0.854 15.768 8.196   1.00 19.79 ? 7   PRO A HG3  1 
ATOM   67   H  HD2  . PRO A 1 5   ? -0.291 14.144 5.975   1.00 17.21 ? 7   PRO A HD2  1 
ATOM   68   H  HD3  . PRO A 1 5   ? -0.311 15.748 6.026   1.00 17.21 ? 7   PRO A HD3  1 
ATOM   69   N  N    . VAL A 1 6   ? 3.165  13.308 9.569   1.00 19.41 ? 8   VAL A N    1 
ATOM   70   C  CA   . VAL A 1 6   ? 4.141  12.298 9.910   1.00 19.46 ? 8   VAL A CA   1 
ATOM   71   C  C    . VAL A 1 6   ? 3.856  11.691 11.264  1.00 21.02 ? 8   VAL A C    1 
ATOM   72   O  O    . VAL A 1 6   ? 3.112  12.268 12.060  1.00 21.59 ? 8   VAL A O    1 
ATOM   73   C  CB   . VAL A 1 6   ? 5.548  12.915 9.912   1.00 16.49 ? 8   VAL A CB   1 
ATOM   74   C  CG1  . VAL A 1 6   ? 5.804  13.536 8.549   1.00 17.94 ? 8   VAL A CG1  1 
ATOM   75   C  CG2  . VAL A 1 6   ? 5.655  13.954 10.988  1.00 18.30 ? 8   VAL A CG2  1 
ATOM   76   H  H    . VAL A 1 6   ? 3.042  13.888 10.192  1.00 15.92 ? 8   VAL A H    1 
ATOM   77   H  HA   . VAL A 1 6   ? 4.117  11.591 9.247   1.00 16.22 ? 8   VAL A HA   1 
ATOM   78   H  HB   . VAL A 1 6   ? 6.211  12.225 10.073  1.00 14.21 ? 8   VAL A HB   1 
ATOM   79   H  HG11 . VAL A 1 6   ? 6.692  13.927 8.543   1.00 16.31 ? 8   VAL A HG11 1 
ATOM   80   H  HG12 . VAL A 1 6   ? 5.742  12.845 7.871   1.00 16.31 ? 8   VAL A HG12 1 
ATOM   81   H  HG13 . VAL A 1 6   ? 5.138  14.221 8.385   1.00 16.31 ? 8   VAL A HG13 1 
ATOM   82   H  HG21 . VAL A 1 6   ? 6.549  14.332 10.974  1.00 15.96 ? 8   VAL A HG21 1 
ATOM   83   H  HG22 . VAL A 1 6   ? 4.999  14.649 10.822  1.00 15.96 ? 8   VAL A HG22 1 
ATOM   84   H  HG23 . VAL A 1 6   ? 5.486  13.537 11.847  1.00 15.96 ? 8   VAL A HG23 1 
ATOM   85   N  N    . THR A 1 7   ? 4.440  10.525 11.519  1.00 18.90 ? 9   THR A N    1 
ATOM   86   C  CA   . THR A 1 7   ? 4.275  9.871  12.818  1.00 22.09 ? 9   THR A CA   1 
ATOM   87   C  C    . THR A 1 7   ? 5.570  9.620  13.606  1.00 20.81 ? 9   THR A C    1 
ATOM   88   O  O    . THR A 1 7   ? 5.542  9.417  14.823  1.00 22.37 ? 9   THR A O    1 
ATOM   89   C  CB   . THR A 1 7   ? 3.594  8.547  12.625  1.00 20.96 ? 9   THR A CB   1 
ATOM   90   O  OG1  . THR A 1 7   ? 4.296  7.786  11.648  1.00 23.74 ? 9   THR A OG1  1 
ATOM   91   C  CG2  . THR A 1 7   ? 2.154  8.783  12.142  1.00 25.35 ? 9   THR A CG2  1 
ATOM   92   H  H    . THR A 1 7   ? 4.934  10.092 10.964  1.00 16.33 ? 9   THR A H    1 
ATOM   93   H  HA   . THR A 1 7   ? 3.698  10.422 13.369  1.00 18.74 ? 9   THR A HA   1 
ATOM   94   H  HB   . THR A 1 7   ? 3.569  8.063  13.465  1.00 16.78 ? 9   THR A HB   1 
ATOM   95   H  HG1  . THR A 1 7   ? 5.087  7.655  11.899  1.00 20.06 ? 9   THR A HG1  1 
ATOM   96   H  HG21 . THR A 1 7   ? 1.704  7.933  12.014  1.00 20.49 ? 9   THR A HG21 1 
ATOM   97   H  HG22 . THR A 1 7   ? 1.665  9.302  12.799  1.00 20.49 ? 9   THR A HG22 1 
ATOM   98   H  HG23 . THR A 1 7   ? 2.161  9.265  11.301  1.00 20.49 ? 9   THR A HG23 1 
ATOM   99   N  N    . HIS A 1 8   ? 6.697  9.629  12.907  1.00 20.08 ? 10  HIS A N    1 
ATOM   100  C  CA   . HIS A 1 8   ? 8.008  9.360  13.509  1.00 17.89 ? 10  HIS A CA   1 
ATOM   101  C  C    . HIS A 1 8   ? 9.016  10.415 13.059  1.00 16.57 ? 10  HIS A C    1 
ATOM   102  O  O    . HIS A 1 8   ? 9.052  10.796 11.903  1.00 14.55 ? 10  HIS A O    1 
ATOM   103  C  CB   . HIS A 1 8   ? 8.478  7.994  13.087  1.00 19.48 ? 10  HIS A CB   1 
ATOM   104  C  CG   . HIS A 1 8   ? 7.656  6.871  13.612  1.00 22.91 ? 10  HIS A CG   1 
ATOM   105  N  ND1  . HIS A 1 8   ? 6.352  6.645  13.228  1.00 22.85 ? 10  HIS A ND1  1 
ATOM   106  C  CD2  . HIS A 1 8   ? 7.991  5.869  14.446  1.00 23.37 ? 10  HIS A CD2  1 
ATOM   107  C  CE1  . HIS A 1 8   ? 5.906  5.568  13.850  1.00 25.94 ? 10  HIS A CE1  1 
ATOM   108  N  NE2  . HIS A 1 8   ? 6.880  5.074  14.589  1.00 26.82 ? 10  HIS A NE2  1 
ATOM   109  H  H    . HIS A 1 8   ? 6.735  9.791  12.063  1.00 17.40 ? 10  HIS A H    1 
ATOM   110  H  HA   . HIS A 1 8   ? 7.938  9.383  14.476  1.00 15.60 ? 10  HIS A HA   1 
ATOM   111  H  HB2  . HIS A 1 8   ? 8.460  7.945  12.119  1.00 17.05 ? 10  HIS A HB2  1 
ATOM   112  H  HB3  . HIS A 1 8   ? 9.386  7.868  13.404  1.00 17.05 ? 10  HIS A HB3  1 
ATOM   113  H  HD2  . HIS A 1 8   ? 8.813  5.750  14.864  1.00 19.28 ? 10  HIS A HD2  1 
ATOM   114  H  HE1  . HIS A 1 8   ? 5.052  5.209  13.768  1.00 20.78 ? 10  HIS A HE1  1 
ATOM   115  H  HE2  . HIS A 1 8   ? 6.828  4.371  15.081  1.00 21.68 ? 10  HIS A HE2  1 
ATOM   116  N  N    . LEU A 1 9   ? 9.840  10.885 13.994  1.00 15.91 ? 11  LEU A N    1 
ATOM   117  C  CA   . LEU A 1 9   ? 10.843 11.913 13.730  1.00 13.05 ? 11  LEU A CA   1 
ATOM   118  C  C    . LEU A 1 9   ? 12.252 11.353 13.875  1.00 14.40 ? 11  LEU A C    1 
ATOM   119  O  O    . LEU A 1 9   ? 12.531 10.513 14.753  1.00 14.74 ? 11  LEU A O    1 
ATOM   120  C  CB   . LEU A 1 9   ? 10.588 13.135 14.602  1.00 13.93 ? 11  LEU A CB   1 
ATOM   121  C  CG   . LEU A 1 9   ? 9.522  14.121 14.090  1.00 16.73 ? 11  LEU A CG   1 
ATOM   122  C  CD1  . LEU A 1 9   ? 8.176  13.484 13.956  1.00 20.40 ? 11  LEU A CD1  1 
ATOM   123  C  CD2  . LEU A 1 9   ? 9.426  15.301 14.965  1.00 16.61 ? 11  LEU A CD2  1 
ATOM   124  H  H    . LEU A 1 9   ? 9.836  10.616 14.811  1.00 13.46 ? 11  LEU A H    1 
ATOM   125  H  HA   . LEU A 1 9   ? 10.745 12.197 12.808  1.00 11.43 ? 11  LEU A HA   1 
ATOM   126  H  HB2  . LEU A 1 9   ? 10.302 12.830 15.478  1.00 12.22 ? 11  LEU A HB2  1 
ATOM   127  H  HB3  . LEU A 1 9   ? 11.419 13.627 14.688  1.00 12.22 ? 11  LEU A HB3  1 
ATOM   128  H  HG   . LEU A 1 9   ? 9.787  14.431 13.209  1.00 14.91 ? 11  LEU A HG   1 
ATOM   129  H  HD11 . LEU A 1 9   ? 7.544  14.145 13.632  1.00 17.83 ? 11  LEU A HD11 1 
ATOM   130  H  HD12 . LEU A 1 9   ? 8.236  12.747 13.328  1.00 17.83 ? 11  LEU A HD12 1 
ATOM   131  H  HD13 . LEU A 1 9   ? 7.895  13.156 14.825  1.00 17.83 ? 11  LEU A HD13 1 
ATOM   132  H  HD21 . LEU A 1 9   ? 8.748  15.900 14.614  1.00 14.65 ? 11  LEU A HD21 1 
ATOM   133  H  HD22 . LEU A 1 9   ? 9.183  15.012 15.858  1.00 14.65 ? 11  LEU A HD22 1 
ATOM   134  H  HD23 . LEU A 1 9   ? 10.286 15.750 14.985  1.00 14.65 ? 11  LEU A HD23 1 
ATOM   135  N  N    . ILE A 1 10  ? 13.135 11.806 13.003  1.00 12.16 ? 12  ILE A N    1 
ATOM   136  C  CA   . ILE A 1 10  ? 14.526 11.395 13.028  1.00 10.66 ? 12  ILE A CA   1 
ATOM   137  C  C    . ILE A 1 10  ? 15.393 12.660 13.048  1.00 12.05 ? 12  ILE A C    1 
ATOM   138  O  O    . ILE A 1 10  ? 15.241 13.511 12.154  1.00 9.81  ? 12  ILE A O    1 
ATOM   139  C  CB   . ILE A 1 10  ? 14.814 10.561 11.784  1.00 13.05 ? 12  ILE A CB   1 
ATOM   140  C  CG1  . ILE A 1 10  ? 14.074 9.230  11.845  1.00 15.00 ? 12  ILE A CG1  1 
ATOM   141  C  CG2  . ILE A 1 10  ? 16.276 10.250 11.671  1.00 14.87 ? 12  ILE A CG2  1 
ATOM   142  C  CD1  . ILE A 1 10  ? 14.087 8.478  10.546  1.00 16.45 ? 12  ILE A CD1  1 
ATOM   143  H  H    . ILE A 1 10  ? 12.949 12.364 12.374  1.00 10.60 ? 12  ILE A H    1 
ATOM   144  H  HA   . ILE A 1 10  ? 14.708 10.866 13.820  1.00 9.44  ? 12  ILE A HA   1 
ATOM   145  H  HB   . ILE A 1 10  ? 14.529 11.051 10.996  1.00 11.98 ? 12  ILE A HB   1 
ATOM   146  H  HG12 . ILE A 1 10  ? 14.491 8.669  12.518  1.00 13.25 ? 12  ILE A HG12 1 
ATOM   147  H  HG13 . ILE A 1 10  ? 13.148 9.396  12.083  1.00 13.25 ? 12  ILE A HG13 1 
ATOM   148  H  HG21 . ILE A 1 10  ? 16.425 9.720  10.873  1.00 14.10 ? 12  ILE A HG21 1 
ATOM   149  H  HG22 . ILE A 1 10  ? 16.772 11.081 11.615  1.00 14.10 ? 12  ILE A HG22 1 
ATOM   150  H  HG23 . ILE A 1 10  ? 16.553 9.751  12.456  1.00 14.10 ? 12  ILE A HG23 1 
ATOM   151  H  HD11 . ILE A 1 10  ? 13.601 7.646  10.658  1.00 14.73 ? 12  ILE A HD11 1 
ATOM   152  H  HD12 . ILE A 1 10  ? 13.662 9.020  9.863   1.00 14.73 ? 12  ILE A HD12 1 
ATOM   153  H  HD13 . ILE A 1 10  ? 15.006 8.293  10.298  1.00 14.73 ? 12  ILE A HD13 1 
ATOM   154  N  N    . PHE A 1 11  ? 16.310 12.812 14.011  1.00 9.96  ? 13  PHE A N    1 
ATOM   155  C  CA   . PHE A 1 11  ? 17.113 14.044 14.161  1.00 9.34  ? 13  PHE A CA   1 
ATOM   156  C  C    . PHE A 1 11  ? 18.560 13.760 13.863  1.00 7.94  ? 13  PHE A C    1 
ATOM   157  O  O    . PHE A 1 11  ? 19.116 12.772 14.351  1.00 10.12 ? 13  PHE A O    1 
ATOM   158  C  CB   . PHE A 1 11  ? 16.999 14.533 15.616  1.00 10.91 ? 13  PHE A CB   1 
ATOM   159  C  CG   . PHE A 1 11  ? 15.693 15.124 15.965  1.00 11.57 ? 13  PHE A CG   1 
ATOM   160  C  CD1  . PHE A 1 11  ? 14.674 14.334 16.450  1.00 12.56 ? 13  PHE A CD1  1 
ATOM   161  C  CD2  . PHE A 1 11  ? 15.475 16.476 15.796  1.00 10.85 ? 13  PHE A CD2  1 
ATOM   162  C  CE1  . PHE A 1 11  ? 13.449 14.883 16.737  1.00 12.82 ? 13  PHE A CE1  1 
ATOM   163  C  CE2  . PHE A 1 11  ? 14.251 17.039 16.083  1.00 12.85 ? 13  PHE A CE2  1 
ATOM   164  C  CZ   . PHE A 1 11  ? 13.214 16.222 16.555  1.00 13.93 ? 13  PHE A CZ   1 
ATOM   165  H  H    . PHE A 1 11  ? 16.491 12.211 14.599  1.00 9.33  ? 13  PHE A H    1 
ATOM   166  H  HA   . PHE A 1 11  ? 16.789 14.735 13.562  1.00 9.14  ? 13  PHE A HA   1 
ATOM   167  H  HB2  . PHE A 1 11  ? 17.149 13.780 16.208  1.00 10.38 ? 13  PHE A HB2  1 
ATOM   168  H  HB3  . PHE A 1 11  ? 17.678 15.209 15.769  1.00 10.38 ? 13  PHE A HB3  1 
ATOM   169  H  HD1  . PHE A 1 11  ? 14.808 13.420 16.559  1.00 11.05 ? 13  PHE A HD1  1 
ATOM   170  H  HD2  . PHE A 1 11  ? 16.159 17.011 15.461  1.00 10.14 ? 13  PHE A HD2  1 
ATOM   171  H  HE1  . PHE A 1 11  ? 12.768 14.339 17.061  1.00 10.88 ? 13  PHE A HE1  1 
ATOM   172  H  HE2  . PHE A 1 11  ? 14.113 17.951 15.962  1.00 11.71 ? 13  PHE A HE2  1 
ATOM   173  H  HZ   . PHE A 1 11  ? 12.388 16.589 16.774  1.00 12.17 ? 13  PHE A HZ   1 
ATOM   174  N  N    . ASP A 1 12  ? 19.165 14.616 13.076  1.00 9.30  ? 14  ASP A N    1 
ATOM   175  C  CA   . ASP A 1 12  ? 20.618 14.741 13.048  1.00 7.72  ? 14  ASP A CA   1 
ATOM   176  C  C    . ASP A 1 12  ? 21.104 15.255 14.400  1.00 10.17 ? 14  ASP A C    1 
ATOM   177  O  O    . ASP A 1 12  ? 20.342 15.862 15.140  1.00 10.69 ? 14  ASP A O    1 
ATOM   178  C  CB   . ASP A 1 12  ? 20.994 15.723 11.951  1.00 9.03  ? 14  ASP A CB   1 
ATOM   179  C  CG   . ASP A 1 12  ? 22.482 15.924 11.844  1.00 8.58  ? 14  ASP A CG   1 
ATOM   180  O  OD1  . ASP A 1 12  ? 23.206 14.897 11.791  1.00 10.51 ? 14  ASP A OD1  1 
ATOM   181  O  OD2  . ASP A 1 12  ? 22.920 17.108 11.805  1.00 10.88 ? 14  ASP A OD2  1 
ATOM   182  H  H    . ASP A 1 12  ? 18.759 15.148 12.536  1.00 9.03  ? 14  ASP A H    1 
ATOM   183  H  HA   . ASP A 1 12  ? 21.028 13.881 12.864  1.00 7.68  ? 14  ASP A HA   1 
ATOM   184  H  HB2  . ASP A 1 12  ? 20.674 15.384 11.100  1.00 9.38  ? 14  ASP A HB2  1 
ATOM   185  H  HB3  . ASP A 1 12  ? 20.586 16.582 12.141  1.00 9.38  ? 14  ASP A HB3  1 
ATOM   186  N  N    . MET A 1 13  ? 22.386 15.117 14.691  1.00 8.26  ? 15  MET A N    1 
ATOM   187  C  CA   . MET A 1 13  ? 22.958 15.670 15.903  1.00 8.06  ? 15  MET A CA   1 
ATOM   188  C  C    . MET A 1 13  ? 23.788 16.918 15.634  1.00 7.42  ? 15  MET A C    1 
ATOM   189  O  O    . MET A 1 13  ? 23.462 18.026 16.078  1.00 8.46  ? 15  MET A O    1 
ATOM   190  C  CB   . MET A 1 13  ? 23.836 14.641 16.584  1.00 9.74  ? 15  MET A CB   1 
ATOM   191  C  CG   . MET A 1 13  ? 24.376 15.138 17.920  1.00 9.49  ? 15  MET A CG   1 
ATOM   192  S  SD   . MET A 1 13  ? 25.380 13.863 18.810  1.00 14.44 ? 15  MET A SD   1 
ATOM   193  C  CE   . MET A 1 13  ? 26.712 13.637 17.662  1.00 17.45 ? 15  MET A CE   1 
ATOM   194  H  H    . MET A 1 13  ? 22.953 14.701 14.196  1.00 8.68  ? 15  MET A H    1 
ATOM   195  H  HA   . MET A 1 13  ? 22.238 15.898 16.512  1.00 8.35  ? 15  MET A HA   1 
ATOM   196  H  HB2  . MET A 1 13  ? 23.317 13.838 16.748  1.00 9.76  ? 15  MET A HB2  1 
ATOM   197  H  HB3  . MET A 1 13  ? 24.592 14.439 16.010  1.00 9.76  ? 15  MET A HB3  1 
ATOM   198  H  HG2  . MET A 1 13  ? 24.942 15.910 17.764  1.00 9.31  ? 15  MET A HG2  1 
ATOM   199  H  HG3  . MET A 1 13  ? 23.630 15.383 18.490  1.00 9.31  ? 15  MET A HG3  1 
ATOM   200  H  HE1  . MET A 1 13  ? 27.326 12.976 18.017  1.00 17.06 ? 15  MET A HE1  1 
ATOM   201  H  HE2  . MET A 1 13  ? 26.350 13.331 16.815  1.00 17.06 ? 15  MET A HE2  1 
ATOM   202  H  HE3  . MET A 1 13  ? 27.170 14.483 17.540  1.00 17.06 ? 15  MET A HE3  1 
ATOM   203  N  N    . ASP A 1 14  ? 24.930 16.791 14.953  1.00 7.53  ? 16  ASP A N    1 
ATOM   204  C  CA   . ASP A 1 14  ? 25.860 17.876 14.826  1.00 9.77  ? 16  ASP A CA   1 
ATOM   205  C  C    . ASP A 1 14  ? 25.315 19.010 14.026  1.00 7.76  ? 16  ASP A C    1 
ATOM   206  O  O    . ASP A 1 14  ? 24.908 18.858 12.887  1.00 7.95  ? 16  ASP A O    1 
ATOM   207  C  CB   . ASP A 1 14  ? 27.192 17.376 14.257  1.00 10.65 ? 16  ASP A CB   1 
ATOM   208  C  CG   . ASP A 1 14  ? 27.882 16.426 15.146  1.00 14.76 ? 16  ASP A CG   1 
ATOM   209  O  OD1  . ASP A 1 14  ? 28.126 16.775 16.290  1.00 12.97 ? 16  ASP A OD1  1 
ATOM   210  O  OD2  . ASP A 1 14  ? 28.107 15.308 14.690  1.00 17.25 ? 16  ASP A OD2  1 
ATOM   211  H  H    . ASP A 1 14  ? 25.178 16.070 14.554  1.00 7.77  ? 16  ASP A H    1 
ATOM   212  H  HA   . ASP A 1 14  ? 26.042 18.219 15.715  1.00 10.12 ? 16  ASP A HA   1 
ATOM   213  H  HB2  . ASP A 1 14  ? 27.025 16.928 13.413  1.00 10.98 ? 16  ASP A HB2  1 
ATOM   214  H  HB3  . ASP A 1 14  ? 27.779 18.135 14.118  1.00 10.98 ? 16  ASP A HB3  1 
ATOM   215  N  N    . GLY A 1 15  ? 25.346 20.206 14.603  1.00 8.73  ? 17  GLY A N    1 
ATOM   216  C  CA   . GLY A 1 15  ? 24.889 21.412 13.952  1.00 8.75  ? 17  GLY A CA   1 
ATOM   217  C  C    . GLY A 1 15  ? 23.408 21.613 13.995  1.00 9.27  ? 17  GLY A C    1 
ATOM   218  O  O    . GLY A 1 15  ? 22.902 22.655 13.519  1.00 12.11 ? 17  GLY A O    1 
ATOM   219  H  H    . GLY A 1 15  ? 25.640 20.341 15.400  1.00 9.14  ? 17  GLY A H    1 
ATOM   220  H  HA2  . GLY A 1 15  ? 25.309 22.178 14.373  1.00 9.22  ? 17  GLY A HA2  1 
ATOM   221  H  HA3  . GLY A 1 15  ? 25.162 21.392 13.021  1.00 9.22  ? 17  GLY A HA3  1 
ATOM   222  N  N    . LEU A 1 16  ? 22.690 20.580 14.448  1.00 10.09 ? 18  LEU A N    1 
ATOM   223  C  CA   . LEU A 1 16  ? 21.209 20.568 14.433  1.00 8.57  ? 18  LEU A CA   1 
ATOM   224  C  C    . LEU A 1 16  ? 20.739 20.566 15.901  1.00 10.08 ? 18  LEU A C    1 
ATOM   225  O  O    . LEU A 1 16  ? 19.969 21.444 16.298  1.00 10.74 ? 18  LEU A O    1 
ATOM   226  C  CB   . LEU A 1 16  ? 20.660 19.434 13.523  1.00 8.95  ? 18  LEU A CB   1 
ATOM   227  C  CG   . LEU A 1 16  ? 19.153 19.428 13.243  1.00 8.42  ? 18  LEU A CG   1 
ATOM   228  C  CD1  . LEU A 1 16  ? 18.347 19.017 14.469  1.00 12.24 ? 18  LEU A CD1  1 
ATOM   229  C  CD2  . LEU A 1 16  ? 18.642 20.749 12.675  1.00 9.70  ? 18  LEU A CD2  1 
ATOM   230  H  H    . LEU A 1 16  ? 23.036 19.863 14.774  1.00 10.49 ? 18  LEU A H    1 
ATOM   231  H  HA   . LEU A 1 16  ? 20.909 21.405 14.046  1.00 8.84  ? 18  LEU A HA   1 
ATOM   232  H  HB2  . LEU A 1 16  ? 21.108 19.493 12.665  1.00 9.34  ? 18  LEU A HB2  1 
ATOM   233  H  HB3  . LEU A 1 16  ? 20.876 18.584 13.937  1.00 9.34  ? 18  LEU A HB3  1 
ATOM   234  H  HG   . LEU A 1 16  ? 18.985 18.754 12.565  1.00 8.65  ? 18  LEU A HG   1 
ATOM   235  H  HD11 . LEU A 1 16  ? 17.404 19.028 14.244  1.00 12.04 ? 18  LEU A HD11 1 
ATOM   236  H  HD12 . LEU A 1 16  ? 18.614 18.124 14.737  1.00 12.04 ? 18  LEU A HD12 1 
ATOM   237  H  HD13 . LEU A 1 16  ? 18.524 19.645 15.187  1.00 12.04 ? 18  LEU A HD13 1 
ATOM   238  H  HD21 . LEU A 1 16  ? 17.687 20.679 12.522  1.00 9.94  ? 18  LEU A HD21 1 
ATOM   239  H  HD22 . LEU A 1 16  ? 18.824 21.458 13.312  1.00 9.94  ? 18  LEU A HD22 1 
ATOM   240  H  HD23 . LEU A 1 16  ? 19.100 20.931 11.839  1.00 9.94  ? 18  LEU A HD23 1 
ATOM   241  N  N    . LEU A 1 17  ? 21.111 19.570 16.664  1.00 9.40  ? 19  LEU A N    1 
ATOM   242  C  CA   . LEU A 1 17  ? 20.813 19.544 18.092  1.00 10.65 ? 19  LEU A CA   1 
ATOM   243  C  C    . LEU A 1 17  ? 21.931 20.106 18.923  1.00 10.20 ? 19  LEU A C    1 
ATOM   244  O  O    . LEU A 1 17  ? 21.644 20.680 20.006  1.00 11.67 ? 19  LEU A O    1 
ATOM   245  C  CB   . LEU A 1 17  ? 20.515 18.112 18.543  1.00 11.67 ? 19  LEU A CB   1 
ATOM   246  C  CG   . LEU A 1 17  ? 19.290 17.508 17.913  1.00 12.84 ? 19  LEU A CG   1 
ATOM   247  C  CD1  . LEU A 1 17  ? 19.114 16.069 18.443  1.00 15.95 ? 19  LEU A CD1  1 
ATOM   248  C  CD2  . LEU A 1 17  ? 18.027 18.287 18.237  1.00 12.88 ? 19  LEU A CD2  1 
ATOM   249  H  H    . LEU A 1 17  ? 21.544 18.882 16.384  1.00 9.42  ? 19  LEU A H    1 
ATOM   250  H  HA   . LEU A 1 17  ? 20.021 20.080 18.257  1.00 10.24 ? 19  LEU A HA   1 
ATOM   251  H  HB2  . LEU A 1 17  ? 21.272 17.550 18.315  1.00 11.02 ? 19  LEU A HB2  1 
ATOM   252  H  HB3  . LEU A 1 17  ? 20.384 18.110 19.504  1.00 11.02 ? 19  LEU A HB3  1 
ATOM   253  H  HG   . LEU A 1 17  ? 19.399 17.475 16.950  1.00 12.10 ? 19  LEU A HG   1 
ATOM   254  H  HD11 . LEU A 1 17  ? 18.324 15.678 18.037  1.00 14.85 ? 19  LEU A HD11 1 
ATOM   255  H  HD12 . LEU A 1 17  ? 19.898 15.548 18.208  1.00 14.85 ? 19  LEU A HD12 1 
ATOM   256  H  HD13 . LEU A 1 17  ? 19.011 16.097 19.407  1.00 14.85 ? 19  LEU A HD13 1 
ATOM   257  H  HD21 . LEU A 1 17  ? 17.272 17.855 17.807  1.00 11.80 ? 19  LEU A HD21 1 
ATOM   258  H  HD22 . LEU A 1 17  ? 17.900 18.297 19.199  1.00 11.80 ? 19  LEU A HD22 1 
ATOM   259  H  HD23 . LEU A 1 17  ? 18.122 19.194 17.906  1.00 11.80 ? 19  LEU A HD23 1 
ATOM   260  N  N    . LEU A 1 18  ? 23.171 19.939 18.520  1.00 10.90 ? 20  LEU A N    1 
ATOM   261  C  CA   . LEU A 1 18  ? 24.325 20.499 19.252  1.00 11.48 ? 20  LEU A CA   1 
ATOM   262  C  C    . LEU A 1 18  ? 25.136 21.464 18.386  1.00 9.14  ? 20  LEU A C    1 
ATOM   263  O  O    . LEU A 1 18  ? 25.254 21.253 17.169  1.00 9.62  ? 20  LEU A O    1 
ATOM   264  C  CB   . LEU A 1 18  ? 25.252 19.360 19.610  1.00 11.81 ? 20  LEU A CB   1 
ATOM   265  C  CG   . LEU A 1 18  ? 24.756 18.324 20.631  1.00 12.74 ? 20  LEU A CG   1 
ATOM   266  C  CD1  . LEU A 1 18  ? 25.820 17.249 20.845  1.00 13.72 ? 20  LEU A CD1  1 
ATOM   267  C  CD2  . LEU A 1 18  ? 24.393 18.913 21.968  1.00 14.36 ? 20  LEU A CD2  1 
ATOM   268  H  H    . LEU A 1 18  ? 23.391 19.499 17.814  1.00 10.94 ? 20  LEU A H    1 
ATOM   269  H  HA   . LEU A 1 18  ? 24.033 20.949 20.060  1.00 11.41 ? 20  LEU A HA   1 
ATOM   270  H  HB2  . LEU A 1 18  ? 25.460 18.877 18.795  1.00 11.69 ? 20  LEU A HB2  1 
ATOM   271  H  HB3  . LEU A 1 18  ? 26.069 19.742 19.969  1.00 11.69 ? 20  LEU A HB3  1 
ATOM   272  H  HG   . LEU A 1 18  ? 23.965 17.891 20.275  1.00 12.27 ? 20  LEU A HG   1 
ATOM   273  H  HD11 . LEU A 1 18  ? 25.491 16.604 21.491  1.00 13.15 ? 20  LEU A HD11 1 
ATOM   274  H  HD12 . LEU A 1 18  ? 25.998 16.809 19.999  1.00 13.15 ? 20  LEU A HD12 1 
ATOM   275  H  HD13 . LEU A 1 18  ? 26.629 17.667 21.177  1.00 13.15 ? 20  LEU A HD13 1 
ATOM   276  H  HD21 . LEU A 1 18  ? 24.091 18.202 22.554  1.00 13.48 ? 20  LEU A HD21 1 
ATOM   277  H  HD22 . LEU A 1 18  ? 25.175 19.345 22.346  1.00 13.48 ? 20  LEU A HD22 1 
ATOM   278  H  HD23 . LEU A 1 18  ? 23.684 19.563 21.844  1.00 13.48 ? 20  LEU A HD23 1 
ATOM   279  N  N    . ASP A 1 19  ? 25.740 22.444 19.027  1.00 11.45 ? 21  ASP A N    1 
ATOM   280  C  CA   . ASP A 1 19  ? 26.503 23.505 18.361  1.00 10.73 ? 21  ASP A CA   1 
ATOM   281  C  C    . ASP A 1 19  ? 27.919 23.065 18.098  1.00 10.88 ? 21  ASP A C    1 
ATOM   282  O  O    . ASP A 1 19  ? 28.883 23.782 18.390  1.00 15.28 ? 21  ASP A O    1 
ATOM   283  C  CB   . ASP A 1 19  ? 26.459 24.785 19.211  1.00 15.03 ? 21  ASP A CB   1 
ATOM   284  C  CG   . ASP A 1 19  ? 26.901 25.992 18.458  1.00 27.72 ? 21  ASP A CG   1 
ATOM   285  O  OD1  . ASP A 1 19  ? 27.097 25.944 17.218  1.00 36.25 ? 21  ASP A OD1  1 
ATOM   286  O  OD2  . ASP A 1 19  ? 27.038 27.032 19.120  1.00 25.87 ? 21  ASP A OD2  1 
ATOM   287  H  H    . ASP A 1 19  ? 25.728 22.527 19.883  1.00 11.55 ? 21  ASP A H    1 
ATOM   288  H  HA   . ASP A 1 19  ? 26.088 23.701 17.507  1.00 10.88 ? 21  ASP A HA   1 
ATOM   289  H  HB2  . ASP A 1 19  ? 25.549 24.934 19.510  1.00 14.81 ? 21  ASP A HB2  1 
ATOM   290  H  HB3  . ASP A 1 19  ? 27.046 24.676 19.975  1.00 14.81 ? 21  ASP A HB3  1 
ATOM   291  N  N    . THR A 1 20  ? 28.098 21.883 17.521  1.00 10.10 ? 22  THR A N    1 
ATOM   292  C  CA   . THR A 1 20  ? 29.414 21.327 17.329  1.00 10.41 ? 22  THR A CA   1 
ATOM   293  C  C    . THR A 1 20  ? 30.046 21.648 15.989  1.00 11.08 ? 22  THR A C    1 
ATOM   294  O  O    . THR A 1 20  ? 31.270 21.491 15.837  1.00 10.95 ? 22  THR A O    1 
ATOM   295  C  CB   . THR A 1 20  ? 29.345 19.819 17.390  1.00 11.11 ? 22  THR A CB   1 
ATOM   296  O  OG1  . THR A 1 20  ? 28.202 19.402 16.631  1.00 12.66 ? 22  THR A OG1  1 
ATOM   297  C  CG2  . THR A 1 20  ? 29.186 19.338 18.805  1.00 13.79 ? 22  THR A CG2  1 
ATOM   298  H  H    . THR A 1 20  ? 27.461 21.383 17.231  1.00 9.92  ? 22  THR A H    1 
ATOM   299  H  HA   . THR A 1 20  ? 30.005 21.639 18.033  1.00 10.18 ? 22  THR A HA   1 
ATOM   300  H  HB   . THR A 1 20  ? 30.152 19.434 17.014  1.00 10.90 ? 22  THR A HB   1 
ATOM   301  H  HG1  . THR A 1 20  ? 28.137 18.565 16.647  1.00 12.69 ? 22  THR A HG1  1 
ATOM   302  H  HG21 . THR A 1 20  ? 29.143 18.369 18.822  1.00 13.32 ? 22  THR A HG21 1 
ATOM   303  H  HG22 . THR A 1 20  ? 29.940 19.630 19.341  1.00 13.32 ? 22  THR A HG22 1 
ATOM   304  H  HG23 . THR A 1 20  ? 28.369 19.696 19.187  1.00 13.32 ? 22  THR A HG23 1 
ATOM   305  N  N    . GLU A 1 21  ? 29.301 22.126 15.001  1.00 12.06 ? 23  GLU A N    1 
ATOM   306  C  CA   . GLU A 1 21  ? 29.929 22.438 13.710  1.00 12.52 ? 23  GLU A CA   1 
ATOM   307  C  C    . GLU A 1 21  ? 30.983 23.573 13.792  1.00 11.63 ? 23  GLU A C    1 
ATOM   308  O  O    . GLU A 1 21  ? 32.001 23.563 13.111  1.00 12.15 ? 23  GLU A O    1 
ATOM   309  C  CB   . GLU A 1 21  ? 28.866 22.734 12.648  1.00 12.84 ? 23  GLU A CB   1 
ATOM   310  C  CG   . GLU A 1 21  ? 28.138 21.479 12.130  1.00 12.08 ? 23  GLU A CG   1 
ATOM   311  C  CD   . GLU A 1 21  ? 29.022 20.491 11.411  1.00 14.03 ? 23  GLU A CD   1 
ATOM   312  O  OE1  . GLU A 1 21  ? 30.186 20.852 11.101  1.00 13.15 ? 23  GLU A OE1  1 
ATOM   313  O  OE2  . GLU A 1 21  ? 28.607 19.333 11.137  1.00 13.36 ? 23  GLU A OE2  1 
ATOM   314  H  H    . GLU A 1 21  ? 28.455 22.277 15.041  1.00 11.87 ? 23  GLU A H    1 
ATOM   315  H  HA   . GLU A 1 21  ? 30.401 21.643 13.416  1.00 12.36 ? 23  GLU A HA   1 
ATOM   316  H  HB2  . GLU A 1 21  ? 28.200 23.327 13.029  1.00 12.91 ? 23  GLU A HB2  1 
ATOM   317  H  HB3  . GLU A 1 21  ? 29.293 23.163 11.890  1.00 12.91 ? 23  GLU A HB3  1 
ATOM   318  H  HG2  . GLU A 1 21  ? 27.737 21.020 12.885  1.00 12.39 ? 23  GLU A HG2  1 
ATOM   319  H  HG3  . GLU A 1 21  ? 27.444 21.756 11.512  1.00 12.39 ? 23  GLU A HG3  1 
ATOM   320  N  N    . ARG A 1 22  ? 30.789 24.505 14.717  1.00 11.95 ? 24  ARG A N    1 
ATOM   321  C  CA   . ARG A 1 22  ? 31.786 25.545 14.881  1.00 15.89 ? 24  ARG A CA   1 
ATOM   322  C  C    . ARG A 1 22  ? 33.087 24.978 15.467  1.00 12.68 ? 24  ARG A C    1 
ATOM   323  O  O    . ARG A 1 22  ? 34.159 25.510 15.203  1.00 15.58 ? 24  ARG A O    1 
ATOM   324  C  CB   . ARG A 1 22  ? 31.302 26.749 15.682  1.00 20.13 ? 24  ARG A CB   1 
ATOM   325  C  CG   . ARG A 1 22  ? 30.948 26.447 17.096  1.00 17.70 ? 24  ARG A CG   1 
ATOM   326  C  CD   . ARG A 1 22  ? 30.814 27.729 17.932  1.00 22.01 ? 24  ARG A CD   1 
ATOM   327  N  NE   . ARG A 1 22  ? 30.377 27.331 19.252  1.00 22.15 ? 24  ARG A NE   1 
ATOM   328  C  CZ   . ARG A 1 22  ? 31.183 26.995 20.230  1.00 20.26 ? 24  ARG A CZ   1 
ATOM   329  N  NH1  . ARG A 1 22  ? 30.670 26.611 21.402  1.00 25.41 ? 24  ARG A NH1  1 
ATOM   330  N  NH2  . ARG A 1 22  ? 32.504 27.100 20.061  1.00 19.88 ? 24  ARG A NH2  1 
ATOM   331  H  H    . ARG A 1 22  ? 30.111 24.556 15.244  1.00 12.43 ? 24  ARG A H    1 
ATOM   332  H  HA   . ARG A 1 22  ? 32.006 25.876 13.996  1.00 15.98 ? 24  ARG A HA   1 
ATOM   333  H  HB2  . ARG A 1 22  ? 32.004 27.419 15.690  1.00 19.97 ? 24  ARG A HB2  1 
ATOM   334  H  HB3  . ARG A 1 22  ? 30.512 27.110 15.251  1.00 19.97 ? 24  ARG A HB3  1 
ATOM   335  H  HG2  . ARG A 1 22  ? 30.099 25.978 17.120  1.00 17.50 ? 24  ARG A HG2  1 
ATOM   336  H  HG3  . ARG A 1 22  ? 31.645 25.899 17.490  1.00 17.50 ? 24  ARG A HG3  1 
ATOM   337  H  HD2  . ARG A 1 22  ? 31.673 28.173 18.002  1.00 21.39 ? 24  ARG A HD2  1 
ATOM   338  H  HD3  . ARG A 1 22  ? 30.147 28.314 17.540  1.00 21.39 ? 24  ARG A HD3  1 
ATOM   339  H  HE   . ARG A 1 22  ? 29.531 27.313 19.406  1.00 21.46 ? 24  ARG A HE   1 
ATOM   340  H  HH11 . ARG A 1 22  ? 29.818 26.565 21.504  1.00 24.41 ? 24  ARG A HH11 1 
ATOM   341  H  HH12 . ARG A 1 22  ? 31.193 26.416 22.056  1.00 24.41 ? 24  ARG A HH12 1 
ATOM   342  H  HH21 . ARG A 1 22  ? 32.823 27.345 19.301  1.00 18.78 ? 24  ARG A HH21 1 
ATOM   343  H  HH22 . ARG A 1 22  ? 33.037 26.895 20.704  1.00 18.78 ? 24  ARG A HH22 1 
ATOM   344  N  N    . LEU A 1 23  ? 33.008 23.893 16.250  1.00 12.28 ? 25  LEU A N    1 
ATOM   345  C  CA   . LEU A 1 23  ? 34.190 23.215 16.784  1.00 14.12 ? 25  LEU A CA   1 
ATOM   346  C  C    . LEU A 1 23  ? 34.993 22.565 15.680  1.00 13.33 ? 25  LEU A C    1 
ATOM   347  O  O    . LEU A 1 23  ? 36.209 22.713 15.618  1.00 14.66 ? 25  LEU A O    1 
ATOM   348  C  CB   . LEU A 1 23  ? 33.787 22.199 17.849  1.00 12.87 ? 25  LEU A CB   1 
ATOM   349  C  CG   . LEU A 1 23  ? 33.004 22.800 19.019  1.00 12.12 ? 25  LEU A CG   1 
ATOM   350  C  CD1  . LEU A 1 23  ? 32.654 21.693 19.980  1.00 14.46 ? 25  LEU A CD1  1 
ATOM   351  C  CD2  . LEU A 1 23  ? 33.788 23.884 19.737  1.00 15.85 ? 25  LEU A CD2  1 
ATOM   352  H  H    . LEU A 1 23  ? 32.267 23.528 16.489  1.00 12.37 ? 25  LEU A H    1 
ATOM   353  H  HA   . LEU A 1 23  ? 34.759 23.875 17.210  1.00 13.94 ? 25  LEU A HA   1 
ATOM   354  H  HB2  . LEU A 1 23  ? 33.230 21.520 17.437  1.00 12.75 ? 25  LEU A HB2  1 
ATOM   355  H  HB3  . LEU A 1 23  ? 34.590 21.790 18.209  1.00 12.75 ? 25  LEU A HB3  1 
ATOM   356  H  HG   . LEU A 1 23  ? 32.179 23.189 18.687  1.00 11.95 ? 25  LEU A HG   1 
ATOM   357  H  HD11 . LEU A 1 23  ? 32.157 22.066 20.724  1.00 14.27 ? 25  LEU A HD11 1 
ATOM   358  H  HD12 . LEU A 1 23  ? 32.113 21.034 19.518  1.00 14.27 ? 25  LEU A HD12 1 
ATOM   359  H  HD13 . LEU A 1 23  ? 33.473 21.283 20.300  1.00 14.27 ? 25  LEU A HD13 1 
ATOM   360  H  HD21 . LEU A 1 23  ? 33.251 24.232 20.466  1.00 15.28 ? 25  LEU A HD21 1 
ATOM   361  H  HD22 . LEU A 1 23  ? 34.610 23.502 20.084  1.00 15.28 ? 25  LEU A HD22 1 
ATOM   362  H  HD23 . LEU A 1 23  ? 33.992 24.595 19.109  1.00 15.28 ? 25  LEU A HD23 1 
ATOM   363  N  N    . TYR A 1 24  ? 34.314 21.843 14.769  1.00 14.55 ? 26  TYR A N    1 
ATOM   364  C  CA   . TYR A 1 24  ? 34.996 21.297 13.600  1.00 12.43 ? 26  TYR A CA   1 
ATOM   365  C  C    . TYR A 1 24  ? 35.632 22.374 12.768  1.00 15.41 ? 26  TYR A C    1 
ATOM   366  O  O    . TYR A 1 24  ? 36.770 22.209 12.293  1.00 16.56 ? 26  TYR A O    1 
ATOM   367  C  CB   . TYR A 1 24  ? 34.023 20.536 12.712  1.00 12.87 ? 26  TYR A CB   1 
ATOM   368  C  CG   . TYR A 1 24  ? 33.573 19.214 13.246  1.00 13.22 ? 26  TYR A CG   1 
ATOM   369  C  CD1  . TYR A 1 24  ? 34.367 18.093 13.153  1.00 14.86 ? 26  TYR A CD1  1 
ATOM   370  C  CD2  . TYR A 1 24  ? 32.298 19.039 13.772  1.00 13.46 ? 26  TYR A CD2  1 
ATOM   371  C  CE1  . TYR A 1 24  ? 33.927 16.870 13.601  1.00 15.37 ? 26  TYR A CE1  1 
ATOM   372  C  CE2  . TYR A 1 24  ? 31.867 17.838 14.224  1.00 14.95 ? 26  TYR A CE2  1 
ATOM   373  C  CZ   . TYR A 1 24  ? 32.666 16.757 14.111  1.00 17.74 ? 26  TYR A CZ   1 
ATOM   374  O  OH   . TYR A 1 24  ? 32.205 15.540 14.510  1.00 18.72 ? 26  TYR A OH   1 
ATOM   375  H  H    . TYR A 1 24  ? 33.474 21.664 14.811  1.00 13.97 ? 26  TYR A H    1 
ATOM   376  H  HA   . TYR A 1 24  ? 35.689 20.684 13.890  1.00 11.74 ? 26  TYR A HA   1 
ATOM   377  H  HB2  . TYR A 1 24  ? 33.232 21.082 12.583  1.00 12.55 ? 26  TYR A HB2  1 
ATOM   378  H  HB3  . TYR A 1 24  ? 34.449 20.375 11.856  1.00 12.55 ? 26  TYR A HB3  1 
ATOM   379  H  HD1  . TYR A 1 24  ? 35.220 18.166 12.789  1.00 14.38 ? 26  TYR A HD1  1 
ATOM   380  H  HD2  . TYR A 1 24  ? 31.733 19.775 13.837  1.00 13.54 ? 26  TYR A HD2  1 
ATOM   381  H  HE1  . TYR A 1 24  ? 34.471 16.119 13.526  1.00 14.89 ? 26  TYR A HE1  1 
ATOM   382  H  HE2  . TYR A 1 24  ? 31.005 17.748 14.562  1.00 15.04 ? 26  TYR A HE2  1 
ATOM   383  H  HH   . TYR A 1 24  ? 32.795 14.955 14.386  1.00 18.45 ? 26  TYR A HH   1 
ATOM   384  N  N    . SER A 1 25  ? 34.910 23.484 12.576  1.00 13.15 ? 27  SER A N    1 
ATOM   385  C  CA   . SER A 1 25  ? 35.410 24.557 11.734  1.00 17.30 ? 27  SER A CA   1 
ATOM   386  C  C    . SER A 1 25  ? 36.736 25.097 12.255  1.00 17.08 ? 27  SER A C    1 
ATOM   387  O  O    . SER A 1 25  ? 37.691 25.298 11.507  1.00 19.45 ? 27  SER A O    1 
ATOM   388  C  CB   . SER A 1 25  ? 34.401 25.696 11.636  1.00 16.90 ? 27  SER A CB   1 
ATOM   389  O  OG   . SER A 1 25  ? 33.246 25.285 10.897  1.00 20.34 ? 27  SER A OG   1 
ATOM   390  H  H    . SER A 1 25  ? 34.137 23.632 12.922  1.00 12.95 ? 27  SER A H    1 
ATOM   391  H  HA   . SER A 1 25  ? 35.559 24.212 10.839  1.00 16.78 ? 27  SER A HA   1 
ATOM   392  H  HB2  . SER A 1 25  ? 34.128 25.955 12.531  1.00 16.51 ? 27  SER A HB2  1 
ATOM   393  H  HB3  . SER A 1 25  ? 34.815 26.448 11.184  1.00 16.51 ? 27  SER A HB3  1 
ATOM   394  H  HG   . SER A 1 25  ? 33.469 25.057 10.120  1.00 20.39 ? 27  SER A HG   1 
ATOM   395  N  N    . VAL A 1 26  ? 36.780 25.385 13.542  1.00 16.81 ? 28  VAL A N    1 
ATOM   396  C  CA   . VAL A 1 26  ? 38.022 25.920 14.130  1.00 18.51 ? 28  VAL A CA   1 
ATOM   397  C  C    . VAL A 1 26  ? 39.202 24.970 13.971  1.00 18.64 ? 28  VAL A C    1 
ATOM   398  O  O    . VAL A 1 26  ? 40.308 25.421 13.628  1.00 20.59 ? 28  VAL A O    1 
ATOM   399  C  CB   . VAL A 1 26  ? 37.856 26.281 15.620  1.00 23.30 ? 28  VAL A CB   1 
ATOM   400  C  CG1  . VAL A 1 26  ? 39.207 26.632 16.227  1.00 26.88 ? 28  VAL A CG1  1 
ATOM   401  C  CG2  . VAL A 1 26  ? 36.916 27.425 15.782  1.00 26.66 ? 28  VAL A CG2  1 
ATOM   402  H  H    . VAL A 1 26  ? 36.129 25.288 14.096  1.00 15.84 ? 28  VAL A H    1 
ATOM   403  H  HA   . VAL A 1 26  ? 38.248 26.738 13.661  1.00 16.93 ? 28  VAL A HA   1 
ATOM   404  H  HB   . VAL A 1 26  ? 37.494 25.519 16.098  1.00 21.67 ? 28  VAL A HB   1 
ATOM   405  H  HG11 . VAL A 1 26  ? 39.083 26.856 17.163  1.00 24.59 ? 28  VAL A HG11 1 
ATOM   406  H  HG12 . VAL A 1 26  ? 39.797 25.867 16.145  1.00 24.59 ? 28  VAL A HG12 1 
ATOM   407  H  HG13 . VAL A 1 26  ? 39.579 27.391 15.751  1.00 24.59 ? 28  VAL A HG13 1 
ATOM   408  H  HG21 . VAL A 1 26  ? 36.830 27.632 16.726  1.00 25.10 ? 28  VAL A HG21 1 
ATOM   409  H  HG22 . VAL A 1 26  ? 37.270 28.193 15.306  1.00 25.10 ? 28  VAL A HG22 1 
ATOM   410  H  HG23 . VAL A 1 26  ? 36.053 27.178 15.417  1.00 25.10 ? 28  VAL A HG23 1 
ATOM   411  N  N    . VAL A 1 27  ? 38.993 23.678 14.173  1.00 16.67 ? 29  VAL A N    1 
ATOM   412  C  CA   . VAL A 1 27  ? 40.096 22.730 14.116  1.00 19.95 ? 29  VAL A CA   1 
ATOM   413  C  C    . VAL A 1 27  ? 40.536 22.552 12.675  1.00 21.41 ? 29  VAL A C    1 
ATOM   414  O  O    . VAL A 1 27  ? 41.748 22.472 12.375  1.00 21.02 ? 29  VAL A O    1 
ATOM   415  C  CB   . VAL A 1 27  ? 39.701 21.386 14.727  1.00 16.63 ? 29  VAL A CB   1 
ATOM   416  C  CG1  . VAL A 1 27  ? 40.614 20.284 14.344  1.00 18.95 ? 29  VAL A CG1  1 
ATOM   417  C  CG2  . VAL A 1 27  ? 39.531 21.493 16.254  1.00 20.34 ? 29  VAL A CG2  1 
ATOM   418  H  H    . VAL A 1 27  ? 38.227 23.325 14.344  1.00 15.52 ? 29  VAL A H    1 
ATOM   419  H  HA   . VAL A 1 27  ? 40.846 23.083 14.620  1.00 18.40 ? 29  VAL A HA   1 
ATOM   420  H  HB   . VAL A 1 27  ? 38.829 21.153 14.371  1.00 15.36 ? 29  VAL A HB   1 
ATOM   421  H  HG11 . VAL A 1 27  ? 40.310 19.463 14.761  1.00 17.29 ? 29  VAL A HG11 1 
ATOM   422  H  HG12 . VAL A 1 27  ? 40.604 20.187 13.379  1.00 17.29 ? 29  VAL A HG12 1 
ATOM   423  H  HG13 . VAL A 1 27  ? 41.510 20.497 14.647  1.00 17.29 ? 29  VAL A HG13 1 
ATOM   424  H  HG21 . VAL A 1 27  ? 39.281 20.625 16.606  1.00 19.10 ? 29  VAL A HG21 1 
ATOM   425  H  HG22 . VAL A 1 27  ? 40.371 21.780 16.645  1.00 19.10 ? 29  VAL A HG22 1 
ATOM   426  H  HG23 . VAL A 1 27  ? 38.837 22.142 16.450  1.00 19.10 ? 29  VAL A HG23 1 
ATOM   427  N  N    . PHE A 1 28  ? 39.573 22.485 11.756  1.00 18.20 ? 30  PHE A N    1 
ATOM   428  C  CA   . PHE A 1 28  ? 39.963 22.351 10.349  1.00 17.99 ? 30  PHE A CA   1 
ATOM   429  C  C    . PHE A 1 28  ? 40.576 23.617 9.784   1.00 19.81 ? 30  PHE A C    1 
ATOM   430  O  O    . PHE A 1 28  ? 41.509 23.541 8.994   1.00 22.91 ? 30  PHE A O    1 
ATOM   431  C  CB   . PHE A 1 28  ? 38.792 21.867 9.504   1.00 16.19 ? 30  PHE A CB   1 
ATOM   432  C  CG   . PHE A 1 28  ? 38.486 20.421 9.703   1.00 14.10 ? 30  PHE A CG   1 
ATOM   433  C  CD1  . PHE A 1 28  ? 39.482 19.470 9.577   1.00 19.34 ? 30  PHE A CD1  1 
ATOM   434  C  CD2  . PHE A 1 28  ? 37.196 19.990 9.984   1.00 15.52 ? 30  PHE A CD2  1 
ATOM   435  C  CE1  . PHE A 1 28  ? 39.224 18.146 9.761   1.00 17.75 ? 30  PHE A CE1  1 
ATOM   436  C  CE2  . PHE A 1 28  ? 36.948 18.632 10.162  1.00 16.00 ? 30  PHE A CE2  1 
ATOM   437  C  CZ   . PHE A 1 28  ? 37.951 17.723 10.042  1.00 18.88 ? 30  PHE A CZ   1 
ATOM   438  H  H    . PHE A 1 28  ? 38.727 22.513 11.908  1.00 16.77 ? 30  PHE A H    1 
ATOM   439  H  HA   . PHE A 1 28  ? 40.647 21.665 10.297  1.00 16.30 ? 30  PHE A HA   1 
ATOM   440  H  HB2  . PHE A 1 28  ? 38.001 22.375 9.741   1.00 15.06 ? 30  PHE A HB2  1 
ATOM   441  H  HB3  . PHE A 1 28  ? 39.004 22.001 8.567   1.00 15.06 ? 30  PHE A HB3  1 
ATOM   442  H  HD1  . PHE A 1 28  ? 40.351 19.743 9.389   1.00 17.96 ? 30  PHE A HD1  1 
ATOM   443  H  HD2  . PHE A 1 28  ? 36.505 20.606 10.069  1.00 15.23 ? 30  PHE A HD2  1 
ATOM   444  H  HE1  . PHE A 1 28  ? 39.911 17.524 9.676   1.00 16.47 ? 30  PHE A HE1  1 
ATOM   445  H  HE2  . PHE A 1 28  ? 36.085 18.343 10.356  1.00 15.81 ? 30  PHE A HE2  1 
ATOM   446  H  HZ   . PHE A 1 28  ? 37.776 16.818 10.162  1.00 18.20 ? 30  PHE A HZ   1 
ATOM   447  N  N    . GLN A 1 29  ? 40.088 24.777 10.191  1.00 19.50 ? 31  GLN A N    1 
ATOM   448  C  CA   . GLN A 1 29  ? 40.687 26.035 9.729   1.00 22.98 ? 31  GLN A CA   1 
ATOM   449  C  C    . GLN A 1 29  ? 42.146 26.091 10.195  1.00 24.96 ? 31  GLN A C    1 
ATOM   450  O  O    . GLN A 1 29  ? 43.042 26.429 9.418   1.00 28.35 ? 31  GLN A O    1 
ATOM   451  C  CB   . GLN A 1 29  ? 39.899 27.254 10.194  1.00 23.54 ? 31  GLN A CB   1 
ATOM   452  C  CG   . GLN A 1 29  ? 40.532 28.600 9.852   1.00 31.63 ? 31  GLN A CG   1 
ATOM   453  C  CD   . GLN A 1 29  ? 40.802 28.798 8.362   1.00 35.82 ? 31  GLN A CD   1 
ATOM   454  O  OE1  . GLN A 1 29  ? 40.286 28.071 7.511   1.00 35.75 ? 31  GLN A OE1  1 
ATOM   455  N  NE2  . GLN A 1 29  ? 41.596 29.822 8.042   1.00 39.96 ? 31  GLN A NE2  1 
ATOM   456  H  H    . GLN A 1 29  ? 39.421 24.872 10.726  1.00 18.51 ? 31  GLN A H    1 
ATOM   457  H  HA   . GLN A 1 29  ? 40.688 26.039 8.759   1.00 21.38 ? 31  GLN A HA   1 
ATOM   458  H  HB2  . GLN A 1 29  ? 39.021 27.229 9.781   1.00 22.11 ? 31  GLN A HB2  1 
ATOM   459  H  HB3  . GLN A 1 29  ? 39.805 27.211 11.159  1.00 22.11 ? 31  GLN A HB3  1 
ATOM   460  H  HG2  . GLN A 1 29  ? 39.935 29.307 10.141  1.00 29.45 ? 31  GLN A HG2  1 
ATOM   461  H  HG3  . GLN A 1 29  ? 41.379 28.674 10.319  1.00 29.45 ? 31  GLN A HG3  1 
ATOM   462  H  HE21 . GLN A 1 29  ? 41.922 30.323 8.660   1.00 36.55 ? 31  GLN A HE21 1 
ATOM   463  H  HE22 . GLN A 1 29  ? 41.783 29.981 7.217   1.00 36.55 ? 31  GLN A HE22 1 
ATOM   464  N  N    . GLU A 1 30  ? 42.390 25.681 11.427  1.00 24.74 ? 32  GLU A N    1 
ATOM   465  C  CA   . GLU A 1 30  ? 43.743 25.762 11.964  1.00 27.96 ? 32  GLU A CA   1 
ATOM   466  C  C    . GLU A 1 30  ? 44.676 24.849 11.170  1.00 27.34 ? 32  GLU A C    1 
ATOM   467  O  O    . GLU A 1 30  ? 45.796 25.228 10.817  1.00 31.26 ? 32  GLU A O    1 
ATOM   468  C  CB   . GLU A 1 30  ? 43.750 25.401 13.442  1.00 30.29 ? 32  GLU A CB   1 
ATOM   469  C  CG   . GLU A 1 30  ? 45.083 25.686 14.074  1.00 32.63 ? 32  GLU A CG   1 
ATOM   470  C  CD   . GLU A 1 30  ? 45.173 25.251 15.512  1.00 37.30 ? 32  GLU A CD   1 
ATOM   471  O  OE1  . GLU A 1 30  ? 44.380 24.387 15.924  1.00 34.20 ? 32  GLU A OE1  1 
ATOM   472  O  OE2  . GLU A 1 30  ? 46.060 25.770 16.230  1.00 41.60 ? 32  GLU A OE2  1 
ATOM   473  H  H    . GLU A 1 30  ? 41.805 25.356 11.968  1.00 23.64 ? 32  GLU A H    1 
ATOM   474  H  HA   . GLU A 1 30  ? 44.065 26.673 11.874  1.00 26.09 ? 32  GLU A HA   1 
ATOM   475  H  HB2  . GLU A 1 30  ? 43.077 25.925 13.903  1.00 28.59 ? 32  GLU A HB2  1 
ATOM   476  H  HB3  . GLU A 1 30  ? 43.564 24.454 13.541  1.00 28.59 ? 32  GLU A HB3  1 
ATOM   477  H  HG2  . GLU A 1 30  ? 45.772 25.216 13.578  1.00 30.10 ? 32  GLU A HG2  1 
ATOM   478  H  HG3  . GLU A 1 30  ? 45.247 26.641 14.042  1.00 30.10 ? 32  GLU A HG3  1 
ATOM   479  N  N    . ILE A 1 31  ? 44.219 23.642 10.868  1.00 25.00 ? 33  ILE A N    1 
ATOM   480  C  CA   . ILE A 1 31  ? 45.023 22.708 10.095  1.00 23.47 ? 33  ILE A CA   1 
ATOM   481  C  C    . ILE A 1 31  ? 45.234 23.211 8.667   1.00 26.75 ? 33  ILE A C    1 
ATOM   482  O  O    . ILE A 1 31  ? 46.363 23.148 8.127   1.00 26.99 ? 33  ILE A O    1 
ATOM   483  C  CB   . ILE A 1 31  ? 44.404 21.293 10.108  1.00 21.30 ? 33  ILE A CB   1 
ATOM   484  C  CG1  . ILE A 1 31  ? 44.477 20.725 11.528  1.00 24.64 ? 33  ILE A CG1  1 
ATOM   485  C  CG2  . ILE A 1 31  ? 45.136 20.361 9.162   1.00 23.73 ? 33  ILE A CG2  1 
ATOM   486  C  CD1  . ILE A 1 31  ? 43.808 19.373 11.715  1.00 23.22 ? 33  ILE A CD1  1 
ATOM   487  H  H    . ILE A 1 31  ? 43.448 23.339 11.098  1.00 22.92 ? 33  ILE A H    1 
ATOM   488  H  HA   . ILE A 1 31  ? 45.897 22.644 10.511  1.00 20.89 ? 33  ILE A HA   1 
ATOM   489  H  HB   . ILE A 1 31  ? 43.475 21.351 9.838   1.00 19.24 ? 33  ILE A HB   1 
ATOM   490  H  HG12 . ILE A 1 31  ? 45.411 20.625 11.773  1.00 22.71 ? 33  ILE A HG12 1 
ATOM   491  H  HG13 . ILE A 1 31  ? 44.048 21.350 12.133  1.00 22.71 ? 33  ILE A HG13 1 
ATOM   492  H  HG21 . ILE A 1 31  ? 44.720 19.485 9.197   1.00 21.09 ? 33  ILE A HG21 1 
ATOM   493  H  HG22 . ILE A 1 31  ? 45.079 20.718 8.262   1.00 21.09 ? 33  ILE A HG22 1 
ATOM   494  H  HG23 . ILE A 1 31  ? 46.064 20.299 9.436   1.00 21.09 ? 33  ILE A HG23 1 
ATOM   495  H  HD11 . ILE A 1 31  ? 43.906 19.098 12.640  1.00 21.74 ? 33  ILE A HD11 1 
ATOM   496  H  HD12 . ILE A 1 31  ? 42.867 19.453 11.491  1.00 21.74 ? 33  ILE A HD12 1 
ATOM   497  H  HD13 . ILE A 1 31  ? 44.234 18.727 11.131  1.00 21.74 ? 33  ILE A HD13 1 
ATOM   498  N  N    . CYS A 1 32  ? 44.174 23.729 8.048   1.00 26.55 ? 34  CYS A N    1 
ATOM   499  C  CA   . CYS A 1 32  ? 44.247 24.189 6.648   1.00 24.96 ? 34  CYS A CA   1 
ATOM   500  C  C    . CYS A 1 32  ? 45.160 25.401 6.516   1.00 30.74 ? 34  CYS A C    1 
ATOM   501  O  O    . CYS A 1 32  ? 45.876 25.541 5.522   1.00 32.42 ? 34  CYS A O    1 
ATOM   502  C  CB   . CYS A 1 32  ? 42.848 24.512 6.116   1.00 26.12 ? 34  CYS A CB   1 
ATOM   503  S  SG   . CYS A 1 32  ? 41.863 23.019 5.801   1.00 24.27 ? 34  CYS A SG   1 
ATOM   504  H  H    . CYS A 1 32  ? 43.400 23.829 8.410   1.00 23.20 ? 34  CYS A H    1 
ATOM   505  H  HA   . CYS A 1 32  ? 44.616 23.477 6.103   1.00 21.24 ? 34  CYS A HA   1 
ATOM   506  H  HB2  . CYS A 1 32  ? 42.377 25.051 6.769   1.00 23.18 ? 34  CYS A HB2  1 
ATOM   507  H  HB3  . CYS A 1 32  ? 42.932 24.998 5.281   1.00 23.18 ? 34  CYS A HB3  1 
ATOM   508  H  HG   . CYS A 1 32  ? 41.742 22.408 6.827   1.00 22.12 ? 34  CYS A HG   1 
ATOM   509  N  N    . ASN A 1 33  ? 45.136 26.262 7.525   1.00 32.13 ? 35  ASN A N    1 
ATOM   510  C  CA   . ASN A 1 33  ? 45.885 27.502 7.500   1.00 34.05 ? 35  ASN A CA   1 
ATOM   511  C  C    . ASN A 1 33  ? 47.381 27.277 7.377   1.00 34.61 ? 35  ASN A C    1 
ATOM   512  O  O    . ASN A 1 33  ? 48.074 28.107 6.795   1.00 37.36 ? 35  ASN A O    1 
ATOM   513  C  CB   . ASN A 1 33  ? 45.631 28.309 8.775   1.00 33.41 ? 35  ASN A CB   1 
ATOM   514  C  CG   . ASN A 1 33  ? 44.321 29.068 8.747   1.00 37.58 ? 35  ASN A CG   1 
ATOM   515  O  OD1  . ASN A 1 33  ? 43.732 29.298 7.687   1.00 39.96 ? 35  ASN A OD1  1 
ATOM   516  N  ND2  . ASN A 1 33  ? 43.867 29.491 9.923   1.00 41.65 ? 35  ASN A ND2  1 
ATOM   517  H  H    . ASN A 1 33  ? 44.683 26.145 8.246   1.00 26.68 ? 35  ASN A H    1 
ATOM   518  H  HA   . ASN A 1 33  ? 45.595 28.034 6.743   1.00 27.75 ? 35  ASN A HA   1 
ATOM   519  H  HB2  . ASN A 1 33  ? 45.609 27.704 9.533   1.00 27.29 ? 35  ASN A HB2  1 
ATOM   520  H  HB3  . ASN A 1 33  ? 46.347 28.954 8.888   1.00 27.29 ? 35  ASN A HB3  1 
ATOM   521  H  HD21 . ASN A 1 33  ? 43.128 29.927 9.967   1.00 36.51 ? 35  ASN A HD21 1 
ATOM   522  H  HD22 . ASN A 1 33  ? 44.314 29.327 10.640  1.00 36.51 ? 35  ASN A HD22 1 
ATOM   523  N  N    . ARG A 1 34  ? 47.891 26.171 7.921   1.00 30.22 ? 36  ARG A N    1 
ATOM   524  C  CA   . ARG A 1 34  ? 49.341 25.980 7.954   1.00 34.43 ? 36  ARG A CA   1 
ATOM   525  C  C    . ARG A 1 34  ? 49.821 25.628 6.572   1.00 34.29 ? 36  ARG A C    1 
ATOM   526  O  O    . ARG A 1 34  ? 51.018 25.678 6.279   1.00 36.72 ? 36  ARG A O    1 
ATOM   527  C  CB   . ARG A 1 34  ? 49.775 24.928 8.994   1.00 31.15 ? 36  ARG A CB   1 
ATOM   528  C  CG   . ARG A 1 34  ? 49.524 23.489 8.652   1.00 34.63 ? 36  ARG A CG   1 
ATOM   529  C  CD   . ARG A 1 34  ? 49.469 22.694 9.942   1.00 33.55 ? 36  ARG A CD   1 
ATOM   530  N  NE   . ARG A 1 34  ? 49.322 21.282 9.678   1.00 28.21 ? 36  ARG A NE   1 
ATOM   531  C  CZ   . ARG A 1 34  ? 48.799 20.404 10.515  1.00 25.95 ? 36  ARG A CZ   1 
ATOM   532  N  NH1  . ARG A 1 34  ? 48.361 20.792 11.701  1.00 27.36 ? 36  ARG A NH1  1 
ATOM   533  N  NH2  . ARG A 1 34  ? 48.710 19.133 10.161  1.00 29.45 ? 36  ARG A NH2  1 
ATOM   534  H  H    . ARG A 1 34  ? 47.432 25.533 8.269   1.00 25.68 ? 36  ARG A H    1 
ATOM   535  H  HA   . ARG A 1 34  ? 49.756 26.821 8.202   1.00 28.77 ? 36  ARG A HA   1 
ATOM   536  H  HB2  . ARG A 1 34  ? 50.729 25.025 9.140   1.00 25.57 ? 36  ARG A HB2  1 
ATOM   537  H  HB3  . ARG A 1 34  ? 49.305 25.111 9.822   1.00 25.57 ? 36  ARG A HB3  1 
ATOM   538  H  HG2  . ARG A 1 34  ? 48.674 23.403 8.193   1.00 29.41 ? 36  ARG A HG2  1 
ATOM   539  H  HG3  . ARG A 1 34  ? 50.249 23.149 8.105   1.00 29.41 ? 36  ARG A HG3  1 
ATOM   540  H  HD2  . ARG A 1 34  ? 50.292 22.828 10.437  1.00 28.72 ? 36  ARG A HD2  1 
ATOM   541  H  HD3  . ARG A 1 34  ? 48.708 22.987 10.467  1.00 28.72 ? 36  ARG A HD3  1 
ATOM   542  H  HE   . ARG A 1 34  ? 49.596 20.990 8.917   1.00 23.56 ? 36  ARG A HE   1 
ATOM   543  H  HH11 . ARG A 1 34  ? 48.417 21.619 11.930  1.00 23.80 ? 36  ARG A HH11 1 
ATOM   544  H  HH12 . ARG A 1 34  ? 48.021 20.218 12.243  1.00 23.80 ? 36  ARG A HH12 1 
ATOM   545  H  HH21 . ARG A 1 34  ? 48.995 18.880 9.390   1.00 25.41 ? 36  ARG A HH21 1 
ATOM   546  H  HH22 . ARG A 1 34  ? 48.372 18.558 10.704  1.00 25.41 ? 36  ARG A HH22 1 
ATOM   547  N  N    . TYR A 1 35  ? 48.861 25.315 5.708   1.00 31.70 ? 37  TYR A N    1 
ATOM   548  C  CA   . TYR A 1 35  ? 49.134 25.039 4.319   1.00 35.33 ? 37  TYR A CA   1 
ATOM   549  C  C    . TYR A 1 35  ? 48.640 26.170 3.439   1.00 33.59 ? 37  TYR A C    1 
ATOM   550  O  O    . TYR A 1 35  ? 48.535 26.012 2.235   1.00 36.48 ? 37  TYR A O    1 
ATOM   551  C  CB   . TYR A 1 35  ? 48.456 23.746 3.908   1.00 30.92 ? 37  TYR A CB   1 
ATOM   552  C  CG   . TYR A 1 35  ? 48.805 22.575 4.784   1.00 29.36 ? 37  TYR A CG   1 
ATOM   553  C  CD1  . TYR A 1 35  ? 50.089 22.020 4.756   1.00 31.65 ? 37  TYR A CD1  1 
ATOM   554  C  CD2  . TYR A 1 35  ? 47.871 22.022 5.653   1.00 29.01 ? 37  TYR A CD2  1 
ATOM   555  C  CE1  . TYR A 1 35  ? 50.423 20.932 5.548   1.00 31.76 ? 37  TYR A CE1  1 
ATOM   556  C  CE2  . TYR A 1 35  ? 48.190 20.937 6.442   1.00 27.88 ? 37  TYR A CE2  1 
ATOM   557  C  CZ   . TYR A 1 35  ? 49.479 20.402 6.399   1.00 28.60 ? 37  TYR A CZ   1 
ATOM   558  O  OH   . TYR A 1 35  ? 49.803 19.323 7.188   1.00 28.39 ? 37  TYR A OH   1 
ATOM   559  H  H    . TYR A 1 35  ? 48.028 25.256 5.914   1.00 25.95 ? 37  TYR A H    1 
ATOM   560  H  HA   . TYR A 1 35  ? 50.090 24.942 4.189   1.00 29.02 ? 37  TYR A HA   1 
ATOM   561  H  HB2  . TYR A 1 35  ? 47.495 23.871 3.948   1.00 25.30 ? 37  TYR A HB2  1 
ATOM   562  H  HB3  . TYR A 1 35  ? 48.722 23.528 3.001   1.00 25.30 ? 37  TYR A HB3  1 
ATOM   563  H  HD1  . TYR A 1 35  ? 50.727 22.377 4.181   1.00 25.07 ? 37  TYR A HD1  1 
ATOM   564  H  HD2  . TYR A 1 35  ? 47.010 22.374 5.685   1.00 24.54 ? 37  TYR A HD2  1 
ATOM   565  H  HE1  . TYR A 1 35  ? 51.280 20.573 5.516   1.00 25.18 ? 37  TYR A HE1  1 
ATOM   566  H  HE2  . TYR A 1 35  ? 47.555 20.577 7.018   1.00 23.41 ? 37  TYR A HE2  1 
ATOM   567  H  HH   . TYR A 1 35  ? 49.142 19.100 7.656   1.00 22.79 ? 37  TYR A HH   1 
ATOM   568  N  N    . ASP A 1 36  ? 48.358 27.313 4.048   1.00 33.93 ? 38  ASP A N    1 
ATOM   569  C  CA   . ASP A 1 36  ? 47.868 28.488 3.326   1.00 37.06 ? 38  ASP A CA   1 
ATOM   570  C  C    . ASP A 1 36  ? 46.578 28.241 2.555   1.00 38.36 ? 38  ASP A C    1 
ATOM   571  O  O    . ASP A 1 36  ? 46.341 28.875 1.530   1.00 36.63 ? 38  ASP A O    1 
ATOM   572  C  CB   . ASP A 1 36  ? 48.939 29.022 2.378   1.00 36.52 ? 38  ASP A CB   1 
ATOM   573  C  CG   . ASP A 1 36  ? 50.175 29.479 3.111   1.00 45.47 ? 38  ASP A CG   1 
ATOM   574  O  OD1  . ASP A 1 36  ? 50.023 30.284 4.049   1.00 48.77 ? 38  ASP A OD1  1 
ATOM   575  O  OD2  . ASP A 1 36  ? 51.287 29.019 2.778   1.00 49.80 ? 38  ASP A OD2  1 
ATOM   576  H  H    . ASP A 1 36  ? 48.443 27.439 4.895   1.00 26.85 ? 38  ASP A H    1 
ATOM   577  H  HA   . ASP A 1 36  ? 47.684 29.186 3.974   1.00 29.83 ? 38  ASP A HA   1 
ATOM   578  H  HB2  . ASP A 1 36  ? 49.197 28.319 1.761   1.00 27.90 ? 38  ASP A HB2  1 
ATOM   579  H  HB3  . ASP A 1 36  ? 48.582 29.779 1.888   1.00 27.90 ? 38  ASP A HB3  1 
ATOM   580  N  N    . LYS A 1 37  ? 45.744 27.337 3.067   1.00 33.27 ? 39  LYS A N    1 
ATOM   581  C  CA   . LYS A 1 37  ? 44.435 27.069 2.490   1.00 31.37 ? 39  LYS A CA   1 
ATOM   582  C  C    . LYS A 1 37  ? 43.354 27.520 3.465   1.00 31.32 ? 39  LYS A C    1 
ATOM   583  O  O    . LYS A 1 37  ? 43.569 27.545 4.673   1.00 31.25 ? 39  LYS A O    1 
ATOM   584  C  CB   . LYS A 1 37  ? 44.280 25.587 2.157   1.00 28.69 ? 39  LYS A CB   1 
ATOM   585  C  CG   . LYS A 1 37  ? 45.396 25.010 1.285   1.00 32.60 ? 39  LYS A CG   1 
ATOM   586  C  CD   . LYS A 1 37  ? 45.340 25.536 -0.135  1.00 37.26 ? 39  LYS A CD   1 
ATOM   587  C  CE   . LYS A 1 37  ? 46.520 25.059 -1.003  1.00 38.50 ? 39  LYS A CE   1 
ATOM   588  N  NZ   . LYS A 1 37  ? 46.571 23.587 -1.257  1.00 38.93 ? 39  LYS A NZ   1 
ATOM   589  H  H    . LYS A 1 37  ? 45.920 26.859 3.760   1.00 27.43 ? 39  LYS A H    1 
ATOM   590  H  HA   . LYS A 1 37  ? 44.336 27.578 1.670   1.00 26.43 ? 39  LYS A HA   1 
ATOM   591  H  HB2  . LYS A 1 37  ? 44.264 25.083 2.986   1.00 24.13 ? 39  LYS A HB2  1 
ATOM   592  H  HB3  . LYS A 1 37  ? 43.443 25.462 1.684   1.00 24.13 ? 39  LYS A HB3  1 
ATOM   593  H  HG2  . LYS A 1 37  ? 46.255 25.255 1.664   1.00 27.07 ? 39  LYS A HG2  1 
ATOM   594  H  HG3  . LYS A 1 37  ? 45.308 24.045 1.253   1.00 27.07 ? 39  LYS A HG3  1 
ATOM   595  H  HD2  . LYS A 1 37  ? 44.519 25.230 -0.551  1.00 31.21 ? 39  LYS A HD2  1 
ATOM   596  H  HD3  . LYS A 1 37  ? 45.358 26.505 -0.112  1.00 31.21 ? 39  LYS A HD3  1 
ATOM   597  H  HE2  . LYS A 1 37  ? 46.466 25.501 -1.865  1.00 31.29 ? 39  LYS A HE2  1 
ATOM   598  H  HE3  . LYS A 1 37  ? 47.347 25.307 -0.562  1.00 31.29 ? 39  LYS A HE3  1 
ATOM   599  H  HZ1  . LYS A 1 37  ? 45.831 23.325 -1.677  1.00 31.86 ? 39  LYS A HZ1  1 
ATOM   600  H  HZ2  . LYS A 1 37  ? 47.276 23.390 -1.763  1.00 31.86 ? 39  LYS A HZ2  1 
ATOM   601  H  HZ3  . LYS A 1 37  ? 46.637 23.148 -0.486  1.00 31.86 ? 39  LYS A HZ3  1 
ATOM   602  N  N    . LYS A 1 38  ? 42.200 27.891 2.929   1.00 29.49 ? 40  LYS A N    1 
ATOM   603  C  CA   . LYS A 1 38  ? 41.075 28.362 3.735   1.00 28.41 ? 40  LYS A CA   1 
ATOM   604  C  C    . LYS A 1 38  ? 39.956 27.326 3.813   1.00 25.80 ? 40  LYS A C    1 
ATOM   605  O  O    . LYS A 1 38  ? 39.430 26.919 2.803   1.00 25.41 ? 40  LYS A O    1 
ATOM   606  C  CB   . LYS A 1 38  ? 40.536 29.674 3.170   1.00 32.45 ? 40  LYS A CB   1 
ATOM   607  C  CG   . LYS A 1 38  ? 39.291 30.173 3.887   1.00 34.76 ? 40  LYS A CG   1 
ATOM   608  C  CD   . LYS A 1 38  ? 38.989 31.628 3.566   1.00 35.78 ? 40  LYS A CD   1 
ATOM   609  C  CE   . LYS A 1 38  ? 37.583 31.996 4.028   1.00 39.48 ? 40  LYS A CE   1 
ATOM   610  N  NZ   . LYS A 1 38  ? 37.277 31.574 5.407   1.00 37.36 ? 40  LYS A NZ   1 
ATOM   611  H  H    . LYS A 1 38  ? 42.038 27.880 2.085   1.00 24.78 ? 40  LYS A H    1 
ATOM   612  H  HA   . LYS A 1 38  ? 41.386 28.532 4.637   1.00 24.46 ? 40  LYS A HA   1 
ATOM   613  H  HB2  . LYS A 1 38  ? 41.221 30.356 3.251   1.00 28.26 ? 40  LYS A HB2  1 
ATOM   614  H  HB3  . LYS A 1 38  ? 40.309 29.543 2.236   1.00 28.26 ? 40  LYS A HB3  1 
ATOM   615  H  HG2  . LYS A 1 38  ? 38.530 29.639 3.613   1.00 31.26 ? 40  LYS A HG2  1 
ATOM   616  H  HG3  . LYS A 1 38  ? 39.424 30.097 4.845   1.00 31.26 ? 40  LYS A HG3  1 
ATOM   617  H  HD2  . LYS A 1 38  ? 39.623 32.200 4.026   1.00 31.80 ? 40  LYS A HD2  1 
ATOM   618  H  HD3  . LYS A 1 38  ? 39.043 31.766 2.607   1.00 31.80 ? 40  LYS A HD3  1 
ATOM   619  H  HE2  . LYS A 1 38  ? 37.483 32.960 3.984   1.00 36.17 ? 40  LYS A HE2  1 
ATOM   620  H  HE3  . LYS A 1 38  ? 36.940 31.572 3.438   1.00 36.17 ? 40  LYS A HE3  1 
ATOM   621  H  HZ1  . LYS A 1 38  ? 36.447 31.814 5.621   1.00 34.62 ? 40  LYS A HZ1  1 
ATOM   622  H  HZ2  . LYS A 1 38  ? 37.350 30.690 5.478   1.00 34.62 ? 40  LYS A HZ2  1 
ATOM   623  H  HZ3  . LYS A 1 38  ? 37.845 31.957 5.976   1.00 34.62 ? 40  LYS A HZ3  1 
ATOM   624  N  N    . TYR A 1 39  ? 39.611 26.918 5.032   1.00 25.87 ? 41  TYR A N    1 
ATOM   625  C  CA   . TYR A 1 39  ? 38.507 26.005 5.274   1.00 22.01 ? 41  TYR A CA   1 
ATOM   626  C  C    . TYR A 1 39  ? 37.206 26.816 5.168   1.00 23.36 ? 41  TYR A C    1 
ATOM   627  O  O    . TYR A 1 39  ? 36.686 27.312 6.156   1.00 23.36 ? 41  TYR A O    1 
ATOM   628  C  CB   . TYR A 1 39  ? 38.607 25.334 6.645   1.00 20.77 ? 41  TYR A CB   1 
ATOM   629  C  CG   . TYR A 1 39  ? 37.619 24.205 6.805   1.00 17.70 ? 41  TYR A CG   1 
ATOM   630  C  CD1  . TYR A 1 39  ? 37.690 23.071 6.017   1.00 19.61 ? 41  TYR A CD1  1 
ATOM   631  C  CD2  . TYR A 1 39  ? 36.591 24.286 7.703   1.00 16.45 ? 41  TYR A CD2  1 
ATOM   632  C  CE1  . TYR A 1 39  ? 36.790 22.055 6.144   1.00 17.00 ? 41  TYR A CE1  1 
ATOM   633  C  CE2  . TYR A 1 39  ? 35.764 23.254 7.865   1.00 15.79 ? 41  TYR A CE2  1 
ATOM   634  C  CZ   . TYR A 1 39  ? 35.836 22.162 7.052   1.00 17.19 ? 41  TYR A CZ   1 
ATOM   635  O  OH   . TYR A 1 39  ? 34.914 21.166 7.210   1.00 17.08 ? 41  TYR A OH   1 
ATOM   636  H  H    . TYR A 1 39  ? 40.014 27.166 5.750   1.00 22.85 ? 41  TYR A H    1 
ATOM   637  H  HA   . TYR A 1 39  ? 38.499 25.316 4.591   1.00 19.85 ? 41  TYR A HA   1 
ATOM   638  H  HB2  . TYR A 1 39  ? 39.499 24.971 6.757   1.00 18.91 ? 41  TYR A HB2  1 
ATOM   639  H  HB3  . TYR A 1 39  ? 38.426 25.992 7.335   1.00 18.91 ? 41  TYR A HB3  1 
ATOM   640  H  HD1  . TYR A 1 39  ? 38.364 23.003 5.380   1.00 18.49 ? 41  TYR A HD1  1 
ATOM   641  H  HD2  . TYR A 1 39  ? 36.527 25.022 8.268   1.00 15.85 ? 41  TYR A HD2  1 
ATOM   642  H  HE1  . TYR A 1 39  ? 36.854 21.295 5.610   1.00 16.43 ? 41  TYR A HE1  1 
ATOM   643  H  HE2  . TYR A 1 39  ? 35.064 23.323 8.472   1.00 15.70 ? 41  TYR A HE2  1 
ATOM   644  H  HH   . TYR A 1 39  ? 34.372 21.369 7.819   1.00 17.48 ? 41  TYR A HH   1 
ATOM   645  N  N    . SER A 1 40  ? 36.670 26.939 3.963   1.00 21.84 ? 42  SER A N    1 
ATOM   646  C  CA   . SER A 1 40  ? 35.581 27.872 3.741   1.00 21.97 ? 42  SER A CA   1 
ATOM   647  C  C    . SER A 1 40  ? 34.243 27.168 3.752   1.00 21.39 ? 42  SER A C    1 
ATOM   648  O  O    . SER A 1 40  ? 34.172 25.953 3.725   1.00 19.98 ? 42  SER A O    1 
ATOM   649  C  CB   . SER A 1 40  ? 35.775 28.532 2.399   1.00 27.79 ? 42  SER A CB   1 
ATOM   650  O  OG   . SER A 1 40  ? 36.144 27.580 1.448   1.00 26.56 ? 42  SER A OG   1 
ATOM   651  H  H    . SER A 1 40  ? 36.916 26.500 3.265   1.00 19.77 ? 42  SER A H    1 
ATOM   652  H  HA   . SER A 1 40  ? 35.584 28.554 4.431   1.00 20.10 ? 42  SER A HA   1 
ATOM   653  H  HB2  . SER A 1 40  ? 34.943 28.949 2.126   1.00 25.39 ? 42  SER A HB2  1 
ATOM   654  H  HB3  . SER A 1 40  ? 36.476 29.198 2.471   1.00 25.39 ? 42  SER A HB3  1 
ATOM   655  H  HG   . SER A 1 40  ? 35.545 26.995 1.380   1.00 24.09 ? 42  SER A HG   1 
ATOM   656  N  N    . TRP A 1 41  ? 33.184 27.952 3.715   1.00 20.28 ? 43  TRP A N    1 
ATOM   657  C  CA   . TRP A 1 41  ? 31.848 27.393 3.652   1.00 19.70 ? 43  TRP A CA   1 
ATOM   658  C  C    . TRP A 1 41  ? 31.620 26.476 2.453   1.00 16.95 ? 43  TRP A C    1 
ATOM   659  O  O    . TRP A 1 41  ? 30.888 25.482 2.583   1.00 16.81 ? 43  TRP A O    1 
ATOM   660  C  CB   . TRP A 1 41  ? 30.771 28.485 3.772   1.00 19.19 ? 43  TRP A CB   1 
ATOM   661  C  CG   . TRP A 1 41  ? 30.425 28.717 5.205   1.00 23.00 ? 43  TRP A CG   1 
ATOM   662  C  CD1  . TRP A 1 41  ? 30.814 29.765 6.018   1.00 24.59 ? 43  TRP A CD1  1 
ATOM   663  C  CD2  . TRP A 1 41  ? 29.656 27.849 6.029   1.00 18.88 ? 43  TRP A CD2  1 
ATOM   664  N  NE1  . TRP A 1 41  ? 30.305 29.590 7.270   1.00 23.29 ? 43  TRP A NE1  1 
ATOM   665  C  CE2  . TRP A 1 41  ? 29.601 28.416 7.314   1.00 20.77 ? 43  TRP A CE2  1 
ATOM   666  C  CE3  . TRP A 1 41  ? 28.977 26.652 5.789   1.00 21.27 ? 43  TRP A CE3  1 
ATOM   667  C  CZ2  . TRP A 1 41  ? 28.913 27.821 8.360   1.00 21.74 ? 43  TRP A CZ2  1 
ATOM   668  C  CZ3  . TRP A 1 41  ? 28.290 26.071 6.808   1.00 18.83 ? 43  TRP A CZ3  1 
ATOM   669  C  CH2  . TRP A 1 41  ? 28.254 26.651 8.087   1.00 22.60 ? 43  TRP A CH2  1 
ATOM   670  H  H    . TRP A 1 41  ? 33.209 28.812 3.725   1.00 18.66 ? 43  TRP A H    1 
ATOM   671  H  HA   . TRP A 1 41  ? 31.744 26.832 4.436   1.00 18.70 ? 43  TRP A HA   1 
ATOM   672  H  HB2  . TRP A 1 41  ? 31.107 29.314 3.398   1.00 18.21 ? 43  TRP A HB2  1 
ATOM   673  H  HB3  . TRP A 1 41  ? 29.970 28.202 3.305   1.00 18.21 ? 43  TRP A HB3  1 
ATOM   674  H  HD1  . TRP A 1 41  ? 31.350 30.477 5.753   1.00 23.38 ? 43  TRP A HD1  1 
ATOM   675  H  HE1  . TRP A 1 41  ? 30.435 30.117 7.937   1.00 22.35 ? 43  TRP A HE1  1 
ATOM   676  H  HE3  . TRP A 1 41  ? 29.002 26.255 4.948   1.00 21.45 ? 43  TRP A HE3  1 
ATOM   677  H  HZ2  . TRP A 1 41  ? 28.870 28.218 9.200   1.00 21.69 ? 43  TRP A HZ2  1 
ATOM   678  H  HZ3  . TRP A 1 41  ? 27.852 25.264 6.660   1.00 19.32 ? 43  TRP A HZ3  1 
ATOM   679  H  HH2  . TRP A 1 41  ? 27.780 26.226 8.766   1.00 22.98 ? 43  TRP A HH2  1 
ATOM   680  N  N    . ASP A 1 42  ? 32.230 26.731 1.313   1.00 22.85 ? 44  ASP A N    1 
ATOM   681  C  CA   . ASP A 1 42  ? 32.045 25.835 0.197   1.00 23.87 ? 44  ASP A CA   1 
ATOM   682  C  C    . ASP A 1 42  ? 32.533 24.412 0.500   1.00 21.91 ? 44  ASP A C    1 
ATOM   683  O  O    . ASP A 1 42  ? 31.804 23.456 0.240   1.00 24.52 ? 44  ASP A O    1 
ATOM   684  C  CB   . ASP A 1 42  ? 32.627 26.414 -1.104  1.00 28.42 ? 44  ASP A CB   1 
ATOM   685  C  CG   . ASP A 1 42  ? 34.156 26.466 -1.131  1.00 32.29 ? 44  ASP A CG   1 
ATOM   686  O  OD1  . ASP A 1 42  ? 34.795 26.417 -0.056  1.00 36.78 ? 44  ASP A OD1  1 
ATOM   687  O  OD2  . ASP A 1 42  ? 34.721 26.562 -2.250  1.00 41.40 ? 44  ASP A OD2  1 
ATOM   688  H  H    . ASP A 1 42  ? 32.746 27.402 1.162   1.00 19.27 ? 44  ASP A H    1 
ATOM   689  H  HA   . ASP A 1 42  ? 31.089 25.762 0.051   1.00 20.38 ? 44  ASP A HA   1 
ATOM   690  H  HB2  . ASP A 1 42  ? 32.336 25.863 -1.848  1.00 24.29 ? 44  ASP A HB2  1 
ATOM   691  H  HB3  . ASP A 1 42  ? 32.298 27.319 -1.218  1.00 24.29 ? 44  ASP A HB3  1 
ATOM   692  N  N    . VAL A 1 43  ? 33.722 24.299 1.104   1.00 16.17 ? 45  VAL A N    1 
ATOM   693  C  CA   . VAL A 1 43  ? 34.272 23.038 1.550   1.00 16.90 ? 45  VAL A CA   1 
ATOM   694  C  C    . VAL A 1 43  ? 33.421 22.427 2.660   1.00 15.05 ? 45  VAL A C    1 
ATOM   695  O  O    . VAL A 1 43  ? 33.078 21.253 2.603   1.00 13.31 ? 45  VAL A O    1 
ATOM   696  C  CB   . VAL A 1 43  ? 35.747 23.190 2.048   1.00 18.27 ? 45  VAL A CB   1 
ATOM   697  C  CG1  . VAL A 1 43  ? 36.302 21.854 2.419   1.00 20.94 ? 45  VAL A CG1  1 
ATOM   698  C  CG2  . VAL A 1 43  ? 36.637 23.805 0.992   1.00 24.29 ? 45  VAL A CG2  1 
ATOM   699  H  H    . VAL A 1 43  ? 34.236 24.969 1.266   1.00 14.87 ? 45  VAL A H    1 
ATOM   700  H  HA   . VAL A 1 43  ? 34.274 22.418 0.804   1.00 15.65 ? 45  VAL A HA   1 
ATOM   701  H  HB   . VAL A 1 43  ? 35.765 23.758 2.833   1.00 16.43 ? 45  VAL A HB   1 
ATOM   702  H  HG11 . VAL A 1 43  ? 37.216 21.966 2.725   1.00 19.06 ? 45  VAL A HG11 1 
ATOM   703  H  HG12 . VAL A 1 43  ? 35.760 21.473 3.128   1.00 19.06 ? 45  VAL A HG12 1 
ATOM   704  H  HG13 . VAL A 1 43  ? 36.282 21.276 1.640   1.00 19.06 ? 45  VAL A HG13 1 
ATOM   705  H  HG21 . VAL A 1 43  ? 37.538 23.879 1.344   1.00 21.71 ? 45  VAL A HG21 1 
ATOM   706  H  HG22 . VAL A 1 43  ? 36.634 23.236 0.207   1.00 21.71 ? 45  VAL A HG22 1 
ATOM   707  H  HG23 . VAL A 1 43  ? 36.296 24.684 0.766   1.00 21.71 ? 45  VAL A HG23 1 
ATOM   708  N  N    . LYS A 1 44  ? 33.044 23.216 3.665   1.00 13.80 ? 46  LYS A N    1 
ATOM   709  C  CA   . LYS A 1 44  ? 32.264 22.685 4.766   1.00 14.96 ? 46  LYS A CA   1 
ATOM   710  C  C    . LYS A 1 44  ? 30.967 22.064 4.286   1.00 15.21 ? 46  LYS A C    1 
ATOM   711  O  O    . LYS A 1 44  ? 30.558 21.029 4.759   1.00 13.04 ? 46  LYS A O    1 
ATOM   712  C  CB   . LYS A 1 44  ? 31.970 23.809 5.775   1.00 17.81 ? 46  LYS A CB   1 
ATOM   713  C  CG   . LYS A 1 44  ? 31.457 23.351 7.070   1.00 16.75 ? 46  LYS A CG   1 
ATOM   714  C  CD   . LYS A 1 44  ? 31.356 24.435 8.081   1.00 16.35 ? 46  LYS A CD   1 
ATOM   715  C  CE   . LYS A 1 44  ? 30.782 23.912 9.420   1.00 16.62 ? 46  LYS A CE   1 
ATOM   716  N  NZ   . LYS A 1 44  ? 31.764 23.011 10.265  1.00 14.00 ? 46  LYS A NZ   1 
ATOM   717  H  H    . LYS A 1 44  ? 33.227 24.054 3.727   1.00 12.67 ? 46  LYS A H    1 
ATOM   718  H  HA   . LYS A 1 44  ? 32.778 21.999 5.219   1.00 14.29 ? 46  LYS A HA   1 
ATOM   719  H  HB2  . LYS A 1 44  ? 32.791 24.298 5.942   1.00 17.17 ? 46  LYS A HB2  1 
ATOM   720  H  HB3  . LYS A 1 44  ? 31.308 24.405 5.391   1.00 17.17 ? 46  LYS A HB3  1 
ATOM   721  H  HG2  . LYS A 1 44  ? 30.570 22.980 6.942   1.00 16.41 ? 46  LYS A HG2  1 
ATOM   722  H  HG3  . LYS A 1 44  ? 32.052 22.671 7.421   1.00 16.41 ? 46  LYS A HG3  1 
ATOM   723  H  HD2  . LYS A 1 44  ? 32.239 24.798 8.250   1.00 15.92 ? 46  LYS A HD2  1 
ATOM   724  H  HD3  . LYS A 1 44  ? 30.766 25.129 7.748   1.00 15.92 ? 46  LYS A HD3  1 
ATOM   725  H  HE2  . LYS A 1 44  ? 30.539 24.674 9.969   1.00 16.43 ? 46  LYS A HE2  1 
ATOM   726  H  HE3  . LYS A 1 44  ? 29.991 23.383 9.230   1.00 16.43 ? 46  LYS A HE3  1 
ATOM   727  H  HZ1  . LYS A 1 44  ? 31.365 22.750 11.017  1.00 13.68 ? 46  LYS A HZ1  1 
ATOM   728  H  HZ2  . LYS A 1 44  ? 31.996 22.292 9.796   1.00 13.68 ? 46  LYS A HZ2  1 
ATOM   729  H  HZ3  . LYS A 1 44  ? 32.497 23.471 10.471  1.00 13.68 ? 46  LYS A HZ3  1 
ATOM   730  N  N    . SER A 1 45  ? 30.344 22.691 3.279   1.00 12.72 ? 47  SER A N    1 
ATOM   731  C  CA   . SER A 1 45  ? 29.084 22.187 2.747   1.00 12.03 ? 47  SER A CA   1 
ATOM   732  C  C    . SER A 1 45  ? 29.196 20.808 2.154   1.00 13.33 ? 47  SER A C    1 
ATOM   733  O  O    . SER A 1 45  ? 28.242 20.098 2.075   1.00 12.84 ? 47  SER A O    1 
ATOM   734  C  CB   . SER A 1 45  ? 28.528 23.031 1.609   1.00 17.81 ? 47  SER A CB   1 
ATOM   735  O  OG   . SER A 1 45  ? 28.439 24.370 1.995   1.00 25.06 ? 47  SER A OG   1 
ATOM   736  H  H    . SER A 1 45  ? 30.633 23.403 2.893   1.00 12.14 ? 47  SER A H    1 
ATOM   737  H  HA   . SER A 1 45  ? 28.425 22.161 3.458   1.00 11.79 ? 47  SER A HA   1 
ATOM   738  H  HB2  . SER A 1 45  ? 29.120 22.960 0.844   1.00 17.48 ? 47  SER A HB2  1 
ATOM   739  H  HB3  . SER A 1 45  ? 27.644 22.708 1.377   1.00 17.48 ? 47  SER A HB3  1 
ATOM   740  H  HG   . SER A 1 45  ? 29.200 24.661 2.201   1.00 24.59 ? 47  SER A HG   1 
ATOM   741  N  N    . LEU A 1 46  ? 30.374 20.430 1.716   1.00 9.57  ? 48  LEU A N    1 
ATOM   742  C  CA   . LEU A 1 46  ? 30.599 19.170 1.085   1.00 10.28 ? 48  LEU A CA   1 
ATOM   743  C  C    . LEU A 1 46  ? 30.725 18.086 2.100   1.00 9.23  ? 48  LEU A C    1 
ATOM   744  O  O    . LEU A 1 46  ? 30.543 16.906 1.767   1.00 10.98 ? 48  LEU A O    1 
ATOM   745  C  CB   . LEU A 1 46  ? 31.904 19.181 0.258   1.00 12.02 ? 48  LEU A CB   1 
ATOM   746  C  CG   . LEU A 1 46  ? 31.924 20.228 -0.809  1.00 12.41 ? 48  LEU A CG   1 
ATOM   747  C  CD1  . LEU A 1 46  ? 33.339 20.203 -1.413  1.00 15.48 ? 48  LEU A CD1  1 
ATOM   748  C  CD2  . LEU A 1 46  ? 30.870 19.981 -1.889  1.00 14.26 ? 48  LEU A CD2  1 
ATOM   749  H  H    . LEU A 1 46  ? 31.083 20.913 1.779   1.00 9.90  ? 48  LEU A H    1 
ATOM   750  H  HA   . LEU A 1 46  ? 29.858 18.962 0.496   1.00 10.48 ? 48  LEU A HA   1 
ATOM   751  H  HB2  . LEU A 1 46  ? 32.651 19.349 0.853   1.00 11.65 ? 48  LEU A HB2  1 
ATOM   752  H  HB3  . LEU A 1 46  ? 32.010 18.317 -0.170  1.00 11.65 ? 48  LEU A HB3  1 
ATOM   753  H  HG   . LEU A 1 46  ? 31.769 21.100 -0.415  1.00 11.80 ? 48  LEU A HG   1 
ATOM   754  H  HD11 . LEU A 1 46  ? 33.395 20.871 -2.114  1.00 14.18 ? 48  LEU A HD11 1 
ATOM   755  H  HD12 . LEU A 1 46  ? 33.983 20.400 -0.715  1.00 14.18 ? 48  LEU A HD12 1 
ATOM   756  H  HD13 . LEU A 1 46  ? 33.509 19.322 -1.781  1.00 14.18 ? 48  LEU A HD13 1 
ATOM   757  H  HD21 . LEU A 1 46  ? 30.927 20.686 -2.552  1.00 13.83 ? 48  LEU A HD21 1 
ATOM   758  H  HD22 . LEU A 1 46  ? 31.038 19.121 -2.304  1.00 13.83 ? 48  LEU A HD22 1 
ATOM   759  H  HD23 . LEU A 1 46  ? 29.991 19.985 -1.477  1.00 13.83 ? 48  LEU A HD23 1 
ATOM   760  N  N    . VAL A 1 47  ? 31.117 18.376 3.333   1.00 10.42 ? 49  VAL A N    1 
ATOM   761  C  CA   . VAL A 1 47  ? 31.538 17.334 4.274   1.00 10.22 ? 49  VAL A CA   1 
ATOM   762  C  C    . VAL A 1 47  ? 30.622 17.172 5.495   1.00 9.88  ? 49  VAL A C    1 
ATOM   763  O  O    . VAL A 1 47  ? 30.642 16.137 6.141   1.00 10.78 ? 49  VAL A O    1 
ATOM   764  C  CB   . VAL A 1 47  ? 33.045 17.494 4.730   1.00 10.78 ? 49  VAL A CB   1 
ATOM   765  C  CG1  . VAL A 1 47  ? 33.912 17.517 3.521   1.00 15.39 ? 49  VAL A CG1  1 
ATOM   766  C  CG2  . VAL A 1 47  ? 33.233 18.731 5.463   1.00 12.50 ? 49  VAL A CG2  1 
ATOM   767  H  H    . VAL A 1 47  ? 31.151 19.173 3.656   1.00 10.68 ? 49  VAL A H    1 
ATOM   768  H  HA   . VAL A 1 47  ? 31.493 16.491 3.796   1.00 10.39 ? 49  VAL A HA   1 
ATOM   769  H  HB   . VAL A 1 47  ? 33.305 16.748 5.293   1.00 10.50 ? 49  VAL A HB   1 
ATOM   770  H  HG11 . VAL A 1 47  ? 34.837 17.615 3.798   1.00 14.65 ? 49  VAL A HG11 1 
ATOM   771  H  HG12 . VAL A 1 47  ? 33.799 16.685 3.035   1.00 14.65 ? 49  VAL A HG12 1 
ATOM   772  H  HG13 . VAL A 1 47  ? 33.653 18.266 2.961   1.00 14.65 ? 49  VAL A HG13 1 
ATOM   773  H  HG21 . VAL A 1 47  ? 34.163 18.801 5.728   1.00 12.27 ? 49  VAL A HG21 1 
ATOM   774  H  HG22 . VAL A 1 47  ? 32.995 19.476 4.890   1.00 12.27 ? 49  VAL A HG22 1 
ATOM   775  H  HG23 . VAL A 1 47  ? 32.664 18.721 6.248   1.00 12.27 ? 49  VAL A HG23 1 
ATOM   776  N  N    . MET A 1 48  ? 29.829 18.174 5.816   1.00 10.44 ? 50  MET A N    1 
ATOM   777  C  CA   . MET A 1 48  ? 28.863 17.962 6.943   1.00 11.06 ? 50  MET A CA   1 
ATOM   778  C  C    . MET A 1 48  ? 27.972 16.778 6.633   1.00 9.86  ? 50  MET A C    1 
ATOM   779  O  O    . MET A 1 48  ? 27.503 16.686 5.527   1.00 9.40  ? 50  MET A O    1 
ATOM   780  C  CB   . MET A 1 48  ? 28.040 19.211 7.129   1.00 9.68  ? 50  MET A CB   1 
ATOM   781  C  CG   . MET A 1 48  ? 28.870 20.333 7.686   1.00 9.65  ? 50  MET A CG   1 
ATOM   782  S  SD   . MET A 1 48  ? 27.822 21.674 8.308   1.00 16.34 ? 50  MET A SD   1 
ATOM   783  C  CE   . MET A 1 48  ? 27.761 22.235 6.776   1.00 11.00 ? 50  MET A CE   1 
ATOM   784  H  H    . MET A 1 48  ? 29.808 18.947 5.441   1.00 10.63 ? 50  MET A H    1 
ATOM   785  H  HA   . MET A 1 48  ? 29.354 17.792 7.762   1.00 11.49 ? 50  MET A HA   1 
ATOM   786  H  HB2  . MET A 1 48  ? 27.685 19.492 6.271   1.00 10.30 ? 50  MET A HB2  1 
ATOM   787  H  HB3  . MET A 1 48  ? 27.317 19.030 7.749   1.00 10.30 ? 50  MET A HB3  1 
ATOM   788  H  HG2  . MET A 1 48  ? 29.408 19.999 8.422   1.00 10.11 ? 50  MET A HG2  1 
ATOM   789  H  HG3  . MET A 1 48  ? 29.440 20.689 6.987   1.00 10.11 ? 50  MET A HG3  1 
ATOM   790  H  HE1  . MET A 1 48  ? 27.216 23.038 6.755   1.00 11.53 ? 50  MET A HE1  1 
ATOM   791  H  HE2  . MET A 1 48  ? 28.661 22.438 6.478   1.00 11.53 ? 50  MET A HE2  1 
ATOM   792  H  HE3  . MET A 1 48  ? 27.369 21.555 6.206   1.00 11.53 ? 50  MET A HE3  1 
ATOM   793  N  N    . GLY A 1 49  ? 27.861 15.866 7.554   1.00 10.33 ? 51  GLY A N    1 
ATOM   794  C  CA   . GLY A 1 49  ? 27.044 14.667 7.361   1.00 11.32 ? 51  GLY A CA   1 
ATOM   795  C  C    . GLY A 1 49  ? 27.790 13.431 6.890   1.00 11.05 ? 51  GLY A C    1 
ATOM   796  O  O    . GLY A 1 49  ? 27.246 12.321 6.949   1.00 11.97 ? 51  GLY A O    1 
ATOM   797  H  H    . GLY A 1 49  ? 28.249 15.903 8.321   1.00 11.03 ? 51  GLY A H    1 
ATOM   798  H  HA2  . GLY A 1 49  ? 26.609 14.447 8.200   1.00 11.97 ? 51  GLY A HA2  1 
ATOM   799  H  HA3  . GLY A 1 49  ? 26.353 14.862 6.709   1.00 11.97 ? 51  GLY A HA3  1 
ATOM   800  N  N    . LYS A 1 50  ? 29.052 13.616 6.503   1.00 10.23 ? 52  LYS A N    1 
ATOM   801  C  CA   . LYS A 1 50  ? 29.915 12.510 6.096   1.00 10.87 ? 52  LYS A CA   1 
ATOM   802  C  C    . LYS A 1 50  ? 30.550 11.894 7.345   1.00 11.29 ? 52  LYS A C    1 
ATOM   803  O  O    . LYS A 1 50  ? 30.725 12.559 8.364   1.00 14.27 ? 52  LYS A O    1 
ATOM   804  C  CB   . LYS A 1 50  ? 31.048 13.012 5.203   1.00 12.42 ? 52  LYS A CB   1 
ATOM   805  C  CG   . LYS A 1 50  ? 30.629 13.456 3.802   1.00 13.06 ? 52  LYS A CG   1 
ATOM   806  C  CD   . LYS A 1 50  ? 30.444 12.372 2.744   1.00 14.24 ? 52  LYS A CD   1 
ATOM   807  C  CE   . LYS A 1 50  ? 29.934 12.958 1.466   1.00 14.65 ? 52  LYS A CE   1 
ATOM   808  N  NZ   . LYS A 1 50  ? 29.820 11.831 0.512   1.00 16.37 ? 52  LYS A NZ   1 
ATOM   809  H  H    . LYS A 1 50  ? 29.436 14.385 6.467   1.00 10.86 ? 52  LYS A H    1 
ATOM   810  H  HA   . LYS A 1 50  ? 29.404 11.834 5.624   1.00 11.05 ? 52  LYS A HA   1 
ATOM   811  H  HB2  . LYS A 1 50  ? 31.467 13.772 5.636   1.00 12.37 ? 52  LYS A HB2  1 
ATOM   812  H  HB3  . LYS A 1 50  ? 31.697 12.299 5.100   1.00 12.37 ? 52  LYS A HB3  1 
ATOM   813  H  HG2  . LYS A 1 50  ? 29.784 13.927 3.877   1.00 13.13 ? 52  LYS A HG2  1 
ATOM   814  H  HG3  . LYS A 1 50  ? 31.304 14.067 3.468   1.00 13.13 ? 52  LYS A HG3  1 
ATOM   815  H  HD2  . LYS A 1 50  ? 31.297 11.946 2.566   1.00 14.04 ? 52  LYS A HD2  1 
ATOM   816  H  HD3  . LYS A 1 50  ? 29.800 11.719 3.060   1.00 14.04 ? 52  LYS A HD3  1 
ATOM   817  H  HE2  . LYS A 1 50  ? 29.058 13.352 1.602   1.00 14.59 ? 52  LYS A HE2  1 
ATOM   818  H  HE3  . LYS A 1 50  ? 30.563 13.609 1.119   1.00 14.59 ? 52  LYS A HE3  1 
ATOM   819  H  HZ1  . LYS A 1 50  ? 29.518 12.125 -0.271  1.00 15.97 ? 52  LYS A HZ1  1 
ATOM   820  H  HZ2  . LYS A 1 50  ? 30.616 11.453 0.392   1.00 15.97 ? 52  LYS A HZ2  1 
ATOM   821  H  HZ3  . LYS A 1 50  ? 29.255 11.221 0.829   1.00 15.97 ? 52  LYS A HZ3  1 
ATOM   822  N  N    . LYS A 1 51  ? 30.954 10.649 7.215   1.00 13.84 ? 53  LYS A N    1 
ATOM   823  C  CA   . LYS A 1 51  ? 31.713 10.000 8.262   1.00 14.54 ? 53  LYS A CA   1 
ATOM   824  C  C    . LYS A 1 51  ? 33.091 10.668 8.268   1.00 12.36 ? 53  LYS A C    1 
ATOM   825  O  O    . LYS A 1 51  ? 33.532 11.294 7.300   1.00 13.48 ? 53  LYS A O    1 
ATOM   826  C  CB   . LYS A 1 51  ? 31.923 8.521  7.981   1.00 16.75 ? 53  LYS A CB   1 
ATOM   827  C  CG   . LYS A 1 51  ? 30.724 7.679  7.918   1.00 17.83 ? 53  LYS A CG   1 
ATOM   828  C  CD   . LYS A 1 51  ? 31.166 6.253  7.769   1.00 24.05 ? 53  LYS A CD   1 
ATOM   829  C  CE   . LYS A 1 51  ? 29.993 5.341  7.621   1.00 24.00 ? 53  LYS A CE   1 
ATOM   830  N  NZ   . LYS A 1 51  ? 30.375 3.909  7.854   1.00 31.40 ? 53  LYS A NZ   1 
ATOM   831  H  H    . LYS A 1 51  ? 30.801 10.154 6.529   1.00 14.35 ? 53  LYS A H    1 
ATOM   832  H  HA   . LYS A 1 51  ? 31.286 10.117 9.125   1.00 14.64 ? 53  LYS A HA   1 
ATOM   833  H  HB2  . LYS A 1 51  ? 32.376 8.438  7.127   1.00 16.27 ? 53  LYS A HB2  1 
ATOM   834  H  HB3  . LYS A 1 51  ? 32.490 8.159  8.680   1.00 16.27 ? 53  LYS A HB3  1 
ATOM   835  H  HG2  . LYS A 1 51  ? 30.215 7.767  8.739   1.00 17.34 ? 53  LYS A HG2  1 
ATOM   836  H  HG3  . LYS A 1 51  ? 30.187 7.925  7.149   1.00 17.34 ? 53  LYS A HG3  1 
ATOM   837  H  HD2  . LYS A 1 51  ? 31.720 6.169  6.978   1.00 22.83 ? 53  LYS A HD2  1 
ATOM   838  H  HD3  . LYS A 1 51  ? 31.663 5.986  8.559   1.00 22.83 ? 53  LYS A HD3  1 
ATOM   839  H  HE2  . LYS A 1 51  ? 29.315 5.584  8.270   1.00 22.65 ? 53  LYS A HE2  1 
ATOM   840  H  HE3  . LYS A 1 51  ? 29.640 5.419  6.721   1.00 22.65 ? 53  LYS A HE3  1 
ATOM   841  H  HZ1  . LYS A 1 51  ? 29.661 3.385  7.760   1.00 29.22 ? 53  LYS A HZ1  1 
ATOM   842  H  HZ2  . LYS A 1 51  ? 30.995 3.660  7.266   1.00 29.22 ? 53  LYS A HZ2  1 
ATOM   843  H  HZ3  . LYS A 1 51  ? 30.700 3.811  8.677   1.00 29.22 ? 53  LYS A HZ3  1 
ATOM   844  N  N    . ALA A 1 52  ? 33.816 10.537 9.371   1.00 14.52 ? 54  ALA A N    1 
ATOM   845  C  CA   . ALA A 1 52  ? 35.045 11.326 9.567   1.00 13.76 ? 54  ALA A CA   1 
ATOM   846  C  C    . ALA A 1 52  ? 36.095 11.078 8.491   1.00 14.25 ? 54  ALA A C    1 
ATOM   847  O  O    . ALA A 1 52  ? 36.679 12.024 7.989   1.00 16.22 ? 54  ALA A O    1 
ATOM   848  C  CB   . ALA A 1 52  ? 35.652 11.071 10.943  1.00 17.61 ? 54  ALA A CB   1 
ATOM   849  H  H    . ALA A 1 52  ? 33.628 10.005 10.020  1.00 14.22 ? 54  ALA A H    1 
ATOM   850  H  HA   . ALA A 1 52  ? 34.809 12.266 9.527   1.00 13.27 ? 54  ALA A HA   1 
ATOM   851  H  HB1  . ALA A 1 52  ? 36.456 11.605 11.036  1.00 16.82 ? 54  ALA A HB1  1 
ATOM   852  H  HB2  . ALA A 1 52  ? 35.007 11.321 11.623  1.00 16.82 ? 54  ALA A HB2  1 
ATOM   853  H  HB3  . ALA A 1 52  ? 35.869 10.129 11.022  1.00 16.82 ? 54  ALA A HB3  1 
ATOM   854  N  N    . LEU A 1 53  ? 36.326 9.817  8.155   1.00 17.85 ? 55  LEU A N    1 
ATOM   855  C  CA   . LEU A 1 53  ? 37.294 9.487  7.133   1.00 18.51 ? 55  LEU A CA   1 
ATOM   856  C  C    . LEU A 1 53  ? 36.862 10.009 5.740   1.00 18.10 ? 55  LEU A C    1 
ATOM   857  O  O    . LEU A 1 53  ? 37.690 10.453 4.942   1.00 17.34 ? 55  LEU A O    1 
ATOM   858  C  CB   . LEU A 1 53  ? 37.569 7.973  7.116   1.00 22.75 ? 55  LEU A CB   1 
ATOM   859  C  CG   . LEU A 1 53  ? 38.521 7.469  8.217   1.00 20.94 ? 55  LEU A CG   1 
ATOM   860  C  CD1  . LEU A 1 53  ? 38.451 5.973  8.329   1.00 26.71 ? 55  LEU A CD1  1 
ATOM   861  C  CD2  . LEU A 1 53  ? 39.957 7.927  7.935   1.00 24.43 ? 55  LEU A CD2  1 
ATOM   862  H  H    . LEU A 1 53  ? 35.934 9.136  8.506   1.00 16.09 ? 55  LEU A H    1 
ATOM   863  H  HA   . LEU A 1 53  ? 38.129 9.927  7.356   1.00 16.14 ? 55  LEU A HA   1 
ATOM   864  H  HB2  . LEU A 1 53  ? 36.726 7.506  7.222   1.00 19.69 ? 55  LEU A HB2  1 
ATOM   865  H  HB3  . LEU A 1 53  ? 37.963 7.742  6.261   1.00 19.69 ? 55  LEU A HB3  1 
ATOM   866  H  HG   . LEU A 1 53  ? 38.247 7.846  9.068   1.00 17.30 ? 55  LEU A HG   1 
ATOM   867  H  HD11 . LEU A 1 53  ? 39.058 5.681  9.027   1.00 22.44 ? 55  LEU A HD11 1 
ATOM   868  H  HD12 . LEU A 1 53  ? 37.542 5.716  8.550   1.00 22.44 ? 55  LEU A HD12 1 
ATOM   869  H  HD13 . LEU A 1 53  ? 38.709 5.581  7.480   1.00 22.44 ? 55  LEU A HD13 1 
ATOM   870  H  HD21 . LEU A 1 53  ? 40.537 7.598  8.640   1.00 20.21 ? 55  LEU A HD21 1 
ATOM   871  H  HD22 . LEU A 1 53  ? 40.241 7.570  7.079   1.00 20.21 ? 55  LEU A HD22 1 
ATOM   872  H  HD23 . LEU A 1 53  ? 39.980 8.897  7.913   1.00 20.21 ? 55  LEU A HD23 1 
ATOM   873  N  N    . GLU A 1 54  ? 35.550 9.972  5.461   1.00 16.40 ? 56  GLU A N    1 
ATOM   874  C  CA   . GLU A 1 54  ? 35.005 10.465 4.197   1.00 14.52 ? 56  GLU A CA   1 
ATOM   875  C  C    . GLU A 1 54  ? 35.218 11.970 4.091   1.00 12.74 ? 56  GLU A C    1 
ATOM   876  O  O    . GLU A 1 54  ? 35.648 12.496 3.051   1.00 15.06 ? 56  GLU A O    1 
ATOM   877  C  CB   . GLU A 1 54  ? 33.497 10.167 4.147   1.00 16.55 ? 56  GLU A CB   1 
ATOM   878  C  CG   . GLU A 1 54  ? 33.150 8.725  4.009   1.00 16.90 ? 56  GLU A CG   1 
ATOM   879  C  CD   . GLU A 1 54  ? 31.613 8.447  4.113   1.00 19.75 ? 56  GLU A CD   1 
ATOM   880  O  OE1  . GLU A 1 54  ? 30.859 9.220  4.710   1.00 17.71 ? 56  GLU A OE1  1 
ATOM   881  O  OE2  . GLU A 1 54  ? 31.159 7.381  3.621   1.00 23.55 ? 56  GLU A OE2  1 
ATOM   882  H  H    . GLU A 1 54  ? 34.953 9.661  5.997   1.00 14.84 ? 56  GLU A H    1 
ATOM   883  H  HA   . GLU A 1 54  ? 35.442 10.027 3.449   1.00 13.22 ? 56  GLU A HA   1 
ATOM   884  H  HB2  . GLU A 1 54  ? 33.091 10.489 4.968   1.00 15.75 ? 56  GLU A HB2  1 
ATOM   885  H  HB3  . GLU A 1 54  ? 33.113 10.635 3.389   1.00 15.75 ? 56  GLU A HB3  1 
ATOM   886  H  HG2  . GLU A 1 54  ? 33.452 8.411  3.142   1.00 15.73 ? 56  GLU A HG2  1 
ATOM   887  H  HG3  . GLU A 1 54  ? 33.592 8.226  4.714   1.00 15.73 ? 56  GLU A HG3  1 
ATOM   888  N  N    . ALA A 1 55  ? 34.876 12.658 5.173   1.00 13.91 ? 57  ALA A N    1 
ATOM   889  C  CA   . ALA A 1 55  ? 35.055 14.110 5.241   1.00 13.65 ? 57  ALA A CA   1 
ATOM   890  C  C    . ALA A 1 55  ? 36.514 14.482 5.032   1.00 13.16 ? 57  ALA A C    1 
ATOM   891  O  O    . ALA A 1 55  ? 36.843 15.376 4.283   1.00 14.70 ? 57  ALA A O    1 
ATOM   892  C  CB   . ALA A 1 55  ? 34.577 14.610 6.545   1.00 14.13 ? 57  ALA A CB   1 
ATOM   893  H  H    . ALA A 1 55  ? 34.538 12.312 5.884   1.00 13.02 ? 57  ALA A H    1 
ATOM   894  H  HA   . ALA A 1 55  ? 34.530 14.530 4.542   1.00 13.00 ? 57  ALA A HA   1 
ATOM   895  H  HB1  . ALA A 1 55  ? 34.701 15.572 6.578   1.00 13.87 ? 57  ALA A HB1  1 
ATOM   896  H  HB2  . ALA A 1 55  ? 33.637 14.394 6.640   1.00 13.87 ? 57  ALA A HB2  1 
ATOM   897  H  HB3  . ALA A 1 55  ? 35.088 14.186 7.252   1.00 13.87 ? 57  ALA A HB3  1 
ATOM   898  N  N    . ALA A 1 56  ? 37.412 13.803 5.739   1.00 14.36 ? 58  ALA A N    1 
ATOM   899  C  CA   . ALA A 1 56  ? 38.832 14.070 5.645   1.00 14.91 ? 58  ALA A CA   1 
ATOM   900  C  C    . ALA A 1 56  ? 39.356 13.935 4.207   1.00 13.84 ? 58  ALA A C    1 
ATOM   901  O  O    . ALA A 1 56  ? 40.062 14.827 3.716   1.00 16.35 ? 58  ALA A O    1 
ATOM   902  C  CB   . ALA A 1 56  ? 39.602 13.157 6.625   1.00 15.90 ? 58  ALA A CB   1 
ATOM   903  H  H    . ALA A 1 56  ? 37.214 13.171 6.288   1.00 13.56 ? 58  ALA A H    1 
ATOM   904  H  HA   . ALA A 1 56  ? 38.988 14.986 5.922   1.00 13.43 ? 58  ALA A HA   1 
ATOM   905  H  HB1  . ALA A 1 56  ? 40.551 13.345 6.552   1.00 13.95 ? 58  ALA A HB1  1 
ATOM   906  H  HB2  . ALA A 1 56  ? 39.297 13.335 7.528   1.00 13.95 ? 58  ALA A HB2  1 
ATOM   907  H  HB3  . ALA A 1 56  ? 39.430 12.230 6.394   1.00 13.95 ? 58  ALA A HB3  1 
ATOM   908  N  N    . GLN A 1 57  ? 38.939 12.890 3.517   1.00 15.02 ? 59  GLN A N    1 
ATOM   909  C  CA   . GLN A 1 57  ? 39.388 12.694 2.165   1.00 16.17 ? 59  GLN A CA   1 
ATOM   910  C  C    . GLN A 1 57  ? 38.897 13.811 1.236   1.00 15.95 ? 59  GLN A C    1 
ATOM   911  O  O    . GLN A 1 57  ? 39.618 14.290 0.381   1.00 16.35 ? 59  GLN A O    1 
ATOM   912  C  CB   . GLN A 1 57  ? 38.906 11.352 1.667   1.00 17.75 ? 59  GLN A CB   1 
ATOM   913  C  CG   . GLN A 1 57  ? 39.527 10.945 0.310   1.00 20.04 ? 59  GLN A CG   1 
ATOM   914  C  CD   . GLN A 1 57  ? 41.043 10.825 0.345   1.00 23.91 ? 59  GLN A CD   1 
ATOM   915  O  OE1  . GLN A 1 57  ? 41.587 9.898  0.944   1.00 26.24 ? 59  GLN A OE1  1 
ATOM   916  N  NE2  . GLN A 1 57  ? 41.720 11.794 -0.250  1.00 23.74 ? 59  GLN A NE2  1 
ATOM   917  H  H    . GLN A 1 57  ? 38.400 12.286 3.810   1.00 13.67 ? 59  GLN A H    1 
ATOM   918  H  HA   . GLN A 1 57  ? 40.358 12.692 2.149   1.00 14.27 ? 59  GLN A HA   1 
ATOM   919  H  HB2  . GLN A 1 57  ? 39.140 10.672 2.318   1.00 15.70 ? 59  GLN A HB2  1 
ATOM   920  H  HB3  . GLN A 1 57  ? 37.942 11.386 1.557   1.00 15.70 ? 59  GLN A HB3  1 
ATOM   921  H  HG2  . GLN A 1 57  ? 39.167 10.084 0.046   1.00 17.21 ? 59  GLN A HG2  1 
ATOM   922  H  HG3  . GLN A 1 57  ? 39.297 11.615 -0.353  1.00 17.21 ? 59  GLN A HG3  1 
ATOM   923  H  HE21 . GLN A 1 57  ? 41.300 12.443 -0.628  1.00 19.59 ? 59  GLN A HE21 1 
ATOM   924  H  HE22 . GLN A 1 57  ? 42.580 11.775 -0.259  1.00 19.59 ? 59  GLN A HE22 1 
ATOM   925  N  N    . ILE A 1 58  ? 37.659 14.252 1.427   1.00 15.27 ? 60  ILE A N    1 
ATOM   926  C  CA   . ILE A 1 58  ? 37.157 15.362 0.637   1.00 12.75 ? 60  ILE A CA   1 
ATOM   927  C  C    . ILE A 1 58  ? 37.900 16.652 0.875   1.00 14.42 ? 60  ILE A C    1 
ATOM   928  O  O    . ILE A 1 58  ? 38.276 17.364 -0.073  1.00 16.00 ? 60  ILE A O    1 
ATOM   929  C  CB   . ILE A 1 58  ? 35.645 15.560 0.888   1.00 13.12 ? 60  ILE A CB   1 
ATOM   930  C  CG1  . ILE A 1 58  ? 34.894 14.346 0.339   1.00 13.61 ? 60  ILE A CG1  1 
ATOM   931  C  CG2  . ILE A 1 58  ? 35.133 16.870 0.264   1.00 14.35 ? 60  ILE A CG2  1 
ATOM   932  C  CD1  . ILE A 1 58  ? 33.437 14.232 0.833   1.00 13.27 ? 60  ILE A CD1  1 
ATOM   933  H  H    . ILE A 1 58  ? 37.101 13.931 1.998   1.00 13.63 ? 60  ILE A H    1 
ATOM   934  H  HA   . ILE A 1 58  ? 37.266 15.138 -0.300  1.00 11.37 ? 60  ILE A HA   1 
ATOM   935  H  HB   . ILE A 1 58  ? 35.498 15.601 1.846   1.00 12.58 ? 60  ILE A HB   1 
ATOM   936  H  HG12 . ILE A 1 58  ? 34.874 14.403 -0.629  1.00 13.14 ? 60  ILE A HG12 1 
ATOM   937  H  HG13 . ILE A 1 58  ? 35.362 13.541 0.611   1.00 13.14 ? 60  ILE A HG13 1 
ATOM   938  H  HG21 . ILE A 1 58  ? 34.184 16.955 0.444   1.00 14.06 ? 60  ILE A HG21 1 
ATOM   939  H  HG22 . ILE A 1 58  ? 35.613 17.615 0.658   1.00 14.06 ? 60  ILE A HG22 1 
ATOM   940  H  HG23 . ILE A 1 58  ? 35.288 16.844 -0.693  1.00 14.06 ? 60  ILE A HG23 1 
ATOM   941  H  HD11 . ILE A 1 58  ? 33.033 13.441 0.442   1.00 13.51 ? 60  ILE A HD11 1 
ATOM   942  H  HD12 . ILE A 1 58  ? 33.436 14.160 1.800   1.00 13.51 ? 60  ILE A HD12 1 
ATOM   943  H  HD13 . ILE A 1 58  ? 32.948 15.024 0.558   1.00 13.51 ? 60  ILE A HD13 1 
ATOM   944  N  N    . ILE A 1 59  ? 38.160 16.967 2.153   1.00 14.75 ? 61  ILE A N    1 
ATOM   945  C  CA   . ILE A 1 59  ? 38.929 18.170 2.507   1.00 15.15 ? 61  ILE A CA   1 
ATOM   946  C  C    . ILE A 1 59  ? 40.298 18.147 1.800   1.00 15.67 ? 61  ILE A C    1 
ATOM   947  O  O    . ILE A 1 59  ? 40.738 19.141 1.212   1.00 19.26 ? 61  ILE A O    1 
ATOM   948  C  CB   . ILE A 1 59  ? 39.047 18.339 4.007   1.00 14.97 ? 61  ILE A CB   1 
ATOM   949  C  CG1  . ILE A 1 59  ? 37.638 18.569 4.603   1.00 14.34 ? 61  ILE A CG1  1 
ATOM   950  C  CG2  . ILE A 1 59  ? 40.036 19.482 4.313   1.00 17.73 ? 61  ILE A CG2  1 
ATOM   951  C  CD1  . ILE A 1 59  ? 37.604 18.354 6.136   1.00 14.96 ? 61  ILE A CD1  1 
ATOM   952  H  H    . ILE A 1 59  ? 37.903 16.502 2.830   1.00 13.18 ? 61  ILE A H    1 
ATOM   953  H  HA   . ILE A 1 59  ? 38.449 18.944 2.171   1.00 13.29 ? 61  ILE A HA   1 
ATOM   954  H  HB   . ILE A 1 59  ? 39.405 17.518 4.379   1.00 13.34 ? 61  ILE A HB   1 
ATOM   955  H  HG12 . ILE A 1 59  ? 37.361 19.481 4.420   1.00 13.55 ? 61  ILE A HG12 1 
ATOM   956  H  HG13 . ILE A 1 59  ? 37.016 17.945 4.197   1.00 13.55 ? 61  ILE A HG13 1 
ATOM   957  H  HG21 . ILE A 1 59  ? 40.109 19.586 5.275   1.00 15.61 ? 61  ILE A HG21 1 
ATOM   958  H  HG22 . ILE A 1 59  ? 40.902 19.258 3.938   1.00 15.61 ? 61  ILE A HG22 1 
ATOM   959  H  HG23 . ILE A 1 59  ? 39.705 20.301 3.915   1.00 15.61 ? 61  ILE A HG23 1 
ATOM   960  H  HD11 . ILE A 1 59  ? 36.702 18.510 6.457   1.00 14.38 ? 61  ILE A HD11 1 
ATOM   961  H  HD12 . ILE A 1 59  ? 37.873 17.443 6.332   1.00 14.38 ? 61  ILE A HD12 1 
ATOM   962  H  HD13 . ILE A 1 59  ? 38.217 18.978 6.555   1.00 14.38 ? 61  ILE A HD13 1 
ATOM   963  N  N    . ILE A 1 60  ? 40.914 16.987 1.878   1.00 14.95 ? 62  ILE A N    1 
ATOM   964  C  CA   . ILE A 1 60  ? 42.253 16.794 1.315   1.00 17.98 ? 62  ILE A CA   1 
ATOM   965  C  C    . ILE A 1 60  ? 42.216 16.992 -0.188  1.00 19.47 ? 62  ILE A C    1 
ATOM   966  O  O    . ILE A 1 60  ? 43.041 17.715 -0.746  1.00 20.61 ? 62  ILE A O    1 
ATOM   967  C  CB   . ILE A 1 60  ? 42.835 15.413 1.665   1.00 18.89 ? 62  ILE A CB   1 
ATOM   968  C  CG1  . ILE A 1 60  ? 43.267 15.405 3.128   1.00 17.92 ? 62  ILE A CG1  1 
ATOM   969  C  CG2  . ILE A 1 60  ? 44.043 15.051 0.752   1.00 21.64 ? 62  ILE A CG2  1 
ATOM   970  C  CD1  . ILE A 1 60  ? 43.313 13.996 3.707   1.00 21.35 ? 62  ILE A CD1  1 
ATOM   971  H  H    . ILE A 1 60  ? 40.585 16.286 2.253   1.00 13.24 ? 62  ILE A H    1 
ATOM   972  H  HA   . ILE A 1 60  ? 42.846 17.466 1.686   1.00 15.24 ? 62  ILE A HA   1 
ATOM   973  H  HB   . ILE A 1 60  ? 42.143 14.744 1.542   1.00 15.70 ? 62  ILE A HB   1 
ATOM   974  H  HG12 . ILE A 1 60  ? 44.155 15.790 3.200   1.00 14.78 ? 62  ILE A HG12 1 
ATOM   975  H  HG13 . ILE A 1 60  ? 42.635 15.925 3.649   1.00 14.78 ? 62  ILE A HG13 1 
ATOM   976  H  HG21 . ILE A 1 60  ? 44.379 14.177 1.005   1.00 17.29 ? 62  ILE A HG21 1 
ATOM   977  H  HG22 . ILE A 1 60  ? 43.747 15.038 -0.171  1.00 17.29 ? 62  ILE A HG22 1 
ATOM   978  H  HG23 . ILE A 1 60  ? 44.737 15.719 0.869   1.00 17.29 ? 62  ILE A HG23 1 
ATOM   979  H  HD11 . ILE A 1 60  ? 43.592 14.046 4.635   1.00 18.09 ? 62  ILE A HD11 1 
ATOM   980  H  HD12 . ILE A 1 60  ? 42.429 13.602 3.647   1.00 18.09 ? 62  ILE A HD12 1 
ATOM   981  H  HD13 . ILE A 1 60  ? 43.947 13.467 3.198   1.00 18.09 ? 62  ILE A HD13 1 
ATOM   982  N  N    . ASP A 1 61  ? 41.252 16.374 -0.871  1.00 19.39 ? 63  ASP A N    1 
ATOM   983  C  CA   . ASP A 1 61  ? 41.159 16.472 -2.338  1.00 19.65 ? 63  ASP A CA   1 
ATOM   984  C  C    . ASP A 1 61  ? 40.797 17.880 -2.807  1.00 20.93 ? 63  ASP A C    1 
ATOM   985  O  O    . ASP A 1 61  ? 41.316 18.393 -3.790  1.00 23.62 ? 63  ASP A O    1 
ATOM   986  C  CB   . ASP A 1 61  ? 40.150 15.459 -2.892  1.00 22.42 ? 63  ASP A CB   1 
ATOM   987  C  CG   . ASP A 1 61  ? 40.602 14.017 -2.701  1.00 23.09 ? 63  ASP A CG   1 
ATOM   988  O  OD1  . ASP A 1 61  ? 41.821 13.795 -2.537  1.00 27.75 ? 63  ASP A OD1  1 
ATOM   989  O  OD2  . ASP A 1 61  ? 39.759 13.094 -2.744  1.00 23.50 ? 63  ASP A OD2  1 
ATOM   990  H  H    . ASP A 1 61  ? 40.638 15.891 -0.513  1.00 16.29 ? 63  ASP A H    1 
ATOM   991  H  HA   . ASP A 1 61  ? 42.026 16.255 -2.715  1.00 16.18 ? 63  ASP A HA   1 
ATOM   992  H  HB2  . ASP A 1 61  ? 39.303 15.572 -2.432  1.00 19.35 ? 63  ASP A HB2  1 
ATOM   993  H  HB3  . ASP A 1 61  ? 40.035 15.615 -3.842  1.00 19.35 ? 63  ASP A HB3  1 
ATOM   994  N  N    . VAL A 1 62  ? 39.815 18.492 -2.158  1.00 18.98 ? 64  VAL A N    1 
ATOM   995  C  CA   . VAL A 1 62  ? 39.390 19.832 -2.571  1.00 19.30 ? 64  VAL A CA   1 
ATOM   996  C  C    . VAL A 1 62  ? 40.435 20.929 -2.287  1.00 23.23 ? 64  VAL A C    1 
ATOM   997  O  O    . VAL A 1 62  ? 40.653 21.826 -3.099  1.00 23.54 ? 64  VAL A O    1 
ATOM   998  C  CB   . VAL A 1 62  ? 38.025 20.207 -1.909  1.00 19.11 ? 64  VAL A CB   1 
ATOM   999  C  CG1  . VAL A 1 62  ? 37.663 21.664 -2.227  1.00 25.43 ? 64  VAL A CG1  1 
ATOM   1000 C  CG2  . VAL A 1 62  ? 36.950 19.212 -2.356  1.00 17.90 ? 64  VAL A CG2  1 
ATOM   1001 H  H    . VAL A 1 62  ? 39.384 18.165 -1.490  1.00 16.03 ? 64  VAL A H    1 
ATOM   1002 H  HA   . VAL A 1 62  ? 39.247 19.819 -3.531  1.00 16.48 ? 64  VAL A HA   1 
ATOM   1003 H  HB   . VAL A 1 62  ? 38.116 20.129 -0.947  1.00 17.29 ? 64  VAL A HB   1 
ATOM   1004 H  HG11 . VAL A 1 62  ? 36.814 21.877 -1.808  1.00 23.63 ? 64  VAL A HG11 1 
ATOM   1005 H  HG12 . VAL A 1 62  ? 38.358 22.245 -1.880  1.00 23.63 ? 64  VAL A HG12 1 
ATOM   1006 H  HG13 . VAL A 1 62  ? 37.593 21.770 -3.188  1.00 23.63 ? 64  VAL A HG13 1 
ATOM   1007 H  HG21 . VAL A 1 62  ? 36.107 19.452 -1.941  1.00 16.60 ? 64  VAL A HG21 1 
ATOM   1008 H  HG22 . VAL A 1 62  ? 36.866 19.251 -3.322  1.00 16.60 ? 64  VAL A HG22 1 
ATOM   1009 H  HG23 . VAL A 1 62  ? 37.212 18.320 -2.082  1.00 16.60 ? 64  VAL A HG23 1 
ATOM   1010 N  N    . LEU A 1 63  ? 41.075 20.849 -1.128  1.00 23.47 ? 65  LEU A N    1 
ATOM   1011 C  CA   . LEU A 1 63  ? 42.095 21.830 -0.725  1.00 23.69 ? 65  LEU A CA   1 
ATOM   1012 C  C    . LEU A 1 63  ? 43.551 21.406 -1.048  1.00 25.36 ? 65  LEU A C    1 
ATOM   1013 O  O    . LEU A 1 63  ? 44.475 22.180 -0.845  1.00 29.89 ? 65  LEU A O    1 
ATOM   1014 C  CB   . LEU A 1 63  ? 41.937 22.186 0.759   1.00 21.45 ? 65  LEU A CB   1 
ATOM   1015 C  CG   . LEU A 1 63  ? 40.627 22.896 1.073   1.00 22.35 ? 65  LEU A CG   1 
ATOM   1016 C  CD1  . LEU A 1 63  ? 40.582 23.172 2.569   1.00 21.27 ? 65  LEU A CD1  1 
ATOM   1017 C  CD2  . LEU A 1 63  ? 40.495 24.171 0.277   1.00 24.51 ? 65  LEU A CD2  1 
ATOM   1018 H  H    . LEU A 1 63  ? 40.940 20.230 -0.545  1.00 20.09 ? 65  LEU A H    1 
ATOM   1019 H  HA   . LEU A 1 63  ? 41.928 22.645 -1.224  1.00 19.65 ? 65  LEU A HA   1 
ATOM   1020 H  HB2  . LEU A 1 63  ? 41.967 21.369 1.282   1.00 17.92 ? 65  LEU A HB2  1 
ATOM   1021 H  HB3  . LEU A 1 63  ? 42.664 22.772 1.020   1.00 17.92 ? 65  LEU A HB3  1 
ATOM   1022 H  HG   . LEU A 1 63  ? 39.884 22.316 0.846   1.00 19.67 ? 65  LEU A HG   1 
ATOM   1023 H  HD11 . LEU A 1 63  ? 39.751 23.625 2.781   1.00 18.94 ? 65  LEU A HD11 1 
ATOM   1024 H  HD12 . LEU A 1 63  ? 40.631 22.329 3.046   1.00 18.94 ? 65  LEU A HD12 1 
ATOM   1025 H  HD13 . LEU A 1 63  ? 41.336 23.733 2.809   1.00 18.94 ? 65  LEU A HD13 1 
ATOM   1026 H  HD21 . LEU A 1 63  ? 39.652 24.596 0.500   1.00 21.51 ? 65  LEU A HD21 1 
ATOM   1027 H  HD22 . LEU A 1 63  ? 41.232 24.760 0.500   1.00 21.51 ? 65  LEU A HD22 1 
ATOM   1028 H  HD23 . LEU A 1 63  ? 40.517 23.956 -0.669  1.00 21.51 ? 65  LEU A HD23 1 
ATOM   1029 N  N    . GLN A 1 64  ? 43.720 20.200 -1.576  1.00 22.60 ? 66  GLN A N    1 
ATOM   1030 C  CA   . GLN A 1 64  ? 45.024 19.655 -1.927  1.00 27.02 ? 66  GLN A CA   1 
ATOM   1031 C  C    . GLN A 1 64  ? 45.988 19.711 -0.748  1.00 29.17 ? 66  GLN A C    1 
ATOM   1032 O  O    . GLN A 1 64  ? 47.110 20.230 -0.837  1.00 30.27 ? 66  GLN A O    1 
ATOM   1033 C  CB   . GLN A 1 64  ? 45.596 20.386 -3.146  1.00 33.12 ? 66  GLN A CB   1 
ATOM   1034 C  CG   . GLN A 1 64  ? 46.877 19.771 -3.723  1.00 47.57 ? 66  GLN A CG   1 
ATOM   1035 C  CD   . GLN A 1 64  ? 46.675 18.345 -4.227  1.00 51.42 ? 66  GLN A CD   1 
ATOM   1036 O  OE1  . GLN A 1 64  ? 45.755 18.082 -5.004  1.00 43.76 ? 66  GLN A OE1  1 
ATOM   1037 N  NE2  . GLN A 1 64  ? 47.531 17.419 -3.777  1.00 44.92 ? 66  GLN A NE2  1 
ATOM   1038 H  H    . GLN A 1 64  ? 43.071 19.661 -1.745  1.00 18.76 ? 66  GLN A H    1 
ATOM   1039 H  HA   . GLN A 1 64  ? 44.913 18.723 -2.170  1.00 22.07 ? 66  GLN A HA   1 
ATOM   1040 H  HB2  . GLN A 1 64  ? 44.928 20.385 -3.850  1.00 27.23 ? 66  GLN A HB2  1 
ATOM   1041 H  HB3  . GLN A 1 64  ? 45.799 21.300 -2.892  1.00 27.23 ? 66  GLN A HB3  1 
ATOM   1042 H  HG2  . GLN A 1 64  ? 47.179 20.312 -4.469  1.00 40.39 ? 66  GLN A HG2  1 
ATOM   1043 H  HG3  . GLN A 1 64  ? 47.556 19.750 -3.031  1.00 40.39 ? 66  GLN A HG3  1 
ATOM   1044 H  HE21 . GLN A 1 64  ? 48.157 17.642 -3.230  1.00 37.11 ? 66  GLN A HE21 1 
ATOM   1045 H  HE22 . GLN A 1 64  ? 47.456 16.602 -4.034  1.00 37.11 ? 66  GLN A HE22 1 
ATOM   1046 N  N    . LEU A 1 65  ? 45.538 19.168 0.369   1.00 23.32 ? 67  LEU A N    1 
ATOM   1047 C  CA   . LEU A 1 65  ? 46.366 19.079 1.549   1.00 25.07 ? 67  LEU A CA   1 
ATOM   1048 C  C    . LEU A 1 65  ? 47.306 17.906 1.416   1.00 27.56 ? 67  LEU A C    1 
ATOM   1049 O  O    . LEU A 1 65  ? 46.932 16.857 0.916   1.00 26.47 ? 67  LEU A O    1 
ATOM   1050 C  CB   . LEU A 1 65  ? 45.512 18.858 2.770   1.00 22.68 ? 67  LEU A CB   1 
ATOM   1051 C  CG   . LEU A 1 65  ? 44.454 19.921 3.095   1.00 19.63 ? 67  LEU A CG   1 
ATOM   1052 C  CD1  . LEU A 1 65  ? 43.856 19.637 4.460   1.00 19.11 ? 67  LEU A CD1  1 
ATOM   1053 C  CD2  . LEU A 1 65  ? 45.037 21.291 3.006   1.00 24.77 ? 67  LEU A CD2  1 
ATOM   1054 H  H    . LEU A 1 65  ? 44.749 18.840 0.468   1.00 19.60 ? 67  LEU A H    1 
ATOM   1055 H  HA   . LEU A 1 65  ? 46.882 19.892 1.661   1.00 21.05 ? 67  LEU A HA   1 
ATOM   1056 H  HB2  . LEU A 1 65  ? 45.043 18.016 2.661   1.00 19.67 ? 67  LEU A HB2  1 
ATOM   1057 H  HB3  . LEU A 1 65  ? 46.099 18.798 3.540   1.00 19.67 ? 67  LEU A HB3  1 
ATOM   1058 H  HG   . LEU A 1 65  ? 43.740 19.861 2.441   1.00 17.49 ? 67  LEU A HG   1 
ATOM   1059 H  HD11 . LEU A 1 65  ? 43.189 20.313 4.658   1.00 17.72 ? 67  LEU A HD11 1 
ATOM   1060 H  HD12 . LEU A 1 65  ? 43.445 18.759 4.447   1.00 17.72 ? 67  LEU A HD12 1 
ATOM   1061 H  HD13 . LEU A 1 65  ? 44.562 19.663 5.125   1.00 17.72 ? 67  LEU A HD13 1 
ATOM   1062 H  HD21 . LEU A 1 65  ? 44.349 21.942 3.216   1.00 22.12 ? 67  LEU A HD21 1 
ATOM   1063 H  HD22 . LEU A 1 65  ? 45.767 21.365 3.641   1.00 22.12 ? 67  LEU A HD22 1 
ATOM   1064 H  HD23 . LEU A 1 65  ? 45.366 21.436 2.105   1.00 22.12 ? 67  LEU A HD23 1 
ATOM   1065 N  N    . PRO A 1 66  ? 48.539 18.067 1.929   1.00 27.69 ? 68  PRO A N    1 
ATOM   1066 C  CA   . PRO A 1 66  ? 49.586 17.058 1.754   1.00 31.31 ? 68  PRO A CA   1 
ATOM   1067 C  C    . PRO A 1 66  ? 49.560 15.969 2.830   1.00 28.47 ? 68  PRO A C    1 
ATOM   1068 O  O    . PRO A 1 66  ? 50.595 15.650 3.415   1.00 29.64 ? 68  PRO A O    1 
ATOM   1069 C  CB   . PRO A 1 66  ? 50.857 17.904 1.820   1.00 30.87 ? 68  PRO A CB   1 
ATOM   1070 C  CG   . PRO A 1 66  ? 50.534 18.986 2.766   1.00 28.79 ? 68  PRO A CG   1 
ATOM   1071 C  CD   . PRO A 1 66  ? 49.072 19.300 2.542   1.00 28.39 ? 68  PRO A CD   1 
ATOM   1072 H  HA   . PRO A 1 66  ? 49.518 16.648 0.878   1.00 25.87 ? 68  PRO A HA   1 
ATOM   1073 H  HB2  . PRO A 1 66  ? 51.593 17.366 2.150   1.00 24.33 ? 68  PRO A HB2  1 
ATOM   1074 H  HB3  . PRO A 1 66  ? 51.058 18.263 0.941   1.00 24.33 ? 68  PRO A HB3  1 
ATOM   1075 H  HG2  . PRO A 1 66  ? 50.683 18.680 3.674   1.00 22.89 ? 68  PRO A HG2  1 
ATOM   1076 H  HG3  . PRO A 1 66  ? 51.084 19.762 2.572   1.00 22.89 ? 68  PRO A HG3  1 
ATOM   1077 H  HD2  . PRO A 1 66  ? 48.631 19.474 3.388   1.00 23.74 ? 68  PRO A HD2  1 
ATOM   1078 H  HD3  . PRO A 1 66  ? 48.977 20.048 1.931   1.00 23.74 ? 68  PRO A HD3  1 
ATOM   1079 N  N    . MET A 1 67  ? 48.376 15.430 3.114   1.00 25.76 ? 69  MET A N    1 
ATOM   1080 C  CA   . MET A 1 67  ? 48.206 14.393 4.137   1.00 27.72 ? 69  MET A CA   1 
ATOM   1081 C  C    . MET A 1 67  ? 47.275 13.280 3.702   1.00 27.36 ? 69  MET A C    1 
ATOM   1082 O  O    . MET A 1 67  ? 46.568 13.411 2.699   1.00 29.21 ? 69  MET A O    1 
ATOM   1083 C  CB   . MET A 1 67  ? 47.731 14.988 5.476   1.00 30.88 ? 69  MET A CB   1 
ATOM   1084 C  CG   . MET A 1 67  ? 46.535 15.925 5.458   1.00 29.12 ? 69  MET A CG   1 
ATOM   1085 S  SD   . MET A 1 67  ? 46.508 17.007 6.916   1.00 32.27 ? 69  MET A SD   1 
ATOM   1086 C  CE   . MET A 1 67  ? 46.823 15.805 8.195   1.00 30.60 ? 69  MET A CE   1 
ATOM   1087 H  H    . MET A 1 67  ? 47.643 15.650 2.722   1.00 19.32 ? 69  MET A H    1 
ATOM   1088 H  HA   . MET A 1 67  ? 49.077 13.999 4.301   1.00 21.54 ? 69  MET A HA   1 
ATOM   1089 H  HB2  . MET A 1 67  ? 47.503 14.252 6.065   1.00 25.52 ? 69  MET A HB2  1 
ATOM   1090 H  HB3  . MET A 1 67  ? 48.471 15.483 5.861   1.00 25.52 ? 69  MET A HB3  1 
ATOM   1091 H  HG2  . MET A 1 67  ? 46.579 16.484 4.666   1.00 24.82 ? 69  MET A HG2  1 
ATOM   1092 H  HG3  . MET A 1 67  ? 45.719 15.401 5.453   1.00 24.82 ? 69  MET A HG3  1 
ATOM   1093 H  HE1  . MET A 1 67  ? 46.836 16.255 9.054   1.00 26.60 ? 69  MET A HE1  1 
ATOM   1094 H  HE2  . MET A 1 67  ? 46.119 15.138 8.181   1.00 26.60 ? 69  MET A HE2  1 
ATOM   1095 H  HE3  . MET A 1 67  ? 47.681 15.385 8.028   1.00 26.60 ? 69  MET A HE3  1 
ATOM   1096 N  N    . SER A 1 68  ? 47.252 12.187 4.457   1.00 24.50 ? 70  SER A N    1 
ATOM   1097 C  CA   . SER A 1 68  ? 46.293 11.122 4.222   1.00 22.45 ? 70  SER A CA   1 
ATOM   1098 C  C    . SER A 1 68  ? 45.054 11.373 5.067   1.00 20.91 ? 70  SER A C    1 
ATOM   1099 O  O    . SER A 1 68  ? 45.083 12.151 6.003   1.00 20.81 ? 70  SER A O    1 
ATOM   1100 C  CB   . SER A 1 68  ? 46.845 9.754  4.547   1.00 27.01 ? 70  SER A CB   1 
ATOM   1101 O  OG   . SER A 1 68  ? 46.918 9.574  5.944   1.00 25.93 ? 70  SER A OG   1 
ATOM   1102 H  H    . SER A 1 68  ? 47.785 12.040 5.115   1.00 19.73 ? 70  SER A H    1 
ATOM   1103 H  HA   . SER A 1 68  ? 46.030 11.129 3.288   1.00 18.09 ? 70  SER A HA   1 
ATOM   1104 H  HB2  . SER A 1 68  ? 46.261 9.078  4.170   1.00 21.87 ? 70  SER A HB2  1 
ATOM   1105 H  HB3  . SER A 1 68  ? 47.735 9.674  4.170   1.00 21.87 ? 70  SER A HB3  1 
ATOM   1106 H  HG   . SER A 1 68  ? 47.226 8.812  6.120   1.00 20.98 ? 70  SER A HG   1 
ATOM   1107 N  N    . LYS A 1 69  ? 43.954 10.724 4.705   1.00 23.38 ? 71  LYS A N    1 
ATOM   1108 C  CA   . LYS A 1 69  ? 42.742 10.887 5.446   1.00 19.76 ? 71  LYS A CA   1 
ATOM   1109 C  C    . LYS A 1 69  ? 42.881 10.365 6.872   1.00 20.65 ? 71  LYS A C    1 
ATOM   1110 O  O    . LYS A 1 69  ? 42.309 10.911 7.791   1.00 20.40 ? 71  LYS A O    1 
ATOM   1111 C  CB   . LYS A 1 69  ? 41.549 10.244 4.707   1.00 20.38 ? 71  LYS A CB   1 
ATOM   1112 C  CG   . LYS A 1 69  ? 41.624 8.767  4.510   1.00 25.13 ? 71  LYS A CG   1 
ATOM   1113 C  CD   . LYS A 1 69  ? 40.404 8.208  3.795   1.00 21.72 ? 71  LYS A CD   1 
ATOM   1114 C  CE   . LYS A 1 69  ? 40.346 6.684  3.825   1.00 29.67 ? 71  LYS A CE   1 
ATOM   1115 N  NZ   . LYS A 1 69  ? 41.436 6.043  3.031   1.00 35.59 ? 71  LYS A NZ   1 
ATOM   1116 H  H    . LYS A 1 69  ? 43.896 10.188 4.034   1.00 19.15 ? 71  LYS A H    1 
ATOM   1117 H  HA   . LYS A 1 69  ? 42.557 11.837 5.510   1.00 16.54 ? 71  LYS A HA   1 
ATOM   1118 H  HB2  . LYS A 1 69  ? 40.742 10.429 5.211   1.00 17.59 ? 71  LYS A HB2  1 
ATOM   1119 H  HB3  . LYS A 1 69  ? 41.480 10.650 3.828   1.00 17.59 ? 71  LYS A HB3  1 
ATOM   1120 H  HG2  . LYS A 1 69  ? 42.407 8.558  3.977   1.00 21.76 ? 71  LYS A HG2  1 
ATOM   1121 H  HG3  . LYS A 1 69  ? 41.687 8.335  5.377   1.00 21.76 ? 71  LYS A HG3  1 
ATOM   1122 H  HD2  . LYS A 1 69  ? 39.603 8.547  4.224   1.00 18.76 ? 71  LYS A HD2  1 
ATOM   1123 H  HD3  . LYS A 1 69  ? 40.427 8.489  2.866   1.00 18.76 ? 71  LYS A HD3  1 
ATOM   1124 H  HE2  . LYS A 1 69  ? 40.428 6.384  4.744   1.00 26.13 ? 71  LYS A HE2  1 
ATOM   1125 H  HE3  . LYS A 1 69  ? 39.497 6.394  3.456   1.00 26.13 ? 71  LYS A HE3  1 
ATOM   1126 H  HZ1  . LYS A 1 69  ? 41.365 5.158  3.076   1.00 30.95 ? 71  LYS A HZ1  1 
ATOM   1127 H  HZ2  . LYS A 1 69  ? 41.380 6.295  2.180   1.00 30.95 ? 71  LYS A HZ2  1 
ATOM   1128 H  HZ3  . LYS A 1 69  ? 42.230 6.286  3.353   1.00 30.95 ? 71  LYS A HZ3  1 
ATOM   1129 N  N    . GLU A 1 70  ? 43.652 9.296  7.043   1.00 23.07 ? 72  GLU A N    1 
ATOM   1130 C  CA   . GLU A 1 70  ? 43.862 8.749  8.376   1.00 23.62 ? 72  GLU A CA   1 
ATOM   1131 C  C    . GLU A 1 70  ? 44.631 9.726  9.251   1.00 22.71 ? 72  GLU A C    1 
ATOM   1132 O  O    . GLU A 1 70  ? 44.315 9.925  10.424  1.00 21.07 ? 72  GLU A O    1 
ATOM   1133 C  CB   . GLU A 1 70  ? 44.636 7.447  8.257   1.00 28.45 ? 72  GLU A CB   1 
ATOM   1134 C  CG   . GLU A 1 70  ? 43.841 6.315  7.620   1.00 24.65 ? 72  GLU A CG   1 
ATOM   1135 C  CD   . GLU A 1 70  ? 43.843 6.316  6.100   1.00 29.22 ? 72  GLU A CD   1 
ATOM   1136 O  OE1  . GLU A 1 70  ? 44.593 7.085  5.470   1.00 28.56 ? 72  GLU A OE1  1 
ATOM   1137 O  OE2  . GLU A 1 70  ? 43.042 5.541  5.537   1.00 31.55 ? 72  GLU A OE2  1 
ATOM   1138 H  H    . GLU A 1 70  ? 44.058 8.874  6.413   1.00 19.50 ? 72  GLU A H    1 
ATOM   1139 H  HA   . GLU A 1 70  ? 43.006 8.565  8.793   1.00 19.89 ? 72  GLU A HA   1 
ATOM   1140 H  HB2  . GLU A 1 70  ? 45.423 7.600  7.710   1.00 23.67 ? 72  GLU A HB2  1 
ATOM   1141 H  HB3  . GLU A 1 70  ? 44.902 7.159  9.144   1.00 23.67 ? 72  GLU A HB3  1 
ATOM   1142 H  HG2  . GLU A 1 70  ? 44.215 5.470  7.914   1.00 19.83 ? 72  GLU A HG2  1 
ATOM   1143 H  HG3  . GLU A 1 70  ? 42.918 6.382  7.913   1.00 19.83 ? 72  GLU A HG3  1 
ATOM   1144 N  N    . GLU A 1 71  ? 45.618 10.383 8.660   1.00 20.68 ? 73  GLU A N    1 
ATOM   1145 C  CA   . GLU A 1 71  ? 46.390 11.396 9.378   1.00 23.36 ? 73  GLU A CA   1 
ATOM   1146 C  C    . GLU A 1 71  ? 45.551 12.599 9.772   1.00 20.32 ? 73  GLU A C    1 
ATOM   1147 O  O    . GLU A 1 71  ? 45.654 13.102 10.892  1.00 20.18 ? 73  GLU A O    1 
ATOM   1148 C  CB   . GLU A 1 71  ? 47.558 11.838 8.489   1.00 25.88 ? 73  GLU A CB   1 
ATOM   1149 C  CG   . GLU A 1 71  ? 48.712 10.830 8.460   1.00 26.60 ? 73  GLU A CG   1 
ATOM   1150 C  CD   . GLU A 1 71  ? 49.698 11.069 7.325   1.00 30.41 ? 73  GLU A CD   1 
ATOM   1151 O  OE1  . GLU A 1 71  ? 49.427 11.870 6.397   1.00 28.26 ? 73  GLU A OE1  1 
ATOM   1152 O  OE2  . GLU A 1 71  ? 50.791 10.447 7.377   1.00 32.19 ? 73  GLU A OE2  1 
ATOM   1153 H  H    . GLU A 1 71  ? 45.863 10.263 7.845   1.00 17.31 ? 73  GLU A H    1 
ATOM   1154 H  HA   . GLU A 1 71  ? 46.756 11.004 10.186  1.00 19.84 ? 73  GLU A HA   1 
ATOM   1155 H  HB2  . GLU A 1 71  ? 47.237 11.950 7.581   1.00 21.48 ? 73  GLU A HB2  1 
ATOM   1156 H  HB3  . GLU A 1 71  ? 47.905 12.680 8.823   1.00 21.48 ? 73  GLU A HB3  1 
ATOM   1157 H  HG2  . GLU A 1 71  ? 49.201 10.888 9.296   1.00 21.00 ? 73  GLU A HG2  1 
ATOM   1158 H  HG3  . GLU A 1 71  ? 48.347 9.938  8.354   1.00 21.00 ? 73  GLU A HG3  1 
ATOM   1159 N  N    . LEU A 1 72  ? 44.665 13.033 8.870   1.00 22.23 ? 74  LEU A N    1 
ATOM   1160 C  CA   . LEU A 1 72  ? 43.821 14.187 9.146   1.00 17.19 ? 74  LEU A CA   1 
ATOM   1161 C  C    . LEU A 1 72  ? 42.763 13.849 10.190  1.00 16.39 ? 74  LEU A C    1 
ATOM   1162 O  O    . LEU A 1 72  ? 42.492 14.648 11.079  1.00 17.96 ? 74  LEU A O    1 
ATOM   1163 C  CB   . LEU A 1 72  ? 43.149 14.678 7.838   1.00 19.57 ? 74  LEU A CB   1 
ATOM   1164 C  CG   . LEU A 1 72  ? 42.246 15.900 7.939   1.00 16.40 ? 74  LEU A CG   1 
ATOM   1165 C  CD1  . LEU A 1 72  ? 42.870 16.997 8.733   1.00 17.94 ? 74  LEU A CD1  1 
ATOM   1166 C  CD2  . LEU A 1 72  ? 41.842 16.457 6.578   1.00 17.83 ? 74  LEU A CD2  1 
ATOM   1167 H  H    . LEU A 1 72  ? 44.538 12.677 8.098   1.00 18.56 ? 74  LEU A H    1 
ATOM   1168 H  HA   . LEU A 1 72  ? 44.370 14.908 9.493   1.00 14.35 ? 74  LEU A HA   1 
ATOM   1169 H  HB2  . LEU A 1 72  ? 43.849 14.892 7.202   1.00 17.08 ? 74  LEU A HB2  1 
ATOM   1170 H  HB3  . LEU A 1 72  ? 42.610 13.952 7.487   1.00 17.08 ? 74  LEU A HB3  1 
ATOM   1171 H  HG   . LEU A 1 72  ? 41.432 15.640 8.398   1.00 14.67 ? 74  LEU A HG   1 
ATOM   1172 H  HD11 . LEU A 1 72  ? 42.258 17.749 8.767   1.00 16.04 ? 74  LEU A HD11 1 
ATOM   1173 H  HD12 . LEU A 1 72  ? 43.049 16.675 9.630   1.00 16.04 ? 74  LEU A HD12 1 
ATOM   1174 H  HD13 . LEU A 1 72  ? 43.699 17.264 8.304   1.00 16.04 ? 74  LEU A HD13 1 
ATOM   1175 H  HD21 . LEU A 1 72  ? 41.271 17.229 6.710   1.00 16.22 ? 74  LEU A HD21 1 
ATOM   1176 H  HD22 . LEU A 1 72  ? 42.642 16.714 6.093   1.00 16.22 ? 74  LEU A HD22 1 
ATOM   1177 H  HD23 . LEU A 1 72  ? 41.363 15.771 6.087   1.00 16.22 ? 74  LEU A HD23 1 
ATOM   1178 N  N    . VAL A 1 73  ? 42.202 12.650 10.123  1.00 16.41 ? 75  VAL A N    1 
ATOM   1179 C  CA   . VAL A 1 73  ? 41.266 12.227 11.165  1.00 17.99 ? 75  VAL A CA   1 
ATOM   1180 C  C    . VAL A 1 73  ? 41.980 12.145 12.519  1.00 19.18 ? 75  VAL A C    1 
ATOM   1181 O  O    . VAL A 1 73  ? 41.452 12.643 13.499  1.00 19.11 ? 75  VAL A O    1 
ATOM   1182 C  CB   . VAL A 1 73  ? 40.586 10.901 10.853  1.00 17.43 ? 75  VAL A CB   1 
ATOM   1183 C  CG1  . VAL A 1 73  ? 39.794 10.389 12.038  1.00 23.02 ? 75  VAL A CG1  1 
ATOM   1184 C  CG2  . VAL A 1 73  ? 39.647 11.091 9.651   1.00 16.46 ? 75  VAL A CG2  1 
ATOM   1185 H  H    . VAL A 1 73  ? 42.339 12.072 9.501   1.00 13.98 ? 75  VAL A H    1 
ATOM   1186 H  HA   . VAL A 1 73  ? 40.570 12.899 11.243  1.00 16.05 ? 75  VAL A HA   1 
ATOM   1187 H  HB   . VAL A 1 73  ? 41.255 10.239 10.620  1.00 15.47 ? 75  VAL A HB   1 
ATOM   1188 H  HG11 . VAL A 1 73  ? 39.378 9.545  11.799  1.00 21.33 ? 75  VAL A HG11 1 
ATOM   1189 H  HG12 . VAL A 1 73  ? 40.396 10.260 12.788  1.00 21.33 ? 75  VAL A HG12 1 
ATOM   1190 H  HG13 . VAL A 1 73  ? 39.113 11.040 12.268  1.00 21.33 ? 75  VAL A HG13 1 
ATOM   1191 H  HG21 . VAL A 1 73  ? 39.213 10.246 9.453   1.00 14.98 ? 75  VAL A HG21 1 
ATOM   1192 H  HG22 . VAL A 1 73  ? 38.981 11.760 9.874   1.00 14.98 ? 75  VAL A HG22 1 
ATOM   1193 H  HG23 . VAL A 1 73  ? 40.168 11.383 8.887   1.00 14.98 ? 75  VAL A HG23 1 
ATOM   1194 N  N    . GLU A 1 74  ? 43.157 11.501 12.583  1.00 20.25 ? 76  GLU A N    1 
ATOM   1195 C  CA   . GLU A 1 74  ? 43.826 11.365 13.865  1.00 23.04 ? 76  GLU A CA   1 
ATOM   1196 C  C    . GLU A 1 74  ? 44.139 12.722 14.455  1.00 18.46 ? 76  GLU A C    1 
ATOM   1197 O  O    . GLU A 1 74  ? 43.835 12.970 15.622  1.00 21.96 ? 76  GLU A O    1 
ATOM   1198 C  CB   . GLU A 1 74  ? 45.106 10.553 13.699  1.00 27.47 ? 76  GLU A CB   1 
ATOM   1199 C  CG   . GLU A 1 74  ? 45.860 10.304 15.008  1.00 31.98 ? 76  GLU A CG   1 
ATOM   1200 C  CD   . GLU A 1 74  ? 47.258 9.725  14.794  1.00 44.98 ? 76  GLU A CD   1 
ATOM   1201 O  OE1  . GLU A 1 74  ? 47.530 9.150  13.713  1.00 47.94 ? 76  GLU A OE1  1 
ATOM   1202 O  OE2  . GLU A 1 74  ? 48.091 9.847  15.722  1.00 52.70 ? 76  GLU A OE2  1 
ATOM   1203 H  H    . GLU A 1 74  ? 43.569 11.148 11.916  1.00 18.35 ? 76  GLU A H    1 
ATOM   1204 H  HA   . GLU A 1 74  ? 43.244 10.892 14.481  1.00 20.75 ? 76  GLU A HA   1 
ATOM   1205 H  HB2  . GLU A 1 74  ? 44.881 9.690  13.318  1.00 24.13 ? 76  GLU A HB2  1 
ATOM   1206 H  HB3  . GLU A 1 74  ? 45.702 11.031 13.101  1.00 24.13 ? 76  GLU A HB3  1 
ATOM   1207 H  HG2  . GLU A 1 74  ? 45.954 11.144 15.482  1.00 28.11 ? 76  GLU A HG2  1 
ATOM   1208 H  HG3  . GLU A 1 74  ? 45.355 9.674  15.546  1.00 28.11 ? 76  GLU A HG3  1 
ATOM   1209 N  N    . GLU A 1 75  ? 44.732 13.609 13.676  1.00 25.07 ? 77  GLU A N    1 
ATOM   1210 C  CA   . GLU A 1 75  ? 45.106 14.913 14.217  1.00 25.64 ? 77  GLU A CA   1 
ATOM   1211 C  C    . GLU A 1 75  ? 43.880 15.699 14.647  1.00 23.61 ? 77  GLU A C    1 
ATOM   1212 O  O    . GLU A 1 75  ? 43.834 16.260 15.722  1.00 26.50 ? 77  GLU A O    1 
ATOM   1213 C  CB   . GLU A 1 75  ? 45.924 15.720 13.222  1.00 29.00 ? 77  GLU A CB   1 
ATOM   1214 C  CG   . GLU A 1 75  ? 46.275 17.123 13.726  1.00 32.02 ? 77  GLU A CG   1 
ATOM   1215 C  CD   . GLU A 1 75  ? 47.294 17.843 12.854  1.00 33.77 ? 77  GLU A CD   1 
ATOM   1216 O  OE1  . GLU A 1 75  ? 47.606 17.341 11.757  1.00 34.81 ? 77  GLU A OE1  1 
ATOM   1217 O  OE2  . GLU A 1 75  ? 47.790 18.919 13.257  1.00 35.03 ? 77  GLU A OE2  1 
ATOM   1218 H  H    . GLU A 1 75  ? 44.928 13.490 12.847  1.00 20.82 ? 77  GLU A H    1 
ATOM   1219 H  HA   . GLU A 1 75  ? 45.656 14.774 15.004  1.00 21.43 ? 77  GLU A HA   1 
ATOM   1220 H  HB2  . GLU A 1 75  ? 46.754 15.251 13.044  1.00 24.34 ? 77  GLU A HB2  1 
ATOM   1221 H  HB3  . GLU A 1 75  ? 45.416 15.817 12.402  1.00 24.34 ? 77  GLU A HB3  1 
ATOM   1222 H  HG2  . GLU A 1 75  ? 45.467 17.660 13.746  1.00 27.32 ? 77  GLU A HG2  1 
ATOM   1223 H  HG3  . GLU A 1 75  ? 46.646 17.052 14.620  1.00 27.32 ? 77  GLU A HG3  1 
ATOM   1224 N  N    . SER A 1 76  ? 42.859 15.721 13.798  1.00 21.77 ? 78  SER A N    1 
ATOM   1225 C  CA   . SER A 1 76  ? 41.677 16.551 14.077  1.00 18.75 ? 78  SER A CA   1 
ATOM   1226 C  C    . SER A 1 76  ? 40.928 16.004 15.292  1.00 20.64 ? 78  SER A C    1 
ATOM   1227 O  O    . SER A 1 76  ? 40.508 16.786 16.146  1.00 18.67 ? 78  SER A O    1 
ATOM   1228 C  CB   . SER A 1 76  ? 40.763 16.743 12.842  1.00 19.32 ? 78  SER A CB   1 
ATOM   1229 O  OG   . SER A 1 76  ? 40.234 15.530 12.332  1.00 18.07 ? 78  SER A OG   1 
ATOM   1230 H  H    . SER A 1 76  ? 42.820 15.275 13.063  1.00 18.85 ? 78  SER A H    1 
ATOM   1231 H  HA   . SER A 1 76  ? 41.993 17.434 14.323  1.00 16.59 ? 78  SER A HA   1 
ATOM   1232 H  HB2  . SER A 1 76  ? 40.023 17.317 13.095  1.00 17.64 ? 78  SER A HB2  1 
ATOM   1233 H  HB3  . SER A 1 76  ? 41.280 17.171 12.142  1.00 17.64 ? 78  SER A HB3  1 
ATOM   1234 H  HG   . SER A 1 76  ? 40.860 15.020 12.099  1.00 16.49 ? 78  SER A HG   1 
ATOM   1235 N  N    . GLN A 1 77  ? 40.779 14.680 15.395  1.00 20.54 ? 79  GLN A N    1 
ATOM   1236 C  CA   . GLN A 1 77  ? 40.080 14.075 16.526  1.00 21.72 ? 79  GLN A CA   1 
ATOM   1237 C  C    . GLN A 1 77  ? 40.852 14.355 17.824  1.00 26.02 ? 79  GLN A C    1 
ATOM   1238 O  O    . GLN A 1 77  ? 40.252 14.604 18.865  1.00 27.20 ? 79  GLN A O    1 
ATOM   1239 C  CB   . GLN A 1 77  ? 39.874 12.574 16.307  1.00 24.12 ? 79  GLN A CB   1 
ATOM   1240 C  CG   . GLN A 1 77  ? 38.881 12.236 15.199  1.00 25.84 ? 79  GLN A CG   1 
ATOM   1241 C  CD   . GLN A 1 77  ? 37.464 12.617 15.561  1.00 25.96 ? 79  GLN A CD   1 
ATOM   1242 O  OE1  . GLN A 1 77  ? 37.013 12.359 16.678  1.00 28.20 ? 79  GLN A OE1  1 
ATOM   1243 N  NE2  . GLN A 1 77  ? 36.765 13.261 14.634  1.00 23.47 ? 79  GLN A NE2  1 
ATOM   1244 H  H    . GLN A 1 77  ? 41.074 14.112 14.822  1.00 17.39 ? 79  GLN A H    1 
ATOM   1245 H  HA   . GLN A 1 77  ? 39.204 14.485 16.608  1.00 18.73 ? 79  GLN A HA   1 
ATOM   1246 H  HB2  . GLN A 1 77  ? 40.726 12.174 16.072  1.00 20.89 ? 79  GLN A HB2  1 
ATOM   1247 H  HB3  . GLN A 1 77  ? 39.543 12.181 17.130  1.00 20.89 ? 79  GLN A HB3  1 
ATOM   1248 H  HG2  . GLN A 1 77  ? 39.127 12.720 14.395  1.00 23.02 ? 79  GLN A HG2  1 
ATOM   1249 H  HG3  . GLN A 1 77  ? 38.904 11.281 15.034  1.00 23.02 ? 79  GLN A HG3  1 
ATOM   1250 H  HE21 . GLN A 1 77  ? 37.123 13.441 13.873  1.00 21.78 ? 79  GLN A HE21 1 
ATOM   1251 H  HE22 . GLN A 1 77  ? 35.954 13.498 14.794  1.00 21.78 ? 79  GLN A HE22 1 
ATOM   1252 N  N    . THR A 1 78  ? 42.168 14.367 17.746  1.00 22.89 ? 80  THR A N    1 
ATOM   1253 C  CA   . THR A 1 78  ? 42.964 14.602 18.942  1.00 25.39 ? 80  THR A CA   1 
ATOM   1254 C  C    . THR A 1 78  ? 42.661 15.989 19.500  1.00 26.29 ? 80  THR A C    1 
ATOM   1255 O  O    . THR A 1 78  ? 42.522 16.169 20.717  1.00 27.76 ? 80  THR A O    1 
ATOM   1256 C  CB   . THR A 1 78  ? 44.453 14.451 18.647  1.00 25.67 ? 80  THR A CB   1 
ATOM   1257 O  OG1  . THR A 1 78  ? 44.722 13.098 18.283  1.00 32.77 ? 80  THR A OG1  1 
ATOM   1258 C  CG2  . THR A 1 78  ? 45.285 14.786 19.885  1.00 29.04 ? 80  THR A CG2  1 
ATOM   1259 H  H    . THR A 1 78  ? 42.623 14.245 17.027  1.00 20.38 ? 80  THR A H    1 
ATOM   1260 H  HA   . THR A 1 78  ? 42.723 13.948 19.616  1.00 22.44 ? 80  THR A HA   1 
ATOM   1261 H  HB   . THR A 1 78  ? 44.710 15.045 17.925  1.00 21.90 ? 80  THR A HB   1 
ATOM   1262 H  HG1  . THR A 1 78  ? 44.280 12.891 17.599  1.00 28.56 ? 80  THR A HG1  1 
ATOM   1263 H  HG21 . THR A 1 78  ? 46.229 14.687 19.687  1.00 24.78 ? 80  THR A HG21 1 
ATOM   1264 H  HG22 . THR A 1 78  ? 45.115 15.701 20.161  1.00 24.78 ? 80  THR A HG22 1 
ATOM   1265 H  HG23 . THR A 1 78  ? 45.051 14.189 20.613  1.00 24.78 ? 80  THR A HG23 1 
ATOM   1266 N  N    . LYS A 1 79  ? 42.524 16.956 18.597  1.00 22.79 ? 81  LYS A N    1 
ATOM   1267 C  CA   . LYS A 1 79  ? 42.199 18.322 18.970  1.00 25.06 ? 81  LYS A CA   1 
ATOM   1268 C  C    . LYS A 1 79  ? 40.748 18.461 19.384  1.00 24.64 ? 81  LYS A C    1 
ATOM   1269 O  O    . LYS A 1 79  ? 40.444 19.214 20.290  1.00 24.05 ? 81  LYS A O    1 
ATOM   1270 C  CB   . LYS A 1 79  ? 42.500 19.278 17.818  1.00 26.25 ? 81  LYS A CB   1 
ATOM   1271 C  CG   . LYS A 1 79  ? 43.983 19.328 17.490  1.00 26.45 ? 81  LYS A CG   1 
ATOM   1272 C  CD   . LYS A 1 79  ? 44.282 20.308 16.387  1.00 33.47 ? 81  LYS A CD   1 
ATOM   1273 C  CE   . LYS A 1 79  ? 45.770 20.386 16.123  1.00 37.19 ? 81  LYS A CE   1 
ATOM   1274 N  NZ   . LYS A 1 79  ? 46.098 21.371 15.051  1.00 40.73 ? 81  LYS A NZ   1 
ATOM   1275 H  H    . LYS A 1 79  ? 42.616 16.841 17.749  1.00 19.83 ? 81  LYS A H    1 
ATOM   1276 H  HA   . LYS A 1 79  ? 42.750 18.581 19.725  1.00 22.35 ? 81  LYS A HA   1 
ATOM   1277 H  HB2  . LYS A 1 79  ? 42.025 18.982 17.026  1.00 23.51 ? 81  LYS A HB2  1 
ATOM   1278 H  HB3  . LYS A 1 79  ? 42.214 20.172 18.064  1.00 23.51 ? 81  LYS A HB3  1 
ATOM   1279 H  HG2  . LYS A 1 79  ? 44.475 19.602 18.280  1.00 22.93 ? 81  LYS A HG2  1 
ATOM   1280 H  HG3  . LYS A 1 79  ? 44.276 18.450 17.202  1.00 22.93 ? 81  LYS A HG3  1 
ATOM   1281 H  HD2  . LYS A 1 79  ? 43.841 20.020 15.573  1.00 29.80 ? 81  LYS A HD2  1 
ATOM   1282 H  HD3  . LYS A 1 79  ? 43.971 21.190 16.646  1.00 29.80 ? 81  LYS A HD3  1 
ATOM   1283 H  HE2  . LYS A 1 79  ? 46.223 20.661 16.935  1.00 32.61 ? 81  LYS A HE2  1 
ATOM   1284 H  HE3  . LYS A 1 79  ? 46.089 19.514 15.841  1.00 32.61 ? 81  LYS A HE3  1 
ATOM   1285 H  HZ1  . LYS A 1 79  ? 46.978 21.394 14.919  1.00 35.88 ? 81  LYS A HZ1  1 
ATOM   1286 H  HZ2  . LYS A 1 79  ? 45.697 21.138 14.292  1.00 35.88 ? 81  LYS A HZ2  1 
ATOM   1287 H  HZ3  . LYS A 1 79  ? 45.820 22.182 15.289  1.00 35.88 ? 81  LYS A HZ3  1 
ATOM   1288 N  N    . LEU A 1 80  ? 39.842 17.785 18.684  1.00 18.73 ? 82  LEU A N    1 
ATOM   1289 C  CA   . LEU A 1 80  ? 38.427 17.931 18.955  1.00 21.48 ? 82  LEU A CA   1 
ATOM   1290 C  C    . LEU A 1 80  ? 38.051 17.320 20.316  1.00 18.94 ? 82  LEU A C    1 
ATOM   1291 O  O    . LEU A 1 80  ? 37.059 17.740 20.940  1.00 19.12 ? 82  LEU A O    1 
ATOM   1292 C  CB   . LEU A 1 80  ? 37.606 17.353 17.812  1.00 19.72 ? 82  LEU A CB   1 
ATOM   1293 C  CG   . LEU A 1 80  ? 37.639 18.214 16.539  1.00 16.74 ? 82  LEU A CG   1 
ATOM   1294 C  CD1  . LEU A 1 80  ? 37.200 17.406 15.340  1.00 18.53 ? 82  LEU A CD1  1 
ATOM   1295 C  CD2  . LEU A 1 80  ? 36.787 19.434 16.705  1.00 19.61 ? 82  LEU A CD2  1 
ATOM   1296 H  H    . LEU A 1 80  ? 40.026 17.236 18.048  1.00 16.68 ? 82  LEU A H    1 
ATOM   1297 H  HA   . LEU A 1 80  ? 38.224 18.879 19.002  1.00 19.98 ? 82  LEU A HA   1 
ATOM   1298 H  HB2  . LEU A 1 80  ? 37.955 16.476 17.588  1.00 18.60 ? 82  LEU A HB2  1 
ATOM   1299 H  HB3  . LEU A 1 80  ? 36.681 17.277 18.097  1.00 18.60 ? 82  LEU A HB3  1 
ATOM   1300 H  HG   . LEU A 1 80  ? 38.550 18.507 16.383  1.00 15.79 ? 82  LEU A HG   1 
ATOM   1301 H  HD11 . LEU A 1 80  ? 37.230 17.970 14.552  1.00 17.77 ? 82  LEU A HD11 1 
ATOM   1302 H  HD12 . LEU A 1 80  ? 37.801 16.652 15.230  1.00 17.77 ? 82  LEU A HD12 1 
ATOM   1303 H  HD13 . LEU A 1 80  ? 36.295 17.089 15.487  1.00 17.77 ? 82  LEU A HD13 1 
ATOM   1304 H  HD21 . LEU A 1 80  ? 36.825 19.958 15.890  1.00 19.01 ? 82  LEU A HD21 1 
ATOM   1305 H  HD22 . LEU A 1 80  ? 35.873 19.159 16.879  1.00 19.01 ? 82  LEU A HD22 1 
ATOM   1306 H  HD23 . LEU A 1 80  ? 37.123 19.955 17.451  1.00 19.01 ? 82  LEU A HD23 1 
ATOM   1307 N  N    . LYS A 1 81  ? 38.838 16.346 20.788  1.00 26.11 ? 83  LYS A N    1 
ATOM   1308 C  CA   . LYS A 1 81  ? 38.487 15.640 22.015  1.00 29.94 ? 83  LYS A CA   1 
ATOM   1309 C  C    . LYS A 1 81  ? 38.493 16.609 23.196  1.00 27.87 ? 83  LYS A C    1 
ATOM   1310 O  O    . LYS A 1 81  ? 37.771 16.425 24.161  1.00 30.40 ? 83  LYS A O    1 
ATOM   1311 C  CB   . LYS A 1 81  ? 39.427 14.452 22.249  1.00 36.86 ? 83  LYS A CB   1 
ATOM   1312 C  CG   . LYS A 1 81  ? 40.668 14.765 23.021  1.00 37.41 ? 83  LYS A CG   1 
ATOM   1313 C  CD   . LYS A 1 81  ? 41.558 13.521 23.136  1.00 38.08 ? 83  LYS A CD   1 
ATOM   1314 C  CE   . LYS A 1 81  ? 43.045 13.896 23.195  1.00 38.67 ? 83  LYS A CE   1 
ATOM   1315 N  NZ   . LYS A 1 81  ? 43.972 12.688 23.172  1.00 39.42 ? 83  LYS A NZ   1 
ATOM   1316 H  H    . LYS A 1 81  ? 39.568 16.081 20.420  1.00 19.93 ? 83  LYS A H    1 
ATOM   1317 H  HA   . LYS A 1 81  ? 37.587 15.290 21.926  1.00 23.58 ? 83  LYS A HA   1 
ATOM   1318 H  HB2  . LYS A 1 81  ? 38.943 13.769 22.738  1.00 29.90 ? 83  LYS A HB2  1 
ATOM   1319 H  HB3  . LYS A 1 81  ? 39.700 14.102 21.386  1.00 29.90 ? 83  LYS A HB3  1 
ATOM   1320 H  HG2  . LYS A 1 81  ? 41.168 15.458 22.562  1.00 29.90 ? 83  LYS A HG2  1 
ATOM   1321 H  HG3  . LYS A 1 81  ? 40.429 15.055 23.915  1.00 29.90 ? 83  LYS A HG3  1 
ATOM   1322 H  HD2  . LYS A 1 81  ? 41.333 13.041 23.949  1.00 29.90 ? 83  LYS A HD2  1 
ATOM   1323 H  HD3  . LYS A 1 81  ? 41.417 12.954 22.362  1.00 29.90 ? 83  LYS A HD3  1 
ATOM   1324 H  HE2  . LYS A 1 81  ? 43.260 14.452 22.429  1.00 29.90 ? 83  LYS A HE2  1 
ATOM   1325 H  HE3  . LYS A 1 81  ? 43.214 14.386 24.016  1.00 29.90 ? 83  LYS A HE3  1 
ATOM   1326 H  HZ1  . LYS A 1 81  ? 44.820 12.954 23.208  1.00 29.90 ? 83  LYS A HZ1  1 
ATOM   1327 H  HZ2  . LYS A 1 81  ? 43.804 12.163 23.871  1.00 29.90 ? 83  LYS A HZ2  1 
ATOM   1328 H  HZ3  . LYS A 1 81  ? 43.846 12.223 22.424  1.00 29.90 ? 83  LYS A HZ3  1 
ATOM   1329 N  N    . GLU A 1 82  ? 39.280 17.659 23.080  1.00 22.93 ? 84  GLU A N    1 
ATOM   1330 C  CA   . GLU A 1 82  ? 39.421 18.629 24.143  1.00 27.32 ? 84  GLU A CA   1 
ATOM   1331 C  C    . GLU A 1 82  ? 38.234 19.553 24.188  1.00 25.44 ? 84  GLU A C    1 
ATOM   1332 O  O    . GLU A 1 82  ? 37.973 20.136 25.221  1.00 26.04 ? 84  GLU A O    1 
ATOM   1333 C  CB   . GLU A 1 82  ? 40.690 19.473 23.953  1.00 35.76 ? 84  GLU A CB   1 
ATOM   1334 C  CG   . GLU A 1 82  ? 41.940 18.666 23.681  1.00 38.48 ? 84  GLU A CG   1 
ATOM   1335 C  CD   . GLU A 1 82  ? 43.181 19.540 23.560  1.00 52.52 ? 84  GLU A CD   1 
ATOM   1336 O  OE1  . GLU A 1 82  ? 44.175 19.095 22.934  1.00 55.51 ? 84  GLU A OE1  1 
ATOM   1337 O  OE2  . GLU A 1 82  ? 43.169 20.670 24.100  1.00 63.14 ? 84  GLU A OE2  1 
ATOM   1338 H  H    . GLU A 1 82  ? 39.752 17.835 22.383  1.00 19.19 ? 84  GLU A H    1 
ATOM   1339 H  HA   . GLU A 1 82  ? 39.483 18.169 24.994  1.00 23.40 ? 84  GLU A HA   1 
ATOM   1340 H  HB2  . GLU A 1 82  ? 40.556 20.071 23.201  1.00 31.45 ? 84  GLU A HB2  1 
ATOM   1341 H  HB3  . GLU A 1 82  ? 40.842 19.990 24.760  1.00 31.45 ? 84  GLU A HB3  1 
ATOM   1342 H  HG2  . GLU A 1 82  ? 42.080 18.043 24.412  1.00 33.66 ? 84  GLU A HG2  1 
ATOM   1343 H  HG3  . GLU A 1 82  ? 41.830 18.182 22.848  1.00 33.66 ? 84  GLU A HG3  1 
ATOM   1344 N  N    . VAL A 1 83  ? 37.515 19.694 23.078  1.00 18.57 ? 85  VAL A N    1 
ATOM   1345 C  CA   . VAL A 1 83  ? 36.428 20.671 23.037  1.00 17.81 ? 85  VAL A CA   1 
ATOM   1346 C  C    . VAL A 1 83  ? 35.036 20.062 22.851  1.00 14.51 ? 85  VAL A C    1 
ATOM   1347 O  O    . VAL A 1 83  ? 34.050 20.677 23.192  1.00 15.64 ? 85  VAL A O    1 
ATOM   1348 C  CB   . VAL A 1 83  ? 36.690 21.772 21.989  1.00 17.59 ? 85  VAL A CB   1 
ATOM   1349 C  CG1  . VAL A 1 83  ? 37.908 22.590 22.380  1.00 21.13 ? 85  VAL A CG1  1 
ATOM   1350 C  CG2  . VAL A 1 83  ? 36.846 21.176 20.598  1.00 17.28 ? 85  VAL A CG2  1 
ATOM   1351 H  H    . VAL A 1 83  ? 37.630 19.249 22.351  1.00 16.49 ? 85  VAL A H    1 
ATOM   1352 H  HA   . VAL A 1 83  ? 36.413 21.116 23.899  1.00 16.06 ? 85  VAL A HA   1 
ATOM   1353 H  HB   . VAL A 1 83  ? 35.928 22.371 21.970  1.00 15.94 ? 85  VAL A HB   1 
ATOM   1354 H  HG11 . VAL A 1 83  ? 38.056 23.275 21.710  1.00 18.98 ? 85  VAL A HG11 1 
ATOM   1355 H  HG12 . VAL A 1 83  ? 37.748 23.000 23.244  1.00 18.98 ? 85  VAL A HG12 1 
ATOM   1356 H  HG13 . VAL A 1 83  ? 38.679 22.003 22.430  1.00 18.98 ? 85  VAL A HG13 1 
ATOM   1357 H  HG21 . VAL A 1 83  ? 37.009 21.892 19.965  1.00 15.84 ? 85  VAL A HG21 1 
ATOM   1358 H  HG22 . VAL A 1 83  ? 37.594 20.559 20.601  1.00 15.84 ? 85  VAL A HG22 1 
ATOM   1359 H  HG23 . VAL A 1 83  ? 36.030 20.706 20.364  1.00 15.84 ? 85  VAL A HG23 1 
ATOM   1360 N  N    . PHE A 1 84  ? 34.930 18.849 22.341  1.00 14.92 ? 86  PHE A N    1 
ATOM   1361 C  CA   . PHE A 1 84  ? 33.631 18.248 22.130  1.00 15.26 ? 86  PHE A CA   1 
ATOM   1362 C  C    . PHE A 1 84  ? 32.734 18.187 23.381  1.00 15.50 ? 86  PHE A C    1 
ATOM   1363 O  O    . PHE A 1 84  ? 31.510 18.377 23.266  1.00 15.58 ? 86  PHE A O    1 
ATOM   1364 C  CB   . PHE A 1 84  ? 33.787 16.821 21.602  1.00 15.75 ? 86  PHE A CB   1 
ATOM   1365 C  CG   . PHE A 1 84  ? 33.948 16.686 20.098  1.00 17.03 ? 86  PHE A CG   1 
ATOM   1366 C  CD1  . PHE A 1 84  ? 33.509 17.628 19.201  1.00 15.95 ? 86  PHE A CD1  1 
ATOM   1367 C  CD2  . PHE A 1 84  ? 34.510 15.514 19.627  1.00 16.85 ? 86  PHE A CD2  1 
ATOM   1368 C  CE1  . PHE A 1 84  ? 33.641 17.403 17.823  1.00 16.77 ? 86  PHE A CE1  1 
ATOM   1369 C  CE2  . PHE A 1 84  ? 34.639 15.306 18.268  1.00 18.94 ? 86  PHE A CE2  1 
ATOM   1370 C  CZ   . PHE A 1 84  ? 34.210 16.225 17.393  1.00 17.68 ? 86  PHE A CZ   1 
ATOM   1371 H  H    . PHE A 1 84  ? 35.594 18.354 22.111  1.00 13.83 ? 86  PHE A H    1 
ATOM   1372 H  HA   . PHE A 1 84  ? 33.160 18.761 21.456  1.00 14.45 ? 86  PHE A HA   1 
ATOM   1373 H  HB2  . PHE A 1 84  ? 34.572 16.427 22.014  1.00 14.89 ? 86  PHE A HB2  1 
ATOM   1374 H  HB3  . PHE A 1 84  ? 33.000 16.313 21.855  1.00 14.89 ? 86  PHE A HB3  1 
ATOM   1375 H  HD1  . PHE A 1 84  ? 33.113 18.412 19.507  1.00 15.70 ? 86  PHE A HD1  1 
ATOM   1376 H  HD2  . PHE A 1 84  ? 34.797 14.863 20.226  1.00 16.03 ? 86  PHE A HD2  1 
ATOM   1377 H  HE1  . PHE A 1 84  ? 33.355 18.042 17.211  1.00 16.69 ? 86  PHE A HE1  1 
ATOM   1378 H  HE2  . PHE A 1 84  ? 35.025 14.519 17.958  1.00 18.27 ? 86  PHE A HE2  1 
ATOM   1379 H  HZ   . PHE A 1 84  ? 34.320 16.075 16.481  1.00 17.39 ? 86  PHE A HZ   1 
ATOM   1380 N  N    . PRO A 1 85  ? 33.310 17.923 24.567  1.00 16.20 ? 87  PRO A N    1 
ATOM   1381 C  CA   . PRO A 1 85  ? 32.440 17.871 25.742  1.00 17.35 ? 87  PRO A CA   1 
ATOM   1382 C  C    . PRO A 1 85  ? 31.733 19.171 26.101  1.00 15.82 ? 87  PRO A C    1 
ATOM   1383 O  O    . PRO A 1 85  ? 30.772 19.074 26.868  1.00 18.75 ? 87  PRO A O    1 
ATOM   1384 C  CB   . PRO A 1 85  ? 33.407 17.433 26.856  1.00 20.06 ? 87  PRO A CB   1 
ATOM   1385 C  CG   . PRO A 1 85  ? 34.466 16.694 26.200  1.00 22.07 ? 87  PRO A CG   1 
ATOM   1386 C  CD   . PRO A 1 85  ? 34.673 17.462 24.886  1.00 17.03 ? 87  PRO A CD   1 
ATOM   1387 H  HA   . PRO A 1 85  ? 31.771 17.178 25.622  1.00 15.45 ? 87  PRO A HA   1 
ATOM   1388 H  HB2  . PRO A 1 85  ? 33.765 18.217 27.301  1.00 17.64 ? 87  PRO A HB2  1 
ATOM   1389 H  HB3  . PRO A 1 85  ? 32.938 16.867 27.489  1.00 17.64 ? 87  PRO A HB3  1 
ATOM   1390 H  HG2  . PRO A 1 85  ? 35.270 16.711 26.743  1.00 19.60 ? 87  PRO A HG2  1 
ATOM   1391 H  HG3  . PRO A 1 85  ? 34.179 15.783 26.029  1.00 19.60 ? 87  PRO A HG3  1 
ATOM   1392 H  HD2  . PRO A 1 85  ? 35.264 18.219 25.024  1.00 14.99 ? 87  PRO A HD2  1 
ATOM   1393 H  HD3  . PRO A 1 85  ? 35.003 16.870 24.193  1.00 14.99 ? 87  PRO A HD3  1 
ATOM   1394 N  N    . THR A 1 86  ? 32.178 20.303 25.553  1.00 16.05 ? 88  THR A N    1 
ATOM   1395 C  CA   . THR A 1 86  ? 31.611 21.608 25.765  1.00 17.78 ? 88  THR A CA   1 
ATOM   1396 C  C    . THR A 1 86  ? 30.449 21.919 24.835  1.00 18.90 ? 88  THR A C    1 
ATOM   1397 O  O    . THR A 1 86  ? 29.923 23.016 24.898  1.00 19.39 ? 88  THR A O    1 
ATOM   1398 C  CB   . THR A 1 86  ? 32.672 22.710 25.626  1.00 20.56 ? 88  THR A CB   1 
ATOM   1399 O  OG1  . THR A 1 86  ? 33.048 22.875 24.260  1.00 20.00 ? 88  THR A OG1  1 
ATOM   1400 C  CG2  . THR A 1 86  ? 33.953 22.377 26.390  1.00 21.89 ? 88  THR A CG2  1 
ATOM   1401 H  H    . THR A 1 86  ? 32.853 20.325 25.022  1.00 14.21 ? 88  THR A H    1 
ATOM   1402 H  HA   . THR A 1 86  ? 31.271 21.647 26.673  1.00 15.91 ? 88  THR A HA   1 
ATOM   1403 H  HB   . THR A 1 86  ? 32.318 23.546 25.968  1.00 18.56 ? 88  THR A HB   1 
ATOM   1404 H  HG1  . THR A 1 86  ? 33.365 22.157 23.960  1.00 18.31 ? 88  THR A HG1  1 
ATOM   1405 H  HG21 . THR A 1 86  ? 34.599 23.093 26.280  1.00 19.50 ? 88  THR A HG21 1 
ATOM   1406 H  HG22 . THR A 1 86  ? 33.758 22.271 27.334  1.00 19.50 ? 88  THR A HG22 1 
ATOM   1407 H  HG23 . THR A 1 86  ? 34.336 21.552 26.052  1.00 19.50 ? 88  THR A HG23 1 
ATOM   1408 N  N    . ALA A 1 87  ? 30.084 20.946 23.998  1.00 18.08 ? 89  ALA A N    1 
ATOM   1409 C  CA   . ALA A 1 87  ? 28.970 21.119 23.043  1.00 18.74 ? 89  ALA A CA   1 
ATOM   1410 C  C    . ALA A 1 87  ? 27.726 21.626 23.787  1.00 18.83 ? 89  ALA A C    1 
ATOM   1411 O  O    . ALA A 1 87  ? 27.414 21.127 24.855  1.00 19.09 ? 89  ALA A O    1 
ATOM   1412 C  CB   . ALA A 1 87  ? 28.704 19.831 22.310  1.00 19.69 ? 89  ALA A CB   1 
ATOM   1413 H  H    . ALA A 1 87  ? 30.461 20.174 23.958  1.00 16.59 ? 89  ALA A H    1 
ATOM   1414 H  HA   . ALA A 1 87  ? 29.219 21.789 22.387  1.00 17.58 ? 89  ALA A HA   1 
ATOM   1415 H  HB1  . ALA A 1 87  ? 27.971 19.966 21.690  1.00 18.75 ? 89  ALA A HB1  1 
ATOM   1416 H  HB2  . ALA A 1 87  ? 29.504 19.572 21.826  1.00 18.75 ? 89  ALA A HB2  1 
ATOM   1417 H  HB3  . ALA A 1 87  ? 28.470 19.144 22.955  1.00 18.75 ? 89  ALA A HB3  1 
ATOM   1418 N  N    . ALA A 1 88  ? 27.058 22.646 23.252  1.00 15.90 ? 90  ALA A N    1 
ATOM   1419 C  CA   . ALA A 1 88  ? 25.814 23.160 23.815  1.00 14.29 ? 90  ALA A CA   1 
ATOM   1420 C  C    . ALA A 1 88  ? 24.593 22.797 22.957  1.00 11.82 ? 90  ALA A C    1 
ATOM   1421 O  O    . ALA A 1 88  ? 24.707 22.656 21.740  1.00 11.74 ? 90  ALA A O    1 
ATOM   1422 C  CB   . ALA A 1 88  ? 25.912 24.638 23.969  1.00 20.22 ? 90  ALA A CB   1 
ATOM   1423 H  H    . ALA A 1 88  ? 27.313 23.066 22.546  1.00 15.63 ? 90  ALA A H    1 
ATOM   1424 H  HA   . ALA A 1 88  ? 25.685 22.775 24.696  1.00 13.73 ? 90  ALA A HA   1 
ATOM   1425 H  HB1  . ALA A 1 88  ? 25.081 24.972 24.344  1.00 19.44 ? 90  ALA A HB1  1 
ATOM   1426 H  HB2  . ALA A 1 88  ? 26.650 24.845 24.564  1.00 19.44 ? 90  ALA A HB2  1 
ATOM   1427 H  HB3  . ALA A 1 88  ? 26.066 25.036 23.099  1.00 19.44 ? 90  ALA A HB3  1 
ATOM   1428 N  N    . LEU A 1 89  ? 23.456 22.649 23.569  1.00 14.69 ? 91  LEU A N    1 
ATOM   1429 C  CA   . LEU A 1 89  ? 22.216 22.398 22.888  1.00 14.35 ? 91  LEU A CA   1 
ATOM   1430 C  C    . LEU A 1 89  ? 21.790 23.589 22.102  1.00 12.83 ? 91  LEU A C    1 
ATOM   1431 O  O    . LEU A 1 89  ? 21.889 24.738 22.512  1.00 16.10 ? 91  LEU A O    1 
ATOM   1432 C  CB   . LEU A 1 89  ? 21.128 22.037 23.868  1.00 16.58 ? 91  LEU A CB   1 
ATOM   1433 C  CG   . LEU A 1 89  ? 21.312 20.634 24.425  1.00 16.82 ? 91  LEU A CG   1 
ATOM   1434 C  CD1  . LEU A 1 89  ? 20.444 20.497 25.690  1.00 22.68 ? 91  LEU A CD1  1 
ATOM   1435 C  CD2  . LEU A 1 89  ? 20.965 19.585 23.407  1.00 19.89 ? 91  LEU A CD2  1 
ATOM   1436 H  H    . LEU A 1 89  ? 23.370 22.692 24.423  1.00 13.56 ? 91  LEU A H    1 
ATOM   1437 H  HA   . LEU A 1 89  ? 22.332 21.655 22.276  1.00 13.29 ? 91  LEU A HA   1 
ATOM   1438 H  HB2  . LEU A 1 89  ? 21.146 22.663 24.609  1.00 14.97 ? 91  LEU A HB2  1 
ATOM   1439 H  HB3  . LEU A 1 89  ? 20.269 22.075 23.419  1.00 14.97 ? 91  LEU A HB3  1 
ATOM   1440 H  HG   . LEU A 1 89  ? 22.240 20.512 24.681  1.00 15.08 ? 91  LEU A HG   1 
ATOM   1441 H  HD11 . LEU A 1 89  ? 20.555 19.604 26.053  1.00 20.22 ? 91  LEU A HD11 1 
ATOM   1442 H  HD12 . LEU A 1 89  ? 20.728 21.157 26.341  1.00 20.22 ? 91  LEU A HD12 1 
ATOM   1443 H  HD13 . LEU A 1 89  ? 19.515 20.645 25.452  1.00 20.22 ? 91  LEU A HD13 1 
ATOM   1444 H  HD21 . LEU A 1 89  ? 21.095 18.708 23.800  1.00 18.46 ? 91  LEU A HD21 1 
ATOM   1445 H  HD22 . LEU A 1 89  ? 20.038 19.696 23.144  1.00 18.46 ? 91  LEU A HD22 1 
ATOM   1446 H  HD23 . LEU A 1 89  ? 21.543 19.692 22.635  1.00 18.46 ? 91  LEU A HD23 1 
ATOM   1447 N  N    . MET A 1 90  ? 21.331 23.326 20.879  1.00 12.76 ? 92  MET A N    1 
ATOM   1448 C  CA   . MET A 1 90  ? 20.909 24.385 19.979  1.00 13.42 ? 92  MET A CA   1 
ATOM   1449 C  C    . MET A 1 90  ? 19.559 24.988 20.416  1.00 14.98 ? 92  MET A C    1 
ATOM   1450 O  O    . MET A 1 90  ? 18.750 24.308 21.002  1.00 14.63 ? 92  MET A O    1 
ATOM   1451 C  CB   . MET A 1 90  ? 20.789 23.853 18.535  1.00 12.05 ? 92  MET A CB   1 
ATOM   1452 C  CG   . MET A 1 90  ? 22.125 23.563 17.963  1.00 12.69 ? 92  MET A CG   1 
ATOM   1453 S  SD   . MET A 1 90  ? 23.150 24.980 17.564  1.00 13.70 ? 92  MET A SD   1 
ATOM   1454 C  CE   . MET A 1 90  ? 22.373 25.445 15.999  1.00 15.60 ? 92  MET A CE   1 
ATOM   1455 H  H    . MET A 1 90  ? 21.255 22.535 20.550  1.00 11.76 ? 92  MET A H    1 
ATOM   1456 H  HA   . MET A 1 90  ? 21.580 25.085 19.983  1.00 12.49 ? 92  MET A HA   1 
ATOM   1457 H  HB2  . MET A 1 90  ? 20.272 23.032 18.536  1.00 11.59 ? 92  MET A HB2  1 
ATOM   1458 H  HB3  . MET A 1 90  ? 20.358 24.522 17.980  1.00 11.59 ? 92  MET A HB3  1 
ATOM   1459 H  HG2  . MET A 1 90  ? 22.617 23.023 18.601  1.00 12.62 ? 92  MET A HG2  1 
ATOM   1460 H  HG3  . MET A 1 90  ? 22.001 23.058 17.144  1.00 12.62 ? 92  MET A HG3  1 
ATOM   1461 H  HE1  . MET A 1 90  ? 22.446 24.704 15.378  1.00 15.72 ? 92  MET A HE1  1 
ATOM   1462 H  HE2  . MET A 1 90  ? 21.439 25.652 16.160  1.00 15.72 ? 92  MET A HE2  1 
ATOM   1463 H  HE3  . MET A 1 90  ? 22.827 26.224 15.640  1.00 15.72 ? 92  MET A HE3  1 
ATOM   1464 N  N    . PRO A 1 91  ? 19.301 26.245 20.026  1.00 13.43 ? 93  PRO A N    1 
ATOM   1465 C  CA   . PRO A 1 91  ? 18.010 26.846 20.373  1.00 18.51 ? 93  PRO A CA   1 
ATOM   1466 C  C    . PRO A 1 91  ? 16.812 26.083 19.874  1.00 17.36 ? 93  PRO A C    1 
ATOM   1467 O  O    . PRO A 1 91  ? 16.807 25.649 18.730  1.00 15.68 ? 93  PRO A O    1 
ATOM   1468 C  CB   . PRO A 1 91  ? 18.067 28.220 19.712  1.00 21.83 ? 93  PRO A CB   1 
ATOM   1469 C  CG   . PRO A 1 91  ? 19.490 28.474 19.493  1.00 22.42 ? 93  PRO A CG   1 
ATOM   1470 C  CD   . PRO A 1 91  ? 20.120 27.163 19.228  1.00 16.16 ? 93  PRO A CD   1 
ATOM   1471 H  HA   . PRO A 1 91  ? 17.940 26.957 21.334  1.00 16.86 ? 93  PRO A HA   1 
ATOM   1472 H  HB2  . PRO A 1 91  ? 17.588 28.198 18.869  1.00 20.06 ? 93  PRO A HB2  1 
ATOM   1473 H  HB3  . PRO A 1 91  ? 17.687 28.885 20.307  1.00 20.06 ? 93  PRO A HB3  1 
ATOM   1474 H  HG2  . PRO A 1 91  ? 19.598 29.062 18.729  1.00 21.00 ? 93  PRO A HG2  1 
ATOM   1475 H  HG3  . PRO A 1 91  ? 19.871 28.879 20.288  1.00 21.00 ? 93  PRO A HG3  1 
ATOM   1476 H  HD2  . PRO A 1 91  ? 20.060 26.941 18.286  1.00 15.30 ? 93  PRO A HD2  1 
ATOM   1477 H  HD3  . PRO A 1 91  ? 21.038 27.158 19.540  1.00 15.30 ? 93  PRO A HD3  1 
ATOM   1478 N  N    . GLY A 1 92  ? 15.803 25.914 20.720  1.00 16.99 ? 94  GLY A N    1 
ATOM   1479 C  CA   . GLY A 1 92  ? 14.633 25.142 20.376  1.00 17.09 ? 94  GLY A CA   1 
ATOM   1480 C  C    . GLY A 1 92  ? 14.720 23.651 20.532  1.00 18.04 ? 94  GLY A C    1 
ATOM   1481 O  O    . GLY A 1 92  ? 13.676 23.002 20.489  1.00 17.27 ? 94  GLY A O    1 
ATOM   1482 H  H    . GLY A 1 92  ? 15.779 26.246 21.513  1.00 15.21 ? 94  GLY A H    1 
ATOM   1483 H  HA2  . GLY A 1 92  ? 13.893 25.448 20.923  1.00 15.16 ? 94  GLY A HA2  1 
ATOM   1484 H  HA3  . GLY A 1 92  ? 14.408 25.324 19.450  1.00 15.16 ? 94  GLY A HA3  1 
ATOM   1485 N  N    . ALA A 1 93  ? 15.917 23.086 20.686  1.00 14.08 ? 95  ALA A N    1 
ATOM   1486 C  CA   . ALA A 1 93  ? 16.057 21.643 20.724  1.00 14.37 ? 95  ALA A CA   1 
ATOM   1487 C  C    . ALA A 1 93  ? 15.338 21.004 21.904  1.00 16.10 ? 95  ALA A C    1 
ATOM   1488 O  O    . ALA A 1 93  ? 14.605 20.036 21.746  1.00 16.46 ? 95  ALA A O    1 
ATOM   1489 C  CB   . ALA A 1 93  ? 17.493 21.229 20.676  1.00 14.93 ? 95  ALA A CB   1 
ATOM   1490 H  H    . ALA A 1 93  ? 16.656 23.518 20.769  1.00 12.92 ? 95  ALA A H    1 
ATOM   1491 H  HA   . ALA A 1 93  ? 15.640 21.289 19.923  1.00 13.36 ? 95  ALA A HA   1 
ATOM   1492 H  HB1  . ALA A 1 93  ? 17.543 20.260 20.703  1.00 14.41 ? 95  ALA A HB1  1 
ATOM   1493 H  HB2  . ALA A 1 93  ? 17.888 21.557 19.853  1.00 14.41 ? 95  ALA A HB2  1 
ATOM   1494 H  HB3  . ALA A 1 93  ? 17.956 21.606 21.440  1.00 14.41 ? 95  ALA A HB3  1 
ATOM   1495 N  N    . GLU A 1 94  ? 15.612 21.523 23.088  1.00 18.32 ? 96  GLU A N    1 
ATOM   1496 C  CA   . GLU A 1 94  ? 14.999 20.991 24.301  1.00 20.19 ? 96  GLU A CA   1 
ATOM   1497 C  C    . GLU A 1 94  ? 13.473 21.102 24.266  1.00 20.21 ? 96  GLU A C    1 
ATOM   1498 O  O    . GLU A 1 94  ? 12.774 20.141 24.572  1.00 19.89 ? 96  GLU A O    1 
ATOM   1499 C  CB   . GLU A 1 94  ? 15.514 21.718 25.546  1.00 25.52 ? 96  GLU A CB   1 
ATOM   1500 C  CG   . GLU A 1 94  ? 16.941 21.505 25.882  1.00 24.58 ? 96  GLU A CG   1 
ATOM   1501 C  CD   . GLU A 1 94  ? 17.294 22.038 27.269  1.00 37.88 ? 96  GLU A CD   1 
ATOM   1502 O  OE1  . GLU A 1 94  ? 16.369 22.260 28.084  1.00 42.65 ? 96  GLU A OE1  1 
ATOM   1503 O  OE2  . GLU A 1 94  ? 18.494 22.234 27.547  1.00 41.04 ? 96  GLU A OE2  1 
ATOM   1504 H  H    . GLU A 1 94  ? 16.148 22.182 23.221  1.00 16.15 ? 96  GLU A H    1 
ATOM   1505 H  HA   . GLU A 1 94  ? 15.229 20.053 24.385  1.00 17.26 ? 96  GLU A HA   1 
ATOM   1506 H  HB2  . GLU A 1 94  ? 15.386 22.670 25.417  1.00 22.19 ? 96  GLU A HB2  1 
ATOM   1507 H  HB3  . GLU A 1 94  ? 14.991 21.423 26.308  1.00 22.19 ? 96  GLU A HB3  1 
ATOM   1508 H  HG2  . GLU A 1 94  ? 17.133 20.555 25.866  1.00 21.66 ? 96  GLU A HG2  1 
ATOM   1509 H  HG3  . GLU A 1 94  ? 17.492 21.968 25.231  1.00 21.66 ? 96  GLU A HG3  1 
ATOM   1510 N  N    . LYS A 1 95  ? 12.972 22.259 23.849  1.00 19.53 ? 97  LYS A N    1 
ATOM   1511 C  CA   . LYS A 1 95  ? 11.536 22.504 23.793  1.00 22.63 ? 97  LYS A CA   1 
ATOM   1512 C  C    . LYS A 1 95  ? 10.856 21.470 22.907  1.00 20.05 ? 97  LYS A C    1 
ATOM   1513 O  O    . LYS A 1 95  ? 9.872  20.834 23.278  1.00 23.72 ? 97  LYS A O    1 
ATOM   1514 C  CB   . LYS A 1 95  ? 11.255 23.907 23.281  1.00 21.72 ? 97  LYS A CB   1 
ATOM   1515 C  CG   . LYS A 1 95  ? 9.770  24.259 23.268  1.00 30.55 ? 97  LYS A CG   1 
ATOM   1516 C  CD   . LYS A 1 95  ? 9.480  25.632 22.670  1.00 33.21 ? 97  LYS A CD   1 
ATOM   1517 C  CE   . LYS A 1 95  ? 7.994  25.972 22.759  1.00 37.69 ? 97  LYS A CE   1 
ATOM   1518 N  NZ   . LYS A 1 95  ? 7.678  27.221 22.023  1.00 40.35 ? 97  LYS A NZ   1 
ATOM   1519 H  H    . LYS A 1 95  ? 13.448 22.927 23.591  1.00 16.61 ? 97  LYS A H    1 
ATOM   1520 H  HA   . LYS A 1 95  ? 11.165 22.427 24.686  1.00 19.02 ? 97  LYS A HA   1 
ATOM   1521 H  HB2  . LYS A 1 95  ? 11.707 24.547 23.854  1.00 18.06 ? 97  LYS A HB2  1 
ATOM   1522 H  HB3  . LYS A 1 95  ? 11.588 23.983 22.373  1.00 18.06 ? 97  LYS A HB3  1 
ATOM   1523 H  HG2  . LYS A 1 95  ? 9.295  23.598 22.739  1.00 26.05 ? 97  LYS A HG2  1 
ATOM   1524 H  HG3  . LYS A 1 95  ? 9.437  24.254 24.179  1.00 26.05 ? 97  LYS A HG3  1 
ATOM   1525 H  HD2  . LYS A 1 95  ? 9.977  26.307 23.160  1.00 28.62 ? 97  LYS A HD2  1 
ATOM   1526 H  HD3  . LYS A 1 95  ? 9.739  25.637 21.735  1.00 28.62 ? 97  LYS A HD3  1 
ATOM   1527 H  HE2  . LYS A 1 95  ? 7.476  25.250 22.368  1.00 32.11 ? 97  LYS A HE2  1 
ATOM   1528 H  HE3  . LYS A 1 95  ? 7.748  26.097 23.689  1.00 32.11 ? 97  LYS A HE3  1 
ATOM   1529 H  HZ1  . LYS A 1 95  ? 6.809  27.401 22.087  1.00 34.66 ? 97  LYS A HZ1  1 
ATOM   1530 H  HZ2  . LYS A 1 95  ? 8.140  27.901 22.366  1.00 34.66 ? 97  LYS A HZ2  1 
ATOM   1531 H  HZ3  . LYS A 1 95  ? 7.892  27.131 21.164  1.00 34.66 ? 97  LYS A HZ3  1 
ATOM   1532 N  N    . LEU A 1 96  ? 11.412 21.259 21.734  1.00 20.19 ? 98  LEU A N    1 
ATOM   1533 C  CA   . LEU A 1 96  ? 10.806 20.344 20.784  1.00 20.35 ? 98  LEU A CA   1 
ATOM   1534 C  C    . LEU A 1 96  ? 10.849 18.892 21.296  1.00 18.78 ? 98  LEU A C    1 
ATOM   1535 O  O    . LEU A 1 96  ? 9.872  18.174 21.270  1.00 20.67 ? 98  LEU A O    1 
ATOM   1536 C  CB   . LEU A 1 96  ? 11.552 20.477 19.437  1.00 17.47 ? 98  LEU A CB   1 
ATOM   1537 C  CG   . LEU A 1 96  ? 11.053 19.536 18.319  1.00 17.86 ? 98  LEU A CG   1 
ATOM   1538 C  CD1  . LEU A 1 96  ? 9.505  19.581 18.079  1.00 17.94 ? 98  LEU A CD1  1 
ATOM   1539 C  CD2  . LEU A 1 96  ? 11.754 19.850 17.006  1.00 17.00 ? 98  LEU A CD2  1 
ATOM   1540 H  H    . LEU A 1 96  ? 12.138 21.630 21.460  1.00 16.78 ? 98  LEU A H    1 
ATOM   1541 H  HA   . LEU A 1 96  ? 9.878  20.591 20.646  1.00 17.08 ? 98  LEU A HA   1 
ATOM   1542 H  HB2  . LEU A 1 96  ? 11.452 21.388 19.119  1.00 15.12 ? 98  LEU A HB2  1 
ATOM   1543 H  HB3  . LEU A 1 96  ? 12.491 20.285 19.585  1.00 15.12 ? 98  LEU A HB3  1 
ATOM   1544 H  HG   . LEU A 1 96  ? 11.283 18.625 18.561  1.00 15.72 ? 98  LEU A HG   1 
ATOM   1545 H  HD11 . LEU A 1 96  ? 9.278  18.965 17.365  1.00 15.13 ? 98  LEU A HD11 1 
ATOM   1546 H  HD12 . LEU A 1 96  ? 9.052  19.323 18.897  1.00 15.13 ? 98  LEU A HD12 1 
ATOM   1547 H  HD13 . LEU A 1 96  ? 9.251  20.484 17.830  1.00 15.13 ? 98  LEU A HD13 1 
ATOM   1548 H  HD21 . LEU A 1 96  ? 11.425 19.247 16.321  1.00 15.66 ? 98  LEU A HD21 1 
ATOM   1549 H  HD22 . LEU A 1 96  ? 11.562 20.768 16.759  1.00 15.66 ? 98  LEU A HD22 1 
ATOM   1550 H  HD23 . LEU A 1 96  ? 12.709 19.730 17.122  1.00 15.66 ? 98  LEU A HD23 1 
ATOM   1551 N  N    . ILE A 1 97  ? 12.007 18.449 21.763  1.00 16.55 ? 99  ILE A N    1 
ATOM   1552 C  CA   . ILE A 1 97  ? 12.191 17.075 22.224  1.00 17.68 ? 99  ILE A CA   1 
ATOM   1553 C  C    . ILE A 1 97  ? 11.265 16.736 23.411  1.00 20.39 ? 99  ILE A C    1 
ATOM   1554 O  O    . ILE A 1 97  ? 10.663 15.677 23.452  1.00 19.57 ? 99  ILE A O    1 
ATOM   1555 C  CB   . ILE A 1 97  ? 13.691 16.813 22.512  1.00 17.31 ? 99  ILE A CB   1 
ATOM   1556 C  CG1  . ILE A 1 97  ? 14.381 16.219 21.284  1.00 18.06 ? 99  ILE A CG1  1 
ATOM   1557 C  CG2  . ILE A 1 97  ? 13.910 15.849 23.650  1.00 21.49 ? 99  ILE A CG2  1 
ATOM   1558 C  CD1  . ILE A 1 97  ? 14.364 17.086 20.052  1.00 18.69 ? 99  ILE A CD1  1 
ATOM   1559 H  H    . ILE A 1 97  ? 12.716 18.931 21.824  1.00 13.56 ? 99  ILE A H    1 
ATOM   1560 H  HA   . ILE A 1 97  ? 11.939 16.483 21.497  1.00 14.46 ? 99  ILE A HA   1 
ATOM   1561 H  HB   . ILE A 1 97  ? 14.117 17.656 22.732  1.00 14.61 ? 99  ILE A HB   1 
ATOM   1562 H  HG12 . ILE A 1 97  ? 15.310 16.047 21.506  1.00 16.09 ? 99  ILE A HG12 1 
ATOM   1563 H  HG13 . ILE A 1 97  ? 13.942 15.384 21.058  1.00 16.09 ? 99  ILE A HG13 1 
ATOM   1564 H  HG21 . ILE A 1 97  ? 14.864 15.727 23.780  1.00 18.23 ? 99  ILE A HG21 1 
ATOM   1565 H  HG22 . ILE A 1 97  ? 13.510 16.214 24.454  1.00 18.23 ? 99  ILE A HG22 1 
ATOM   1566 H  HG23 . ILE A 1 97  ? 13.495 15.000 23.428  1.00 18.23 ? 99  ILE A HG23 1 
ATOM   1567 H  HD11 . ILE A 1 97  ? 14.824 16.623 19.334  1.00 17.32 ? 99  ILE A HD11 1 
ATOM   1568 H  HD12 . ILE A 1 97  ? 13.443 17.257 19.800  1.00 17.32 ? 99  ILE A HD12 1 
ATOM   1569 H  HD13 . ILE A 1 97  ? 14.815 17.922 20.249  1.00 17.32 ? 99  ILE A HD13 1 
ATOM   1570 N  N    . ILE A 1 98  ? 11.148 17.654 24.354  1.00 20.67 ? 100 ILE A N    1 
ATOM   1571 C  CA   . ILE A 1 98  ? 10.297 17.421 25.518  1.00 21.42 ? 100 ILE A CA   1 
ATOM   1572 C  C    . ILE A 1 98  ? 8.831  17.341 25.103  1.00 23.83 ? 100 ILE A C    1 
ATOM   1573 O  O    . ILE A 1 98  ? 8.107  16.466 25.589  1.00 27.56 ? 100 ILE A O    1 
ATOM   1574 C  CB   . ILE A 1 98  ? 10.507 18.510 26.581  1.00 24.81 ? 100 ILE A CB   1 
ATOM   1575 C  CG1  . ILE A 1 98  ? 11.929 18.438 27.157  1.00 26.00 ? 100 ILE A CG1  1 
ATOM   1576 C  CG2  . ILE A 1 98  ? 9.533  18.335 27.723  1.00 25.95 ? 100 ILE A CG2  1 
ATOM   1577 C  CD1  . ILE A 1 98  ? 12.355 19.690 27.899  1.00 31.28 ? 100 ILE A CD1  1 
ATOM   1578 H  H    . ILE A 1 98  ? 11.546 18.416 24.349  1.00 17.51 ? 100 ILE A H    1 
ATOM   1579 H  HA   . ILE A 1 98  ? 10.538 16.570 25.916  1.00 17.17 ? 100 ILE A HA   1 
ATOM   1580 H  HB   . ILE A 1 98  ? 10.371 19.381 26.176  1.00 20.19 ? 100 ILE A HB   1 
ATOM   1581 H  HG12 . ILE A 1 98  ? 11.976 17.695 27.779  1.00 21.85 ? 100 ILE A HG12 1 
ATOM   1582 H  HG13 . ILE A 1 98  ? 12.554 18.297 26.429  1.00 21.85 ? 100 ILE A HG13 1 
ATOM   1583 H  HG21 . ILE A 1 98  ? 9.686  19.033 28.378  1.00 20.10 ? 100 ILE A HG21 1 
ATOM   1584 H  HG22 . ILE A 1 98  ? 8.628  18.397 27.378  1.00 20.10 ? 100 ILE A HG22 1 
ATOM   1585 H  HG23 . ILE A 1 98  ? 9.674  17.464 28.127  1.00 20.10 ? 100 ILE A HG23 1 
ATOM   1586 H  HD11 . ILE A 1 98  ? 13.258 19.568 28.231  1.00 27.01 ? 100 ILE A HD11 1 
ATOM   1587 H  HD12 . ILE A 1 98  ? 12.325 20.443 27.288  1.00 27.01 ? 100 ILE A HD12 1 
ATOM   1588 H  HD13 . ILE A 1 98  ? 11.746 19.840 28.639  1.00 27.01 ? 100 ILE A HD13 1 
ATOM   1589 N  N    . HIS A 1 99  ? 8.410  18.216 24.188  1.00 21.60 ? 101 HIS A N    1 
ATOM   1590 C  CA   . HIS A 1 99  ? 7.069  18.189 23.592  1.00 21.40 ? 101 HIS A CA   1 
ATOM   1591 C  C    . HIS A 1 99  ? 6.728  16.841 22.917  1.00 22.51 ? 101 HIS A C    1 
ATOM   1592 O  O    . HIS A 1 99  ? 5.668  16.256 23.146  1.00 25.71 ? 101 HIS A O    1 
ATOM   1593 C  CB   . HIS A 1 99  ? 6.974  19.356 22.606  1.00 23.27 ? 101 HIS A CB   1 
ATOM   1594 C  CG   . HIS A 1 99  ? 5.683  19.439 21.867  1.00 25.11 ? 101 HIS A CG   1 
ATOM   1595 N  ND1  . HIS A 1 99  ? 4.503  19.831 22.469  1.00 27.14 ? 101 HIS A ND1  1 
ATOM   1596 C  CD2  . HIS A 1 99  ? 5.376  19.160 20.580  1.00 24.55 ? 101 HIS A CD2  1 
ATOM   1597 C  CE1  . HIS A 1 99  ? 3.533  19.809 21.576  1.00 28.59 ? 101 HIS A CE1  1 
ATOM   1598 N  NE2  . HIS A 1 99  ? 4.031  19.396 20.425  1.00 25.20 ? 101 HIS A NE2  1 
ATOM   1599 H  H    . HIS A 1 99  ? 8.899  18.856 23.886  1.00 18.23 ? 101 HIS A H    1 
ATOM   1600 H  HA   . HIS A 1 99  ? 6.415  18.341 24.292  1.00 17.50 ? 101 HIS A HA   1 
ATOM   1601 H  HB2  . HIS A 1 99  ? 7.087  20.185 23.095  1.00 19.88 ? 101 HIS A HB2  1 
ATOM   1602 H  HB3  . HIS A 1 99  ? 7.683  19.265 21.950  1.00 19.88 ? 101 HIS A HB3  1 
ATOM   1603 H  HD1  . HIS A 1 99  ? 4.419  20.068 23.291  1.00 22.16 ? 101 HIS A HD1  1 
ATOM   1604 H  HD2  . HIS A 1 99  ? 5.965  18.866 19.923  1.00 21.12 ? 101 HIS A HD2  1 
ATOM   1605 H  HE1  . HIS A 1 99  ? 2.644  20.031 21.735  1.00 23.37 ? 101 HIS A HE1  1 
ATOM   1606 H  HE2  . HIS A 1 99  ? 3.588  19.300 19.694  1.00 20.93 ? 101 HIS A HE2  1 
ATOM   1607 N  N    . LEU A 1 100 ? 7.618  16.349 22.059  1.00 21.32 ? 102 LEU A N    1 
ATOM   1608 C  CA   . LEU A 1 100 ? 7.426  15.046 21.448  1.00 22.73 ? 102 LEU A CA   1 
ATOM   1609 C  C    . LEU A 1 100 ? 7.276  13.910 22.463  1.00 25.04 ? 102 LEU A C    1 
ATOM   1610 O  O    . LEU A 1 100 ? 6.430  13.039 22.324  1.00 25.13 ? 102 LEU A O    1 
ATOM   1611 C  CB   . LEU A 1 100 ? 8.619  14.774 20.504  1.00 18.77 ? 102 LEU A CB   1 
ATOM   1612 C  CG   . LEU A 1 100 ? 8.767  15.766 19.342  1.00 19.69 ? 102 LEU A CG   1 
ATOM   1613 C  CD1  . LEU A 1 100 ? 10.102 15.519 18.606  1.00 16.11 ? 102 LEU A CD1  1 
ATOM   1614 C  CD2  . LEU A 1 100 ? 7.587  15.724 18.431  1.00 19.61 ? 102 LEU A CD2  1 
ATOM   1615 H  H    . LEU A 1 100 ? 8.339  16.752 21.816  1.00 16.93 ? 102 LEU A H    1 
ATOM   1616 H  HA   . LEU A 1 100 ? 6.620  15.070 20.909  1.00 18.32 ? 102 LEU A HA   1 
ATOM   1617 H  HB2  . LEU A 1 100 ? 9.438  14.809 21.024  1.00 15.47 ? 102 LEU A HB2  1 
ATOM   1618 H  HB3  . LEU A 1 100 ? 8.514  13.889 20.122  1.00 15.47 ? 102 LEU A HB3  1 
ATOM   1619 H  HG   . LEU A 1 100 ? 8.807  16.662 19.713  1.00 17.16 ? 102 LEU A HG   1 
ATOM   1620 H  HD11 . LEU A 1 100 ? 10.182 16.152 17.875  1.00 14.56 ? 102 LEU A HD11 1 
ATOM   1621 H  HD12 . LEU A 1 100 ? 10.834 15.641 19.231  1.00 14.56 ? 102 LEU A HD12 1 
ATOM   1622 H  HD13 . LEU A 1 100 ? 10.109 14.613 18.261  1.00 14.56 ? 102 LEU A HD13 1 
ATOM   1623 H  HD21 . LEU A 1 100 ? 7.720  16.363 17.713  1.00 16.81 ? 102 LEU A HD21 1 
ATOM   1624 H  HD22 . LEU A 1 100 ? 7.503  14.829 18.066  1.00 16.81 ? 102 LEU A HD22 1 
ATOM   1625 H  HD23 . LEU A 1 100 ? 6.791  15.952 18.935  1.00 16.81 ? 102 LEU A HD23 1 
ATOM   1626 N  N    . ARG A 1 101 ? 8.122  13.920 23.480  1.00 24.93 ? 103 ARG A N    1 
ATOM   1627 C  CA   . ARG A 1 101 ? 8.127  12.840 24.466  1.00 25.42 ? 103 ARG A CA   1 
ATOM   1628 C  C    . ARG A 1 101 ? 6.800  12.849 25.244  1.00 27.76 ? 103 ARG A C    1 
ATOM   1629 O  O    . ARG A 1 101 ? 6.191  11.809 25.485  1.00 33.42 ? 103 ARG A O    1 
ATOM   1630 C  CB   . ARG A 1 101 ? 9.395  13.011 25.336  1.00 29.48 ? 103 ARG A CB   1 
ATOM   1631 C  CG   . ARG A 1 101 ? 9.462  12.307 26.647  1.00 29.79 ? 103 ARG A CG   1 
ATOM   1632 C  CD   . ARG A 1 101 ? 9.674  10.874 26.462  1.00 30.38 ? 103 ARG A CD   1 
ATOM   1633 N  NE   . ARG A 1 101 ? 10.418 10.226 27.556  1.00 30.44 ? 103 ARG A NE   1 
ATOM   1634 C  CZ   . ARG A 1 101 ? 11.210 9.184  27.369  1.00 34.11 ? 103 ARG A CZ   1 
ATOM   1635 N  NH1  . ARG A 1 101 ? 11.439 8.742  26.147  1.00 33.31 ? 103 ARG A NH1  1 
ATOM   1636 N  NH2  . ARG A 1 101 ? 11.799 8.591  28.374  1.00 33.75 ? 103 ARG A NH2  1 
ATOM   1637 H  H    . ARG A 1 101 ? 8.703  14.536 23.626  1.00 19.36 ? 103 ARG A H    1 
ATOM   1638 H  HA   . ARG A 1 101 ? 8.196  11.990 24.003  1.00 19.07 ? 103 ARG A HA   1 
ATOM   1639 H  HB2  . ARG A 1 101 ? 10.155 12.707 24.815  1.00 23.47 ? 103 ARG A HB2  1 
ATOM   1640 H  HB3  . ARG A 1 101 ? 9.501  13.958 25.522  1.00 23.47 ? 103 ARG A HB3  1 
ATOM   1641 H  HG2  . ARG A 1 101 ? 10.202 12.661 27.165  1.00 22.89 ? 103 ARG A HG2  1 
ATOM   1642 H  HG3  . ARG A 1 101 ? 8.626  12.433 27.123  1.00 22.89 ? 103 ARG A HG3  1 
ATOM   1643 H  HD2  . ARG A 1 101 ? 8.811  10.438 26.394  1.00 23.27 ? 103 ARG A HD2  1 
ATOM   1644 H  HD3  . ARG A 1 101 ? 10.176 10.737 25.643  1.00 23.27 ? 103 ARG A HD3  1 
ATOM   1645 H  HE   . ARG A 1 101 ? 10.203 10.427 28.364  1.00 22.91 ? 103 ARG A HE   1 
ATOM   1646 H  HH11 . ARG A 1 101 ? 11.044 9.108  25.476  1.00 26.59 ? 103 ARG A HH11 1 
ATOM   1647 H  HH12 . ARG A 1 101 ? 11.964 8.073  26.023  1.00 26.59 ? 103 ARG A HH12 1 
ATOM   1648 H  HH21 . ARG A 1 101 ? 11.679 8.881  29.175  1.00 25.89 ? 103 ARG A HH21 1 
ATOM   1649 H  HH22 . ARG A 1 101 ? 12.341 7.939  28.230  1.00 25.89 ? 103 ARG A HH22 1 
ATOM   1650 N  N    . LYS A 1 102 ? 6.343  14.049 25.548  1.00 24.97 ? 104 LYS A N    1 
ATOM   1651 C  CA   . LYS A 1 102 ? 5.110  14.231 26.298  1.00 29.67 ? 104 LYS A CA   1 
ATOM   1652 C  C    . LYS A 1 102 ? 3.890  13.718 25.538  1.00 33.93 ? 104 LYS A C    1 
ATOM   1653 O  O    . LYS A 1 102 ? 2.975  13.160 26.128  1.00 35.66 ? 104 LYS A O    1 
ATOM   1654 C  CB   . LYS A 1 102 ? 4.963  15.708 26.650  1.00 31.64 ? 104 LYS A CB   1 
ATOM   1655 C  CG   . LYS A 1 102 ? 3.684  16.060 27.379  1.00 41.55 ? 104 LYS A CG   1 
ATOM   1656 C  CD   . LYS A 1 102 ? 3.557  17.561 27.595  1.00 46.26 ? 104 LYS A CD   1 
ATOM   1657 C  CE   . LYS A 1 102 ? 4.537  18.050 28.652  1.00 52.98 ? 104 LYS A CE   1 
ATOM   1658 N  NZ   . LYS A 1 102 ? 4.237  19.449 29.163  1.00 60.18 ? 104 LYS A NZ   1 
ATOM   1659 H  H    . LYS A 1 102 ? 6.732  14.785 25.331  1.00 20.48 ? 104 LYS A H    1 
ATOM   1660 H  HA   . LYS A 1 102 ? 5.172  13.733 27.129  1.00 23.89 ? 104 LYS A HA   1 
ATOM   1661 H  HB2  . LYS A 1 102 ? 5.705  15.966 27.219  1.00 25.82 ? 104 LYS A HB2  1 
ATOM   1662 H  HB3  . LYS A 1 102 ? 4.985  16.225 25.830  1.00 25.82 ? 104 LYS A HB3  1 
ATOM   1663 H  HG2  . LYS A 1 102 ? 2.925  15.764 26.853  1.00 34.34 ? 104 LYS A HG2  1 
ATOM   1664 H  HG3  . LYS A 1 102 ? 3.681  15.627 28.246  1.00 34.34 ? 104 LYS A HG3  1 
ATOM   1665 H  HD2  . LYS A 1 102 ? 3.749  18.023 26.764  1.00 39.00 ? 104 LYS A HD2  1 
ATOM   1666 H  HD3  . LYS A 1 102 ? 2.658  17.767 27.895  1.00 39.00 ? 104 LYS A HD3  1 
ATOM   1667 H  HE2  . LYS A 1 102 ? 4.508  17.445 29.410  1.00 45.86 ? 104 LYS A HE2  1 
ATOM   1668 H  HE3  . LYS A 1 102 ? 5.429  18.058 28.272  1.00 45.86 ? 104 LYS A HE3  1 
ATOM   1669 H  HZ1  . LYS A 1 102 ? 4.838  19.684 29.776  1.00 52.57 ? 104 LYS A HZ1  1 
ATOM   1670 H  HZ2  . LYS A 1 102 ? 4.267  20.031 28.490  1.00 52.57 ? 104 LYS A HZ2  1 
ATOM   1671 H  HZ3  . LYS A 1 102 ? 3.426  19.472 29.529  1.00 52.57 ? 104 LYS A HZ3  1 
ATOM   1672 N  N    . HIS A 1 103 ? 3.885  13.887 24.224  1.00 29.99 ? 105 HIS A N    1 
ATOM   1673 C  CA   . HIS A 1 103 ? 2.778  13.439 23.401  1.00 31.39 ? 105 HIS A CA   1 
ATOM   1674 C  C    . HIS A 1 103 ? 3.006  12.063 22.792  1.00 28.92 ? 105 HIS A C    1 
ATOM   1675 O  O    . HIS A 1 103 ? 2.269  11.632 21.910  1.00 29.98 ? 105 HIS A O    1 
ATOM   1676 C  CB   . HIS A 1 103 ? 2.524  14.465 22.305  1.00 32.20 ? 105 HIS A CB   1 
ATOM   1677 C  CG   . HIS A 1 103 ? 1.861  15.717 22.785  1.00 32.83 ? 105 HIS A CG   1 
ATOM   1678 N  ND1  . HIS A 1 103 ? 2.557  16.815 23.234  1.00 32.18 ? 105 HIS A ND1  1 
ATOM   1679 C  CD2  . HIS A 1 103 ? 0.551  16.040 22.888  1.00 33.37 ? 105 HIS A CD2  1 
ATOM   1680 C  CE1  . HIS A 1 103 ? 1.709  17.761 23.592  1.00 33.43 ? 105 HIS A CE1  1 
ATOM   1681 N  NE2  . HIS A 1 103 ? 0.485  17.318 23.385  1.00 36.13 ? 105 HIS A NE2  1 
ATOM   1682 H  H    . HIS A 1 103 ? 4.520  14.262 23.781  1.00 22.88 ? 105 HIS A H    1 
ATOM   1683 H  HA   . HIS A 1 103 ? 1.981  13.390 23.952  1.00 23.81 ? 105 HIS A HA   1 
ATOM   1684 H  HB2  . HIS A 1 103 ? 3.374  14.714 21.908  1.00 25.27 ? 105 HIS A HB2  1 
ATOM   1685 H  HB3  . HIS A 1 103 ? 1.951  14.067 21.631  1.00 25.27 ? 105 HIS A HB3  1 
ATOM   1686 H  HD1  . HIS A 1 103 ? 3.413  16.875 23.276  1.00 25.12 ? 105 HIS A HD1  1 
ATOM   1687 H  HD2  . HIS A 1 103 ? -0.170 15.500 22.657  1.00 24.77 ? 105 HIS A HD2  1 
ATOM   1688 H  HE1  . HIS A 1 103 ? 1.936  18.598 23.926  1.00 25.58 ? 105 HIS A HE1  1 
ATOM   1689 N  N    . GLY A 1 104 ? 4.047  11.388 23.260  1.00 29.72 ? 106 GLY A N    1 
ATOM   1690 C  CA   . GLY A 1 104 ? 4.343  10.039 22.839  1.00 28.43 ? 106 GLY A CA   1 
ATOM   1691 C  C    . GLY A 1 104 ? 4.675  9.881  21.374  1.00 25.98 ? 106 GLY A C    1 
ATOM   1692 O  O    . GLY A 1 104 ? 4.401  8.845  20.786  1.00 29.58 ? 106 GLY A O    1 
ATOM   1693 H  H    . GLY A 1 104 ? 4.605  11.702 23.834  1.00 22.90 ? 106 GLY A H    1 
ATOM   1694 H  HA2  . GLY A 1 104 ? 5.096  9.709  23.353  1.00 21.62 ? 106 GLY A HA2  1 
ATOM   1695 H  HA3  . GLY A 1 104 ? 3.578  9.475  23.033  1.00 21.62 ? 106 GLY A HA3  1 
ATOM   1696 N  N    . ILE A 1 105 ? 5.268  10.916 20.785  1.00 24.53 ? 107 ILE A N    1 
ATOM   1697 C  CA   . ILE A 1 105 ? 5.657  10.866 19.382  1.00 24.01 ? 107 ILE A CA   1 
ATOM   1698 C  C    . ILE A 1 105 ? 7.035  10.225 19.341  1.00 21.35 ? 107 ILE A C    1 
ATOM   1699 O  O    . ILE A 1 105 ? 7.955  10.757 19.949  1.00 21.26 ? 107 ILE A O    1 
ATOM   1700 C  CB   . ILE A 1 105 ? 5.769  12.255 18.755  1.00 21.87 ? 107 ILE A CB   1 
ATOM   1701 C  CG1  . ILE A 1 105 ? 4.487  13.060 18.910  1.00 27.15 ? 107 ILE A CG1  1 
ATOM   1702 C  CG2  . ILE A 1 105 ? 6.158  12.144 17.276  1.00 21.81 ? 107 ILE A CG2  1 
ATOM   1703 C  CD1  . ILE A 1 105 ? 3.276  12.413 18.382  1.00 31.31 ? 107 ILE A CD1  1 
ATOM   1704 H  H    . ILE A 1 105 ? 5.456  11.658 21.177  1.00 19.47 ? 107 ILE A H    1 
ATOM   1705 H  HA   . ILE A 1 105 ? 5.032  10.327 18.872  1.00 19.89 ? 107 ILE A HA   1 
ATOM   1706 H  HB   . ILE A 1 105 ? 6.478  12.733 19.215  1.00 18.52 ? 107 ILE A HB   1 
ATOM   1707 H  HG12 . ILE A 1 105 ? 4.341  13.228 19.854  1.00 23.09 ? 107 ILE A HG12 1 
ATOM   1708 H  HG13 . ILE A 1 105 ? 4.595  13.904 18.443  1.00 23.09 ? 107 ILE A HG13 1 
ATOM   1709 H  HG21 . ILE A 1 105 ? 6.224  13.035 16.899  1.00 19.34 ? 107 ILE A HG21 1 
ATOM   1710 H  HG22 . ILE A 1 105 ? 7.014  11.692 17.209  1.00 19.34 ? 107 ILE A HG22 1 
ATOM   1711 H  HG23 . ILE A 1 105 ? 5.477  11.636 16.809  1.00 19.34 ? 107 ILE A HG23 1 
ATOM   1712 H  HD11 . ILE A 1 105 ? 2.517  13.000 18.527  1.00 26.50 ? 107 ILE A HD11 1 
ATOM   1713 H  HD12 . ILE A 1 105 ? 3.393  12.251 17.433  1.00 26.50 ? 107 ILE A HD12 1 
ATOM   1714 H  HD13 . ILE A 1 105 ? 3.138  11.573 18.848  1.00 26.50 ? 107 ILE A HD13 1 
ATOM   1715 N  N    . PRO A 1 106 ? 7.182  9.074  18.688  1.00 19.72 ? 108 PRO A N    1 
ATOM   1716 C  CA   . PRO A 1 106 ? 8.494  8.428  18.628  1.00 22.06 ? 108 PRO A CA   1 
ATOM   1717 C  C    . PRO A 1 106 ? 9.495  9.268  17.869  1.00 18.93 ? 108 PRO A C    1 
ATOM   1718 O  O    . PRO A 1 106 ? 9.163  9.856  16.816  1.00 19.49 ? 108 PRO A O    1 
ATOM   1719 C  CB   . PRO A 1 106 ? 8.232  7.138  17.859  1.00 21.27 ? 108 PRO A CB   1 
ATOM   1720 C  CG   . PRO A 1 106 ? 6.722  6.980  17.893  1.00 27.74 ? 108 PRO A CG   1 
ATOM   1721 C  CD   . PRO A 1 106 ? 6.169  8.329  17.932  1.00 24.55 ? 108 PRO A CD   1 
ATOM   1722 H  HA   . PRO A 1 106 ? 8.828  8.227  19.516  1.00 19.00 ? 108 PRO A HA   1 
ATOM   1723 H  HB2  . PRO A 1 106 ? 8.549  7.228  16.946  1.00 17.86 ? 108 PRO A HB2  1 
ATOM   1724 H  HB3  . PRO A 1 106 ? 8.667  6.395  18.305  1.00 17.86 ? 108 PRO A HB3  1 
ATOM   1725 H  HG2  . PRO A 1 106 ? 6.427  6.516  17.094  1.00 23.38 ? 108 PRO A HG2  1 
ATOM   1726 H  HG3  . PRO A 1 106 ? 6.467  6.485  18.687  1.00 23.38 ? 108 PRO A HG3  1 
ATOM   1727 H  HD2  . PRO A 1 106 ? 6.083  8.688  17.035  1.00 20.41 ? 108 PRO A HD2  1 
ATOM   1728 H  HD3  . PRO A 1 106 ? 5.321  8.335  18.403  1.00 20.41 ? 108 PRO A HD3  1 
ATOM   1729 N  N    . PHE A 1 107 ? 10.732 9.282  18.358  1.00 17.60 ? 109 PHE A N    1 
ATOM   1730 C  CA   . PHE A 1 107 ? 11.778 9.954  17.643  1.00 16.30 ? 109 PHE A CA   1 
ATOM   1731 C  C    . PHE A 1 107 ? 13.115 9.336  17.957  1.00 16.96 ? 109 PHE A C    1 
ATOM   1732 O  O    . PHE A 1 107 ? 13.319 8.695  19.003  1.00 17.29 ? 109 PHE A O    1 
ATOM   1733 C  CB   . PHE A 1 107 ? 11.788 11.448 17.936  1.00 16.47 ? 109 PHE A CB   1 
ATOM   1734 C  CG   . PHE A 1 107 ? 12.006 11.818 19.382  1.00 15.44 ? 109 PHE A CG   1 
ATOM   1735 C  CD1  . PHE A 1 107 ? 10.921 11.946 20.239  1.00 17.70 ? 109 PHE A CD1  1 
ATOM   1736 C  CD2  . PHE A 1 107 ? 13.271 12.113 19.850  1.00 15.84 ? 109 PHE A CD2  1 
ATOM   1737 C  CE1  . PHE A 1 107 ? 11.116 12.300 21.570  1.00 19.65 ? 109 PHE A CE1  1 
ATOM   1738 C  CE2  . PHE A 1 107 ? 13.475 12.483 21.165  1.00 18.12 ? 109 PHE A CE2  1 
ATOM   1739 C  CZ   . PHE A 1 107 ? 12.389 12.601 22.017  1.00 18.21 ? 109 PHE A CZ   1 
ATOM   1740 H  H    . PHE A 1 107 ? 10.978 8.911  19.094  1.00 14.75 ? 109 PHE A H    1 
ATOM   1741 H  HA   . PHE A 1 107 ? 11.621 9.843  16.692  1.00 14.45 ? 109 PHE A HA   1 
ATOM   1742 H  HB2  . PHE A 1 107 ? 12.499 11.858 17.419  1.00 14.99 ? 109 PHE A HB2  1 
ATOM   1743 H  HB3  . PHE A 1 107 ? 10.934 11.820 17.665  1.00 14.99 ? 109 PHE A HB3  1 
ATOM   1744 H  HD1  . PHE A 1 107 ? 10.064 11.755 19.932  1.00 15.01 ? 109 PHE A HD1  1 
ATOM   1745 H  HD2  . PHE A 1 107 ? 13.999 12.047 19.275  1.00 14.43 ? 109 PHE A HD2  1 
ATOM   1746 H  HE1  . PHE A 1 107 ? 10.388 12.379 22.144  1.00 16.55 ? 109 PHE A HE1  1 
ATOM   1747 H  HE2  . PHE A 1 107 ? 14.333 12.670 21.471  1.00 16.34 ? 109 PHE A HE2  1 
ATOM   1748 H  HZ   . PHE A 1 107 ? 12.524 12.834 22.907  1.00 15.60 ? 109 PHE A HZ   1 
ATOM   1749 N  N    . ALA A 1 108 ? 14.060 9.555  17.067  1.00 15.48 ? 110 ALA A N    1 
ATOM   1750 C  CA   . ALA A 1 108 ? 15.330 8.868  17.150  1.00 15.40 ? 110 ALA A CA   1 
ATOM   1751 C  C    . ALA A 1 108 ? 16.449 9.752  16.602  1.00 13.82 ? 110 ALA A C    1 
ATOM   1752 O  O    . ALA A 1 108 ? 16.171 10.803 16.015  1.00 13.18 ? 110 ALA A O    1 
ATOM   1753 C  CB   . ALA A 1 108 ? 15.242 7.546  16.415  1.00 17.46 ? 110 ALA A CB   1 
ATOM   1754 H  H    . ALA A 1 108 ? 13.991 10.098 16.404  1.00 13.38 ? 110 ALA A H    1 
ATOM   1755 H  HA   . ALA A 1 108 ? 15.527 8.680  18.081  1.00 13.45 ? 110 ALA A HA   1 
ATOM   1756 H  HB1  . ALA A 1 108 ? 16.097 7.093  16.476  1.00 15.19 ? 110 ALA A HB1  1 
ATOM   1757 H  HB2  . ALA A 1 108 ? 14.550 7.003  16.825  1.00 15.19 ? 110 ALA A HB2  1 
ATOM   1758 H  HB3  . ALA A 1 108 ? 15.022 7.716  15.486  1.00 15.19 ? 110 ALA A HB3  1 
ATOM   1759 N  N    . LEU A 1 109 ? 17.702 9.360  16.801  1.00 12.33 ? 111 LEU A N    1 
ATOM   1760 C  CA   . LEU A 1 109 ? 18.868 10.131 16.362  1.00 12.94 ? 111 LEU A CA   1 
ATOM   1761 C  C    . LEU A 1 109 ? 19.642 9.334  15.321  1.00 13.48 ? 111 LEU A C    1 
ATOM   1762 O  O    . LEU A 1 109 ? 19.802 8.129  15.468  1.00 15.34 ? 111 LEU A O    1 
ATOM   1763 C  CB   . LEU A 1 109 ? 19.753 10.387 17.582  1.00 13.59 ? 111 LEU A CB   1 
ATOM   1764 C  CG   . LEU A 1 109 ? 20.843 11.451 17.424  1.00 10.92 ? 111 LEU A CG   1 
ATOM   1765 C  CD1  . LEU A 1 109 ? 20.283 12.855 17.539  1.00 16.05 ? 111 LEU A CD1  1 
ATOM   1766 C  CD2  . LEU A 1 109 ? 21.927 11.213 18.487  1.00 15.88 ? 111 LEU A CD2  1 
ATOM   1767 H  H    . LEU A 1 109 ? 17.911 8.628  17.200  1.00 10.62 ? 111 LEU A H    1 
ATOM   1768 H  HA   . LEU A 1 109 ? 18.590 10.978 15.981  1.00 11.90 ? 111 LEU A HA   1 
ATOM   1769 H  HB2  . LEU A 1 109 ? 19.184 10.665 18.317  1.00 12.45 ? 111 LEU A HB2  1 
ATOM   1770 H  HB3  . LEU A 1 109 ? 20.196 9.556  17.816  1.00 12.45 ? 111 LEU A HB3  1 
ATOM   1771 H  HG   . LEU A 1 109 ? 21.252 11.360 16.549  1.00 10.35 ? 111 LEU A HG   1 
ATOM   1772 H  HD11 . LEU A 1 109 ? 21.006 13.493 17.432  1.00 15.73 ? 111 LEU A HD11 1 
ATOM   1773 H  HD12 . LEU A 1 109 ? 19.620 12.988 16.844  1.00 15.73 ? 111 LEU A HD12 1 
ATOM   1774 H  HD13 . LEU A 1 109 ? 19.874 12.961 18.412  1.00 15.73 ? 111 LEU A HD13 1 
ATOM   1775 H  HD21 . LEU A 1 109 ? 22.618 11.886 18.389  1.00 15.08 ? 111 LEU A HD21 1 
ATOM   1776 H  HD22 . LEU A 1 109 ? 21.525 11.278 19.368  1.00 15.08 ? 111 LEU A HD22 1 
ATOM   1777 H  HD23 . LEU A 1 109 ? 22.305 10.329 18.360  1.00 15.08 ? 111 LEU A HD23 1 
ATOM   1778 N  N    . ALA A 1 110 ? 20.117 9.999  14.249  1.00 12.56 ? 112 ALA A N    1 
ATOM   1779 C  CA   . ALA A 1 110 ? 20.825 9.365  13.147  1.00 13.23 ? 112 ALA A CA   1 
ATOM   1780 C  C    . ALA A 1 110 ? 21.946 10.338 12.804  1.00 12.97 ? 112 ALA A C    1 
ATOM   1781 O  O    . ALA A 1 110 ? 21.732 11.412 12.158  1.00 10.33 ? 112 ALA A O    1 
ATOM   1782 C  CB   . ALA A 1 110 ? 19.881 9.154  11.999  1.00 14.30 ? 112 ALA A CB   1 
ATOM   1783 H  H    . ALA A 1 110 ? 20.031 10.849 14.147  1.00 11.83 ? 112 ALA A H    1 
ATOM   1784 H  HA   . ALA A 1 110 ? 21.201 8.515  13.424  1.00 12.62 ? 112 ALA A HA   1 
ATOM   1785 H  HB1  . ALA A 1 110 ? 20.362 8.731  11.270  1.00 13.73 ? 112 ALA A HB1  1 
ATOM   1786 H  HB2  . ALA A 1 110 ? 19.153 8.584  12.290  1.00 13.73 ? 112 ALA A HB2  1 
ATOM   1787 H  HB3  . ALA A 1 110 ? 19.535 10.014 11.713  1.00 13.73 ? 112 ALA A HB3  1 
ATOM   1788 N  N    . THR A 1 111 ? 23.147 9.996  13.255  1.00 10.42 ? 113 THR A N    1 
ATOM   1789 C  CA   . THR A 1 111 ? 24.324 10.828 13.189  1.00 13.76 ? 113 THR A CA   1 
ATOM   1790 C  C    . THR A 1 111 ? 25.477 10.059 12.591  1.00 13.15 ? 113 THR A C    1 
ATOM   1791 O  O    . THR A 1 111 ? 25.716 8.907  12.966  1.00 15.09 ? 113 THR A O    1 
ATOM   1792 C  CB   . THR A 1 111 ? 24.778 11.355 14.591  1.00 11.41 ? 113 THR A CB   1 
ATOM   1793 O  OG1  . THR A 1 111 ? 26.079 11.927 14.486  1.00 13.11 ? 113 THR A OG1  1 
ATOM   1794 C  CG2  . THR A 1 111 ? 24.791 10.272 15.621  1.00 17.75 ? 113 THR A CG2  1 
ATOM   1795 H  H    . THR A 1 111 ? 23.304 9.236  13.625  1.00 10.49 ? 113 THR A H    1 
ATOM   1796 H  HA   . THR A 1 111 ? 24.142 11.593 12.621  1.00 14.13 ? 113 THR A HA   1 
ATOM   1797 H  HB   . THR A 1 111 ? 24.157 12.040 14.885  1.00 11.69 ? 113 THR A HB   1 
ATOM   1798 H  HG1  . THR A 1 111 ? 26.070 12.566 13.941  1.00 13.55 ? 113 THR A HG1  1 
ATOM   1799 H  HG21 . THR A 1 111 ? 25.076 10.632 16.476  1.00 17.48 ? 113 THR A HG21 1 
ATOM   1800 H  HG22 . THR A 1 111 ? 23.902 9.896  15.718  1.00 17.48 ? 113 THR A HG22 1 
ATOM   1801 H  HG23 . THR A 1 111 ? 25.403 9.569  15.355  1.00 17.48 ? 113 THR A HG23 1 
ATOM   1802 N  N    . SER A 1 112 ? 26.243 10.681 11.711  1.00 12.83 ? 114 SER A N    1 
ATOM   1803 C  CA   . SER A 1 112 ? 27.401 10.026 11.120  1.00 12.68 ? 114 SER A CA   1 
ATOM   1804 C  C    . SER A 1 112 ? 28.601 9.983  12.052  1.00 15.11 ? 114 SER A C    1 
ATOM   1805 O  O    . SER A 1 112 ? 29.649 9.428  11.707  1.00 15.36 ? 114 SER A O    1 
ATOM   1806 C  CB   . SER A 1 112 ? 27.783 10.657 9.787   1.00 12.78 ? 114 SER A CB   1 
ATOM   1807 O  OG   . SER A 1 112 ? 26.738 10.466 8.835   1.00 13.63 ? 114 SER A OG   1 
ATOM   1808 H  H    . SER A 1 112 ? 26.115 11.486 11.437  1.00 12.77 ? 114 SER A H    1 
ATOM   1809 H  HA   . SER A 1 112 ? 27.157 9.106  10.935  1.00 12.36 ? 114 SER A HA   1 
ATOM   1810 H  HB2  . SER A 1 112 ? 27.926 11.608 9.914   1.00 12.73 ? 114 SER A HB2  1 
ATOM   1811 H  HB3  . SER A 1 112 ? 28.593 10.239 9.457   1.00 12.73 ? 114 SER A HB3  1 
ATOM   1812 H  HG   . SER A 1 112 ? 26.951 10.815 8.101   1.00 13.71 ? 114 SER A HG   1 
ATOM   1813 N  N    . SER A 1 113 ? 28.455 10.611 13.211  1.00 11.64 ? 115 SER A N    1 
ATOM   1814 C  CA   . SER A 1 113 ? 29.511 10.608 14.237  1.00 13.71 ? 115 SER A CA   1 
ATOM   1815 C  C    . SER A 1 113 ? 29.790 9.170  14.670  1.00 14.40 ? 115 SER A C    1 
ATOM   1816 O  O    . SER A 1 113 ? 28.855 8.397  14.793  1.00 15.84 ? 115 SER A O    1 
ATOM   1817 C  CB   . SER A 1 113 ? 29.012 11.403 15.442  1.00 16.68 ? 115 SER A CB   1 
ATOM   1818 O  OG   . SER A 1 113 ? 29.928 11.483 16.512  1.00 21.12 ? 115 SER A OG   1 
ATOM   1819 H  H    . SER A 1 113 ? 27.752 11.052 13.437  1.00 12.00 ? 115 SER A H    1 
ATOM   1820 H  HA   . SER A 1 113 ? 30.324 11.010 13.894  1.00 13.78 ? 115 SER A HA   1 
ATOM   1821 H  HB2  . SER A 1 113 ? 28.810 12.305 15.148  1.00 16.89 ? 115 SER A HB2  1 
ATOM   1822 H  HB3  . SER A 1 113 ? 28.200 10.983 15.768  1.00 16.89 ? 115 SER A HB3  1 
ATOM   1823 H  HG   . SER A 1 113 ? 29.597 11.931 17.141  1.00 21.05 ? 115 SER A HG   1 
ATOM   1824 N  N    . GLY A 1 114 ? 31.048 8.845  14.971  1.00 14.93 ? 116 GLY A N    1 
ATOM   1825 C  CA   . GLY A 1 114 ? 31.360 7.547  15.541  1.00 20.33 ? 116 GLY A CA   1 
ATOM   1826 C  C    . GLY A 1 114 ? 31.107 7.482  17.041  1.00 18.96 ? 116 GLY A C    1 
ATOM   1827 O  O    . GLY A 1 114 ? 30.750 8.454  17.675  1.00 17.70 ? 116 GLY A O    1 
ATOM   1828 H  H    . GLY A 1 114 ? 31.730 9.356  14.854  1.00 14.78 ? 116 GLY A H    1 
ATOM   1829 H  HA2  . GLY A 1 114 ? 30.817 6.868  15.110  1.00 19.51 ? 116 GLY A HA2  1 
ATOM   1830 H  HA3  . GLY A 1 114 ? 32.293 7.340  15.379  1.00 19.51 ? 116 GLY A HA3  1 
ATOM   1831 N  N    . SER A 1 115 ? 31.317 6.305  17.615  1.00 21.02 ? 117 SER A N    1 
ATOM   1832 C  CA   . SER A 1 115 ? 31.007 6.063  19.013  1.00 20.18 ? 117 SER A CA   1 
ATOM   1833 C  C    . SER A 1 115 ? 31.731 6.972  19.985  1.00 17.89 ? 117 SER A C    1 
ATOM   1834 O  O    . SER A 1 115 ? 31.136 7.534  20.891  1.00 17.33 ? 117 SER A O    1 
ATOM   1835 C  CB   . SER A 1 115 ? 31.367 4.610  19.395  1.00 22.60 ? 117 SER A CB   1 
ATOM   1836 O  OG   . SER A 1 115 ? 30.591 3.659  18.674  1.00 33.07 ? 117 SER A OG   1 
ATOM   1837 H  H    . SER A 1 115 ? 31.644 5.621  17.209  1.00 19.39 ? 117 SER A H    1 
ATOM   1838 H  HA   . SER A 1 115 ? 30.054 6.181  19.148  1.00 18.20 ? 117 SER A HA   1 
ATOM   1839 H  HB2  . SER A 1 115 ? 32.305 4.459  19.200  1.00 19.73 ? 117 SER A HB2  1 
ATOM   1840 H  HB3  . SER A 1 115 ? 31.206 4.488  20.344  1.00 19.73 ? 117 SER A HB3  1 
ATOM   1841 H  HG   . SER A 1 115 ? 30.721 3.748  17.849  1.00 29.95 ? 117 SER A HG   1 
ATOM   1842 N  N    . ALA A 1 116 ? 33.021 7.148  19.796  1.00 18.01 ? 118 ALA A N    1 
ATOM   1843 C  CA   . ALA A 1 116 ? 33.779 7.929  20.778  1.00 19.24 ? 118 ALA A CA   1 
ATOM   1844 C  C    . ALA A 1 116 ? 33.399 9.378  20.709  1.00 18.11 ? 118 ALA A C    1 
ATOM   1845 O  O    . ALA A 1 116 ? 33.182 10.035 21.709  1.00 18.46 ? 118 ALA A O    1 
ATOM   1846 C  CB   . ALA A 1 116 ? 35.284 7.795  20.561  1.00 21.91 ? 118 ALA A CB   1 
ATOM   1847 H  H    . ALA A 1 116 ? 33.479 6.842  19.135  1.00 16.24 ? 118 ALA A H    1 
ATOM   1848 H  HA   . ALA A 1 116 ? 33.572 7.605  21.669  1.00 17.44 ? 118 ALA A HA   1 
ATOM   1849 H  HB1  . ALA A 1 116 ? 35.747 8.325  21.229  1.00 19.74 ? 118 ALA A HB1  1 
ATOM   1850 H  HB2  . ALA A 1 116 ? 35.534 6.862  20.648  1.00 19.74 ? 118 ALA A HB2  1 
ATOM   1851 H  HB3  . ALA A 1 116 ? 35.505 8.116  19.673  1.00 19.74 ? 118 ALA A HB3  1 
ATOM   1852 N  N    . SER A 1 117 ? 33.289 9.853  19.491  1.00 18.50 ? 119 SER A N    1 
ATOM   1853 C  CA   . SER A 1 117 ? 32.878 11.223 19.250  1.00 14.68 ? 119 SER A CA   1 
ATOM   1854 C  C    . SER A 1 117 ? 31.490 11.500 19.855  1.00 14.59 ? 119 SER A C    1 
ATOM   1855 O  O    . SER A 1 117 ? 31.275 12.473 20.553  1.00 12.81 ? 119 SER A O    1 
ATOM   1856 C  CB   . SER A 1 117 ? 32.873 11.449 17.733  1.00 20.56 ? 119 SER A CB   1 
ATOM   1857 O  OG   . SER A 1 117 ? 32.257 12.662 17.367  1.00 25.87 ? 119 SER A OG   1 
ATOM   1858 H  H    . SER A 1 117 ? 33.446 9.401  18.776  1.00 17.36 ? 119 SER A H    1 
ATOM   1859 H  HA   . SER A 1 117 ? 33.519 11.831 19.652  1.00 14.13 ? 119 SER A HA   1 
ATOM   1860 H  HB2  . SER A 1 117 ? 33.791 11.461 17.419  1.00 20.35 ? 119 SER A HB2  1 
ATOM   1861 H  HB3  . SER A 1 117 ? 32.394 10.718 17.313  1.00 20.35 ? 119 SER A HB3  1 
ATOM   1862 H  HG   . SER A 1 117 ? 31.458 12.667 17.627  1.00 26.19 ? 119 SER A HG   1 
ATOM   1863 N  N    . PHE A 1 118 ? 30.559 10.605 19.618  1.00 13.13 ? 120 PHE A N    1 
ATOM   1864 C  CA   . PHE A 1 118 ? 29.225 10.752 20.223  1.00 16.08 ? 120 PHE A CA   1 
ATOM   1865 C  C    . PHE A 1 118 ? 29.295 10.772 21.740  1.00 16.13 ? 120 PHE A C    1 
ATOM   1866 O  O    . PHE A 1 118 ? 28.684 11.622 22.365  1.00 14.87 ? 120 PHE A O    1 
ATOM   1867 C  CB   . PHE A 1 118 ? 28.344 9.622  19.757  1.00 16.04 ? 120 PHE A CB   1 
ATOM   1868 C  CG   . PHE A 1 118 ? 27.025 9.590  20.405  1.00 17.49 ? 120 PHE A CG   1 
ATOM   1869 C  CD1  . PHE A 1 118 ? 25.983 10.337 19.911  1.00 19.93 ? 120 PHE A CD1  1 
ATOM   1870 C  CD2  . PHE A 1 118 ? 26.802 8.774  21.518  1.00 20.01 ? 120 PHE A CD2  1 
ATOM   1871 C  CE1  . PHE A 1 118 ? 24.762 10.321 20.529  1.00 17.76 ? 120 PHE A CE1  1 
ATOM   1872 C  CE2  . PHE A 1 118 ? 25.567 8.751  22.115  1.00 22.95 ? 120 PHE A CE2  1 
ATOM   1873 C  CZ   . PHE A 1 118 ? 24.547 9.523  21.608  1.00 20.79 ? 120 PHE A CZ   1 
ATOM   1874 H  H    . PHE A 1 118 ? 30.655 9.910  19.121  1.00 12.01 ? 120 PHE A H    1 
ATOM   1875 H  HA   . PHE A 1 118 ? 28.830 11.586 19.927  1.00 15.00 ? 120 PHE A HA   1 
ATOM   1876 H  HB2  . PHE A 1 118 ? 28.203 9.710  18.801  1.00 14.75 ? 120 PHE A HB2  1 
ATOM   1877 H  HB3  . PHE A 1 118 ? 28.788 8.781  19.947  1.00 14.75 ? 120 PHE A HB3  1 
ATOM   1878 H  HD1  . PHE A 1 118 ? 26.120 10.889 19.175  1.00 18.89 ? 120 PHE A HD1  1 
ATOM   1879 H  HD2  . PHE A 1 118 ? 27.494 8.255  21.860  1.00 17.94 ? 120 PHE A HD2  1 
ATOM   1880 H  HE1  . PHE A 1 118 ? 24.064 10.832 20.187  1.00 16.48 ? 120 PHE A HE1  1 
ATOM   1881 H  HE2  . PHE A 1 118 ? 25.419 8.213  22.859  1.00 20.64 ? 120 PHE A HE2  1 
ATOM   1882 H  HZ   . PHE A 1 118 ? 23.711 9.508  22.015  1.00 18.87 ? 120 PHE A HZ   1 
ATOM   1883 N  N    A ASP A 1 119 ? 30.040 9.834  22.328  0.53 17.17 ? 121 ASP A N    1 
ATOM   1884 N  N    B ASP A 1 119 ? 30.046 9.844  22.322  0.47 17.18 ? 121 ASP A N    1 
ATOM   1885 C  CA   A ASP A 1 119 ? 30.189 9.793  23.781  0.53 19.55 ? 121 ASP A CA   1 
ATOM   1886 C  CA   B ASP A 1 119 ? 30.159 9.785  23.768  0.47 19.54 ? 121 ASP A CA   1 
ATOM   1887 C  C    A ASP A 1 119 ? 30.694 11.132 24.305  0.53 16.82 ? 121 ASP A C    1 
ATOM   1888 C  C    B ASP A 1 119 ? 30.709 11.109 24.319  0.47 16.85 ? 121 ASP A C    1 
ATOM   1889 O  O    A ASP A 1 119 ? 30.144 11.685 25.244  0.53 16.06 ? 121 ASP A O    1 
ATOM   1890 O  O    B ASP A 1 119 ? 30.182 11.640 25.283  0.47 16.14 ? 121 ASP A O    1 
ATOM   1891 C  CB   A ASP A 1 119 ? 31.173 8.709  24.215  0.53 21.18 ? 121 ASP A CB   1 
ATOM   1892 C  CB   B ASP A 1 119 ? 31.037 8.607  24.186  0.47 21.18 ? 121 ASP A CB   1 
ATOM   1893 C  CG   A ASP A 1 119 ? 30.637 7.313  24.022  0.53 23.87 ? 121 ASP A CG   1 
ATOM   1894 C  CG   B ASP A 1 119 ? 31.084 8.421  25.683  0.47 23.14 ? 121 ASP A CG   1 
ATOM   1895 O  OD1  A ASP A 1 119 ? 29.404 7.139  23.899  0.53 23.20 ? 121 ASP A OD1  1 
ATOM   1896 O  OD1  B ASP A 1 119 ? 30.075 7.983  26.267  0.47 24.58 ? 121 ASP A OD1  1 
ATOM   1897 O  OD2  A ASP A 1 119 ? 31.472 6.373  24.015  0.53 24.42 ? 121 ASP A OD2  1 
ATOM   1898 O  OD2  B ASP A 1 119 ? 32.138 8.721  26.256  0.47 26.86 ? 121 ASP A OD2  1 
ATOM   1899 H  H    A ASP A 1 119 ? 30.467 9.215  21.910  0.53 16.13 ? 121 ASP A H    1 
ATOM   1900 H  H    B ASP A 1 119 ? 30.495 9.241  21.904  0.47 16.13 ? 121 ASP A H    1 
ATOM   1901 H  HA   A ASP A 1 119 ? 29.328 9.608  24.188  0.53 18.03 ? 121 ASP A HA   1 
ATOM   1902 H  HA   B ASP A 1 119 ? 29.277 9.648  24.147  0.47 18.03 ? 121 ASP A HA   1 
ATOM   1903 H  HB2  A ASP A 1 119 ? 31.985 8.793  23.692  0.53 19.01 ? 121 ASP A HB2  1 
ATOM   1904 H  HB2  B ASP A 1 119 ? 30.684 7.794  23.793  0.47 19.01 ? 121 ASP A HB2  1 
ATOM   1905 H  HB3  A ASP A 1 119 ? 31.373 8.824  25.158  0.53 19.01 ? 121 ASP A HB3  1 
ATOM   1906 H  HB3  B ASP A 1 119 ? 31.943 8.761  23.874  0.47 19.01 ? 121 ASP A HB3  1 
ATOM   1907 N  N    . MET A 1 120 ? 31.730 11.671 23.682  1.00 16.48 ? 122 MET A N    1 
ATOM   1908 C  CA   . MET A 1 120 ? 32.284 12.961 24.145  1.00 15.10 ? 122 MET A CA   1 
ATOM   1909 C  C    . MET A 1 120 ? 31.284 14.088 24.019  1.00 15.39 ? 122 MET A C    1 
ATOM   1910 O  O    . MET A 1 120 ? 31.249 14.999 24.836  1.00 15.96 ? 122 MET A O    1 
ATOM   1911 C  CB   . MET A 1 120 ? 33.565 13.360 23.422  1.00 19.67 ? 122 MET A CB   1 
ATOM   1912 C  CG   . MET A 1 120 ? 34.733 12.416 23.661  1.00 21.09 ? 122 MET A CG   1 
ATOM   1913 S  SD   . MET A 1 120 ? 36.161 12.777 22.578  1.00 38.15 ? 122 MET A SD   1 
ATOM   1914 C  CE   . MET A 1 120 ? 37.069 11.209 22.695  1.00 33.07 ? 122 MET A CE   1 
ATOM   1915 H  H    A MET A 1 120 ? 32.131 11.329 23.002  0.53 15.41 ? 122 MET A H    1 
ATOM   1916 H  H    B MET A 1 120 ? 32.120 11.341 22.990  0.47 15.41 ? 122 MET A H    1 
ATOM   1917 H  HA   . MET A 1 120 ? 32.509 12.866 25.084  1.00 14.19 ? 122 MET A HA   1 
ATOM   1918 H  HB2  . MET A 1 120 ? 33.391 13.378 22.468  1.00 18.86 ? 122 MET A HB2  1 
ATOM   1919 H  HB3  . MET A 1 120 ? 33.832 14.242 23.724  1.00 18.86 ? 122 MET A HB3  1 
ATOM   1920 H  HG2  . MET A 1 120 ? 35.025 12.501 24.582  1.00 19.74 ? 122 MET A HG2  1 
ATOM   1921 H  HG3  . MET A 1 120 ? 34.445 11.506 23.486  1.00 19.74 ? 122 MET A HG3  1 
ATOM   1922 H  HE1  . MET A 1 120 ? 37.871 11.268 22.151  1.00 31.00 ? 122 MET A HE1  1 
ATOM   1923 H  HE2  . MET A 1 120 ? 37.308 11.051 23.621  1.00 31.00 ? 122 MET A HE2  1 
ATOM   1924 H  HE3  . MET A 1 120 ? 36.502 10.491 22.371  1.00 31.00 ? 122 MET A HE3  1 
ATOM   1925 N  N    . LYS A 1 121 ? 30.582 14.140 22.905  1.00 14.44 ? 123 LYS A N    1 
ATOM   1926 C  CA   . LYS A 1 121 ? 29.716 15.260 22.642  1.00 14.49 ? 123 LYS A CA   1 
ATOM   1927 C  C    . LYS A 1 121 ? 28.510 15.289 23.556  1.00 13.98 ? 123 LYS A C    1 
ATOM   1928 O  O    . LYS A 1 121 ? 28.043 16.391 23.858  1.00 15.03 ? 123 LYS A O    1 
ATOM   1929 C  CB   . LYS A 1 121 ? 29.217 15.216 21.209  1.00 12.28 ? 123 LYS A CB   1 
ATOM   1930 C  CG   . LYS A 1 121 ? 30.346 15.514 20.210  1.00 13.25 ? 123 LYS A CG   1 
ATOM   1931 C  CD   . LYS A 1 121 ? 29.838 15.159 18.853  1.00 14.71 ? 123 LYS A CD   1 
ATOM   1932 C  CE   . LYS A 1 121 ? 30.847 15.325 17.808  1.00 12.63 ? 123 LYS A CE   1 
ATOM   1933 N  NZ   . LYS A 1 121 ? 30.377 14.702 16.525  1.00 15.37 ? 123 LYS A NZ   1 
ATOM   1934 H  H    . LYS A 1 121 ? 30.591 13.540 22.289  1.00 13.21 ? 123 LYS A H    1 
ATOM   1935 H  HA   . LYS A 1 121 ? 30.211 16.084 22.767  1.00 13.63 ? 123 LYS A HA   1 
ATOM   1936 H  HB2  . LYS A 1 121 ? 28.868 14.331 21.019  1.00 11.83 ? 123 LYS A HB2  1 
ATOM   1937 H  HB3  . LYS A 1 121 ? 28.523 15.883 21.091  1.00 11.83 ? 123 LYS A HB3  1 
ATOM   1938 H  HG2  . LYS A 1 121 ? 30.568 16.458 20.230  1.00 13.00 ? 123 LYS A HG2  1 
ATOM   1939 H  HG3  . LYS A 1 121 ? 31.122 14.967 20.411  1.00 13.00 ? 123 LYS A HG3  1 
ATOM   1940 H  HD2  . LYS A 1 121 ? 29.557 14.231 18.853  1.00 14.75 ? 123 LYS A HD2  1 
ATOM   1941 H  HD3  . LYS A 1 121 ? 29.086 15.733 18.637  1.00 14.75 ? 123 LYS A HD3  1 
ATOM   1942 H  HE2  . LYS A 1 121 ? 31.000 16.271 17.653  1.00 12.77 ? 123 LYS A HE2  1 
ATOM   1943 H  HE3  . LYS A 1 121 ? 31.669 14.888 18.079  1.00 12.77 ? 123 LYS A HE3  1 
ATOM   1944 H  HZ1  . LYS A 1 121 ? 30.994 14.806 15.893  1.00 15.69 ? 123 LYS A HZ1  1 
ATOM   1945 H  HZ2  . LYS A 1 121 ? 30.230 13.833 16.646  1.00 15.69 ? 123 LYS A HZ2  1 
ATOM   1946 H  HZ3  . LYS A 1 121 ? 29.621 15.089 16.258  1.00 15.69 ? 123 LYS A HZ3  1 
ATOM   1947 N  N    . THR A 1 122 ? 28.064 14.118 24.009  1.00 13.86 ? 124 THR A N    1 
ATOM   1948 C  CA   . THR A 1 122 ? 26.808 13.982 24.754  1.00 13.69 ? 124 THR A CA   1 
ATOM   1949 C  C    . THR A 1 122 ? 27.034 13.712 26.229  1.00 16.63 ? 124 THR A C    1 
ATOM   1950 O  O    . THR A 1 122 ? 26.091 13.579 26.989  1.00 18.48 ? 124 THR A O    1 
ATOM   1951 C  CB   . THR A 1 122 ? 25.955 12.850 24.146  1.00 19.73 ? 124 THR A CB   1 
ATOM   1952 O  OG1  . THR A 1 122 ? 26.601 11.588 24.283  1.00 21.39 ? 124 THR A OG1  1 
ATOM   1953 C  CG2  . THR A 1 122 ? 25.693 13.138 22.655  1.00 14.64 ? 124 THR A CG2  1 
ATOM   1954 H  H    . THR A 1 122 ? 28.477 13.372 23.897  1.00 12.56 ? 124 THR A H    1 
ATOM   1955 H  HA   . THR A 1 122 ? 26.306 14.809 24.676  1.00 12.07 ? 124 THR A HA   1 
ATOM   1956 H  HB   . THR A 1 122 ? 25.099 12.819 24.601  1.00 18.01 ? 124 THR A HB   1 
ATOM   1957 H  HG1  . THR A 1 122 ? 27.343 11.601 23.889  1.00 19.30 ? 124 THR A HG1  1 
ATOM   1958 H  HG21 . THR A 1 122 ? 25.157 12.427 22.270  1.00 13.49 ? 124 THR A HG21 1 
ATOM   1959 H  HG22 . THR A 1 122 ? 25.220 13.978 22.558  1.00 13.49 ? 124 THR A HG22 1 
ATOM   1960 H  HG23 . THR A 1 122 ? 26.535 13.193 22.176  1.00 13.49 ? 124 THR A HG23 1 
ATOM   1961 N  N    . SER A 1 123 ? 28.294 13.693 26.637  1.00 20.32 ? 125 SER A N    1 
ATOM   1962 C  CA   . SER A 1 123 ? 28.727 13.336 27.992  1.00 21.25 ? 125 SER A CA   1 
ATOM   1963 C  C    . SER A 1 123 ? 28.088 14.236 29.035  1.00 22.11 ? 125 SER A C    1 
ATOM   1964 O  O    . SER A 1 123 ? 27.851 13.806 30.161  1.00 23.68 ? 125 SER A O    1 
ATOM   1965 C  CB   . SER A 1 123 ? 30.280 13.392 28.148  1.00 23.18 ? 125 SER A CB   1 
ATOM   1966 O  OG   . SER A 1 123 ? 30.847 14.701 27.899  1.00 25.12 ? 125 SER A OG   1 
ATOM   1967 H  H    . SER A 1 123 ? 28.953 13.893 26.123  1.00 17.97 ? 125 SER A H    1 
ATOM   1968 H  HA   . SER A 1 123 ? 28.445 12.427 28.177  1.00 18.29 ? 125 SER A HA   1 
ATOM   1969 H  HB2  . SER A 1 123 ? 30.506 13.128 29.054  1.00 20.17 ? 125 SER A HB2  1 
ATOM   1970 H  HB3  . SER A 1 123 ? 30.673 12.764 27.521  1.00 20.17 ? 125 SER A HB3  1 
ATOM   1971 H  HG   . SER A 1 123 ? 30.671 14.946 27.115  1.00 22.49 ? 125 SER A HG   1 
ATOM   1972 N  N    . ARG A 1 124 ? 27.848 15.473 28.693  1.00 18.31 ? 126 ARG A N    1 
ATOM   1973 C  CA   . ARG A 1 124 ? 27.268 16.454 29.595  1.00 18.84 ? 126 ARG A CA   1 
ATOM   1974 C  C    . ARG A 1 124 ? 25.806 16.840 29.291  1.00 18.15 ? 126 ARG A C    1 
ATOM   1975 O  O    . ARG A 1 124 ? 25.303 17.829 29.807  1.00 20.25 ? 126 ARG A O    1 
ATOM   1976 C  CB   . ARG A 1 124 ? 28.163 17.674 29.667  1.00 20.84 ? 126 ARG A CB   1 
ATOM   1977 C  CG   . ARG A 1 124 ? 29.604 17.225 30.100  1.00 21.15 ? 126 ARG A CG   1 
ATOM   1978 C  CD   . ARG A 1 124 ? 30.640 18.310 30.181  1.00 19.25 ? 126 ARG A CD   1 
ATOM   1979 N  NE   . ARG A 1 124 ? 31.987 17.774 30.417  1.00 19.63 ? 126 ARG A NE   1 
ATOM   1980 C  CZ   . ARG A 1 124 ? 33.098 18.436 30.152  1.00 19.78 ? 126 ARG A CZ   1 
ATOM   1981 N  NH1  . ARG A 1 124 ? 33.031 19.700 29.723  1.00 21.83 ? 126 ARG A NH1  1 
ATOM   1982 N  NH2  . ARG A 1 124 ? 34.285 17.837 30.387  1.00 20.03 ? 126 ARG A NH2  1 
ATOM   1983 H  H    . ARG A 1 124 ? 28.016 15.790 27.912  1.00 15.70 ? 126 ARG A H    1 
ATOM   1984 H  HA   . ARG A 1 124 ? 27.266 16.063 30.483  1.00 15.96 ? 126 ARG A HA   1 
ATOM   1985 H  HB2  . ARG A 1 124 ? 28.216 18.093 28.794  1.00 18.15 ? 126 ARG A HB2  1 
ATOM   1986 H  HB3  . ARG A 1 124 ? 27.818 18.295 30.327  1.00 18.15 ? 126 ARG A HB3  1 
ATOM   1987 H  HG2  . ARG A 1 124 ? 29.545 16.818 30.978  1.00 18.27 ? 126 ARG A HG2  1 
ATOM   1988 H  HG3  . ARG A 1 124 ? 29.924 16.569 29.462  1.00 18.27 ? 126 ARG A HG3  1 
ATOM   1989 H  HD2  . ARG A 1 124 ? 30.653 18.800 29.344  1.00 16.45 ? 126 ARG A HD2  1 
ATOM   1990 H  HD3  . ARG A 1 124 ? 30.420 18.906 30.914  1.00 16.45 ? 126 ARG A HD3  1 
ATOM   1991 H  HE   . ARG A 1 124 ? 32.054 17.025 30.835  1.00 16.64 ? 126 ARG A HE   1 
ATOM   1992 H  HH11 . ARG A 1 124 ? 32.266 20.065 29.578  1.00 19.16 ? 126 ARG A HH11 1 
ATOM   1993 H  HH12 . ARG A 1 124 ? 33.754 20.139 29.563  1.00 19.16 ? 126 ARG A HH12 1 
ATOM   1994 H  HH21 . ARG A 1 124 ? 34.309 17.029 30.680  1.00 16.84 ? 126 ARG A HH21 1 
ATOM   1995 H  HH22 . ARG A 1 124 ? 35.018 18.264 30.244  1.00 16.84 ? 126 ARG A HH22 1 
ATOM   1996 N  N    . HIS A 1 125 ? 25.154 16.046 28.461  1.00 16.76 ? 127 HIS A N    1 
ATOM   1997 C  CA   . HIS A 1 125 ? 23.759 16.238 28.120  1.00 16.09 ? 127 HIS A CA   1 
ATOM   1998 C  C    . HIS A 1 125 ? 23.026 14.913 28.160  1.00 16.47 ? 127 HIS A C    1 
ATOM   1999 O  O    . HIS A 1 125 ? 22.156 14.641 27.323  1.00 16.41 ? 127 HIS A O    1 
ATOM   2000 C  CB   . HIS A 1 125 ? 23.661 16.817 26.708  1.00 15.17 ? 127 HIS A CB   1 
ATOM   2001 C  CG   . HIS A 1 125 ? 24.227 18.189 26.564  1.00 13.85 ? 127 HIS A CG   1 
ATOM   2002 N  ND1  . HIS A 1 125 ? 23.690 19.279 27.208  1.00 21.47 ? 127 HIS A ND1  1 
ATOM   2003 C  CD2  . HIS A 1 125 ? 25.300 18.651 25.874  1.00 15.89 ? 127 HIS A CD2  1 
ATOM   2004 C  CE1  . HIS A 1 125 ? 24.396 20.358 26.914  1.00 20.52 ? 127 HIS A CE1  1 
ATOM   2005 N  NE2  . HIS A 1 125 ? 25.387 20.000 26.122  1.00 20.34 ? 127 HIS A NE2  1 
ATOM   2006 H  H    . HIS A 1 125 ? 25.510 15.368 28.071  1.00 14.70 ? 127 HIS A H    1 
ATOM   2007 H  HA   . HIS A 1 125 ? 23.342 16.851 28.745  1.00 13.99 ? 127 HIS A HA   1 
ATOM   2008 H  HB2  . HIS A 1 125 ? 24.142 16.234 26.100  1.00 13.75 ? 127 HIS A HB2  1 
ATOM   2009 H  HB3  . HIS A 1 125 ? 22.726 16.856 26.452  1.00 13.75 ? 127 HIS A HB3  1 
ATOM   2010 H  HD2  . HIS A 1 125 ? 25.877 18.147 25.346  1.00 15.21 ? 127 HIS A HD2  1 
ATOM   2011 H  HE1  . HIS A 1 125 ? 24.232 21.219 27.226  1.00 19.37 ? 127 HIS A HE1  1 
ATOM   2012 H  HE2  . HIS A 1 125 ? 25.977 20.530 25.790  1.00 19.63 ? 127 HIS A HE2  1 
ATOM   2013 N  N    . LYS A 1 126 ? 23.349 14.078 29.131  1.00 15.97 ? 128 LYS A N    1 
ATOM   2014 C  CA   . LYS A 1 126 ? 22.817 12.742 29.114  1.00 19.34 ? 128 LYS A CA   1 
ATOM   2015 C  C    . LYS A 1 126 ? 21.282 12.687 29.278  1.00 18.68 ? 128 LYS A C    1 
ATOM   2016 O  O    . LYS A 1 126 ? 20.617 11.796 28.731  1.00 18.36 ? 128 LYS A O    1 
ATOM   2017 C  CB   . LYS A 1 126 ? 23.498 11.946 30.205  1.00 19.54 ? 128 LYS A CB   1 
ATOM   2018 C  CG   . LYS A 1 126 ? 25.002 11.904 30.029  1.00 22.84 ? 128 LYS A CG   1 
ATOM   2019 C  CD   . LYS A 1 126 ? 25.425 11.135 28.769  1.00 25.89 ? 128 LYS A CD   1 
ATOM   2020 C  CE   . LYS A 1 126 ? 25.251 9.661  28.995  1.00 30.01 ? 128 LYS A CE   1 
ATOM   2021 N  NZ   . LYS A 1 126 ? 26.000 8.752  27.970  1.00 30.35 ? 128 LYS A NZ   1 
ATOM   2022 H  H    . LYS A 1 126 ? 23.863 14.259 29.796  1.00 13.40 ? 128 LYS A H    1 
ATOM   2023 H  HA   . LYS A 1 126 ? 23.037 12.330 28.264  1.00 16.33 ? 128 LYS A HA   1 
ATOM   2024 H  HB2  . LYS A 1 126 ? 23.306 12.355 31.063  1.00 15.90 ? 128 LYS A HB2  1 
ATOM   2025 H  HB3  . LYS A 1 126 ? 23.167 11.035 30.187  1.00 15.90 ? 128 LYS A HB3  1 
ATOM   2026 H  HG2  . LYS A 1 126 ? 25.338 12.811 29.954  1.00 19.55 ? 128 LYS A HG2  1 
ATOM   2027 H  HG3  . LYS A 1 126 ? 25.399 11.464 30.797  1.00 19.55 ? 128 LYS A HG3  1 
ATOM   2028 H  HD2  . LYS A 1 126 ? 24.867 11.402 28.022  1.00 23.00 ? 128 LYS A HD2  1 
ATOM   2029 H  HD3  . LYS A 1 126 ? 26.359 11.310 28.578  1.00 23.00 ? 128 LYS A HD3  1 
ATOM   2030 H  HE2  . LYS A 1 126 ? 25.583 9.442  29.880  1.00 26.47 ? 128 LYS A HE2  1 
ATOM   2031 H  HE3  . LYS A 1 126 ? 24.306 9.448  28.939  1.00 26.47 ? 128 LYS A HE3  1 
ATOM   2032 H  HZ1  . LYS A 1 126 ? 25.855 7.895  28.161  1.00 27.00 ? 128 LYS A HZ1  1 
ATOM   2033 H  HZ2  . LYS A 1 126 ? 25.709 8.918  27.146  1.00 27.00 ? 128 LYS A HZ2  1 
ATOM   2034 H  HZ3  . LYS A 1 126 ? 26.875 8.912  28.005  1.00 27.00 ? 128 LYS A HZ3  1 
ATOM   2035 N  N    . GLU A 1 127 ? 20.728 13.662 29.993  1.00 17.78 ? 129 GLU A N    1 
ATOM   2036 C  CA   . GLU A 1 127 ? 19.297 13.684 30.241  1.00 19.06 ? 129 GLU A CA   1 
ATOM   2037 C  C    . GLU A 1 127 ? 18.524 13.983 28.963  1.00 21.62 ? 129 GLU A C    1 
ATOM   2038 O  O    . GLU A 1 127 ? 17.416 13.497 28.767  1.00 20.80 ? 129 GLU A O    1 
ATOM   2039 C  CB   . GLU A 1 127 ? 18.922 14.654 31.380  1.00 20.36 ? 129 GLU A CB   1 
ATOM   2040 C  CG   . GLU A 1 127 ? 18.854 16.118 31.104  1.00 24.59 ? 129 GLU A CG   1 
ATOM   2041 C  CD   . GLU A 1 127 ? 20.181 16.842 31.161  1.00 29.52 ? 129 GLU A CD   1 
ATOM   2042 O  OE1  . GLU A 1 127 ? 21.079 16.563 30.330  1.00 26.76 ? 129 GLU A OE1  1 
ATOM   2043 O  OE2  . GLU A 1 127 ? 20.295 17.739 32.019  1.00 33.41 ? 129 GLU A OE2  1 
ATOM   2044 H  H    . GLU A 1 127 ? 21.160 14.318 30.344  1.00 14.54 ? 129 GLU A H    1 
ATOM   2045 H  HA   . GLU A 1 127 ? 19.032 12.797 30.529  1.00 15.25 ? 129 GLU A HA   1 
ATOM   2046 H  HB2  . GLU A 1 127 ? 18.047 14.393 31.710  1.00 16.01 ? 129 GLU A HB2  1 
ATOM   2047 H  HB3  . GLU A 1 127 ? 19.571 14.536 32.091  1.00 16.01 ? 129 GLU A HB3  1 
ATOM   2048 H  HG2  . GLU A 1 127 ? 18.488 16.248 30.215  1.00 20.65 ? 129 GLU A HG2  1 
ATOM   2049 H  HG3  . GLU A 1 127 ? 18.269 16.529 31.760  1.00 20.65 ? 129 GLU A HG3  1 
ATOM   2050 N  N    . PHE A 1 128 ? 19.111 14.760 28.064  1.00 17.56 ? 130 PHE A N    1 
ATOM   2051 C  CA   . PHE A 1 128 ? 18.504 15.080 26.791  1.00 18.01 ? 130 PHE A CA   1 
ATOM   2052 C  C    . PHE A 1 128 ? 18.573 13.863 25.876  1.00 15.51 ? 130 PHE A C    1 
ATOM   2053 O  O    . PHE A 1 128 ? 17.548 13.431 25.303  1.00 17.01 ? 130 PHE A O    1 
ATOM   2054 C  CB   . PHE A 1 128 ? 19.262 16.247 26.194  1.00 16.78 ? 130 PHE A CB   1 
ATOM   2055 C  CG   . PHE A 1 128 ? 18.776 16.622 24.828  1.00 15.39 ? 130 PHE A CG   1 
ATOM   2056 C  CD1  . PHE A 1 128 ? 17.654 17.417 24.668  1.00 16.38 ? 130 PHE A CD1  1 
ATOM   2057 C  CD2  . PHE A 1 128 ? 19.432 16.177 23.692  1.00 12.84 ? 130 PHE A CD2  1 
ATOM   2058 C  CE1  . PHE A 1 128 ? 17.214 17.782 23.369  1.00 18.57 ? 130 PHE A CE1  1 
ATOM   2059 C  CE2  . PHE A 1 128 ? 18.990 16.532 22.392  1.00 16.85 ? 130 PHE A CE2  1 
ATOM   2060 C  CZ   . PHE A 1 128 ? 17.900 17.320 22.258  1.00 14.80 ? 130 PHE A CZ   1 
ATOM   2061 H  H    . PHE A 1 128 ? 19.883 15.122 28.176  1.00 14.39 ? 130 PHE A H    1 
ATOM   2062 H  HA   . PHE A 1 128 ? 17.575 15.333 26.916  1.00 15.32 ? 130 PHE A HA   1 
ATOM   2063 H  HB2  . PHE A 1 128 ? 19.158 17.020 26.771  1.00 14.81 ? 130 PHE A HB2  1 
ATOM   2064 H  HB3  . PHE A 1 128 ? 20.200 16.011 26.123  1.00 14.81 ? 130 PHE A HB3  1 
ATOM   2065 H  HD1  . PHE A 1 128 ? 17.200 17.732 25.416  1.00 14.74 ? 130 PHE A HD1  1 
ATOM   2066 H  HD2  . PHE A 1 128 ? 20.187 15.641 23.784  1.00 11.99 ? 130 PHE A HD2  1 
ATOM   2067 H  HE1  . PHE A 1 128 ? 16.461 18.317 23.264  1.00 17.38 ? 130 PHE A HE1  1 
ATOM   2068 H  HE2  . PHE A 1 128 ? 19.446 16.227 21.640  1.00 16.45 ? 130 PHE A HE2  1 
ATOM   2069 H  HZ   . PHE A 1 128 ? 17.603 17.551 21.407  1.00 14.23 ? 130 PHE A HZ   1 
ATOM   2070 N  N    . PHE A 1 129 ? 19.754 13.271 25.754  1.00 15.03 ? 131 PHE A N    1 
ATOM   2071 C  CA   . PHE A 1 129 ? 19.929 12.144 24.843  1.00 17.28 ? 131 PHE A CA   1 
ATOM   2072 C  C    . PHE A 1 129 ? 19.203 10.864 25.317  1.00 20.96 ? 131 PHE A C    1 
ATOM   2073 O  O    . PHE A 1 129 ? 18.870 10.017 24.516  1.00 23.12 ? 131 PHE A O    1 
ATOM   2074 C  CB   . PHE A 1 129 ? 21.392 12.003 24.449  1.00 14.83 ? 131 PHE A CB   1 
ATOM   2075 C  CG   . PHE A 1 129 ? 21.826 13.114 23.530  1.00 13.04 ? 131 PHE A CG   1 
ATOM   2076 C  CD1  . PHE A 1 129 ? 21.490 13.101 22.181  1.00 13.48 ? 131 PHE A CD1  1 
ATOM   2077 C  CD2  . PHE A 1 129 ? 22.467 14.206 24.039  1.00 15.20 ? 131 PHE A CD2  1 
ATOM   2078 C  CE1  . PHE A 1 129 ? 21.906 14.145 21.355  1.00 15.74 ? 131 PHE A CE1  1 
ATOM   2079 C  CE2  . PHE A 1 129 ? 22.834 15.275 23.235  1.00 13.19 ? 131 PHE A CE2  1 
ATOM   2080 C  CZ   . PHE A 1 129 ? 22.561 15.239 21.867  1.00 16.56 ? 131 PHE A CZ   1 
ATOM   2081 H  H    . PHE A 1 129 ? 20.465 13.498 26.181  1.00 12.37 ? 131 PHE A H    1 
ATOM   2082 H  HA   . PHE A 1 129 ? 19.475 12.393 24.023  1.00 14.77 ? 131 PHE A HA   1 
ATOM   2083 H  HB2  . PHE A 1 129 ? 21.943 12.036 25.246  1.00 12.79 ? 131 PHE A HB2  1 
ATOM   2084 H  HB3  . PHE A 1 129 ? 21.519 11.160 23.987  1.00 12.79 ? 131 PHE A HB3  1 
ATOM   2085 H  HD1  . PHE A 1 129 ? 21.059 12.362 21.816  1.00 12.63 ? 131 PHE A HD1  1 
ATOM   2086 H  HD2  . PHE A 1 129 ? 22.662 14.234 24.948  1.00 14.08 ? 131 PHE A HD2  1 
ATOM   2087 H  HE1  . PHE A 1 129 ? 21.694 14.123 20.450  1.00 15.49 ? 131 PHE A HE1  1 
ATOM   2088 H  HE2  . PHE A 1 129 ? 23.297 15.995 23.599  1.00 12.64 ? 131 PHE A HE2  1 
ATOM   2089 H  HZ   . PHE A 1 129 ? 22.814 15.942 21.314  1.00 16.45 ? 131 PHE A HZ   1 
ATOM   2090 N  N    . SER A 1 130 ? 18.840 10.771 26.601  1.00 18.17 ? 132 SER A N    1 
ATOM   2091 C  CA   . SER A 1 130 ? 18.140 9.606  27.108  1.00 21.41 ? 132 SER A CA   1 
ATOM   2092 C  C    . SER A 1 130 ? 16.685 9.583  26.600  1.00 23.98 ? 132 SER A C    1 
ATOM   2093 O  O    . SER A 1 130 ? 16.044 8.545  26.657  1.00 25.60 ? 132 SER A O    1 
ATOM   2094 C  CB   . SER A 1 130 ? 18.151 9.567  28.638  1.00 23.06 ? 132 SER A CB   1 
ATOM   2095 O  OG   . SER A 1 130 ? 17.293 10.557 29.115  1.00 24.39 ? 132 SER A OG   1 
ATOM   2096 H  H    . SER A 1 130 ? 18.992 11.375 27.194  1.00 16.06 ? 132 SER A H    1 
ATOM   2097 H  HA   . SER A 1 130 ? 18.583 8.806  26.785  1.00 18.40 ? 132 SER A HA   1 
ATOM   2098 H  HB2  . SER A 1 130 ? 17.842 8.699  28.942  1.00 19.25 ? 132 SER A HB2  1 
ATOM   2099 H  HB3  . SER A 1 130 ? 19.050 9.738  28.959  1.00 19.25 ? 132 SER A HB3  1 
ATOM   2100 H  HG   . SER A 1 130 ? 17.550 11.312 28.850  1.00 20.37 ? 132 SER A HG   1 
ATOM   2101 N  N    . LEU A 1 131 ? 16.156 10.711 26.121  1.00 20.86 ? 133 LEU A N    1 
ATOM   2102 C  CA   . LEU A 1 131 ? 14.759 10.755 25.681  1.00 22.10 ? 133 LEU A CA   1 
ATOM   2103 C  C    . LEU A 1 131 ? 14.529 10.195 24.279  1.00 23.54 ? 133 LEU A C    1 
ATOM   2104 O  O    . LEU A 1 131 ? 13.371 9.952  23.893  1.00 25.65 ? 133 LEU A O    1 
ATOM   2105 C  CB   . LEU A 1 131 ? 14.258 12.189 25.748  1.00 19.28 ? 133 LEU A CB   1 
ATOM   2106 C  CG   . LEU A 1 131 ? 14.446 12.903 27.076  1.00 20.61 ? 133 LEU A CG   1 
ATOM   2107 C  CD1  . LEU A 1 131 ? 13.828 14.265 26.995  1.00 21.05 ? 133 LEU A CD1  1 
ATOM   2108 C  CD2  . LEU A 1 131 ? 13.791 12.067 28.171  1.00 26.55 ? 133 LEU A CD2  1 
ATOM   2109 H  H    . LEU A 1 131 ? 16.578 11.456 26.042  1.00 18.52 ? 133 LEU A H    1 
ATOM   2110 H  HA   . LEU A 1 131 ? 14.226 10.229 26.296  1.00 19.43 ? 133 LEU A HA   1 
ATOM   2111 H  HB2  . LEU A 1 131 ? 14.724 12.706 25.073  1.00 16.80 ? 133 LEU A HB2  1 
ATOM   2112 H  HB3  . LEU A 1 131 ? 13.308 12.188 25.552  1.00 16.80 ? 133 LEU A HB3  1 
ATOM   2113 H  HG   . LEU A 1 131 ? 15.391 12.996 27.272  1.00 17.72 ? 133 LEU A HG   1 
ATOM   2114 H  HD11 . LEU A 1 131 ? 13.950 14.718 27.845  1.00 18.24 ? 133 LEU A HD11 1 
ATOM   2115 H  HD12 . LEU A 1 131 ? 14.262 14.767 26.287  1.00 18.24 ? 133 LEU A HD12 1 
ATOM   2116 H  HD13 . LEU A 1 131 ? 12.882 14.172 26.803  1.00 18.24 ? 133 LEU A HD13 1 
ATOM   2117 H  HD21 . LEU A 1 131 ? 13.907 12.516 29.023  1.00 22.52 ? 133 LEU A HD21 1 
ATOM   2118 H  HD22 . LEU A 1 131 ? 12.846 11.971 27.972  1.00 22.52 ? 133 LEU A HD22 1 
ATOM   2119 H  HD23 . LEU A 1 131 ? 14.214 11.194 28.197  1.00 22.52 ? 133 LEU A HD23 1 
ATOM   2120 N  N    . PHE A 1 132 ? 15.600 9.941  23.535  1.00 20.36 ? 134 PHE A N    1 
ATOM   2121 C  CA   . PHE A 1 132 ? 15.455 9.401  22.194  1.00 21.09 ? 134 PHE A CA   1 
ATOM   2122 C  C    . PHE A 1 132 ? 15.111 7.929  22.242  1.00 26.29 ? 134 PHE A C    1 
ATOM   2123 O  O    . PHE A 1 132 ? 15.584 7.209  23.099  1.00 25.30 ? 134 PHE A O    1 
ATOM   2124 C  CB   . PHE A 1 132 ? 16.724 9.653  21.399  1.00 19.59 ? 134 PHE A CB   1 
ATOM   2125 C  CG   . PHE A 1 132 ? 16.926 11.090 21.058  1.00 17.75 ? 134 PHE A CG   1 
ATOM   2126 C  CD1  . PHE A 1 132 ? 17.416 11.967 21.996  1.00 20.27 ? 134 PHE A CD1  1 
ATOM   2127 C  CD2  . PHE A 1 132 ? 16.654 11.562 19.793  1.00 14.71 ? 134 PHE A CD2  1 
ATOM   2128 C  CE1  . PHE A 1 132 ? 17.602 13.298 21.689  1.00 17.00 ? 134 PHE A CE1  1 
ATOM   2129 C  CE2  . PHE A 1 132 ? 16.789 12.871 19.501  1.00 13.23 ? 134 PHE A CE2  1 
ATOM   2130 C  CZ   . PHE A 1 132 ? 17.288 13.742 20.429  1.00 13.41 ? 134 PHE A CZ   1 
ATOM   2131 H  H    . PHE A 1 132 ? 16.413 10.071 23.782  1.00 17.46 ? 134 PHE A H    1 
ATOM   2132 H  HA   . PHE A 1 132 ? 14.728 9.862  21.747  1.00 18.54 ? 134 PHE A HA   1 
ATOM   2133 H  HB2  . PHE A 1 132 ? 17.487 9.360  21.922  1.00 17.91 ? 134 PHE A HB2  1 
ATOM   2134 H  HB3  . PHE A 1 132 ? 16.681 9.153  20.569  1.00 17.91 ? 134 PHE A HB3  1 
ATOM   2135 H  HD1  . PHE A 1 132 ? 17.619 11.660 22.850  1.00 19.32 ? 134 PHE A HD1  1 
ATOM   2136 H  HD2  . PHE A 1 132 ? 16.303 10.984 19.154  1.00 14.26 ? 134 PHE A HD2  1 
ATOM   2137 H  HE1  . PHE A 1 132 ? 17.926 13.888 22.330  1.00 16.58 ? 134 PHE A HE1  1 
ATOM   2138 H  HE2  . PHE A 1 132 ? 16.601 13.172 18.641  1.00 13.29 ? 134 PHE A HE2  1 
ATOM   2139 H  HZ   . PHE A 1 132 ? 17.409 14.637 20.208  1.00 13.48 ? 134 PHE A HZ   1 
ATOM   2140 N  N    . SER A 1 133 ? 14.250 7.486  21.337  1.00 23.37 ? 135 SER A N    1 
ATOM   2141 C  CA   . SER A 1 133 ? 13.839 6.095  21.308  1.00 21.54 ? 135 SER A CA   1 
ATOM   2142 C  C    . SER A 1 133 ? 15.024 5.157  21.001  1.00 25.06 ? 135 SER A C    1 
ATOM   2143 O  O    . SER A 1 133 ? 15.136 4.082  21.583  1.00 31.73 ? 135 SER A O    1 
ATOM   2144 C  CB   . SER A 1 133 ? 12.681 5.917  20.302  1.00 27.19 ? 135 SER A CB   1 
ATOM   2145 O  OG   . SER A 1 133 ? 11.526 6.744  20.612  1.00 28.72 ? 135 SER A OG   1 
ATOM   2146 H  H    . SER A 1 133 ? 13.889 7.974  20.728  1.00 20.61 ? 135 SER A H    1 
ATOM   2147 H  HA   . SER A 1 133 ? 13.500 5.856  22.185  1.00 17.98 ? 135 SER A HA   1 
ATOM   2148 H  HB2  . SER A 1 133 ? 13.002 6.155  19.417  1.00 23.50 ? 135 SER A HB2  1 
ATOM   2149 H  HB3  . SER A 1 133 ? 12.406 4.987  20.309  1.00 23.50 ? 135 SER A HB3  1 
ATOM   2150 H  HG   . SER A 1 133 ? 11.742 7.556  20.604  1.00 24.76 ? 135 SER A HG   1 
ATOM   2151 N  N    . HIS A 1 134 ? 15.933 5.575  20.124  1.00 21.02 ? 136 HIS A N    1 
ATOM   2152 C  CA   . HIS A 1 134 ? 17.136 4.823  19.792  1.00 20.88 ? 136 HIS A CA   1 
ATOM   2153 C  C    . HIS A 1 134 ? 18.084 5.749  19.006  1.00 19.03 ? 136 HIS A C    1 
ATOM   2154 O  O    . HIS A 1 134 ? 17.661 6.836  18.603  1.00 19.16 ? 136 HIS A O    1 
ATOM   2155 C  CB   . HIS A 1 134 ? 16.823 3.518  19.033  1.00 23.23 ? 136 HIS A CB   1 
ATOM   2156 C  CG   . HIS A 1 134 ? 16.148 3.722  17.716  1.00 23.30 ? 136 HIS A CG   1 
ATOM   2157 N  ND1  . HIS A 1 134 ? 14.786 3.891  17.611  1.00 23.22 ? 136 HIS A ND1  1 
ATOM   2158 C  CD2  . HIS A 1 134 ? 16.645 3.808  16.461  1.00 22.51 ? 136 HIS A CD2  1 
ATOM   2159 C  CE1  . HIS A 1 134 ? 14.470 4.067  16.341  1.00 21.45 ? 136 HIS A CE1  1 
ATOM   2160 N  NE2  . HIS A 1 134 ? 15.579 4.026  15.625  1.00 19.84 ? 136 HIS A NE2  1 
ATOM   2161 H  H    . HIS A 1 134 ? 15.870 6.318  19.694  1.00 18.53 ? 136 HIS A H    1 
ATOM   2162 H  HA   . HIS A 1 134 ? 17.584 4.579  20.617  1.00 18.51 ? 136 HIS A HA   1 
ATOM   2163 H  HB2  . HIS A 1 134 ? 17.654 3.046  18.869  1.00 20.33 ? 136 HIS A HB2  1 
ATOM   2164 H  HB3  . HIS A 1 134 ? 16.239 2.971  19.582  1.00 20.33 ? 136 HIS A HB3  1 
ATOM   2165 H  HD2  . HIS A 1 134 ? 17.538 3.738  16.213  1.00 20.63 ? 136 HIS A HD2  1 
ATOM   2166 H  HE1  . HIS A 1 134 ? 13.612 4.199  16.007  1.00 19.08 ? 136 HIS A HE1  1 
ATOM   2167 H  HE2  . HIS A 1 134 ? 15.625 4.110  14.771  1.00 18.04 ? 136 HIS A HE2  1 
ATOM   2168 N  N    . ILE A 1 135 ? 19.309 5.296  18.779  1.00 19.10 ? 137 ILE A N    1 
ATOM   2169 C  CA   . ILE A 1 135 ? 20.366 6.109  18.150  1.00 17.10 ? 137 ILE A CA   1 
ATOM   2170 C  C    . ILE A 1 135 ? 21.100 5.245  17.144  1.00 23.23 ? 137 ILE A C    1 
ATOM   2171 O  O    . ILE A 1 135 ? 21.426 4.076  17.438  1.00 22.22 ? 137 ILE A O    1 
ATOM   2172 C  CB   . ILE A 1 135 ? 21.333 6.615  19.277  1.00 22.50 ? 137 ILE A CB   1 
ATOM   2173 C  CG1  . ILE A 1 135 ? 20.566 7.587  20.165  1.00 19.52 ? 137 ILE A CG1  1 
ATOM   2174 C  CG2  . ILE A 1 135 ? 22.599 7.234  18.709  1.00 21.58 ? 137 ILE A CG2  1 
ATOM   2175 C  CD1  . ILE A 1 135 ? 21.278 8.011  21.401  1.00 24.09 ? 137 ILE A CD1  1 
ATOM   2176 H  H    . ILE A 1 135 ? 19.567 4.501  18.982  1.00 16.40 ? 137 ILE A H    1 
ATOM   2177 H  HA   . ILE A 1 135 ? 19.978 6.872  17.694  1.00 15.22 ? 137 ILE A HA   1 
ATOM   2178 H  HB   . ILE A 1 135 ? 21.589 5.852  19.819  1.00 20.66 ? 137 ILE A HB   1 
ATOM   2179 H  HG12 . ILE A 1 135 ? 20.374 8.387  19.651  1.00 17.68 ? 137 ILE A HG12 1 
ATOM   2180 H  HG13 . ILE A 1 135 ? 19.735 7.167  20.436  1.00 17.68 ? 137 ILE A HG13 1 
ATOM   2181 H  HG21 . ILE A 1 135 ? 23.161 7.531  19.442  1.00 20.37 ? 137 ILE A HG21 1 
ATOM   2182 H  HG22 . ILE A 1 135 ? 23.066 6.568  18.181  1.00 20.37 ? 137 ILE A HG22 1 
ATOM   2183 H  HG23 . ILE A 1 135 ? 22.357 7.990  18.151  1.00 20.37 ? 137 ILE A HG23 1 
ATOM   2184 H  HD11 . ILE A 1 135 ? 20.713 8.625  21.896  1.00 22.13 ? 137 ILE A HD11 1 
ATOM   2185 H  HD12 . ILE A 1 135 ? 21.467 7.227  21.940  1.00 22.13 ? 137 ILE A HD12 1 
ATOM   2186 H  HD13 . ILE A 1 135 ? 22.107 8.450  21.153  1.00 22.13 ? 137 ILE A HD13 1 
ATOM   2187 N  N    . VAL A 1 136 ? 21.317 5.766  15.945  1.00 17.45 ? 138 VAL A N    1 
ATOM   2188 C  CA   . VAL A 1 136 ? 22.192 5.156  14.980  1.00 16.98 ? 138 VAL A CA   1 
ATOM   2189 C  C    . VAL A 1 136 ? 23.386 6.047  14.731  1.00 18.86 ? 138 VAL A C    1 
ATOM   2190 O  O    . VAL A 1 136 ? 23.239 7.241  14.397  1.00 16.16 ? 138 VAL A O    1 
ATOM   2191 C  CB   . VAL A 1 136 ? 21.487 4.892  13.614  1.00 16.96 ? 138 VAL A CB   1 
ATOM   2192 C  CG1  . VAL A 1 136 ? 22.394 4.145  12.668  1.00 18.11 ? 138 VAL A CG1  1 
ATOM   2193 C  CG2  . VAL A 1 136 ? 20.169 4.126  13.814  1.00 19.19 ? 138 VAL A CG2  1 
ATOM   2194 H  H    . VAL A 1 136 ? 20.955 6.494  15.667  1.00 16.26 ? 138 VAL A H    1 
ATOM   2195 H  HA   . VAL A 1 136 ? 22.511 4.308  15.327  1.00 15.82 ? 138 VAL A HA   1 
ATOM   2196 H  HB   . VAL A 1 136 ? 21.274 5.745  13.206  1.00 15.91 ? 138 VAL A HB   1 
ATOM   2197 H  HG11 . VAL A 1 136 ? 21.925 3.999  11.832  1.00 16.93 ? 138 VAL A HG11 1 
ATOM   2198 H  HG12 . VAL A 1 136 ? 23.192 4.675  12.512  1.00 16.93 ? 138 VAL A HG12 1 
ATOM   2199 H  HG13 . VAL A 1 136 ? 22.634 3.294  13.067  1.00 16.93 ? 138 VAL A HG13 1 
ATOM   2200 H  HG21 . VAL A 1 136 ? 19.756 3.978  12.948  1.00 17.54 ? 138 VAL A HG21 1 
ATOM   2201 H  HG22 . VAL A 1 136 ? 20.359 3.276  14.240  1.00 17.54 ? 138 VAL A HG22 1 
ATOM   2202 H  HG23 . VAL A 1 136 ? 19.580 4.654  14.375  1.00 17.54 ? 138 VAL A HG23 1 
ATOM   2203 N  N    . LEU A 1 137 ? 24.568 5.460  14.841  1.00 16.68 ? 139 LEU A N    1 
ATOM   2204 C  CA   . LEU A 1 137 ? 25.830 6.165  14.653  1.00 15.88 ? 139 LEU A CA   1 
ATOM   2205 C  C    . LEU A 1 137 ? 26.483 5.789  13.354  1.00 19.24 ? 139 LEU A C    1 
ATOM   2206 O  O    . LEU A 1 137 ? 26.097 4.818  12.688  1.00 19.05 ? 139 LEU A O    1 
ATOM   2207 C  CB   . LEU A 1 137 ? 26.792 5.826  15.788  1.00 18.75 ? 139 LEU A CB   1 
ATOM   2208 C  CG   . LEU A 1 137 ? 26.293 6.029  17.205  1.00 22.51 ? 139 LEU A CG   1 
ATOM   2209 C  CD1  . LEU A 1 137 ? 27.368 5.685  18.227  1.00 24.67 ? 139 LEU A CD1  1 
ATOM   2210 C  CD2  . LEU A 1 137 ? 25.861 7.463  17.379  1.00 20.38 ? 139 LEU A CD2  1 
ATOM   2211 H  H    . LEU A 1 137 ? 24.669 4.627  15.029  1.00 15.89 ? 139 LEU A H    1 
ATOM   2212 H  HA   . LEU A 1 137 ? 25.673 7.122  14.655  1.00 15.46 ? 139 LEU A HA   1 
ATOM   2213 H  HB2  . LEU A 1 137 ? 27.039 4.892  15.705  1.00 17.90 ? 139 LEU A HB2  1 
ATOM   2214 H  HB3  . LEU A 1 137 ? 27.584 6.376  15.685  1.00 17.90 ? 139 LEU A HB3  1 
ATOM   2215 H  HG   . LEU A 1 137 ? 25.526 5.456  17.362  1.00 21.47 ? 139 LEU A HG   1 
ATOM   2216 H  HD11 . LEU A 1 137 ? 27.013 5.826  19.118  1.00 23.18 ? 139 LEU A HD11 1 
ATOM   2217 H  HD12 . LEU A 1 137 ? 27.624 4.756  18.116  1.00 23.18 ? 139 LEU A HD12 1 
ATOM   2218 H  HD13 . LEU A 1 137 ? 28.137 6.259  18.082  1.00 23.18 ? 139 LEU A HD13 1 
ATOM   2219 H  HD21 . LEU A 1 137 ? 25.542 7.588  18.287  1.00 19.96 ? 139 LEU A HD21 1 
ATOM   2220 H  HD22 . LEU A 1 137 ? 26.620 8.043  17.212  1.00 19.96 ? 139 LEU A HD22 1 
ATOM   2221 H  HD23 . LEU A 1 137 ? 25.150 7.657  16.749  1.00 19.96 ? 139 LEU A HD23 1 
ATOM   2222 N  N    . GLY A 1 138 ? 27.515 6.528  12.981  1.00 17.56 ? 140 GLY A N    1 
ATOM   2223 C  CA   . GLY A 1 138 ? 28.138 6.340  11.694  1.00 18.98 ? 140 GLY A CA   1 
ATOM   2224 C  C    . GLY A 1 138 ? 29.012 5.106  11.620  1.00 21.80 ? 140 GLY A C    1 
ATOM   2225 O  O    . GLY A 1 138 ? 29.335 4.642  10.527  1.00 21.76 ? 140 GLY A O    1 
ATOM   2226 H  H    . GLY A 1 138 ? 27.872 7.147  13.460  1.00 17.07 ? 140 GLY A H    1 
ATOM   2227 H  HA2  . GLY A 1 138 ? 27.451 6.266  11.014  1.00 18.50 ? 140 GLY A HA2  1 
ATOM   2228 H  HA3  . GLY A 1 138 ? 28.687 7.113  11.489  1.00 18.50 ? 140 GLY A HA3  1 
ATOM   2229 N  N    . ASP A 1 139 ? 29.428 4.612  12.766  1.00 19.55 ? 141 ASP A N    1 
ATOM   2230 C  CA   . ASP A 1 139 ? 30.157 3.338  12.814  1.00 21.12 ? 141 ASP A CA   1 
ATOM   2231 C  C    . ASP A 1 139 ? 29.250 2.108  12.976  1.00 24.79 ? 141 ASP A C    1 
ATOM   2232 O  O    . ASP A 1 139 ? 29.738 1.007  13.202  1.00 25.64 ? 141 ASP A O    1 
ATOM   2233 C  CB   . ASP A 1 139 ? 31.249 3.355  13.883  1.00 25.98 ? 141 ASP A CB   1 
ATOM   2234 C  CG   . ASP A 1 139 ? 30.723 3.667  15.258  1.00 24.47 ? 141 ASP A CG   1 
ATOM   2235 O  OD1  . ASP A 1 139 ? 29.501 3.685  15.480  1.00 22.97 ? 141 ASP A OD1  1 
ATOM   2236 O  OD2  . ASP A 1 139 ? 31.566 3.866  16.161  1.00 25.70 ? 141 ASP A OD2  1 
ATOM   2237 H  H    . ASP A 1 139 ? 29.308 4.984  13.532  1.00 19.63 ? 141 ASP A H    1 
ATOM   2238 H  HA   . ASP A 1 139 ? 30.610 3.233  11.963  1.00 20.38 ? 141 ASP A HA   1 
ATOM   2239 H  HB2  . ASP A 1 139 ? 31.671 2.482  13.915  1.00 24.90 ? 141 ASP A HB2  1 
ATOM   2240 H  HB3  . ASP A 1 139 ? 31.905 4.031  13.653  1.00 24.90 ? 141 ASP A HB3  1 
ATOM   2241 N  N    . ASP A 1 140 ? 27.936 2.293  12.839  1.00 22.05 ? 142 ASP A N    1 
ATOM   2242 C  CA   . ASP A 1 140 ? 26.996 1.185  12.930  1.00 22.96 ? 142 ASP A CA   1 
ATOM   2243 C  C    . ASP A 1 140 ? 27.298 0.250  11.753  1.00 24.96 ? 142 ASP A C    1 
ATOM   2244 O  O    . ASP A 1 140 ? 27.598 0.696  10.651  1.00 20.01 ? 142 ASP A O    1 
ATOM   2245 C  CB   . ASP A 1 140 ? 25.562 1.688  12.862  1.00 24.74 ? 142 ASP A CB   1 
ATOM   2246 C  CG   . ASP A 1 140 ? 24.539 0.591  13.179  1.00 18.04 ? 142 ASP A CG   1 
ATOM   2247 O  OD1  . ASP A 1 140 ? 24.327 -0.256 12.263  1.00 26.98 ? 142 ASP A OD1  1 
ATOM   2248 O  OD2  . ASP A 1 140 ? 23.932 0.664  14.264  1.00 23.82 ? 142 ASP A OD2  1 
ATOM   2249 H  H    . ASP A 1 140 ? 27.566 3.055  12.693  1.00 22.13 ? 142 ASP A H    1 
ATOM   2250 H  HA   . ASP A 1 140 ? 27.126 0.703  13.761  1.00 22.44 ? 142 ASP A HA   1 
ATOM   2251 H  HB2  . ASP A 1 140 ? 25.446 2.402  13.508  1.00 24.64 ? 142 ASP A HB2  1 
ATOM   2252 H  HB3  . ASP A 1 140 ? 25.384 2.016  11.967  1.00 24.64 ? 142 ASP A HB3  1 
ATOM   2253 N  N    . PRO A 1 141 ? 27.277 -1.083 12.000  1.00 26.10 ? 143 PRO A N    1 
ATOM   2254 C  CA   . PRO A 1 141 ? 27.631 -2.032 10.947  1.00 28.41 ? 143 PRO A CA   1 
ATOM   2255 C  C    . PRO A 1 141 ? 26.730 -1.978 9.723   1.00 28.78 ? 143 PRO A C    1 
ATOM   2256 O  O    . PRO A 1 141 ? 27.165 -2.345 8.642   1.00 32.71 ? 143 PRO A O    1 
ATOM   2257 C  CB   . PRO A 1 141 ? 27.493 -3.376 11.656  1.00 28.23 ? 143 PRO A CB   1 
ATOM   2258 C  CG   . PRO A 1 141 ? 27.826 -3.102 13.043  1.00 25.79 ? 143 PRO A CG   1 
ATOM   2259 C  CD   . PRO A 1 141 ? 27.253 -1.736 13.324  1.00 26.97 ? 143 PRO A CD   1 
ATOM   2260 H  HA   . PRO A 1 141 ? 28.553 -1.906 10.674  1.00 25.65 ? 143 PRO A HA   1 
ATOM   2261 H  HB2  . PRO A 1 141 ? 26.580 -3.695 11.578  1.00 24.36 ? 143 PRO A HB2  1 
ATOM   2262 H  HB3  . PRO A 1 141 ? 28.115 -4.014 11.273  1.00 24.36 ? 143 PRO A HB3  1 
ATOM   2263 H  HG2  . PRO A 1 141 ? 27.417 -3.770 13.615  1.00 21.89 ? 143 PRO A HG2  1 
ATOM   2264 H  HG3  . PRO A 1 141 ? 28.790 -3.099 13.153  1.00 21.89 ? 143 PRO A HG3  1 
ATOM   2265 H  HD2  . PRO A 1 141 ? 26.342 -1.811 13.649  1.00 24.13 ? 143 PRO A HD2  1 
ATOM   2266 H  HD3  . PRO A 1 141 ? 27.816 -1.255 13.950  1.00 24.13 ? 143 PRO A HD3  1 
ATOM   2267 N  N    . GLU A 1 142 ? 25.519 -1.461 9.903   1.00 33.47 ? 144 GLU A N    1 
ATOM   2268 C  CA   . GLU A 1 142 ? 24.557 -1.321 8.822   1.00 33.74 ? 144 GLU A CA   1 
ATOM   2269 C  C    . GLU A 1 142 ? 24.760 -0.097 7.906   1.00 35.00 ? 144 GLU A C    1 
ATOM   2270 O  O    . GLU A 1 142 ? 24.179 -0.039 6.831   1.00 35.68 ? 144 GLU A O    1 
ATOM   2271 C  CB   . GLU A 1 142 ? 23.161 -1.319 9.431   1.00 36.22 ? 144 GLU A CB   1 
ATOM   2272 C  CG   . GLU A 1 142 ? 22.068 -1.549 8.427   1.00 44.05 ? 144 GLU A CG   1 
ATOM   2273 C  CD   . GLU A 1 142 ? 20.695 -1.698 9.063   1.00 44.56 ? 144 GLU A CD   1 
ATOM   2274 O  OE1  . GLU A 1 142 ? 20.613 -1.804 10.300  1.00 39.59 ? 144 GLU A OE1  1 
ATOM   2275 O  OE2  . GLU A 1 142 ? 19.693 -1.691 8.308   1.00 51.36 ? 144 GLU A OE2  1 
ATOM   2276 H  H    . GLU A 1 142 ? 25.227 -1.180 10.661  1.00 26.58 ? 144 GLU A H    1 
ATOM   2277 H  HA   . GLU A 1 142 ? 24.621 -2.108 8.260   1.00 27.13 ? 144 GLU A HA   1 
ATOM   2278 H  HB2  . GLU A 1 142 ? 23.108 -2.024 10.095  1.00 29.58 ? 144 GLU A HB2  1 
ATOM   2279 H  HB3  . GLU A 1 142 ? 23.004 -0.459 9.851   1.00 29.58 ? 144 GLU A HB3  1 
ATOM   2280 H  HG2  . GLU A 1 142 ? 22.036 -0.793 7.820   1.00 37.36 ? 144 GLU A HG2  1 
ATOM   2281 H  HG3  . GLU A 1 142 ? 22.260 -2.362 7.935   1.00 37.36 ? 144 GLU A HG3  1 
ATOM   2282 N  N    . VAL A 1 143 ? 25.587 0.861  8.323   1.00 30.35 ? 145 VAL A N    1 
ATOM   2283 C  CA   . VAL A 1 143 ? 25.856 2.117  7.586   1.00 26.20 ? 145 VAL A CA   1 
ATOM   2284 C  C    . VAL A 1 143 ? 27.183 2.128  6.817   1.00 27.79 ? 145 VAL A C    1 
ATOM   2285 O  O    . VAL A 1 143 ? 28.248 2.379  7.371   1.00 26.87 ? 145 VAL A O    1 
ATOM   2286 C  CB   . VAL A 1 143 ? 25.829 3.315  8.563   1.00 22.77 ? 145 VAL A CB   1 
ATOM   2287 C  CG1  . VAL A 1 143 ? 26.066 4.668  7.833   1.00 23.99 ? 145 VAL A CG1  1 
ATOM   2288 C  CG2  . VAL A 1 143 ? 24.519 3.322  9.290   1.00 20.88 ? 145 VAL A CG2  1 
ATOM   2289 H  H    . VAL A 1 143 ? 26.026 0.811  9.060   1.00 28.33 ? 145 VAL A H    1 
ATOM   2290 H  HA   . VAL A 1 143 ? 25.144 2.251  6.941   1.00 24.99 ? 145 VAL A HA   1 
ATOM   2291 H  HB   . VAL A 1 143 ? 26.534 3.201  9.219   1.00 22.18 ? 145 VAL A HB   1 
ATOM   2292 H  HG11 . VAL A 1 143 ? 26.041 5.386  8.485   1.00 24.16 ? 145 VAL A HG11 1 
ATOM   2293 H  HG12 . VAL A 1 143 ? 26.934 4.645  7.399   1.00 24.16 ? 145 VAL A HG12 1 
ATOM   2294 H  HG13 . VAL A 1 143 ? 25.368 4.797  7.172   1.00 24.16 ? 145 VAL A HG13 1 
ATOM   2295 H  HG21 . VAL A 1 143 ? 24.502 4.073  9.902   1.00 20.32 ? 145 VAL A HG21 1 
ATOM   2296 H  HG22 . VAL A 1 143 ? 23.800 3.405  8.643   1.00 20.32 ? 145 VAL A HG22 1 
ATOM   2297 H  HG23 . VAL A 1 143 ? 24.427 2.491  9.782   1.00 20.32 ? 145 VAL A HG23 1 
ATOM   2298 N  N    . GLN A 1 144 ? 27.116 1.849  5.527   1.00 26.89 ? 146 GLN A N    1 
ATOM   2299 C  CA   . GLN A 1 144 ? 28.320 1.739  4.722   1.00 32.95 ? 146 GLN A CA   1 
ATOM   2300 C  C    . GLN A 1 144 ? 28.952 3.089  4.339   1.00 31.63 ? 146 GLN A C    1 
ATOM   2301 O  O    . GLN A 1 144 ? 30.175 3.174  4.204   1.00 34.49 ? 146 GLN A O    1 
ATOM   2302 C  CB   . GLN A 1 144 ? 28.013 0.904  3.471   1.00 37.14 ? 146 GLN A CB   1 
ATOM   2303 C  CG   . GLN A 1 144 ? 27.689 -0.560 3.793   1.00 40.01 ? 146 GLN A CG   1 
ATOM   2304 C  CD   . GLN A 1 144 ? 27.329 -1.400 2.565   1.00 49.22 ? 146 GLN A CD   1 
ATOM   2305 O  OE1  . GLN A 1 144 ? 27.056 -0.876 1.479   1.00 43.71 ? 146 GLN A OE1  1 
ATOM   2306 N  NE2  . GLN A 1 144 ? 27.330 -2.724 2.743   1.00 54.80 ? 146 GLN A NE2  1 
ATOM   2307 H  H    . GLN A 1 144 ? 26.386 1.719  5.092   1.00 23.52 ? 146 GLN A H    1 
ATOM   2308 H  HA   . GLN A 1 144 ? 28.982 1.251  5.237   1.00 29.28 ? 146 GLN A HA   1 
ATOM   2309 H  HB2  . GLN A 1 144 ? 27.247 1.287  3.016   1.00 32.99 ? 146 GLN A HB2  1 
ATOM   2310 H  HB3  . GLN A 1 144 ? 28.787 0.917  2.886   1.00 32.99 ? 146 GLN A HB3  1 
ATOM   2311 H  HG2  . GLN A 1 144 ? 28.464 -0.966 4.212   1.00 34.97 ? 146 GLN A HG2  1 
ATOM   2312 H  HG3  . GLN A 1 144 ? 26.935 -0.586 4.401   1.00 34.97 ? 146 GLN A HG3  1 
ATOM   2313 H  HE21 . GLN A 1 144 ? 27.525 -3.054 3.513   1.00 48.25 ? 146 GLN A HE21 1 
ATOM   2314 H  HE22 . GLN A 1 144 ? 27.135 -3.246 2.089   1.00 48.25 ? 146 GLN A HE22 1 
ATOM   2315 N  N    . HIS A 1 145 ? 28.132 4.131  4.152   1.00 24.45 ? 147 HIS A N    1 
ATOM   2316 C  CA   . HIS A 1 145 ? 28.631 5.451  3.778   1.00 22.87 ? 147 HIS A CA   1 
ATOM   2317 C  C    . HIS A 1 145 ? 27.849 6.500  4.526   1.00 16.97 ? 147 HIS A C    1 
ATOM   2318 O  O    . HIS A 1 145 ? 26.720 6.252  4.941   1.00 17.51 ? 147 HIS A O    1 
ATOM   2319 C  CB   . HIS A 1 145 ? 28.517 5.696  2.282   1.00 23.25 ? 147 HIS A CB   1 
ATOM   2320 C  CG   . HIS A 1 145 ? 29.076 4.586  1.465   1.00 29.39 ? 147 HIS A CG   1 
ATOM   2321 N  ND1  . HIS A 1 145 ? 30.410 4.507  1.129   1.00 32.46 ? 147 HIS A ND1  1 
ATOM   2322 C  CD2  . HIS A 1 145 ? 28.485 3.489  0.938   1.00 34.12 ? 147 HIS A CD2  1 
ATOM   2323 C  CE1  . HIS A 1 145 ? 30.614 3.412  0.416   1.00 33.58 ? 147 HIS A CE1  1 
ATOM   2324 N  NE2  . HIS A 1 145 ? 29.463 2.775  0.290   1.00 35.04 ? 147 HIS A NE2  1 
ATOM   2325 H  H    . HIS A 1 145 ? 27.277 4.094  4.238   1.00 22.68 ? 147 HIS A H    1 
ATOM   2326 H  HA   . HIS A 1 145 ? 29.565 5.526  4.031   1.00 21.64 ? 147 HIS A HA   1 
ATOM   2327 H  HB2  . HIS A 1 145 ? 27.581 5.796  2.050   1.00 22.07 ? 147 HIS A HB2  1 
ATOM   2328 H  HB3  . HIS A 1 145 ? 29.002 6.506  2.057   1.00 22.07 ? 147 HIS A HB3  1 
ATOM   2329 H  HD2  . HIS A 1 145 ? 27.585 3.261  1.002   1.00 31.73 ? 147 HIS A HD2  1 
ATOM   2330 H  HE1  . HIS A 1 145 ? 31.430 3.135  0.066   1.00 30.47 ? 147 HIS A HE1  1 
ATOM   2331 H  HE2  . HIS A 1 145 ? 29.344 2.037  -0.135  1.00 31.92 ? 147 HIS A HE2  1 
ATOM   2332 N  N    . GLY A 1 146 ? 28.470 7.654  4.691   1.00 15.90 ? 148 GLY A N    1 
ATOM   2333 C  CA   . GLY A 1 146 ? 27.809 8.787  5.301   1.00 17.17 ? 148 GLY A CA   1 
ATOM   2334 C  C    . GLY A 1 146 ? 26.745 9.398  4.416   1.00 10.49 ? 148 GLY A C    1 
ATOM   2335 O  O    . GLY A 1 146 ? 26.495 9.011  3.275   1.00 12.20 ? 148 GLY A O    1 
ATOM   2336 H  H    . GLY A 1 146 ? 29.283 7.806  4.455   1.00 15.31 ? 148 GLY A H    1 
ATOM   2337 H  HA2  . GLY A 1 146 ? 27.393 8.507  6.131   1.00 17.16 ? 148 GLY A HA2  1 
ATOM   2338 H  HA3  . GLY A 1 146 ? 28.467 9.471  5.504   1.00 17.16 ? 148 GLY A HA3  1 
ATOM   2339 N  N    . LYS A 1 147 ? 26.056 10.385 4.949   1.00 9.84  ? 149 LYS A N    1 
ATOM   2340 C  CA   . LYS A 1 147 ? 25.101 11.140 4.144   1.00 10.77 ? 149 LYS A CA   1 
ATOM   2341 C  C    . LYS A 1 147 ? 25.909 11.758 2.955   1.00 10.36 ? 149 LYS A C    1 
ATOM   2342 O  O    . LYS A 1 147 ? 27.029 12.226 3.161   1.00 10.27 ? 149 LYS A O    1 
ATOM   2343 C  CB   . LYS A 1 147 ? 24.483 12.218 5.020   1.00 8.77  ? 149 LYS A CB   1 
ATOM   2344 C  CG   . LYS A 1 147 ? 23.853 11.618 6.298   1.00 9.94  ? 149 LYS A CG   1 
ATOM   2345 C  CD   . LYS A 1 147 ? 23.560 12.597 7.408   1.00 9.20  ? 149 LYS A CD   1 
ATOM   2346 C  CE   . LYS A 1 147 ? 23.015 11.920 8.611   1.00 9.37  ? 149 LYS A CE   1 
ATOM   2347 N  NZ   . LYS A 1 147 ? 22.769 12.845 9.743   1.00 9.41  ? 149 LYS A NZ   1 
ATOM   2348 H  H    . LYS A 1 147 ? 26.116 10.643 5.767   1.00 9.55  ? 149 LYS A H    1 
ATOM   2349 H  HA   . LYS A 1 147 ? 24.406 10.558 3.800   1.00 10.81 ? 149 LYS A HA   1 
ATOM   2350 H  HB2  . LYS A 1 147 ? 25.170 12.848 5.287   1.00 9.16  ? 149 LYS A HB2  1 
ATOM   2351 H  HB3  . LYS A 1 147 ? 23.785 12.674 4.522   1.00 9.16  ? 149 LYS A HB3  1 
ATOM   2352 H  HG2  . LYS A 1 147 ? 23.015 11.195 6.055   1.00 10.19 ? 149 LYS A HG2  1 
ATOM   2353 H  HG3  . LYS A 1 147 ? 24.461 10.950 6.653   1.00 10.19 ? 149 LYS A HG3  1 
ATOM   2354 H  HD2  . LYS A 1 147 ? 24.380 13.048 7.660   1.00 9.65  ? 149 LYS A HD2  1 
ATOM   2355 H  HD3  . LYS A 1 147 ? 22.904 13.241 7.100   1.00 9.65  ? 149 LYS A HD3  1 
ATOM   2356 H  HE2  . LYS A 1 147 ? 22.171 11.500 8.380   1.00 9.57  ? 149 LYS A HE2  1 
ATOM   2357 H  HE3  . LYS A 1 147 ? 23.648 11.247 8.907   1.00 9.57  ? 149 LYS A HE3  1 
ATOM   2358 H  HZ1  . LYS A 1 147 ? 22.444 12.395 10.439  1.00 9.72  ? 149 LYS A HZ1  1 
ATOM   2359 H  HZ2  . LYS A 1 147 ? 23.530 13.239 9.984   1.00 9.72  ? 149 LYS A HZ2  1 
ATOM   2360 H  HZ3  . LYS A 1 147 ? 22.183 13.470 9.503   1.00 9.72  ? 149 LYS A HZ3  1 
ATOM   2361 N  N    . PRO A 1 148 ? 25.377 11.814 1.723   1.00 10.05 ? 150 PRO A N    1 
ATOM   2362 C  CA   . PRO A 1 148 ? 23.960 11.687 1.356   1.00 8.07  ? 150 PRO A CA   1 
ATOM   2363 C  C    . PRO A 1 148 ? 23.460 10.299 1.057   1.00 10.46 ? 150 PRO A C    1 
ATOM   2364 O  O    . PRO A 1 148 ? 22.314 10.201 0.638   1.00 11.21 ? 150 PRO A O    1 
ATOM   2365 C  CB   . PRO A 1 148 ? 23.861 12.548 0.112   1.00 9.87  ? 150 PRO A CB   1 
ATOM   2366 C  CG   . PRO A 1 148 ? 25.205 12.316 -0.534  1.00 11.00 ? 150 PRO A CG   1 
ATOM   2367 C  CD   . PRO A 1 148 ? 26.161 12.346 0.609   1.00 11.88 ? 150 PRO A CD   1 
ATOM   2368 H  HA   . PRO A 1 148 ? 23.404 12.076 2.050   1.00 8.36  ? 150 PRO A HA   1 
ATOM   2369 H  HB2  . PRO A 1 148 ? 23.139 12.236 -0.456  1.00 10.29 ? 150 PRO A HB2  1 
ATOM   2370 H  HB3  . PRO A 1 148 ? 23.743 13.479 0.356   1.00 10.29 ? 150 PRO A HB3  1 
ATOM   2371 H  HG2  . PRO A 1 148 ? 25.217 11.451 -0.973  1.00 11.12 ? 150 PRO A HG2  1 
ATOM   2372 H  HG3  . PRO A 1 148 ? 25.397 13.028 -1.164  1.00 11.12 ? 150 PRO A HG3  1 
ATOM   2373 H  HD2  . PRO A 1 148 ? 26.922 11.772 0.428   1.00 11.95 ? 150 PRO A HD2  1 
ATOM   2374 H  HD3  . PRO A 1 148 ? 26.438 13.257 0.795   1.00 11.95 ? 150 PRO A HD3  1 
ATOM   2375 N  N    . ASP A 1 149 ? 24.214 9.249  1.368   1.00 10.64 ? 151 ASP A N    1 
ATOM   2376 C  CA   . ASP A 1 149 ? 23.678 7.897  1.240   1.00 13.75 ? 151 ASP A CA   1 
ATOM   2377 C  C    . ASP A 1 149 ? 22.536 7.804  2.262   1.00 11.52 ? 151 ASP A C    1 
ATOM   2378 O  O    . ASP A 1 149 ? 22.706 8.243  3.410   1.00 11.40 ? 151 ASP A O    1 
ATOM   2379 C  CB   . ASP A 1 149 ? 24.801 6.905  1.502   1.00 16.70 ? 151 ASP A CB   1 
ATOM   2380 C  CG   . ASP A 1 149 ? 24.383 5.472  1.294   1.00 18.09 ? 151 ASP A CG   1 
ATOM   2381 O  OD1  . ASP A 1 149 ? 23.342 5.036  1.833   1.00 16.73 ? 151 ASP A OD1  1 
ATOM   2382 O  OD2  . ASP A 1 149 ? 25.140 4.788  0.585   1.00 23.93 ? 151 ASP A OD2  1 
ATOM   2383 H  H    . ASP A 1 149 ? 25.026 9.289  1.650   1.00 10.72 ? 151 ASP A H    1 
ATOM   2384 H  HA   . ASP A 1 149 ? 23.325 7.756  0.348   1.00 13.40 ? 151 ASP A HA   1 
ATOM   2385 H  HB2  . ASP A 1 149 ? 25.535 7.093  0.896   1.00 15.83 ? 151 ASP A HB2  1 
ATOM   2386 H  HB3  . ASP A 1 149 ? 25.097 7.000  2.421   1.00 15.83 ? 151 ASP A HB3  1 
ATOM   2387 N  N    . PRO A 1 150 ? 21.371 7.250  1.880   1.00 10.19 ? 152 PRO A N    1 
ATOM   2388 C  CA   . PRO A 1 150 ? 20.223 7.157  2.798   1.00 11.84 ? 152 PRO A CA   1 
ATOM   2389 C  C    . PRO A 1 150 ? 20.327 6.088  3.865   1.00 13.11 ? 152 PRO A C    1 
ATOM   2390 O  O    . PRO A 1 150 ? 19.460 6.085  4.751   1.00 12.82 ? 152 PRO A O    1 
ATOM   2391 C  CB   . PRO A 1 150 ? 19.056 6.856  1.852   1.00 12.77 ? 152 PRO A CB   1 
ATOM   2392 C  CG   . PRO A 1 150 ? 19.638 6.172  0.755   1.00 17.10 ? 152 PRO A CG   1 
ATOM   2393 C  CD   . PRO A 1 150 ? 21.043 6.752  0.546   1.00 15.43 ? 152 PRO A CD   1 
ATOM   2394 H  HA   . PRO A 1 150 ? 20.070 8.014  3.225   1.00 11.32 ? 152 PRO A HA   1 
ATOM   2395 H  HB2  . PRO A 1 150 ? 18.407 6.292  2.302   1.00 12.11 ? 152 PRO A HB2  1 
ATOM   2396 H  HB3  . PRO A 1 150 ? 18.647 7.686  1.562   1.00 12.11 ? 152 PRO A HB3  1 
ATOM   2397 H  HG2  . PRO A 1 150 ? 19.692 5.226  0.959   1.00 16.16 ? 152 PRO A HG2  1 
ATOM   2398 H  HG3  . PRO A 1 150 ? 19.095 6.315  -0.036  1.00 16.16 ? 152 PRO A HG3  1 
ATOM   2399 H  HD2  . PRO A 1 150 ? 21.664 6.057  0.279   1.00 14.73 ? 152 PRO A HD2  1 
ATOM   2400 H  HD3  . PRO A 1 150 ? 21.021 7.481  -0.094  1.00 14.73 ? 152 PRO A HD3  1 
ATOM   2401 N  N    . ASP A 1 151 ? 21.351 5.244  3.780   1.00 14.07 ? 153 ASP A N    1 
ATOM   2402 C  CA   . ASP A 1 151 ? 21.566 4.092  4.712   1.00 18.81 ? 153 ASP A CA   1 
ATOM   2403 C  C    . ASP A 1 151 ? 21.189 4.450  6.142   1.00 16.21 ? 153 ASP A C    1 
ATOM   2404 O  O    . ASP A 1 151 ? 20.396 3.744  6.810   1.00 16.89 ? 153 ASP A O    1 
ATOM   2405 C  CB   . ASP A 1 151 ? 23.057 3.600  4.727   1.00 21.22 ? 153 ASP A CB   1 
ATOM   2406 C  CG   . ASP A 1 151 ? 23.439 2.673  3.575   1.00 28.32 ? 153 ASP A CG   1 
ATOM   2407 O  OD1  . ASP A 1 151 ? 22.564 2.109  2.886   1.00 26.80 ? 153 ASP A OD1  1 
ATOM   2408 O  OD2  . ASP A 1 151 ? 24.680 2.456  3.411   1.00 30.14 ? 153 ASP A OD2  1 
ATOM   2409 H  H    . ASP A 1 151 ? 21.963 5.305  3.179   1.00 13.38 ? 153 ASP A H    1 
ATOM   2410 H  HA   . ASP A 1 151 ? 21.007 3.350  4.431   1.00 17.50 ? 153 ASP A HA   1 
ATOM   2411 H  HB2  . ASP A 1 151 ? 23.639 4.375  4.685   1.00 19.61 ? 153 ASP A HB2  1 
ATOM   2412 H  HB3  . ASP A 1 151 ? 23.215 3.119  5.555   1.00 19.61 ? 153 ASP A HB3  1 
ATOM   2413 N  N    . ILE A 1 152 ? 21.770 5.519  6.669   1.00 12.49 ? 154 ILE A N    1 
ATOM   2414 C  CA   . ILE A 1 152 ? 21.640 5.805  8.088   1.00 14.95 ? 154 ILE A CA   1 
ATOM   2415 C  C    . ILE A 1 152 ? 20.224 6.132  8.496   1.00 12.55 ? 154 ILE A C    1 
ATOM   2416 O  O    . ILE A 1 152 ? 19.777 5.782  9.589   1.00 14.01 ? 154 ILE A O    1 
ATOM   2417 C  CB   . ILE A 1 152 ? 22.633 6.897  8.553   1.00 14.81 ? 154 ILE A CB   1 
ATOM   2418 C  CG1  . ILE A 1 152 ? 22.746 6.904  10.079  1.00 16.02 ? 154 ILE A CG1  1 
ATOM   2419 C  CG2  . ILE A 1 152 ? 22.317 8.252  7.966   1.00 15.04 ? 154 ILE A CG2  1 
ATOM   2420 C  CD1  . ILE A 1 152 ? 23.830 7.800  10.666  1.00 18.52 ? 154 ILE A CD1  1 
ATOM   2421 H  H    . ILE A 1 152 ? 22.240 6.090  6.231   1.00 11.40 ? 154 ILE A H    1 
ATOM   2422 H  HA   . ILE A 1 152 ? 21.881 4.997  8.567   1.00 13.86 ? 154 ILE A HA   1 
ATOM   2423 H  HB   . ILE A 1 152 ? 23.505 6.644  8.211   1.00 14.18 ? 154 ILE A HB   1 
ATOM   2424 H  HG12 . ILE A 1 152 ? 21.898 7.198  10.446  1.00 15.21 ? 154 ILE A HG12 1 
ATOM   2425 H  HG13 . ILE A 1 152 ? 22.928 5.998  10.375  1.00 15.21 ? 154 ILE A HG13 1 
ATOM   2426 H  HG21 . ILE A 1 152 ? 22.967 8.896  8.289   1.00 15.02 ? 154 ILE A HG21 1 
ATOM   2427 H  HG22 . ILE A 1 152 ? 22.360 8.195  6.998   1.00 15.02 ? 154 ILE A HG22 1 
ATOM   2428 H  HG23 . ILE A 1 152 ? 21.425 8.515  8.243   1.00 15.02 ? 154 ILE A HG23 1 
ATOM   2429 H  HD11 . ILE A 1 152 ? 23.810 7.726  11.633  1.00 18.02 ? 154 ILE A HD11 1 
ATOM   2430 H  HD12 . ILE A 1 152 ? 24.693 7.513  10.329  1.00 18.02 ? 154 ILE A HD12 1 
ATOM   2431 H  HD13 . ILE A 1 152 ? 23.659 8.717  10.400  1.00 18.02 ? 154 ILE A HD13 1 
ATOM   2432 N  N    . PHE A 1 153 ? 19.477 6.829  7.620   1.00 12.26 ? 155 PHE A N    1 
ATOM   2433 C  CA   . PHE A 1 153 ? 18.083 7.147  7.931   1.00 11.93 ? 155 PHE A CA   1 
ATOM   2434 C  C    . PHE A 1 153 ? 17.167 5.933  7.741   1.00 12.30 ? 155 PHE A C    1 
ATOM   2435 O  O    . PHE A 1 153 ? 16.251 5.749  8.497   1.00 14.47 ? 155 PHE A O    1 
ATOM   2436 C  CB   . PHE A 1 153 ? 17.554 8.343  7.068   1.00 12.33 ? 155 PHE A CB   1 
ATOM   2437 C  CG   . PHE A 1 153 ? 18.216 9.689  7.370   1.00 10.20 ? 155 PHE A CG   1 
ATOM   2438 C  CD1  . PHE A 1 153 ? 18.595 9.993  8.668   1.00 12.81 ? 155 PHE A CD1  1 
ATOM   2439 C  CD2  . PHE A 1 153 ? 18.473 10.635 6.354   1.00 9.44  ? 155 PHE A CD2  1 
ATOM   2440 C  CE1  . PHE A 1 153 ? 19.193 11.226 8.947   1.00 11.16 ? 155 PHE A CE1  1 
ATOM   2441 C  CE2  . PHE A 1 153 ? 19.044 11.852 6.646   1.00 8.16  ? 155 PHE A CE2  1 
ATOM   2442 C  CZ   . PHE A 1 153 ? 19.417 12.137 7.913   1.00 8.10  ? 155 PHE A CZ   1 
ATOM   2443 H  H    . PHE A 1 153 ? 19.751 7.119  6.858   1.00 11.37 ? 155 PHE A H    1 
ATOM   2444 H  HA   . PHE A 1 153 ? 18.029 7.412  8.863   1.00 10.97 ? 155 PHE A HA   1 
ATOM   2445 H  HB2  . PHE A 1 153 ? 17.710 8.142  6.132   1.00 11.89 ? 155 PHE A HB2  1 
ATOM   2446 H  HB3  . PHE A 1 153 ? 16.602 8.442  7.226   1.00 11.89 ? 155 PHE A HB3  1 
ATOM   2447 H  HD1  . PHE A 1 153 ? 18.441 9.384  9.354   1.00 12.89 ? 155 PHE A HD1  1 
ATOM   2448 H  HD2  . PHE A 1 153 ? 18.217 10.448 5.480   1.00 9.99  ? 155 PHE A HD2  1 
ATOM   2449 H  HE1  . PHE A 1 153 ? 19.446 11.435 9.817   1.00 11.65 ? 155 PHE A HE1  1 
ATOM   2450 H  HE2  . PHE A 1 153 ? 19.207 12.463 5.965   1.00 9.08  ? 155 PHE A HE2  1 
ATOM   2451 H  HZ   . PHE A 1 153 ? 19.816 12.956 8.101   1.00 8.99  ? 155 PHE A HZ   1 
ATOM   2452 N  N    . LEU A 1 154 ? 17.394 5.157  6.707   1.00 13.08 ? 156 LEU A N    1 
ATOM   2453 C  CA   . LEU A 1 154 ? 16.657 3.901  6.557   1.00 14.97 ? 156 LEU A CA   1 
ATOM   2454 C  C    . LEU A 1 154 ? 16.869 2.939  7.713   1.00 18.53 ? 156 LEU A C    1 
ATOM   2455 O  O    . LEU A 1 154 ? 15.892 2.363  8.214   1.00 19.89 ? 156 LEU A O    1 
ATOM   2456 C  CB   . LEU A 1 154 ? 17.049 3.226  5.255   1.00 18.90 ? 156 LEU A CB   1 
ATOM   2457 C  CG   . LEU A 1 154 ? 16.774 3.980  3.959   1.00 16.58 ? 156 LEU A CG   1 
ATOM   2458 C  CD1  . LEU A 1 154 ? 17.491 3.340  2.814   1.00 18.61 ? 156 LEU A CD1  1 
ATOM   2459 C  CD2  . LEU A 1 154 ? 15.317 3.995  3.662   1.00 19.36 ? 156 LEU A CD2  1 
ATOM   2460 H  H    . LEU A 1 154 ? 17.960 5.321  6.080   1.00 12.47 ? 156 LEU A H    1 
ATOM   2461 H  HA   . LEU A 1 154 ? 15.709 4.102  6.511   1.00 13.61 ? 156 LEU A HA   1 
ATOM   2462 H  HB2  . LEU A 1 154 ? 18.003 3.050  5.284   1.00 17.40 ? 156 LEU A HB2  1 
ATOM   2463 H  HB3  . LEU A 1 154 ? 16.573 2.383  5.199   1.00 17.40 ? 156 LEU A HB3  1 
ATOM   2464 H  HG   . LEU A 1 154 ? 17.082 4.896  4.044   1.00 15.57 ? 156 LEU A HG   1 
ATOM   2465 H  HD11 . LEU A 1 154 ? 17.299 3.838  2.004   1.00 17.43 ? 156 LEU A HD11 1 
ATOM   2466 H  HD12 . LEU A 1 154 ? 18.444 3.352  2.993   1.00 17.43 ? 156 LEU A HD12 1 
ATOM   2467 H  HD13 . LEU A 1 154 ? 17.182 2.425  2.721   1.00 17.43 ? 156 LEU A HD13 1 
ATOM   2468 H  HD21 . LEU A 1 154 ? 15.168 4.479  2.835   1.00 18.15 ? 156 LEU A HD21 1 
ATOM   2469 H  HD22 . LEU A 1 154 ? 15.004 3.081  3.570   1.00 18.15 ? 156 LEU A HD22 1 
ATOM   2470 H  HD23 . LEU A 1 154 ? 14.850 4.433  4.391   1.00 18.15 ? 156 LEU A HD23 1 
ATOM   2471 N  N    . ALA A 1 155 ? 18.118 2.758  8.132   1.00 13.54 ? 157 ALA A N    1 
ATOM   2472 C  CA   . ALA A 1 155 ? 18.396 1.931  9.322   1.00 17.82 ? 157 ALA A CA   1 
ATOM   2473 C  C    . ALA A 1 155 ? 17.672 2.488  10.538  1.00 19.79 ? 157 ALA A C    1 
ATOM   2474 O  O    . ALA A 1 155 ? 17.110 1.745  11.331  1.00 21.99 ? 157 ALA A O    1 
ATOM   2475 C  CB   . ALA A 1 155 ? 19.925 1.845  9.585   1.00 17.68 ? 157 ALA A CB   1 
ATOM   2476 H  H    . ALA A 1 155 ? 18.816 3.094  7.759   1.00 11.67 ? 157 ALA A H    1 
ATOM   2477 H  HA   . ALA A 1 155 ? 18.068 1.032  9.165   1.00 15.30 ? 157 ALA A HA   1 
ATOM   2478 H  HB1  . ALA A 1 155 ? 20.079 1.297  10.371  1.00 15.25 ? 157 ALA A HB1  1 
ATOM   2479 H  HB2  . ALA A 1 155 ? 20.355 1.446  8.813   1.00 15.25 ? 157 ALA A HB2  1 
ATOM   2480 H  HB3  . ALA A 1 155 ? 20.270 2.739  9.732   1.00 15.25 ? 157 ALA A HB3  1 
ATOM   2481 N  N    . CYS A 1 156 ? 17.711 3.804  10.727  1.00 16.54 ? 158 CYS A N    1 
ATOM   2482 C  CA   . CYS A 1 156 ? 17.070 4.417  11.853  1.00 18.02 ? 158 CYS A CA   1 
ATOM   2483 C  C    . CYS A 1 156 ? 15.567 4.154  11.864  1.00 16.40 ? 158 CYS A C    1 
ATOM   2484 O  O    . CYS A 1 156 ? 15.027 3.712  12.880  1.00 18.80 ? 158 CYS A O    1 
ATOM   2485 C  CB   . CYS A 1 156 ? 17.393 5.906  11.880  1.00 16.37 ? 158 CYS A CB   1 
ATOM   2486 S  SG   . CYS A 1 156 ? 16.829 6.735  13.379  1.00 17.35 ? 158 CYS A SG   1 
ATOM   2487 H  H    . CYS A 1 156 ? 18.109 4.359  10.204  1.00 15.12 ? 158 CYS A H    1 
ATOM   2488 H  HA   . CYS A 1 156 ? 17.436 4.027  12.662  1.00 16.55 ? 158 CYS A HA   1 
ATOM   2489 H  HB2  . CYS A 1 156 ? 18.355 6.020  11.820  1.00 15.71 ? 158 CYS A HB2  1 
ATOM   2490 H  HB3  . CYS A 1 156 ? 16.963 6.334  11.123  1.00 15.71 ? 158 CYS A HB3  1 
ATOM   2491 H  HG   . CYS A 1 156 ? 17.123 7.897  13.317  1.00 16.59 ? 158 CYS A HG   1 
ATOM   2492 N  N    . ALA A 1 157 ? 14.898 4.347  10.737  1.00 15.09 ? 159 ALA A N    1 
ATOM   2493 C  CA   . ALA A 1 157 ? 13.441 4.137  10.660  1.00 18.01 ? 159 ALA A CA   1 
ATOM   2494 C  C    . ALA A 1 157 ? 13.076 2.658  10.910  1.00 17.91 ? 159 ALA A C    1 
ATOM   2495 O  O    . ALA A 1 157 ? 12.111 2.394  11.588  1.00 21.62 ? 159 ALA A O    1 
ATOM   2496 C  CB   . ALA A 1 157 ? 12.942 4.610  9.335   1.00 15.80 ? 159 ALA A CB   1 
ATOM   2497 H  H    . ALA A 1 157 ? 15.256 4.599  9.996   1.00 14.16 ? 159 ALA A H    1 
ATOM   2498 H  HA   . ALA A 1 157 ? 13.010 4.669  11.347  1.00 16.57 ? 159 ALA A HA   1 
ATOM   2499 H  HB1  . ALA A 1 157 ? 11.983 4.469  9.290   1.00 14.76 ? 159 ALA A HB1  1 
ATOM   2500 H  HB2  . ALA A 1 157 ? 13.143 5.554  9.241   1.00 14.76 ? 159 ALA A HB2  1 
ATOM   2501 H  HB3  . ALA A 1 157 ? 13.384 4.105  8.634   1.00 14.76 ? 159 ALA A HB3  1 
ATOM   2502 N  N    . LYS A 1 158 ? 13.879 1.737  10.392  1.00 20.23 ? 160 LYS A N    1 
ATOM   2503 C  CA   . LYS A 1 158 ? 13.589 0.306  10.552  1.00 25.22 ? 160 LYS A CA   1 
ATOM   2504 C  C    . LYS A 1 158 ? 13.734 -0.213 11.978  1.00 28.33 ? 160 LYS A C    1 
ATOM   2505 O  O    . LYS A 1 158 ? 13.419 -1.366 12.244  1.00 30.95 ? 160 LYS A O    1 
ATOM   2506 C  CB   . LYS A 1 158 ? 14.506 -0.542 9.686   1.00 25.07 ? 160 LYS A CB   1 
ATOM   2507 C  CG   . LYS A 1 158 ? 14.250 -0.460 8.240   1.00 28.93 ? 160 LYS A CG   1 
ATOM   2508 C  CD   . LYS A 1 158 ? 15.398 -1.078 7.462   1.00 32.90 ? 160 LYS A CD   1 
ATOM   2509 C  CE   . LYS A 1 158 ? 15.236 -0.797 6.004   1.00 37.43 ? 160 LYS A CE   1 
ATOM   2510 N  NZ   . LYS A 1 158 ? 16.445 -1.138 5.224   1.00 43.48 ? 160 LYS A NZ   1 
ATOM   2511 H  H    . LYS A 1 158 ? 14.594 1.907  9.946   1.00 17.91 ? 160 LYS A H    1 
ATOM   2512 H  HA   . LYS A 1 158 ? 12.676 0.140  10.268  1.00 21.86 ? 160 LYS A HA   1 
ATOM   2513 H  HB2  . LYS A 1 158 ? 15.422 -0.258 9.837   1.00 21.60 ? 160 LYS A HB2  1 
ATOM   2514 H  HB3  . LYS A 1 158 ? 14.407 -1.471 9.948   1.00 21.60 ? 160 LYS A HB3  1 
ATOM   2515 H  HG2  . LYS A 1 158 ? 13.438 -0.946 8.027   1.00 25.76 ? 160 LYS A HG2  1 
ATOM   2516 H  HG3  . LYS A 1 158 ? 14.167 0.470  7.978   1.00 25.76 ? 160 LYS A HG3  1 
ATOM   2517 H  HD2  . LYS A 1 158 ? 16.237 -0.693 7.760   1.00 29.72 ? 160 LYS A HD2  1 
ATOM   2518 H  HD3  . LYS A 1 158 ? 15.398 -2.040 7.593   1.00 29.72 ? 160 LYS A HD3  1 
ATOM   2519 H  HE2  . LYS A 1 158 ? 14.498 -1.323 5.659   1.00 34.65 ? 160 LYS A HE2  1 
ATOM   2520 H  HE3  . LYS A 1 158 ? 15.057 0.149  5.882   1.00 34.65 ? 160 LYS A HE3  1 
ATOM   2521 H  HZ1  . LYS A 1 158 ? 16.312 -0.958 4.363   1.00 40.79 ? 160 LYS A HZ1  1 
ATOM   2522 H  HZ2  . LYS A 1 158 ? 17.139 -0.664 5.515   1.00 40.79 ? 160 LYS A HZ2  1 
ATOM   2523 H  HZ3  . LYS A 1 158 ? 16.629 -2.005 5.313   1.00 40.79 ? 160 LYS A HZ3  1 
ATOM   2524 N  N    . ARG A 1 159 ? 14.220 0.610  12.895  1.00 22.84 ? 161 ARG A N    1 
ATOM   2525 C  CA   . ARG A 1 159 ? 14.459 0.157  14.270  1.00 22.53 ? 161 ARG A CA   1 
ATOM   2526 C  C    . ARG A 1 159 ? 13.374 0.646  15.215  1.00 26.51 ? 161 ARG A C    1 
ATOM   2527 O  O    . ARG A 1 159 ? 13.404 0.288  16.390  1.00 28.44 ? 161 ARG A O    1 
ATOM   2528 C  CB   . ARG A 1 159 ? 15.848 0.575  14.781  1.00 24.64 ? 161 ARG A CB   1 
ATOM   2529 C  CG   . ARG A 1 159 ? 16.964 -0.099 14.045  1.00 21.13 ? 161 ARG A CG   1 
ATOM   2530 C  CD   . ARG A 1 159 ? 18.352 0.350  14.432  1.00 23.90 ? 161 ARG A CD   1 
ATOM   2531 N  NE   . ARG A 1 159 ? 19.258 -0.139 13.413  1.00 21.74 ? 161 ARG A NE   1 
ATOM   2532 C  CZ   . ARG A 1 159 ? 20.579 -0.068 13.456  1.00 23.88 ? 161 ARG A CZ   1 
ATOM   2533 N  NH1  . ARG A 1 159 ? 21.178 0.486  14.492  1.00 21.87 ? 161 ARG A NH1  1 
ATOM   2534 N  NH2  . ARG A 1 159 ? 21.285 -0.509 12.437  1.00 23.32 ? 161 ARG A NH2  1 
ATOM   2535 H  H    . ARG A 1 159 ? 14.422 1.434  12.753  1.00 21.07 ? 161 ARG A H    1 
ATOM   2536 H  HA   . ARG A 1 159 ? 14.430 -0.813 14.278  1.00 20.12 ? 161 ARG A HA   1 
ATOM   2537 H  HB2  . ARG A 1 159 ? 15.951 1.533  14.670  1.00 22.77 ? 161 ARG A HB2  1 
ATOM   2538 H  HB3  . ARG A 1 159 ? 15.923 0.339  15.720  1.00 22.77 ? 161 ARG A HB3  1 
ATOM   2539 H  HG2  . ARG A 1 159 ? 16.909 -1.053 14.210  1.00 19.31 ? 161 ARG A HG2  1 
ATOM   2540 H  HG3  . ARG A 1 159 ? 16.855 0.073  13.097  1.00 19.31 ? 161 ARG A HG3  1 
ATOM   2541 H  HD2  . ARG A 1 159 ? 18.395 1.319  14.456  1.00 22.58 ? 161 ARG A HD2  1 
ATOM   2542 H  HD3  . ARG A 1 159 ? 18.601 -0.033 15.287  1.00 22.58 ? 161 ARG A HD3  1 
ATOM   2543 H  HE   . ARG A 1 159 ? 18.907 -0.507 12.719  1.00 20.51 ? 161 ARG A HE   1 
ATOM   2544 H  HH11 . ARG A 1 159 ? 20.711 0.788  15.148  1.00 21.06 ? 161 ARG A HH11 1 
ATOM   2545 H  HH12 . ARG A 1 159 ? 22.036 0.532  14.518  1.00 21.06 ? 161 ARG A HH12 1 
ATOM   2546 H  HH21 . ARG A 1 159 ? 20.890 -0.871 11.765  1.00 22.31 ? 161 ARG A HH21 1 
ATOM   2547 H  HH22 . ARG A 1 159 ? 22.144 -0.475 12.463  1.00 22.31 ? 161 ARG A HH22 1 
ATOM   2548 N  N    . PHE A 1 160 ? 12.422 1.452  14.737  1.00 27.35 ? 162 PHE A N    1 
ATOM   2549 C  CA   . PHE A 1 160 ? 11.227 1.772  15.521  1.00 29.23 ? 162 PHE A CA   1 
ATOM   2550 C  C    . PHE A 1 160 ? 10.357 0.523  15.580  1.00 34.59 ? 162 PHE A C    1 
ATOM   2551 O  O    . PHE A 1 160 ? 10.399 -0.309 14.669  1.00 35.03 ? 162 PHE A O    1 
ATOM   2552 C  CB   . PHE A 1 160 ? 10.388 2.888  14.909  1.00 26.56 ? 162 PHE A CB   1 
ATOM   2553 C  CG   . PHE A 1 160 ? 10.948 4.260  15.080  1.00 24.49 ? 162 PHE A CG   1 
ATOM   2554 C  CD1  . PHE A 1 160 ? 10.902 4.903  16.297  1.00 25.25 ? 162 PHE A CD1  1 
ATOM   2555 C  CD2  . PHE A 1 160 ? 11.467 4.954  13.983  1.00 21.60 ? 162 PHE A CD2  1 
ATOM   2556 C  CE1  . PHE A 1 160 ? 11.416 6.208  16.431  1.00 24.99 ? 162 PHE A CE1  1 
ATOM   2557 C  CE2  . PHE A 1 160 ? 11.950 6.247  14.124  1.00 22.24 ? 162 PHE A CE2  1 
ATOM   2558 C  CZ   . PHE A 1 160 ? 11.935 6.859  15.352  1.00 22.30 ? 162 PHE A CZ   1 
ATOM   2559 H  H    . PHE A 1 160 ? 12.445 1.826  13.963  1.00 22.99 ? 162 PHE A H    1 
ATOM   2560 H  HA   . PHE A 1 160 ? 11.479 2.024  16.423  1.00 24.30 ? 162 PHE A HA   1 
ATOM   2561 H  HB2  . PHE A 1 160 ? 10.302 2.723  13.957  1.00 22.16 ? 162 PHE A HB2  1 
ATOM   2562 H  HB3  . PHE A 1 160 ? 9.510  2.876  15.321  1.00 22.16 ? 162 PHE A HB3  1 
ATOM   2563 H  HD1  . PHE A 1 160 ? 10.558 4.463  17.040  1.00 21.68 ? 162 PHE A HD1  1 
ATOM   2564 H  HD2  . PHE A 1 160 ? 11.488 4.544  13.148  1.00 19.12 ? 162 PHE A HD2  1 
ATOM   2565 H  HE1  . PHE A 1 160 ? 11.396 6.629  17.260  1.00 22.24 ? 162 PHE A HE1  1 
ATOM   2566 H  HE2  . PHE A 1 160 ? 12.311 6.690  13.390  1.00 20.54 ? 162 PHE A HE2  1 
ATOM   2567 H  HZ   . PHE A 1 160 ? 12.265 7.723  15.445  1.00 20.46 ? 162 PHE A HZ   1 
ATOM   2568 N  N    . SER A 1 161 ? 9.547  0.434  16.633  1.00 43.11 ? 163 SER A N    1 
ATOM   2569 C  CA   . SER A 1 161 ? 8.704  -0.729 16.902  1.00 46.11 ? 163 SER A CA   1 
ATOM   2570 C  C    . SER A 1 161 ? 7.250  -0.321 17.154  1.00 46.72 ? 163 SER A C    1 
ATOM   2571 O  O    . SER A 1 161 ? 6.941  0.260  18.199  1.00 50.81 ? 163 SER A O    1 
ATOM   2572 C  CB   . SER A 1 161 ? 9.236  -1.451 18.130  1.00 46.60 ? 163 SER A CB   1 
ATOM   2573 O  OG   . SER A 1 161 ? 8.471  -2.605 18.395  1.00 52.91 ? 163 SER A OG   1 
ATOM   2574 H  H    . SER A 1 161 ? 9.466  1.054  17.223  1.00 31.12 ? 163 SER A H    1 
ATOM   2575 H  HA   . SER A 1 161 ? 8.732  -1.336 16.146  1.00 32.77 ? 163 SER A HA   1 
ATOM   2576 H  HB2  . SER A 1 161 ? 10.157 -1.711 17.971  1.00 32.48 ? 163 SER A HB2  1 
ATOM   2577 H  HB3  . SER A 1 161 ? 9.187  -0.855 18.894  1.00 32.48 ? 163 SER A HB3  1 
ATOM   2578 H  HG   . SER A 1 161 ? 8.770  -2.999 19.074  1.00 37.38 ? 163 SER A HG   1 
ATOM   2579 N  N    . PRO A 1 162 ? 6.354  -0.585 16.188  1.00 40.84 ? 164 PRO A N    1 
ATOM   2580 C  CA   . PRO A 1 162 ? 6.609  -1.171 14.868  1.00 39.86 ? 164 PRO A CA   1 
ATOM   2581 C  C    . PRO A 1 162 ? 7.190  -0.155 13.871  1.00 33.58 ? 164 PRO A C    1 
ATOM   2582 O  O    . PRO A 1 162 ? 7.051  1.034  14.093  1.00 35.08 ? 164 PRO A O    1 
ATOM   2583 C  CB   . PRO A 1 162 ? 5.225  -1.609 14.419  1.00 41.60 ? 164 PRO A CB   1 
ATOM   2584 C  CG   . PRO A 1 162 ? 4.313  -0.658 15.089  1.00 44.28 ? 164 PRO A CG   1 
ATOM   2585 C  CD   . PRO A 1 162 ? 4.917  -0.351 16.404  1.00 41.26 ? 164 PRO A CD   1 
ATOM   2586 H  HA   . PRO A 1 162 ? 7.194  -1.942 14.937  1.00 32.78 ? 164 PRO A HA   1 
ATOM   2587 H  HB2  . PRO A 1 162 ? 5.152  -1.538 13.455  1.00 33.58 ? 164 PRO A HB2  1 
ATOM   2588 H  HB3  . PRO A 1 162 ? 5.055  -2.518 14.714  1.00 33.58 ? 164 PRO A HB3  1 
ATOM   2589 H  HG2  . PRO A 1 162 ? 4.237  0.147  14.555  1.00 36.09 ? 164 PRO A HG2  1 
ATOM   2590 H  HG3  . PRO A 1 162 ? 3.443  -1.072 15.204  1.00 36.09 ? 164 PRO A HG3  1 
ATOM   2591 H  HD2  . PRO A 1 162 ? 4.757  0.576  16.641  1.00 33.08 ? 164 PRO A HD2  1 
ATOM   2592 H  HD3  . PRO A 1 162 ? 4.575  -0.954 17.083  1.00 33.08 ? 164 PRO A HD3  1 
ATOM   2593 N  N    . PRO A 1 163 ? 7.806  -0.627 12.789  1.00 36.18 ? 165 PRO A N    1 
ATOM   2594 C  CA   . PRO A 1 163 ? 8.489  0.300  11.884  1.00 28.78 ? 165 PRO A CA   1 
ATOM   2595 C  C    . PRO A 1 163 ? 7.532  1.045  10.970  1.00 33.24 ? 165 PRO A C    1 
ATOM   2596 O  O    . PRO A 1 163 ? 6.727  0.392  10.318  1.00 34.81 ? 165 PRO A O    1 
ATOM   2597 C  CB   . PRO A 1 163 ? 9.392  -0.622 11.056  1.00 33.25 ? 165 PRO A CB   1 
ATOM   2598 C  CG   . PRO A 1 163 ? 9.428  -1.912 11.798  1.00 39.36 ? 165 PRO A CG   1 
ATOM   2599 C  CD   . PRO A 1 163 ? 8.113  -2.019 12.465  1.00 39.56 ? 165 PRO A CD   1 
ATOM   2600 H  HA   . PRO A 1 163 ? 9.032  0.932  12.381  1.00 24.24 ? 165 PRO A HA   1 
ATOM   2601 H  HB2  . PRO A 1 163 ? 9.010  -0.745 10.173  1.00 28.76 ? 165 PRO A HB2  1 
ATOM   2602 H  HB3  . PRO A 1 163 ? 10.281 -0.238 10.994  1.00 28.76 ? 165 PRO A HB3  1 
ATOM   2603 H  HG2  . PRO A 1 163 ? 9.556  -2.644 11.173  1.00 33.72 ? 165 PRO A HG2  1 
ATOM   2604 H  HG3  . PRO A 1 163 ? 10.143 -1.892 12.453  1.00 33.72 ? 165 PRO A HG3  1 
ATOM   2605 H  HD2  . PRO A 1 163 ? 7.450  -2.381 11.855  1.00 32.99 ? 165 PRO A HD2  1 
ATOM   2606 H  HD3  . PRO A 1 163 ? 8.183  -2.550 13.274  1.00 32.99 ? 165 PRO A HD3  1 
ATOM   2607 N  N    . PRO A 1 164 ? 7.639  2.377  10.893  1.00 28.95 ? 166 PRO A N    1 
ATOM   2608 C  CA   . PRO A 1 164 ? 6.775  3.151  10.001  1.00 30.10 ? 166 PRO A CA   1 
ATOM   2609 C  C    . PRO A 1 164 ? 7.175  3.028  8.538   1.00 29.20 ? 166 PRO A C    1 
ATOM   2610 O  O    . PRO A 1 164 ? 8.302  2.640  8.224   1.00 27.34 ? 166 PRO A O    1 
ATOM   2611 C  CB   . PRO A 1 164 ? 7.023  4.590  10.465  1.00 27.72 ? 166 PRO A CB   1 
ATOM   2612 C  CG   . PRO A 1 164 ? 8.435  4.580  10.900  1.00 28.15 ? 166 PRO A CG   1 
ATOM   2613 C  CD   . PRO A 1 164 ? 8.637  3.238  11.555  1.00 24.73 ? 166 PRO A CD   1 
ATOM   2614 H  HA   . PRO A 1 164 ? 5.841  2.915  10.119  1.00 26.17 ? 166 PRO A HA   1 
ATOM   2615 H  HB2  . PRO A 1 164 ? 6.892  5.204  9.725   1.00 24.55 ? 166 PRO A HB2  1 
ATOM   2616 H  HB3  . PRO A 1 164 ? 6.434  4.806  11.205  1.00 24.55 ? 166 PRO A HB3  1 
ATOM   2617 H  HG2  . PRO A 1 164 ? 9.015  4.675  10.128  1.00 25.54 ? 166 PRO A HG2  1 
ATOM   2618 H  HG3  . PRO A 1 164 ? 8.588  5.297  11.534  1.00 25.54 ? 166 PRO A HG3  1 
ATOM   2619 H  HD2  . PRO A 1 164 ? 9.533  2.909  11.383  1.00 21.28 ? 166 PRO A HD2  1 
ATOM   2620 H  HD3  . PRO A 1 164 ? 8.456  3.295  12.506  1.00 21.28 ? 166 PRO A HD3  1 
ATOM   2621 N  N    . ALA A 1 165 ? 6.261  3.372  7.641   1.00 27.52 ? 167 ALA A N    1 
ATOM   2622 C  CA   . ALA A 1 165 ? 6.606  3.613  6.269   1.00 25.14 ? 167 ALA A CA   1 
ATOM   2623 C  C    . ALA A 1 165 ? 7.538  4.820  6.248   1.00 22.42 ? 167 ALA A C    1 
ATOM   2624 O  O    . ALA A 1 165 ? 7.365  5.756  7.020   1.00 22.53 ? 167 ALA A O    1 
ATOM   2625 C  CB   . ALA A 1 165 ? 5.366  3.914  5.455   1.00 24.22 ? 167 ALA A CB   1 
ATOM   2626 H  H    . ALA A 1 165 ? 5.424  3.472  7.815   1.00 23.54 ? 167 ALA A H    1 
ATOM   2627 H  HA   . ALA A 1 165 ? 7.063  2.844  5.893   1.00 21.80 ? 167 ALA A HA   1 
ATOM   2628 H  HB1  . ALA A 1 165 ? 5.624  4.073  4.533   1.00 20.62 ? 167 ALA A HB1  1 
ATOM   2629 H  HB2  . ALA A 1 165 ? 4.764  3.155  5.504   1.00 20.62 ? 167 ALA A HB2  1 
ATOM   2630 H  HB3  . ALA A 1 165 ? 4.934  4.703  5.818   1.00 20.62 ? 167 ALA A HB3  1 
ATOM   2631 N  N    . MET A 1 166 ? 8.493  4.806  5.338   1.00 26.00 ? 168 MET A N    1 
ATOM   2632 C  CA   . MET A 1 166 ? 9.464  5.880  5.298   1.00 22.08 ? 168 MET A CA   1 
ATOM   2633 C  C    . MET A 1 166 ? 8.766  7.216  5.062   1.00 22.34 ? 168 MET A C    1 
ATOM   2634 O  O    . MET A 1 166 ? 9.171  8.249  5.600   1.00 21.03 ? 168 MET A O    1 
ATOM   2635 C  CB   . MET A 1 166 ? 10.506 5.613  4.208   1.00 21.61 ? 168 MET A CB   1 
ATOM   2636 C  CG   . MET A 1 166 ? 11.296 4.305  4.378   1.00 26.18 ? 168 MET A CG   1 
ATOM   2637 S  SD   . MET A 1 166 ? 12.129 4.061  5.949   1.00 26.53 ? 168 MET A SD   1 
ATOM   2638 C  CE   . MET A 1 166 ? 10.783 3.447  6.987   1.00 32.04 ? 168 MET A CE   1 
ATOM   2639 H  H    . MET A 1 166 ? 8.602  4.197  4.740   1.00 22.58 ? 168 MET A H    1 
ATOM   2640 H  HA   . MET A 1 166 ? 9.927  5.915  6.149   1.00 19.56 ? 168 MET A HA   1 
ATOM   2641 H  HB2  . MET A 1 166 ? 10.054 5.574  3.351   1.00 19.53 ? 168 MET A HB2  1 
ATOM   2642 H  HB3  . MET A 1 166 ? 11.145 6.343  4.206   1.00 19.53 ? 168 MET A HB3  1 
ATOM   2643 H  HG2  . MET A 1 166 ? 10.681 3.563  4.262   1.00 23.68 ? 168 MET A HG2  1 
ATOM   2644 H  HG3  . MET A 1 166 ? 11.974 4.269  3.685   1.00 23.68 ? 168 MET A HG3  1 
ATOM   2645 H  HE1  . MET A 1 166 ? 11.124 3.277  7.879   1.00 28.45 ? 168 MET A HE1  1 
ATOM   2646 H  HE2  . MET A 1 166 ? 10.081 4.116  7.022   1.00 28.45 ? 168 MET A HE2  1 
ATOM   2647 H  HE3  . MET A 1 166 ? 10.438 2.626  6.602   1.00 28.45 ? 168 MET A HE3  1 
ATOM   2648 N  N    . GLU A 1 167 ? 7.705  7.205  4.280   1.00 22.06 ? 169 GLU A N    1 
ATOM   2649 C  CA   . GLU A 1 167 ? 7.023  8.434  3.980   1.00 20.37 ? 169 GLU A CA   1 
ATOM   2650 C  C    . GLU A 1 167 ? 6.311  9.055  5.180   1.00 19.35 ? 169 GLU A C    1 
ATOM   2651 O  O    . GLU A 1 167 ? 5.867  10.178 5.107   1.00 20.42 ? 169 GLU A O    1 
ATOM   2652 C  CB   . GLU A 1 167 ? 6.040  8.242  2.808   1.00 25.90 ? 169 GLU A CB   1 
ATOM   2653 C  CG   . GLU A 1 167 ? 4.905  7.286  3.125   1.00 30.66 ? 169 GLU A CG   1 
ATOM   2654 C  CD   . GLU A 1 167 ? 3.865  7.145  2.027   1.00 43.35 ? 169 GLU A CD   1 
ATOM   2655 O  OE1  . GLU A 1 167 ? 4.187  7.374  0.833   1.00 49.83 ? 169 GLU A OE1  1 
ATOM   2656 O  OE2  . GLU A 1 167 ? 2.712  6.802  2.387   1.00 45.63 ? 169 GLU A OE2  1 
ATOM   2657 H  H    . GLU A 1 167 ? 7.366  6.504  3.914   1.00 19.79 ? 169 GLU A H    1 
ATOM   2658 H  HA   . GLU A 1 167 ? 7.687  9.077  3.686   1.00 18.34 ? 169 GLU A HA   1 
ATOM   2659 H  HB2  . GLU A 1 167 ? 5.651  9.101  2.581   1.00 23.56 ? 169 GLU A HB2  1 
ATOM   2660 H  HB3  . GLU A 1 167 ? 6.524  7.886  2.047   1.00 23.56 ? 169 GLU A HB3  1 
ATOM   2661 H  HG2  . GLU A 1 167 ? 5.278  6.406  3.290   1.00 27.34 ? 169 GLU A HG2  1 
ATOM   2662 H  HG3  . GLU A 1 167 ? 4.449  7.600  3.922   1.00 27.34 ? 169 GLU A HG3  1 
ATOM   2663 N  N    . LYS A 1 168 ? 6.231  8.343  6.296   1.00 16.53 ? 170 LYS A N    1 
ATOM   2664 C  CA   . LYS A 1 168 ? 5.659  8.920  7.520   1.00 19.21 ? 170 LYS A CA   1 
ATOM   2665 C  C    . LYS A 1 168 ? 6.733  9.384  8.507   1.00 16.91 ? 170 LYS A C    1 
ATOM   2666 O  O    . LYS A 1 168 ? 6.451  9.712  9.636   1.00 18.60 ? 170 LYS A O    1 
ATOM   2667 C  CB   . LYS A 1 168 ? 4.737  7.913  8.198   1.00 21.17 ? 170 LYS A CB   1 
ATOM   2668 C  CG   . LYS A 1 168 ? 3.469  7.554  7.428   1.00 22.59 ? 170 LYS A CG   1 
ATOM   2669 C  CD   . LYS A 1 168 ? 2.637  8.729  7.048   1.00 26.67 ? 170 LYS A CD   1 
ATOM   2670 C  CE   . LYS A 1 168 ? 1.547  8.279  6.119   1.00 32.63 ? 170 LYS A CE   1 
ATOM   2671 N  NZ   . LYS A 1 168 ? 0.850  9.467  5.579   1.00 35.98 ? 170 LYS A NZ   1 
ATOM   2672 H  H    . LYS A 1 168 ? 6.497  7.529  6.378   1.00 14.62 ? 170 LYS A H    1 
ATOM   2673 H  HA   . LYS A 1 168 ? 5.126  9.693  7.279   1.00 16.92 ? 170 LYS A HA   1 
ATOM   2674 H  HB2  . LYS A 1 168 ? 5.233  7.091  8.340   1.00 17.82 ? 170 LYS A HB2  1 
ATOM   2675 H  HB3  . LYS A 1 168 ? 4.463  8.277  9.054   1.00 17.82 ? 170 LYS A HB3  1 
ATOM   2676 H  HG2  . LYS A 1 168 ? 3.720  7.092  6.612   1.00 18.58 ? 170 LYS A HG2  1 
ATOM   2677 H  HG3  . LYS A 1 168 ? 2.924  6.971  7.980   1.00 18.58 ? 170 LYS A HG3  1 
ATOM   2678 H  HD2  . LYS A 1 168 ? 2.232  9.114  7.840   1.00 22.72 ? 170 LYS A HD2  1 
ATOM   2679 H  HD3  . LYS A 1 168 ? 3.186  9.384  6.590   1.00 22.72 ? 170 LYS A HD3  1 
ATOM   2680 H  HE2  . LYS A 1 168 ? 1.931  7.781  5.381   1.00 28.10 ? 170 LYS A HE2  1 
ATOM   2681 H  HE3  . LYS A 1 168 ? 0.907  7.736  6.604   1.00 28.10 ? 170 LYS A HE3  1 
ATOM   2682 H  HZ1  . LYS A 1 168 ? 0.201  9.213  5.026   1.00 31.57 ? 170 LYS A HZ1  1 
ATOM   2683 H  HZ2  . LYS A 1 168 ? 0.495  9.940  6.244   1.00 31.57 ? 170 LYS A HZ2  1 
ATOM   2684 H  HZ3  . LYS A 1 168 ? 1.425  9.981  5.133   1.00 31.57 ? 170 LYS A HZ3  1 
ATOM   2685 N  N    . CYS A 1 169 ? 7.979  9.384  8.039   1.00 16.28 ? 171 CYS A N    1 
ATOM   2686 C  CA   . CYS A 1 169 ? 9.098  9.838  8.849   1.00 16.29 ? 171 CYS A CA   1 
ATOM   2687 C  C    . CYS A 1 169 ? 9.499  11.254 8.425   1.00 14.43 ? 171 CYS A C    1 
ATOM   2688 O  O    . CYS A 1 169 ? 9.545  11.618 7.220   1.00 14.18 ? 171 CYS A O    1 
ATOM   2689 C  CB   . CYS A 1 169 ? 10.286 8.929  8.642   1.00 16.86 ? 171 CYS A CB   1 
ATOM   2690 S  SG   . CYS A 1 169 ? 10.038 7.286  9.301   1.00 20.44 ? 171 CYS A SG   1 
ATOM   2691 H  H    . CYS A 1 169 ? 8.201  9.124  7.249   1.00 13.94 ? 171 CYS A H    1 
ATOM   2692 H  HA   . CYS A 1 169 ? 8.855  9.840  9.789   1.00 14.40 ? 171 CYS A HA   1 
ATOM   2693 H  HB2  . CYS A 1 169 ? 10.457 8.847  7.691   1.00 15.19 ? 171 CYS A HB2  1 
ATOM   2694 H  HB3  . CYS A 1 169 ? 11.058 9.315  9.085   1.00 15.19 ? 171 CYS A HB3  1 
ATOM   2695 H  HG   . CYS A 1 169 ? 11.022 6.631  9.096   1.00 17.87 ? 171 CYS A HG   1 
ATOM   2696 N  N    . LEU A 1 170 ? 9.826  12.060 9.415   1.00 13.16 ? 172 LEU A N    1 
ATOM   2697 C  CA   . LEU A 1 170 ? 10.326 13.424 9.205   1.00 12.05 ? 172 LEU A CA   1 
ATOM   2698 C  C    . LEU A 1 170 ? 11.706 13.561 9.752   1.00 9.77  ? 172 LEU A C    1 
ATOM   2699 O  O    . LEU A 1 170 ? 11.892 13.362 10.965  1.00 11.40 ? 172 LEU A O    1 
ATOM   2700 C  CB   . LEU A 1 170 ? 9.375  14.422 9.880   1.00 12.81 ? 172 LEU A CB   1 
ATOM   2701 C  CG   . LEU A 1 170 ? 9.697  15.891 9.753   1.00 12.83 ? 172 LEU A CG   1 
ATOM   2702 C  CD1  . LEU A 1 170 ? 9.670  16.270 8.291   1.00 12.59 ? 172 LEU A CD1  1 
ATOM   2703 C  CD2  . LEU A 1 170 ? 8.825  16.755 10.589  1.00 15.75 ? 172 LEU A CD2  1 
ATOM   2704 H  H    . LEU A 1 170 ? 9.769  11.842 10.245  1.00 11.66 ? 172 LEU A H    1 
ATOM   2705 H  HA   . LEU A 1 170 ? 10.351 13.617 8.255   1.00 11.12 ? 172 LEU A HA   1 
ATOM   2706 H  HB2  . LEU A 1 170 ? 8.490  14.292 9.505   1.00 11.51 ? 172 LEU A HB2  1 
ATOM   2707 H  HB3  . LEU A 1 170 ? 9.351  14.218 10.828  1.00 11.51 ? 172 LEU A HB3  1 
ATOM   2708 H  HG   . LEU A 1 170 ? 10.606 16.025 10.063  1.00 11.92 ? 172 LEU A HG   1 
ATOM   2709 H  HD11 . LEU A 1 170 ? 9.876  17.214 8.207   1.00 12.05 ? 172 LEU A HD11 1 
ATOM   2710 H  HD12 . LEU A 1 170 ? 10.331 15.743 7.817   1.00 12.05 ? 172 LEU A HD12 1 
ATOM   2711 H  HD13 . LEU A 1 170 ? 8.786  16.091 7.935   1.00 12.05 ? 172 LEU A HD13 1 
ATOM   2712 H  HD21 . LEU A 1 170 ? 9.083  17.681 10.462  1.00 14.34 ? 172 LEU A HD21 1 
ATOM   2713 H  HD22 . LEU A 1 170 ? 7.902  16.628 10.318  1.00 14.34 ? 172 LEU A HD22 1 
ATOM   2714 H  HD23 . LEU A 1 170 ? 8.933  16.506 11.521  1.00 14.34 ? 172 LEU A HD23 1 
ATOM   2715 N  N    . VAL A 1 171 ? 12.653 13.942 8.914   1.00 10.13 ? 173 VAL A N    1 
ATOM   2716 C  CA   . VAL A 1 171 ? 14.036 14.200 9.309   1.00 8.21  ? 173 VAL A CA   1 
ATOM   2717 C  C    . VAL A 1 171 ? 14.213 15.673 9.607   1.00 7.69  ? 173 VAL A C    1 
ATOM   2718 O  O    . VAL A 1 171 ? 13.674 16.541 8.931   1.00 9.74  ? 173 VAL A O    1 
ATOM   2719 C  CB   . VAL A 1 171 ? 14.957 13.741 8.179   1.00 8.91  ? 173 VAL A CB   1 
ATOM   2720 C  CG1  . VAL A 1 171 ? 16.392 14.147 8.396   1.00 9.28  ? 173 VAL A CG1  1 
ATOM   2721 C  CG2  . VAL A 1 171 ? 14.854 12.267 7.951   1.00 10.31 ? 173 VAL A CG2  1 
ATOM   2722 H  H    . VAL A 1 171 ? 12.517 14.064 8.074   1.00 9.46  ? 173 VAL A H    1 
ATOM   2723 H  HA   . VAL A 1 171 ? 14.248 13.693 10.109  1.00 7.93  ? 173 VAL A HA   1 
ATOM   2724 H  HB   . VAL A 1 171 ? 14.663 14.173 7.362   1.00 8.99  ? 173 VAL A HB   1 
ATOM   2725 H  HG11 . VAL A 1 171 ? 16.925 13.830 7.651   1.00 9.72  ? 173 VAL A HG11 1 
ATOM   2726 H  HG12 . VAL A 1 171 ? 16.441 15.114 8.451   1.00 9.72  ? 173 VAL A HG12 1 
ATOM   2727 H  HG13 . VAL A 1 171 ? 16.710 13.752 9.223   1.00 9.72  ? 173 VAL A HG13 1 
ATOM   2728 H  HG21 . VAL A 1 171 ? 15.452 12.018 7.229   1.00 10.07 ? 173 VAL A HG21 1 
ATOM   2729 H  HG22 . VAL A 1 171 ? 15.107 11.804 8.765   1.00 10.07 ? 173 VAL A HG22 1 
ATOM   2730 H  HG23 . VAL A 1 171 ? 13.939 12.048 7.715   1.00 10.07 ? 173 VAL A HG23 1 
ATOM   2731 N  N    . PHE A 1 172 ? 15.045 15.964 10.607  1.00 9.33  ? 174 PHE A N    1 
ATOM   2732 C  CA   . PHE A 1 172 ? 15.547 17.300 10.885  1.00 8.04  ? 174 PHE A CA   1 
ATOM   2733 C  C    . PHE A 1 172 ? 17.075 17.315 10.645  1.00 6.74  ? 174 PHE A C    1 
ATOM   2734 O  O    . PHE A 1 172 ? 17.796 16.509 11.202  1.00 8.95  ? 174 PHE A O    1 
ATOM   2735 C  CB   . PHE A 1 172 ? 15.290 17.710 12.337  1.00 8.54  ? 174 PHE A CB   1 
ATOM   2736 C  CG   . PHE A 1 172 ? 13.859 17.974 12.598  1.00 11.18 ? 174 PHE A CG   1 
ATOM   2737 C  CD1  . PHE A 1 172 ? 12.984 16.936 12.688  1.00 12.20 ? 174 PHE A CD1  1 
ATOM   2738 C  CD2  . PHE A 1 172 ? 13.376 19.255 12.715  1.00 13.26 ? 174 PHE A CD2  1 
ATOM   2739 C  CE1  . PHE A 1 172 ? 11.641 17.121 12.932  1.00 15.91 ? 174 PHE A CE1  1 
ATOM   2740 C  CE2  . PHE A 1 172 ? 11.981 19.445 12.964  1.00 16.81 ? 174 PHE A CE2  1 
ATOM   2741 C  CZ   . PHE A 1 172 ? 11.152 18.396 13.030  1.00 16.63 ? 174 PHE A CZ   1 
ATOM   2742 H  H    . PHE A 1 172 ? 15.341 15.375 11.159  1.00 9.07  ? 174 PHE A H    1 
ATOM   2743 H  HA   . PHE A 1 172 ? 15.127 17.944 10.294  1.00 7.99  ? 174 PHE A HA   1 
ATOM   2744 H  HB2  . PHE A 1 172 ? 15.577 16.993 12.925  1.00 8.13  ? 174 PHE A HB2  1 
ATOM   2745 H  HB3  . PHE A 1 172 ? 15.787 18.520 12.532  1.00 8.13  ? 174 PHE A HB3  1 
ATOM   2746 H  HD1  . PHE A 1 172 ? 13.309 16.069 12.605  1.00 10.92 ? 174 PHE A HD1  1 
ATOM   2747 H  HD2  . PHE A 1 172 ? 13.950 19.985 12.653  1.00 12.24 ? 174 PHE A HD2  1 
ATOM   2748 H  HE1  . PHE A 1 172 ? 11.067 16.391 12.985  1.00 14.08 ? 174 PHE A HE1  1 
ATOM   2749 H  HE2  . PHE A 1 172 ? 11.641 20.306 13.043  1.00 15.22 ? 174 PHE A HE2  1 
ATOM   2750 H  HZ   . PHE A 1 172 ? 10.248 18.532 13.202  1.00 14.66 ? 174 PHE A HZ   1 
ATOM   2751 N  N    . GLU A 1 173 ? 17.541 18.250 9.827   1.00 7.11  ? 175 GLU A N    1 
ATOM   2752 C  CA   . GLU A 1 173 ? 18.925 18.320 9.358   1.00 7.29  ? 175 GLU A CA   1 
ATOM   2753 C  C    . GLU A 1 173 ? 19.404 19.747 9.262   1.00 6.52  ? 175 GLU A C    1 
ATOM   2754 O  O    . GLU A 1 173 ? 18.653 20.660 8.961   1.00 8.52  ? 175 GLU A O    1 
ATOM   2755 C  CB   . GLU A 1 173 ? 19.028 17.656 7.993   1.00 7.59  ? 175 GLU A CB   1 
ATOM   2756 C  CG   . GLU A 1 173 ? 19.495 16.229 8.089   1.00 6.48  ? 175 GLU A CG   1 
ATOM   2757 C  CD   . GLU A 1 173 ? 20.989 16.136 8.435   1.00 6.27  ? 175 GLU A CD   1 
ATOM   2758 O  OE1  . GLU A 1 173 ? 21.443 14.980 8.629   1.00 9.59  ? 175 GLU A OE1  1 
ATOM   2759 O  OE2  . GLU A 1 173 ? 21.667 17.158 8.487   1.00 7.73  ? 175 GLU A OE2  1 
ATOM   2760 H  H    . GLU A 1 173 ? 17.052 18.885 9.515   1.00 7.45  ? 175 GLU A H    1 
ATOM   2761 H  HA   . GLU A 1 173 ? 19.500 17.843 9.977   1.00 7.92  ? 175 GLU A HA   1 
ATOM   2762 H  HB2  . GLU A 1 173 ? 18.155 17.660 7.571   1.00 8.36  ? 175 GLU A HB2  1 
ATOM   2763 H  HB3  . GLU A 1 173 ? 19.665 18.145 7.449   1.00 8.36  ? 175 GLU A HB3  1 
ATOM   2764 H  HG2  . GLU A 1 173 ? 18.994 15.777 8.786   1.00 7.17  ? 175 GLU A HG2  1 
ATOM   2765 H  HG3  . GLU A 1 173 ? 19.354 15.790 7.236   1.00 7.17  ? 175 GLU A HG3  1 
ATOM   2766 N  N    . ASP A 1 174 ? 20.684 19.954 9.479   1.00 6.07  ? 176 ASP A N    1 
ATOM   2767 C  CA   . ASP A 1 174 ? 21.312 21.239 9.191   1.00 7.04  ? 176 ASP A CA   1 
ATOM   2768 C  C    . ASP A 1 174 ? 22.122 21.212 7.898   1.00 7.44  ? 176 ASP A C    1 
ATOM   2769 O  O    . ASP A 1 174 ? 22.483 22.282 7.416   1.00 8.81  ? 176 ASP A O    1 
ATOM   2770 C  CB   . ASP A 1 174 ? 22.246 21.688 10.297  1.00 7.43  ? 176 ASP A CB   1 
ATOM   2771 C  CG   . ASP A 1 174 ? 23.478 20.815 10.437  1.00 8.43  ? 176 ASP A CG   1 
ATOM   2772 O  OD1  . ASP A 1 174 ? 23.325 19.578 10.442  1.00 9.53  ? 176 ASP A OD1  1 
ATOM   2773 O  OD2  . ASP A 1 174 ? 24.641 21.328 10.505  1.00 9.45  ? 176 ASP A OD2  1 
ATOM   2774 H  H    . ASP A 1 174 ? 21.224 19.364 9.795   1.00 6.92  ? 176 ASP A H    1 
ATOM   2775 H  HA   . ASP A 1 174 ? 20.619 21.911 9.094   1.00 7.91  ? 176 ASP A HA   1 
ATOM   2776 H  HB2  . ASP A 1 174 ? 22.542 22.593 10.111  1.00 8.20  ? 176 ASP A HB2  1 
ATOM   2777 H  HB3  . ASP A 1 174 ? 21.767 21.664 11.141  1.00 8.20  ? 176 ASP A HB3  1 
ATOM   2778 N  N    . ALA A 1 175 ? 22.399 20.038 7.332   1.00 7.70  ? 177 ALA A N    1 
ATOM   2779 C  CA   . ALA A 1 175 ? 23.416 19.905 6.268   1.00 8.13  ? 177 ALA A CA   1 
ATOM   2780 C  C    . ALA A 1 175 ? 22.734 19.509 4.951   1.00 6.55  ? 177 ALA A C    1 
ATOM   2781 O  O    . ALA A 1 175 ? 21.856 18.640 4.930   1.00 5.91  ? 177 ALA A O    1 
ATOM   2782 C  CB   . ALA A 1 175 ? 24.356 18.842 6.659   1.00 9.41  ? 177 ALA A CB   1 
ATOM   2783 H  H    . ALA A 1 175 ? 22.015 19.297 7.541   1.00 8.34  ? 177 ALA A H    1 
ATOM   2784 H  HA   . ALA A 1 175 ? 23.897 20.739 6.149   1.00 8.80  ? 177 ALA A HA   1 
ATOM   2785 H  HB1  . ALA A 1 175 ? 25.029 18.747 5.966   1.00 10.02 ? 177 ALA A HB1  1 
ATOM   2786 H  HB2  . ALA A 1 175 ? 24.777 19.086 7.498   1.00 10.02 ? 177 ALA A HB2  1 
ATOM   2787 H  HB3  . ALA A 1 175 ? 23.867 18.011 6.762   1.00 10.02 ? 177 ALA A HB3  1 
ATOM   2788 N  N    . PRO A 1 176 ? 23.312 19.960 3.829   1.00 7.03  ? 178 PRO A N    1 
ATOM   2789 C  CA   . PRO A 1 176 ? 22.778 19.559 2.533   1.00 6.42  ? 178 PRO A CA   1 
ATOM   2790 C  C    . PRO A 1 176 ? 22.880 18.060 2.316   1.00 7.95  ? 178 PRO A C    1 
ATOM   2791 O  O    . PRO A 1 176 ? 22.005 17.470 1.731   1.00 7.03  ? 178 PRO A O    1 
ATOM   2792 C  CB   . PRO A 1 176 ? 23.706 20.353 1.577   1.00 9.15  ? 178 PRO A CB   1 
ATOM   2793 C  CG   . PRO A 1 176 ? 24.320 21.457 2.397   1.00 12.06 ? 178 PRO A CG   1 
ATOM   2794 C  CD   . PRO A 1 176 ? 24.339 21.034 3.760   1.00 6.79  ? 178 PRO A CD   1 
ATOM   2795 H  HA   . PRO A 1 176 ? 21.859 19.853 2.427   1.00 7.31  ? 178 PRO A HA   1 
ATOM   2796 H  HB2  . PRO A 1 176 ? 24.395 19.764 1.233   1.00 9.89  ? 178 PRO A HB2  1 
ATOM   2797 H  HB3  . PRO A 1 176 ? 23.181 20.723 0.850   1.00 9.89  ? 178 PRO A HB3  1 
ATOM   2798 H  HG2  . PRO A 1 176 ? 25.224 21.621 2.085   1.00 12.72 ? 178 PRO A HG2  1 
ATOM   2799 H  HG3  . PRO A 1 176 ? 23.783 22.260 2.303   1.00 12.72 ? 178 PRO A HG3  1 
ATOM   2800 H  HD2  . PRO A 1 176 ? 25.212 20.679 3.988   1.00 7.54  ? 178 PRO A HD2  1 
ATOM   2801 H  HD3  . PRO A 1 176 ? 24.094 21.770 4.343   1.00 7.54  ? 178 PRO A HD3  1 
ATOM   2802 N  N    . ASN A 1 177 ? 24.017 17.478 2.708   1.00 7.00  ? 179 ASN A N    1 
ATOM   2803 C  CA   . ASN A 1 177 ? 24.139 16.040 2.506   1.00 6.80  ? 179 ASN A CA   1 
ATOM   2804 C  C    . ASN A 1 177 ? 23.029 15.311 3.263   1.00 8.18  ? 179 ASN A C    1 
ATOM   2805 O  O    . ASN A 1 177 ? 22.550 14.269 2.790   1.00 7.54  ? 179 ASN A O    1 
ATOM   2806 C  CB   . ASN A 1 177 ? 25.475 15.538 3.023   1.00 8.94  ? 179 ASN A CB   1 
ATOM   2807 C  CG   . ASN A 1 177 ? 26.643 15.855 2.158   1.00 10.94 ? 179 ASN A CG   1 
ATOM   2808 O  OD1  . ASN A 1 177 ? 26.506 16.041 0.996   1.00 10.77 ? 179 ASN A OD1  1 
ATOM   2809 N  ND2  . ASN A 1 177 ? 27.828 15.898 2.753   1.00 11.01 ? 179 ASN A ND2  1 
ATOM   2810 H  H    . ASN A 1 177 ? 24.691 17.868 3.073   1.00 8.04  ? 179 ASN A H    1 
ATOM   2811 H  HA   . ASN A 1 177 ? 24.068 15.831 1.561   1.00 7.70  ? 179 ASN A HA   1 
ATOM   2812 H  HB2  . ASN A 1 177 ? 25.639 15.935 3.892   1.00 9.65  ? 179 ASN A HB2  1 
ATOM   2813 H  HB3  . ASN A 1 177 ? 25.429 14.573 3.110   1.00 9.65  ? 179 ASN A HB3  1 
ATOM   2814 H  HD21 . ASN A 1 177 ? 28.533 16.078 2.294   1.00 11.33 ? 179 ASN A HD21 1 
ATOM   2815 H  HD22 . ASN A 1 177 ? 27.892 15.747 3.597   1.00 11.33 ? 179 ASN A HD22 1 
ATOM   2816 N  N    . GLY A 1 178 ? 22.641 15.813 4.428   1.00 7.11  ? 180 GLY A N    1 
ATOM   2817 C  CA   . GLY A 1 178 ? 21.590 15.221 5.167   1.00 7.55  ? 180 GLY A CA   1 
ATOM   2818 C  C    . GLY A 1 178 ? 20.222 15.410 4.568   1.00 7.05  ? 180 GLY A C    1 
ATOM   2819 O  O    . GLY A 1 178 ? 19.408 14.486 4.558   1.00 6.90  ? 180 GLY A O    1 
ATOM   2820 H  H    . GLY A 1 178 ? 22.987 16.506 4.800   1.00 7.80  ? 180 GLY A H    1 
ATOM   2821 H  HA2  . GLY A 1 178 ? 21.755 14.268 5.243   1.00 8.16  ? 180 GLY A HA2  1 
ATOM   2822 H  HA3  . GLY A 1 178 ? 21.580 15.597 6.061   1.00 8.16  ? 180 GLY A HA3  1 
ATOM   2823 N  N    . VAL A 1 179 ? 19.933 16.558 3.978   1.00 5.67  ? 181 VAL A N    1 
ATOM   2824 C  CA   . VAL A 1 179 ? 18.660 16.769 3.269   1.00 6.55  ? 181 VAL A CA   1 
ATOM   2825 C  C    . VAL A 1 179 ? 18.609 15.764 2.119   1.00 5.95  ? 181 VAL A C    1 
ATOM   2826 O  O    . VAL A 1 179 ? 17.577 15.151 1.907   1.00 7.84  ? 181 VAL A O    1 
ATOM   2827 C  CB   . VAL A 1 179 ? 18.566 18.227 2.712   1.00 7.17  ? 181 VAL A CB   1 
ATOM   2828 C  CG1  . VAL A 1 179 ? 17.475 18.388 1.726   1.00 8.31  ? 181 VAL A CG1  1 
ATOM   2829 C  CG2  . VAL A 1 179 ? 18.429 19.179 3.895   1.00 7.76  ? 181 VAL A CG2  1 
ATOM   2830 H  H    . VAL A 1 179 ? 20.454 17.241 3.969   1.00 6.70  ? 181 VAL A H    1 
ATOM   2831 H  HA   . VAL A 1 179 ? 17.913 16.608 3.866   1.00 7.54  ? 181 VAL A HA   1 
ATOM   2832 H  HB   . VAL A 1 179 ? 19.399 18.438 2.262   1.00 8.24  ? 181 VAL A HB   1 
ATOM   2833 H  HG11 . VAL A 1 179 ? 17.464 19.307 1.416   1.00 9.30  ? 181 VAL A HG11 1 
ATOM   2834 H  HG12 . VAL A 1 179 ? 17.634 17.789 0.980   1.00 9.30  ? 181 VAL A HG12 1 
ATOM   2835 H  HG13 . VAL A 1 179 ? 16.631 18.172 2.151   1.00 9.30  ? 181 VAL A HG13 1 
ATOM   2836 H  HG21 . VAL A 1 179 ? 18.370 20.088 3.563   1.00 8.81  ? 181 VAL A HG21 1 
ATOM   2837 H  HG22 . VAL A 1 179 ? 17.626 18.954 4.390   1.00 8.81  ? 181 VAL A HG22 1 
ATOM   2838 H  HG23 . VAL A 1 179 ? 19.207 19.085 4.467   1.00 8.81  ? 181 VAL A HG23 1 
ATOM   2839 N  N    . GLU A 1 180 ? 19.703 15.614 1.371   1.00 7.12  ? 182 GLU A N    1 
ATOM   2840 C  CA   . GLU A 1 180 ? 19.705 14.697 0.233   1.00 8.41  ? 182 GLU A CA   1 
ATOM   2841 C  C    . GLU A 1 180 ? 19.488 13.245 0.675   1.00 8.86  ? 182 GLU A C    1 
ATOM   2842 O  O    . GLU A 1 180 ? 18.773 12.484 0.015   1.00 8.59  ? 182 GLU A O    1 
ATOM   2843 C  CB   . GLU A 1 180 ? 20.978 14.850 -0.602  1.00 9.59  ? 182 GLU A CB   1 
ATOM   2844 C  CG   . GLU A 1 180 ? 21.064 16.192 -1.378  1.00 11.04 ? 182 GLU A CG   1 
ATOM   2845 C  CD   . GLU A 1 180 ? 19.970 16.434 -2.400  1.00 13.85 ? 182 GLU A CD   1 
ATOM   2846 O  OE1  . GLU A 1 180 ? 19.240 15.519 -2.844  1.00 12.63 ? 182 GLU A OE1  1 
ATOM   2847 O  OE2  . GLU A 1 180 ? 19.823 17.637 -2.733  1.00 19.52 ? 182 GLU A OE2  1 
ATOM   2848 H  H    . GLU A 1 180 ? 20.447 16.026 1.499   1.00 8.14  ? 182 GLU A H    1 
ATOM   2849 H  HA   . GLU A 1 180 ? 18.959 14.933 -0.342  1.00 9.28  ? 182 GLU A HA   1 
ATOM   2850 H  HB2  . GLU A 1 180 ? 21.746 14.798 -0.012  1.00 10.42 ? 182 GLU A HB2  1 
ATOM   2851 H  HB3  . GLU A 1 180 ? 21.013 14.129 -1.251  1.00 10.42 ? 182 GLU A HB3  1 
ATOM   2852 H  HG2  . GLU A 1 180 ? 21.028 16.918 -0.737  1.00 11.96 ? 182 GLU A HG2  1 
ATOM   2853 H  HG3  . GLU A 1 180 ? 21.912 16.218 -1.849  1.00 11.96 ? 182 GLU A HG3  1 
ATOM   2854 N  N    . ALA A 1 181 ? 20.071 12.859 1.806   1.00 7.44  ? 183 ALA A N    1 
ATOM   2855 C  CA   . ALA A 1 181 ? 19.879 11.517 2.314   1.00 8.84  ? 183 ALA A CA   1 
ATOM   2856 C  C    . ALA A 1 181 ? 18.473 11.253 2.723   1.00 7.51  ? 183 ALA A C    1 
ATOM   2857 O  O    . ALA A 1 181 ? 17.905 10.204 2.445   1.00 9.24  ? 183 ALA A O    1 
ATOM   2858 C  CB   . ALA A 1 181 ? 20.808 11.257 3.513   1.00 9.22  ? 183 ALA A CB   1 
ATOM   2859 H  H    . ALA A 1 181 ? 20.579 13.356 2.292   1.00 8.07  ? 183 ALA A H    1 
ATOM   2860 H  HA   . ALA A 1 181 ? 20.109 10.884 1.616   1.00 9.15  ? 183 ALA A HA   1 
ATOM   2861 H  HB1  . ALA A 1 181 ? 20.662 10.354 3.835   1.00 9.46  ? 183 ALA A HB1  1 
ATOM   2862 H  HB2  . ALA A 1 181 ? 21.729 11.361 3.227   1.00 9.46  ? 183 ALA A HB2  1 
ATOM   2863 H  HB3  . ALA A 1 181 ? 20.605 11.896 4.214   1.00 9.46  ? 183 ALA A HB3  1 
ATOM   2864 N  N    . ALA A 1 182 ? 17.843 12.236 3.315   1.00 7.66  ? 184 ALA A N    1 
ATOM   2865 C  CA   . ALA A 1 182 ? 16.407 12.137 3.679   1.00 8.19  ? 184 ALA A CA   1 
ATOM   2866 C  C    . ALA A 1 182 ? 15.534 12.018 2.423   1.00 8.31  ? 184 ALA A C    1 
ATOM   2867 O  O    . ALA A 1 182 ? 14.686 11.103 2.369   1.00 11.11 ? 184 ALA A O    1 
ATOM   2868 C  CB   . ALA A 1 182 ? 15.962 13.344 4.505   1.00 8.24  ? 184 ALA A CB   1 
ATOM   2869 H  H    . ALA A 1 182 ? 18.207 12.986 3.528   1.00 7.93  ? 184 ALA A H    1 
ATOM   2870 H  HA   . ALA A 1 182 ? 16.272 11.340 4.216   1.00 8.24  ? 184 ALA A HA   1 
ATOM   2871 H  HB1  . ALA A 1 182 ? 15.022 13.246 4.725   1.00 8.42  ? 184 ALA A HB1  1 
ATOM   2872 H  HB2  . ALA A 1 182 ? 16.490 13.382 5.318   1.00 8.42  ? 184 ALA A HB2  1 
ATOM   2873 H  HB3  . ALA A 1 182 ? 16.098 14.150 3.984   1.00 8.42  ? 184 ALA A HB3  1 
ATOM   2874 N  N    . LEU A 1 183 ? 15.752 12.830 1.410   1.00 7.85  ? 185 LEU A N    1 
ATOM   2875 C  CA   . LEU A 1 183 ? 14.978 12.708 0.181   1.00 9.52  ? 185 LEU A CA   1 
ATOM   2876 C  C    . LEU A 1 183 ? 15.233 11.363 -0.474  1.00 10.89 ? 185 LEU A C    1 
ATOM   2877 O  O    . LEU A 1 183 ? 14.304 10.725 -0.992  1.00 13.11 ? 185 LEU A O    1 
ATOM   2878 C  CB   . LEU A 1 183 ? 15.322 13.843 -0.754  1.00 9.66  ? 185 LEU A CB   1 
ATOM   2879 C  CG   . LEU A 1 183 ? 14.983 15.281 -0.257  1.00 9.37  ? 185 LEU A CG   1 
ATOM   2880 C  CD1  . LEU A 1 183 ? 15.428 16.328 -1.258  1.00 12.09 ? 185 LEU A CD1  1 
ATOM   2881 C  CD2  . LEU A 1 183 ? 13.505 15.426 0.023   1.00 11.95 ? 185 LEU A CD2  1 
ATOM   2882 H  H    . LEU A 1 183 ? 16.338 13.459 1.402   1.00 8.39  ? 185 LEU A H    1 
ATOM   2883 H  HA   . LEU A 1 183 ? 14.033 12.767 0.393   1.00 9.94  ? 185 LEU A HA   1 
ATOM   2884 H  HB2  . LEU A 1 183 ? 16.276 13.815 -0.926  1.00 10.35 ? 185 LEU A HB2  1 
ATOM   2885 H  HB3  . LEU A 1 183 ? 14.842 13.706 -1.586  1.00 10.35 ? 185 LEU A HB3  1 
ATOM   2886 H  HG   . LEU A 1 183 ? 15.459 15.444 0.572   1.00 10.23 ? 185 LEU A HG   1 
ATOM   2887 H  HD11 . LEU A 1 183 ? 15.202 17.207 -0.917  1.00 13.12 ? 185 LEU A HD11 1 
ATOM   2888 H  HD12 . LEU A 1 183 ? 16.387 16.258 -1.383  1.00 13.12 ? 185 LEU A HD12 1 
ATOM   2889 H  HD13 . LEU A 1 183 ? 14.973 16.173 -2.101  1.00 13.12 ? 185 LEU A HD13 1 
ATOM   2890 H  HD21 . LEU A 1 183 ? 13.329 16.329 0.330   1.00 12.57 ? 185 LEU A HD21 1 
ATOM   2891 H  HD22 . LEU A 1 183 ? 13.010 15.250 -0.792  1.00 12.57 ? 185 LEU A HD22 1 
ATOM   2892 H  HD23 . LEU A 1 183 ? 13.250 14.788 0.709   1.00 12.57 ? 185 LEU A HD23 1 
ATOM   2893 N  N    . ALA A 1 184 ? 16.466 10.922 -0.481  1.00 8.87  ? 186 ALA A N    1 
ATOM   2894 C  CA   . ALA A 1 184 ? 16.764 9.616  -1.072  1.00 12.15 ? 186 ALA A CA   1 
ATOM   2895 C  C    . ALA A 1 184 ? 16.125 8.460  -0.327  1.00 13.32 ? 186 ALA A C    1 
ATOM   2896 O  O    . ALA A 1 184 ? 15.906 7.410  -0.912  1.00 16.30 ? 186 ALA A O    1 
ATOM   2897 C  CB   . ALA A 1 184 ? 18.258 9.404  -1.141  1.00 11.22 ? 186 ALA A CB   1 
ATOM   2898 H  H    . ALA A 1 184 ? 17.146 11.340 -0.160  1.00 9.15  ? 186 ALA A H    1 
ATOM   2899 H  HA   . ALA A 1 184 ? 16.423 9.603  -1.980  1.00 12.06 ? 186 ALA A HA   1 
ATOM   2900 H  HB1  . ALA A 1 184 ? 18.436 8.535  -1.534  1.00 11.15 ? 186 ALA A HB1  1 
ATOM   2901 H  HB2  . ALA A 1 184 ? 18.651 10.102 -1.688  1.00 11.15 ? 186 ALA A HB2  1 
ATOM   2902 H  HB3  . ALA A 1 184 ? 18.624 9.442  -0.243  1.00 11.15 ? 186 ALA A HB3  1 
ATOM   2903 N  N    . ALA A 1 185 ? 15.889 8.649  0.958   1.00 10.81 ? 187 ALA A N    1 
ATOM   2904 C  CA   . ALA A 1 185 ? 15.211 7.673  1.785   1.00 12.51 ? 187 ALA A CA   1 
ATOM   2905 C  C    . ALA A 1 185 ? 13.692 7.733  1.611   1.00 15.06 ? 187 ALA A C    1 
ATOM   2906 O  O    . ALA A 1 185 ? 12.978 6.892  2.187   1.00 19.00 ? 187 ALA A O    1 
ATOM   2907 C  CB   . ALA A 1 185 ? 15.551 7.851  3.259   1.00 12.24 ? 187 ALA A CB   1 
ATOM   2908 H  H    . ALA A 1 185 ? 16.120 9.358  1.386   1.00 10.68 ? 187 ALA A H    1 
ATOM   2909 H  HA   . ALA A 1 185 ? 15.502 6.786  1.520   1.00 11.88 ? 187 ALA A HA   1 
ATOM   2910 H  HB1  . ALA A 1 185 ? 15.078 7.180  3.775   1.00 11.64 ? 187 ALA A HB1  1 
ATOM   2911 H  HB2  . ALA A 1 185 ? 16.508 7.746  3.377   1.00 11.64 ? 187 ALA A HB2  1 
ATOM   2912 H  HB3  . ALA A 1 185 ? 15.279 8.738  3.540   1.00 11.64 ? 187 ALA A HB3  1 
ATOM   2913 N  N    . GLY A 1 186 ? 13.197 8.707  0.873   1.00 12.74 ? 188 GLY A N    1 
ATOM   2914 C  CA   . GLY A 1 186 ? 11.763 8.906  0.683   1.00 14.55 ? 188 GLY A CA   1 
ATOM   2915 C  C    . GLY A 1 186 ? 11.030 9.579  1.820   1.00 13.38 ? 188 GLY A C    1 
ATOM   2916 O  O    . GLY A 1 186 ? 9.805  9.431  1.991   1.00 15.89 ? 188 GLY A O    1 
ATOM   2917 H  H    . GLY A 1 186 ? 13.681 9.284  0.457   1.00 12.22 ? 188 GLY A H    1 
ATOM   2918 H  HA2  . GLY A 1 186 ? 11.628 9.443  -0.114  1.00 13.77 ? 188 GLY A HA2  1 
ATOM   2919 H  HA3  . GLY A 1 186 ? 11.347 8.043  0.533   1.00 13.77 ? 188 GLY A HA3  1 
ATOM   2920 N  N    . MET A 1 187 ? 11.787 10.374 2.594   1.00 12.25 ? 189 MET A N    1 
ATOM   2921 C  CA   . MET A 1 187 ? 11.288 11.011 3.798   1.00 12.32 ? 189 MET A CA   1 
ATOM   2922 C  C    . MET A 1 187 ? 11.135 12.506 3.594   1.00 10.47 ? 189 MET A C    1 
ATOM   2923 O  O    . MET A 1 187 ? 11.856 13.106 2.779   1.00 13.32 ? 189 MET A O    1 
ATOM   2924 C  CB   . MET A 1 187 ? 12.218 10.762 4.978   1.00 10.79 ? 189 MET A CB   1 
ATOM   2925 C  CG   . MET A 1 187 ? 12.447 9.306  5.284   1.00 11.77 ? 189 MET A CG   1 
ATOM   2926 S  SD   . MET A 1 187 ? 13.652 9.072  6.622   1.00 13.36 ? 189 MET A SD   1 
ATOM   2927 C  CE   . MET A 1 187 ? 13.447 7.333  6.787   1.00 15.61 ? 189 MET A CE   1 
ATOM   2928 H  H    . MET A 1 187 ? 12.610 10.557 2.427   1.00 11.72 ? 189 MET A H    1 
ATOM   2929 H  HA   . MET A 1 187 ? 10.422 10.634 4.017   1.00 11.70 ? 189 MET A HA   1 
ATOM   2930 H  HB2  . MET A 1 187 ? 13.080 11.163 4.785   1.00 10.22 ? 189 MET A HB2  1 
ATOM   2931 H  HB3  . MET A 1 187 ? 11.835 11.173 5.768   1.00 10.22 ? 189 MET A HB3  1 
ATOM   2932 H  HG2  . MET A 1 187 ? 11.608 8.903  5.558   1.00 10.76 ? 189 MET A HG2  1 
ATOM   2933 H  HG3  . MET A 1 187 ? 12.787 8.864  4.490   1.00 10.76 ? 189 MET A HG3  1 
ATOM   2934 H  HE1  . MET A 1 187 ? 14.037 7.012  7.488   1.00 13.90 ? 189 MET A HE1  1 
ATOM   2935 H  HE2  . MET A 1 187 ? 12.524 7.145  7.019   1.00 13.90 ? 189 MET A HE2  1 
ATOM   2936 H  HE3  . MET A 1 187 ? 13.671 6.908  5.945   1.00 13.90 ? 189 MET A HE3  1 
ATOM   2937 N  N    . GLN A 1 188 ? 10.223 13.156 4.299   1.00 11.83 ? 190 GLN A N    1 
ATOM   2938 C  CA   . GLN A 1 188 ? 10.232 14.613 4.310   1.00 12.20 ? 190 GLN A CA   1 
ATOM   2939 C  C    . GLN A 1 188 ? 11.390 15.087 5.244   1.00 9.51  ? 190 GLN A C    1 
ATOM   2940 O  O    . GLN A 1 188 ? 11.851 14.340 6.100   1.00 9.17  ? 190 GLN A O    1 
ATOM   2941 C  CB   . GLN A 1 188 ? 8.907  15.216 4.758   1.00 13.39 ? 190 GLN A CB   1 
ATOM   2942 C  CG   . GLN A 1 188 ? 7.700  14.901 3.834   1.00 15.00 ? 190 GLN A CG   1 
ATOM   2943 C  CD   . GLN A 1 188 ? 6.410  15.369 4.446   1.00 16.11 ? 190 GLN A CD   1 
ATOM   2944 O  OE1  . GLN A 1 188 ? 5.888  16.410 4.074   1.00 18.50 ? 190 GLN A OE1  1 
ATOM   2945 N  NE2  . GLN A 1 188 ? 5.980  14.674 5.422   1.00 17.83 ? 190 GLN A NE2  1 
ATOM   2946 H  H    . GLN A 1 188 ? 9.603  12.791 4.769   1.00 11.00 ? 190 GLN A H    1 
ATOM   2947 H  HA   . GLN A 1 188 ? 10.419 14.934 3.414   1.00 11.64 ? 190 GLN A HA   1 
ATOM   2948 H  HB2  . GLN A 1 188 ? 8.696  14.876 5.641   1.00 12.36 ? 190 GLN A HB2  1 
ATOM   2949 H  HB3  . GLN A 1 188 ? 9.003  16.180 4.795   1.00 12.36 ? 190 GLN A HB3  1 
ATOM   2950 H  HG2  . GLN A 1 188 ? 7.817  15.357 2.986   1.00 13.58 ? 190 GLN A HG2  1 
ATOM   2951 H  HG3  . GLN A 1 188 ? 7.642  13.943 3.696   1.00 13.58 ? 190 GLN A HG3  1 
ATOM   2952 H  HE21 . GLN A 1 188 ? 6.423  13.987 5.688   1.00 15.30 ? 190 GLN A HE21 1 
ATOM   2953 H  HE22 . GLN A 1 188 ? 5.246  14.891 5.814   1.00 15.30 ? 190 GLN A HE22 1 
ATOM   2954 N  N    . VAL A 1 189 ? 11.780 16.327 5.093   1.00 9.07  ? 191 VAL A N    1 
ATOM   2955 C  CA   . VAL A 1 189 ? 12.908 16.885 5.806   1.00 8.76  ? 191 VAL A CA   1 
ATOM   2956 C  C    . VAL A 1 189 ? 12.721 18.371 6.080   1.00 9.17  ? 191 VAL A C    1 
ATOM   2957 O  O    . VAL A 1 189 ? 12.421 19.164 5.170   1.00 9.83  ? 191 VAL A O    1 
ATOM   2958 C  CB   . VAL A 1 189 ? 14.266 16.532 5.152   1.00 8.14  ? 191 VAL A CB   1 
ATOM   2959 C  CG1  . VAL A 1 189 ? 14.347 16.983 3.730   1.00 8.18  ? 191 VAL A CG1  1 
ATOM   2960 C  CG2  . VAL A 1 189 ? 15.436 17.037 5.948   1.00 8.85  ? 191 VAL A CG2  1 
ATOM   2961 H  H    . VAL A 1 189 ? 11.396 16.888 4.566   1.00 8.69  ? 191 VAL A H    1 
ATOM   2962 H  HA   . VAL A 1 189 ? 12.922 16.460 6.677   1.00 8.66  ? 191 VAL A HA   1 
ATOM   2963 H  HB   . VAL A 1 189 ? 14.339 15.565 5.138   1.00 8.44  ? 191 VAL A HB   1 
ATOM   2964 H  HG11 . VAL A 1 189 ? 15.214 16.738 3.370   1.00 8.67  ? 191 VAL A HG11 1 
ATOM   2965 H  HG12 . VAL A 1 189 ? 13.643 16.551 3.221   1.00 8.67  ? 191 VAL A HG12 1 
ATOM   2966 H  HG13 . VAL A 1 189 ? 14.235 17.946 3.698   1.00 8.67  ? 191 VAL A HG13 1 
ATOM   2967 H  HG21 . VAL A 1 189 ? 16.257 16.789 5.495   1.00 9.36  ? 191 VAL A HG21 1 
ATOM   2968 H  HG22 . VAL A 1 189 ? 15.376 18.002 6.019   1.00 9.36  ? 191 VAL A HG22 1 
ATOM   2969 H  HG23 . VAL A 1 189 ? 15.412 16.638 6.832   1.00 9.36  ? 191 VAL A HG23 1 
ATOM   2970 N  N    . VAL A 1 190 ? 12.915 18.710 7.367   1.00 9.15  ? 192 VAL A N    1 
ATOM   2971 C  CA   . VAL A 1 190 ? 13.072 20.084 7.811   1.00 10.19 ? 192 VAL A CA   1 
ATOM   2972 C  C    . VAL A 1 190 ? 14.544 20.417 7.882   1.00 8.52  ? 192 VAL A C    1 
ATOM   2973 O  O    . VAL A 1 190 ? 15.261 19.729 8.589   1.00 9.16  ? 192 VAL A O    1 
ATOM   2974 C  CB   . VAL A 1 190 ? 12.380 20.315 9.174   1.00 11.09 ? 192 VAL A CB   1 
ATOM   2975 C  CG1  . VAL A 1 190 ? 12.597 21.764 9.656   1.00 13.48 ? 192 VAL A CG1  1 
ATOM   2976 C  CG2  . VAL A 1 190 ? 10.900 19.996 9.063   1.00 13.09 ? 192 VAL A CG2  1 
ATOM   2977 H  H    . VAL A 1 190 ? 12.958 18.138 8.008   1.00 8.76  ? 192 VAL A H    1 
ATOM   2978 H  HA   . VAL A 1 190 ? 12.661 20.675 7.161   1.00 9.77  ? 192 VAL A HA   1 
ATOM   2979 H  HB   . VAL A 1 190 ? 12.769 19.717 9.832   1.00 10.20 ? 192 VAL A HB   1 
ATOM   2980 H  HG11 . VAL A 1 190 ? 12.154 21.882 10.511  1.00 12.49 ? 192 VAL A HG11 1 
ATOM   2981 H  HG12 . VAL A 1 190 ? 13.548 21.926 9.751   1.00 12.49 ? 192 VAL A HG12 1 
ATOM   2982 H  HG13 . VAL A 1 190 ? 12.221 22.374 9.002   1.00 12.49 ? 192 VAL A HG13 1 
ATOM   2983 H  HG21 . VAL A 1 190 ? 10.480 20.145 9.925   1.00 11.70 ? 192 VAL A HG21 1 
ATOM   2984 H  HG22 . VAL A 1 190 ? 10.502 20.576 8.395   1.00 11.70 ? 192 VAL A HG22 1 
ATOM   2985 H  HG23 . VAL A 1 190 ? 10.796 19.068 8.800   1.00 11.70 ? 192 VAL A HG23 1 
ATOM   2986 N  N    . MET A 1 191 ? 14.984 21.442 7.154   1.00 8.32  ? 193 MET A N    1 
ATOM   2987 C  CA   . MET A 1 191 ? 16.368 21.893 7.209   1.00 7.69  ? 193 MET A CA   1 
ATOM   2988 C  C    . MET A 1 191 ? 16.419 23.111 8.104   1.00 9.49  ? 193 MET A C    1 
ATOM   2989 O  O    . MET A 1 191 ? 15.596 24.063 7.960   1.00 9.94  ? 193 MET A O    1 
ATOM   2990 C  CB   . MET A 1 191 ? 16.912 22.215 5.833   1.00 6.18  ? 193 MET A CB   1 
ATOM   2991 C  CG   . MET A 1 191 ? 18.420 22.291 5.815   1.00 7.36  ? 193 MET A CG   1 
ATOM   2992 S  SD   . MET A 1 191 ? 18.999 23.022 4.275   1.00 7.87  ? 193 MET A SD   1 
ATOM   2993 C  CE   . MET A 1 191 ? 20.684 22.531 4.245   1.00 11.27 ? 193 MET A CE   1 
ATOM   2994 H  H    . MET A 1 191 ? 14.492 21.897 6.614   1.00 8.15  ? 193 MET A H    1 
ATOM   2995 H  HA   . MET A 1 191 ? 16.916 21.191 7.594   1.00 7.77  ? 193 MET A HA   1 
ATOM   2996 H  HB2  . MET A 1 191 ? 16.638 21.521 5.213   1.00 6.46  ? 193 MET A HB2  1 
ATOM   2997 H  HB3  . MET A 1 191 ? 16.563 23.074 5.547   1.00 6.46  ? 193 MET A HB3  1 
ATOM   2998 H  HG2  . MET A 1 191 ? 18.725 22.845 6.551   1.00 7.83  ? 193 MET A HG2  1 
ATOM   2999 H  HG3  . MET A 1 191 ? 18.790 21.397 5.888   1.00 7.83  ? 193 MET A HG3  1 
ATOM   3000 H  HE1  . MET A 1 191 ? 21.099 22.879 3.440   1.00 11.93 ? 193 MET A HE1  1 
ATOM   3001 H  HE2  . MET A 1 191 ? 21.130 22.888 5.029   1.00 11.93 ? 193 MET A HE2  1 
ATOM   3002 H  HE3  . MET A 1 191 ? 20.730 21.562 4.249   1.00 11.93 ? 193 MET A HE3  1 
ATOM   3003 N  N    . VAL A 1 192 ? 17.435 23.163 8.966   1.00 7.80  ? 194 VAL A N    1 
ATOM   3004 C  CA   . VAL A 1 192 ? 17.729 24.388 9.764   1.00 9.78  ? 194 VAL A CA   1 
ATOM   3005 C  C    . VAL A 1 192 ? 19.200 24.777 9.469   1.00 8.06  ? 194 VAL A C    1 
ATOM   3006 O  O    . VAL A 1 192 ? 20.074 24.442 10.209  1.00 8.49  ? 194 VAL A O    1 
ATOM   3007 C  CB   . VAL A 1 192 ? 17.471 24.146 11.274  1.00 10.15 ? 194 VAL A CB   1 
ATOM   3008 C  CG1  . VAL A 1 192 ? 17.610 25.435 12.038  1.00 12.30 ? 194 VAL A CG1  1 
ATOM   3009 C  CG2  . VAL A 1 192 ? 16.117 23.558 11.501  1.00 11.79 ? 194 VAL A CG2  1 
ATOM   3010 H  H    . VAL A 1 192 ? 17.975 22.510 9.116   1.00 8.30  ? 194 VAL A H    1 
ATOM   3011 H  HA   . VAL A 1 192 ? 17.155 25.112 9.468   1.00 10.04 ? 194 VAL A HA   1 
ATOM   3012 H  HB   . VAL A 1 192 ? 18.132 23.522 11.613  1.00 10.16 ? 194 VAL A HB   1 
ATOM   3013 H  HG11 . VAL A 1 192 ? 17.445 25.264 12.978  1.00 11.97 ? 194 VAL A HG11 1 
ATOM   3014 H  HG12 . VAL A 1 192 ? 18.508 25.779 11.916  1.00 11.97 ? 194 VAL A HG12 1 
ATOM   3015 H  HG13 . VAL A 1 192 ? 16.962 26.073 11.699  1.00 11.97 ? 194 VAL A HG13 1 
ATOM   3016 H  HG21 . VAL A 1 192 ? 15.989 23.419 12.452  1.00 11.55 ? 194 VAL A HG21 1 
ATOM   3017 H  HG22 . VAL A 1 192 ? 15.446 24.171 11.162  1.00 11.55 ? 194 VAL A HG22 1 
ATOM   3018 H  HG23 . VAL A 1 192 ? 16.059 22.710 11.032  1.00 11.55 ? 194 VAL A HG23 1 
ATOM   3019 N  N    . PRO A 1 193 ? 19.420 25.365 8.291   1.00 8.62  ? 195 PRO A N    1 
ATOM   3020 C  CA   . PRO A 1 193 ? 20.796 25.575 7.843   1.00 8.31  ? 195 PRO A CA   1 
ATOM   3021 C  C    . PRO A 1 193 ? 21.419 26.797 8.451   1.00 10.26 ? 195 PRO A C    1 
ATOM   3022 O  O    . PRO A 1 193 ? 20.747 27.808 8.713   1.00 10.32 ? 195 PRO A O    1 
ATOM   3023 C  CB   . PRO A 1 193 ? 20.589 25.868 6.350   1.00 9.48  ? 195 PRO A CB   1 
ATOM   3024 C  CG   . PRO A 1 193 ? 19.276 26.445 6.262   1.00 10.09 ? 195 PRO A CG   1 
ATOM   3025 C  CD   . PRO A 1 193 ? 18.418 25.833 7.312   1.00 10.57 ? 195 PRO A CD   1 
ATOM   3026 H  HA   . PRO A 1 193 ? 21.351 24.790 7.973   1.00 8.58  ? 195 PRO A HA   1 
ATOM   3027 H  HB2  . PRO A 1 193 ? 21.261 26.496 6.044   1.00 9.77  ? 195 PRO A HB2  1 
ATOM   3028 H  HB3  . PRO A 1 193 ? 20.634 25.041 5.845   1.00 9.77  ? 195 PRO A HB3  1 
ATOM   3029 H  HG2  . PRO A 1 193 ? 19.342 27.403 6.403   1.00 10.15 ? 195 PRO A HG2  1 
ATOM   3030 H  HG3  . PRO A 1 193 ? 18.909 26.263 5.383   1.00 10.15 ? 195 PRO A HG3  1 
ATOM   3031 H  HD2  . PRO A 1 193 ? 17.835 26.499 7.710   1.00 10.61 ? 195 PRO A HD2  1 
ATOM   3032 H  HD3  . PRO A 1 193 ? 17.917 25.084 6.951   1.00 10.61 ? 195 PRO A HD3  1 
ATOM   3033 N  N    . ASP A 1 194 ? 22.715 26.769 8.505   1.00 8.63  ? 196 ASP A N    1 
ATOM   3034 C  CA   . ASP A 1 194 ? 23.475 27.992 8.699   1.00 9.71  ? 196 ASP A CA   1 
ATOM   3035 C  C    . ASP A 1 194 ? 23.201 28.882 7.480   1.00 8.67  ? 196 ASP A C    1 
ATOM   3036 O  O    . ASP A 1 194 ? 23.214 28.449 6.358   1.00 9.90  ? 196 ASP A O    1 
ATOM   3037 C  CB   . ASP A 1 194 ? 25.005 27.726 8.792   1.00 10.48 ? 196 ASP A CB   1 
ATOM   3038 C  CG   . ASP A 1 194 ? 25.789 28.925 9.253   1.00 14.76 ? 196 ASP A CG   1 
ATOM   3039 O  OD1  . ASP A 1 194 ? 26.048 29.782 8.436   1.00 12.52 ? 196 ASP A OD1  1 
ATOM   3040 O  OD2  . ASP A 1 194 ? 26.192 29.021 10.429  1.00 17.82 ? 196 ASP A OD2  1 
ATOM   3041 H  H    . ASP A 1 194 ? 23.194 26.059 8.434   1.00 8.89  ? 196 ASP A H    1 
ATOM   3042 H  HA   . ASP A 1 194 ? 23.179 28.448 9.502   1.00 9.63  ? 196 ASP A HA   1 
ATOM   3043 H  HB2  . ASP A 1 194 ? 25.161 27.007 9.424   1.00 10.41 ? 196 ASP A HB2  1 
ATOM   3044 H  HB3  . ASP A 1 194 ? 25.334 27.473 7.916   1.00 10.41 ? 196 ASP A HB3  1 
ATOM   3045 N  N    . GLY A 1 195 ? 23.008 30.159 7.705   1.00 10.18 ? 197 GLY A N    1 
ATOM   3046 C  CA   . GLY A 1 195 ? 22.762 31.150 6.654   1.00 10.89 ? 197 GLY A CA   1 
ATOM   3047 C  C    . GLY A 1 195 ? 23.876 31.338 5.672   1.00 9.93  ? 197 GLY A C    1 
ATOM   3048 O  O    . GLY A 1 195 ? 23.594 31.946 4.601   1.00 9.65  ? 197 GLY A O    1 
ATOM   3049 H  H    . GLY A 1 195 ? 23.013 30.503 8.493   1.00 10.36 ? 197 GLY A H    1 
ATOM   3050 H  HA2  . GLY A 1 195 ? 21.970 30.889 6.158   1.00 10.72 ? 197 GLY A HA2  1 
ATOM   3051 H  HA3  . GLY A 1 195 ? 22.584 32.009 7.069   1.00 10.72 ? 197 GLY A HA3  1 
ATOM   3052 N  N    . ASN A 1 196 ? 25.084 30.924 5.992   1.00 9.92  ? 198 ASN A N    1 
ATOM   3053 C  CA   . ASN A 1 196 ? 26.169 30.975 5.040   1.00 10.99 ? 198 ASN A CA   1 
ATOM   3054 C  C    . ASN A 1 196 ? 26.127 29.944 3.936   1.00 10.73 ? 198 ASN A C    1 
ATOM   3055 O  O    . ASN A 1 196 ? 26.842 30.101 2.941   1.00 12.30 ? 198 ASN A O    1 
ATOM   3056 C  CB   . ASN A 1 196 ? 27.500 30.868 5.767   1.00 14.22 ? 198 ASN A CB   1 
ATOM   3057 C  CG   . ASN A 1 196 ? 27.865 32.093 6.513   1.00 19.22 ? 198 ASN A CG   1 
ATOM   3058 O  OD1  . ASN A 1 196 ? 28.339 33.037 5.913   1.00 22.79 ? 198 ASN A OD1  1 
ATOM   3059 N  ND2  . ASN A 1 196 ? 27.685 32.091 7.832   1.00 18.89 ? 198 ASN A ND2  1 
ATOM   3060 H  H    . ASN A 1 196 ? 25.303 30.607 6.760   1.00 9.49  ? 198 ASN A H    1 
ATOM   3061 H  HA   . ASN A 1 196 ? 26.149 31.846 4.613   1.00 10.39 ? 198 ASN A HA   1 
ATOM   3062 H  HB2  . ASN A 1 196 ? 27.453 30.136 6.401   1.00 13.49 ? 198 ASN A HB2  1 
ATOM   3063 H  HB3  . ASN A 1 196 ? 28.200 30.697 5.117   1.00 13.49 ? 198 ASN A HB3  1 
ATOM   3064 H  HD21 . ASN A 1 196 ? 27.887 32.787 8.295   1.00 17.68 ? 198 ASN A HD21 1 
ATOM   3065 H  HD22 . ASN A 1 196 ? 27.366 31.393 8.221   1.00 17.68 ? 198 ASN A HD22 1 
ATOM   3066 N  N    . LEU A 1 197 ? 25.349 28.895 4.106   1.00 9.58  ? 199 LEU A N    1 
ATOM   3067 C  CA   . LEU A 1 197 ? 25.187 27.908 3.034   1.00 9.43  ? 199 LEU A CA   1 
ATOM   3068 C  C    . LEU A 1 197 ? 24.540 28.519 1.840   1.00 13.17 ? 199 LEU A C    1 
ATOM   3069 O  O    . LEU A 1 197 ? 23.667 29.379 1.977   1.00 9.76  ? 199 LEU A O    1 
ATOM   3070 C  CB   . LEU A 1 197 ? 24.374 26.725 3.522   1.00 10.52 ? 199 LEU A CB   1 
ATOM   3071 C  CG   . LEU A 1 197 ? 25.031 25.779 4.533   1.00 11.79 ? 199 LEU A CG   1 
ATOM   3072 C  CD1  . LEU A 1 197 ? 24.070 24.727 4.957   1.00 13.81 ? 199 LEU A CD1  1 
ATOM   3073 C  CD2  . LEU A 1 197 ? 26.159 25.039 3.865   1.00 15.86 ? 199 LEU A CD2  1 
ATOM   3074 H  H    . LEU A 1 197 ? 24.903 28.723 4.821   1.00 9.05  ? 199 LEU A H    1 
ATOM   3075 H  HA   . LEU A 1 197 ? 26.062 27.583 2.768   1.00 9.17  ? 199 LEU A HA   1 
ATOM   3076 H  HB2  . LEU A 1 197 ? 23.567 27.068 3.937   1.00 10.72 ? 199 LEU A HB2  1 
ATOM   3077 H  HB3  . LEU A 1 197 ? 24.131 26.191 2.750   1.00 10.72 ? 199 LEU A HB3  1 
ATOM   3078 H  HG   . LEU A 1 197 ? 25.360 26.263 5.306   1.00 12.19 ? 199 LEU A HG   1 
ATOM   3079 H  HD11 . LEU A 1 197 ? 24.506 24.141 5.596   1.00 14.53 ? 199 LEU A HD11 1 
ATOM   3080 H  HD12 . LEU A 1 197 ? 23.300 25.150 5.368   1.00 14.53 ? 199 LEU A HD12 1 
ATOM   3081 H  HD13 . LEU A 1 197 ? 23.793 24.220 4.178   1.00 14.53 ? 199 LEU A HD13 1 
ATOM   3082 H  HD21 . LEU A 1 197 ? 26.570 24.442 4.510   1.00 16.24 ? 199 LEU A HD21 1 
ATOM   3083 H  HD22 . LEU A 1 197 ? 25.804 24.528 3.121   1.00 16.24 ? 199 LEU A HD22 1 
ATOM   3084 H  HD23 . LEU A 1 197 ? 26.812 25.681 3.545   1.00 16.24 ? 199 LEU A HD23 1 
ATOM   3085 N  N    . SER A 1 198 ? 24.904 28.038 0.654   1.00 10.13 ? 200 SER A N    1 
ATOM   3086 C  CA   . SER A 1 198 ? 24.363 28.657 -0.587  1.00 10.76 ? 200 SER A CA   1 
ATOM   3087 C  C    . SER A 1 198 ? 22.873 28.418 -0.726  1.00 10.60 ? 200 SER A C    1 
ATOM   3088 O  O    . SER A 1 198 ? 22.267 27.467 -0.169  1.00 10.06 ? 200 SER A O    1 
ATOM   3089 C  CB   . SER A 1 198 ? 25.035 28.066 -1.807  1.00 13.33 ? 200 SER A CB   1 
ATOM   3090 O  OG   . SER A 1 198 ? 24.586 26.739 -2.012  1.00 11.58 ? 200 SER A OG   1 
ATOM   3091 H  H    . SER A 1 198 ? 25.442 27.379 0.528   1.00 9.67  ? 200 SER A H    1 
ATOM   3092 H  HA   . SER A 1 198 ? 24.525 29.613 -0.574  1.00 10.03 ? 200 SER A HA   1 
ATOM   3093 H  HB2  . SER A 1 198 ? 24.812 28.601 -2.585  1.00 12.51 ? 200 SER A HB2  1 
ATOM   3094 H  HB3  . SER A 1 198 ? 25.996 28.059 -1.670  1.00 12.51 ? 200 SER A HB3  1 
ATOM   3095 H  HG   . SER A 1 198 ? 24.959 26.411 -2.689  1.00 11.19 ? 200 SER A HG   1 
ATOM   3096 N  N    . ARG A 1 199 ? 22.285 29.303 -1.503  1.00 9.15  ? 201 ARG A N    1 
ATOM   3097 C  CA   . ARG A 1 199 ? 20.938 29.154 -1.940  1.00 8.74  ? 201 ARG A CA   1 
ATOM   3098 C  C    . ARG A 1 199 ? 20.671 27.754 -2.579  1.00 8.96  ? 201 ARG A C    1 
ATOM   3099 O  O    . ARG A 1 199 ? 19.674 27.068 -2.260  1.00 10.14 ? 201 ARG A O    1 
ATOM   3100 C  CB   . ARG A 1 199 ? 20.574 30.283 -2.916  1.00 11.08 ? 201 ARG A CB   1 
ATOM   3101 C  CG   . ARG A 1 199 ? 19.265 30.099 -3.670  1.00 13.05 ? 201 ARG A CG   1 
ATOM   3102 C  CD   . ARG A 1 199 ? 18.908 31.360 -4.396  1.00 12.13 ? 201 ARG A CD   1 
ATOM   3103 H  H    . ARG A 1 199 ? 22.666 30.018 -1.793  1.00 8.39  ? 201 ARG A H    1 
ATOM   3104 H  HA   . ARG A 1 199 ? 20.354 29.237 -1.170  1.00 8.06  ? 201 ARG A HA   1 
ATOM   3105 H  HB2  . ARG A 1 199 ? 20.507 31.111 -2.415  1.00 9.87  ? 201 ARG A HB2  1 
ATOM   3106 H  HB3  . ARG A 1 199 ? 21.281 30.358 -3.575  1.00 9.87  ? 201 ARG A HB3  1 
ATOM   3107 H  HG2  . ARG A 1 199 ? 19.362 29.385 -4.319  1.00 11.84 ? 201 ARG A HG2  1 
ATOM   3108 H  HG3  . ARG A 1 199 ? 18.555 29.893 -3.042  1.00 11.84 ? 201 ARG A HG3  1 
ATOM   3109 N  N    . ASP A 1 200 ? 21.503 27.354 -3.508  1.00 9.63  ? 202 ASP A N    1 
ATOM   3110 C  CA   . ASP A 1 200 ? 21.293 26.032 -4.121  1.00 10.05 ? 202 ASP A CA   1 
ATOM   3111 C  C    . ASP A 1 200 ? 21.240 24.891 -3.109  1.00 9.25  ? 202 ASP A C    1 
ATOM   3112 O  O    . ASP A 1 200 ? 20.439 23.943 -3.263  1.00 12.33 ? 202 ASP A O    1 
ATOM   3113 C  CB   . ASP A 1 200 ? 22.399 25.750 -5.144  1.00 13.03 ? 202 ASP A CB   1 
ATOM   3114 C  CG   . ASP A 1 200 ? 22.234 26.527 -6.464  1.00 16.54 ? 202 ASP A CG   1 
ATOM   3115 O  OD1  . ASP A 1 200 ? 21.124 26.926 -6.780  1.00 16.90 ? 202 ASP A OD1  1 
ATOM   3116 O  OD2  . ASP A 1 200 ? 23.275 26.686 -7.107  1.00 19.83 ? 202 ASP A OD2  1 
ATOM   3117 H  H    . ASP A 1 200 ? 22.178 27.797 -3.804  1.00 9.29  ? 202 ASP A H    1 
ATOM   3118 H  HA   . ASP A 1 200 ? 20.447 26.043 -4.596  1.00 9.99  ? 202 ASP A HA   1 
ATOM   3119 H  HB2  . ASP A 1 200 ? 23.253 25.998 -4.758  1.00 12.75 ? 202 ASP A HB2  1 
ATOM   3120 H  HB3  . ASP A 1 200 ? 22.395 24.803 -5.355  1.00 12.75 ? 202 ASP A HB3  1 
ATOM   3121 N  N    . LEU A 1 201 ? 22.045 24.996 -2.059  1.00 8.00  ? 203 LEU A N    1 
ATOM   3122 C  CA   . LEU A 1 201 ? 22.148 23.967 -1.018  1.00 8.29  ? 203 LEU A CA   1 
ATOM   3123 C  C    . LEU A 1 201 ? 21.112 24.107 0.047   1.00 8.77  ? 203 LEU A C    1 
ATOM   3124 O  O    . LEU A 1 201 ? 21.090 23.263 0.970   1.00 8.97  ? 203 LEU A O    1 
ATOM   3125 C  CB   . LEU A 1 201 ? 23.552 23.989 -0.422  1.00 8.80  ? 203 LEU A CB   1 
ATOM   3126 C  CG   . LEU A 1 201 ? 24.601 23.574 -1.406  1.00 11.32 ? 203 LEU A CG   1 
ATOM   3127 C  CD1  . LEU A 1 201 ? 25.959 23.803 -0.801  1.00 12.39 ? 203 LEU A CD1  1 
ATOM   3128 C  CD2  . LEU A 1 201 ? 24.428 22.103 -1.830  1.00 13.41 ? 203 LEU A CD2  1 
ATOM   3129 H  H    . LEU A 1 201 ? 22.558 25.672 -1.921  1.00 8.27  ? 203 LEU A H    1 
ATOM   3130 H  HA   . LEU A 1 201 ? 22.021 23.099 -1.432  1.00 8.87  ? 203 LEU A HA   1 
ATOM   3131 H  HB2  . LEU A 1 201 ? 23.757 24.890 -0.126  1.00 9.31  ? 203 LEU A HB2  1 
ATOM   3132 H  HB3  . LEU A 1 201 ? 23.586 23.377 0.330   1.00 9.31  ? 203 LEU A HB3  1 
ATOM   3133 H  HG   . LEU A 1 201 ? 24.528 24.127 -2.199  1.00 11.63 ? 203 LEU A HG   1 
ATOM   3134 H  HD11 . LEU A 1 201 ? 26.638 23.534 -1.439  1.00 12.51 ? 203 LEU A HD11 1 
ATOM   3135 H  HD12 . LEU A 1 201 ? 26.057 24.745 -0.591  1.00 12.51 ? 203 LEU A HD12 1 
ATOM   3136 H  HD13 . LEU A 1 201 ? 26.037 23.273 0.008   1.00 12.51 ? 203 LEU A HD13 1 
ATOM   3137 H  HD21 . LEU A 1 201 ? 25.125 21.874 -2.465  1.00 13.89 ? 203 LEU A HD21 1 
ATOM   3138 H  HD22 . LEU A 1 201 ? 24.498 21.538 -1.044  1.00 13.89 ? 203 LEU A HD22 1 
ATOM   3139 H  HD23 . LEU A 1 201 ? 23.556 21.993 -2.240  1.00 13.89 ? 203 LEU A HD23 1 
ATOM   3140 N  N    . THR A 1 202 ? 20.214 25.086 -0.010  1.00 9.10  ? 204 THR A N    1 
ATOM   3141 C  CA   . THR A 1 202 ? 19.220 25.332 1.044   1.00 10.75 ? 204 THR A CA   1 
ATOM   3142 C  C    . THR A 1 202 ? 17.803 25.448 0.492   1.00 10.54 ? 204 THR A C    1 
ATOM   3143 O  O    . THR A 1 202 ? 16.928 25.908 1.193   1.00 13.92 ? 204 THR A O    1 
ATOM   3144 C  CB   . THR A 1 202 ? 19.560 26.571 1.911   1.00 10.01 ? 204 THR A CB   1 
ATOM   3145 O  OG1  . THR A 1 202 ? 19.660 27.740 1.082   1.00 10.99 ? 204 THR A OG1  1 
ATOM   3146 C  CG2  . THR A 1 202 ? 20.883 26.420 2.665   1.00 9.93  ? 204 THR A CG2  1 
ATOM   3147 H  H    . THR A 1 202 ? 20.156 25.639 -0.667  1.00 9.12  ? 204 THR A H    1 
ATOM   3148 H  HA   . THR A 1 202 ? 19.226 24.565 1.638   1.00 10.76 ? 204 THR A HA   1 
ATOM   3149 H  HB   . THR A 1 202 ? 18.855 26.705 2.564   1.00 9.77  ? 204 THR A HB   1 
ATOM   3150 H  HG1  . THR A 1 202 ? 20.265 27.634 0.509   1.00 10.39 ? 204 THR A HG1  1 
ATOM   3151 H  HG21 . THR A 1 202 ? 21.056 27.215 3.193   1.00 9.77  ? 204 THR A HG21 1 
ATOM   3152 H  HG22 . THR A 1 202 ? 20.842 25.652 3.256   1.00 9.77  ? 204 THR A HG22 1 
ATOM   3153 H  HG23 . THR A 1 202 ? 21.611 26.295 2.035   1.00 9.77  ? 204 THR A HG23 1 
ATOM   3154 N  N    . THR A 1 203 ? 17.571 24.979 -0.715  1.00 10.50 ? 205 THR A N    1 
ATOM   3155 C  CA   . THR A 1 203 ? 16.283 25.097 -1.379  1.00 12.19 ? 205 THR A CA   1 
ATOM   3156 C  C    . THR A 1 203 ? 15.735 23.732 -1.782  1.00 15.47 ? 205 THR A C    1 
ATOM   3157 O  O    . THR A 1 203 ? 14.829 23.663 -2.637  1.00 17.26 ? 205 THR A O    1 
ATOM   3158 C  CB   . THR A 1 203 ? 16.389 26.086 -2.608  1.00 15.19 ? 205 THR A CB   1 
ATOM   3159 O  OG1  . THR A 1 203 ? 17.499 25.708 -3.413  1.00 13.91 ? 205 THR A OG1  1 
ATOM   3160 C  CG2  . THR A 1 203 ? 16.506 27.556 -2.154  1.00 18.87 ? 205 THR A CG2  1 
ATOM   3161 H  H    . THR A 1 203 ? 18.163 24.573 -1.190  1.00 10.49 ? 205 THR A H    1 
ATOM   3162 H  HA   . THR A 1 203 ? 15.653 25.485 -0.752  1.00 12.00 ? 205 THR A HA   1 
ATOM   3163 H  HB   . THR A 1 203 ? 15.581 26.007 -3.138  1.00 14.70 ? 205 THR A HB   1 
ATOM   3164 H  HG1  . THR A 1 203 ? 18.206 25.745 -2.962  1.00 13.51 ? 205 THR A HG1  1 
ATOM   3165 H  HG21 . THR A 1 203 ? 16.569 28.137 -2.928  1.00 18.02 ? 205 THR A HG21 1 
ATOM   3166 H  HG22 . THR A 1 203 ? 15.726 27.806 -1.635  1.00 18.02 ? 205 THR A HG22 1 
ATOM   3167 H  HG23 . THR A 1 203 ? 17.299 27.671 -1.608  1.00 18.02 ? 205 THR A HG23 1 
ATOM   3168 N  N    . LYS A 1 204 ? 16.226 22.628 -1.200  1.00 11.94 ? 206 LYS A N    1 
ATOM   3169 C  CA   . LYS A 1 204 ? 15.763 21.301 -1.567  1.00 11.81 ? 206 LYS A CA   1 
ATOM   3170 C  C    . LYS A 1 204 ? 14.834 20.645 -0.537  1.00 11.85 ? 206 LYS A C    1 
ATOM   3171 O  O    . LYS A 1 204 ? 14.138 19.672 -0.820  1.00 13.65 ? 206 LYS A O    1 
ATOM   3172 C  CB   . LYS A 1 204 ? 16.959 20.393 -1.777  1.00 14.23 ? 206 LYS A CB   1 
ATOM   3173 C  CG   . LYS A 1 204 ? 17.959 20.849 -2.796  1.00 16.98 ? 206 LYS A CG   1 
ATOM   3174 C  CD   . LYS A 1 204 ? 17.302 21.195 -4.139  1.00 25.24 ? 206 LYS A CD   1 
ATOM   3175 C  CE   . LYS A 1 204 ? 18.341 21.632 -5.177  1.00 27.61 ? 206 LYS A CE   1 
ATOM   3176 N  NZ   . LYS A 1 204 ? 19.302 20.503 -5.419  1.00 28.26 ? 206 LYS A NZ   1 
ATOM   3177 H  H    . LYS A 1 204 ? 16.830 22.631 -0.587  1.00 12.05 ? 206 LYS A H    1 
ATOM   3178 H  HA   . LYS A 1 204 ? 15.282 21.359 -2.407  1.00 11.99 ? 206 LYS A HA   1 
ATOM   3179 H  HB2  . LYS A 1 204 ? 17.427 20.304 -0.932  1.00 14.58 ? 206 LYS A HB2  1 
ATOM   3180 H  HB3  . LYS A 1 204 ? 16.636 19.523 -2.060  1.00 14.58 ? 206 LYS A HB3  1 
ATOM   3181 H  HG2  . LYS A 1 204 ? 18.409 21.643 -2.466  1.00 17.28 ? 206 LYS A HG2  1 
ATOM   3182 H  HG3  . LYS A 1 204 ? 18.604 20.140 -2.949  1.00 17.28 ? 206 LYS A HG3  1 
ATOM   3183 H  HD2  . LYS A 1 204 ? 16.841 20.412 -4.481  1.00 25.35 ? 206 LYS A HD2  1 
ATOM   3184 H  HD3  . LYS A 1 204 ? 16.675 21.924 -4.010  1.00 25.35 ? 206 LYS A HD3  1 
ATOM   3185 H  HE2  . LYS A 1 204 ? 17.898 21.849 -6.013  1.00 27.57 ? 206 LYS A HE2  1 
ATOM   3186 H  HE3  . LYS A 1 204 ? 18.836 22.396 -4.843  1.00 27.57 ? 206 LYS A HE3  1 
ATOM   3187 H  HZ1  . LYS A 1 204 ? 19.911 20.745 -6.021  1.00 28.27 ? 206 LYS A HZ1  1 
ATOM   3188 H  HZ2  . LYS A 1 204 ? 19.714 20.288 -4.660  1.00 28.27 ? 206 LYS A HZ2  1 
ATOM   3189 H  HZ3  . LYS A 1 204 ? 18.863 19.790 -5.722  1.00 28.27 ? 206 LYS A HZ3  1 
ATOM   3190 N  N    . ALA A 1 205 ? 14.810 21.147 0.690   1.00 10.14 ? 207 ALA A N    1 
ATOM   3191 C  CA   . ALA A 1 205 ? 14.119 20.469 1.784   1.00 11.14 ? 207 ALA A CA   1 
ATOM   3192 C  C    . ALA A 1 205 ? 12.655 20.751 1.734   1.00 11.50 ? 207 ALA A C    1 
ATOM   3193 O  O    . ALA A 1 205 ? 12.233 21.691 1.030   1.00 12.81 ? 207 ALA A O    1 
ATOM   3194 C  CB   . ALA A 1 205 ? 14.687 20.904 3.142   1.00 10.61 ? 207 ALA A CB   1 
ATOM   3195 H  H    . ALA A 1 205 ? 15.189 21.884 0.919   1.00 10.39 ? 207 ALA A H    1 
ATOM   3196 H  HA   . ALA A 1 205 ? 14.246 19.512 1.696   1.00 11.28 ? 207 ALA A HA   1 
ATOM   3197 H  HB1  . ALA A 1 205 ? 14.210 20.439 3.847   1.00 10.77 ? 207 ALA A HB1  1 
ATOM   3198 H  HB2  . ALA A 1 205 ? 15.630 20.680 3.176   1.00 10.77 ? 207 ALA A HB2  1 
ATOM   3199 H  HB3  . ALA A 1 205 ? 14.571 21.862 3.239   1.00 10.77 ? 207 ALA A HB3  1 
ATOM   3200 N  N    . THR A 1 206 ? 11.872 19.992 2.459   1.00 9.45  ? 208 THR A N    1 
ATOM   3201 C  CA   . THR A 1 206 ? 10.420 20.189 2.544   1.00 12.24 ? 208 THR A CA   1 
ATOM   3202 C  C    . THR A 1 206 ? 10.089 21.556 3.139   1.00 12.57 ? 208 THR A C    1 
ATOM   3203 O  O    . THR A 1 206 ? 9.154  22.254 2.694   1.00 16.31 ? 208 THR A O    1 
ATOM   3204 C  CB   . THR A 1 206 ? 9.752  19.059 3.388   1.00 11.42 ? 208 THR A CB   1 
ATOM   3205 O  OG1  . THR A 1 206 ? 10.238 17.794 3.010   1.00 11.05 ? 208 THR A OG1  1 
ATOM   3206 C  CG2  . THR A 1 206 ? 8.184  19.136 3.299   1.00 16.76 ? 208 THR A CG2  1 
ATOM   3207 H  H    . THR A 1 206 ? 12.154 19.330 2.931   1.00 9.89  ? 208 THR A H    1 
ATOM   3208 H  HA   . THR A 1 206 ? 10.045 20.155 1.650   1.00 12.23 ? 208 THR A HA   1 
ATOM   3209 H  HB   . THR A 1 206 ? 9.989  19.203 4.318   1.00 11.11 ? 208 THR A HB   1 
ATOM   3210 H  HG1  . THR A 1 206 ? 10.071 17.653 2.199   1.00 10.92 ? 208 THR A HG1  1 
ATOM   3211 H  HG21 . THR A 1 206 ? 7.787  18.427 3.829   1.00 15.87 ? 208 THR A HG21 1 
ATOM   3212 H  HG22 . THR A 1 206 ? 7.875  19.992 3.635   1.00 15.87 ? 208 THR A HG22 1 
ATOM   3213 H  HG23 . THR A 1 206 ? 7.900  19.037 2.377   1.00 15.87 ? 208 THR A HG23 1 
ATOM   3214 N  N    . LEU A 1 207 ? 10.855 21.937 4.134   1.00 12.32 ? 209 LEU A N    1 
ATOM   3215 C  CA   . LEU A 1 207 ? 10.675 23.178 4.872   1.00 13.80 ? 209 LEU A CA   1 
ATOM   3216 C  C    . LEU A 1 207 ? 12.056 23.648 5.310   1.00 12.46 ? 209 LEU A C    1 
ATOM   3217 O  O    . LEU A 1 207 ? 12.867 22.842 5.782   1.00 11.22 ? 209 LEU A O    1 
ATOM   3218 C  CB   . LEU A 1 207 ? 9.786  22.994 6.111   1.00 15.72 ? 209 LEU A CB   1 
ATOM   3219 C  CG   . LEU A 1 207 ? 9.615  24.158 7.059   1.00 17.99 ? 209 LEU A CG   1 
ATOM   3220 C  CD1  . LEU A 1 207 ? 8.925  25.305 6.421   1.00 23.30 ? 209 LEU A CD1  1 
ATOM   3221 C  CD2  . LEU A 1 207 ? 8.799  23.680 8.236   1.00 18.69 ? 209 LEU A CD2  1 
ATOM   3222 H  H    . LEU A 1 207 ? 11.521 21.473 4.420   1.00 11.61 ? 209 LEU A H    1 
ATOM   3223 H  HA   . LEU A 1 207 ? 10.280 23.852 4.297   1.00 12.79 ? 209 LEU A HA   1 
ATOM   3224 H  HB2  . LEU A 1 207 ? 8.898  22.751 5.804   1.00 14.24 ? 209 LEU A HB2  1 
ATOM   3225 H  HB3  . LEU A 1 207 ? 10.150 22.261 6.630   1.00 14.24 ? 209 LEU A HB3  1 
ATOM   3226 H  HG   . LEU A 1 207 ? 10.483 24.452 7.379   1.00 16.11 ? 209 LEU A HG   1 
ATOM   3227 H  HD11 . LEU A 1 207 ? 8.841  26.022 7.068   1.00 21.03 ? 209 LEU A HD11 1 
ATOM   3228 H  HD12 . LEU A 1 207 ? 9.449  25.604 5.661   1.00 21.03 ? 209 LEU A HD12 1 
ATOM   3229 H  HD13 . LEU A 1 207 ? 8.046  25.020 6.126   1.00 21.03 ? 209 LEU A HD13 1 
ATOM   3230 H  HD21 . LEU A 1 207 ? 8.680  24.416 8.856   1.00 16.31 ? 209 LEU A HD21 1 
ATOM   3231 H  HD22 . LEU A 1 207 ? 7.937  23.372 7.917   1.00 16.31 ? 209 LEU A HD22 1 
ATOM   3232 H  HD23 . LEU A 1 207 ? 9.270  22.952 8.672   1.00 16.31 ? 209 LEU A HD23 1 
ATOM   3233 N  N    . VAL A 1 208 ? 12.328 24.927 5.184   1.00 11.90 ? 210 VAL A N    1 
ATOM   3234 C  CA   . VAL A 1 208 ? 13.634 25.478 5.588   1.00 11.77 ? 210 VAL A CA   1 
ATOM   3235 C  C    . VAL A 1 208 ? 13.401 26.582 6.618   1.00 14.08 ? 210 VAL A C    1 
ATOM   3236 O  O    . VAL A 1 208 ? 12.535 27.455 6.409   1.00 17.72 ? 210 VAL A O    1 
ATOM   3237 C  CB   . VAL A 1 208 ? 14.471 25.976 4.408   1.00 11.43 ? 210 VAL A CB   1 
ATOM   3238 C  CG1  . VAL A 1 208 ? 15.851 26.483 4.890   1.00 13.38 ? 210 VAL A CG1  1 
ATOM   3239 C  CG2  . VAL A 1 208 ? 14.636 24.868 3.281   1.00 15.67 ? 210 VAL A CG2  1 
ATOM   3240 H  H    . VAL A 1 208 ? 11.782 25.512 4.868   1.00 11.31 ? 210 VAL A H    1 
ATOM   3241 H  HA   . VAL A 1 208 ? 14.140 24.775 6.025   1.00 11.38 ? 210 VAL A HA   1 
ATOM   3242 H  HB   . VAL A 1 208 ? 14.011 26.729 4.006   1.00 11.23 ? 210 VAL A HB   1 
ATOM   3243 H  HG11 . VAL A 1 208 ? 16.359 26.791 4.123   1.00 13.30 ? 210 VAL A HG11 1 
ATOM   3244 H  HG12 . VAL A 1 208 ? 15.719 27.213 5.514   1.00 13.30 ? 210 VAL A HG12 1 
ATOM   3245 H  HG13 . VAL A 1 208 ? 16.320 25.754 5.326   1.00 13.30 ? 210 VAL A HG13 1 
ATOM   3246 H  HG21 . VAL A 1 208 ? 15.172 25.231 2.559   1.00 15.82 ? 210 VAL A HG21 1 
ATOM   3247 H  HG22 . VAL A 1 208 ? 15.076 24.093 3.663   1.00 15.82 ? 210 VAL A HG22 1 
ATOM   3248 H  HG23 . VAL A 1 208 ? 13.758 24.621 2.951   1.00 15.82 ? 210 VAL A HG23 1 
ATOM   3249 N  N    . LEU A 1 209 ? 14.055 26.474 7.770   1.00 12.72 ? 211 LEU A N    1 
ATOM   3250 C  CA   . LEU A 1 209 ? 13.851 27.377 8.915   1.00 16.30 ? 211 LEU A CA   1 
ATOM   3251 C  C    . LEU A 1 209 ? 15.131 27.987 9.357   1.00 15.76 ? 211 LEU A C    1 
ATOM   3252 O  O    . LEU A 1 209 ? 16.179 27.402 9.207   1.00 14.30 ? 211 LEU A O    1 
ATOM   3253 C  CB   . LEU A 1 209 ? 13.228 26.616 10.082  1.00 15.53 ? 211 LEU A CB   1 
ATOM   3254 C  CG   . LEU A 1 209 ? 11.953 25.822 9.828   1.00 19.44 ? 211 LEU A CG   1 
ATOM   3255 C  CD1  . LEU A 1 209 ? 11.574 25.042 10.997  1.00 14.58 ? 211 LEU A CD1  1 
ATOM   3256 C  CD2  . LEU A 1 209 ? 10.823 26.756 9.474   1.00 19.46 ? 211 LEU A CD2  1 
ATOM   3257 H  H    . LEU A 1 209 ? 14.643 25.866 7.923   1.00 12.71 ? 211 LEU A H    1 
ATOM   3258 H  HA   . LEU A 1 209 ? 13.246 28.090 8.658   1.00 15.82 ? 211 LEU A HA   1 
ATOM   3259 H  HB2  . LEU A 1 209 ? 13.889 25.989 10.414  1.00 14.85 ? 211 LEU A HB2  1 
ATOM   3260 H  HB3  . LEU A 1 209 ? 13.025 27.259 10.780  1.00 14.85 ? 211 LEU A HB3  1 
ATOM   3261 H  HG   . LEU A 1 209 ? 12.093 25.214 9.085   1.00 18.57 ? 211 LEU A HG   1 
ATOM   3262 H  HD11 . LEU A 1 209 ? 10.761 24.551 10.798  1.00 13.48 ? 211 LEU A HD11 1 
ATOM   3263 H  HD12 . LEU A 1 209 ? 12.291 24.423 11.208  1.00 13.48 ? 211 LEU A HD12 1 
ATOM   3264 H  HD13 . LEU A 1 209 ? 11.425 25.643 11.743  1.00 13.48 ? 211 LEU A HD13 1 
ATOM   3265 H  HD21 . LEU A 1 209 ? 10.020 26.234 9.316   1.00 18.02 ? 211 LEU A HD21 1 
ATOM   3266 H  HD22 . LEU A 1 209 ? 10.679 27.370 10.210  1.00 18.02 ? 211 LEU A HD22 1 
ATOM   3267 H  HD23 . LEU A 1 209 ? 11.060 27.249 8.673   1.00 18.02 ? 211 LEU A HD23 1 
ATOM   3268 N  N    . ASN A 1 210 ? 15.049 29.151 9.983   1.00 16.62 ? 212 ASN A N    1 
ATOM   3269 C  CA   . ASN A 1 210 ? 16.223 29.780 10.567  1.00 18.49 ? 212 ASN A CA   1 
ATOM   3270 C  C    . ASN A 1 210 ? 16.593 29.194 11.914  1.00 15.78 ? 212 ASN A C    1 
ATOM   3271 O  O    . ASN A 1 210 ? 17.745 29.255 12.307  1.00 16.26 ? 212 ASN A O    1 
ATOM   3272 C  CB   . ASN A 1 210 ? 15.969 31.258 10.727  1.00 22.06 ? 212 ASN A CB   1 
ATOM   3273 C  CG   . ASN A 1 210 ? 15.796 31.972 9.403   1.00 24.66 ? 212 ASN A CG   1 
ATOM   3274 O  OD1  . ASN A 1 210 ? 16.458 31.649 8.392   1.00 25.89 ? 212 ASN A OD1  1 
ATOM   3275 N  ND2  . ASN A 1 210 ? 14.896 32.958 9.396   1.00 28.44 ? 212 ASN A ND2  1 
ATOM   3276 H  H    . ASN A 1 210 ? 14.323 29.600 10.082  1.00 14.80 ? 212 ASN A H    1 
ATOM   3277 H  HA   . ASN A 1 210 ? 16.978 29.664 9.969   1.00 16.65 ? 212 ASN A HA   1 
ATOM   3278 H  HB2  . ASN A 1 210 ? 15.158 31.384 11.244  1.00 19.57 ? 212 ASN A HB2  1 
ATOM   3279 H  HB3  . ASN A 1 210 ? 16.722 31.659 11.188  1.00 19.57 ? 212 ASN A HB3  1 
ATOM   3280 H  HD21 . ASN A 1 210 ? 14.752 33.402 8.674   1.00 25.16 ? 212 ASN A HD21 1 
ATOM   3281 H  HD22 . ASN A 1 210 ? 14.461 33.149 10.113  1.00 25.16 ? 212 ASN A HD22 1 
ATOM   3282 N  N    . SER A 1 211 ? 15.636 28.576 12.597  1.00 16.20 ? 213 SER A N    1 
ATOM   3283 C  CA   . SER A 1 211 ? 15.884 28.036 13.915  1.00 15.18 ? 213 SER A CA   1 
ATOM   3284 C  C    . SER A 1 211 ? 14.868 26.970 14.207  1.00 13.44 ? 213 SER A C    1 
ATOM   3285 O  O    . SER A 1 211 ? 13.740 27.032 13.710  1.00 14.68 ? 213 SER A O    1 
ATOM   3286 C  CB   . SER A 1 211 ? 15.732 29.135 14.951  1.00 17.24 ? 213 SER A CB   1 
ATOM   3287 O  OG   . SER A 1 211 ? 15.752 28.618 16.255  1.00 18.80 ? 213 SER A OG   1 
ATOM   3288 H  H    . SER A 1 211 ? 14.832 28.460 12.313  1.00 15.66 ? 213 SER A H    1 
ATOM   3289 H  HA   . SER A 1 211 ? 16.777 27.659 13.968  1.00 14.57 ? 213 SER A HA   1 
ATOM   3290 H  HB2  . SER A 1 211 ? 16.464 29.764 14.851  1.00 16.00 ? 213 SER A HB2  1 
ATOM   3291 H  HB3  . SER A 1 211 ? 14.886 29.587 14.806  1.00 16.00 ? 213 SER A HB3  1 
ATOM   3292 H  HG   . SER A 1 211 ? 15.666 29.241 16.812  1.00 17.38 ? 213 SER A HG   1 
ATOM   3293 N  N    . LEU A 1 212 ? 15.235 26.009 15.048  1.00 14.37 ? 214 LEU A N    1 
ATOM   3294 C  CA   . LEU A 1 212 ? 14.235 25.047 15.545  1.00 15.76 ? 214 LEU A CA   1 
ATOM   3295 C  C    . LEU A 1 212 ? 13.096 25.723 16.298  1.00 19.95 ? 214 LEU A C    1 
ATOM   3296 O  O    . LEU A 1 212 ? 11.994 25.174 16.346  1.00 18.44 ? 214 LEU A O    1 
ATOM   3297 C  CB   . LEU A 1 212 ? 14.847 23.982 16.452  1.00 16.20 ? 214 LEU A CB   1 
ATOM   3298 C  CG   . LEU A 1 212 ? 15.721 22.944 15.767  1.00 12.20 ? 214 LEU A CG   1 
ATOM   3299 C  CD1  . LEU A 1 212 ? 16.554 22.174 16.804  1.00 16.67 ? 214 LEU A CD1  1 
ATOM   3300 C  CD2  . LEU A 1 212 ? 14.909 22.021 14.873  1.00 14.71 ? 214 LEU A CD2  1 
ATOM   3301 H  H    . LEU A 1 212 ? 16.033 25.888 15.345  1.00 13.15 ? 214 LEU A H    1 
ATOM   3302 H  HA   . LEU A 1 212 ? 13.846 24.591 14.782  1.00 14.27 ? 214 LEU A HA   1 
ATOM   3303 H  HB2  . LEU A 1 212 ? 15.395 24.427 17.118  1.00 14.82 ? 214 LEU A HB2  1 
ATOM   3304 H  HB3  . LEU A 1 212 ? 14.127 23.506 16.894  1.00 14.82 ? 214 LEU A HB3  1 
ATOM   3305 H  HG   . LEU A 1 212 ? 16.348 23.413 15.194  1.00 11.43 ? 214 LEU A HG   1 
ATOM   3306 H  HD11 . LEU A 1 212 ? 17.103 21.519 16.344  1.00 15.91 ? 214 LEU A HD11 1 
ATOM   3307 H  HD12 . LEU A 1 212 ? 17.119 22.801 17.283  1.00 15.91 ? 214 LEU A HD12 1 
ATOM   3308 H  HD13 . LEU A 1 212 ? 15.954 21.729 17.422  1.00 15.91 ? 214 LEU A HD13 1 
ATOM   3309 H  HD21 . LEU A 1 212 ? 15.505 21.379 14.458  1.00 14.02 ? 214 LEU A HD21 1 
ATOM   3310 H  HD22 . LEU A 1 212 ? 14.248 21.560 15.413  1.00 14.02 ? 214 LEU A HD22 1 
ATOM   3311 H  HD23 . LEU A 1 212 ? 14.467 22.552 14.191  1.00 14.02 ? 214 LEU A HD23 1 
ATOM   3312 N  N    . GLN A 1 213 ? 13.353 26.905 16.855  1.00 17.41 ? 215 GLN A N    1 
ATOM   3313 C  CA   . GLN A 1 213 ? 12.333 27.688 17.536  1.00 21.57 ? 215 GLN A CA   1 
ATOM   3314 C  C    . GLN A 1 213 ? 11.139 28.031 16.653  1.00 23.55 ? 215 GLN A C    1 
ATOM   3315 O  O    . GLN A 1 213 ? 10.066 28.315 17.144  1.00 28.68 ? 215 GLN A O    1 
ATOM   3316 C  CB   . GLN A 1 213 ? 12.966 28.967 18.038  1.00 22.09 ? 215 GLN A CB   1 
ATOM   3317 C  CG   . GLN A 1 213 ? 13.888 28.729 19.195  1.00 23.84 ? 215 GLN A CG   1 
ATOM   3318 C  CD   . GLN A 1 213 ? 14.694 29.943 19.610  1.00 30.73 ? 215 GLN A CD   1 
ATOM   3319 O  OE1  . GLN A 1 213 ? 15.168 30.723 18.772  1.00 39.95 ? 215 GLN A OE1  1 
ATOM   3320 N  NE2  . GLN A 1 213 ? 14.890 30.085 20.911  1.00 32.28 ? 215 GLN A NE2  1 
ATOM   3321 H  H    . GLN A 1 213 ? 14.127 27.280 16.849  1.00 15.21 ? 215 GLN A H    1 
ATOM   3322 H  HA   . GLN A 1 213 ? 12.008 27.190 18.302  1.00 18.53 ? 215 GLN A HA   1 
ATOM   3323 H  HB2  . GLN A 1 213 ? 13.480 29.370 17.321  1.00 18.77 ? 215 GLN A HB2  1 
ATOM   3324 H  HB3  . GLN A 1 213 ? 12.267 29.574 18.329  1.00 18.77 ? 215 GLN A HB3  1 
ATOM   3325 H  HG2  . GLN A 1 213 ? 13.361 28.450 19.960  1.00 20.56 ? 215 GLN A HG2  1 
ATOM   3326 H  HG3  . GLN A 1 213 ? 14.514 28.028 18.955  1.00 20.56 ? 215 GLN A HG3  1 
ATOM   3327 H  HE21 . GLN A 1 213 ? 14.567 29.508 21.460  1.00 28.33 ? 215 GLN A HE21 1 
ATOM   3328 H  HE22 . GLN A 1 213 ? 15.340 30.756 21.207  1.00 28.33 ? 215 GLN A HE22 1 
ATOM   3329 N  N    . ASP A 1 214 ? 11.346 28.052 15.351  1.00 20.80 ? 216 ASP A N    1 
ATOM   3330 C  CA   . ASP A 1 214 ? 10.318 28.437 14.402  1.00 26.87 ? 216 ASP A CA   1 
ATOM   3331 C  C    . ASP A 1 214 ? 9.518  27.245 13.862  1.00 22.68 ? 216 ASP A C    1 
ATOM   3332 O  O    . ASP A 1 214 ? 8.613  27.430 13.065  1.00 25.55 ? 216 ASP A O    1 
ATOM   3333 C  CB   . ASP A 1 214 ? 10.957 29.158 13.219  1.00 24.38 ? 216 ASP A CB   1 
ATOM   3334 C  CG   . ASP A 1 214 ? 11.757 30.375 13.627  1.00 28.20 ? 216 ASP A CG   1 
ATOM   3335 O  OD1  . ASP A 1 214 ? 11.511 30.939 14.711  1.00 32.18 ? 216 ASP A OD1  1 
ATOM   3336 O  OD2  . ASP A 1 214 ? 12.647 30.757 12.846  1.00 30.30 ? 216 ASP A OD2  1 
ATOM   3337 H  H    . ASP A 1 214 ? 12.093 27.841 14.982  1.00 17.33 ? 216 ASP A H    1 
ATOM   3338 H  HA   . ASP A 1 214 ? 9.700  29.048 14.832  1.00 23.12 ? 216 ASP A HA   1 
ATOM   3339 H  HB2  . ASP A 1 214 ? 11.556 28.546 12.763  1.00 21.02 ? 216 ASP A HB2  1 
ATOM   3340 H  HB3  . ASP A 1 214 ? 10.258 29.450 12.613  1.00 21.02 ? 216 ASP A HB3  1 
ATOM   3341 N  N    . PHE A 1 215 ? 9.866  26.022 14.279  1.00 18.52 ? 217 PHE A N    1 
ATOM   3342 C  CA   . PHE A 1 215 ? 9.158  24.846 13.818  1.00 18.53 ? 217 PHE A CA   1 
ATOM   3343 C  C    . PHE A 1 215 ? 7.770  24.820 14.452  1.00 20.94 ? 217 PHE A C    1 
ATOM   3344 O  O    . PHE A 1 215 ? 7.632  25.001 15.655  1.00 20.38 ? 217 PHE A O    1 
ATOM   3345 C  CB   . PHE A 1 215 ? 9.918  23.580 14.178  1.00 17.04 ? 217 PHE A CB   1 
ATOM   3346 C  CG   . PHE A 1 215 ? 9.215  22.302 13.782  1.00 15.81 ? 217 PHE A CG   1 
ATOM   3347 C  CD1  . PHE A 1 215 ? 8.960  22.019 12.446  1.00 15.87 ? 217 PHE A CD1  1 
ATOM   3348 C  CD2  . PHE A 1 215 ? 8.790  21.410 14.759  1.00 20.28 ? 217 PHE A CD2  1 
ATOM   3349 C  CE1  . PHE A 1 215 ? 8.340  20.870 12.093  1.00 16.76 ? 217 PHE A CE1  1 
ATOM   3350 C  CE2  . PHE A 1 215 ? 8.168  20.258 14.420  1.00 17.30 ? 217 PHE A CE2  1 
ATOM   3351 C  CZ   . PHE A 1 215 ? 7.925  19.984 13.073  1.00 18.16 ? 217 PHE A CZ   1 
ATOM   3352 H  H    . PHE A 1 215 ? 10.508 25.857 14.826  1.00 16.85 ? 217 PHE A H    1 
ATOM   3353 H  HA   . PHE A 1 215 ? 9.057  24.883 12.854  1.00 16.90 ? 217 PHE A HA   1 
ATOM   3354 H  HB2  . PHE A 1 215 ? 10.778 23.595 13.730  1.00 15.85 ? 217 PHE A HB2  1 
ATOM   3355 H  HB3  . PHE A 1 215 ? 10.050 23.559 15.139  1.00 15.85 ? 217 PHE A HB3  1 
ATOM   3356 H  HD1  . PHE A 1 215 ? 9.241  22.612 11.787  1.00 14.92 ? 217 PHE A HD1  1 
ATOM   3357 H  HD2  . PHE A 1 215 ? 8.957  21.596 15.655  1.00 18.56 ? 217 PHE A HD2  1 
ATOM   3358 H  HE1  . PHE A 1 215 ? 8.175  20.685 11.196  1.00 15.69 ? 217 PHE A HE1  1 
ATOM   3359 H  HE2  . PHE A 1 215 ? 7.889  19.663 15.079  1.00 15.42 ? 217 PHE A HE2  1 
ATOM   3360 H  HZ   . PHE A 1 215 ? 7.492  19.197 12.831  1.00 16.61 ? 217 PHE A HZ   1 
ATOM   3361 N  N    . GLN A 1 216 ? 6.763  24.609 13.613  1.00 20.49 ? 218 GLN A N    1 
ATOM   3362 C  CA   . GLN A 1 216 ? 5.374  24.535 14.049  1.00 23.17 ? 218 GLN A CA   1 
ATOM   3363 C  C    . GLN A 1 216 ? 4.909  23.105 13.844  1.00 19.82 ? 218 GLN A C    1 
ATOM   3364 O  O    . GLN A 1 216 ? 4.657  22.699 12.721  1.00 20.28 ? 218 GLN A O    1 
ATOM   3365 C  CB   . GLN A 1 216 ? 4.520  25.492 13.208  1.00 24.55 ? 218 GLN A CB   1 
ATOM   3366 C  CG   . GLN A 1 216 ? 5.013  26.913 13.231  1.00 26.33 ? 218 GLN A CG   1 
ATOM   3367 C  CD   . GLN A 1 216 ? 4.191  27.822 12.370  1.00 30.99 ? 218 GLN A CD   1 
ATOM   3368 O  OE1  . GLN A 1 216 ? 4.300  27.800 11.149  1.00 31.66 ? 218 GLN A OE1  1 
ATOM   3369 N  NE2  . GLN A 1 216 ? 3.324  28.592 12.991  1.00 35.71 ? 218 GLN A NE2  1 
ATOM   3370 H  H    . GLN A 1 216 ? 6.862  24.504 12.766  1.00 19.14 ? 218 GLN A H    1 
ATOM   3371 H  HA   . GLN A 1 216 ? 5.298  24.771 14.987  1.00 20.88 ? 218 GLN A HA   1 
ATOM   3372 H  HB2  . GLN A 1 216 ? 4.525  25.190 12.287  1.00 21.86 ? 218 GLN A HB2  1 
ATOM   3373 H  HB3  . GLN A 1 216 ? 3.613  25.487 13.552  1.00 21.86 ? 218 GLN A HB3  1 
ATOM   3374 H  HG2  . GLN A 1 216 ? 4.976  27.246 14.141  1.00 23.61 ? 218 GLN A HG2  1 
ATOM   3375 H  HG3  . GLN A 1 216 ? 5.927  26.936 12.905  1.00 23.61 ? 218 GLN A HG3  1 
ATOM   3376 H  HE21 . GLN A 1 216 ? 3.252  28.556 13.847  1.00 31.54 ? 218 GLN A HE21 1 
ATOM   3377 H  HE22 . GLN A 1 216 ? 2.828  29.131 12.540  1.00 31.54 ? 218 GLN A HE22 1 
ATOM   3378 N  N    . PRO A 1 217 ? 4.892  22.291 14.895  1.00 21.16 ? 219 PRO A N    1 
ATOM   3379 C  CA   . PRO A 1 217 ? 4.621  20.856 14.739  1.00 20.99 ? 219 PRO A CA   1 
ATOM   3380 C  C    . PRO A 1 217 ? 3.316  20.541 14.011  1.00 21.79 ? 219 PRO A C    1 
ATOM   3381 O  O    . PRO A 1 217 ? 3.238  19.520 13.366  1.00 20.93 ? 219 PRO A O    1 
ATOM   3382 C  CB   . PRO A 1 217 ? 4.554  20.360 16.167  1.00 24.09 ? 219 PRO A CB   1 
ATOM   3383 C  CG   . PRO A 1 217 ? 5.443  21.285 16.921  1.00 25.05 ? 219 PRO A CG   1 
ATOM   3384 C  CD   . PRO A 1 217 ? 5.188  22.630 16.299  1.00 19.18 ? 219 PRO A CD   1 
ATOM   3385 H  HA   . PRO A 1 217 ? 5.357  20.421 14.282  1.00 17.56 ? 219 PRO A HA   1 
ATOM   3386 H  HB2  . PRO A 1 217 ? 3.642  20.416 16.492  1.00 20.06 ? 219 PRO A HB2  1 
ATOM   3387 H  HB3  . PRO A 1 217 ? 4.883  19.449 16.215  1.00 20.06 ? 219 PRO A HB3  1 
ATOM   3388 H  HG2  . PRO A 1 217 ? 5.197  21.286 17.860  1.00 21.25 ? 219 PRO A HG2  1 
ATOM   3389 H  HG3  . PRO A 1 217 ? 6.369  21.020 16.806  1.00 21.25 ? 219 PRO A HG3  1 
ATOM   3390 H  HD2  . PRO A 1 217 ? 4.422  23.057 16.714  1.00 15.38 ? 219 PRO A HD2  1 
ATOM   3391 H  HD3  . PRO A 1 217 ? 5.981  23.186 16.354  1.00 15.38 ? 219 PRO A HD3  1 
ATOM   3392 N  N    . GLU A 1 218 ? 2.327  21.417 14.133  1.00 21.99 ? 220 GLU A N    1 
ATOM   3393 C  CA   . GLU A 1 218 ? 1.009  21.196 13.540  1.00 26.36 ? 220 GLU A CA   1 
ATOM   3394 C  C    . GLU A 1 218 ? 1.082  21.185 12.030  1.00 24.97 ? 220 GLU A C    1 
ATOM   3395 O  O    . GLU A 1 218 ? 0.230  20.591 11.393  1.00 23.26 ? 220 GLU A O    1 
ATOM   3396 C  CB   . GLU A 1 218 ? -0.013 22.246 14.040  1.00 27.32 ? 220 GLU A CB   1 
ATOM   3397 C  CG   . GLU A 1 218 ? 0.275  23.715 13.670  1.00 30.46 ? 220 GLU A CG   1 
ATOM   3398 C  CD   . GLU A 1 218 ? 1.148  24.450 14.692  1.00 29.60 ? 220 GLU A CD   1 
ATOM   3399 O  OE1  . GLU A 1 218 ? 1.840  23.791 15.490  1.00 26.62 ? 220 GLU A OE1  1 
ATOM   3400 O  OE2  . GLU A 1 218 ? 1.134  25.696 14.716  1.00 32.53 ? 220 GLU A OE2  1 
ATOM   3401 H  H    . GLU A 1 218 ? 2.393  22.160 14.561  1.00 17.93 ? 220 GLU A H    1 
ATOM   3402 H  HA   . GLU A 1 218 ? 0.690  20.324 13.821  1.00 21.60 ? 220 GLU A HA   1 
ATOM   3403 H  HB2  . GLU A 1 218 ? -0.883 22.022 13.672  1.00 21.52 ? 220 GLU A HB2  1 
ATOM   3404 H  HB3  . GLU A 1 218 ? -0.052 22.195 15.008  1.00 21.52 ? 220 GLU A HB3  1 
ATOM   3405 H  HG2  . GLU A 1 218 ? 0.736  23.738 12.816  1.00 24.86 ? 220 GLU A HG2  1 
ATOM   3406 H  HG3  . GLU A 1 218 ? -0.567 24.192 13.602  1.00 24.86 ? 220 GLU A HG3  1 
ATOM   3407 N  N    . LEU A 1 219 ? 2.100  21.805 11.438  1.00 22.82 ? 221 LEU A N    1 
ATOM   3408 C  CA   . LEU A 1 219 ? 2.224  21.780 9.987   1.00 20.82 ? 221 LEU A CA   1 
ATOM   3409 C  C    . LEU A 1 219 ? 2.378  20.365 9.485   1.00 22.51 ? 221 LEU A C    1 
ATOM   3410 O  O    . LEU A 1 219 ? 2.019  20.059 8.341   1.00 25.16 ? 221 LEU A O    1 
ATOM   3411 C  CB   . LEU A 1 219 ? 3.401  22.636 9.524   1.00 24.88 ? 221 LEU A CB   1 
ATOM   3412 C  CG   . LEU A 1 219 ? 3.482  23.008 8.063   1.00 29.80 ? 221 LEU A CG   1 
ATOM   3413 C  CD1  . LEU A 1 219 ? 2.154  23.594 7.568   1.00 30.98 ? 221 LEU A CD1  1 
ATOM   3414 C  CD2  . LEU A 1 219 ? 4.668  23.995 7.910   1.00 29.64 ? 221 LEU A CD2  1 
ATOM   3415 H  H    . LEU A 1 219 ? 2.720  22.239 11.847  1.00 19.12 ? 221 LEU A H    1 
ATOM   3416 H  HA   . LEU A 1 219 ? 1.416  22.148 9.597   1.00 17.69 ? 221 LEU A HA   1 
ATOM   3417 H  HB2  . LEU A 1 219 ? 3.380  23.467 10.025  1.00 22.56 ? 221 LEU A HB2  1 
ATOM   3418 H  HB3  . LEU A 1 219 ? 4.218  22.159 9.738   1.00 22.56 ? 221 LEU A HB3  1 
ATOM   3419 H  HG   . LEU A 1 219 ? 3.678  22.214 7.541   1.00 27.89 ? 221 LEU A HG   1 
ATOM   3420 H  HD11 . LEU A 1 219 ? 2.240  23.821 6.629   1.00 28.30 ? 221 LEU A HD11 1 
ATOM   3421 H  HD12 . LEU A 1 219 ? 1.454  22.932 7.686   1.00 28.30 ? 221 LEU A HD12 1 
ATOM   3422 H  HD13 . LEU A 1 219 ? 1.948  24.389 8.084   1.00 28.30 ? 221 LEU A HD13 1 
ATOM   3423 H  HD21 . LEU A 1 219 ? 4.745  24.253 6.978   1.00 28.31 ? 221 LEU A HD21 1 
ATOM   3424 H  HD22 . LEU A 1 219 ? 4.500  24.778 8.457   1.00 28.31 ? 221 LEU A HD22 1 
ATOM   3425 H  HD23 . LEU A 1 219 ? 5.483  23.557 8.201   1.00 28.31 ? 221 LEU A HD23 1 
ATOM   3426 N  N    . PHE A 1 220 ? 2.904  19.493 10.337  1.00 22.45 ? 222 PHE A N    1 
ATOM   3427 C  CA   . PHE A 1 220 ? 3.080  18.092 10.010  1.00 19.90 ? 222 PHE A CA   1 
ATOM   3428 C  C    . PHE A 1 220 ? 2.105  17.174 10.764  1.00 23.57 ? 222 PHE A C    1 
ATOM   3429 O  O    . PHE A 1 220 ? 2.341  15.963 10.922  1.00 23.71 ? 222 PHE A O    1 
ATOM   3430 C  CB   . PHE A 1 220 ? 4.549  17.686 10.243  1.00 19.08 ? 222 PHE A CB   1 
ATOM   3431 C  CG   . PHE A 1 220 ? 5.513  18.312 9.262   1.00 19.60 ? 222 PHE A CG   1 
ATOM   3432 C  CD1  . PHE A 1 220 ? 6.092  19.531 9.521   1.00 19.45 ? 222 PHE A CD1  1 
ATOM   3433 C  CD2  . PHE A 1 220 ? 5.781  17.699 8.063   1.00 17.44 ? 222 PHE A CD2  1 
ATOM   3434 C  CE1  . PHE A 1 220 ? 6.975  20.109 8.599   1.00 17.13 ? 222 PHE A CE1  1 
ATOM   3435 C  CE2  . PHE A 1 220 ? 6.678  18.271 7.143   1.00 16.83 ? 222 PHE A CE2  1 
ATOM   3436 C  CZ   . PHE A 1 220 ? 7.250  19.495 7.424   1.00 16.18 ? 222 PHE A CZ   1 
ATOM   3437 H  H    . PHE A 1 220 ? 3.171  19.697 11.129  1.00 18.61 ? 222 PHE A H    1 
ATOM   3438 H  HA   . PHE A 1 220 ? 2.900  17.980 9.063   1.00 16.24 ? 222 PHE A HA   1 
ATOM   3439 H  HB2  . PHE A 1 220 ? 4.812  17.961 11.135  1.00 16.22 ? 222 PHE A HB2  1 
ATOM   3440 H  HB3  . PHE A 1 220 ? 4.624  16.722 10.160  1.00 16.22 ? 222 PHE A HB3  1 
ATOM   3441 H  HD1  . PHE A 1 220 ? 5.912  19.966 10.323  1.00 17.72 ? 222 PHE A HD1  1 
ATOM   3442 H  HD2  . PHE A 1 220 ? 5.395  16.874 7.874   1.00 15.87 ? 222 PHE A HD2  1 
ATOM   3443 H  HE1  . PHE A 1 220 ? 7.367  20.930 8.791   1.00 16.08 ? 222 PHE A HE1  1 
ATOM   3444 H  HE2  . PHE A 1 220 ? 6.858  17.844 6.337   1.00 15.96 ? 222 PHE A HE2  1 
ATOM   3445 H  HZ   . PHE A 1 220 ? 7.840  19.885 6.819   1.00 15.55 ? 222 PHE A HZ   1 
ATOM   3446 N  N    . GLY A 1 221 ? 0.979  17.739 11.195  1.00 23.48 ? 223 GLY A N    1 
ATOM   3447 C  CA   . GLY A 1 221 ? -0.063 16.949 11.817  1.00 26.66 ? 223 GLY A CA   1 
ATOM   3448 C  C    . GLY A 1 221 ? 0.270  16.513 13.223  1.00 27.94 ? 223 GLY A C    1 
ATOM   3449 O  O    . GLY A 1 221 ? -0.330 15.564 13.722  1.00 29.10 ? 223 GLY A O    1 
ATOM   3450 H  H    . GLY A 1 221 ? 0.800  18.578 11.136  1.00 19.92 ? 223 GLY A H    1 
ATOM   3451 H  HA2  . GLY A 1 221 ? -0.882 17.468 11.846  1.00 22.05 ? 223 GLY A HA2  1 
ATOM   3452 H  HA3  . GLY A 1 221 ? -0.224 16.156 11.283  1.00 22.05 ? 223 GLY A HA3  1 
ATOM   3453 N  N    . LEU A 1 222 ? 1.223  17.189 13.862  1.00 23.80 ? 224 LEU A N    1 
ATOM   3454 C  CA   . LEU A 1 222 ? 1.573  16.881 15.241  1.00 27.95 ? 224 LEU A CA   1 
ATOM   3455 C  C    . LEU A 1 222 ? 0.890  17.869 16.180  1.00 27.68 ? 224 LEU A C    1 
ATOM   3456 O  O    . LEU A 1 222 ? 0.464  18.936 15.765  1.00 26.09 ? 224 LEU A O    1 
ATOM   3457 C  CB   . LEU A 1 222 ? 3.088  16.944 15.424  1.00 26.36 ? 224 LEU A CB   1 
ATOM   3458 C  CG   . LEU A 1 222 ? 3.965  16.134 14.467  1.00 20.24 ? 224 LEU A CG   1 
ATOM   3459 C  CD1  . LEU A 1 222 ? 5.433  16.549 14.529  1.00 22.91 ? 224 LEU A CD1  1 
ATOM   3460 C  CD2  . LEU A 1 222 ? 3.860  14.677 14.734  1.00 26.01 ? 224 LEU A CD2  1 
ATOM   3461 H  H    . LEU A 1 222 ? 1.680  17.831 13.518  1.00 18.72 ? 224 LEU A H    1 
ATOM   3462 H  HA   . LEU A 1 222 ? 1.272  15.986 15.461  1.00 22.51 ? 224 LEU A HA   1 
ATOM   3463 H  HB2  . LEU A 1 222 ? 3.359  17.871 15.338  1.00 21.93 ? 224 LEU A HB2  1 
ATOM   3464 H  HB3  . LEU A 1 222 ? 3.292  16.637 16.321  1.00 21.93 ? 224 LEU A HB3  1 
ATOM   3465 H  HG   . LEU A 1 222 ? 3.656  16.288 13.560  1.00 16.69 ? 224 LEU A HG   1 
ATOM   3466 H  HD11 . LEU A 1 222 ? 5.940  16.007 13.905  1.00 20.31 ? 224 LEU A HD11 1 
ATOM   3467 H  HD12 . LEU A 1 222 ? 5.505  17.486 14.288  1.00 20.31 ? 224 LEU A HD12 1 
ATOM   3468 H  HD13 . LEU A 1 222 ? 5.761  16.413 15.431  1.00 20.31 ? 224 LEU A HD13 1 
ATOM   3469 H  HD21 . LEU A 1 222 ? 4.428  14.199 14.109  1.00 22.07 ? 224 LEU A HD21 1 
ATOM   3470 H  HD22 . LEU A 1 222 ? 4.147  14.501 15.644  1.00 22.07 ? 224 LEU A HD22 1 
ATOM   3471 H  HD23 . LEU A 1 222 ? 2.937  14.401 14.619  1.00 22.07 ? 224 LEU A HD23 1 
ATOM   3472 N  N    . PRO A 1 223 ? 0.776  17.510 17.466  1.00 28.22 ? 225 PRO A N    1 
ATOM   3473 C  CA   . PRO A 1 223 ? 0.198  18.412 18.456  1.00 30.01 ? 225 PRO A CA   1 
ATOM   3474 C  C    . PRO A 1 223 ? 0.881  19.763 18.473  1.00 31.29 ? 225 PRO A C    1 
ATOM   3475 O  O    . PRO A 1 223 ? 2.105  19.807 18.406  1.00 28.97 ? 225 PRO A O    1 
ATOM   3476 C  CB   . PRO A 1 223 ? 0.480  17.688 19.774  1.00 32.94 ? 225 PRO A CB   1 
ATOM   3477 C  CG   . PRO A 1 223 ? 0.535  16.265 19.417  1.00 31.84 ? 225 PRO A CG   1 
ATOM   3478 C  CD   . PRO A 1 223 ? 1.193  16.234 18.070  1.00 31.19 ? 225 PRO A CD   1 
ATOM   3479 H  HA   . PRO A 1 223 ? -0.758 18.516 18.326  1.00 23.39 ? 225 PRO A HA   1 
ATOM   3480 H  HB2  . PRO A 1 223 ? 1.329  17.985 20.136  1.00 25.82 ? 225 PRO A HB2  1 
ATOM   3481 H  HB3  . PRO A 1 223 ? -0.241 17.857 20.401  1.00 25.82 ? 225 PRO A HB3  1 
ATOM   3482 H  HG2  . PRO A 1 223 ? 1.067  15.783 20.070  1.00 24.80 ? 225 PRO A HG2  1 
ATOM   3483 H  HG3  . PRO A 1 223 ? -0.363 15.903 19.370  1.00 24.80 ? 225 PRO A HG3  1 
ATOM   3484 H  HD2  . PRO A 1 223 ? 2.158  16.203 18.164  1.00 25.35 ? 225 PRO A HD2  1 
ATOM   3485 H  HD3  . PRO A 1 223 ? 0.861  15.487 17.547  1.00 25.35 ? 225 PRO A HD3  1 
ATOM   3486 N  N    . SER A 1 224 ? 0.116  20.845 18.534  1.00 29.12 ? 226 SER A N    1 
ATOM   3487 C  CA   . SER A 1 224 ? 0.692  22.172 18.710  1.00 29.98 ? 226 SER A CA   1 
ATOM   3488 C  C    . SER A 1 224 ? 1.315  22.299 20.085  1.00 30.27 ? 226 SER A C    1 
ATOM   3489 O  O    . SER A 1 224 ? 1.002  21.519 20.993  1.00 31.37 ? 226 SER A O    1 
ATOM   3490 C  CB   . SER A 1 224 ? -0.362 23.279 18.573  1.00 33.71 ? 226 SER A CB   1 
ATOM   3491 O  OG   . SER A 1 224 ? -0.914 23.355 17.276  1.00 41.23 ? 226 SER A OG   1 
ATOM   3492 H  H    . SER A 1 224 ? -0.742 20.838 18.476  1.00 23.55 ? 226 SER A H    1 
ATOM   3493 H  HA   . SER A 1 224 ? 1.382  22.318 18.043  1.00 24.71 ? 226 SER A HA   1 
ATOM   3494 H  HB2  . SER A 1 224 ? -1.078 23.103 19.203  1.00 27.55 ? 226 SER A HB2  1 
ATOM   3495 H  HB3  . SER A 1 224 ? 0.054  24.129 18.782  1.00 27.55 ? 226 SER A HB3  1 
ATOM   3496 H  HG   . SER A 1 224 ? -1.286 22.628 17.078  1.00 35.24 ? 226 SER A HG   1 
ATOM   3497 N  N    . TYR A 1 225 ? 2.157  23.317 20.226  1.00 33.41 ? 227 TYR A N    1 
ATOM   3498 C  CA   . TYR A 1 225 ? 2.745  23.674 21.503  1.00 33.19 ? 227 TYR A CA   1 
ATOM   3499 C  C    . TYR A 1 225 ? 1.655  24.241 22.398  1.00 40.05 ? 227 TYR A C    1 
ATOM   3500 O  O    . TYR A 1 225 ? 0.844  25.050 21.946  1.00 44.55 ? 227 TYR A O    1 
ATOM   3501 C  CB   . TYR A 1 225 ? 3.833  24.728 21.324  1.00 37.30 ? 227 TYR A CB   1 
ATOM   3502 C  CG   . TYR A 1 225 ? 5.150  24.205 20.798  1.00 32.70 ? 227 TYR A CG   1 
ATOM   3503 C  CD1  . TYR A 1 225 ? 5.832  23.199 21.456  1.00 31.01 ? 227 TYR A CD1  1 
ATOM   3504 C  CD2  . TYR A 1 225 ? 5.720  24.745 19.668  1.00 32.02 ? 227 TYR A CD2  1 
ATOM   3505 C  CE1  . TYR A 1 225 ? 7.041  22.744 20.998  1.00 30.93 ? 227 TYR A CE1  1 
ATOM   3506 C  CE2  . TYR A 1 225 ? 6.919  24.288 19.193  1.00 28.60 ? 227 TYR A CE2  1 
ATOM   3507 C  CZ   . TYR A 1 225 ? 7.586  23.289 19.863  1.00 30.63 ? 227 TYR A CZ   1 
ATOM   3508 O  OH   . TYR A 1 225 ? 8.806  22.813 19.400  1.00 26.02 ? 227 TYR A OH   1 
ATOM   3509 H  H    . TYR A 1 225 ? 2.406  23.826 19.579  1.00 26.52 ? 227 TYR A H    1 
ATOM   3510 H  HA   . TYR A 1 225 ? 3.129  22.890 21.925  1.00 26.05 ? 227 TYR A HA   1 
ATOM   3511 H  HB2  . TYR A 1 225 ? 3.514  25.398 20.698  1.00 30.91 ? 227 TYR A HB2  1 
ATOM   3512 H  HB3  . TYR A 1 225 ? 4.005  25.143 22.184  1.00 30.91 ? 227 TYR A HB3  1 
ATOM   3513 H  HD1  . TYR A 1 225 ? 5.468  22.831 22.229  1.00 26.15 ? 227 TYR A HD1  1 
ATOM   3514 H  HD2  . TYR A 1 225 ? 5.276  25.424 19.213  1.00 27.73 ? 227 TYR A HD2  1 
ATOM   3515 H  HE1  . TYR A 1 225 ? 7.485  22.063 21.449  1.00 27.12 ? 227 TYR A HE1  1 
ATOM   3516 H  HE2  . TYR A 1 225 ? 7.289  24.662 18.426  1.00 25.35 ? 227 TYR A HE2  1 
ATOM   3517 H  HH   . TYR A 1 225 ? 9.030  23.226 18.703  1.00 23.95 ? 227 TYR A HH   1 
ATOM   3518 N  N    . GLU A 1 226 ? 1.644  23.815 23.656  1.00 47.34 ? 228 GLU A N    1 
ATOM   3519 C  CA   . GLU A 1 226 ? 0.664  24.293 24.636  1.00 55.11 ? 228 GLU A CA   1 
ATOM   3520 C  C    . GLU A 1 226 ? 1.101  25.618 25.249  1.00 61.06 ? 228 GLU A C    1 
ATOM   3521 O  O    . GLU A 1 226 ? 2.298  25.868 25.410  1.00 63.59 ? 228 GLU A O    1 
ATOM   3522 C  CB   . GLU A 1 226 ? 0.475  23.257 25.747  1.00 57.07 ? 228 GLU A CB   1 
ATOM   3523 H  H    . GLU A 1 226 ? 2.200  23.241 23.974  1.00 33.21 ? 228 GLU A H    1 
ATOM   3524 H  HA   . GLU A 1 226 ? -0.190 24.427 24.196  1.00 39.51 ? 228 GLU A HA   1 
HETATM 3525 MG MG   . MG  B 2 .   ? 24.530 17.974 11.021  1.00 7.73  ? 301 MG  A MG   1 
HETATM 3526 O  O01  . FJF C 3 .   ? 33.294 20.927 9.290   1.00 18.96 ? 302 FJF A O01  1 
HETATM 3527 C  C02  . FJF C 3 .   ? 33.000 19.737 9.395   1.00 20.41 ? 302 FJF A C02  1 
HETATM 3528 N  N03  . FJF C 3 .   ? 31.737 19.285 9.865   1.00 19.00 ? 302 FJF A N03  1 
HETATM 3529 C  C04  . FJF C 3 .   ? 31.340 17.955 9.926   1.00 20.20 ? 302 FJF A C04  1 
HETATM 3530 C  C05  . FJF C 3 .   ? 32.227 16.891 9.529   1.00 22.68 ? 302 FJF A C05  1 
HETATM 3531 C  C06  . FJF C 3 .   ? 33.517 17.299 9.035   1.00 21.83 ? 302 FJF A C06  1 
HETATM 3532 O  O07  . FJF C 3 .   ? 34.326 16.470 8.715   1.00 27.94 ? 302 FJF A O07  1 
HETATM 3533 N  N08  . FJF C 3 .   ? 33.888 18.680 8.969   1.00 23.42 ? 302 FJF A N08  1 
HETATM 3534 C  C09  . FJF C 3 .   ? 31.857 15.486 9.529   1.00 22.78 ? 302 FJF A C09  1 
HETATM 3535 O  O10  . FJF C 3 .   ? 30.460 15.243 9.474   1.00 25.85 ? 302 FJF A O10  1 
HETATM 3536 C  C11  . FJF C 3 .   ? 29.992 14.634 10.701  1.00 23.89 ? 302 FJF A C11  1 
HETATM 3537 C  C12  . FJF C 3 .   ? 28.934 15.552 11.280  1.00 22.69 ? 302 FJF A C12  1 
HETATM 3538 O  O13  . FJF C 3 .   ? 28.556 16.582 10.333  1.00 18.63 ? 302 FJF A O13  1 
HETATM 3539 C  C14  . FJF C 3 .   ? 31.243 14.439 11.579  1.00 25.65 ? 302 FJF A C14  1 
HETATM 3540 O  O15  . FJF C 3 .   ? 31.257 13.194 12.269  1.00 30.20 ? 302 FJF A O15  1 
HETATM 3541 C  C16  . FJF C 3 .   ? 32.433 14.603 10.629  1.00 24.14 ? 302 FJF A C16  1 
HETATM 3542 O  O17  . FJF C 3 .   ? 32.750 13.351 10.050  1.00 27.22 ? 302 FJF A O17  1 
HETATM 3543 O  O    . HOH D 4 .   ? 43.904 17.292 -4.807  1.00 34.14 ? 401 HOH A O    1 
HETATM 3544 O  O    . HOH D 4 .   ? 8.080  21.250 -3.719  1.00 44.12 ? 402 HOH A O    1 
HETATM 3545 O  O    . HOH D 4 .   ? 22.724 1.443  0.836   1.00 23.68 ? 403 HOH A O    1 
HETATM 3546 O  O    . HOH D 4 .   ? 27.647 7.275  25.234  1.00 35.03 ? 404 HOH A O    1 
HETATM 3547 O  O    . HOH D 4 .   ? 24.795 0.435  4.300   1.00 34.24 ? 405 HOH A O    1 
HETATM 3548 O  O    . HOH D 4 .   ? 4.894  9.242  -0.254  1.00 49.53 ? 406 HOH A O    1 
HETATM 3549 O  O    . HOH D 4 .   ? 11.101 10.049 23.774  1.00 35.80 ? 407 HOH A O    1 
HETATM 3550 O  O    . HOH D 4 .   ? 0.887  26.202 19.910  1.00 45.66 ? 408 HOH A O    1 
HETATM 3551 O  O    . HOH D 4 .   ? 28.644 0.000  0.000   0.50 47.39 ? 409 HOH A O    1 
HETATM 3552 O  O    . HOH D 4 .   ? 2.798  11.384 3.227   1.00 40.98 ? 410 HOH A O    1 
HETATM 3553 O  O    . HOH D 4 .   ? 6.670  2.618  15.942  1.00 37.85 ? 411 HOH A O    1 
HETATM 3554 O  O    . HOH D 4 .   ? 48.582 15.451 10.435  1.00 42.25 ? 412 HOH A O    1 
HETATM 3555 O  O    . HOH D 4 .   ? 1.988  12.106 5.133   1.00 36.99 ? 413 HOH A O    1 
HETATM 3556 O  O    . HOH D 4 .   ? 25.791 9.283  25.500  1.00 30.84 ? 414 HOH A O    1 
HETATM 3557 O  O    . HOH D 4 .   ? 48.278 22.333 15.968  1.00 40.14 ? 415 HOH A O    1 
HETATM 3558 O  O    . HOH D 4 .   ? 32.497 5.508  2.477   1.00 42.11 ? 416 HOH A O    1 
HETATM 3559 O  O    . HOH D 4 .   ? 17.497 15.702 -4.729  1.00 23.38 ? 417 HOH A O    1 
HETATM 3560 O  O    . HOH D 4 .   ? 0.251  11.865 20.315  1.00 48.03 ? 418 HOH A O    1 
HETATM 3561 O  O    . HOH D 4 .   ? 18.175 7.560  24.110  1.00 40.58 ? 419 HOH A O    1 
HETATM 3562 O  O    . HOH D 4 .   ? 7.705  12.266 5.516   1.00 21.09 ? 420 HOH A O    1 
HETATM 3563 O  O    . HOH D 4 .   ? 20.933 26.076 24.517  1.00 41.39 ? 421 HOH A O    1 
HETATM 3564 O  O    . HOH D 4 .   ? 48.225 27.065 15.593  1.00 41.15 ? 422 HOH A O    1 
HETATM 3565 O  O    . HOH D 4 .   ? 28.977 24.668 26.690  1.00 37.03 ? 423 HOH A O    1 
HETATM 3566 O  O    . HOH D 4 .   ? 28.868 25.743 23.098  1.00 36.69 ? 424 HOH A O    1 
HETATM 3567 O  O    . HOH D 4 .   ? 2.288  9.256  3.218   1.00 45.25 ? 425 HOH A O    1 
HETATM 3568 O  O    . HOH D 4 .   ? 24.164 16.881 9.251   1.00 9.78  ? 426 HOH A O    1 
HETATM 3569 O  O    . HOH D 4 .   ? 40.834 7.463  0.293   1.00 41.39 ? 427 HOH A O    1 
HETATM 3570 O  O    . HOH D 4 .   ? 52.655 25.692 4.217   1.00 48.88 ? 428 HOH A O    1 
HETATM 3571 O  O    . HOH D 4 .   ? 26.132 19.176 10.221  1.00 8.83  ? 429 HOH A O    1 
HETATM 3572 O  O    . HOH D 4 .   ? 52.157 18.160 6.971   1.00 28.67 ? 430 HOH A O    1 
HETATM 3573 O  O    . HOH D 4 .   ? 47.141 25.197 18.570  1.00 46.59 ? 431 HOH A O    1 
HETATM 3574 O  O    . HOH D 4 .   ? 18.099 -1.455 11.033  1.00 39.67 ? 432 HOH A O    1 
HETATM 3575 O  O    . HOH D 4 .   ? 41.533 3.810  6.852   1.00 42.50 ? 433 HOH A O    1 
HETATM 3576 O  O    . HOH D 4 .   ? 38.098 13.163 19.417  1.00 42.20 ? 434 HOH A O    1 
HETATM 3577 O  O    . HOH D 4 .   ? 9.071  27.425 19.435  1.00 43.56 ? 435 HOH A O    1 
HETATM 3578 O  O    . HOH D 4 .   ? 26.760 5.702  -1.307  1.00 35.28 ? 436 HOH A O    1 
HETATM 3579 O  O    . HOH D 4 .   ? 7.483  26.209 10.998  1.00 38.38 ? 437 HOH A O    1 
HETATM 3580 O  O    . HOH D 4 .   ? 31.664 0.980  4.311   1.00 44.10 ? 438 HOH A O    1 
HETATM 3581 O  O    . HOH D 4 .   ? 28.859 31.275 1.676   1.00 31.65 ? 439 HOH A O    1 
HETATM 3582 O  O    . HOH D 4 .   ? 44.135 12.992 -3.563  1.00 40.35 ? 440 HOH A O    1 
HETATM 3583 O  O    . HOH D 4 .   ? 31.117 24.492 22.947  1.00 35.95 ? 441 HOH A O    1 
HETATM 3584 O  O    . HOH D 4 .   ? 6.809  23.974 11.028  1.00 33.94 ? 442 HOH A O    1 
HETATM 3585 O  O    . HOH D 4 .   ? 28.008 17.116 -0.928  1.00 27.17 ? 443 HOH A O    1 
HETATM 3586 O  O    . HOH D 4 .   ? 39.883 10.450 -3.086  1.00 36.87 ? 444 HOH A O    1 
HETATM 3587 O  O    . HOH D 4 .   ? 9.686  24.538 17.558  1.00 32.37 ? 445 HOH A O    1 
HETATM 3588 O  O    . HOH D 4 .   ? 10.802 12.960 0.325   1.00 27.79 ? 446 HOH A O    1 
HETATM 3589 O  O    . HOH D 4 .   ? 36.765 14.410 25.618  1.00 37.93 ? 447 HOH A O    1 
HETATM 3590 O  O    . HOH D 4 .   ? 35.381 20.939 29.336  1.00 23.77 ? 448 HOH A O    1 
HETATM 3591 O  O    . HOH D 4 .   ? 24.963 2.110  0.699   1.00 34.25 ? 449 HOH A O    1 
HETATM 3592 O  O    . HOH D 4 .   ? 12.069 11.924 -1.881  1.00 29.22 ? 450 HOH A O    1 
HETATM 3593 O  O    . HOH D 4 .   ? 32.334 9.316  11.655  1.00 19.39 ? 451 HOH A O    1 
HETATM 3594 O  O    . HOH D 4 .   ? 8.024  8.394  0.262   1.00 36.38 ? 452 HOH A O    1 
HETATM 3595 O  O    . HOH D 4 .   ? 6.497  21.957 2.351   1.00 32.42 ? 453 HOH A O    1 
HETATM 3596 O  O    . HOH D 4 .   ? 20.066 20.780 0.681   1.00 12.89 ? 454 HOH A O    1 
HETATM 3597 O  O    . HOH D 4 .   ? 24.947 2.640  15.803  1.00 23.04 ? 455 HOH A O    1 
HETATM 3598 O  O    . HOH D 4 .   ? 46.621 12.534 0.137   1.00 45.51 ? 456 HOH A O    1 
HETATM 3599 O  O    . HOH D 4 .   ? 44.048 9.541  2.038   1.00 24.06 ? 457 HOH A O    1 
HETATM 3600 O  O    . HOH D 4 .   ? 3.015  5.611  10.641  1.00 32.55 ? 458 HOH A O    1 
HETATM 3601 O  O    . HOH D 4 .   ? 20.335 28.771 11.224  1.00 18.66 ? 459 HOH A O    1 
HETATM 3602 O  O    . HOH D 4 .   ? 27.057 24.252 15.086  1.00 18.32 ? 460 HOH A O    1 
HETATM 3603 O  O    . HOH D 4 .   ? 17.882 25.894 16.241  1.00 14.34 ? 461 HOH A O    1 
HETATM 3604 O  O    . HOH D 4 .   ? 22.221 3.258  0.102   1.00 28.84 ? 462 HOH A O    1 
HETATM 3605 O  O    . HOH D 4 .   ? 24.354 -1.343 16.056  1.00 36.94 ? 463 HOH A O    1 
HETATM 3606 O  O    . HOH D 4 .   ? 21.200 18.660 28.593  1.00 40.96 ? 464 HOH A O    1 
HETATM 3607 O  O    . HOH D 4 .   ? 20.086 1.500  16.775  1.00 36.24 ? 465 HOH A O    1 
HETATM 3608 O  O    . HOH D 4 .   ? 25.432 23.933 10.659  1.00 16.07 ? 466 HOH A O    1 
HETATM 3609 O  O    . HOH D 4 .   ? 25.474 14.376 13.448  1.00 14.46 ? 467 HOH A O    1 
HETATM 3610 O  O    . HOH D 4 .   ? 3.183  9.415  16.193  1.00 31.54 ? 468 HOH A O    1 
HETATM 3611 O  O    . HOH D 4 .   ? 4.314  20.783 25.024  1.00 45.09 ? 469 HOH A O    1 
HETATM 3612 O  O    . HOH D 4 .   ? 17.591 29.526 1.044   1.00 17.23 ? 470 HOH A O    1 
HETATM 3613 O  O    . HOH D 4 .   ? 20.784 24.328 12.847  1.00 11.38 ? 471 HOH A O    1 
HETATM 3614 O  O    . HOH D 4 .   ? -2.227 19.268 15.410  1.00 40.61 ? 472 HOH A O    1 
HETATM 3615 O  O    . HOH D 4 .   ? 26.353 25.745 -3.853  1.00 18.85 ? 473 HOH A O    1 
HETATM 3616 O  O    . HOH D 4 .   ? 50.909 11.580 4.110   1.00 33.98 ? 474 HOH A O    1 
HETATM 3617 O  O    . HOH D 4 .   ? 28.613 8.340  28.689  1.00 38.53 ? 475 HOH A O    1 
HETATM 3618 O  O    . HOH D 4 .   ? 33.668 13.235 14.768  1.00 16.45 ? 476 HOH A O    1 
HETATM 3619 O  O    . HOH D 4 .   ? 19.315 29.991 7.871   1.00 21.58 ? 477 HOH A O    1 
HETATM 3620 O  O    . HOH D 4 .   ? 49.991 8.194  6.031   1.00 53.61 ? 478 HOH A O    1 
HETATM 3621 O  O    . HOH D 4 .   ? 28.110 30.847 11.153  1.00 29.90 ? 479 HOH A O    1 
HETATM 3622 O  O    . HOH D 4 .   ? 24.051 6.849  5.357   1.00 17.15 ? 480 HOH A O    1 
HETATM 3623 O  O    . HOH D 4 .   ? 8.756  9.829  22.413  1.00 30.90 ? 481 HOH A O    1 
HETATM 3624 O  O    . HOH D 4 .   ? 14.659 0.173  18.838  1.00 45.93 ? 482 HOH A O    1 
HETATM 3625 O  O    . HOH D 4 .   ? 21.428 19.572 -1.590  1.00 16.86 ? 483 HOH A O    1 
HETATM 3626 O  O    . HOH D 4 .   ? 49.760 20.034 -1.599  1.00 51.36 ? 484 HOH A O    1 
HETATM 3627 O  O    . HOH D 4 .   ? 17.429 23.913 23.401  1.00 19.55 ? 485 HOH A O    1 
HETATM 3628 O  O    . HOH D 4 .   ? 44.544 6.945  2.705   1.00 39.98 ? 486 HOH A O    1 
HETATM 3629 O  O    . HOH D 4 .   ? 37.866 14.098 12.160  1.00 23.22 ? 487 HOH A O    1 
HETATM 3630 O  O    . HOH D 4 .   ? 47.382 12.518 17.757  1.00 42.83 ? 488 HOH A O    1 
HETATM 3631 O  O    . HOH D 4 .   ? 44.785 24.384 -3.226  1.00 47.69 ? 489 HOH A O    1 
HETATM 3632 O  O    . HOH D 4 .   ? 41.546 21.754 20.513  1.00 35.50 ? 490 HOH A O    1 
HETATM 3633 O  O    . HOH D 4 .   ? 11.617 18.573 -1.216  1.00 30.64 ? 491 HOH A O    1 
HETATM 3634 O  O    . HOH D 4 .   ? 21.795 9.349  28.132  1.00 35.13 ? 492 HOH A O    1 
HETATM 3635 O  O    . HOH D 4 .   ? 47.301 27.468 11.513  1.00 36.82 ? 493 HOH A O    1 
HETATM 3636 O  O    . HOH D 4 .   ? 10.021 17.148 0.307   1.00 25.55 ? 494 HOH A O    1 
HETATM 3637 O  O    . HOH D 4 .   ? 24.148 -3.035 12.444  1.00 30.49 ? 495 HOH A O    1 
HETATM 3638 O  O    . HOH D 4 .   ? 2.742  24.900 18.003  1.00 32.84 ? 496 HOH A O    1 
HETATM 3639 O  O    . HOH D 4 .   ? 12.436 30.405 10.085  1.00 31.23 ? 497 HOH A O    1 
HETATM 3640 O  O    . HOH D 4 .   ? 27.508 2.152  16.698  1.00 31.74 ? 498 HOH A O    1 
HETATM 3641 O  O    . HOH D 4 .   ? 24.184 24.400 8.289   1.00 10.71 ? 499 HOH A O    1 
HETATM 3642 O  O    . HOH D 4 .   ? 28.476 17.346 26.451  1.00 23.26 ? 500 HOH A O    1 
HETATM 3643 O  O    . HOH D 4 .   ? 21.421 21.374 -3.776  1.00 21.09 ? 501 HOH A O    1 
HETATM 3644 O  O    . HOH D 4 .   ? 2.284  28.027 15.751  1.00 47.39 ? 502 HOH A O    1 
HETATM 3645 O  O    . HOH D 4 .   ? 5.958  17.167 1.380   1.00 26.72 ? 503 HOH A O    1 
HETATM 3646 O  O    . HOH D 4 .   ? 39.222 27.833 0.164   1.00 33.68 ? 504 HOH A O    1 
HETATM 3647 O  O    . HOH D 4 .   ? 3.698  3.872  8.654   1.00 31.09 ? 505 HOH A O    1 
HETATM 3648 O  O    . HOH D 4 .   ? 36.973 13.336 -2.532  1.00 33.17 ? 506 HOH A O    1 
HETATM 3649 O  O    . HOH D 4 .   ? 16.344 7.141  -3.677  1.00 26.75 ? 507 HOH A O    1 
HETATM 3650 O  O    . HOH D 4 .   ? 16.118 4.642  -0.457  1.00 34.31 ? 508 HOH A O    1 
HETATM 3651 O  O    . HOH D 4 .   ? 47.315 8.126  11.100  1.00 48.71 ? 509 HOH A O    1 
HETATM 3652 O  O    . HOH D 4 .   ? 33.717 30.717 3.720   1.00 31.07 ? 510 HOH A O    1 
HETATM 3653 O  O    . HOH D 4 .   ? 25.912 16.458 11.295  1.00 12.48 ? 511 HOH A O    1 
HETATM 3654 O  O    . HOH D 4 .   ? 14.052 18.647 -3.444  1.00 26.79 ? 512 HOH A O    1 
HETATM 3655 O  O    . HOH D 4 .   ? 48.179 7.110  6.482   1.00 36.97 ? 513 HOH A O    1 
HETATM 3656 O  O    . HOH D 4 .   ? 24.608 15.804 -1.080  1.00 18.48 ? 514 HOH A O    1 
HETATM 3657 O  O    . HOH D 4 .   ? 36.695 18.923 29.395  1.00 44.24 ? 515 HOH A O    1 
HETATM 3658 O  O    . HOH D 4 .   ? 24.035 27.806 -9.592  1.00 35.34 ? 516 HOH A O    1 
HETATM 3659 O  O    . HOH D 4 .   ? 8.198  21.615 25.425  1.00 30.25 ? 517 HOH A O    1 
HETATM 3660 O  O    . HOH D 4 .   ? 26.469 18.686 3.777   1.00 8.58  ? 518 HOH A O    1 
HETATM 3661 O  O    . HOH D 4 .   ? 32.306 10.461 0.296   1.00 23.20 ? 519 HOH A O    1 
HETATM 3662 O  O    . HOH D 4 .   ? 30.107 1.331  9.456   1.00 28.81 ? 520 HOH A O    1 
HETATM 3663 O  O    . HOH D 4 .   ? 23.138 17.615 32.197  1.00 26.64 ? 521 HOH A O    1 
HETATM 3664 O  O    . HOH D 4 .   ? 20.256 28.712 -8.832  1.00 21.69 ? 522 HOH A O    1 
HETATM 3665 O  O    . HOH D 4 .   ? 34.728 9.110  23.929  1.00 38.03 ? 523 HOH A O    1 
HETATM 3666 O  O    . HOH D 4 .   ? 14.682 24.547 23.621  1.00 22.71 ? 524 HOH A O    1 
HETATM 3667 O  O    . HOH D 4 .   ? 19.153 23.891 15.024  1.00 13.04 ? 525 HOH A O    1 
HETATM 3668 O  O    . HOH D 4 .   ? 42.973 7.716  11.689  1.00 32.81 ? 526 HOH A O    1 
HETATM 3669 O  O    . HOH D 4 .   ? 13.215 2.995  23.430  1.00 50.26 ? 527 HOH A O    1 
HETATM 3670 O  O    . HOH D 4 .   ? 28.396 9.396  1.140   1.00 21.90 ? 528 HOH A O    1 
HETATM 3671 O  O    . HOH D 4 .   ? 17.692 22.169 1.246   1.00 10.98 ? 529 HOH A O    1 
HETATM 3672 O  O    . HOH D 4 .   ? 8.923  5.606  21.143  1.00 40.16 ? 530 HOH A O    1 
HETATM 3673 O  O    . HOH D 4 .   ? 8.232  22.578 -0.028  1.00 44.75 ? 531 HOH A O    1 
HETATM 3674 O  O    . HOH D 4 .   ? 24.611 15.059 31.543  1.00 18.98 ? 532 HOH A O    1 
HETATM 3675 O  O    . HOH D 4 .   ? 24.287 29.961 12.397  1.00 33.83 ? 533 HOH A O    1 
HETATM 3676 O  O    . HOH D 4 .   ? 22.397 9.353  -2.133  1.00 23.83 ? 534 HOH A O    1 
HETATM 3677 O  O    . HOH D 4 .   ? 13.847 6.827  25.863  1.00 41.11 ? 535 HOH A O    1 
HETATM 3678 O  O    . HOH D 4 .   ? 34.373 27.435 17.869  1.00 26.22 ? 536 HOH A O    1 
HETATM 3679 O  O    . HOH D 4 .   ? 23.675 2.427  18.248  1.00 34.72 ? 537 HOH A O    1 
HETATM 3680 O  O    . HOH D 4 .   ? 48.062 23.144 13.382  1.00 39.28 ? 538 HOH A O    1 
HETATM 3681 O  O    . HOH D 4 .   ? 27.479 26.675 0.501   1.00 14.97 ? 539 HOH A O    1 
HETATM 3682 O  O    . HOH D 4 .   ? 24.841 24.775 13.047  1.00 26.66 ? 540 HOH A O    1 
HETATM 3683 O  O    . HOH D 4 .   ? 29.061 23.785 21.297  1.00 21.94 ? 541 HOH A O    1 
HETATM 3684 O  O    . HOH D 4 .   ? 12.492 24.460 0.142   1.00 34.73 ? 542 HOH A O    1 
HETATM 3685 O  O    . HOH D 4 .   ? 30.874 21.667 29.784  1.00 26.77 ? 543 HOH A O    1 
HETATM 3686 O  O    . HOH D 4 .   ? 36.660 14.417 9.666   1.00 22.65 ? 544 HOH A O    1 
HETATM 3687 O  O    . HOH D 4 .   ? 34.999 10.687 0.848   1.00 21.26 ? 545 HOH A O    1 
HETATM 3688 O  O    . HOH D 4 .   ? 30.220 23.657 -2.211  1.00 23.60 ? 546 HOH A O    1 
HETATM 3689 O  O    . HOH D 4 .   ? 29.816 32.765 3.395   1.00 29.73 ? 547 HOH A O    1 
HETATM 3690 O  O    . HOH D 4 .   ? 6.453  27.051 9.295   1.00 42.24 ? 548 HOH A O    1 
HETATM 3691 O  O    . HOH D 4 .   ? 15.727 30.319 5.873   1.00 28.90 ? 549 HOH A O    1 
HETATM 3692 O  O    . HOH D 4 .   ? 40.631 28.344 13.547  1.00 38.79 ? 550 HOH A O    1 
HETATM 3693 O  O    . HOH D 4 .   ? -0.111 26.890 12.329  1.00 45.83 ? 551 HOH A O    1 
HETATM 3694 O  O    . HOH D 4 .   ? 26.959 19.376 -0.480  1.00 19.80 ? 552 HOH A O    1 
HETATM 3695 O  O    . HOH D 4 .   ? 10.623 26.281 3.184   1.00 24.29 ? 553 HOH A O    1 
HETATM 3696 O  O    . HOH D 4 .   ? 34.278 8.714  16.948  1.00 24.45 ? 554 HOH A O    1 
HETATM 3697 O  O    . HOH D 4 .   ? -2.729 20.713 17.734  1.00 48.84 ? 555 HOH A O    1 
HETATM 3698 O  O    . HOH D 4 .   ? -2.504 19.861 19.526  1.00 51.20 ? 556 HOH A O    1 
HETATM 3699 O  O    . HOH D 4 .   ? 12.541 -3.616 10.508  1.00 48.39 ? 557 HOH A O    1 
HETATM 3700 O  O    . HOH D 4 .   ? 34.489 4.082  15.647  1.00 39.39 ? 558 HOH A O    1 
HETATM 3701 O  O    . HOH D 4 .   ? 34.774 5.679  17.891  1.00 33.13 ? 559 HOH A O    1 
HETATM 3702 O  O    . HOH D 4 .   ? 33.447 10.472 14.270  1.00 17.93 ? 560 HOH A O    1 
HETATM 3703 O  O    . HOH D 4 .   ? 40.395 3.250  2.856   1.00 37.36 ? 561 HOH A O    1 
HETATM 3704 O  O    . HOH D 4 .   ? 52.523 27.642 7.952   1.00 47.90 ? 562 HOH A O    1 
HETATM 3705 O  O    . HOH D 4 .   ? 15.126 28.313 0.972   1.00 32.73 ? 563 HOH A O    1 
HETATM 3706 O  O    . HOH D 4 .   ? 1.852  11.107 -0.624  1.00 49.21 ? 564 HOH A O    1 
HETATM 3707 O  O    . HOH D 4 .   ? 19.663 0.172  5.919   1.00 47.45 ? 565 HOH A O    1 
HETATM 3708 O  O    . HOH D 4 .   ? 35.663 29.334 -1.458  1.00 31.57 ? 566 HOH A O    1 
HETATM 3709 O  O    . HOH D 4 .   ? 32.726 4.807  4.536   1.00 42.15 ? 567 HOH A O    1 
HETATM 3710 O  O    . HOH D 4 .   ? 44.378 15.160 -3.479  1.00 48.66 ? 568 HOH A O    1 
HETATM 3711 O  O    . HOH D 4 .   ? 34.469 28.202 13.782  1.00 38.91 ? 569 HOH A O    1 
HETATM 3712 O  O    . HOH D 4 .   ? 16.135 27.430 23.360  1.00 25.27 ? 570 HOH A O    1 
HETATM 3713 O  O    . HOH D 4 .   ? 46.422 10.551 18.239  1.00 46.61 ? 571 HOH A O    1 
HETATM 3714 O  O    . HOH D 4 .   ? 23.329 23.535 26.508  1.00 21.21 ? 572 HOH A O    1 
HETATM 3715 O  O    . HOH D 4 .   ? 26.212 26.122 -6.393  1.00 39.94 ? 573 HOH A O    1 
HETATM 3716 O  O    . HOH D 4 .   ? 44.748 11.276 -0.475  1.00 38.39 ? 574 HOH A O    1 
HETATM 3717 O  O    . HOH D 4 .   ? 27.180 23.181 27.142  1.00 39.29 ? 575 HOH A O    1 
HETATM 3718 O  O    . HOH D 4 .   ? 22.148 30.959 10.570  1.00 22.34 ? 576 HOH A O    1 
HETATM 3719 O  O    . HOH D 4 .   ? 19.333 31.375 13.928  1.00 35.15 ? 577 HOH A O    1 
HETATM 3720 O  O    . HOH D 4 .   ? 25.741 13.495 10.384  1.00 4.13  ? 578 HOH A O    1 
HETATM 3721 O  O    . HOH D 4 .   ? 37.399 23.856 18.255  1.00 24.43 ? 579 HOH A O    1 
HETATM 3722 O  O    . HOH D 4 .   ? 31.001 27.228 11.897  1.00 31.15 ? 580 HOH A O    1 
HETATM 3723 O  O    . HOH D 4 .   ? 23.137 -0.564 1.310   1.00 37.23 ? 581 HOH A O    1 
HETATM 3724 O  O    . HOH D 4 .   ? 20.192 2.765  20.469  1.00 26.94 ? 582 HOH A O    1 
HETATM 3725 O  O    . HOH D 4 .   ? 20.177 27.380 22.960  1.00 34.81 ? 583 HOH A O    1 
HETATM 3726 O  O    . HOH D 4 .   ? 42.045 28.217 -0.237  1.00 33.76 ? 584 HOH A O    1 
HETATM 3727 O  O    . HOH D 4 .   ? 2.251  8.643  18.442  1.00 46.75 ? 585 HOH A O    1 
HETATM 3728 O  O    . HOH D 4 .   ? 35.154 7.231  9.606   1.00 22.24 ? 586 HOH A O    1 
HETATM 3729 O  O    . HOH D 4 .   ? 20.011 0.320  3.556   1.00 40.93 ? 587 HOH A O    1 
HETATM 3730 O  O    . HOH D 4 .   ? 45.619 29.086 12.603  1.00 47.06 ? 588 HOH A O    1 
HETATM 3731 O  O    . HOH D 4 .   ? 33.741 26.830 8.096   1.00 36.21 ? 589 HOH A O    1 
HETATM 3732 O  O    . HOH D 4 .   ? 30.333 31.085 10.152  1.00 31.07 ? 590 HOH A O    1 
HETATM 3733 O  O    . HOH D 4 .   ? 6.714  28.007 16.499  1.00 43.61 ? 591 HOH A O    1 
HETATM 3734 O  O    . HOH D 4 .   ? 21.619 21.963 28.479  1.00 40.57 ? 592 HOH A O    1 
HETATM 3735 O  O    . HOH D 4 .   ? 48.019 13.006 14.791  1.00 42.80 ? 593 HOH A O    1 
HETATM 3736 O  O    . HOH D 4 .   ? 15.429 15.959 29.724  1.00 41.82 ? 594 HOH A O    1 
HETATM 3737 O  O    . HOH D 4 .   ? 42.764 24.305 -3.674  1.00 43.57 ? 595 HOH A O    1 
HETATM 3738 O  O    . HOH D 4 .   ? 28.009 26.898 12.216  1.00 37.66 ? 596 HOH A O    1 
HETATM 3739 O  O    . HOH D 4 .   ? 19.653 -1.591 4.487   1.00 49.28 ? 597 HOH A O    1 
HETATM 3740 O  O    . HOH D 4 .   ? 28.992 28.786 0.766   1.00 26.18 ? 598 HOH A O    1 
HETATM 3741 O  O    . HOH D 4 .   ? 35.202 26.844 22.000  1.00 38.02 ? 599 HOH A O    1 
HETATM 3742 O  O    . HOH D 4 .   ? 18.198 -0.653 2.392   1.00 48.04 ? 600 HOH A O    1 
HETATM 3743 O  O    . HOH D 4 .   ? 7.872  12.056 1.123   1.00 32.98 ? 601 HOH A O    1 
HETATM 3744 O  O    . HOH D 4 .   ? 18.061 18.987 28.498  1.00 32.78 ? 602 HOH A O    1 
HETATM 3745 O  O    . HOH D 4 .   ? 13.001 30.291 4.557   1.00 43.33 ? 603 HOH A O    1 
HETATM 3746 O  O    . HOH D 4 .   ? 6.368  19.785 26.451  1.00 36.99 ? 604 HOH A O    1 
HETATM 3747 O  O    . HOH D 4 .   ? 13.754 4.735  24.736  1.00 43.36 ? 605 HOH A O    1 
HETATM 3748 O  O    . HOH D 4 .   ? 30.493 -0.275 7.101   1.00 40.30 ? 606 HOH A O    1 
HETATM 3749 O  O    . HOH D 4 .   ? 13.795 7.528  -3.784  1.00 41.95 ? 607 HOH A O    1 
HETATM 3750 O  O    . HOH D 4 .   ? 35.434 10.044 25.916  1.00 37.84 ? 608 HOH A O    1 
HETATM 3751 O  O    . HOH D 4 .   ? 24.888 8.776  -2.158  1.00 28.60 ? 609 HOH A O    1 
HETATM 3752 O  O    . HOH D 4 .   ? 33.402 28.716 8.947   1.00 35.88 ? 610 HOH A O    1 
HETATM 3753 O  O    . HOH D 4 .   ? 49.334 14.090 11.872  1.00 40.02 ? 611 HOH A O    1 
HETATM 3754 O  O    . HOH D 4 .   ? 9.384  14.428 0.377   1.00 37.98 ? 612 HOH A O    1 
HETATM 3755 O  O    . HOH D 4 .   ? 36.079 9.278  14.823  1.00 41.66 ? 613 HOH A O    1 
HETATM 3756 O  O    . HOH D 4 .   ? 36.667 6.895  3.696   1.00 29.85 ? 614 HOH A O    1 
HETATM 3757 O  O    . HOH D 4 .   ? 37.879 30.545 0.000   0.50 35.74 ? 615 HOH A O    1 
HETATM 3758 O  O    . HOH D 4 .   ? 41.924 2.978  0.964   1.00 55.04 ? 616 HOH A O    1 
HETATM 3759 O  O    . HOH D 4 .   ? 39.691 3.351  4.935   1.00 46.80 ? 617 HOH A O    1 
HETATM 3760 O  O    . HOH D 4 .   ? 43.359 30.545 0.000   0.50 42.41 ? 618 HOH A O    1 
HETATM 3761 O  O    . HOH D 4 .   ? 25.997 6.039  25.030  1.00 46.40 ? 619 HOH A O    1 
HETATM 3762 O  O    . HOH D 4 .   ? 33.220 1.077  11.618  1.00 42.65 ? 620 HOH A O    1 
HETATM 3763 O  O    . HOH D 4 .   ? 36.250 26.553 19.423  1.00 28.61 ? 621 HOH A O    1 
HETATM 3764 O  O    . HOH D 4 .   ? 26.302 5.387  22.465  1.00 41.41 ? 622 HOH A O    1 
HETATM 3765 O  O    . HOH D 4 .   ? 27.139 2.349  19.786  1.00 46.95 ? 623 HOH A O    1 
HETATM 3766 O  O    . HOH D 4 .   ? 19.529 27.992 15.489  1.00 21.36 ? 624 HOH A O    1 
HETATM 3767 O  O    . HOH D 4 .   ? 34.708 6.256  6.118   1.00 27.39 ? 625 HOH A O    1 
HETATM 3768 O  O    . HOH D 4 .   ? 48.928 26.138 12.969  1.00 40.11 ? 626 HOH A O    1 
HETATM 3769 O  O    . HOH D 4 .   ? 26.984 8.802  -1.364  1.00 32.61 ? 627 HOH A O    1 
HETATM 3770 O  O    . HOH D 4 .   ? 23.375 -0.217 18.050  1.00 32.27 ? 628 HOH A O    1 
HETATM 3771 O  O    . HOH D 4 .   ? 24.054 18.562 -1.449  1.00 22.68 ? 629 HOH A O    1 
HETATM 3772 O  O    . HOH D 4 .   ? 38.569 7.364  0.389   1.00 44.21 ? 630 HOH A O    1 
HETATM 3773 O  O    . HOH D 4 .   ? 22.852 8.479  25.505  1.00 42.97 ? 631 HOH A O    1 
HETATM 3774 O  O    . HOH D 4 .   ? 7.201  8.048  23.573  1.00 42.40 ? 632 HOH A O    1 
HETATM 3775 O  O    . HOH D 4 .   ? 19.102 6.003  -2.932  1.00 37.24 ? 633 HOH A O    1 
HETATM 3776 O  O    . HOH D 4 .   ? 22.298 4.838  -2.294  1.00 36.11 ? 634 HOH A O    1 
HETATM 3777 O  O    . HOH D 4 .   ? 39.686 10.811 20.169  1.00 36.66 ? 635 HOH A O    1 
HETATM 3778 O  O    . HOH D 4 .   ? 47.954 29.077 14.798  1.00 51.82 ? 636 HOH A O    1 
HETATM 3779 O  O    . HOH D 4 .   ? 28.598 25.967 -2.025  1.00 18.76 ? 637 HOH A O    1 
HETATM 3780 O  O    . HOH D 4 .   ? 34.065 6.419  13.632  1.00 42.40 ? 638 HOH A O    1 
HETATM 3781 O  O    . HOH D 4 .   ? 4.617  27.211 17.410  1.00 39.05 ? 639 HOH A O    1 
HETATM 3782 O  O    . HOH D 4 .   ? 21.178 27.087 13.288  1.00 16.75 ? 640 HOH A O    1 
HETATM 3783 O  O    . HOH D 4 .   ? 16.073 17.634 28.253  1.00 39.25 ? 641 HOH A O    1 
HETATM 3784 O  O    . HOH D 4 .   ? 32.918 6.679  11.616  1.00 30.01 ? 642 HOH A O    1 
HETATM 3785 O  O    . HOH D 4 .   ? 31.957 23.233 -3.989  1.00 40.88 ? 643 HOH A O    1 
HETATM 3786 O  O    . HOH D 4 .   ? 36.003 11.400 -1.672  1.00 24.79 ? 644 HOH A O    1 
HETATM 3787 O  O    . HOH D 4 .   ? -0.111 8.806  9.698   1.00 42.12 ? 645 HOH A O    1 
HETATM 3788 O  O    . HOH D 4 .   ? 21.612 32.925 10.668  1.00 20.03 ? 646 HOH A O    1 
HETATM 3789 O  O    . HOH D 4 .   ? 23.682 27.300 13.506  1.00 30.98 ? 647 HOH A O    1 
HETATM 3790 O  O    . HOH D 4 .   ? 50.452 7.812  3.908   1.00 47.67 ? 648 HOH A O    1 
HETATM 3791 O  O    . HOH D 4 .   ? 5.712  27.155 7.034   1.00 39.63 ? 649 HOH A O    1 
HETATM 3792 O  O    . HOH D 4 .   ? 34.022 29.839 16.113  1.00 35.28 ? 650 HOH A O    1 
HETATM 3793 O  O    . HOH D 4 .   ? 37.617 9.208  -2.713  1.00 38.96 ? 651 HOH A O    1 
HETATM 3794 O  O    . HOH D 4 .   ? 6.604  23.146 25.200  1.00 47.34 ? 652 HOH A O    1 
HETATM 3795 O  O    . HOH D 4 .   ? 7.379  25.712 26.191  1.00 49.94 ? 653 HOH A O    1 
HETATM 3796 O  O    . HOH D 4 .   ? 15.410 15.170 -5.126  1.00 38.32 ? 654 HOH A O    1 
HETATM 3797 O  O    . HOH D 4 .   ? 9.809  30.684 9.375   1.00 46.97 ? 655 HOH A O    1 
HETATM 3798 O  O    . HOH D 4 .   ? 44.798 11.094 -4.540  1.00 47.00 ? 656 HOH A O    1 
HETATM 3799 O  O    . HOH D 4 .   ? 38.241 4.514  0.258   1.00 49.88 ? 657 HOH A O    1 
HETATM 3800 O  O    . HOH D 4 .   ? 20.152 0.114  19.147  1.00 38.77 ? 658 HOH A O    1 
HETATM 3801 O  O    . HOH D 4 .   ? 12.206 16.676 -3.587  1.00 35.50 ? 659 HOH A O    1 
HETATM 3802 O  O    . HOH D 4 .   ? 9.623  22.739 27.370  1.00 43.58 ? 660 HOH A O    1 
HETATM 3803 O  O    . HOH D 4 .   ? 27.252 -0.715 17.065  1.00 43.61 ? 661 HOH A O    1 
HETATM 3804 O  O    . HOH D 4 .   ? 36.113 8.241  1.273   1.00 40.32 ? 662 HOH A O    1 
HETATM 3805 O  O    . HOH D 4 .   ? 7.660  28.912 8.239   1.00 40.29 ? 663 HOH A O    1 
HETATM 3806 O  O    . HOH D 4 .   ? 39.929 23.650 19.261  1.00 31.02 ? 664 HOH A O    1 
HETATM 3807 O  O    . HOH D 4 .   ? 26.282 23.367 -4.625  1.00 27.38 ? 665 HOH A O    1 
HETATM 3808 O  O    . HOH D 4 .   ? 34.763 5.257  8.391   1.00 40.98 ? 666 HOH A O    1 
HETATM 3809 O  O    . HOH D 4 .   ? 0.465  6.529  9.384   1.00 35.27 ? 667 HOH A O    1 
HETATM 3810 O  O    . HOH D 4 .   ? 27.438 10.269 -3.133  1.00 40.48 ? 668 HOH A O    1 
HETATM 3811 O  O    . HOH D 4 .   ? 35.371 3.455  13.543  1.00 46.77 ? 669 HOH A O    1 
HETATM 3812 O  O    . HOH D 4 .   ? 48.238 25.801 20.361  1.00 48.42 ? 670 HOH A O    1 
HETATM 3813 O  O    . HOH D 4 .   ? 5.295  24.878 2.919   1.00 42.70 ? 671 HOH A O    1 
HETATM 3814 O  O    . HOH D 4 .   ? 32.474 8.951  -2.071  1.00 43.02 ? 672 HOH A O    1 
HETATM 3815 O  O    . HOH D 4 .   ? 37.538 7.028  11.807  1.00 35.18 ? 673 HOH A O    1 
HETATM 3816 O  O    . HOH D 4 .   ? 20.047 30.745 16.206  1.00 40.55 ? 674 HOH A O    1 
HETATM 3817 O  O    . HOH D 4 .   ? 12.175 14.127 -3.567  1.00 36.11 ? 675 HOH A O    1 
HETATM 3818 O  O    . HOH D 4 .   ? 33.335 10.976 -2.597  1.00 33.80 ? 676 HOH A O    1 
HETATM 3819 O  O    . HOH D 4 .   ? 16.110 29.908 3.733   1.00 19.82 ? 677 HOH A O    1 
HETATM 3820 O  O    . HOH D 4 .   ? 26.975 23.405 29.239  1.00 44.58 ? 678 HOH A O    1 
HETATM 3821 O  O    . HOH D 4 .   ? 41.449 4.014  9.903   1.00 43.22 ? 679 HOH A O    1 
HETATM 3822 O  O    . HOH D 4 .   ? 14.021 29.500 -0.484  1.00 44.84 ? 680 HOH A O    1 
HETATM 3823 O  O    . HOH D 4 .   ? 47.013 5.993  1.293   1.00 52.92 ? 681 HOH A O    1 
HETATM 3824 O  O    . HOH D 4 .   ? 36.969 8.487  27.463  1.00 41.36 ? 682 HOH A O    1 
HETATM 3825 O  O    . HOH D 4 .   ? 35.604 6.587  14.962  1.00 41.48 ? 683 HOH A O    1 
HETATM 3826 O  O    . HOH D 4 .   ? 24.067 -2.630 18.076  1.00 48.46 ? 684 HOH A O    1 
HETATM 3827 O  O    . HOH D 4 .   ? 1.398  4.458  6.847   1.00 45.35 ? 685 HOH A O    1 
HETATM 3828 O  O    . HOH D 4 .   ? 27.965 21.687 -2.728  1.00 37.88 ? 686 HOH A O    1 
HETATM 3829 O  O    . HOH D 4 .   ? 13.607 30.657 2.453   1.00 30.13 ? 687 HOH A O    1 
HETATM 3830 O  O    . HOH D 4 .   ? 40.504 6.400  11.332  1.00 46.24 ? 688 HOH A O    1 
HETATM 3831 O  O    . HOH D 4 .   ? 38.895 2.564  6.898   1.00 45.30 ? 689 HOH A O    1 
HETATM 3832 O  O    . HOH D 4 .   ? 22.271 29.468 16.881  1.00 42.09 ? 690 HOH A O    1 
HETATM 3833 O  O    . HOH D 4 .   ? 24.157 4.587  25.042  1.00 42.20 ? 691 HOH A O    1 
HETATM 3834 O  O    . HOH D 4 .   ? 22.685 27.477 -12.439 1.00 37.35 ? 692 HOH A O    1 
HETATM 3835 O  O    . HOH D 4 .   ? 26.438 -2.547 18.007  1.00 46.29 ? 693 HOH A O    1 
HETATM 3836 O  O    . HOH D 4 .   ? 9.194  25.747 27.248  1.00 46.99 ? 694 HOH A O    1 
HETATM 3837 O  O    . HOH D 4 .   ? 32.980 -1.273 7.375   1.00 48.34 ? 695 HOH A O    1 
HETATM 3838 O  O    . HOH D 4 .   ? 40.665 25.619 20.662  1.00 36.16 ? 696 HOH A O    1 
HETATM 3839 O  O    . HOH D 4 .   ? 42.140 6.764  22.673  1.00 58.30 ? 697 HOH A O    1 
HETATM 3840 O  O    . HOH D 4 .   ? 44.536 6.541  21.329  1.00 59.22 ? 698 HOH A O    1 
HETATM 3841 O  O    . HOH D 4 .   ? 39.042 27.851 19.700  1.00 33.86 ? 699 HOH A O    1 
HETATM 3842 O  O    . HOH D 4 .   ? 22.322 3.680  24.760  1.00 42.64 ? 700 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   . ALA A 1   ? 0.6698 0.6847 0.6861 0.0169  -0.0265 -0.0072 3   ALA A N   
2    C  CA  . ALA A 1   ? 0.6151 0.6471 0.6394 0.0117  -0.0266 -0.0065 3   ALA A CA  
3    C  C   . ALA A 1   ? 0.6108 0.6582 0.6399 0.0125  -0.0238 -0.0080 3   ALA A C   
4    O  O   . ALA A 1   ? 0.5836 0.6267 0.6104 0.0110  -0.0208 -0.0069 3   ALA A O   
5    C  CB  . ALA A 1   ? 0.5345 0.5612 0.5586 0.0032  -0.0263 -0.0024 3   ALA A CB  
10   N  N   . PRO A 2   ? 0.4862 0.5528 0.5218 0.0150  -0.0248 -0.0108 4   PRO A N   
11   C  CA  . PRO A 2   ? 0.4522 0.5362 0.4921 0.0166  -0.0220 -0.0131 4   PRO A CA  
12   C  C   . PRO A 2   ? 0.3794 0.4693 0.4212 0.0069  -0.0186 -0.0088 4   PRO A C   
13   O  O   . PRO A 2   ? 0.3608 0.4468 0.4030 -0.0016 -0.0195 -0.0044 4   PRO A O   
14   C  CB  . PRO A 2   ? 0.3903 0.4966 0.4381 0.0192  -0.0240 -0.0162 4   PRO A CB  
15   C  CG  . PRO A 2   ? 0.4886 0.5845 0.5341 0.0228  -0.0285 -0.0170 4   PRO A CG  
16   C  CD  . PRO A 2   ? 0.4695 0.5443 0.5089 0.0166  -0.0286 -0.0124 4   PRO A CD  
24   N  N   . PRO A 3   ? 0.3101 0.4088 0.3524 0.0082  -0.0154 -0.0101 5   PRO A N   
25   C  CA  . PRO A 3   ? 0.2776 0.3804 0.3202 -0.0010 -0.0126 -0.0056 5   PRO A CA  
26   C  C   . PRO A 3   ? 0.2601 0.3843 0.3098 -0.0092 -0.0126 -0.0032 5   PRO A C   
27   O  O   . PRO A 3   ? 0.2525 0.3943 0.3067 -0.0056 -0.0122 -0.0066 5   PRO A O   
28   C  CB  . PRO A 3   ? 0.2817 0.3892 0.3224 0.0043  -0.0095 -0.0088 5   PRO A CB  
29   C  CG  . PRO A 3   ? 0.3574 0.4731 0.3997 0.0152  -0.0109 -0.0154 5   PRO A CG  
30   C  CD  . PRO A 3   ? 0.3089 0.4112 0.3496 0.0185  -0.0148 -0.0158 5   PRO A CD  
38   N  N   . GLN A 4   ? 0.2200 0.3391 0.2686 -0.0200 -0.0131 0.0028  6   GLN A N   
39   C  CA  . GLN A 4   ? 0.2280 0.3564 0.2780 -0.0288 -0.0129 0.0064  6   GLN A CA  
40   C  C   . GLN A 4   ? 0.2537 0.3847 0.2996 -0.0350 -0.0097 0.0101  6   GLN A C   
41   O  O   . GLN A 4   ? 0.1822 0.3031 0.2244 -0.0351 -0.0088 0.0113  6   GLN A O   
42   C  CB  . GLN A 4   ? 0.2227 0.3362 0.2708 -0.0353 -0.0172 0.0102  6   GLN A CB  
43   C  CG  . GLN A 4   ? 0.2732 0.3815 0.3235 -0.0292 -0.0210 0.0069  6   GLN A CG  
44   C  CD  . GLN A 4   ? 0.3701 0.4626 0.4173 -0.0346 -0.0255 0.0098  6   GLN A CD  
45   O  OE1 . GLN A 4   ? 0.4368 0.5256 0.4815 -0.0426 -0.0261 0.0137  6   GLN A OE1 
46   N  NE2 . GLN A 4   ? 0.4044 0.4832 0.4489 -0.0286 -0.0281 0.0075  6   GLN A NE2 
55   N  N   . PRO A 5   ? 0.1923 0.3373 0.2382 -0.0403 -0.0082 0.0120  7   PRO A N   
56   C  CA  . PRO A 5   ? 0.1982 0.3469 0.2390 -0.0459 -0.0058 0.0155  7   PRO A CA  
57   C  C   . PRO A 5   ? 0.1739 0.3021 0.2080 -0.0531 -0.0082 0.0214  7   PRO A C   
58   O  O   . PRO A 5   ? 0.2042 0.3182 0.2368 -0.0564 -0.0120 0.0238  7   PRO A O   
59   C  CB  . PRO A 5   ? 0.2108 0.3785 0.2529 -0.0508 -0.0050 0.0166  7   PRO A CB  
60   C  CG  . PRO A 5   ? 0.2299 0.4088 0.2789 -0.0434 -0.0051 0.0110  7   PRO A CG  
61   C  CD  . PRO A 5   ? 0.1912 0.3523 0.2419 -0.0403 -0.0086 0.0102  7   PRO A CD  
69   N  N   . VAL A 6   ? 0.1939 0.3207 0.2231 -0.0545 -0.0064 0.0232  8   VAL A N   
70   C  CA  . VAL A 6   ? 0.2029 0.3114 0.2249 -0.0597 -0.0090 0.0281  8   VAL A CA  
71   C  C   . VAL A 6   ? 0.2221 0.3380 0.2386 -0.0661 -0.0084 0.0319  8   VAL A C   
72   O  O   . VAL A 6   ? 0.2222 0.3579 0.2404 -0.0654 -0.0051 0.0301  8   VAL A O   
73   C  CB  . VAL A 6   ? 0.1701 0.2655 0.1911 -0.0544 -0.0083 0.0263  8   VAL A CB  
74   C  CG1 . VAL A 6   ? 0.1888 0.2779 0.2148 -0.0487 -0.0094 0.0228  8   VAL A CG1 
75   C  CG2 . VAL A 6   ? 0.1884 0.2968 0.2100 -0.0505 -0.0041 0.0234  8   VAL A CG2 
85   N  N   . THR A 7   ? 0.2026 0.3032 0.2122 -0.0716 -0.0122 0.0369  9   THR A N   
86   C  CA  . THR A 7   ? 0.2432 0.3491 0.2468 -0.0782 -0.0129 0.0410  9   THR A CA  
87   C  C   . THR A 7   ? 0.2336 0.3258 0.2313 -0.0778 -0.0143 0.0426  9   THR A C   
88   O  O   . THR A 7   ? 0.2525 0.3514 0.2461 -0.0817 -0.0140 0.0448  9   THR A O   
89   C  CB  . THR A 7   ? 0.2313 0.3341 0.2310 -0.0867 -0.0174 0.0460  9   THR A CB  
90   O  OG1 . THR A 7   ? 0.2747 0.3555 0.2719 -0.0861 -0.0221 0.0472  9   THR A OG1 
91   C  CG2 . THR A 7   ? 0.2787 0.4001 0.2842 -0.0885 -0.0156 0.0448  9   THR A CG2 
99   N  N   . HIS A 8   ? 0.2306 0.3043 0.2280 -0.0730 -0.0160 0.0413  10  HIS A N   
100  C  CA  . HIS A 8   ? 0.2091 0.2689 0.2016 -0.0717 -0.0178 0.0423  10  HIS A CA  
101  C  C   . HIS A 8   ? 0.1934 0.2468 0.1894 -0.0637 -0.0152 0.0380  10  HIS A C   
102  O  O   . HIS A 8   ? 0.1678 0.2171 0.1679 -0.0598 -0.0149 0.0355  10  HIS A O   
103  C  CB  . HIS A 8   ? 0.2371 0.2787 0.2242 -0.0745 -0.0240 0.0454  10  HIS A CB  
104  C  CG  . HIS A 8   ? 0.2812 0.3262 0.2632 -0.0833 -0.0277 0.0504  10  HIS A CG  
105  N  ND1 . HIS A 8   ? 0.2761 0.3321 0.2601 -0.0882 -0.0276 0.0518  10  HIS A ND1 
106  C  CD2 . HIS A 8   ? 0.2917 0.3298 0.2666 -0.0886 -0.0322 0.0543  10  HIS A CD2 
107  C  CE1 . HIS A 8   ? 0.3173 0.3734 0.2951 -0.0966 -0.0317 0.0569  10  HIS A CE1 
108  N  NE2 . HIS A 8   ? 0.3340 0.3789 0.3061 -0.0971 -0.0347 0.0585  10  HIS A NE2 
116  N  N   . LEU A 9   ? 0.1857 0.2388 0.1798 -0.0618 -0.0136 0.0374  11  LEU A N   
117  C  CA  . LEU A 9   ? 0.1505 0.1983 0.1471 -0.0553 -0.0112 0.0339  11  LEU A CA  
118  C  C   . LEU A 9   ? 0.1748 0.2052 0.1671 -0.0536 -0.0144 0.0348  11  LEU A C   
119  O  O   . LEU A 9   ? 0.1820 0.2090 0.1692 -0.0572 -0.0172 0.0377  11  LEU A O   
120  C  CB  . LEU A 9   ? 0.1555 0.2195 0.1542 -0.0533 -0.0063 0.0313  11  LEU A CB  
121  C  CG  . LEU A 9   ? 0.1833 0.2638 0.1885 -0.0502 -0.0027 0.0274  11  LEU A CG  
122  C  CD1 . LEU A 9   ? 0.2258 0.3171 0.2320 -0.0546 -0.0035 0.0290  11  LEU A CD1 
123  C  CD2 . LEU A 9   ? 0.1764 0.2718 0.1827 -0.0462 0.0016  0.0236  11  LEU A CD2 
135  N  N   . ILE A 10  ? 0.1490 0.1694 0.1435 -0.0481 -0.0143 0.0321  12  ILE A N   
136  C  CA  . ILE A 10  ? 0.1357 0.1421 0.1273 -0.0450 -0.0169 0.0318  12  ILE A CA  
137  C  C   . ILE A 10  ? 0.1527 0.1587 0.1465 -0.0403 -0.0138 0.0289  12  ILE A C   
138  O  O   . ILE A 10  ? 0.1226 0.1297 0.1203 -0.0374 -0.0117 0.0265  12  ILE A O   
139  C  CB  . ILE A 10  ? 0.1699 0.1646 0.1614 -0.0428 -0.0205 0.0310  12  ILE A CB  
140  C  CG1 . ILE A 10  ? 0.1964 0.1894 0.1843 -0.0481 -0.0247 0.0342  12  ILE A CG1 
141  C  CG2 . ILE A 10  ? 0.1971 0.1807 0.1870 -0.0383 -0.0226 0.0294  12  ILE A CG2 
142  C  CD1 . ILE A 10  ? 0.2178 0.2014 0.2056 -0.0462 -0.0281 0.0332  12  ILE A CD1 
154  N  N   . PHE A 11  ? 0.1278 0.1317 0.1189 -0.0398 -0.0138 0.0292  13  PHE A N   
155  C  CA  . PHE A 11  ? 0.1195 0.1234 0.1119 -0.0364 -0.0112 0.0270  13  PHE A CA  
156  C  C   . PHE A 11  ? 0.1059 0.0981 0.0976 -0.0325 -0.0136 0.0258  13  PHE A C   
157  O  O   . PHE A 11  ? 0.1362 0.1234 0.1250 -0.0333 -0.0168 0.0274  13  PHE A O   
158  C  CB  . PHE A 11  ? 0.1372 0.1506 0.1266 -0.0391 -0.0091 0.0281  13  PHE A CB  
159  C  CG  . PHE A 11  ? 0.1396 0.1695 0.1304 -0.0413 -0.0053 0.0277  13  PHE A CG  
160  C  CD1 . PHE A 11  ? 0.1498 0.1878 0.1394 -0.0457 -0.0060 0.0299  13  PHE A CD1 
161  C  CD2 . PHE A 11  ? 0.1279 0.1634 0.1211 -0.0347 -0.0023 0.0219  13  PHE A CD2 
162  C  CE1 . PHE A 11  ? 0.1464 0.2024 0.1382 -0.0465 -0.0024 0.0285  13  PHE A CE1 
163  C  CE2 . PHE A 11  ? 0.1472 0.1989 0.1421 -0.0337 0.0007  0.0194  13  PHE A CE2 
164  C  CZ  . PHE A 11  ? 0.1566 0.2214 0.1515 -0.0408 0.0014  0.0234  13  PHE A CZ  
174  N  N   . ASP A 12  ? 0.1234 0.1122 0.1178 -0.0284 -0.0122 0.0231  14  ASP A N   
175  C  CA  . ASP A 12  ? 0.1054 0.0880 0.0999 -0.0251 -0.0132 0.0216  14  ASP A CA  
176  C  C   . ASP A 12  ? 0.1365 0.1216 0.1283 -0.0270 -0.0129 0.0228  14  ASP A C   
177  O  O   . ASP A 12  ? 0.1409 0.1338 0.1313 -0.0288 -0.0106 0.0227  14  ASP A O   
178  C  CB  . ASP A 12  ? 0.1217 0.1021 0.1193 -0.0214 -0.0114 0.0186  14  ASP A CB  
179  C  CG  . ASP A 12  ? 0.1170 0.0937 0.1154 -0.0187 -0.0121 0.0172  14  ASP A CG  
180  O  OD1 . ASP A 12  ? 0.1426 0.1161 0.1407 -0.0176 -0.0147 0.0177  14  ASP A OD1 
181  O  OD2 . ASP A 12  ? 0.1457 0.1227 0.1450 -0.0178 -0.0104 0.0155  14  ASP A OD2 
186  N  N   . MET A 13  ? 0.1139 0.0945 0.1053 -0.0254 -0.0149 0.0225  15  MET A N   
187  C  CA  . MET A 13  ? 0.1115 0.0944 0.1003 -0.0263 -0.0149 0.0227  15  MET A CA  
188  C  C   . MET A 13  ? 0.1024 0.0857 0.0938 -0.0228 -0.0133 0.0187  15  MET A C   
189  O  O   . MET A 13  ? 0.1146 0.1019 0.1048 -0.0221 -0.0111 0.0162  15  MET A O   
190  C  CB  . MET A 13  ? 0.1353 0.1134 0.1214 -0.0273 -0.0192 0.0255  15  MET A CB  
191  C  CG  . MET A 13  ? 0.1323 0.1135 0.1150 -0.0282 -0.0195 0.0255  15  MET A CG  
192  S  SD  . MET A 13  ? 0.1987 0.1731 0.1768 -0.0294 -0.0258 0.0294  15  MET A SD  
193  C  CE  . MET A 13  ? 0.2365 0.2058 0.2206 -0.0237 -0.0281 0.0265  15  MET A CE  
203  N  N   . ASP A 14  ? 0.1041 0.0835 0.0985 -0.0206 -0.0147 0.0178  16  ASP A N   
204  C  CA  . ASP A 14  ? 0.1316 0.1119 0.1279 -0.0191 -0.0138 0.0149  16  ASP A CA  
205  C  C   . ASP A 14  ? 0.1058 0.0860 0.1029 -0.0181 -0.0110 0.0125  16  ASP A C   
206  O  O   . ASP A 14  ? 0.1082 0.0868 0.1072 -0.0171 -0.0100 0.0124  16  ASP A O   
207  C  CB  . ASP A 14  ? 0.1419 0.1210 0.1418 -0.0173 -0.0158 0.0147  16  ASP A CB  
208  C  CG  . ASP A 14  ? 0.1946 0.1730 0.1932 -0.0173 -0.0196 0.0164  16  ASP A CG  
209  O  OD1 . ASP A 14  ? 0.1721 0.1524 0.1683 -0.0187 -0.0204 0.0167  16  ASP A OD1 
210  O  OD2 . ASP A 14  ? 0.2270 0.2020 0.2262 -0.0154 -0.0222 0.0175  16  ASP A OD2 
215  N  N   . GLY A 15  ? 0.1186 0.0996 0.1137 -0.0182 -0.0102 0.0103  17  GLY A N   
216  C  CA  . GLY A 15  ? 0.1198 0.0984 0.1141 -0.0169 -0.0088 0.0078  17  GLY A CA  
217  C  C   . GLY A 15  ? 0.1264 0.1071 0.1188 -0.0153 -0.0073 0.0068  17  GLY A C   
218  O  O   . GLY A 15  ? 0.1637 0.1418 0.1546 -0.0132 -0.0068 0.0042  17  GLY A O   
222  N  N   . LEU A 16  ? 0.1352 0.1207 0.1276 -0.0165 -0.0070 0.0089  18  LEU A N   
223  C  CA  . LEU A 16  ? 0.1142 0.1053 0.1062 -0.0157 -0.0054 0.0084  18  LEU A CA  
224  C  C   . LEU A 16  ? 0.1319 0.1307 0.1204 -0.0168 -0.0049 0.0082  18  LEU A C   
225  O  O   . LEU A 16  ? 0.1393 0.1430 0.1258 -0.0140 -0.0037 0.0048  18  LEU A O   
226  C  CB  . LEU A 16  ? 0.1180 0.1091 0.1129 -0.0172 -0.0056 0.0112  18  LEU A CB  
227  C  CG  . LEU A 16  ? 0.1087 0.1066 0.1045 -0.0168 -0.0041 0.0106  18  LEU A CG  
228  C  CD1 . LEU A 16  ? 0.1542 0.1624 0.1482 -0.0196 -0.0033 0.0120  18  LEU A CD1 
229  C  CD2 . LEU A 16  ? 0.1251 0.1226 0.1208 -0.0121 -0.0032 0.0064  18  LEU A CD2 
241  N  N   . LEU A 17  ? 0.1233 0.1234 0.1105 -0.0203 -0.0060 0.0117  19  LEU A N   
242  C  CA  . LEU A 17  ? 0.1381 0.1455 0.1209 -0.0219 -0.0056 0.0121  19  LEU A CA  
243  C  C   . LEU A 17  ? 0.1346 0.1385 0.1144 -0.0212 -0.0072 0.0106  19  LEU A C   
244  O  O   . LEU A 17  ? 0.1528 0.1623 0.1281 -0.0204 -0.0066 0.0084  19  LEU A O   
245  C  CB  . LEU A 17  ? 0.1507 0.1607 0.1319 -0.0272 -0.0067 0.0176  19  LEU A CB  
246  C  CG  . LEU A 17  ? 0.1632 0.1782 0.1467 -0.0295 -0.0055 0.0195  19  LEU A CG  
247  C  CD1 . LEU A 17  ? 0.2036 0.2186 0.1840 -0.0361 -0.0077 0.0258  19  LEU A CD1 
248  C  CD2 . LEU A 17  ? 0.1593 0.1873 0.1427 -0.0278 -0.0022 0.0164  19  LEU A CD2 
260  N  N   . LEU A 18  ? 0.1453 0.1417 0.1272 -0.0214 -0.0094 0.0114  20  LEU A N   
261  C  CA  . LEU A 18  ? 0.1540 0.1479 0.1341 -0.0211 -0.0113 0.0099  20  LEU A CA  
262  C  C   . LEU A 18  ? 0.1254 0.1134 0.1083 -0.0195 -0.0118 0.0072  20  LEU A C   
263  O  O   . LEU A 18  ? 0.1311 0.1162 0.1182 -0.0192 -0.0113 0.0079  20  LEU A O   
264  C  CB  . LEU A 18  ? 0.1588 0.1507 0.1391 -0.0234 -0.0142 0.0136  20  LEU A CB  
265  C  CG  . LEU A 18  ? 0.1711 0.1664 0.1467 -0.0264 -0.0152 0.0175  20  LEU A CG  
266  C  CD1 . LEU A 18  ? 0.1852 0.1754 0.1607 -0.0275 -0.0194 0.0208  20  LEU A CD1 
267  C  CD2 . LEU A 18  ? 0.1915 0.1929 0.1611 -0.0269 -0.0144 0.0161  20  LEU A CD2 
279  N  N   . ASP A 19  ? 0.1563 0.1425 0.1365 -0.0192 -0.0132 0.0044  21  ASP A N   
280  C  CA  . ASP A 19  ? 0.1487 0.1290 0.1301 -0.0192 -0.0143 0.0022  21  ASP A CA  
281  C  C   . ASP A 19  ? 0.1490 0.1294 0.1349 -0.0216 -0.0160 0.0042  21  ASP A C   
282  O  O   . ASP A 19  ? 0.2055 0.1843 0.1910 -0.0234 -0.0181 0.0029  21  ASP A O   
283  C  CB  . ASP A 19  ? 0.2061 0.1834 0.1816 -0.0182 -0.0159 -0.0019 21  ASP A CB  
284  C  CG  . ASP A 19  ? 0.3698 0.3388 0.3447 -0.0187 -0.0175 -0.0039 21  ASP A CG  
285  O  OD1 . ASP A 19  ? 0.4773 0.4439 0.4561 -0.0198 -0.0166 -0.0022 21  ASP A OD1 
286  O  OD2 . ASP A 19  ? 0.3498 0.3138 0.3192 -0.0182 -0.0201 -0.0073 21  ASP A OD2 
291  N  N   . THR A 20  ? 0.1370 0.1196 0.1272 -0.0215 -0.0156 0.0070  22  THR A N   
292  C  CA  . THR A 20  ? 0.1388 0.1235 0.1334 -0.0223 -0.0175 0.0082  22  THR A CA  
293  C  C   . THR A 20  ? 0.1455 0.1305 0.1450 -0.0227 -0.0165 0.0079  22  THR A C   
294  O  O   . THR A 20  ? 0.1411 0.1305 0.1447 -0.0236 -0.0179 0.0080  22  THR A O   
295  C  CB  . THR A 20  ? 0.1468 0.1328 0.1425 -0.0211 -0.0186 0.0110  22  THR A CB  
296  O  OG1 . THR A 20  ? 0.1672 0.1512 0.1627 -0.0202 -0.0165 0.0119  22  THR A OG1 
297  C  CG2 . THR A 20  ? 0.1822 0.1689 0.1730 -0.0219 -0.0207 0.0124  22  THR A CG2 
305  N  N   . GLU A 21  ? 0.1592 0.1408 0.1582 -0.0223 -0.0142 0.0074  23  GLU A N   
306  C  CA  . GLU A 21  ? 0.1636 0.1460 0.1662 -0.0233 -0.0132 0.0075  23  GLU A CA  
307  C  C   . GLU A 21  ? 0.1520 0.1350 0.1548 -0.0274 -0.0144 0.0067  23  GLU A C   
308  O  O   . GLU A 21  ? 0.1554 0.1439 0.1625 -0.0294 -0.0142 0.0073  23  GLU A O   
309  C  CB  . GLU A 21  ? 0.1697 0.1475 0.1707 -0.0221 -0.0110 0.0074  23  GLU A CB  
310  C  CG  . GLU A 21  ? 0.1591 0.1379 0.1618 -0.0193 -0.0100 0.0086  23  GLU A CG  
311  C  CD  . GLU A 21  ? 0.1810 0.1640 0.1882 -0.0181 -0.0102 0.0093  23  GLU A CD  
312  O  OE1 . GLU A 21  ? 0.1673 0.1549 0.1774 -0.0196 -0.0103 0.0089  23  GLU A OE1 
313  O  OE2 . GLU A 21  ? 0.1724 0.1548 0.1804 -0.0157 -0.0108 0.0101  23  GLU A OE2 
320  N  N   . ARG A 22  ? 0.1593 0.1374 0.1571 -0.0287 -0.0161 0.0052  24  ARG A N   
321  C  CA  . ARG A 22  ? 0.2098 0.1870 0.2070 -0.0334 -0.0183 0.0047  24  ARG A CA  
322  C  C   . ARG A 22  ? 0.1642 0.1509 0.1666 -0.0350 -0.0201 0.0052  24  ARG A C   
323  O  O   . ARG A 22  ? 0.1987 0.1896 0.2038 -0.0391 -0.0210 0.0055  24  ARG A O   
324  C  CB  . ARG A 22  ? 0.2690 0.2370 0.2587 -0.0340 -0.0208 0.0023  24  ARG A CB  
325  C  CG  . ARG A 22  ? 0.2391 0.2080 0.2256 -0.0314 -0.0220 0.0007  24  ARG A CG  
326  C  CD  . ARG A 22  ? 0.2990 0.2595 0.2779 -0.0322 -0.0254 -0.0026 24  ARG A CD  
327  N  NE  . ARG A 22  ? 0.3009 0.2643 0.2764 -0.0291 -0.0259 -0.0042 24  ARG A NE  
328  C  CZ  . ARG A 22  ? 0.2752 0.2432 0.2512 -0.0306 -0.0280 -0.0040 24  ARG A CZ  
329  N  NH1 . ARG A 22  ? 0.3410 0.3116 0.3127 -0.0279 -0.0281 -0.0051 24  ARG A NH1 
330  N  NH2 . ARG A 22  ? 0.2680 0.2388 0.2484 -0.0351 -0.0301 -0.0028 24  ARG A NH2 
344  N  N   . LEU A 23  ? 0.1576 0.1480 0.1610 -0.0316 -0.0207 0.0054  25  LEU A N   
345  C  CA  . LEU A 23  ? 0.1764 0.1755 0.1846 -0.0316 -0.0230 0.0058  25  LEU A CA  
346  C  C   . LEU A 23  ? 0.1610 0.1689 0.1766 -0.0308 -0.0218 0.0065  25  LEU A C   
347  O  O   . LEU A 23  ? 0.1730 0.1902 0.1938 -0.0331 -0.0231 0.0061  25  LEU A O   
348  C  CB  . LEU A 23  ? 0.1616 0.1600 0.1672 -0.0281 -0.0246 0.0064  25  LEU A CB  
349  C  CG  . LEU A 23  ? 0.1567 0.1491 0.1546 -0.0286 -0.0254 0.0053  25  LEU A CG  
350  C  CD1 . LEU A 23  ? 0.1871 0.1802 0.1821 -0.0262 -0.0268 0.0068  25  LEU A CD1 
351  C  CD2 . LEU A 23  ? 0.2047 0.1968 0.2008 -0.0321 -0.0283 0.0034  25  LEU A CD2 
363  N  N   . TYR A 24  ? 0.1767 0.1831 0.1930 -0.0273 -0.0194 0.0071  26  TYR A N   
364  C  CA  . TYR A 24  ? 0.1450 0.1597 0.1674 -0.0258 -0.0180 0.0071  26  TYR A CA  
365  C  C   . TYR A 24  ? 0.1805 0.2001 0.2050 -0.0311 -0.0162 0.0072  26  TYR A C   
366  O  O   . TYR A 24  ? 0.1888 0.2209 0.2194 -0.0319 -0.0160 0.0068  26  TYR A O   
367  C  CB  . TYR A 24  ? 0.1526 0.1625 0.1738 -0.0218 -0.0159 0.0075  26  TYR A CB  
368  C  CG  . TYR A 24  ? 0.1586 0.1651 0.1785 -0.0172 -0.0181 0.0079  26  TYR A CG  
369  C  CD1 . TYR A 24  ? 0.1764 0.1883 0.2000 -0.0128 -0.0206 0.0072  26  TYR A CD1 
370  C  CD2 . TYR A 24  ? 0.1664 0.1641 0.1807 -0.0171 -0.0180 0.0092  26  TYR A CD2 
371  C  CE1 . TYR A 24  ? 0.1857 0.1915 0.2066 -0.0090 -0.0236 0.0081  26  TYR A CE1 
372  C  CE2 . TYR A 24  ? 0.1874 0.1813 0.1996 -0.0144 -0.0203 0.0104  26  TYR A CE2 
373  C  CZ  . TYR A 24  ? 0.2208 0.2173 0.2358 -0.0106 -0.0234 0.0101  26  TYR A CZ  
374  O  OH  . TYR A 24  ? 0.2367 0.2266 0.2481 -0.0084 -0.0267 0.0118  26  TYR A OH  
384  N  N   . SER A 25  ? 0.1569 0.1669 0.1758 -0.0348 -0.0153 0.0078  27  SER A N   
385  C  CA  . SER A 25  ? 0.2090 0.2205 0.2278 -0.0408 -0.0142 0.0088  27  SER A CA  
386  C  C   . SER A 25  ? 0.2026 0.2222 0.2241 -0.0447 -0.0158 0.0085  27  SER A C   
387  O  O   . SER A 25  ? 0.2280 0.2577 0.2534 -0.0475 -0.0144 0.0092  27  SER A O   
388  C  CB  . SER A 25  ? 0.2117 0.2087 0.2218 -0.0408 -0.0137 0.0087  27  SER A CB  
389  O  OG  . SER A 25  ? 0.2577 0.2491 0.2659 -0.0372 -0.0117 0.0089  27  SER A OG  
395  N  N   . VAL A 26  ? 0.2015 0.2168 0.2205 -0.0449 -0.0188 0.0075  28  VAL A N   
396  C  CA  . VAL A 26  ? 0.2199 0.2421 0.2412 -0.0486 -0.0209 0.0071  28  VAL A CA  
397  C  C   . VAL A 26  ? 0.2124 0.2526 0.2434 -0.0478 -0.0211 0.0068  28  VAL A C   
398  O  O   . VAL A 26  ? 0.2325 0.2825 0.2672 -0.0513 -0.0205 0.0071  28  VAL A O   
399  C  CB  . VAL A 26  ? 0.2846 0.2995 0.3012 -0.0485 -0.0245 0.0058  28  VAL A CB  
400  C  CG1 . VAL A 26  ? 0.3258 0.3494 0.3460 -0.0520 -0.0269 0.0053  28  VAL A CG1 
401  C  CG2 . VAL A 26  ? 0.3353 0.3349 0.3427 -0.0491 -0.0248 0.0053  28  VAL A CG2 
411  N  N   . VAL A 27  ? 0.1843 0.2296 0.2194 -0.0428 -0.0223 0.0062  29  VAL A N   
412  C  CA  . VAL A 27  ? 0.2173 0.2794 0.2611 -0.0392 -0.0234 0.0049  29  VAL A CA  
413  C  C   . VAL A 27  ? 0.2301 0.3042 0.2792 -0.0392 -0.0196 0.0049  29  VAL A C   
414  O  O   . VAL A 27  ? 0.2178 0.3076 0.2734 -0.0392 -0.0191 0.0038  29  VAL A O   
415  C  CB  . VAL A 27  ? 0.1769 0.2350 0.2198 -0.0305 -0.0254 0.0039  29  VAL A CB  
416  C  CG1 . VAL A 27  ? 0.1990 0.2714 0.2496 -0.0243 -0.0265 0.0020  29  VAL A CG1 
417  C  CG2 . VAL A 27  ? 0.2281 0.2786 0.2663 -0.0309 -0.0294 0.0040  29  VAL A CG2 
427  N  N   . PHE A 28  ? 0.1937 0.2592 0.2388 -0.0375 -0.0164 0.0057  30  PHE A N   
428  C  CA  . PHE A 28  ? 0.1859 0.2629 0.2349 -0.0376 -0.0127 0.0057  30  PHE A CA  
429  C  C   . PHE A 28  ? 0.2087 0.2881 0.2558 -0.0454 -0.0105 0.0075  30  PHE A C   
430  O  O   . PHE A 28  ? 0.2415 0.3357 0.2931 -0.0459 -0.0082 0.0071  30  PHE A O   
431  C  CB  . PHE A 28  ? 0.1682 0.2344 0.2126 -0.0329 -0.0102 0.0058  30  PHE A CB  
432  C  CG  . PHE A 28  ? 0.1420 0.2062 0.1874 -0.0232 -0.0119 0.0037  30  PHE A CG  
433  C  CD1 . PHE A 28  ? 0.2013 0.2801 0.2535 -0.0174 -0.0132 0.0009  30  PHE A CD1 
434  C  CD2 . PHE A 28  ? 0.1675 0.2155 0.2067 -0.0200 -0.0126 0.0043  30  PHE A CD2 
435  C  CE1 . PHE A 28  ? 0.1828 0.2571 0.2345 -0.0085 -0.0160 -0.0011 30  PHE A CE1 
436  C  CE2 . PHE A 28  ? 0.1746 0.2196 0.2139 -0.0123 -0.0149 0.0029  30  PHE A CE2 
437  C  CZ  . PHE A 28  ? 0.2054 0.2619 0.2502 -0.0066 -0.0170 0.0003  30  PHE A CZ  
447  N  N   . GLN A 29  ? 0.2126 0.2764 0.2519 -0.0502 -0.0114 0.0092  31  GLN A N   
448  C  CA  . GLN A 29  ? 0.2582 0.3211 0.2938 -0.0568 -0.0105 0.0111  31  GLN A CA  
449  C  C   . GLN A 29  ? 0.2761 0.3542 0.3179 -0.0593 -0.0118 0.0105  31  GLN A C   
450  O  O   . GLN A 29  ? 0.3147 0.4042 0.3585 -0.0631 -0.0099 0.0116  31  GLN A O   
451  C  CB  . GLN A 29  ? 0.2752 0.3183 0.3011 -0.0596 -0.0125 0.0123  31  GLN A CB  
452  C  CG  . GLN A 29  ? 0.3799 0.4206 0.4012 -0.0667 -0.0132 0.0145  31  GLN A CG  
453  C  CD  . GLN A 29  ? 0.4312 0.4782 0.4518 -0.0697 -0.0101 0.0167  31  GLN A CD  
454  O  OE1 . GLN A 29  ? 0.4289 0.4786 0.4508 -0.0660 -0.0073 0.0165  31  GLN A OE1 
455  N  NE2 . GLN A 29  ? 0.4839 0.5328 0.5015 -0.0768 -0.0110 0.0191  31  GLN A NE2 
464  N  N   . GLU A 30  ? 0.2719 0.3513 0.3168 -0.0570 -0.0150 0.0087  32  GLU A N   
465  C  CA  . GLU A 30  ? 0.3062 0.3992 0.3569 -0.0590 -0.0168 0.0079  32  GLU A CA  
466  C  C   . GLU A 30  ? 0.2883 0.4028 0.3479 -0.0555 -0.0144 0.0064  32  GLU A C   
467  O  O   . GLU A 30  ? 0.3324 0.4602 0.3953 -0.0593 -0.0134 0.0068  32  GLU A O   
468  C  CB  . GLU A 30  ? 0.3365 0.4262 0.3881 -0.0562 -0.0211 0.0060  32  GLU A CB  
469  C  CG  . GLU A 30  ? 0.3607 0.4619 0.4173 -0.0591 -0.0234 0.0053  32  GLU A CG  
470  C  CD  . GLU A 30  ? 0.4202 0.5193 0.4776 -0.0558 -0.0281 0.0033  32  GLU A CD  
471  O  OE1 . GLU A 30  ? 0.3833 0.4768 0.4395 -0.0499 -0.0294 0.0023  32  GLU A OE1 
472  O  OE2 . GLU A 30  ? 0.4727 0.5762 0.5318 -0.0593 -0.0307 0.0029  32  GLU A OE2 
479  N  N   . ILE A 31  ? 0.2562 0.3744 0.3192 -0.0477 -0.0138 0.0044  33  ILE A N   
480  C  CA  . ILE A 31  ? 0.2280 0.3655 0.2984 -0.0420 -0.0119 0.0019  33  ILE A CA  
481  C  C   . ILE A 31  ? 0.2680 0.4120 0.3365 -0.0461 -0.0071 0.0036  33  ILE A C   
482  O  O   . ILE A 31  ? 0.2636 0.4255 0.3366 -0.0465 -0.0053 0.0026  33  ILE A O   
483  C  CB  . ILE A 31  ? 0.1997 0.3369 0.2727 -0.0316 -0.0133 -0.0009 33  ILE A CB  
484  C  CG1 . ILE A 31  ? 0.2427 0.3762 0.3173 -0.0274 -0.0189 -0.0023 33  ILE A CG1 
485  C  CG2 . ILE A 31  ? 0.2229 0.3772 0.3014 -0.0243 -0.0113 -0.0042 33  ILE A CG2 
486  C  CD1 . ILE A 31  ? 0.2261 0.3553 0.3008 -0.0174 -0.0219 -0.0044 33  ILE A CD1 
498  N  N   . CYS A 32  ? 0.2725 0.4024 0.3338 -0.0492 -0.0052 0.0060  34  CYS A N   
499  C  CA  . CYS A 32  ? 0.2520 0.3862 0.3100 -0.0529 -0.0011 0.0079  34  CYS A CA  
500  C  C   . CYS A 32  ? 0.3248 0.4629 0.3803 -0.0622 -0.0010 0.0107  34  CYS A C   
501  O  O   . CYS A 32  ? 0.3412 0.4932 0.3975 -0.0648 0.0018  0.0114  34  CYS A O   
502  C  CB  . CYS A 32  ? 0.2754 0.3914 0.3257 -0.0538 0.0000  0.0099  34  CYS A CB  
503  S  SG  . CYS A 32  ? 0.2509 0.3670 0.3044 -0.0437 0.0008  0.0069  34  CYS A SG  
509  N  N   . ASN A 33  ? 0.3474 0.4738 0.3996 -0.0671 -0.0043 0.0123  35  ASN A N   
510  C  CA  . ASN A 33  ? 0.3728 0.4997 0.4215 -0.0764 -0.0053 0.0153  35  ASN A CA  
511  C  C   . ASN A 33  ? 0.3693 0.5200 0.4256 -0.0781 -0.0044 0.0143  35  ASN A C   
512  O  O   . ASN A 33  ? 0.4028 0.5600 0.4566 -0.0859 -0.0036 0.0171  35  ASN A O   
513  C  CB  . ASN A 33  ? 0.3714 0.4822 0.4158 -0.0796 -0.0097 0.0159  35  ASN A CB  
514  C  CG  . ASN A 33  ? 0.4355 0.5225 0.4698 -0.0805 -0.0109 0.0176  35  ASN A CG  
515  O  OD1 . ASN A 33  ? 0.4692 0.5508 0.4985 -0.0812 -0.0088 0.0193  35  ASN A OD1 
516  N  ND2 . ASN A 33  ? 0.4930 0.5658 0.5237 -0.0802 -0.0145 0.0168  35  ASN A ND2 
523  N  N   . ARG A 34  ? 0.3064 0.4703 0.3715 -0.0707 -0.0049 0.0104  36  ARG A N   
524  C  CA  . ARG A 34  ? 0.3496 0.5363 0.4222 -0.0715 -0.0047 0.0090  36  ARG A CA  
525  C  C   . ARG A 34  ? 0.3415 0.5458 0.4157 -0.0704 -0.0003 0.0085  36  ARG A C   
526  O  O   . ARG A 34  ? 0.3640 0.5886 0.4426 -0.0729 0.0008  0.0079  36  ARG A O   
527  C  CB  . ARG A 34  ? 0.3027 0.4973 0.3837 -0.0630 -0.0076 0.0047  36  ARG A CB  
528  C  CG  . ARG A 34  ? 0.3429 0.5443 0.4285 -0.0512 -0.0066 0.0005  36  ARG A CG  
529  C  CD  . ARG A 34  ? 0.3292 0.5266 0.4189 -0.0440 -0.0114 -0.0023 36  ARG A CD  
530  N  NE  . ARG A 34  ? 0.2586 0.4613 0.3518 -0.0320 -0.0117 -0.0064 36  ARG A NE  
531  C  CZ  . ARG A 34  ? 0.2330 0.4264 0.3267 -0.0243 -0.0158 -0.0084 36  ARG A CZ  
532  N  NH1 . ARG A 34  ? 0.2561 0.4360 0.3473 -0.0275 -0.0195 -0.0067 36  ARG A NH1 
533  N  NH2 . ARG A 34  ? 0.2756 0.4722 0.3711 -0.0131 -0.0165 -0.0121 36  ARG A NH2 
547  N  N   . TYR A 35  ? 0.3127 0.5092 0.3826 -0.0671 0.0021  0.0086  37  TYR A N   
548  C  CA  . TYR A 35  ? 0.3541 0.5646 0.4236 -0.0662 0.0062  0.0082  37  TYR A CA  
549  C  C   . TYR A 35  ? 0.3389 0.5385 0.3989 -0.0754 0.0076  0.0132  37  TYR A C   
550  O  O   . TYR A 35  ? 0.3741 0.5802 0.4317 -0.0749 0.0108  0.0134  37  TYR A O   
551  C  CB  . TYR A 35  ? 0.2975 0.5083 0.3692 -0.0547 0.0076  0.0041  37  TYR A CB  
552  C  CG  . TYR A 35  ? 0.2728 0.4904 0.3523 -0.0444 0.0050  -0.0009 37  TYR A CG  
553  C  CD1 . TYR A 35  ? 0.2922 0.5320 0.3785 -0.0402 0.0051  -0.0046 37  TYR A CD1 
554  C  CD2 . TYR A 35  ? 0.2736 0.4754 0.3533 -0.0388 0.0020  -0.0021 37  TYR A CD2 
555  C  CE1 . TYR A 35  ? 0.2900 0.5343 0.3825 -0.0299 0.0019  -0.0093 37  TYR A CE1 
556  C  CE2 . TYR A 35  ? 0.2557 0.4621 0.3413 -0.0292 -0.0013 -0.0063 37  TYR A CE2 
557  C  CZ  . TYR A 35  ? 0.2561 0.4828 0.3479 -0.0246 -0.0015 -0.0100 37  TYR A CZ  
558  O  OH  . TYR A 35  ? 0.2510 0.4801 0.3476 -0.0145 -0.0056 -0.0142 37  TYR A OH  
568  N  N   . ASP A 36  ? 0.3507 0.5335 0.4049 -0.0833 0.0047  0.0170  38  ASP A N   
569  C  CA  . ASP A 36  ? 0.3983 0.5675 0.4423 -0.0918 0.0046  0.0218  38  ASP A CA  
570  C  C   . ASP A 36  ? 0.4213 0.5767 0.4597 -0.0877 0.0063  0.0220  38  ASP A C   
571  O  O   . ASP A 36  ? 0.4029 0.5545 0.4344 -0.0927 0.0074  0.0251  38  ASP A O   
572  C  CB  . ASP A 36  ? 0.3858 0.5729 0.4288 -0.0996 0.0065  0.0243  38  ASP A CB  
573  C  CG  . ASP A 36  ? 0.4937 0.6930 0.5409 -0.1057 0.0045  0.0249  38  ASP A CG  
574  O  OD1 . ASP A 36  ? 0.5418 0.7257 0.5856 -0.1103 0.0006  0.0269  38  ASP A OD1 
575  O  OD2 . ASP A 36  ? 0.5379 0.7623 0.5918 -0.1053 0.0067  0.0232  38  ASP A OD2 
580  N  N   . LYS A 37  ? 0.3582 0.5061 0.3996 -0.0789 0.0061  0.0188  39  LYS A N   
581  C  CA  . LYS A 37  ? 0.3405 0.4744 0.3771 -0.0749 0.0072  0.0189  39  LYS A CA  
582  C  C   . LYS A 37  ? 0.3494 0.4595 0.3812 -0.0745 0.0038  0.0196  39  LYS A C   
583  O  O   . LYS A 37  ? 0.3484 0.4558 0.3831 -0.0741 0.0011  0.0185  39  LYS A O   
584  C  CB  . LYS A 37  ? 0.3004 0.4459 0.3437 -0.0648 0.0098  0.0146  39  LYS A CB  
585  C  CG  . LYS A 37  ? 0.3399 0.5106 0.3882 -0.0627 0.0128  0.0124  39  LYS A CG  
586  C  CD  . LYS A 37  ? 0.4002 0.5735 0.4421 -0.0675 0.0156  0.0150  39  LYS A CD  
587  C  CE  . LYS A 37  ? 0.4056 0.6054 0.4518 -0.0661 0.0186  0.0127  39  LYS A CE  
588  N  NZ  . LYS A 37  ? 0.4049 0.6172 0.4572 -0.0537 0.0201  0.0066  39  LYS A NZ  
602  N  N   . LYS A 38  ? 0.3343 0.4276 0.3585 -0.0744 0.0039  0.0212  40  LYS A N   
603  C  CA  . LYS A 38  ? 0.3299 0.4009 0.3486 -0.0731 0.0007  0.0214  40  LYS A CA  
604  C  C   . LYS A 38  ? 0.2982 0.3634 0.3187 -0.0652 0.0018  0.0190  40  LYS A C   
605  O  O   . LYS A 38  ? 0.2935 0.3594 0.3126 -0.0630 0.0043  0.0192  40  LYS A O   
606  C  CB  . LYS A 38  ? 0.3900 0.4448 0.3981 -0.0783 -0.0010 0.0246  40  LYS A CB  
607  C  CG  . LYS A 38  ? 0.4287 0.4614 0.4306 -0.0752 -0.0042 0.0240  40  LYS A CG  
608  C  CD  . LYS A 38  ? 0.4501 0.4677 0.4417 -0.0803 -0.0074 0.0268  40  LYS A CD  
609  C  CE  . LYS A 38  ? 0.5055 0.5034 0.4912 -0.0752 -0.0099 0.0253  40  LYS A CE  
610  N  NZ  . LYS A 38  ? 0.4785 0.4733 0.4677 -0.0705 -0.0112 0.0223  40  LYS A NZ  
624  N  N   . TYR A 39  ? 0.2999 0.3598 0.3231 -0.0616 -0.0004 0.0171  41  TYR A N   
625  C  CA  . TYR A 39  ? 0.2530 0.3061 0.2771 -0.0552 -0.0003 0.0153  41  TYR A CA  
626  C  C   . TYR A 39  ? 0.2804 0.3123 0.2951 -0.0551 -0.0016 0.0165  41  TYR A C   
627  O  O   . TYR A 39  ? 0.2855 0.3052 0.2967 -0.0544 -0.0044 0.0159  41  TYR A O   
628  C  CB  . TYR A 39  ? 0.2350 0.2898 0.2643 -0.0519 -0.0029 0.0131  41  TYR A CB  
629  C  CG  . TYR A 39  ? 0.1966 0.2481 0.2278 -0.0460 -0.0030 0.0117  41  TYR A CG  
630  C  CD1 . TYR A 39  ? 0.2159 0.2775 0.2515 -0.0399 -0.0009 0.0099  41  TYR A CD1 
631  C  CD2 . TYR A 39  ? 0.1874 0.2235 0.2142 -0.0442 -0.0053 0.0115  41  TYR A CD2 
632  C  CE1 . TYR A 39  ? 0.1862 0.2391 0.2204 -0.0316 -0.0016 0.0080  41  TYR A CE1 
633  C  CE2 . TYR A 39  ? 0.1808 0.2116 0.2073 -0.0366 -0.0055 0.0099  41  TYR A CE2 
634  C  CZ  . TYR A 39  ? 0.1952 0.2331 0.2250 -0.0307 -0.0038 0.0085  41  TYR A CZ  
635  O  OH  . TYR A 39  ? 0.1970 0.2269 0.2251 -0.0241 -0.0047 0.0073  41  TYR A OH  
645  N  N   . SER A 40  ? 0.2635 0.2921 0.2741 -0.0551 0.0004  0.0178  42  SER A N   
646  C  CA  . SER A 40  ? 0.2741 0.2846 0.2759 -0.0548 -0.0013 0.0187  42  SER A CA  
647  C  C   . SER A 40  ? 0.2699 0.2719 0.2708 -0.0485 -0.0009 0.0172  42  SER A C   
648  O  O   . SER A 40  ? 0.2478 0.2572 0.2540 -0.0455 0.0007  0.0161  42  SER A O   
649  C  CB  . SER A 40  ? 0.3493 0.3604 0.3462 -0.0588 -0.0002 0.0213  42  SER A CB  
650  O  OG  . SER A 40  ? 0.3276 0.3528 0.3288 -0.0580 0.0036  0.0212  42  SER A OG  
656  N  N   . TRP A 41  ? 0.2630 0.2503 0.2571 -0.0466 -0.0028 0.0171  43  TRP A N   
657  C  CA  . TRP A 41  ? 0.2585 0.2384 0.2514 -0.0407 -0.0025 0.0157  43  TRP A CA  
658  C  C   . TRP A 41  ? 0.2216 0.2065 0.2158 -0.0394 0.0003  0.0164  43  TRP A C   
659  O  O   . TRP A 41  ? 0.2195 0.2033 0.2158 -0.0351 0.0008  0.0152  43  TRP A O   
660  C  CB  . TRP A 41  ? 0.2589 0.2251 0.2450 -0.0385 -0.0051 0.0150  43  TRP A CB  
661  C  CG  . TRP A 41  ? 0.3087 0.2705 0.2947 -0.0363 -0.0073 0.0129  43  TRP A CG  
662  C  CD1 . TRP A 41  ? 0.3315 0.2886 0.3142 -0.0389 -0.0101 0.0127  43  TRP A CD1 
663  C  CD2 . TRP A 41  ? 0.2555 0.2175 0.2443 -0.0315 -0.0069 0.0109  43  TRP A CD2 
664  N  NE1 . TRP A 41  ? 0.3158 0.2703 0.2989 -0.0357 -0.0114 0.0104  43  TRP A NE1 
665  C  CE2 . TRP A 41  ? 0.2814 0.2394 0.2684 -0.0314 -0.0093 0.0094  43  TRP A CE2 
666  C  CE3 . TRP A 41  ? 0.2839 0.2486 0.2759 -0.0277 -0.0051 0.0103  43  TRP A CE3 
667  C  CZ2 . TRP A 41  ? 0.2935 0.2511 0.2815 -0.0280 -0.0096 0.0075  43  TRP A CZ2 
668  C  CZ3 . TRP A 41  ? 0.2527 0.2167 0.2459 -0.0245 -0.0056 0.0087  43  TRP A CZ3 
669  C  CH2 . TRP A 41  ? 0.3022 0.2631 0.2934 -0.0248 -0.0077 0.0074  43  TRP A CH2 
680  N  N   . ASP A 42  ? 0.2949 0.2856 0.2876 -0.0432 0.0020  0.0184  44  ASP A N   
681  C  CA  . ASP A 42  ? 0.3057 0.3023 0.2990 -0.0419 0.0050  0.0189  44  ASP A CA  
682  C  C   . ASP A 42  ? 0.2737 0.2835 0.2751 -0.0380 0.0067  0.0165  44  ASP A C   
683  O  O   . ASP A 42  ? 0.3074 0.3149 0.3095 -0.0311 0.0068  0.0143  44  ASP A O   
684  C  CB  . ASP A 42  ? 0.3628 0.3647 0.3522 -0.0463 0.0067  0.0212  44  ASP A CB  
685  C  CG  . ASP A 42  ? 0.4046 0.4234 0.3987 -0.0511 0.0084  0.0218  44  ASP A CG  
686  O  OD1 . ASP A 42  ? 0.4584 0.4818 0.4575 -0.0518 0.0073  0.0208  44  ASP A OD1 
687  O  OD2 . ASP A 42  ? 0.5174 0.5456 0.5098 -0.0539 0.0108  0.0232  44  ASP A OD2 
692  N  N   . VAL A 43  ? 0.1948 0.2173 0.2023 -0.0404 0.0070  0.0161  45  VAL A N   
693  C  CA  . VAL A 43  ? 0.1977 0.2316 0.2129 -0.0339 0.0071  0.0126  45  VAL A CA  
694  C  C   . VAL A 43  ? 0.1778 0.2008 0.1934 -0.0285 0.0043  0.0109  45  VAL A C   
695  O  O   . VAL A 43  ? 0.1551 0.1782 0.1726 -0.0216 0.0037  0.0086  45  VAL A O   
696  C  CB  . VAL A 43  ? 0.2074 0.2577 0.2291 -0.0379 0.0073  0.0125  45  VAL A CB  
697  C  CG1 . VAL A 43  ? 0.2351 0.2965 0.2640 -0.0299 0.0067  0.0086  45  VAL A CG1 
698  C  CG2 . VAL A 43  ? 0.2791 0.3431 0.3006 -0.0447 0.0105  0.0147  45  VAL A CG2 
708  N  N   . LYS A 44  ? 0.1660 0.1793 0.1791 -0.0318 0.0021  0.0121  46  LYS A N   
709  C  CA  . LYS A 44  ? 0.1833 0.1886 0.1965 -0.0276 -0.0001 0.0108  46  LYS A CA  
710  C  C   . LYS A 44  ? 0.1902 0.1872 0.2006 -0.0226 0.0000  0.0101  46  LYS A C   
711  O  O   . LYS A 44  ? 0.1625 0.1584 0.1747 -0.0181 -0.0013 0.0089  46  LYS A O   
712  C  CB  . LYS A 44  ? 0.2236 0.2198 0.2331 -0.0318 -0.0022 0.0117  46  LYS A CB  
713  C  CG  . LYS A 44  ? 0.2114 0.2035 0.2213 -0.0285 -0.0042 0.0105  46  LYS A CG  
714  C  CD  . LYS A 44  ? 0.2100 0.1954 0.2161 -0.0315 -0.0062 0.0103  46  LYS A CD  
715  C  CE  . LYS A 44  ? 0.2143 0.1969 0.2202 -0.0286 -0.0080 0.0092  46  LYS A CE  
716  N  NZ  . LYS A 44  ? 0.1764 0.1680 0.1874 -0.0276 -0.0093 0.0088  46  LYS A NZ  
730  N  N   . SER A 45  ? 0.1621 0.1534 0.1677 -0.0240 0.0011  0.0113  47  SER A N   
731  C  CA  . SER A 45  ? 0.1565 0.1408 0.1597 -0.0198 0.0010  0.0107  47  SER A CA  
732  C  C   . SER A 45  ? 0.1702 0.1599 0.1763 -0.0147 0.0013  0.0089  47  SER A C   
733  O  O   . SER A 45  ? 0.1660 0.1504 0.1713 -0.0113 0.0002  0.0082  47  SER A O   
734  C  CB  . SER A 45  ? 0.2337 0.2119 0.2310 -0.0217 0.0017  0.0121  47  SER A CB  
735  O  OG  . SER A 45  ? 0.3292 0.3005 0.3225 -0.0256 0.0005  0.0134  47  SER A OG  
741  N  N   . LEU A 46  ? 0.1178 0.1186 0.1272 -0.0142 0.0026  0.0080  48  LEU A N   
742  C  CA  . LEU A 46  ? 0.1244 0.1302 0.1358 -0.0084 0.0024  0.0054  48  LEU A CA  
743  C  C   . LEU A 46  ? 0.1103 0.1154 0.1250 -0.0044 -0.0007 0.0039  48  LEU A C   
744  O  O   . LEU A 46  ? 0.1330 0.1365 0.1477 0.0011  -0.0026 0.0018  48  LEU A O   
745  C  CB  . LEU A 46  ? 0.1408 0.1614 0.1547 -0.0085 0.0048  0.0043  48  LEU A CB  
746  C  CG  . LEU A 46  ? 0.1465 0.1688 0.1561 -0.0137 0.0078  0.0065  48  LEU A CG  
747  C  CD1 . LEU A 46  ? 0.1780 0.2190 0.1912 -0.0147 0.0105  0.0056  48  LEU A CD1 
748  C  CD2 . LEU A 46  ? 0.1744 0.1887 0.1786 -0.0109 0.0079  0.0062  48  LEU A CD2 
760  N  N   . VAL A 47  ? 0.1243 0.1303 0.1413 -0.0067 -0.0018 0.0047  49  VAL A N   
761  C  CA  . VAL A 47  ? 0.1204 0.1275 0.1403 -0.0029 -0.0050 0.0034  49  VAL A CA  
762  C  C   . VAL A 47  ? 0.1203 0.1173 0.1379 -0.0040 -0.0074 0.0051  49  VAL A C   
763  O  O   . VAL A 47  ? 0.1325 0.1268 0.1503 -0.0010 -0.0108 0.0048  49  VAL A O   
764  C  CB  . VAL A 47  ? 0.1214 0.1416 0.1466 -0.0034 -0.0051 0.0024  49  VAL A CB  
765  C  CG1 . VAL A 47  ? 0.1748 0.2076 0.2024 -0.0020 -0.0025 0.0005  49  VAL A CG1 
766  C  CG2 . VAL A 47  ? 0.1431 0.1636 0.1682 -0.0100 -0.0042 0.0046  49  VAL A CG2 
776  N  N   . MET A 48  ? 0.1299 0.1218 0.1448 -0.0082 -0.0061 0.0069  50  MET A N   
777  C  CA  . MET A 48  ? 0.1409 0.1258 0.1535 -0.0089 -0.0079 0.0082  50  MET A CA  
778  C  C   . MET A 48  ? 0.1281 0.1073 0.1391 -0.0061 -0.0098 0.0083  50  MET A C   
779  O  O   . MET A 48  ? 0.1232 0.1007 0.1332 -0.0049 -0.0088 0.0077  50  MET A O   
780  C  CB  . MET A 48  ? 0.1257 0.1066 0.1353 -0.0122 -0.0062 0.0090  50  MET A CB  
781  C  CG  . MET A 48  ? 0.1244 0.1080 0.1343 -0.0156 -0.0058 0.0090  50  MET A CG  
782  S  SD  . MET A 48  ? 0.2133 0.1895 0.2181 -0.0178 -0.0057 0.0090  50  MET A SD  
783  C  CE  . MET A 48  ? 0.1468 0.1210 0.1501 -0.0185 -0.0041 0.0093  50  MET A CE  
793  N  N   . GLY A 49  ? 0.1353 0.1117 0.1456 -0.0055 -0.0128 0.0092  51  GLY A N   
794  C  CA  . GLY A 49  ? 0.1508 0.1204 0.1588 -0.0042 -0.0157 0.0100  51  GLY A CA  
795  C  C   . GLY A 49  ? 0.1480 0.1156 0.1562 0.0007  -0.0194 0.0083  51  GLY A C   
796  O  O   . GLY A 49  ? 0.1633 0.1230 0.1685 0.0014  -0.0234 0.0093  51  GLY A O   
800  N  N   . LYS A 50  ? 0.1340 0.1092 0.1455 0.0038  -0.0186 0.0058  52  LYS A N   
801  C  CA  . LYS A 50  ? 0.1417 0.1173 0.1539 0.0102  -0.0223 0.0031  52  LYS A CA  
802  C  C   . LYS A 50  ? 0.1476 0.1216 0.1596 0.0114  -0.0267 0.0038  52  LYS A C   
803  O  O   . LYS A 50  ? 0.1840 0.1612 0.1971 0.0076  -0.0256 0.0056  52  LYS A O   
804  C  CB  . LYS A 50  ? 0.1557 0.1439 0.1722 0.0130  -0.0191 -0.0002 52  LYS A CB  
805  C  CG  . LYS A 50  ? 0.1635 0.1536 0.1791 0.0129  -0.0154 -0.0012 52  LYS A CG  
806  C  CD  . LYS A 50  ? 0.1809 0.1666 0.1938 0.0189  -0.0180 -0.0042 52  LYS A CD  
807  C  CE  . LYS A 50  ? 0.1860 0.1734 0.1972 0.0177  -0.0142 -0.0046 52  LYS A CE  
808  N  NZ  . LYS A 50  ? 0.2104 0.1933 0.2185 0.0242  -0.0174 -0.0081 52  LYS A NZ  
822  N  N   . LYS A 51  ? 0.1823 0.1511 0.1926 0.0173  -0.0322 0.0019  53  LYS A N   
823  C  CA  . LYS A 51  ? 0.1918 0.1589 0.2016 0.0199  -0.0374 0.0020  53  LYS A CA  
824  C  C   . LYS A 51  ? 0.1567 0.1396 0.1733 0.0224  -0.0349 -0.0009 53  LYS A C   
825  O  O   . LYS A 51  ? 0.1657 0.1598 0.1866 0.0233  -0.0304 -0.0034 53  LYS A O   
826  C  CB  . LYS A 51  ? 0.2240 0.1833 0.2291 0.0249  -0.0423 -0.0007 53  LYS A CB  
827  C  CG  . LYS A 51  ? 0.2438 0.1916 0.2420 0.0206  -0.0435 0.0011  53  LYS A CG  
828  C  CD  . LYS A 51  ? 0.3264 0.2674 0.3200 0.0251  -0.0490 -0.0020 53  LYS A CD  
829  C  CE  . LYS A 51  ? 0.3314 0.2620 0.3187 0.0206  -0.0515 -0.0004 53  LYS A CE  
830  N  NZ  . LYS A 51  ? 0.4304 0.3512 0.4116 0.0235  -0.0586 -0.0025 53  LYS A NZ  
844  N  N   . ALA A 52  ? 0.1830 0.1681 0.2006 0.0231  -0.0381 -0.0004 54  ALA A N   
845  C  CA  . ALA A 52  ? 0.1656 0.1670 0.1902 0.0233  -0.0357 -0.0024 54  ALA A CA  
846  C  C   . ALA A 52  ? 0.1657 0.1803 0.1956 0.0305  -0.0351 -0.0076 54  ALA A C   
847  O  O   . ALA A 52  ? 0.1838 0.2132 0.2192 0.0279  -0.0299 -0.0087 54  ALA A O   
848  C  CB  . ALA A 52  ? 0.2146 0.2155 0.2389 0.0238  -0.0404 -0.0012 54  ALA A CB  
854  N  N   . LEU A 53  ? 0.2138 0.2229 0.2415 0.0392  -0.0407 -0.0108 55  LEU A N   
855  C  CA  . LEU A 53  ? 0.2164 0.2387 0.2481 0.0466  -0.0398 -0.0165 55  LEU A CA  
856  C  C   . LEU A 53  ? 0.2090 0.2369 0.2417 0.0457  -0.0342 -0.0178 55  LEU A C   
857  O  O   . LEU A 53  ? 0.1914 0.2377 0.2297 0.0475  -0.0301 -0.0210 55  LEU A O   
858  C  CB  . LEU A 53  ? 0.2762 0.2873 0.3009 0.0527  -0.0447 -0.0195 55  LEU A CB  
859  C  CG  . LEU A 53  ? 0.2530 0.2650 0.2778 0.0554  -0.0490 -0.0203 55  LEU A CG  
860  C  CD1 . LEU A 53  ? 0.3342 0.3302 0.3503 0.0598  -0.0551 -0.0223 55  LEU A CD1 
861  C  CD2 . LEU A 53  ? 0.2865 0.3216 0.3201 0.0594  -0.0465 -0.0245 55  LEU A CD2 
873  N  N   . GLU A 54  ? 0.1946 0.2073 0.2212 0.0416  -0.0335 -0.0148 56  GLU A N   
874  C  CA  . GLU A 54  ? 0.1703 0.1855 0.1961 0.0395  -0.0283 -0.0152 56  GLU A CA  
875  C  C   . GLU A 54  ? 0.1420 0.1698 0.1721 0.0315  -0.0211 -0.0127 56  GLU A C   
876  O  O   . GLU A 54  ? 0.1664 0.2069 0.1988 0.0313  -0.0165 -0.0145 56  GLU A O   
877  C  CB  . GLU A 54  ? 0.2045 0.2009 0.2233 0.0359  -0.0297 -0.0119 56  GLU A CB  
878  C  CG  . GLU A 54  ? 0.2158 0.1980 0.2283 0.0410  -0.0360 -0.0137 56  GLU A CG  
879  C  CD  . GLU A 54  ? 0.2594 0.2257 0.2654 0.0343  -0.0367 -0.0096 56  GLU A CD  
880  O  OE1 . GLU A 54  ? 0.2341 0.1978 0.2408 0.0279  -0.0347 -0.0051 56  GLU A OE1 
881  O  OE2 . GLU A 54  ? 0.3123 0.2699 0.3124 0.0351  -0.0395 -0.0110 56  GLU A OE2 
888  N  N   . ALA A 55  ? 0.1584 0.1817 0.1883 0.0245  -0.0205 -0.0085 57  ALA A N   
889  C  CA  . ALA A 55  ? 0.1515 0.1832 0.1841 0.0165  -0.0152 -0.0061 57  ALA A CA  
890  C  C   . ALA A 55  ? 0.1363 0.1880 0.1757 0.0173  -0.0134 -0.0085 57  ALA A C   
891  O  O   . ALA A 55  ? 0.1517 0.2138 0.1929 0.0129  -0.0087 -0.0080 57  ALA A O   
892  C  CB  . ALA A 55  ? 0.1608 0.1845 0.1917 0.0109  -0.0162 -0.0025 57  ALA A CB  
898  N  N   . ALA A 56  ? 0.1483 0.2059 0.1914 0.0225  -0.0175 -0.0108 58  ALA A N   
899  C  CA  . ALA A 56  ? 0.1455 0.2246 0.1963 0.0237  -0.0163 -0.0135 58  ALA A CA  
900  C  C   . ALA A 56  ? 0.1261 0.2204 0.1794 0.0277  -0.0129 -0.0172 58  ALA A C   
901  O  O   . ALA A 56  ? 0.1506 0.2622 0.2083 0.0224  -0.0082 -0.0168 58  ALA A O   
902  C  CB  . ALA A 56  ? 0.1564 0.2376 0.2100 0.0307  -0.0226 -0.0160 58  ALA A CB  
908  N  N   . GLN A 57  ? 0.1447 0.2317 0.1942 0.0360  -0.0151 -0.0205 59  GLN A N   
909  C  CA  . GLN A 57  ? 0.1542 0.2552 0.2050 0.0408  -0.0121 -0.0246 59  GLN A CA  
910  C  C   . GLN A 57  ? 0.1515 0.2548 0.1998 0.0320  -0.0054 -0.0211 59  GLN A C   
911  O  O   . GLN A 57  ? 0.1491 0.2715 0.2006 0.0304  -0.0008 -0.0223 59  GLN A O   
912  C  CB  . GLN A 57  ? 0.1801 0.2688 0.2256 0.0514  -0.0169 -0.0289 59  GLN A CB  
913  C  CG  . GLN A 57  ? 0.2060 0.3060 0.2494 0.0565  -0.0143 -0.0338 59  GLN A CG  
914  C  CD  . GLN A 57  ? 0.2473 0.3663 0.2948 0.0591  -0.0136 -0.0372 59  GLN A CD  
915  O  OE1 . GLN A 57  ? 0.2787 0.3932 0.3250 0.0653  -0.0189 -0.0402 59  GLN A OE1 
916  N  NE2 . GLN A 57  ? 0.2368 0.3766 0.2887 0.0534  -0.0074 -0.0363 59  GLN A NE2 
925  N  N   . ILE A 58  ? 0.1512 0.2355 0.1936 0.0259  -0.0050 -0.0166 60  ILE A N   
926  C  CA  . ILE A 58  ? 0.1204 0.2044 0.1596 0.0177  0.0002  -0.0130 60  ILE A CA  
927  C  C   . ILE A 58  ? 0.1360 0.2327 0.1790 0.0082  0.0038  -0.0098 60  ILE A C   
928  O  O   . ILE A 58  ? 0.1523 0.2608 0.1950 0.0035  0.0083  -0.0087 60  ILE A O   
929  C  CB  . ILE A 58  ? 0.1348 0.1963 0.1674 0.0142  -0.0009 -0.0094 60  ILE A CB  
930  C  CG1 . ILE A 58  ? 0.1462 0.1965 0.1744 0.0220  -0.0041 -0.0123 60  ILE A CG1 
931  C  CG2 . ILE A 58  ? 0.1523 0.2118 0.1812 0.0055  0.0035  -0.0053 60  ILE A CG2 
932  C  CD1 . ILE A 58  ? 0.1505 0.1803 0.1736 0.0195  -0.0065 -0.0092 60  ILE A CD1 
944  N  N   . ILE A 59  ? 0.1400 0.2345 0.1859 0.0049  0.0015  -0.0080 61  ILE A N   
945  C  CA  . ILE A 59  ? 0.1402 0.2457 0.1895 -0.0046 0.0037  -0.0051 61  ILE A CA  
946  C  C   . ILE A 59  ? 0.1357 0.2681 0.1918 -0.0039 0.0065  -0.0077 61  ILE A C   
947  O  O   . ILE A 59  ? 0.1774 0.3207 0.2337 -0.0126 0.0104  -0.0049 61  ILE A O   
948  C  CB  . ILE A 59  ? 0.1394 0.2389 0.1906 -0.0067 0.0001  -0.0038 61  ILE A CB  
949  C  CG1 . ILE A 59  ? 0.1417 0.2175 0.1857 -0.0087 -0.0015 -0.0010 61  ILE A CG1 
950  C  CG2 . ILE A 59  ? 0.1684 0.2815 0.2238 -0.0161 0.0016  -0.0016 61  ILE A CG2 
951  C  CD1 . ILE A 59  ? 0.1517 0.2203 0.1963 -0.0081 -0.0058 -0.0006 61  ILE A CD1 
963  N  N   . ILE A 60  ? 0.1217 0.2637 0.1825 0.0065  0.0040  -0.0130 62  ILE A N   
964  C  CA  . ILE A 60  ? 0.1512 0.3154 0.2164 0.0091  0.0058  -0.0163 62  ILE A CA  
965  C  C   . ILE A 60  ? 0.1693 0.3403 0.2302 0.0080  0.0106  -0.0165 62  ILE A C   
966  O  O   . ILE A 60  ? 0.1796 0.3633 0.2401 0.0014  0.0138  -0.0148 62  ILE A O   
967  C  CB  . ILE A 60  ? 0.1615 0.3275 0.2288 0.0218  0.0011  -0.0223 62  ILE A CB  
968  C  CG1 . ILE A 60  ? 0.1486 0.3123 0.2199 0.0211  -0.0031 -0.0215 62  ILE A CG1 
969  C  CG2 . ILE A 60  ? 0.1900 0.3744 0.2578 0.0261  0.0031  -0.0265 62  ILE A CG2 
970  C  CD1 . ILE A 60  ? 0.1955 0.3500 0.2658 0.0330  -0.0095 -0.0258 62  ILE A CD1 
982  N  N   . ASP A 61  ? 0.1727 0.3346 0.2296 0.0141  0.0106  -0.0184 63  ASP A N   
983  C  CA  . ASP A 61  ? 0.1759 0.3433 0.2276 0.0140  0.0146  -0.0189 63  ASP A CA  
984  C  C   . ASP A 61  ? 0.1941 0.3595 0.2417 0.0008  0.0190  -0.0123 63  ASP A C   
985  O  O   . ASP A 61  ? 0.2260 0.4011 0.2703 -0.0038 0.0222  -0.0110 63  ASP A O   
986  C  CB  . ASP A 61  ? 0.2165 0.3717 0.2638 0.0239  0.0128  -0.0227 63  ASP A CB  
987  C  CG  . ASP A 61  ? 0.2255 0.3787 0.2732 0.0368  0.0073  -0.0293 63  ASP A CG  
988  O  OD1 . ASP A 61  ? 0.2788 0.4457 0.3298 0.0389  0.0066  -0.0318 63  ASP A OD1 
989  O  OD2 . ASP A 61  ? 0.2376 0.3743 0.2811 0.0445  0.0033  -0.0318 63  ASP A OD2 
994  N  N   . VAL A 62  ? 0.1762 0.3239 0.2211 -0.0052 0.0180  -0.0079 64  VAL A N   
995  C  CA  . VAL A 62  ? 0.1845 0.3254 0.2234 -0.0172 0.0208  -0.0015 64  VAL A CA  
996  C  C   . VAL A 62  ? 0.2317 0.3796 0.2713 -0.0272 0.0211  0.0021  64  VAL A C   
997  O  O   . VAL A 62  ? 0.2374 0.3859 0.2713 -0.0345 0.0229  0.0056  64  VAL A O   
998  C  CB  . VAL A 62  ? 0.1937 0.3060 0.2262 -0.0193 0.0176  0.0017  64  VAL A CB  
999  C  CG1 . VAL A 62  ? 0.2788 0.3827 0.3046 -0.0311 0.0192  0.0078  64  VAL A CG1 
1000 C  CG2 . VAL A 62  ? 0.1845 0.2830 0.2127 -0.0101 0.0160  -0.0012 64  VAL A CG2 
1010 N  N   . LEU A 63  ? 0.2316 0.3831 0.2772 -0.0269 0.0184  0.0011  65  LEU A N   
1011 C  CA  . LEU A 63  ? 0.2323 0.3891 0.2785 -0.0354 0.0179  0.0039  65  LEU A CA  
1012 C  C   . LEU A 63  ? 0.2440 0.4242 0.2954 -0.0324 0.0189  0.0006  65  LEU A C   
1013 O  O   . LEU A 63  ? 0.2987 0.4863 0.3507 -0.0396 0.0188  0.0028  65  LEU A O   
1014 C  CB  . LEU A 63  ? 0.2071 0.3528 0.2553 -0.0382 0.0142  0.0053  65  LEU A CB  
1015 C  CG  . LEU A 63  ? 0.2286 0.3509 0.2698 -0.0428 0.0129  0.0090  65  LEU A CG  
1016 C  CD1 . LEU A 63  ? 0.2173 0.3305 0.2603 -0.0445 0.0090  0.0095  65  LEU A CD1 
1017 C  CD2 . LEU A 63  ? 0.2617 0.3756 0.2942 -0.0513 0.0139  0.0135  65  LEU A CD2 
1029 N  N   . GLN A 64  ? 0.2045 0.3952 0.2588 -0.0217 0.0195  -0.0049 66  GLN A N   
1030 C  CA  . GLN A 64  ? 0.2519 0.4642 0.3105 -0.0169 0.0201  -0.0091 66  GLN A CA  
1031 C  C   . GLN A 64  ? 0.2747 0.4941 0.3395 -0.0178 0.0174  -0.0098 66  GLN A C   
1032 O  O   . GLN A 64  ? 0.2829 0.5175 0.3497 -0.0230 0.0184  -0.0090 66  GLN A O   
1033 C  CB  . GLN A 64  ? 0.3264 0.5511 0.3809 -0.0241 0.0236  -0.0067 66  GLN A CB  
1034 C  CG  . GLN A 64  ? 0.5000 0.7494 0.5582 -0.0186 0.0246  -0.0115 66  GLN A CG  
1035 C  CD  . GLN A 64  ? 0.5476 0.7999 0.6063 -0.0042 0.0238  -0.0186 66  GLN A CD  
1036 O  OE1 . GLN A 64  ? 0.4553 0.6984 0.5089 -0.0013 0.0249  -0.0189 66  GLN A OE1 
1037 N  NE2 . GLN A 64  ? 0.4597 0.7233 0.5236 0.0051  0.0213  -0.0245 66  GLN A NE2 
1046 N  N   . LEU A 65  ? 0.2032 0.4117 0.2712 -0.0126 0.0138  -0.0113 67  LEU A N   
1047 C  CA  . LEU A 65  ? 0.2217 0.4354 0.2955 -0.0120 0.0107  -0.0124 67  LEU A CA  
1048 C  C   . LEU A 65  ? 0.2467 0.4756 0.3248 -0.0007 0.0093  -0.0189 67  LEU A C   
1049 O  O   . LEU A 65  ? 0.2343 0.4606 0.3107 0.0096  0.0084  -0.0233 67  LEU A O   
1050 C  CB  . LEU A 65  ? 0.1970 0.3930 0.2716 -0.0101 0.0067  -0.0116 67  LEU A CB  
1051 C  CG  . LEU A 65  ? 0.1660 0.3441 0.2357 -0.0199 0.0071  -0.0059 67  LEU A CG  
1052 C  CD1 . LEU A 65  ? 0.1633 0.3281 0.2346 -0.0177 0.0025  -0.0059 67  LEU A CD1 
1053 C  CD2 . LEU A 65  ? 0.2313 0.4117 0.2983 -0.0319 0.0087  -0.0014 67  LEU A CD2 
1065 N  N   . PRO A 66  ? 0.2418 0.4855 0.3249 -0.0022 0.0084  -0.0198 68  PRO A N   
1066 C  CA  . PRO A 66  ? 0.2808 0.5413 0.3676 0.0081  0.0071  -0.0263 68  PRO A CA  
1067 C  C   . PRO A 66  ? 0.2469 0.4987 0.3363 0.0187  0.0013  -0.0303 68  PRO A C   
1068 O  O   . PRO A 66  ? 0.2563 0.5195 0.3505 0.0222  -0.0010 -0.0331 68  PRO A O   
1069 C  CB  . PRO A 66  ? 0.2674 0.5475 0.3580 -0.0003 0.0089  -0.0245 68  PRO A CB  
1070 C  CG  . PRO A 66  ? 0.2451 0.5130 0.3357 -0.0113 0.0079  -0.0185 68  PRO A CG  
1071 C  CD  . PRO A 66  ? 0.2493 0.4957 0.3338 -0.0143 0.0088  -0.0150 68  PRO A CD  
1079 N  N   . MET A 67  ? 0.2205 0.4517 0.3065 0.0233  -0.0013 -0.0301 69  MET A N   
1080 C  CA  . MET A 67  ? 0.2492 0.4682 0.3357 0.0326  -0.0075 -0.0329 69  MET A CA  
1081 C  C   . MET A 67  ? 0.2519 0.4549 0.3326 0.0424  -0.0101 -0.0360 69  MET A C   
1082 O  O   . MET A 67  ? 0.2777 0.4777 0.3546 0.0413  -0.0069 -0.0354 69  MET A O   
1083 C  CB  . MET A 67  ? 0.2930 0.4993 0.3810 0.0259  -0.0101 -0.0281 69  MET A CB  
1084 C  CG  . MET A 67  ? 0.2761 0.4694 0.3609 0.0166  -0.0078 -0.0226 69  MET A CG  
1085 S  SD  . MET A 67  ? 0.3176 0.5043 0.4043 0.0060  -0.0099 -0.0175 69  MET A SD  
1086 C  CE  . MET A 67  ? 0.2977 0.4786 0.3862 0.0163  -0.0173 -0.0207 69  MET A CE  
1096 N  N   . SER A 68  ? 0.2202 0.4116 0.2993 0.0515  -0.0164 -0.0389 70  SER A N   
1097 C  CA  . SER A 68  ? 0.2032 0.3746 0.2751 0.0594  -0.0202 -0.0409 70  SER A CA  
1098 C  C   . SER A 68  ? 0.1913 0.3423 0.2610 0.0547  -0.0224 -0.0357 70  SER A C   
1099 O  O   . SER A 68  ? 0.1884 0.3403 0.2618 0.0476  -0.0224 -0.0317 70  SER A O   
1100 C  CB  . SER A 68  ? 0.2638 0.4298 0.3326 0.0709  -0.0266 -0.0465 70  SER A CB  
1101 O  OG  . SER A 68  ? 0.2530 0.4095 0.3228 0.0707  -0.0315 -0.0444 70  SER A OG  
1107 N  N   . LYS A 69  ? 0.2309 0.3635 0.2938 0.0584  -0.0244 -0.0358 71  LYS A N   
1108 C  CA  . LYS A 69  ? 0.1924 0.3062 0.2524 0.0544  -0.0267 -0.0311 71  LYS A CA  
1109 C  C   . LYS A 69  ? 0.2078 0.3104 0.2663 0.0560  -0.0330 -0.0298 71  LYS A C   
1110 O  O   . LYS A 69  ? 0.2071 0.3023 0.2657 0.0501  -0.0341 -0.0253 71  LYS A O   
1111 C  CB  . LYS A 69  ? 0.2086 0.3047 0.2609 0.0576  -0.0279 -0.0315 71  LYS A CB  
1112 C  CG  . LYS A 69  ? 0.2754 0.3589 0.3205 0.0667  -0.0334 -0.0358 71  LYS A CG  
1113 C  CD  . LYS A 69  ? 0.2409 0.3063 0.2780 0.0678  -0.0346 -0.0355 71  LYS A CD  
1114 C  CE  . LYS A 69  ? 0.3501 0.3988 0.3785 0.0748  -0.0415 -0.0389 71  LYS A CE  
1115 N  NZ  . LYS A 69  ? 0.4211 0.4820 0.4492 0.0832  -0.0423 -0.0460 71  LYS A NZ  
1129 N  N   . GLU A 70  ? 0.2396 0.3411 0.2959 0.0641  -0.0373 -0.0340 72  GLU A N   
1130 C  CA  . GLU A 70  ? 0.2507 0.3419 0.3049 0.0657  -0.0434 -0.0328 72  GLU A CA  
1131 C  C   . GLU A 70  ? 0.2316 0.3375 0.2936 0.0600  -0.0421 -0.0306 72  GLU A C   
1132 O  O   . GLU A 70  ? 0.2143 0.3112 0.2750 0.0562  -0.0451 -0.0267 72  GLU A O   
1133 C  CB  . GLU A 70  ? 0.3139 0.4028 0.3643 0.0759  -0.0483 -0.0386 72  GLU A CB  
1134 C  CG  . GLU A 70  ? 0.2754 0.3452 0.3161 0.0809  -0.0517 -0.0407 72  GLU A CG  
1135 C  CD  . GLU A 70  ? 0.3302 0.4090 0.3708 0.0839  -0.0477 -0.0448 72  GLU A CD  
1136 O  OE1 . GLU A 70  ? 0.3119 0.4134 0.3597 0.0829  -0.0421 -0.0466 72  GLU A OE1 
1137 O  OE2 . GLU A 70  ? 0.3678 0.4305 0.4005 0.0864  -0.0502 -0.0459 72  GLU A OE2 
1144 N  N   . GLU A 71  ? 0.1959 0.3245 0.2652 0.0585  -0.0374 -0.0328 73  GLU A N   
1145 C  CA  . GLU A 71  ? 0.2226 0.3658 0.2991 0.0515  -0.0357 -0.0306 73  GLU A CA  
1146 C  C   . GLU A 71  ? 0.1853 0.3244 0.2625 0.0406  -0.0332 -0.0250 73  GLU A C   
1147 O  O   . GLU A 71  ? 0.1836 0.3210 0.2621 0.0356  -0.0354 -0.0221 73  GLU A O   
1148 C  CB  . GLU A 71  ? 0.2442 0.4121 0.3269 0.0509  -0.0308 -0.0338 73  GLU A CB  
1149 C  CG  . GLU A 71  ? 0.2500 0.4269 0.3337 0.0611  -0.0341 -0.0399 73  GLU A CG  
1150 C  CD  . GLU A 71  ? 0.2890 0.4898 0.3768 0.0620  -0.0291 -0.0438 73  GLU A CD  
1151 O  OE1 . GLU A 71  ? 0.2589 0.4675 0.3474 0.0554  -0.0231 -0.0419 73  GLU A OE1 
1152 O  OE2 . GLU A 71  ? 0.3068 0.5193 0.3967 0.0693  -0.0315 -0.0489 73  GLU A OE2 
1159 N  N   . LEU A 72  ? 0.2110 0.3473 0.2865 0.0371  -0.0290 -0.0236 74  LEU A N   
1160 C  CA  . LEU A 72  ? 0.1486 0.2807 0.2240 0.0268  -0.0266 -0.0189 74  LEU A CA  
1161 C  C   . LEU A 72  ? 0.1470 0.2590 0.2168 0.0273  -0.0318 -0.0163 74  LEU A C   
1162 O  O   . LEU A 72  ? 0.1690 0.2760 0.2374 0.0195  -0.0319 -0.0128 74  LEU A O   
1163 C  CB  . LEU A 72  ? 0.1784 0.3125 0.2527 0.0235  -0.0209 -0.0182 74  LEU A CB  
1164 C  CG  . LEU A 72  ? 0.1421 0.2679 0.2133 0.0122  -0.0175 -0.0131 74  LEU A CG  
1165 C  CD1 . LEU A 72  ? 0.1577 0.2914 0.2325 0.0030  -0.0172 -0.0106 74  LEU A CD1 
1166 C  CD2 . LEU A 72  ? 0.1599 0.2884 0.2292 0.0083  -0.0115 -0.0121 74  LEU A CD2 
1178 N  N   . VAL A 73  ? 0.1545 0.2510 0.2181 0.0352  -0.0357 -0.0175 75  VAL A N   
1179 C  CA  . VAL A 73  ? 0.1838 0.2596 0.2402 0.0347  -0.0408 -0.0143 75  VAL A CA  
1180 C  C   . VAL A 73  ? 0.1985 0.2750 0.2552 0.0343  -0.0451 -0.0134 75  VAL A C   
1181 O  O   . VAL A 73  ? 0.2015 0.2697 0.2549 0.0284  -0.0464 -0.0098 75  VAL A O   
1182 C  CB  . VAL A 73  ? 0.1857 0.2430 0.2338 0.0414  -0.0443 -0.0149 75  VAL A CB  
1183 C  CG1 . VAL A 73  ? 0.2659 0.3030 0.3056 0.0394  -0.0492 -0.0108 75  VAL A CG1 
1184 C  CG2 . VAL A 73  ? 0.1751 0.2287 0.2217 0.0403  -0.0403 -0.0149 75  VAL A CG2 
1194 N  N   . GLU A 74  ? 0.2084 0.2932 0.2677 0.0404  -0.0469 -0.0166 76  GLU A N   
1195 C  CA  . GLU A 74  ? 0.2439 0.3286 0.3030 0.0405  -0.0513 -0.0157 76  GLU A CA  
1196 C  C   . GLU A 74  ? 0.1802 0.2764 0.2447 0.0315  -0.0492 -0.0136 76  GLU A C   
1197 O  O   . GLU A 74  ? 0.2285 0.3167 0.2892 0.0277  -0.0523 -0.0107 76  GLU A O   
1198 C  CB  . GLU A 74  ? 0.2958 0.3900 0.3579 0.0486  -0.0533 -0.0203 76  GLU A CB  
1199 C  CG  . GLU A 74  ? 0.3530 0.4472 0.4149 0.0498  -0.0584 -0.0197 76  GLU A CG  
1200 C  CD  . GLU A 74  ? 0.5114 0.6195 0.5784 0.0573  -0.0600 -0.0249 76  GLU A CD  
1201 O  OE1 . GLU A 74  ? 0.5470 0.6597 0.6146 0.0637  -0.0585 -0.0294 76  GLU A OE1 
1202 O  OE2 . GLU A 74  ? 0.6059 0.7205 0.6758 0.0571  -0.0629 -0.0248 76  GLU A OE2 
1209 N  N   . GLU A 75  ? 0.2555 0.3694 0.3275 0.0273  -0.0439 -0.0149 77  GLU A N   
1210 C  CA  . GLU A 75  ? 0.2584 0.3813 0.3344 0.0175  -0.0420 -0.0128 77  GLU A CA  
1211 C  C   . GLU A 75  ? 0.2384 0.3493 0.3093 0.0099  -0.0415 -0.0094 77  GLU A C   
1212 O  O   . GLU A 75  ? 0.2773 0.3837 0.3457 0.0047  -0.0435 -0.0074 77  GLU A O   
1213 C  CB  . GLU A 75  ? 0.2926 0.4339 0.3754 0.0129  -0.0361 -0.0140 77  GLU A CB  
1214 C  CG  . GLU A 75  ? 0.3285 0.4747 0.4132 0.0015  -0.0343 -0.0114 77  GLU A CG  
1215 C  CD  . GLU A 75  ? 0.3430 0.5068 0.4333 -0.0033 -0.0293 -0.0120 77  GLU A CD  
1216 O  OE1 . GLU A 75  ? 0.3522 0.5257 0.4446 0.0016  -0.0263 -0.0145 77  GLU A OE1 
1217 O  OE2 . GLU A 75  ? 0.3574 0.5249 0.4488 -0.0121 -0.0285 -0.0101 77  GLU A OE2 
1224 N  N   . SER A 76  ? 0.2199 0.3208 0.2863 0.0090  -0.0375 -0.0082 78  SER A N   
1225 C  CA  . SER A 76  ? 0.1896 0.2743 0.2484 0.0011  -0.0345 -0.0042 78  SER A CA  
1226 C  C   . SER A 76  ? 0.2220 0.2894 0.2727 0.0026  -0.0388 -0.0021 78  SER A C   
1227 O  O   . SER A 76  ? 0.2007 0.2614 0.2471 -0.0036 -0.0385 0.0002  78  SER A O   
1228 C  CB  . SER A 76  ? 0.1998 0.2785 0.2558 -0.0002 -0.0292 -0.0034 78  SER A CB  
1229 O  OG  . SER A 76  ? 0.1875 0.2582 0.2407 0.0077  -0.0307 -0.0046 78  SER A OG  
1235 N  N   . GLN A 77  ? 0.2240 0.2843 0.2720 0.0106  -0.0432 -0.0028 79  GLN A N   
1236 C  CA  . GLN A 77  ? 0.2472 0.2914 0.2866 0.0111  -0.0476 0.0000  79  GLN A CA  
1237 C  C   . GLN A 77  ? 0.2999 0.3487 0.3399 0.0095  -0.0517 0.0002  79  GLN A C   
1238 O  O   . GLN A 77  ? 0.3206 0.3595 0.3535 0.0054  -0.0528 0.0031  79  GLN A O   
1239 C  CB  . GLN A 77  ? 0.2821 0.3166 0.3178 0.0194  -0.0527 -0.0006 79  GLN A CB  
1240 C  CG  . GLN A 77  ? 0.3077 0.3336 0.3405 0.0202  -0.0495 -0.0002 79  GLN A CG  
1241 C  CD  . GLN A 77  ? 0.3162 0.3287 0.3415 0.0132  -0.0466 0.0041  79  GLN A CD  
1242 O  OE1 . GLN A 77  ? 0.3498 0.3529 0.3686 0.0109  -0.0497 0.0072  79  GLN A OE1 
1243 N  NE2 . GLN A 77  ? 0.2843 0.2970 0.3104 0.0097  -0.0407 0.0042  79  GLN A NE2 
1252 N  N   . THR A 78  ? 0.2520 0.3174 0.3004 0.0126  -0.0538 -0.0030 80  THR A N   
1253 C  CA  . THR A 78  ? 0.2816 0.3524 0.3310 0.0114  -0.0583 -0.0030 80  THR A CA  
1254 C  C   . THR A 78  ? 0.2940 0.3637 0.3412 0.0014  -0.0549 -0.0011 80  THR A C   
1255 O  O   . THR A 78  ? 0.3167 0.3797 0.3582 -0.0011 -0.0580 0.0006  80  THR A O   
1256 C  CB  . THR A 78  ? 0.2761 0.3650 0.3343 0.0151  -0.0583 -0.0060 80  THR A CB  
1257 O  OG1 . THR A 78  ? 0.3677 0.4529 0.4245 0.0246  -0.0606 -0.0077 80  THR A OG1 
1258 C  CG2 . THR A 78  ? 0.3170 0.4108 0.3756 0.0126  -0.0619 -0.0054 80  THR A CG2 
1266 N  N   . LYS A 79  ? 0.2467 0.3218 0.2975 -0.0042 -0.0489 -0.0013 81  LYS A N   
1267 C  CA  . LYS A 79  ? 0.2775 0.3493 0.3253 -0.0133 -0.0462 0.0002  81  LYS A CA  
1268 C  C   . LYS A 79  ? 0.2817 0.3352 0.3191 -0.0152 -0.0445 0.0027  81  LYS A C   
1269 O  O   . LYS A 79  ? 0.2780 0.3256 0.3100 -0.0198 -0.0452 0.0035  81  LYS A O   
1270 C  CB  . LYS A 79  ? 0.2874 0.3690 0.3409 -0.0188 -0.0412 -0.0004 81  LYS A CB  
1271 C  CG  . LYS A 79  ? 0.2795 0.3820 0.3435 -0.0186 -0.0421 -0.0028 81  LYS A CG  
1272 C  CD  . LYS A 79  ? 0.3652 0.4741 0.4323 -0.0248 -0.0364 -0.0025 81  LYS A CD  
1273 C  CE  . LYS A 79  ? 0.4037 0.5300 0.4791 -0.0246 -0.0359 -0.0043 81  LYS A CE  
1274 N  NZ  . LYS A 79  ? 0.4461 0.5786 0.5228 -0.0317 -0.0305 -0.0031 81  LYS A NZ  
1288 N  N   . LEU A 80  ? 0.2105 0.2559 0.2451 -0.0119 -0.0423 0.0036  82  LEU A N   
1289 C  CA  . LEU A 80  ? 0.2531 0.2840 0.2790 -0.0139 -0.0401 0.0059  82  LEU A CA  
1290 C  C   . LEU A 80  ? 0.2262 0.2489 0.2446 -0.0128 -0.0443 0.0078  82  LEU A C   
1291 O  O   . LEU A 80  ? 0.2336 0.2482 0.2447 -0.0160 -0.0427 0.0093  82  LEU A O   
1292 C  CB  . LEU A 80  ? 0.2326 0.2585 0.2582 -0.0112 -0.0370 0.0064  82  LEU A CB  
1293 C  CG  . LEU A 80  ? 0.1916 0.2228 0.2216 -0.0141 -0.0320 0.0054  82  LEU A CG  
1294 C  CD1 . LEU A 80  ? 0.2144 0.2440 0.2456 -0.0097 -0.0302 0.0051  82  LEU A CD1 
1295 C  CD2 . LEU A 80  ? 0.2320 0.2561 0.2571 -0.0198 -0.0290 0.0063  82  LEU A CD2 
1307 N  N   . LYS A 81  ? 0.3157 0.3410 0.3353 -0.0081 -0.0497 0.0076  83  LYS A N   
1308 C  CA  . LYS A 81  ? 0.3700 0.3864 0.3812 -0.0072 -0.0542 0.0102  83  LYS A CA  
1309 C  C   . LYS A 81  ? 0.3452 0.3620 0.3519 -0.0122 -0.0545 0.0103  83  LYS A C   
1310 O  O   . LYS A 81  ? 0.3827 0.3917 0.3805 -0.0137 -0.0557 0.0127  83  LYS A O   
1311 C  CB  . LYS A 81  ? 0.4564 0.4747 0.4694 -0.0005 -0.0611 0.0097  83  LYS A CB  
1312 C  CG  . LYS A 81  ? 0.4589 0.4871 0.4755 0.0001  -0.0645 0.0077  83  LYS A CG  
1313 C  CD  . LYS A 81  ? 0.4665 0.4961 0.4842 0.0080  -0.0688 0.0065  83  LYS A CD  
1314 C  CE  . LYS A 81  ? 0.4651 0.5121 0.4921 0.0098  -0.0702 0.0031  83  LYS A CE  
1315 N  NZ  . LYS A 81  ? 0.4731 0.5227 0.5020 0.0181  -0.0741 0.0016  83  LYS A NZ  
1329 N  N   . GLU A 82  ? 0.2775 0.3035 0.2901 -0.0151 -0.0536 0.0077  84  GLU A N   
1330 C  CA  . GLU A 82  ? 0.3345 0.3605 0.3430 -0.0196 -0.0548 0.0070  84  GLU A CA  
1331 C  C   . GLU A 82  ? 0.3154 0.3335 0.3175 -0.0236 -0.0503 0.0072  84  GLU A C   
1332 O  O   . GLU A 82  ? 0.3264 0.3411 0.3217 -0.0260 -0.0514 0.0067  84  GLU A O   
1333 C  CB  . GLU A 82  ? 0.4346 0.4727 0.4514 -0.0224 -0.0560 0.0043  84  GLU A CB  
1334 C  CG  . GLU A 82  ? 0.4622 0.5122 0.4877 -0.0176 -0.0593 0.0030  84  GLU A CG  
1335 C  CD  . GLU A 82  ? 0.6328 0.6965 0.6663 -0.0209 -0.0590 0.0002  84  GLU A CD  
1336 O  OE1 . GLU A 82  ? 0.6630 0.7404 0.7059 -0.0175 -0.0598 -0.0017 84  GLU A OE1 
1337 O  OE2 . GLU A 82  ? 0.7694 0.8301 0.7995 -0.0266 -0.0581 -0.0004 84  GLU A OE2 
1344 N  N   . VAL A 83  ? 0.2287 0.2443 0.2326 -0.0237 -0.0455 0.0073  85  VAL A N   
1345 C  CA  . VAL A 83  ? 0.2231 0.2321 0.2216 -0.0267 -0.0416 0.0067  85  VAL A CA  
1346 C  C   . VAL A 83  ? 0.1851 0.1874 0.1787 -0.0249 -0.0386 0.0088  85  VAL A C   
1347 O  O   . VAL A 83  ? 0.2028 0.2008 0.1904 -0.0262 -0.0364 0.0082  85  VAL A O   
1348 C  CB  . VAL A 83  ? 0.2180 0.2290 0.2214 -0.0299 -0.0389 0.0050  85  VAL A CB  
1349 C  CG1 . VAL A 83  ? 0.2597 0.2767 0.2663 -0.0338 -0.0422 0.0033  85  VAL A CG1 
1350 C  CG2 . VAL A 83  ? 0.2102 0.2254 0.2208 -0.0279 -0.0364 0.0057  85  VAL A CG2 
1360 N  N   . PHE A 84  ? 0.1899 0.1916 0.1855 -0.0219 -0.0390 0.0109  86  PHE A N   
1361 C  CA  . PHE A 84  ? 0.1976 0.1933 0.1888 -0.0214 -0.0367 0.0132  86  PHE A CA  
1362 C  C   . PHE A 84  ? 0.2049 0.1975 0.1867 -0.0232 -0.0369 0.0149  86  PHE A C   
1363 O  O   . PHE A 84  ? 0.2076 0.1984 0.1861 -0.0242 -0.0333 0.0153  86  PHE A O   
1364 C  CB  . PHE A 84  ? 0.2039 0.1975 0.1971 -0.0180 -0.0390 0.0154  86  PHE A CB  
1365 C  CG  . PHE A 84  ? 0.2171 0.2125 0.2173 -0.0157 -0.0368 0.0140  86  PHE A CG  
1366 C  CD1 . PHE A 84  ? 0.2022 0.1987 0.2050 -0.0175 -0.0321 0.0124  86  PHE A CD1 
1367 C  CD2 . PHE A 84  ? 0.2141 0.2090 0.2171 -0.0113 -0.0402 0.0144  86  PHE A CD2 
1368 C  CE1 . PHE A 84  ? 0.2102 0.2085 0.2184 -0.0154 -0.0302 0.0116  86  PHE A CE1 
1369 C  CE2 . PHE A 84  ? 0.2380 0.2350 0.2465 -0.0086 -0.0383 0.0128  86  PHE A CE2 
1370 C  CZ  . PHE A 84  ? 0.2206 0.2197 0.2315 -0.0109 -0.0331 0.0116  86  PHE A CZ  
1380 N  N   . PRO A 85  ? 0.2149 0.2081 0.1925 -0.0235 -0.0411 0.0157  87  PRO A N   
1381 C  CA  . PRO A 85  ? 0.2332 0.2249 0.2011 -0.0255 -0.0409 0.0175  87  PRO A CA  
1382 C  C   . PRO A 85  ? 0.2143 0.2079 0.1787 -0.0269 -0.0373 0.0141  87  PRO A C   
1383 O  O   . PRO A 85  ? 0.2536 0.2482 0.2105 -0.0281 -0.0358 0.0153  87  PRO A O   
1384 C  CB  . PRO A 85  ? 0.2685 0.2606 0.2330 -0.0252 -0.0466 0.0186  87  PRO A CB  
1385 C  CG  . PRO A 85  ? 0.2916 0.2838 0.2632 -0.0222 -0.0503 0.0189  87  PRO A CG  
1386 C  CD  . PRO A 85  ? 0.2235 0.2194 0.2044 -0.0216 -0.0463 0.0156  87  PRO A CD  
1394 N  N   . THR A 86  ? 0.2156 0.2097 0.1845 -0.0267 -0.0362 0.0102  88  THR A N   
1395 C  CA  . THR A 86  ? 0.2390 0.2322 0.2042 -0.0270 -0.0341 0.0064  88  THR A CA  
1396 C  C   . THR A 86  ? 0.2534 0.2452 0.2197 -0.0260 -0.0295 0.0056  88  THR A C   
1397 O  O   . THR A 86  ? 0.2611 0.2513 0.2243 -0.0251 -0.0282 0.0019  88  THR A O   
1398 C  CB  . THR A 86  ? 0.2736 0.2658 0.2419 -0.0283 -0.0364 0.0030  88  THR A CB  
1399 O  OG1 . THR A 86  ? 0.2638 0.2557 0.2402 -0.0288 -0.0350 0.0030  88  THR A OG1 
1400 C  CG2 . THR A 86  ? 0.2890 0.2843 0.2583 -0.0293 -0.0414 0.0036  88  THR A CG2 
1408 N  N   . ALA A 87  ? 0.2415 0.2335 0.2119 -0.0256 -0.0279 0.0088  89  ALA A N   
1409 C  CA  . ALA A 87  ? 0.2496 0.2408 0.2216 -0.0246 -0.0239 0.0083  89  ALA A CA  
1410 C  C   . ALA A 87  ? 0.2521 0.2462 0.2172 -0.0239 -0.0215 0.0065  89  ALA A C   
1411 O  O   . ALA A 87  ? 0.2559 0.2539 0.2155 -0.0250 -0.0220 0.0082  89  ALA A O   
1412 C  CB  . ALA A 87  ? 0.2606 0.2514 0.2360 -0.0247 -0.0234 0.0123  89  ALA A CB  
1418 N  N   . ALA A 88  ? 0.2154 0.2082 0.1806 -0.0218 -0.0194 0.0028  90  ALA A N   
1419 C  CA  . ALA A 88  ? 0.1952 0.1926 0.1549 -0.0196 -0.0171 0.0000  90  ALA A CA  
1420 C  C   . ALA A 88  ? 0.1619 0.1628 0.1245 -0.0186 -0.0136 0.0011  90  ALA A C   
1421 O  O   . ALA A 88  ? 0.1603 0.1570 0.1286 -0.0186 -0.0131 0.0022  90  ALA A O   
1422 C  CB  . ALA A 88  ? 0.2731 0.2657 0.2293 -0.0168 -0.0184 -0.0058 90  ALA A CB  
1428 N  N   . LEU A 89  ? 0.1965 0.2062 0.1555 -0.0179 -0.0112 0.0006  91  LEU A N   
1429 C  CA  . LEU A 89  ? 0.1894 0.2048 0.1511 -0.0171 -0.0081 0.0011  91  LEU A CA  
1430 C  C   . LEU A 89  ? 0.1708 0.1826 0.1339 -0.0121 -0.0076 -0.0041 91  LEU A C   
1431 O  O   . LEU A 89  ? 0.2147 0.2235 0.1736 -0.0084 -0.0090 -0.0093 91  LEU A O   
1432 C  CB  . LEU A 89  ? 0.2146 0.2434 0.1719 -0.0181 -0.0056 0.0016  91  LEU A CB  
1433 C  CG  . LEU A 89  ? 0.2174 0.2487 0.1730 -0.0244 -0.0063 0.0085  91  LEU A CG  
1434 C  CD1 . LEU A 89  ? 0.2891 0.3346 0.2381 -0.0261 -0.0041 0.0088  91  LEU A CD1 
1435 C  CD2 . LEU A 89  ? 0.2552 0.2845 0.2161 -0.0277 -0.0060 0.0133  91  LEU A CD2 
1447 N  N   . MET A 90  ? 0.1687 0.1791 0.1371 -0.0119 -0.0064 -0.0028 92  MET A N   
1448 C  CA  . MET A 90  ? 0.1784 0.1838 0.1478 -0.0073 -0.0065 -0.0070 92  MET A CA  
1449 C  C   . MET A 90  ? 0.1958 0.2111 0.1623 -0.0022 -0.0048 -0.0118 92  MET A C   
1450 O  O   . MET A 90  ? 0.1870 0.2154 0.1535 -0.0036 -0.0023 -0.0103 92  MET A O   
1451 C  CB  . MET A 90  ? 0.1602 0.1619 0.1356 -0.0086 -0.0058 -0.0040 92  MET A CB  
1452 C  CG  . MET A 90  ? 0.1704 0.1632 0.1485 -0.0116 -0.0075 -0.0012 92  MET A CG  
1453 S  SD  . MET A 90  ? 0.1879 0.1688 0.1639 -0.0105 -0.0103 -0.0044 92  MET A SD  
1454 C  CE  . MET A 90  ? 0.2128 0.1890 0.1909 -0.0078 -0.0095 -0.0053 92  MET A CE  
1464 N  N   . PRO A 91  ? 0.1791 0.1880 0.1433 0.0037  -0.0065 -0.0173 93  PRO A N   
1465 C  CA  . PRO A 91  ? 0.2408 0.2597 0.2027 0.0102  -0.0054 -0.0228 93  PRO A CA  
1466 C  C   . PRO A 91  ? 0.2200 0.2523 0.1873 0.0099  -0.0020 -0.0209 93  PRO A C   
1467 O  O   . PRO A 91  ? 0.1986 0.2263 0.1710 0.0077  -0.0019 -0.0176 93  PRO A O   
1468 C  CB  . PRO A 91  ? 0.2885 0.2936 0.2471 0.0163  -0.0091 -0.0281 93  PRO A CB  
1469 C  CG  . PRO A 91  ? 0.3017 0.2913 0.2590 0.0119  -0.0121 -0.0258 93  PRO A CG  
1470 C  CD  . PRO A 91  ? 0.2193 0.2121 0.1826 0.0045  -0.0098 -0.0187 93  PRO A CD  
1478 N  N   . GLY A 92  ? 0.2097 0.2598 0.1760 0.0116  0.0006  -0.0229 94  GLY A N   
1479 C  CA  . GLY A 92  ? 0.2040 0.2697 0.1758 0.0099  0.0038  -0.0207 94  GLY A CA  
1480 C  C   . GLY A 92  ? 0.2130 0.2847 0.1877 0.0003  0.0057  -0.0127 94  GLY A C   
1481 O  O   . GLY A 92  ? 0.1971 0.2841 0.1752 -0.0023 0.0082  -0.0107 94  GLY A O   
1485 N  N   . ALA A 93  ? 0.1672 0.2272 0.1404 -0.0051 0.0041  -0.0080 95  ALA A N   
1486 C  CA  . ALA A 93  ? 0.1698 0.2316 0.1447 -0.0136 0.0046  -0.0004 95  ALA A CA  
1487 C  C   . ALA A 93  ? 0.1870 0.2660 0.1587 -0.0181 0.0070  0.0022  95  ALA A C   
1488 O  O   . ALA A 93  ? 0.1879 0.2757 0.1620 -0.0240 0.0082  0.0069  95  ALA A O   
1489 C  CB  . ALA A 93  ? 0.1824 0.2288 0.1562 -0.0168 0.0017  0.0031  95  ALA A CB  
1495 N  N   . GLU A 94  ? 0.2159 0.2990 0.1814 -0.0162 0.0073  -0.0006 96  GLU A N   
1496 C  CA  . GLU A 94  ? 0.2353 0.3356 0.1963 -0.0207 0.0098  0.0017  96  GLU A CA  
1497 C  C   . GLU A 94  ? 0.2273 0.3485 0.1921 -0.0191 0.0133  -0.0007 96  GLU A C   
1498 O  O   . GLU A 94  ? 0.2190 0.3496 0.1870 -0.0259 0.0139  0.0044  96  GLU A O   
1499 C  CB  . GLU A 94  ? 0.3049 0.4065 0.2581 -0.0171 0.0094  -0.0024 96  GLU A CB  
1500 C  CG  . GLU A 94  ? 0.2998 0.3849 0.2494 -0.0196 0.0058  0.0004  96  GLU A CG  
1501 C  CD  . GLU A 94  ? 0.4696 0.5590 0.4106 -0.0176 0.0055  -0.0029 96  GLU A CD  
1502 O  OE1 . GLU A 94  ? 0.5253 0.6295 0.4655 -0.0157 0.0082  -0.0055 96  GLU A OE1 
1503 O  OE2 . GLU A 94  ? 0.5151 0.5910 0.4533 -0.0175 0.0020  -0.0029 96  GLU A OE2 
1510 N  N   . LYS A 95  ? 0.2169 0.3418 0.1833 -0.0096 0.0140  -0.0087 97  LYS A N   
1511 C  CA  . LYS A 95  ? 0.2482 0.3909 0.2208 -0.0061 0.0158  -0.0120 97  LYS A CA  
1512 C  C   . LYS A 95  ? 0.2117 0.3592 0.1910 -0.0131 0.0163  -0.0062 97  LYS A C   
1513 O  O   . LYS A 95  ? 0.2522 0.4144 0.2349 -0.0179 0.0169  -0.0035 97  LYS A O   
1514 C  CB  . LYS A 95  ? 0.2374 0.3774 0.2103 0.0060  0.0147  -0.0214 97  LYS A CB  
1515 C  CG  . LYS A 95  ? 0.3409 0.4996 0.3201 0.0110  0.0155  -0.0254 97  LYS A CG  
1516 C  CD  . LYS A 95  ? 0.3766 0.5293 0.3561 0.0235  0.0128  -0.0342 97  LYS A CD  
1517 C  CE  . LYS A 95  ? 0.4248 0.5973 0.4098 0.0286  0.0127  -0.0381 97  LYS A CE  
1518 N  NZ  . LYS A 95  ? 0.4613 0.6254 0.4465 0.0403  0.0089  -0.0455 97  LYS A NZ  
1532 N  N   . LEU A 96  ? 0.2175 0.3511 0.1984 -0.0142 0.0152  -0.0040 98  LEU A N   
1533 C  CA  . LEU A 96  ? 0.2167 0.3528 0.2038 -0.0201 0.0152  0.0010  98  LEU A CA  
1534 C  C   . LEU A 96  ? 0.1977 0.3321 0.1839 -0.0315 0.0134  0.0096  98  LEU A C   
1535 O  O   . LEU A 96  ? 0.2175 0.3612 0.2068 -0.0364 0.0128  0.0123  98  LEU A O   
1536 C  CB  . LEU A 96  ? 0.1868 0.3002 0.1769 -0.0175 0.0118  0.0010  98  LEU A CB  
1537 C  CG  . LEU A 96  ? 0.1902 0.3024 0.1861 -0.0229 0.0109  0.0057  98  LEU A CG  
1538 C  CD1 . LEU A 96  ? 0.1819 0.3164 0.1834 -0.0223 0.0131  0.0037  98  LEU A CD1 
1539 C  CD2 . LEU A 96  ? 0.1853 0.2773 0.1833 -0.0188 0.0081  0.0045  98  LEU A CD2 
1551 N  N   . ILE A 97  ? 0.1757 0.2964 0.1566 -0.0353 0.0117  0.0135  99  ILE A N   
1552 C  CA  . ILE A 97  ? 0.1928 0.3074 0.1717 -0.0444 0.0086  0.0208  99  ILE A CA  
1553 C  C   . ILE A 97  ? 0.2219 0.3534 0.1995 -0.0482 0.0093  0.0217  99  ILE A C   
1554 O  O   . ILE A 97  ? 0.2106 0.3444 0.1885 -0.0554 0.0072  0.0264  99  ILE A O   
1555 C  CB  . ILE A 97  ? 0.1959 0.2925 0.1695 -0.0456 0.0060  0.0236  99  ILE A CB  
1556 C  CG1 . ILE A 97  ? 0.2105 0.2892 0.1865 -0.0468 0.0029  0.0266  99  ILE A CG1 
1557 C  CG2 . ILE A 97  ? 0.2507 0.3459 0.2199 -0.0519 0.0035  0.0283  99  ILE A CG2 
1558 C  CD1 . ILE A 97  ? 0.2179 0.2937 0.1987 -0.0406 0.0043  0.0223  99  ILE A CD1 
1570 N  N   . ILE A 98  ? 0.2223 0.3652 0.1977 -0.0433 0.0120  0.0169  100 ILE A N   
1571 C  CA  . ILE A 98  ? 0.2264 0.3868 0.2007 -0.0466 0.0130  0.0174  100 ILE A CA  
1572 C  C   . ILE A 98  ? 0.2492 0.4270 0.2291 -0.0472 0.0140  0.0162  100 ILE A C   
1573 O  O   . ILE A 98  ? 0.2936 0.4809 0.2728 -0.0549 0.0130  0.0205  100 ILE A O   
1574 C  CB  . ILE A 98  ? 0.2679 0.4360 0.2385 -0.0396 0.0154  0.0115  100 ILE A CB  
1575 C  CG1 . ILE A 98  ? 0.2908 0.4425 0.2545 -0.0405 0.0138  0.0135  100 ILE A CG1 
1576 C  CG2 . ILE A 98  ? 0.2758 0.4645 0.2459 -0.0425 0.0168  0.0115  100 ILE A CG2 
1577 C  CD1 . ILE A 98  ? 0.3587 0.5120 0.3179 -0.0319 0.0152  0.0065  100 ILE A CD1 
1589 N  N   . HIS A 99  ? 0.2182 0.3995 0.2029 -0.0394 0.0154  0.0105  101 HIS A N   
1590 C  CA  . HIS A 99  ? 0.2089 0.4051 0.1992 -0.0390 0.0157  0.0089  101 HIS A CA  
1591 C  C   . HIS A 99  ? 0.2246 0.4150 0.2158 -0.0488 0.0131  0.0162  101 HIS A C   
1592 O  O   . HIS A 99  ? 0.2602 0.4646 0.2521 -0.0543 0.0127  0.0184  101 HIS A O   
1593 C  CB  . HIS A 99  ? 0.2317 0.4263 0.2260 -0.0282 0.0167  0.0017  101 HIS A CB  
1594 C  CG  . HIS A 99  ? 0.2487 0.4566 0.2487 -0.0262 0.0167  -0.0006 101 HIS A CG  
1595 N  ND1 . HIS A 99  ? 0.2665 0.4966 0.2682 -0.0233 0.0176  -0.0046 101 HIS A ND1 
1596 C  CD2 . HIS A 99  ? 0.2420 0.4445 0.2462 -0.0269 0.0156  0.0006  101 HIS A CD2 
1597 C  CE1 . HIS A 99  ? 0.2808 0.5183 0.2871 -0.0221 0.0171  -0.0059 101 HIS A CE1 
1598 N  NE2 . HIS A 99  ? 0.2429 0.4638 0.2509 -0.0244 0.0160  -0.0027 101 HIS A NE2 
1607 N  N   . LEU A 100 ? 0.2166 0.3861 0.2073 -0.0508 0.0109  0.0197  102 LEU A N   
1608 C  CA  . LEU A 100 ? 0.2377 0.3979 0.2278 -0.0591 0.0074  0.0260  102 LEU A CA  
1609 C  C   . LEU A 100 ? 0.2682 0.4304 0.2530 -0.0686 0.0049  0.0320  102 LEU A C   
1610 O  O   . LEU A 100 ? 0.2677 0.4349 0.2521 -0.0754 0.0029  0.0358  102 LEU A O   
1611 C  CB  . LEU A 100 ? 0.1957 0.3319 0.1855 -0.0581 0.0050  0.0279  102 LEU A CB  
1612 C  CG  . LEU A 100 ? 0.2066 0.3397 0.2017 -0.0502 0.0069  0.0229  102 LEU A CG  
1613 C  CD1 . LEU A 100 ? 0.1693 0.2795 0.1633 -0.0497 0.0046  0.0250  102 LEU A CD1 
1614 C  CD2 . LEU A 100 ? 0.2009 0.3432 0.2011 -0.0498 0.0071  0.0217  102 LEU A CD2 
1626 N  N   . ARG A 101 ? 0.2698 0.4273 0.2500 -0.0694 0.0048  0.0331  103 ARG A N   
1627 C  CA  . ARG A 101 ? 0.2781 0.4352 0.2526 -0.0784 0.0019  0.0389  103 ARG A CA  
1628 C  C   . ARG A 101 ? 0.2991 0.4814 0.2742 -0.0822 0.0039  0.0388  103 ARG A C   
1629 O  O   . ARG A 101 ? 0.3705 0.5565 0.3429 -0.0912 0.0012  0.0440  103 ARG A O   
1630 C  CB  . ARG A 101 ? 0.3346 0.4812 0.3045 -0.0769 0.0016  0.0393  103 ARG A CB  
1631 C  CG  . ARG A 101 ? 0.3394 0.4893 0.3033 -0.0840 0.0000  0.0436  103 ARG A CG  
1632 C  CD  . ARG A 101 ? 0.3531 0.4882 0.3130 -0.0921 -0.0057 0.0501  103 ARG A CD  
1633 N  NE  . ARG A 101 ? 0.3588 0.4860 0.3118 -0.0969 -0.0086 0.0542  103 ARG A NE  
1634 C  CZ  . ARG A 101 ? 0.4134 0.5204 0.3622 -0.1003 -0.0143 0.0583  103 ARG A CZ  
1635 N  NH1 . ARG A 101 ? 0.4074 0.4999 0.3583 -0.0985 -0.0173 0.0584  103 ARG A NH1 
1636 N  NH2 . ARG A 101 ? 0.4131 0.5138 0.3555 -0.1046 -0.0171 0.0619  103 ARG A NH2 
1650 N  N   . LYS A 102 ? 0.2569 0.4564 0.2354 -0.0748 0.0083  0.0323  104 LYS A N   
1651 C  CA  . LYS A 102 ? 0.3073 0.5330 0.2869 -0.0764 0.0105  0.0307  104 LYS A CA  
1652 C  C   . LYS A 102 ? 0.3569 0.5927 0.3398 -0.0807 0.0095  0.0323  104 LYS A C   
1653 O  O   . LYS A 102 ? 0.3738 0.6260 0.3552 -0.0880 0.0092  0.0353  104 LYS A O   
1654 C  CB  . LYS A 102 ? 0.3268 0.5661 0.3094 -0.0651 0.0145  0.0221  104 LYS A CB  
1655 C  CG  . LYS A 102 ? 0.4421 0.7100 0.4265 -0.0644 0.0168  0.0189  104 LYS A CG  
1656 C  CD  . LYS A 102 ? 0.4973 0.7758 0.4845 -0.0512 0.0197  0.0092  104 LYS A CD  
1657 C  CE  . LYS A 102 ? 0.5861 0.8587 0.5684 -0.0478 0.0208  0.0075  104 LYS A CE  
1658 N  NZ  . LYS A 102 ? 0.6724 0.9583 0.6558 -0.0354 0.0230  -0.0020 104 LYS A NZ  
1672 N  N   . HIS A 103 ? 0.3089 0.5350 0.2958 -0.0767 0.0090  0.0307  105 HIS A N   
1673 C  CA  . HIS A 103 ? 0.3229 0.5570 0.3129 -0.0801 0.0081  0.0320  105 HIS A CA  
1674 C  C   . HIS A 103 ? 0.2989 0.5147 0.2854 -0.0892 0.0034  0.0394  105 HIS A C   
1675 O  O   . HIS A 103 ? 0.3111 0.5282 0.2998 -0.0919 0.0022  0.0408  105 HIS A O   
1676 C  CB  . HIS A 103 ? 0.3305 0.5661 0.3269 -0.0698 0.0102  0.0253  105 HIS A CB  
1677 C  CG  . HIS A 103 ? 0.3301 0.5873 0.3299 -0.0608 0.0136  0.0174  105 HIS A CG  
1678 N  ND1 . HIS A 103 ? 0.3226 0.5779 0.3223 -0.0515 0.0155  0.0117  105 HIS A ND1 
1679 C  CD2 . HIS A 103 ? 0.3278 0.6091 0.3309 -0.0591 0.0150  0.0140  105 HIS A CD2 
1680 C  CE1 . HIS A 103 ? 0.3307 0.6065 0.3331 -0.0438 0.0174  0.0047  105 HIS A CE1 
1681 N  NE2 . HIS A 103 ? 0.3585 0.6510 0.3633 -0.0481 0.0173  0.0059  105 HIS A NE2 
1689 N  N   . GLY A 104 ? 0.3167 0.5150 0.2976 -0.0933 0.0005  0.0437  106 GLY A N   
1690 C  CA  . GLY A 104 ? 0.3080 0.4879 0.2844 -0.1012 -0.0050 0.0503  106 GLY A CA  
1691 C  C   . GLY A 104 ? 0.2820 0.4440 0.2612 -0.0976 -0.0069 0.0497  106 GLY A C   
1692 O  O   . GLY A 104 ? 0.3313 0.4844 0.3082 -0.1035 -0.0111 0.0540  106 GLY A O   
1696 N  N   . ILE A 105 ? 0.2638 0.4207 0.2475 -0.0880 -0.0040 0.0444  107 ILE A N   
1697 C  CA  . ILE A 105 ? 0.2617 0.4023 0.2483 -0.0841 -0.0055 0.0435  107 ILE A CA  
1698 C  C   . ILE A 105 ? 0.2376 0.3540 0.2197 -0.0844 -0.0095 0.0461  107 ILE A C   
1699 O  O   . ILE A 105 ? 0.2382 0.3507 0.2191 -0.0808 -0.0081 0.0445  107 ILE A O   
1700 C  CB  . ILE A 105 ? 0.2310 0.3760 0.2240 -0.0741 -0.0012 0.0368  107 ILE A CB  
1701 C  CG1 . ILE A 105 ? 0.2879 0.4581 0.2856 -0.0713 0.0026  0.0325  107 ILE A CG1 
1702 C  CG2 . ILE A 105 ? 0.2347 0.3632 0.2308 -0.0710 -0.0030 0.0363  107 ILE A CG2 
1703 C  CD1 . ILE A 105 ? 0.3370 0.5162 0.3364 -0.0765 0.0013  0.0347  107 ILE A CD1 
1715 N  N   . PRO A 106 ? 0.2230 0.3239 0.2022 -0.0885 -0.0146 0.0500  108 PRO A N   
1716 C  CA  . PRO A 106 ? 0.2615 0.3402 0.2365 -0.0876 -0.0189 0.0516  108 PRO A CA  
1717 C  C   . PRO A 106 ? 0.2240 0.2924 0.2029 -0.0786 -0.0170 0.0472  108 PRO A C   
1718 O  O   . PRO A 106 ? 0.2288 0.2989 0.2130 -0.0743 -0.0148 0.0442  108 PRO A O   
1719 C  CB  . PRO A 106 ? 0.2566 0.3232 0.2285 -0.0923 -0.0247 0.0552  108 PRO A CB  
1720 C  CG  . PRO A 106 ? 0.3323 0.4166 0.3053 -0.0986 -0.0236 0.0571  108 PRO A CG  
1721 C  CD  . PRO A 106 ? 0.2834 0.3865 0.2631 -0.0935 -0.0170 0.0524  108 PRO A CD  
1729 N  N   . PHE A 107 ? 0.2119 0.2690 0.1879 -0.0761 -0.0181 0.0470  109 PHE A N   
1730 C  CA  . PHE A 107 ? 0.1979 0.2443 0.1770 -0.0685 -0.0170 0.0434  109 PHE A CA  
1731 C  C   . PHE A 107 ? 0.2131 0.2433 0.1879 -0.0674 -0.0210 0.0445  109 PHE A C   
1732 O  O   . PHE A 107 ? 0.2193 0.2485 0.1890 -0.0719 -0.0236 0.0475  109 PHE A O   
1733 C  CB  . PHE A 107 ? 0.1949 0.2532 0.1777 -0.0638 -0.0112 0.0394  109 PHE A CB  
1734 C  CG  . PHE A 107 ? 0.1801 0.2470 0.1596 -0.0652 -0.0094 0.0397  109 PHE A CG  
1735 C  CD1 . PHE A 107 ? 0.2026 0.2883 0.1817 -0.0689 -0.0071 0.0402  109 PHE A CD1 
1736 C  CD2 . PHE A 107 ? 0.1891 0.2466 0.1663 -0.0623 -0.0097 0.0391  109 PHE A CD2 
1737 C  CE1 . PHE A 107 ? 0.2255 0.3196 0.2014 -0.0698 -0.0053 0.0400  109 PHE A CE1 
1738 C  CE2 . PHE A 107 ? 0.2165 0.2817 0.1902 -0.0634 -0.0081 0.0392  109 PHE A CE2 
1739 C  CZ  . PHE A 107 ? 0.2117 0.2953 0.1849 -0.0669 -0.0057 0.0395  109 PHE A CZ  
1749 N  N   . ALA A 108 ? 0.1976 0.2160 0.1747 -0.0613 -0.0216 0.0418  110 ALA A N   
1750 C  CA  . ALA A 108 ? 0.2026 0.2061 0.1765 -0.0593 -0.0258 0.0422  110 ALA A CA  
1751 C  C   . ALA A 108 ? 0.1833 0.1812 0.1606 -0.0520 -0.0238 0.0383  110 ALA A C   
1752 O  O   . ALA A 108 ? 0.1719 0.1753 0.1537 -0.0489 -0.0197 0.0357  110 ALA A O   
1753 C  CB  . ALA A 108 ? 0.2331 0.2257 0.2046 -0.0610 -0.0314 0.0437  110 ALA A CB  
1759 N  N   . LEU A 109 ? 0.1685 0.1561 0.1438 -0.0494 -0.0268 0.0379  111 LEU A N   
1760 C  CA  . LEU A 109 ? 0.1768 0.1599 0.1551 -0.0431 -0.0253 0.0347  111 LEU A CA  
1761 C  C   . LEU A 109 ? 0.1871 0.1591 0.1661 -0.0391 -0.0289 0.0330  111 LEU A C   
1762 O  O   . LEU A 109 ? 0.2142 0.1792 0.1894 -0.0409 -0.0339 0.0346  111 LEU A O   
1763 C  CB  . LEU A 109 ? 0.1860 0.1690 0.1614 -0.0434 -0.0257 0.0355  111 LEU A CB  
1764 C  CG  . LEU A 109 ? 0.1518 0.1334 0.1298 -0.0384 -0.0236 0.0328  111 LEU A CG  
1765 C  CD1 . LEU A 109 ? 0.2130 0.2040 0.1928 -0.0384 -0.0184 0.0315  111 LEU A CD1 
1766 C  CD2 . LEU A 109 ? 0.2171 0.1948 0.1914 -0.0386 -0.0265 0.0340  111 LEU A CD2 
1778 N  N   . ALA A 110 ? 0.1744 0.1450 0.1577 -0.0337 -0.0267 0.0296  112 ALA A N   
1779 C  CA  . ALA A 110 ? 0.1853 0.1479 0.1696 -0.0295 -0.0294 0.0273  112 ALA A CA  
1780 C  C   . ALA A 110 ? 0.1807 0.1437 0.1685 -0.0245 -0.0269 0.0244  112 ALA A C   
1781 O  O   . ALA A 110 ? 0.1447 0.1119 0.1360 -0.0227 -0.0228 0.0225  112 ALA A O   
1782 C  CB  . ALA A 110 ? 0.1982 0.1611 0.1840 -0.0295 -0.0289 0.0265  112 ALA A CB  
1788 N  N   . THR A 111 ? 0.1503 0.1089 0.1369 -0.0226 -0.0297 0.0243  113 THR A N   
1789 C  CA  . THR A 111 ? 0.1913 0.1507 0.1808 -0.0190 -0.0284 0.0225  113 THR A CA  
1790 C  C   . THR A 111 ? 0.1856 0.1387 0.1755 -0.0144 -0.0322 0.0206  113 THR A C   
1791 O  O   . THR A 111 ? 0.2133 0.1604 0.1996 -0.0145 -0.0370 0.0213  113 THR A O   
1792 C  CB  . THR A 111 ? 0.1614 0.1231 0.1490 -0.0211 -0.0285 0.0244  113 THR A CB  
1793 O  OG1 . THR A 111 ? 0.1822 0.1434 0.1726 -0.0177 -0.0289 0.0229  113 THR A OG1 
1794 C  CG2 . THR A 111 ? 0.2447 0.2024 0.2272 -0.0239 -0.0328 0.0270  113 THR A CG2 
1802 N  N   . SER A 112 ? 0.1797 0.1342 0.1737 -0.0103 -0.0307 0.0181  114 SER A N   
1803 C  CA  . SER A 112 ? 0.1788 0.1293 0.1736 -0.0048 -0.0342 0.0157  114 SER A CA  
1804 C  C   . SER A 112 ? 0.2096 0.1599 0.2047 -0.0027 -0.0375 0.0161  114 SER A C   
1805 O  O   . SER A 112 ? 0.2127 0.1619 0.2090 0.0031  -0.0409 0.0135  114 SER A O   
1806 C  CB  . SER A 112 ? 0.1777 0.1311 0.1769 -0.0009 -0.0317 0.0130  114 SER A CB  
1807 O  OG  . SER A 112 ? 0.1890 0.1416 0.1872 -0.0020 -0.0297 0.0123  114 SER A OG  
1813 N  N   . SER A 113 ? 0.1652 0.1181 0.1592 -0.0067 -0.0365 0.0188  115 SER A N   
1814 C  CA  . SER A 113 ? 0.1913 0.1446 0.1848 -0.0053 -0.0400 0.0196  115 SER A CA  
1815 C  C   . SER A 113 ? 0.2041 0.1501 0.1930 -0.0038 -0.0452 0.0194  115 SER A C   
1816 O  O   . SER A 113 ? 0.2254 0.1665 0.2099 -0.0074 -0.0460 0.0208  115 SER A O   
1817 C  CB  . SER A 113 ? 0.2289 0.1852 0.2198 -0.0109 -0.0379 0.0227  115 SER A CB  
1818 O  OG  . SER A 113 ? 0.2848 0.2428 0.2746 -0.0103 -0.0409 0.0233  115 SER A OG  
1824 N  N   . GLY A 114 ? 0.2103 0.1566 0.2003 0.0013  -0.0491 0.0176  116 GLY A N   
1825 C  CA  . GLY A 114 ? 0.2832 0.2213 0.2679 0.0026  -0.0544 0.0175  116 GLY A CA  
1826 C  C   . GLY A 114 ? 0.2684 0.2042 0.2479 -0.0027 -0.0559 0.0215  116 GLY A C   
1827 O  O   . GLY A 114 ? 0.2504 0.1917 0.2302 -0.0069 -0.0527 0.0238  116 GLY A O   
1831 N  N   . SER A 115 ? 0.2992 0.2263 0.2731 -0.0023 -0.0611 0.0220  117 SER A N   
1832 C  CA  . SER A 115 ? 0.2918 0.2155 0.2595 -0.0078 -0.0630 0.0260  117 SER A CA  
1833 C  C   . SER A 115 ? 0.2600 0.1906 0.2291 -0.0074 -0.0622 0.0268  117 SER A C   
1834 O  O   . SER A 115 ? 0.2528 0.1866 0.2190 -0.0131 -0.0599 0.0300  117 SER A O   
1835 C  CB  . SER A 115 ? 0.3284 0.2403 0.2898 -0.0063 -0.0701 0.0259  117 SER A CB  
1836 O  OG  . SER A 115 ? 0.4647 0.3688 0.4229 -0.0081 -0.0722 0.0257  117 SER A OG  
1842 N  N   . ALA A 116 ? 0.2587 0.1933 0.2323 -0.0005 -0.0641 0.0236  118 ALA A N   
1843 C  CA  . ALA A 116 ? 0.2714 0.2133 0.2462 -0.0003 -0.0644 0.0241  118 ALA A CA  
1844 C  C   . ALA A 116 ? 0.2527 0.2041 0.2312 -0.0039 -0.0593 0.0247  118 ALA A C   
1845 O  O   . ALA A 116 ? 0.2571 0.2116 0.2326 -0.0081 -0.0582 0.0268  118 ALA A O   
1846 C  CB  . ALA A 116 ? 0.3016 0.2489 0.2818 0.0078  -0.0677 0.0199  118 ALA A CB  
1852 N  N   . SER A 117 ? 0.2542 0.2098 0.2387 -0.0020 -0.0565 0.0225  119 SER A N   
1853 C  CA  . SER A 117 ? 0.2022 0.1656 0.1900 -0.0053 -0.0522 0.0229  119 SER A CA  
1854 C  C   . SER A 117 ? 0.2042 0.1647 0.1856 -0.0124 -0.0488 0.0267  119 SER A C   
1855 O  O   . SER A 117 ? 0.1800 0.1463 0.1605 -0.0157 -0.0454 0.0266  119 SER A O   
1856 C  CB  . SER A 117 ? 0.2731 0.2401 0.2678 -0.0024 -0.0484 0.0195  119 SER A CB  
1857 O  OG  . SER A 117 ? 0.3375 0.3105 0.3349 -0.0064 -0.0415 0.0187  119 SER A OG  
1863 N  N   . PHE A 118 ? 0.1890 0.1427 0.1670 -0.0144 -0.0482 0.0281  120 PHE A N   
1864 C  CA  . PHE A 118 ? 0.2277 0.1823 0.2009 -0.0210 -0.0449 0.0310  120 PHE A CA  
1865 C  C   . PHE A 118 ? 0.2300 0.1856 0.1972 -0.0243 -0.0463 0.0334  120 PHE A C   
1866 O  O   . PHE A 118 ? 0.2128 0.1746 0.1776 -0.0280 -0.0429 0.0344  120 PHE A O   
1867 C  CB  . PHE A 118 ? 0.2298 0.1787 0.2011 -0.0229 -0.0456 0.0316  120 PHE A CB  
1868 C  CG  . PHE A 118 ? 0.2483 0.2005 0.2156 -0.0294 -0.0432 0.0345  120 PHE A CG  
1869 C  CD1 . PHE A 118 ? 0.2762 0.2351 0.2459 -0.0314 -0.0381 0.0341  120 PHE A CD1 
1870 C  CD2 . PHE A 118 ? 0.2835 0.2324 0.2445 -0.0335 -0.0462 0.0375  120 PHE A CD2 
1871 C  CE1 . PHE A 118 ? 0.2480 0.2122 0.2145 -0.0368 -0.0358 0.0364  120 PHE A CE1 
1872 C  CE2 . PHE A 118 ? 0.3202 0.2742 0.2778 -0.0397 -0.0439 0.0402  120 PHE A CE2 
1873 C  CZ  . PHE A 118 ? 0.2889 0.2514 0.2497 -0.0411 -0.0386 0.0394  120 PHE A CZ  
1883 N  N   A ASP A 119 ? 0.2461 0.1958 0.2104 -0.0226 -0.0513 0.0339  121 ASP A N   
1884 N  N   B ASP A 119 ? 0.2462 0.1960 0.2106 -0.0226 -0.0513 0.0339  121 ASP A N   
1885 C  CA  A ASP A 119 ? 0.2781 0.2282 0.2363 -0.0254 -0.0530 0.0362  121 ASP A CA  
1886 C  CA  B ASP A 119 ? 0.2781 0.2281 0.2363 -0.0255 -0.0529 0.0362  121 ASP A CA  
1887 C  C   A ASP A 119 ? 0.2403 0.1990 0.1996 -0.0249 -0.0511 0.0349  121 ASP A C   
1888 C  C   B ASP A 119 ? 0.2408 0.1993 0.2000 -0.0248 -0.0512 0.0349  121 ASP A C   
1889 O  O   A ASP A 119 ? 0.2308 0.1940 0.1853 -0.0289 -0.0488 0.0363  121 ASP A O   
1890 O  O   B ASP A 119 ? 0.2320 0.1949 0.1863 -0.0288 -0.0491 0.0363  121 ASP A O   
1891 C  CB  A ASP A 119 ? 0.3023 0.2445 0.2580 -0.0220 -0.0592 0.0362  121 ASP A CB  
1892 C  CB  B ASP A 119 ? 0.3027 0.2441 0.2580 -0.0226 -0.0592 0.0365  121 ASP A CB  
1893 C  CG  A ASP A 119 ? 0.3411 0.2732 0.2928 -0.0239 -0.0624 0.0379  121 ASP A CG  
1894 C  CG  B ASP A 119 ? 0.3302 0.2708 0.2783 -0.0260 -0.0611 0.0395  121 ASP A CG  
1895 O  OD1 A ASP A 119 ? 0.3330 0.2655 0.2828 -0.0295 -0.0599 0.0399  121 ASP A OD1 
1896 O  OD1 B ASP A 119 ? 0.3509 0.2899 0.2933 -0.0322 -0.0603 0.0429  121 ASP A OD1 
1897 O  OD2 A ASP A 119 ? 0.3512 0.2753 0.3015 -0.0196 -0.0679 0.0368  121 ASP A OD2 
1898 O  OD2 B ASP A 119 ? 0.3766 0.3191 0.3249 -0.0226 -0.0635 0.0382  121 ASP A OD2 
1907 N  N   . MET A 120 ? 0.2328 0.1948 0.1986 -0.0200 -0.0523 0.0316  122 MET A N   
1908 C  CA  . MET A 120 ? 0.2120 0.1824 0.1793 -0.0202 -0.0515 0.0295  122 MET A CA  
1909 C  C   . MET A 120 ? 0.2138 0.1897 0.1812 -0.0236 -0.0449 0.0282  122 MET A C   
1910 O  O   . MET A 120 ? 0.2202 0.2009 0.1851 -0.0254 -0.0432 0.0267  122 MET A O   
1911 C  CB  . MET A 120 ? 0.2649 0.2409 0.2416 -0.0153 -0.0527 0.0252  122 MET A CB  
1912 C  CG  . MET A 120 ? 0.2831 0.2571 0.2610 -0.0103 -0.0586 0.0246  122 MET A CG  
1913 S  SD  . MET A 120 ? 0.4915 0.4762 0.4820 -0.0044 -0.0599 0.0194  122 MET A SD  
1914 C  CE  . MET A 120 ? 0.4291 0.4085 0.4188 0.0029  -0.0653 0.0186  122 MET A CE  
1925 N  N   . LYS A 121 ? 0.2006 0.1760 0.1720 -0.0235 -0.0412 0.0275  123 LYS A N   
1926 C  CA  . LYS A 121 ? 0.1992 0.1796 0.1719 -0.0252 -0.0351 0.0252  123 LYS A CA  
1927 C  C   . LYS A 121 ? 0.1946 0.1771 0.1595 -0.0293 -0.0331 0.0277  123 LYS A C   
1928 O  O   . LYS A 121 ? 0.2062 0.1943 0.1704 -0.0297 -0.0293 0.0247  123 LYS A O   
1929 C  CB  . LYS A 121 ? 0.1698 0.1489 0.1479 -0.0239 -0.0322 0.0242  123 LYS A CB  
1930 C  CG  . LYS A 121 ? 0.1790 0.1596 0.1650 -0.0202 -0.0325 0.0209  123 LYS A CG  
1931 C  CD  . LYS A 121 ? 0.1970 0.1752 0.1866 -0.0188 -0.0306 0.0207  123 LYS A CD  
1932 C  CE  . LYS A 121 ? 0.1674 0.1484 0.1640 -0.0153 -0.0305 0.0178  123 LYS A CE  
1933 N  NZ  . LYS A 121 ? 0.2025 0.1802 0.2012 -0.0133 -0.0297 0.0178  123 LYS A NZ  
1947 N  N   . THR A 122 ? 0.1965 0.1748 0.1554 -0.0323 -0.0360 0.0328  124 THR A N   
1948 C  CA  . THR A 122 ? 0.1949 0.1776 0.1475 -0.0372 -0.0333 0.0355  124 THR A CA  
1949 C  C   . THR A 122 ? 0.2339 0.2180 0.1801 -0.0392 -0.0351 0.0371  124 THR A C   
1950 O  O   . THR A 122 ? 0.2569 0.2466 0.1988 -0.0431 -0.0326 0.0387  124 THR A O   
1951 C  CB  . THR A 122 ? 0.2719 0.2512 0.2266 -0.0394 -0.0331 0.0377  124 THR A CB  
1952 O  OG1 . THR A 122 ? 0.2962 0.2666 0.2500 -0.0389 -0.0383 0.0393  124 THR A OG1 
1953 C  CG2 . THR A 122 ? 0.2056 0.1839 0.1669 -0.0369 -0.0309 0.0357  124 THR A CG2 
1961 N  N   . SER A 123 ? 0.2819 0.2623 0.2279 -0.0365 -0.0393 0.0362  125 SER A N   
1962 C  CA  . SER A 123 ? 0.2959 0.2756 0.2358 -0.0376 -0.0420 0.0377  125 SER A CA  
1963 C  C   . SER A 123 ? 0.3058 0.2946 0.2398 -0.0399 -0.0383 0.0367  125 SER A C   
1964 O  O   . SER A 123 ? 0.3272 0.3174 0.2551 -0.0426 -0.0388 0.0390  125 SER A O   
1965 C  CB  . SER A 123 ? 0.3207 0.2970 0.2630 -0.0333 -0.0470 0.0358  125 SER A CB  
1966 O  OG  . SER A 123 ? 0.3423 0.3241 0.2882 -0.0311 -0.0463 0.0314  125 SER A OG  
1972 N  N   . ARG A 124 ? 0.2552 0.2501 0.1905 -0.0385 -0.0352 0.0327  126 ARG A N   
1973 C  CA  . ARG A 124 ? 0.2608 0.2645 0.1905 -0.0389 -0.0319 0.0298  126 ARG A CA  
1974 C  C   . ARG A 124 ? 0.2493 0.2617 0.1787 -0.0402 -0.0261 0.0289  126 ARG A C   
1975 O  O   . ARG A 124 ? 0.2744 0.2948 0.2001 -0.0387 -0.0231 0.0247  126 ARG A O   
1976 C  CB  . ARG A 124 ? 0.2858 0.2895 0.2167 -0.0354 -0.0333 0.0242  126 ARG A CB  
1977 C  CG  . ARG A 124 ? 0.2914 0.2894 0.2228 -0.0345 -0.0394 0.0253  126 ARG A CG  
1978 C  CD  . ARG A 124 ? 0.2663 0.2644 0.2007 -0.0320 -0.0414 0.0200  126 ARG A CD  
1979 N  NE  . ARG A 124 ? 0.2714 0.2662 0.2084 -0.0308 -0.0471 0.0212  126 ARG A NE  
1980 C  CZ  . ARG A 124 ? 0.2711 0.2665 0.2140 -0.0293 -0.0497 0.0176  126 ARG A CZ  
1981 N  NH1 . ARG A 124 ? 0.2953 0.2923 0.2417 -0.0289 -0.0468 0.0127  126 ARG A NH1 
1982 N  NH2 . ARG A 124 ? 0.2733 0.2679 0.2197 -0.0274 -0.0543 0.0185  126 ARG A NH2 
1996 N  N   . HIS A 125 ? 0.2309 0.2417 0.1643 -0.0423 -0.0249 0.0321  127 HIS A N   
1997 C  CA  . HIS A 125 ? 0.2189 0.2388 0.1535 -0.0437 -0.0198 0.0316  127 HIS A CA  
1998 C  C   . HIS A 125 ? 0.2235 0.2432 0.1593 -0.0487 -0.0200 0.0367  127 HIS A C   
1999 O  O   . HIS A 125 ? 0.2204 0.2425 0.1606 -0.0501 -0.0180 0.0374  127 HIS A O   
2000 C  CB  . HIS A 125 ? 0.2056 0.2232 0.1476 -0.0403 -0.0181 0.0284  127 HIS A CB  
2001 C  CG  . HIS A 125 ? 0.1881 0.2049 0.1331 -0.0346 -0.0173 0.0214  127 HIS A CG  
2002 N  ND1 . HIS A 125 ? 0.2833 0.3079 0.2246 -0.0320 -0.0146 0.0164  127 HIS A ND1 
2003 C  CD2 . HIS A 125 ? 0.2148 0.2236 0.1655 -0.0315 -0.0194 0.0187  127 HIS A CD2 
2004 C  CE1 . HIS A 125 ? 0.2722 0.2913 0.2161 -0.0278 -0.0156 0.0111  127 HIS A CE1 
2005 N  NE2 . HIS A 125 ? 0.2710 0.2813 0.2207 -0.0281 -0.0183 0.0128  127 HIS A NE2 
2013 N  N   . LYS A 126 ? 0.2196 0.2362 0.1511 -0.0517 -0.0229 0.0401  128 LYS A N   
2014 C  CA  . LYS A 126 ? 0.2633 0.2765 0.1950 -0.0569 -0.0249 0.0447  128 LYS A CA  
2015 C  C   . LYS A 126 ? 0.2503 0.2768 0.1825 -0.0613 -0.0207 0.0456  128 LYS A C   
2016 O  O   . LYS A 126 ? 0.2460 0.2709 0.1808 -0.0651 -0.0219 0.0481  128 LYS A O   
2017 C  CB  . LYS A 126 ? 0.2700 0.2768 0.1955 -0.0592 -0.0293 0.0480  128 LYS A CB  
2018 C  CG  . LYS A 126 ? 0.3156 0.3107 0.2416 -0.0544 -0.0341 0.0470  128 LYS A CG  
2019 C  CD  . LYS A 126 ? 0.3560 0.3400 0.2877 -0.0525 -0.0375 0.0473  128 LYS A CD  
2020 C  CE  . LYS A 126 ? 0.4120 0.3877 0.3405 -0.0566 -0.0420 0.0513  128 LYS A CE  
2021 N  NZ  . LYS A 126 ? 0.4195 0.3820 0.3516 -0.0531 -0.0472 0.0507  128 LYS A NZ  
2035 N  N   . GLU A 127 ? 0.2351 0.2754 0.1650 -0.0601 -0.0161 0.0427  129 GLU A N   
2036 C  CA  . GLU A 127 ? 0.2458 0.3017 0.1768 -0.0635 -0.0120 0.0428  129 GLU A CA  
2037 C  C   . GLU A 127 ? 0.2745 0.3344 0.2127 -0.0618 -0.0094 0.0406  129 GLU A C   
2038 O  O   . GLU A 127 ? 0.2604 0.3286 0.2013 -0.0659 -0.0083 0.0423  129 GLU A O   
2039 C  CB  . GLU A 127 ? 0.2588 0.3292 0.1855 -0.0613 -0.0079 0.0392  129 GLU A CB  
2040 C  CG  . GLU A 127 ? 0.3099 0.3868 0.2377 -0.0537 -0.0042 0.0321  129 GLU A CG  
2041 C  CD  . GLU A 127 ? 0.3770 0.4430 0.3015 -0.0486 -0.0068 0.0289  129 GLU A CD  
2042 O  OE1 . GLU A 127 ? 0.3457 0.3982 0.2726 -0.0481 -0.0102 0.0304  129 GLU A OE1 
2043 O  OE2 . GLU A 127 ? 0.4261 0.4977 0.3456 -0.0447 -0.0055 0.0243  129 GLU A OE2 
2050 N  N   . PHE A 128 ? 0.2242 0.2780 0.1652 -0.0562 -0.0090 0.0371  130 PHE A N   
2051 C  CA  . PHE A 128 ? 0.2270 0.2829 0.1743 -0.0541 -0.0069 0.0351  130 PHE A CA  
2052 C  C   . PHE A 128 ? 0.1980 0.2423 0.1489 -0.0574 -0.0109 0.0390  130 PHE A C   
2053 O  O   . PHE A 128 ? 0.2141 0.2635 0.1686 -0.0600 -0.0101 0.0399  130 PHE A O   
2054 C  CB  . PHE A 128 ? 0.2131 0.2641 0.1605 -0.0476 -0.0062 0.0305  130 PHE A CB  
2055 C  CG  . PHE A 128 ? 0.1934 0.2447 0.1465 -0.0453 -0.0043 0.0286  130 PHE A CG  
2056 C  CD1 . PHE A 128 ? 0.2007 0.2661 0.1557 -0.0425 0.0002  0.0244  130 PHE A CD1 
2057 C  CD2 . PHE A 128 ? 0.1645 0.2020 0.1215 -0.0449 -0.0071 0.0304  130 PHE A CD2 
2058 C  CE1 . PHE A 128 ? 0.2266 0.2904 0.1887 -0.0390 0.0013  0.0216  130 PHE A CE1 
2059 C  CE2 . PHE A 128 ? 0.2132 0.2496 0.1775 -0.0415 -0.0056 0.0275  130 PHE A CE2 
2060 C  CZ  . PHE A 128 ? 0.1823 0.2311 0.1488 -0.0389 -0.0016 0.0234  130 PHE A CZ  
2070 N  N   . PHE A 129 ? 0.1974 0.2267 0.1470 -0.0568 -0.0155 0.0408  131 PHE A N   
2071 C  CA  . PHE A 129 ? 0.2290 0.2464 0.1814 -0.0579 -0.0198 0.0430  131 PHE A CA  
2072 C  C   . PHE A 129 ? 0.2763 0.2942 0.2259 -0.0646 -0.0227 0.0471  131 PHE A C   
2073 O  O   . PHE A 129 ? 0.3050 0.3170 0.2564 -0.0661 -0.0254 0.0483  131 PHE A O   
2074 C  CB  . PHE A 129 ? 0.2025 0.2058 0.1554 -0.0536 -0.0237 0.0423  131 PHE A CB  
2075 C  CG  . PHE A 129 ? 0.1786 0.1813 0.1356 -0.0482 -0.0212 0.0386  131 PHE A CG  
2076 C  CD1 . PHE A 129 ? 0.1831 0.1833 0.1458 -0.0462 -0.0204 0.0372  131 PHE A CD1 
2077 C  CD2 . PHE A 129 ? 0.2059 0.2112 0.1604 -0.0456 -0.0199 0.0365  131 PHE A CD2 
2078 C  CE1 . PHE A 129 ? 0.2109 0.2100 0.1770 -0.0420 -0.0183 0.0342  131 PHE A CE1 
2079 C  CE2 . PHE A 129 ? 0.1794 0.1840 0.1376 -0.0410 -0.0181 0.0326  131 PHE A CE2 
2080 C  CZ  . PHE A 129 ? 0.2210 0.2223 0.1858 -0.0391 -0.0171 0.0313  131 PHE A CZ  
2090 N  N   . SER A 130 ? 0.2399 0.2660 0.1846 -0.0690 -0.0219 0.0493  132 SER A N   
2091 C  CA  . SER A 130 ? 0.2817 0.3088 0.2228 -0.0765 -0.0249 0.0537  132 SER A CA  
2092 C  C   . SER A 130 ? 0.3090 0.3485 0.2537 -0.0798 -0.0223 0.0538  132 SER A C   
2093 O  O   . SER A 130 ? 0.3304 0.3694 0.2729 -0.0862 -0.0255 0.0575  132 SER A O   
2094 C  CB  . SER A 130 ? 0.3026 0.3362 0.2373 -0.0805 -0.0245 0.0561  132 SER A CB  
2095 O  OG  . SER A 130 ? 0.3129 0.3650 0.2487 -0.0801 -0.0184 0.0537  132 SER A OG  
2101 N  N   . LEU A 131 ? 0.2640 0.3148 0.2137 -0.0756 -0.0169 0.0498  133 LEU A N   
2102 C  CA  . LEU A 131 ? 0.2740 0.3384 0.2275 -0.0780 -0.0144 0.0494  133 LEU A CA  
2103 C  C   . LEU A 131 ? 0.2940 0.3493 0.2511 -0.0775 -0.0170 0.0497  133 LEU A C   
2104 O  O   . LEU A 131 ? 0.3169 0.3814 0.2761 -0.0807 -0.0164 0.0504  133 LEU A O   
2105 C  CB  . LEU A 131 ? 0.2317 0.3122 0.1887 -0.0729 -0.0081 0.0444  133 LEU A CB  
2106 C  CG  . LEU A 131 ? 0.2465 0.3370 0.1996 -0.0717 -0.0051 0.0428  133 LEU A CG  
2107 C  CD1 . LEU A 131 ? 0.2457 0.3518 0.2022 -0.0654 0.0005  0.0367  133 LEU A CD1 
2108 C  CD2 . LEU A 131 ? 0.3202 0.4196 0.2691 -0.0797 -0.0063 0.0471  133 LEU A CD2 
2120 N  N   . PHE A 132 ? 0.2592 0.2974 0.2169 -0.0734 -0.0201 0.0490  134 PHE A N   
2121 C  CA  . PHE A 132 ? 0.2704 0.2997 0.2312 -0.0720 -0.0226 0.0486  134 PHE A CA  
2122 C  C   . PHE A 132 ? 0.3401 0.3624 0.2965 -0.0784 -0.0284 0.0529  134 PHE A C   
2123 O  O   . PHE A 132 ? 0.3314 0.3477 0.2823 -0.0820 -0.0321 0.0558  134 PHE A O   
2124 C  CB  . PHE A 132 ? 0.2554 0.2707 0.2183 -0.0650 -0.0238 0.0459  134 PHE A CB  
2125 C  CG  . PHE A 132 ? 0.2288 0.2498 0.1959 -0.0594 -0.0186 0.0419  134 PHE A CG  
2126 C  CD1 . PHE A 132 ? 0.2596 0.2858 0.2248 -0.0581 -0.0160 0.0408  134 PHE A CD1 
2127 C  CD2 . PHE A 132 ? 0.1887 0.2091 0.1610 -0.0556 -0.0168 0.0393  134 PHE A CD2 
2128 C  CE1 . PHE A 132 ? 0.2159 0.2466 0.1835 -0.0533 -0.0118 0.0372  134 PHE A CE1 
2129 C  CE2 . PHE A 132 ? 0.1674 0.1926 0.1427 -0.0513 -0.0125 0.0360  134 PHE A CE2 
2130 C  CZ  . PHE A 132 ? 0.1689 0.1988 0.1417 -0.0501 -0.0102 0.0349  134 PHE A CZ  
2140 N  N   . SER A 133 ? 0.3022 0.3253 0.2605 -0.0802 -0.0294 0.0534  135 SER A N   
2141 C  CA  . SER A 133 ? 0.2829 0.2992 0.2363 -0.0868 -0.0354 0.0576  135 SER A CA  
2142 C  C   . SER A 133 ? 0.3354 0.3315 0.2853 -0.0844 -0.0417 0.0578  135 SER A C   
2143 O  O   . SER A 133 ? 0.4246 0.4131 0.3680 -0.0898 -0.0474 0.0614  135 SER A O   
2144 C  CB  . SER A 133 ? 0.3519 0.3733 0.3081 -0.0886 -0.0350 0.0578  135 SER A CB  
2145 O  OG  . SER A 133 ? 0.3632 0.4053 0.3229 -0.0906 -0.0294 0.0573  135 SER A OG  
2151 N  N   . HIS A 134 ? 0.2857 0.2734 0.2395 -0.0762 -0.0410 0.0538  136 HIS A N   
2152 C  CA  . HIS A 134 ? 0.2903 0.2613 0.2418 -0.0724 -0.0464 0.0528  136 HIS A CA  
2153 C  C   . HIS A 134 ? 0.2656 0.2344 0.2230 -0.0633 -0.0430 0.0479  136 HIS A C   
2154 O  O   . HIS A 134 ? 0.2624 0.2406 0.2249 -0.0609 -0.0374 0.0457  136 HIS A O   
2155 C  CB  . HIS A 134 ? 0.3247 0.2850 0.2727 -0.0749 -0.0528 0.0543  136 HIS A CB  
2156 C  CG  . HIS A 134 ? 0.3234 0.2860 0.2760 -0.0725 -0.0509 0.0523  136 HIS A CG  
2157 N  ND1 . HIS A 134 ? 0.3182 0.2921 0.2719 -0.0775 -0.0485 0.0543  136 HIS A ND1 
2158 C  CD2 . HIS A 134 ? 0.3145 0.2703 0.2707 -0.0656 -0.0510 0.0484  136 HIS A CD2 
2159 C  CE1 . HIS A 134 ? 0.2947 0.2676 0.2526 -0.0739 -0.0473 0.0519  136 HIS A CE1 
2160 N  NE2 . HIS A 134 ? 0.2775 0.2395 0.2368 -0.0667 -0.0487 0.0483  136 HIS A NE2 
2168 N  N   . ILE A 135 ? 0.2708 0.2276 0.2272 -0.0588 -0.0468 0.0462  137 ILE A N   
2169 C  CA  . ILE A 135 ? 0.2445 0.1995 0.2059 -0.0508 -0.0442 0.0419  137 ILE A CA  
2170 C  C   . ILE A 135 ? 0.3261 0.2692 0.2874 -0.0462 -0.0488 0.0396  137 ILE A C   
2171 O  O   . ILE A 135 ? 0.3185 0.2515 0.2743 -0.0479 -0.0552 0.0410  137 ILE A O   
2172 C  CB  . ILE A 135 ? 0.3131 0.2688 0.2731 -0.0498 -0.0436 0.0422  137 ILE A CB  
2173 C  CG1 . ILE A 135 ? 0.2709 0.2397 0.2310 -0.0536 -0.0384 0.0437  137 ILE A CG1 
2174 C  CG2 . ILE A 135 ? 0.3012 0.2536 0.2653 -0.0424 -0.0426 0.0384  137 ILE A CG2 
2175 C  CD1 . ILE A 135 ? 0.3293 0.2996 0.2865 -0.0540 -0.0381 0.0446  137 ILE A CD1 
2187 N  N   . VAL A 136 ? 0.2509 0.1947 0.2174 -0.0407 -0.0462 0.0360  138 VAL A N   
2188 C  CA  . VAL A 136 ? 0.2479 0.1826 0.2148 -0.0351 -0.0496 0.0328  138 VAL A CA  
2189 C  C   . VAL A 136 ? 0.2695 0.2060 0.2409 -0.0288 -0.0467 0.0296  138 VAL A C   
2190 O  O   . VAL A 136 ? 0.2311 0.1755 0.2073 -0.0273 -0.0411 0.0283  138 VAL A O   
2191 C  CB  . VAL A 136 ? 0.2474 0.1811 0.2160 -0.0340 -0.0495 0.0312  138 VAL A CB  
2192 C  CG1 . VAL A 136 ? 0.2654 0.1896 0.2332 -0.0283 -0.0536 0.0278  138 VAL A CG1 
2193 C  CG2 . VAL A 136 ? 0.2771 0.2105 0.2416 -0.0411 -0.0522 0.0350  138 VAL A CG2 
2203 N  N   . LEU A 137 ? 0.2450 0.1740 0.2147 -0.0250 -0.0510 0.0281  139 LEU A N   
2204 C  CA  . LEU A 137 ? 0.2330 0.1637 0.2068 -0.0190 -0.0495 0.0252  139 LEU A CA  
2205 C  C   . LEU A 137 ? 0.2761 0.2029 0.2519 -0.0126 -0.0509 0.0211  139 LEU A C   
2206 O  O   . LEU A 137 ? 0.2768 0.1974 0.2498 -0.0124 -0.0543 0.0203  139 LEU A O   
2207 C  CB  . LEU A 137 ? 0.2718 0.1982 0.2423 -0.0183 -0.0533 0.0263  139 LEU A CB  
2208 C  CG  . LEU A 137 ? 0.3197 0.2490 0.2866 -0.0246 -0.0528 0.0304  139 LEU A CG  
2209 C  CD1 . LEU A 137 ? 0.3497 0.2741 0.3133 -0.0231 -0.0570 0.0310  139 LEU A CD1 
2210 C  CD2 . LEU A 137 ? 0.2878 0.2280 0.2586 -0.0262 -0.0463 0.0309  139 LEU A CD2 
2222 N  N   . GLY A 138 ? 0.2520 0.1827 0.2324 -0.0072 -0.0489 0.0185  140 GLY A N   
2223 C  CA  . GLY A 138 ? 0.2695 0.1993 0.2525 -0.0008 -0.0493 0.0143  140 GLY A CA  
2224 C  C   . GLY A 138 ? 0.3090 0.2308 0.2885 0.0043  -0.0557 0.0116  140 GLY A C   
2225 O  O   . GLY A 138 ? 0.3091 0.2291 0.2888 0.0094  -0.0570 0.0078  140 GLY A O   
2229 N  N   . ASP A 139 ? 0.2831 0.2005 0.2590 0.0033  -0.0596 0.0133  141 ASP A N   
2230 C  CA  . ASP A 139 ? 0.3079 0.2158 0.2790 0.0078  -0.0666 0.0108  141 ASP A CA  
2231 C  C   . ASP A 139 ? 0.3606 0.2571 0.3240 0.0030  -0.0720 0.0127  141 ASP A C   
2232 O  O   . ASP A 139 ? 0.3767 0.2630 0.3344 0.0055  -0.0789 0.0113  141 ASP A O   
2233 C  CB  . ASP A 139 ? 0.3693 0.2775 0.3403 0.0106  -0.0691 0.0109  141 ASP A CB  
2234 C  CG  . ASP A 139 ? 0.3512 0.2592 0.3194 0.0032  -0.0685 0.0161  141 ASP A CG  
2235 O  OD1 . ASP A 139 ? 0.3332 0.2405 0.2990 -0.0041 -0.0669 0.0197  141 ASP A OD1 
2236 O  OD2 . ASP A 139 ? 0.3662 0.2758 0.3346 0.0050  -0.0700 0.0166  141 ASP A OD2 
2241 N  N   . ASP A 140 ? 0.3254 0.2238 0.2884 -0.0038 -0.0694 0.0159  142 ASP A N   
2242 C  CA  . ASP A 140 ? 0.3424 0.2317 0.2985 -0.0091 -0.0746 0.0182  142 ASP A CA  
2243 C  C   . ASP A 140 ? 0.3713 0.2524 0.3246 -0.0035 -0.0795 0.0137  142 ASP A C   
2244 O  O   . ASP A 140 ? 0.3054 0.1916 0.2632 0.0018  -0.0762 0.0100  142 ASP A O   
2245 C  CB  . ASP A 140 ? 0.3621 0.2582 0.3198 -0.0162 -0.0702 0.0218  142 ASP A CB  
2246 C  CG  . ASP A 140 ? 0.2822 0.1705 0.2328 -0.0231 -0.0759 0.0253  142 ASP A CG  
2247 O  OD1 . ASP A 140 ? 0.3990 0.2797 0.3464 -0.0216 -0.0804 0.0235  142 ASP A OD1 
2248 O  OD2 . ASP A 140 ? 0.3553 0.2460 0.3036 -0.0300 -0.0755 0.0298  142 ASP A OD2 
2253 N  N   . PRO A 141 ? 0.3929 0.2607 0.3379 -0.0044 -0.0881 0.0139  143 PRO A N   
2254 C  CA  . PRO A 141 ? 0.4266 0.2853 0.3675 0.0016  -0.0939 0.0091  143 PRO A CA  
2255 C  C   . PRO A 141 ? 0.4300 0.2911 0.3723 0.0006  -0.0920 0.0084  143 PRO A C   
2256 O  O   . PRO A 141 ? 0.4810 0.3393 0.4224 0.0072  -0.0941 0.0034  143 PRO A O   
2257 C  CB  . PRO A 141 ? 0.4329 0.2762 0.3636 -0.0017 -0.1038 0.0110  143 PRO A CB  
2258 C  CG  . PRO A 141 ? 0.4016 0.2460 0.3321 -0.0049 -0.1032 0.0144  143 PRO A CG  
2259 C  CD  . PRO A 141 ? 0.4088 0.2685 0.3472 -0.0094 -0.0934 0.0177  143 PRO A CD  
2267 N  N   . GLU A 142 ? 0.4867 0.3540 0.4312 -0.0071 -0.0877 0.0130  144 GLU A N   
2268 C  CA  . GLU A 142 ? 0.4885 0.3589 0.4346 -0.0087 -0.0856 0.0130  144 GLU A CA  
2269 C  C   . GLU A 142 ? 0.4977 0.3800 0.4522 -0.0042 -0.0772 0.0101  144 GLU A C   
2270 O  O   . GLU A 142 ? 0.5055 0.3892 0.4609 -0.0036 -0.0760 0.0089  144 GLU A O   
2271 C  CB  . GLU A 142 ? 0.5197 0.3923 0.4644 -0.0184 -0.0850 0.0190  144 GLU A CB  
2272 C  CG  . GLU A 142 ? 0.6191 0.4914 0.5632 -0.0208 -0.0856 0.0195  144 GLU A CG  
2273 C  CD  . GLU A 142 ? 0.6255 0.5000 0.5675 -0.0306 -0.0862 0.0256  144 GLU A CD  
2274 O  OE1 . GLU A 142 ? 0.5633 0.4380 0.5028 -0.0357 -0.0872 0.0294  144 GLU A OE1 
2275 O  OE2 . GLU A 142 ? 0.7107 0.5874 0.6534 -0.0331 -0.0856 0.0266  144 GLU A OE2 
2282 N  N   . VAL A 143 ? 0.4343 0.3246 0.3943 -0.0013 -0.0719 0.0093  145 VAL A N   
2283 C  CA  . VAL A 143 ? 0.3756 0.2770 0.3430 0.0022  -0.0643 0.0072  145 VAL A CA  
2284 C  C   . VAL A 143 ? 0.3948 0.2972 0.3639 0.0113  -0.0646 0.0017  145 VAL A C   
2285 O  O   . VAL A 143 ? 0.3817 0.2866 0.3527 0.0150  -0.0643 0.0005  145 VAL A O   
2286 C  CB  . VAL A 143 ? 0.3274 0.2379 0.2997 -0.0013 -0.0584 0.0104  145 VAL A CB  
2287 C  CG1 . VAL A 143 ? 0.3373 0.2580 0.3164 0.0016  -0.0512 0.0087  145 VAL A CG1 
2288 C  CG2 . VAL A 143 ? 0.3037 0.2154 0.2743 -0.0095 -0.0578 0.0153  145 VAL A CG2 
2298 N  N   . GLN A 144 ? 0.3841 0.2853 0.3522 0.0152  -0.0652 -0.0018 146 GLN A N   
2299 C  CA  . GLN A 144 ? 0.4598 0.3632 0.4288 0.0243  -0.0659 -0.0076 146 GLN A CA  
2300 C  C   . GLN A 144 ? 0.4363 0.3526 0.4129 0.0274  -0.0584 -0.0088 146 GLN A C   
2301 O  O   . GLN A 144 ? 0.4700 0.3916 0.4488 0.0343  -0.0584 -0.0126 146 GLN A O   
2302 C  CB  . GLN A 144 ? 0.5165 0.4140 0.4807 0.0275  -0.0698 -0.0111 146 GLN A CB  
2303 C  CG  . GLN A 144 ? 0.5604 0.4436 0.5160 0.0262  -0.0791 -0.0109 146 GLN A CG  
2304 C  CD  . GLN A 144 ? 0.6812 0.5576 0.6312 0.0293  -0.0840 -0.0143 146 GLN A CD  
2305 O  OE1 . GLN A 144 ? 0.6086 0.4909 0.5612 0.0309  -0.0799 -0.0159 146 GLN A OE1 
2306 N  NE2 . GLN A 144 ? 0.7592 0.6222 0.7008 0.0301  -0.0934 -0.0154 146 GLN A NE2 
2315 N  N   . HIS A 145 ? 0.3421 0.2642 0.3225 0.0225  -0.0526 -0.0058 147 HIS A N   
2316 C  CA  . HIS A 145 ? 0.3165 0.2493 0.3032 0.0246  -0.0463 -0.0065 147 HIS A CA  
2317 C  C   . HIS A 145 ? 0.2396 0.1757 0.2293 0.0176  -0.0419 -0.0016 147 HIS A C   
2318 O  O   . HIS A 145 ? 0.2485 0.1810 0.2359 0.0115  -0.0424 0.0016  147 HIS A O   
2319 C  CB  . HIS A 145 ? 0.3199 0.2561 0.3072 0.0280  -0.0439 -0.0096 147 HIS A CB  
2320 C  CG  . HIS A 145 ? 0.4004 0.3331 0.3833 0.0347  -0.0486 -0.0147 147 HIS A CG  
2321 N  ND1 . HIS A 145 ? 0.4364 0.3761 0.4210 0.0428  -0.0489 -0.0196 147 HIS A ND1 
2322 C  CD2 . HIS A 145 ? 0.4653 0.3888 0.4421 0.0348  -0.0537 -0.0159 147 HIS A CD2 
2323 C  CE1 . HIS A 145 ? 0.4540 0.3886 0.4331 0.0479  -0.0539 -0.0239 147 HIS A CE1 
2324 N  NE2 . HIS A 145 ? 0.4778 0.4016 0.4519 0.0431  -0.0572 -0.0217 147 HIS A NE2 
2332 N  N   . GLY A 146 ? 0.2217 0.1657 0.2167 0.0187  -0.0380 -0.0014 148 GLY A N   
2333 C  CA  . GLY A 146 ? 0.2358 0.1831 0.2333 0.0128  -0.0338 0.0025  148 GLY A CA  
2334 C  C   . GLY A 146 ? 0.1507 0.0993 0.1484 0.0099  -0.0300 0.0031  148 GLY A C   
2335 O  O   . GLY A 146 ? 0.1736 0.1205 0.1696 0.0123  -0.0304 0.0009  148 GLY A O   
2339 N  N   . LYS A 147 ? 0.1409 0.0928 0.1402 0.0049  -0.0264 0.0059  149 LYS A N   
2340 C  CA  . LYS A 147 ? 0.1517 0.1058 0.1515 0.0029  -0.0226 0.0062  149 LYS A CA  
2341 C  C   . LYS A 147 ? 0.1455 0.1012 0.1471 0.0074  -0.0211 0.0036  149 LYS A C   
2342 O  O   . LYS A 147 ? 0.1414 0.1025 0.1461 0.0094  -0.0201 0.0026  149 LYS A O   
2343 C  CB  . LYS A 147 ? 0.1245 0.0829 0.1257 -0.0017 -0.0192 0.0086  149 LYS A CB  
2344 C  CG  . LYS A 147 ? 0.1401 0.0980 0.1394 -0.0053 -0.0210 0.0109  149 LYS A CG  
2345 C  CD  . LYS A 147 ? 0.1289 0.0914 0.1291 -0.0084 -0.0184 0.0127  149 LYS A CD  
2346 C  CE  . LYS A 147 ? 0.1320 0.0941 0.1299 -0.0118 -0.0205 0.0151  149 LYS A CE  
2347 N  NZ  . LYS A 147 ? 0.1309 0.0976 0.1290 -0.0145 -0.0182 0.0165  149 LYS A NZ  
2361 N  N   . PRO A 148 ? 0.1423 0.0973 0.1424 0.0085  -0.0200 0.0022  150 PRO A N   
2362 C  CA  . PRO A 148 ? 0.1182 0.0721 0.1163 0.0051  -0.0193 0.0032  150 PRO A CA  
2363 C  C   . PRO A 148 ? 0.1511 0.1004 0.1461 0.0056  -0.0234 0.0024  150 PRO A C   
2364 O  O   . PRO A 148 ? 0.1611 0.1098 0.1551 0.0033  -0.0235 0.0031  150 PRO A O   
2365 C  CB  . PRO A 148 ? 0.1408 0.0956 0.1386 0.0066  -0.0168 0.0021  150 PRO A CB  
2366 C  CG  . PRO A 148 ? 0.1549 0.1104 0.1528 0.0125  -0.0177 -0.0011 150 PRO A CG  
2367 C  CD  . PRO A 148 ? 0.1636 0.1233 0.1646 0.0124  -0.0178 -0.0005 150 PRO A CD  
2375 N  N   . ASP A 149 ? 0.1550 0.1007 0.1484 0.0082  -0.0274 0.0011  151 ASP A N   
2376 C  CA  . ASP A 149 ? 0.1979 0.1374 0.1873 0.0077  -0.0323 0.0008  151 ASP A CA  
2377 C  C   . ASP A 149 ? 0.1695 0.1092 0.1589 0.0013  -0.0327 0.0047  151 ASP A C   
2378 O  O   . ASP A 149 ? 0.1666 0.1091 0.1576 -0.0010 -0.0312 0.0068  151 ASP A O   
2379 C  CB  . ASP A 149 ? 0.2374 0.1727 0.2246 0.0121  -0.0368 -0.0015 151 ASP A CB  
2380 C  CG  . ASP A 149 ? 0.2596 0.1864 0.2414 0.0120  -0.0431 -0.0023 151 ASP A CG  
2381 O  OD1 . ASP A 149 ? 0.2440 0.1676 0.2240 0.0065  -0.0452 0.0009  151 ASP A OD1 
2382 O  OD2 . ASP A 149 ? 0.3356 0.2592 0.3146 0.0179  -0.0463 -0.0063 151 ASP A OD2 
2387 N  N   . PRO A 150 ? 0.1543 0.0913 0.1417 -0.0016 -0.0349 0.0056  152 PRO A N   
2388 C  CA  . PRO A 150 ? 0.1746 0.1130 0.1620 -0.0076 -0.0355 0.0093  152 PRO A CA  
2389 C  C   . PRO A 150 ? 0.1936 0.1270 0.1776 -0.0102 -0.0403 0.0115  152 PRO A C   
2390 O  O   . PRO A 150 ? 0.1891 0.1250 0.1730 -0.0155 -0.0404 0.0149  152 PRO A O   
2391 C  CB  . PRO A 150 ? 0.1874 0.1243 0.1737 -0.0092 -0.0372 0.0094  152 PRO A CB  
2392 C  CG  . PRO A 150 ? 0.2451 0.1761 0.2284 -0.0047 -0.0402 0.0062  152 PRO A CG  
2393 C  CD  . PRO A 150 ? 0.2227 0.1559 0.2076 0.0007  -0.0372 0.0033  152 PRO A CD  
2401 N  N   . ASP A 151 ? 0.2089 0.1358 0.1899 -0.0065 -0.0443 0.0094  153 ASP A N   
2402 C  CA  . ASP A 151 ? 0.2729 0.1926 0.2492 -0.0085 -0.0504 0.0110  153 ASP A CA  
2403 C  C   . ASP A 151 ? 0.2384 0.1622 0.2154 -0.0138 -0.0487 0.0150  153 ASP A C   
2404 O  O   . ASP A 151 ? 0.2491 0.1700 0.2226 -0.0193 -0.0523 0.0185  153 ASP A O   
2405 C  CB  . ASP A 151 ? 0.3057 0.2204 0.2802 -0.0024 -0.0533 0.0076  153 ASP A CB  
2406 C  CG  . ASP A 151 ? 0.3994 0.3068 0.3699 0.0028  -0.0582 0.0035  153 ASP A CG  
2407 O  OD1 . ASP A 151 ? 0.3825 0.2857 0.3500 0.0010  -0.0611 0.0038  153 ASP A OD1 
2408 O  OD2 . ASP A 151 ? 0.4232 0.3290 0.3930 0.0091  -0.0596 -0.0002 153 ASP A OD2 
2413 N  N   . ILE A 152 ? 0.1877 0.1181 0.1688 -0.0125 -0.0438 0.0149  154 ILE A N   
2414 C  CA  . ILE A 152 ? 0.2178 0.1516 0.1988 -0.0167 -0.0429 0.0181  154 ILE A CA  
2415 C  C   . ILE A 152 ? 0.1853 0.1248 0.1668 -0.0226 -0.0408 0.0214  154 ILE A C   
2416 O  O   . ILE A 152 ? 0.2046 0.1446 0.1833 -0.0275 -0.0425 0.0248  154 ILE A O   
2417 C  CB  . ILE A 152 ? 0.2130 0.1520 0.1977 -0.0138 -0.0387 0.0171  154 ILE A CB  
2418 C  CG1 . ILE A 152 ? 0.2286 0.1686 0.2115 -0.0174 -0.0395 0.0201  154 ILE A CG1 
2419 C  CG2 . ILE A 152 ? 0.2118 0.1584 0.2012 -0.0129 -0.0326 0.0161  154 ILE A CG2 
2420 C  CD1 . ILE A 152 ? 0.2583 0.2017 0.2439 -0.0149 -0.0371 0.0194  154 ILE A CD1 
2432 N  N   . PHE A 153 ? 0.1789 0.1232 0.1636 -0.0222 -0.0372 0.0205  155 PHE A N   
2433 C  CA  . PHE A 153 ? 0.1724 0.1229 0.1579 -0.0274 -0.0355 0.0233  155 PHE A CA  
2434 C  C   . PHE A 153 ? 0.1800 0.1259 0.1614 -0.0318 -0.0408 0.0257  155 PHE A C   
2435 O  O   . PHE A 153 ? 0.2066 0.1565 0.1866 -0.0377 -0.0413 0.0293  155 PHE A O   
2436 C  CB  . PHE A 153 ? 0.1738 0.1305 0.1640 -0.0254 -0.0307 0.0214  155 PHE A CB  
2437 C  CG  . PHE A 153 ? 0.1442 0.1057 0.1376 -0.0225 -0.0257 0.0198  155 PHE A CG  
2438 C  CD1 . PHE A 153 ? 0.1765 0.1409 0.1694 -0.0241 -0.0247 0.0213  155 PHE A CD1 
2439 C  CD2 . PHE A 153 ? 0.1333 0.0960 0.1296 -0.0186 -0.0226 0.0169  155 PHE A CD2 
2440 C  CE1 . PHE A 153 ? 0.1535 0.1216 0.1489 -0.0218 -0.0209 0.0199  155 PHE A CE1 
2441 C  CE2 . PHE A 153 ? 0.1152 0.0813 0.1136 -0.0167 -0.0188 0.0158  155 PHE A CE2 
2442 C  CZ  . PHE A 153 ? 0.1137 0.0822 0.1117 -0.0182 -0.0181 0.0172  155 PHE A CZ  
2452 N  N   . LEU A 154 ? 0.1932 0.1313 0.1726 -0.0292 -0.0446 0.0237  156 LEU A N   
2453 C  CA  . LEU A 154 ? 0.2210 0.1524 0.1952 -0.0335 -0.0508 0.0261  156 LEU A CA  
2454 C  C   . LEU A 154 ? 0.2698 0.1958 0.2384 -0.0377 -0.0558 0.0293  156 LEU A C   
2455 O  O   . LEU A 154 ? 0.2880 0.2143 0.2533 -0.0446 -0.0586 0.0335  156 LEU A O   
2456 C  CB  . LEU A 154 ? 0.2744 0.1972 0.2465 -0.0290 -0.0547 0.0228  156 LEU A CB  
2457 C  CG  . LEU A 154 ? 0.2424 0.1689 0.2186 -0.0254 -0.0511 0.0199  156 LEU A CG  
2458 C  CD1 . LEU A 154 ? 0.2718 0.1901 0.2452 -0.0199 -0.0546 0.0159  156 LEU A CD1 
2459 C  CD2 . LEU A 154 ? 0.2764 0.2061 0.2530 -0.0305 -0.0514 0.0225  156 LEU A CD2 
2471 N  N   . ALA A 155 ? 0.2087 0.1299 0.1760 -0.0339 -0.0572 0.0274  157 ALA A N   
2472 C  CA  . ALA A 155 ? 0.2665 0.1821 0.2283 -0.0377 -0.0621 0.0304  157 ALA A CA  
2473 C  C   . ALA A 155 ? 0.2881 0.2132 0.2507 -0.0440 -0.0586 0.0345  157 ALA A C   
2474 O  O   . ALA A 155 ? 0.3184 0.2414 0.2758 -0.0506 -0.0626 0.0386  157 ALA A O   
2475 C  CB  . ALA A 155 ? 0.2667 0.1770 0.2280 -0.0319 -0.0633 0.0273  157 ALA A CB  
2481 N  N   . CYS A 156 ? 0.2415 0.1770 0.2100 -0.0420 -0.0514 0.0334  158 CYS A N   
2482 C  CA  . CYS A 156 ? 0.2566 0.2021 0.2258 -0.0470 -0.0479 0.0365  158 CYS A CA  
2483 C  C   . CYS A 156 ? 0.2346 0.1859 0.2026 -0.0539 -0.0483 0.0400  158 CYS A C   
2484 O  O   . CYS A 156 ? 0.2654 0.2196 0.2295 -0.0606 -0.0501 0.0441  158 CYS A O   
2485 C  CB  . CYS A 156 ? 0.2308 0.1851 0.2060 -0.0429 -0.0409 0.0340  158 CYS A CB  
2486 S  SG  . CYS A 156 ? 0.2392 0.2056 0.2145 -0.0478 -0.0367 0.0369  158 CYS A SG  
2492 N  N   . ALA A 157 ? 0.2164 0.1694 0.1874 -0.0527 -0.0471 0.0387  159 ALA A N   
2493 C  CA  . ALA A 157 ? 0.2514 0.2110 0.2219 -0.0593 -0.0473 0.0420  159 ALA A CA  
2494 C  C   . ALA A 157 ? 0.2554 0.2066 0.2184 -0.0657 -0.0549 0.0460  159 ALA A C   
2495 O  O   . ALA A 157 ? 0.3009 0.2590 0.2616 -0.0734 -0.0554 0.0502  159 ALA A O   
2496 C  CB  . ALA A 157 ? 0.2213 0.1826 0.1963 -0.0562 -0.0452 0.0394  159 ALA A CB  
2502 N  N   . LYS A 158 ? 0.2909 0.2279 0.2498 -0.0626 -0.0608 0.0445  160 LYS A N   
2503 C  CA  . LYS A 158 ? 0.3604 0.2869 0.3111 -0.0684 -0.0692 0.0480  160 LYS A CA  
2504 C  C   . LYS A 158 ? 0.4020 0.3273 0.3470 -0.0745 -0.0722 0.0520  160 LYS A C   
2505 O  O   . LYS A 158 ? 0.4406 0.3575 0.3779 -0.0806 -0.0795 0.0557  160 LYS A O   
2506 C  CB  . LYS A 158 ? 0.3648 0.2758 0.3119 -0.0628 -0.0753 0.0447  160 LYS A CB  
2507 C  CG  . LYS A 158 ? 0.4135 0.3225 0.3632 -0.0586 -0.0751 0.0417  160 LYS A CG  
2508 C  CD  . LYS A 158 ? 0.4690 0.3651 0.4159 -0.0512 -0.0798 0.0371  160 LYS A CD  
2509 C  CE  . LYS A 158 ? 0.5252 0.4213 0.4755 -0.0462 -0.0783 0.0334  160 LYS A CE  
2510 N  NZ  . LYS A 158 ? 0.6053 0.4925 0.5540 -0.0378 -0.0810 0.0279  160 LYS A NZ  
2524 N  N   . ARG A 159 ? 0.3289 0.2619 0.2769 -0.0730 -0.0673 0.0515  161 ARG A N   
2525 C  CA  . ARG A 159 ? 0.3274 0.2590 0.2698 -0.0784 -0.0702 0.0550  161 ARG A CA  
2526 C  C   . ARG A 159 ? 0.3723 0.3196 0.3154 -0.0860 -0.0660 0.0590  161 ARG A C   
2527 O  O   . ARG A 159 ? 0.3981 0.3461 0.3362 -0.0917 -0.0681 0.0624  161 ARG A O   
2528 C  CB  . ARG A 159 ? 0.3548 0.2829 0.2986 -0.0721 -0.0687 0.0519  161 ARG A CB  
2529 C  CG  . ARG A 159 ? 0.3160 0.2292 0.2578 -0.0655 -0.0739 0.0482  161 ARG A CG  
2530 C  CD  . ARG A 159 ? 0.3512 0.2620 0.2950 -0.0589 -0.0723 0.0449  161 ARG A CD  
2531 N  NE  . ARG A 159 ? 0.3274 0.2275 0.2710 -0.0516 -0.0760 0.0405  161 ARG A NE  
2532 C  CZ  . ARG A 159 ? 0.3560 0.2511 0.3003 -0.0450 -0.0766 0.0369  161 ARG A CZ  
2533 N  NH1 . ARG A 159 ? 0.3288 0.2279 0.2742 -0.0449 -0.0740 0.0377  161 ARG A NH1 
2534 N  NH2 . ARG A 159 ? 0.3516 0.2388 0.2957 -0.0384 -0.0796 0.0326  161 ARG A NH2 
2548 N  N   . PHE A 160 ? 0.3767 0.3370 0.3256 -0.0862 -0.0602 0.0584  162 PHE A N   
2549 C  CA  . PHE A 160 ? 0.3949 0.3716 0.3440 -0.0939 -0.0569 0.0620  162 PHE A CA  
2550 C  C   . PHE A 160 ? 0.4663 0.4394 0.4084 -0.1034 -0.0635 0.0673  162 PHE A C   
2551 O  O   . PHE A 160 ? 0.4772 0.4374 0.4164 -0.1029 -0.0691 0.0673  162 PHE A O   
2552 C  CB  . PHE A 160 ? 0.3537 0.3449 0.3106 -0.0915 -0.0499 0.0596  162 PHE A CB  
2553 C  CG  . PHE A 160 ? 0.3230 0.3215 0.2861 -0.0844 -0.0430 0.0554  162 PHE A CG  
2554 C  CD1 . PHE A 160 ? 0.3286 0.3390 0.2919 -0.0863 -0.0392 0.0560  162 PHE A CD1 
2555 C  CD2 . PHE A 160 ? 0.2860 0.2802 0.2546 -0.0761 -0.0404 0.0507  162 PHE A CD2 
2556 C  CE1 . PHE A 160 ? 0.3216 0.3379 0.2900 -0.0797 -0.0333 0.0521  162 PHE A CE1 
2557 C  CE2 . PHE A 160 ? 0.2904 0.2907 0.2640 -0.0703 -0.0346 0.0472  162 PHE A CE2 
2558 C  CZ  . PHE A 160 ? 0.2877 0.2986 0.2611 -0.0721 -0.0313 0.0479  162 PHE A CZ  
2568 N  N   . SER A 161 ? 0.5711 0.5564 0.5104 -0.1122 -0.0628 0.0717  163 SER A N   
2569 C  CA  . SER A 161 ? 0.6122 0.5957 0.5439 -0.1230 -0.0692 0.0776  163 SER A CA  
2570 C  C   . SER A 161 ? 0.6118 0.6169 0.5463 -0.1301 -0.0647 0.0802  163 SER A C   
2571 O  O   . SER A 161 ? 0.6579 0.6790 0.5937 -0.1331 -0.0602 0.0811  163 SER A O   
2572 C  CB  . SER A 161 ? 0.6234 0.6001 0.5470 -0.1286 -0.0743 0.0813  163 SER A CB  
2573 O  OG  . SER A 161 ? 0.7071 0.6807 0.6223 -0.1399 -0.0812 0.0874  163 SER A OG  
2579 N  N   . PRO A 162 ? 0.5363 0.5431 0.4723 -0.1324 -0.0657 0.0811  164 PRO A N   
2580 C  CA  . PRO A 162 ? 0.5298 0.5196 0.4649 -0.1285 -0.0704 0.0796  164 PRO A CA  
2581 C  C   . PRO A 162 ? 0.4479 0.4364 0.3917 -0.1166 -0.0650 0.0729  164 PRO A C   
2582 O  O   . PRO A 162 ? 0.4597 0.4627 0.4104 -0.1128 -0.0574 0.0700  164 PRO A O   
2583 C  CB  . PRO A 162 ? 0.5494 0.5474 0.4839 -0.1369 -0.0719 0.0833  164 PRO A CB  
2584 C  CG  . PRO A 162 ? 0.5729 0.5964 0.5132 -0.1398 -0.0641 0.0835  164 PRO A CG  
2585 C  CD  . PRO A 162 ? 0.5338 0.5617 0.4720 -0.1400 -0.0622 0.0838  164 PRO A CD  
2593 N  N   . PRO A 163 ? 0.4867 0.4583 0.4295 -0.1111 -0.0692 0.0704  165 PRO A N   
2594 C  CA  . PRO A 163 ? 0.3913 0.3610 0.3414 -0.1001 -0.0645 0.0642  165 PRO A CA  
2595 C  C   . PRO A 163 ? 0.4415 0.4225 0.3989 -0.0990 -0.0596 0.0624  165 PRO A C   
2596 O  O   . PRO A 163 ? 0.4627 0.4417 0.4183 -0.1036 -0.0632 0.0645  165 PRO A O   
2597 C  CB  . PRO A 163 ? 0.4564 0.4053 0.4018 -0.0956 -0.0716 0.0624  165 PRO A CB  
2598 C  CG  . PRO A 163 ? 0.5404 0.4793 0.4759 -0.1031 -0.0799 0.0672  165 PRO A CG  
2599 C  CD  . PRO A 163 ? 0.5388 0.4913 0.4728 -0.1139 -0.0790 0.0727  165 PRO A CD  
2607 N  N   . PRO A 164 ? 0.3809 0.3729 0.3461 -0.0930 -0.0520 0.0583  166 PRO A N   
2608 C  CA  . PRO A 164 ? 0.3896 0.3921 0.3620 -0.0913 -0.0477 0.0560  166 PRO A CA  
2609 C  C   . PRO A 164 ? 0.3820 0.3716 0.3560 -0.0852 -0.0499 0.0526  166 PRO A C   
2610 O  O   . PRO A 164 ? 0.3644 0.3390 0.3353 -0.0800 -0.0532 0.0507  166 PRO A O   
2611 C  CB  . PRO A 164 ? 0.3531 0.3681 0.3320 -0.0860 -0.0402 0.0525  166 PRO A CB  
2612 C  CG  . PRO A 164 ? 0.3635 0.3667 0.3395 -0.0810 -0.0412 0.0511  166 PRO A CG  
2613 C  CD  . PRO A 164 ? 0.3262 0.3197 0.2937 -0.0870 -0.0478 0.0555  166 PRO A CD  
2621 N  N   . ALA A 165 ? 0.3568 0.3533 0.3357 -0.0857 -0.0483 0.0515  167 ALA A N   
2622 C  CA  . ALA A 165 ? 0.3285 0.3164 0.3103 -0.0791 -0.0488 0.0474  167 ALA A CA  
2623 C  C   . ALA A 165 ? 0.2920 0.2814 0.2785 -0.0708 -0.0436 0.0428  167 ALA A C   
2624 O  O   . ALA A 165 ? 0.2877 0.2901 0.2781 -0.0708 -0.0384 0.0423  167 ALA A O   
2625 C  CB  . ALA A 165 ? 0.3116 0.3097 0.2989 -0.0816 -0.0475 0.0468  167 ALA A CB  
2631 N  N   . MET A 166 ? 0.3418 0.3186 0.3277 -0.0640 -0.0452 0.0394  168 MET A N   
2632 C  CA  . MET A 166 ? 0.2908 0.2678 0.2802 -0.0568 -0.0409 0.0355  168 MET A CA  
2633 C  C   . MET A 166 ? 0.2871 0.2779 0.2839 -0.0558 -0.0355 0.0335  168 MET A C   
2634 O  O   . MET A 166 ? 0.2673 0.2644 0.2673 -0.0529 -0.0311 0.0319  168 MET A O   
2635 C  CB  . MET A 166 ? 0.2902 0.2535 0.2776 -0.0499 -0.0435 0.0320  168 MET A CB  
2636 C  CG  . MET A 166 ? 0.3546 0.3049 0.3350 -0.0496 -0.0495 0.0328  168 MET A CG  
2637 S  SD  . MET A 166 ? 0.3603 0.3101 0.3375 -0.0510 -0.0496 0.0348  168 MET A SD  
2638 C  CE  . MET A 166 ? 0.4286 0.3858 0.4029 -0.0618 -0.0514 0.0411  168 MET A CE  
2648 N  N   . GLU A 167 ? 0.2807 0.2768 0.2806 -0.0581 -0.0363 0.0333  169 GLU A N   
2649 C  CA  . GLU A 167 ? 0.2521 0.2621 0.2597 -0.0566 -0.0322 0.0306  169 GLU A CA  
2650 C  C   . GLU A 167 ? 0.2318 0.2606 0.2430 -0.0597 -0.0279 0.0317  169 GLU A C   
2651 O  O   . GLU A 167 ? 0.2387 0.2808 0.2564 -0.0569 -0.0245 0.0287  169 GLU A O   
2652 C  CB  . GLU A 167 ? 0.3206 0.3328 0.3309 -0.0579 -0.0347 0.0296  169 GLU A CB  
2653 C  CG  . GLU A 167 ? 0.3791 0.3976 0.3882 -0.0658 -0.0370 0.0334  169 GLU A CG  
2654 C  CD  . GLU A 167 ? 0.5373 0.5598 0.5499 -0.0674 -0.0393 0.0322  169 GLU A CD  
2655 O  OE1 . GLU A 167 ? 0.6220 0.6360 0.6352 -0.0625 -0.0412 0.0289  169 GLU A OE1 
2656 O  OE2 . GLU A 167 ? 0.5614 0.5965 0.5759 -0.0737 -0.0393 0.0346  169 GLU A OE2 
2663 N  N   . LYS A 168 ? 0.1971 0.2274 0.2037 -0.0648 -0.0284 0.0355  170 LYS A N   
2664 C  CA  . LYS A 168 ? 0.2243 0.2726 0.2330 -0.0672 -0.0241 0.0363  170 LYS A CA  
2665 C  C   . LYS A 168 ? 0.1970 0.2423 0.2033 -0.0643 -0.0219 0.0359  170 LYS A C   
2666 O  O   . LYS A 168 ? 0.2143 0.2720 0.2204 -0.0663 -0.0190 0.0367  170 LYS A O   
2667 C  CB  . LYS A 168 ? 0.2482 0.3031 0.2531 -0.0758 -0.0262 0.0410  170 LYS A CB  
2668 C  CG  . LYS A 168 ? 0.2624 0.3252 0.2706 -0.0799 -0.0277 0.0416  170 LYS A CG  
2669 C  CD  . LYS A 168 ? 0.3050 0.3860 0.3222 -0.0760 -0.0236 0.0372  170 LYS A CD  
2670 C  CE  . LYS A 168 ? 0.3780 0.4636 0.3983 -0.0794 -0.0261 0.0374  170 LYS A CE  
2671 N  NZ  . LYS A 168 ? 0.4119 0.5137 0.4415 -0.0736 -0.0231 0.0321  170 LYS A NZ  
2685 N  N   . CYS A 169 ? 0.1951 0.2242 0.1993 -0.0594 -0.0233 0.0344  171 CYS A N   
2686 C  CA  . CYS A 169 ? 0.1971 0.2224 0.1995 -0.0562 -0.0215 0.0337  171 CYS A CA  
2687 C  C   . CYS A 169 ? 0.1706 0.1992 0.1784 -0.0502 -0.0178 0.0296  171 CYS A C   
2688 O  O   . CYS A 169 ? 0.1680 0.1922 0.1788 -0.0468 -0.0185 0.0271  171 CYS A O   
2689 C  CB  . CYS A 169 ? 0.2123 0.2191 0.2092 -0.0542 -0.0257 0.0343  171 CYS A CB  
2690 S  SG  . CYS A 169 ? 0.2620 0.2632 0.2515 -0.0612 -0.0313 0.0392  171 CYS A SG  
2696 N  N   . LEU A 170 ? 0.1518 0.1879 0.1603 -0.0489 -0.0144 0.0288  172 LEU A N   
2697 C  CA  . LEU A 170 ? 0.1354 0.1743 0.1481 -0.0436 -0.0114 0.0252  172 LEU A CA  
2698 C  C   . LEU A 170 ? 0.1114 0.1394 0.1202 -0.0414 -0.0112 0.0254  172 LEU A C   
2699 O  O   . LEU A 170 ? 0.1321 0.1634 0.1376 -0.0435 -0.0104 0.0270  172 LEU A O   
2700 C  CB  . LEU A 170 ? 0.1361 0.1970 0.1535 -0.0429 -0.0074 0.0230  172 LEU A CB  
2701 C  CG  . LEU A 170 ? 0.1356 0.1975 0.1543 -0.0334 -0.0048 0.0172  172 LEU A CG  
2702 C  CD1 . LEU A 170 ? 0.1350 0.1880 0.1553 -0.0279 -0.0065 0.0143  172 LEU A CD1 
2703 C  CD2 . LEU A 170 ? 0.1652 0.2469 0.1863 -0.0305 -0.0014 0.0138  172 LEU A CD2 
2715 N  N   . VAL A 171 ? 0.1198 0.1360 0.1289 -0.0370 -0.0119 0.0235  173 VAL A N   
2716 C  CA  . VAL A 171 ? 0.0997 0.1064 0.1058 -0.0338 -0.0115 0.0229  173 VAL A CA  
2717 C  C   . VAL A 171 ? 0.0910 0.1029 0.0981 -0.0280 -0.0079 0.0187  173 VAL A C   
2718 O  O   . VAL A 171 ? 0.1152 0.1304 0.1245 -0.0235 -0.0067 0.0153  173 VAL A O   
2719 C  CB  . VAL A 171 ? 0.1139 0.1063 0.1184 -0.0295 -0.0139 0.0213  173 VAL A CB  
2720 C  CG1 . VAL A 171 ? 0.1214 0.1071 0.1242 -0.0253 -0.0130 0.0197  173 VAL A CG1 
2721 C  CG2 . VAL A 171 ? 0.1344 0.1213 0.1358 -0.0310 -0.0175 0.0227  173 VAL A CG2 
2731 N  N   . PHE A 172 ? 0.1131 0.1237 0.1177 -0.0276 -0.0070 0.0189  174 PHE A N   
2732 C  CA  . PHE A 172 ? 0.0970 0.1077 0.1009 -0.0221 -0.0048 0.0149  174 PHE A CA  
2733 C  C   . PHE A 172 ? 0.0851 0.0835 0.0874 -0.0204 -0.0059 0.0149  174 PHE A C   
2734 O  O   . PHE A 172 ? 0.1150 0.1096 0.1156 -0.0233 -0.0075 0.0176  174 PHE A O   
2735 C  CB  . PHE A 172 ? 0.1004 0.1214 0.1025 -0.0229 -0.0029 0.0144  174 PHE A CB  
2736 C  CG  . PHE A 172 ? 0.1281 0.1644 0.1323 -0.0230 -0.0010 0.0130  174 PHE A CG  
2737 C  CD1 . PHE A 172 ? 0.1377 0.1823 0.1434 -0.0293 -0.0015 0.0168  174 PHE A CD1 
2738 C  CD2 . PHE A 172 ? 0.1522 0.1950 0.1568 -0.0166 0.0007  0.0077  174 PHE A CD2 
2739 C  CE1 . PHE A 172 ? 0.1778 0.2401 0.1865 -0.0300 0.0004  0.0156  174 PHE A CE1 
2740 C  CE2 . PHE A 172 ? 0.1904 0.2506 0.1977 -0.0158 0.0023  0.0058  174 PHE A CE2 
2741 C  CZ  . PHE A 172 ? 0.1837 0.2544 0.1936 -0.0225 0.0025  0.0097  174 PHE A CZ  
2751 N  N   . GLU A 173 ? 0.0915 0.0846 0.0941 -0.0160 -0.0053 0.0120  175 GLU A N   
2752 C  CA  . GLU A 173 ? 0.0970 0.0812 0.0989 -0.0148 -0.0061 0.0119  175 GLU A CA  
2753 C  C   . GLU A 173 ? 0.0885 0.0702 0.0891 -0.0117 -0.0049 0.0090  175 GLU A C   
2754 O  O   . GLU A 173 ? 0.1137 0.0964 0.1136 -0.0090 -0.0044 0.0066  175 GLU A O   
2755 C  CB  . GLU A 173 ? 0.1022 0.0808 0.1052 -0.0142 -0.0073 0.0124  175 GLU A CB  
2756 C  CG  . GLU A 173 ? 0.0891 0.0654 0.0917 -0.0156 -0.0094 0.0142  175 GLU A CG  
2757 C  CD  . GLU A 173 ? 0.0873 0.0616 0.0894 -0.0140 -0.0096 0.0135  175 GLU A CD  
2758 O  OE1 . GLU A 173 ? 0.1303 0.1027 0.1315 -0.0141 -0.0119 0.0143  175 GLU A OE1 
2759 O  OE2 . GLU A 173 ? 0.1058 0.0798 0.1082 -0.0130 -0.0082 0.0123  175 GLU A OE2 
2766 N  N   . ASP A 174 ? 0.0844 0.0621 0.0842 -0.0121 -0.0052 0.0091  176 ASP A N   
2767 C  CA  . ASP A 174 ? 0.0986 0.0720 0.0967 -0.0106 -0.0050 0.0071  176 ASP A CA  
2768 C  C   . ASP A 174 ? 0.1051 0.0739 0.1039 -0.0107 -0.0049 0.0077  176 ASP A C   
2769 O  O   . ASP A 174 ? 0.1244 0.0891 0.1211 -0.0104 -0.0049 0.0067  176 ASP A O   
2770 C  CB  . ASP A 174 ? 0.1041 0.0775 0.1008 -0.0119 -0.0054 0.0067  176 ASP A CB  
2771 C  CG  . ASP A 174 ? 0.1159 0.0896 0.1148 -0.0138 -0.0062 0.0086  176 ASP A CG  
2772 O  OD1 . ASP A 174 ? 0.1288 0.1040 0.1292 -0.0143 -0.0069 0.0105  176 ASP A OD1 
2773 O  OD2 . ASP A 174 ? 0.1292 0.1017 0.1283 -0.0148 -0.0066 0.0082  176 ASP A OD2 
2778 N  N   . ALA A 175 ? 0.1071 0.0772 0.1082 -0.0106 -0.0051 0.0088  177 ALA A N   
2779 C  CA  . ALA A 175 ? 0.1125 0.0822 0.1142 -0.0099 -0.0044 0.0085  177 ALA A CA  
2780 C  C   . ALA A 175 ? 0.0931 0.0616 0.0943 -0.0081 -0.0041 0.0081  177 ALA A C   
2781 O  O   . ALA A 175 ? 0.0846 0.0536 0.0863 -0.0076 -0.0050 0.0084  177 ALA A O   
2782 C  CB  . ALA A 175 ? 0.1275 0.0987 0.1313 -0.0102 -0.0057 0.0094  177 ALA A CB  
2788 N  N   . PRO A 176 ? 0.1000 0.0668 0.1002 -0.0078 -0.0032 0.0079  178 PRO A N   
2789 C  CA  . PRO A 176 ? 0.0932 0.0584 0.0924 -0.0061 -0.0033 0.0076  178 PRO A CA  
2790 C  C   . PRO A 176 ? 0.1120 0.0774 0.1128 -0.0048 -0.0050 0.0075  178 PRO A C   
2791 O  O   . PRO A 176 ? 0.1009 0.0655 0.1010 -0.0037 -0.0058 0.0071  178 PRO A O   
2792 C  CB  . PRO A 176 ? 0.1291 0.0923 0.1262 -0.0074 -0.0025 0.0083  178 PRO A CB  
2793 C  CG  . PRO A 176 ? 0.1659 0.1297 0.1626 -0.0099 -0.0018 0.0087  178 PRO A CG  
2794 C  CD  . PRO A 176 ? 0.0975 0.0637 0.0967 -0.0099 -0.0025 0.0083  178 PRO A CD  
2802 N  N   . ASN A 177 ? 0.0992 0.0648 0.1019 -0.0048 -0.0063 0.0079  179 ASN A N   
2803 C  CA  . ASN A 177 ? 0.0971 0.0609 0.1002 -0.0024 -0.0089 0.0073  179 ASN A CA  
2804 C  C   . ASN A 177 ? 0.1146 0.0792 0.1170 -0.0037 -0.0100 0.0078  179 ASN A C   
2805 O  O   . ASN A 177 ? 0.1076 0.0700 0.1088 -0.0028 -0.0120 0.0074  179 ASN A O   
2806 C  CB  . ASN A 177 ? 0.1224 0.0897 0.1276 -0.0009 -0.0099 0.0065  179 ASN A CB  
2807 C  CG  . ASN A 177 ? 0.1452 0.1189 0.1515 0.0011  -0.0078 0.0047  179 ASN A CG  
2808 O  OD1 . ASN A 177 ? 0.1435 0.1177 0.1481 0.0021  -0.0064 0.0038  179 ASN A OD1 
2809 N  ND2 . ASN A 177 ? 0.1431 0.1230 0.1523 0.0014  -0.0077 0.0042  179 ASN A ND2 
2816 N  N   . GLY A 178 ? 0.1001 0.0672 0.1029 -0.0060 -0.0090 0.0089  180 GLY A N   
2817 C  CA  . GLY A 178 ? 0.1055 0.0735 0.1079 -0.0079 -0.0103 0.0101  180 GLY A CA  
2818 C  C   . GLY A 178 ? 0.0991 0.0676 0.1013 -0.0086 -0.0100 0.0101  180 GLY A C   
2819 O  O   . GLY A 178 ? 0.0974 0.0655 0.0993 -0.0101 -0.0122 0.0110  180 GLY A O   
2823 N  N   . VAL A 179 ? 0.0816 0.0502 0.0838 -0.0076 -0.0082 0.0091  181 VAL A N   
2824 C  CA  . VAL A 179 ? 0.0928 0.0611 0.0951 -0.0076 -0.0089 0.0091  181 VAL A CA  
2825 C  C   . VAL A 179 ? 0.0862 0.0522 0.0876 -0.0064 -0.0104 0.0084  181 VAL A C   
2826 O  O   . VAL A 179 ? 0.1101 0.0759 0.1119 -0.0079 -0.0126 0.0090  181 VAL A O   
2827 C  CB  . VAL A 179 ? 0.1015 0.0682 0.1026 -0.0056 -0.0074 0.0079  181 VAL A CB  
2828 C  CG1 . VAL A 179 ? 0.1166 0.0817 0.1173 -0.0044 -0.0088 0.0074  181 VAL A CG1 
2829 C  CG2 . VAL A 179 ? 0.1085 0.0765 0.1099 -0.0063 -0.0069 0.0080  181 VAL A CG2 
2839 N  N   . GLU A 180 ? 0.1021 0.0661 0.1022 -0.0041 -0.0098 0.0072  182 GLU A N   
2840 C  CA  . GLU A 180 ? 0.1200 0.0810 0.1186 -0.0025 -0.0117 0.0061  182 GLU A CA  
2841 C  C   . GLU A 180 ? 0.1264 0.0857 0.1247 -0.0037 -0.0151 0.0066  182 GLU A C   
2842 O  O   . GLU A 180 ? 0.1242 0.0810 0.1213 -0.0040 -0.0178 0.0063  182 GLU A O   
2843 C  CB  . GLU A 180 ? 0.1360 0.0951 0.1333 0.0003  -0.0109 0.0048  182 GLU A CB  
2844 C  CG  . GLU A 180 ? 0.1549 0.1137 0.1508 0.0008  -0.0086 0.0048  182 GLU A CG  
2845 C  CD  . GLU A 180 ? 0.1916 0.1492 0.1855 0.0014  -0.0091 0.0043  182 GLU A CD  
2846 O  OE1 . GLU A 180 ? 0.1766 0.1331 0.1701 0.0018  -0.0114 0.0036  182 GLU A OE1 
2847 O  OE2 . GLU A 180 ? 0.2641 0.2213 0.2564 0.0012  -0.0076 0.0048  182 GLU A OE2 
2854 N  N   . ALA A 181 ? 0.1080 0.0677 0.1069 -0.0047 -0.0157 0.0076  183 ALA A N   
2855 C  CA  . ALA A 181 ? 0.1272 0.0841 0.1247 -0.0063 -0.0196 0.0086  183 ALA A CA  
2856 C  C   . ALA A 181 ? 0.1098 0.0680 0.1075 -0.0105 -0.0210 0.0107  183 ALA A C   
2857 O  O   . ALA A 181 ? 0.1335 0.0883 0.1293 -0.0120 -0.0247 0.0113  183 ALA A O   
2858 C  CB  . ALA A 181 ? 0.1320 0.0888 0.1295 -0.0066 -0.0202 0.0095  183 ALA A CB  
2864 N  N   . ALA A 182 ? 0.1094 0.0724 0.1091 -0.0125 -0.0185 0.0119  184 ALA A N   
2865 C  CA  . ALA A 182 ? 0.1147 0.0810 0.1155 -0.0170 -0.0197 0.0142  184 ALA A CA  
2866 C  C   . ALA A 182 ? 0.1167 0.0814 0.1177 -0.0168 -0.0214 0.0135  184 ALA A C   
2867 O  O   . ALA A 182 ? 0.1525 0.1167 0.1527 -0.0204 -0.0247 0.0151  184 ALA A O   
2868 C  CB  . ALA A 182 ? 0.1123 0.0850 0.1157 -0.0188 -0.0168 0.0153  184 ALA A CB  
2874 N  N   . LEU A 183 ? 0.1112 0.0747 0.1125 -0.0131 -0.0198 0.0112  185 LEU A N   
2875 C  CA  . LEU A 183 ? 0.1332 0.0944 0.1341 -0.0126 -0.0219 0.0102  185 LEU A CA  
2876 C  C   . LEU A 183 ? 0.1534 0.1093 0.1510 -0.0119 -0.0253 0.0095  185 LEU A C   
2877 O  O   . LEU A 183 ? 0.1824 0.1364 0.1794 -0.0142 -0.0289 0.0100  185 LEU A O   
2878 C  CB  . LEU A 183 ? 0.1355 0.0957 0.1356 -0.0082 -0.0195 0.0080  185 LEU A CB  
2879 C  CG  . LEU A 183 ? 0.1302 0.0932 0.1325 -0.0079 -0.0173 0.0085  185 LEU A CG  
2880 C  CD1 . LEU A 183 ? 0.1664 0.1273 0.1659 -0.0035 -0.0153 0.0065  185 LEU A CD1 
2881 C  CD2 . LEU A 183 ? 0.1591 0.1304 0.1647 -0.0100 -0.0182 0.0089  185 LEU A CD2 
2893 N  N   . ALA A 184 ? 0.1294 0.0826 0.1251 -0.0090 -0.0249 0.0081  186 ALA A N   
2894 C  CA  . ALA A 184 ? 0.1742 0.1212 0.1663 -0.0079 -0.0291 0.0069  186 ALA A CA  
2895 C  C   . ALA A 184 ? 0.1904 0.1348 0.1810 -0.0123 -0.0335 0.0096  186 ALA A C   
2896 O  O   . ALA A 184 ? 0.2311 0.1697 0.2184 -0.0125 -0.0382 0.0091  186 ALA A O   
2897 C  CB  . ALA A 184 ? 0.1635 0.1085 0.1542 -0.0038 -0.0284 0.0049  186 ALA A CB  
2903 N  N   . ALA A 185 ? 0.1566 0.1051 0.1490 -0.0160 -0.0323 0.0123  187 ALA A N   
2904 C  CA  . ALA A 185 ? 0.1792 0.1265 0.1696 -0.0213 -0.0360 0.0157  187 ALA A CA  
2905 C  C   . ALA A 185 ? 0.2097 0.1610 0.2016 -0.0263 -0.0370 0.0181  187 ALA A C   
2906 O  O   . ALA A 185 ? 0.2602 0.2114 0.2502 -0.0317 -0.0401 0.0214  187 ALA A O   
2907 C  CB  . ALA A 185 ? 0.1743 0.1253 0.1653 -0.0235 -0.0343 0.0179  187 ALA A CB  
2913 N  N   . GLY A 186 ? 0.1778 0.1329 0.1731 -0.0250 -0.0346 0.0166  188 GLY A N   
2914 C  CA  . GLY A 186 ? 0.1979 0.1589 0.1960 -0.0297 -0.0354 0.0184  188 GLY A CA  
2915 C  C   . GLY A 186 ? 0.1777 0.1506 0.1800 -0.0343 -0.0322 0.0207  188 GLY A C   
2916 O  O   . GLY A 186 ? 0.2058 0.1873 0.2106 -0.0396 -0.0328 0.0227  188 GLY A O   
2920 N  N   . MET A 187 ? 0.1621 0.1375 0.1656 -0.0321 -0.0286 0.0202  189 MET A N   
2921 C  CA  . MET A 187 ? 0.1581 0.1454 0.1648 -0.0357 -0.0254 0.0220  189 MET A CA  
2922 C  C   . MET A 187 ? 0.1302 0.1249 0.1425 -0.0334 -0.0226 0.0197  189 MET A C   
2923 O  O   . MET A 187 ? 0.1694 0.1565 0.1804 -0.0272 -0.0218 0.0169  189 MET A O   
2924 C  CB  . MET A 187 ? 0.1405 0.1254 0.1441 -0.0354 -0.0244 0.0231  189 MET A CB  
2925 C  CG  . MET A 187 ? 0.1571 0.1348 0.1553 -0.0377 -0.0284 0.0253  189 MET A CG  
2926 S  SD  . MET A 187 ? 0.1792 0.1540 0.1743 -0.0368 -0.0281 0.0261  189 MET A SD  
2927 C  CE  . MET A 187 ? 0.2123 0.1794 0.2014 -0.0411 -0.0345 0.0291  189 MET A CE  
2937 N  N   . GLN A 188 ? 0.1408 0.1514 0.1572 -0.0348 -0.0199 0.0196  190 GLN A N   
2938 C  CA  . GLN A 188 ? 0.1430 0.1594 0.1611 -0.0275 -0.0161 0.0155  190 GLN A CA  
2939 C  C   . GLN A 188 ? 0.1113 0.1234 0.1267 -0.0254 -0.0135 0.0155  190 GLN A C   
2940 O  O   . GLN A 188 ? 0.1083 0.1183 0.1218 -0.0302 -0.0141 0.0186  190 GLN A O   
2941 C  CB  . GLN A 188 ? 0.1501 0.1856 0.1731 -0.0273 -0.0143 0.0140  190 GLN A CB  
2942 C  CG  . GLN A 188 ? 0.1668 0.2095 0.1937 -0.0288 -0.0168 0.0135  190 GLN A CG  
2943 C  CD  . GLN A 188 ? 0.1714 0.2365 0.2041 -0.0292 -0.0150 0.0121  190 GLN A CD  
2944 O  OE1 . GLN A 188 ? 0.1987 0.2705 0.2337 -0.0218 -0.0142 0.0076  190 GLN A OE1 
2945 N  NE2 . GLN A 188 ? 0.1889 0.2654 0.2231 -0.0371 -0.0143 0.0156  190 GLN A NE2 
2954 N  N   . VAL A 189 ? 0.1064 0.1171 0.1213 -0.0188 -0.0113 0.0120  191 VAL A N   
2955 C  CA  . VAL A 189 ? 0.1049 0.1106 0.1171 -0.0168 -0.0094 0.0115  191 VAL A CA  
2956 C  C   . VAL A 189 ? 0.1088 0.1189 0.1209 -0.0110 -0.0073 0.0076  191 VAL A C   
2957 O  O   . VAL A 189 ? 0.1181 0.1255 0.1298 -0.0062 -0.0078 0.0050  191 VAL A O   
2958 C  CB  . VAL A 189 ? 0.1029 0.0943 0.1121 -0.0158 -0.0106 0.0121  191 VAL A CB  
2959 C  CG1 . VAL A 189 ? 0.1058 0.0909 0.1141 -0.0117 -0.0111 0.0100  191 VAL A CG1 
2960 C  CG2 . VAL A 189 ? 0.1136 0.1017 0.1209 -0.0146 -0.0089 0.0119  191 VAL A CG2 
2970 N  N   . VAL A 190 ? 0.1070 0.1225 0.1182 -0.0115 -0.0055 0.0074  192 VAL A N   
2971 C  CA  . VAL A 190 ? 0.1206 0.1366 0.1299 -0.0059 -0.0043 0.0036  192 VAL A CA  
2972 C  C   . VAL A 190 ? 0.1049 0.1084 0.1106 -0.0056 -0.0043 0.0040  192 VAL A C   
2973 O  O   . VAL A 190 ? 0.1135 0.1159 0.1187 -0.0094 -0.0041 0.0065  192 VAL A O   
2974 C  CB  . VAL A 190 ? 0.1269 0.1574 0.1370 -0.0061 -0.0025 0.0022  192 VAL A CB  
2975 C  CG1 . VAL A 190 ? 0.1590 0.1875 0.1657 0.0006  -0.0021 -0.0026 192 VAL A CG1 
2976 C  CG2 . VAL A 190 ? 0.1455 0.1916 0.1601 -0.0068 -0.0022 0.0018  192 VAL A CG2 
2986 N  N   . MET A 191 ? 0.1061 0.1007 0.1093 -0.0015 -0.0050 0.0018  193 MET A N   
2987 C  CA  . MET A 191 ? 0.1025 0.0872 0.1026 -0.0019 -0.0050 0.0022  193 MET A CA  
2988 C  C   . MET A 191 ? 0.1264 0.1109 0.1234 0.0012  -0.0051 -0.0009 193 MET A C   
2989 O  O   . MET A 191 ? 0.1325 0.1176 0.1277 0.0061  -0.0062 -0.0043 193 MET A O   
2990 C  CB  . MET A 191 ? 0.0873 0.0621 0.0855 -0.0009 -0.0059 0.0025  193 MET A CB  
2991 C  CG  . MET A 191 ? 0.1049 0.0731 0.1015 -0.0031 -0.0056 0.0040  193 MET A CG  
2992 S  SD  . MET A 191 ? 0.1158 0.0745 0.1088 -0.0024 -0.0062 0.0042  193 MET A SD  
2993 C  CE  . MET A 191 ? 0.1577 0.1181 0.1523 -0.0056 -0.0044 0.0059  193 MET A CE  
3003 N  N   . VAL A 192 ? 0.1062 0.0884 0.1017 -0.0010 -0.0048 -0.0002 194 VAL A N   
3004 C  CA  . VAL A 192 ? 0.1339 0.1127 0.1250 0.0015  -0.0057 -0.0033 194 VAL A CA  
3005 C  C   . VAL A 192 ? 0.1163 0.0846 0.1052 -0.0011 -0.0066 -0.0019 194 VAL A C   
3006 O  O   . VAL A 192 ? 0.1213 0.0906 0.1107 -0.0041 -0.0062 -0.0006 194 VAL A O   
3007 C  CB  . VAL A 192 ? 0.1353 0.1239 0.1264 0.0010  -0.0046 -0.0042 194 VAL A CB  
3008 C  CG1 . VAL A 192 ? 0.1655 0.1504 0.1515 0.0048  -0.0061 -0.0084 194 VAL A CG1 
3009 C  CG2 . VAL A 192 ? 0.1507 0.1526 0.1449 0.0017  -0.0031 -0.0045 194 VAL A CG2 
3019 N  N   . PRO A 193 ? 0.1269 0.0867 0.1138 -0.0006 -0.0077 -0.0016 195 PRO A N   
3020 C  CA  . PRO A 193 ? 0.1257 0.0786 0.1114 -0.0044 -0.0081 0.0005  195 PRO A CA  
3021 C  C   . PRO A 193 ? 0.1545 0.1001 0.1351 -0.0050 -0.0103 -0.0010 195 PRO A C   
3022 O  O   . PRO A 193 ? 0.1586 0.0990 0.1345 -0.0012 -0.0126 -0.0042 195 PRO A O   
3023 C  CB  . PRO A 193 ? 0.1431 0.0902 0.1270 -0.0037 -0.0086 0.0014  195 PRO A CB  
3024 C  CG  . PRO A 193 ? 0.1519 0.0978 0.1336 0.0013  -0.0102 -0.0014 195 PRO A CG  
3025 C  CD  . PRO A 193 ? 0.1531 0.1101 0.1385 0.0033  -0.0089 -0.0030 195 PRO A CD  
3033 N  N   . ASP A 194 ? 0.1337 0.0788 0.1152 -0.0094 -0.0100 0.0010  196 ASP A N   
3034 C  CA  . ASP A 194 ? 0.1502 0.0907 0.1282 -0.0110 -0.0118 0.0004  196 ASP A CA  
3035 C  C   . ASP A 194 ? 0.1394 0.0755 0.1145 -0.0100 -0.0126 0.0009  196 ASP A C   
3036 O  O   . ASP A 194 ? 0.1531 0.0923 0.1305 -0.0105 -0.0109 0.0027  196 ASP A O   
3037 C  CB  . ASP A 194 ? 0.1571 0.1026 0.1385 -0.0159 -0.0107 0.0027  196 ASP A CB  
3038 C  CG  . ASP A 194 ? 0.2143 0.1549 0.1917 -0.0184 -0.0132 0.0023  196 ASP A CG  
3039 O  OD1 . ASP A 194 ? 0.1881 0.1249 0.1628 -0.0198 -0.0141 0.0033  196 ASP A OD1 
3040 O  OD2 . ASP A 194 ? 0.2535 0.1937 0.2301 -0.0196 -0.0147 0.0011  196 ASP A OD2 
3045 N  N   . GLY A 195 ? 0.1631 0.0914 0.1322 -0.0088 -0.0159 -0.0007 197 GLY A N   
3046 C  CA  . GLY A 195 ? 0.1757 0.0978 0.1402 -0.0082 -0.0179 -0.0001 197 GLY A CA  
3047 C  C   . GLY A 195 ? 0.1633 0.0861 0.1280 -0.0136 -0.0170 0.0034  197 GLY A C   
3048 O  O   . GLY A 195 ? 0.1626 0.0807 0.1233 -0.0135 -0.0183 0.0044  197 GLY A O   
3052 N  N   . ASN A 196 ? 0.1601 0.0883 0.1284 -0.0180 -0.0153 0.0050  198 ASN A N   
3053 C  CA  . ASN A 196 ? 0.1726 0.1035 0.1415 -0.0230 -0.0141 0.0080  198 ASN A CA  
3054 C  C   . ASN A 196 ? 0.1657 0.1032 0.1387 -0.0226 -0.0108 0.0094  198 ASN A C   
3055 O  O   . ASN A 196 ? 0.1857 0.1243 0.1575 -0.0264 -0.0101 0.0118  198 ASN A O   
3056 C  CB  . ASN A 196 ? 0.2110 0.1466 0.1826 -0.0276 -0.0137 0.0089  198 ASN A CB  
3057 C  CG  . ASN A 196 ? 0.2787 0.2068 0.2449 -0.0298 -0.0176 0.0085  198 ASN A CG  
3058 O  OD1 . ASN A 196 ? 0.3272 0.2502 0.2885 -0.0336 -0.0197 0.0103  198 ASN A OD1 
3059 N  ND2 . ASN A 196 ? 0.2750 0.2016 0.2411 -0.0280 -0.0189 0.0061  198 ASN A ND2 
3066 N  N   . LEU A 197 ? 0.1484 0.0899 0.1255 -0.0187 -0.0090 0.0081  199 LEU A N   
3067 C  CA  . LEU A 197 ? 0.1440 0.0901 0.1240 -0.0178 -0.0066 0.0092  199 LEU A CA  
3068 C  C   . LEU A 197 ? 0.1948 0.1356 0.1701 -0.0169 -0.0077 0.0098  199 LEU A C   
3069 O  O   . LEU A 197 ? 0.1552 0.0894 0.1263 -0.0145 -0.0103 0.0085  199 LEU A O   
3070 C  CB  . LEU A 197 ? 0.1551 0.1052 0.1395 -0.0141 -0.0054 0.0078  199 LEU A CB  
3071 C  CG  . LEU A 197 ? 0.1677 0.1235 0.1567 -0.0151 -0.0043 0.0077  199 LEU A CG  
3072 C  CD1 . LEU A 197 ? 0.1917 0.1498 0.1833 -0.0121 -0.0039 0.0068  199 LEU A CD1 
3073 C  CD2 . LEU A 197 ? 0.2166 0.1775 0.2083 -0.0178 -0.0027 0.0094  199 LEU A CD2 
3085 N  N   . SER A 198 ? 0.1554 0.0987 0.1307 -0.0185 -0.0060 0.0116  200 SER A N   
3086 C  CA  . SER A 198 ? 0.1672 0.1049 0.1368 -0.0182 -0.0073 0.0126  200 SER A CA  
3087 C  C   . SER A 198 ? 0.1657 0.1015 0.1355 -0.0127 -0.0084 0.0105  200 SER A C   
3088 O  O   . SER A 198 ? 0.1557 0.0960 0.1305 -0.0097 -0.0073 0.0089  200 SER A O   
3089 C  CB  . SER A 198 ? 0.1988 0.1401 0.1677 -0.0211 -0.0051 0.0150  200 SER A CB  
3090 O  OG  . SER A 198 ? 0.1739 0.1194 0.1467 -0.0179 -0.0033 0.0140  200 SER A OG  
3096 N  N   . ARG A 199 ? 0.1517 0.0806 0.1155 -0.0119 -0.0108 0.0108  201 ARG A N   
3097 C  CA  . ARG A 199 ? 0.1472 0.0745 0.1103 -0.0073 -0.0121 0.0092  201 ARG A CA  
3098 C  C   . ARG A 199 ? 0.1465 0.0800 0.1139 -0.0060 -0.0097 0.0093  201 ARG A C   
3099 O  O   . ARG A 199 ? 0.1591 0.0958 0.1303 -0.0024 -0.0097 0.0075  201 ARG A O   
3100 C  CB  . ARG A 199 ? 0.1826 0.1011 0.1375 -0.0074 -0.0155 0.0101  201 ARG A CB  
3101 C  CG  . ARG A 199 ? 0.2083 0.1255 0.1620 -0.0028 -0.0171 0.0087  201 ARG A CG  
3102 C  CD  . ARG A 199 ? 0.2029 0.1100 0.1477 -0.0026 -0.0213 0.0092  201 ARG A CD  
3109 N  N   . ASP A 200 ? 0.1552 0.0897 0.1211 -0.0089 -0.0080 0.0115  202 ASP A N   
3110 C  CA  . ASP A 200 ? 0.1583 0.0968 0.1267 -0.0074 -0.0064 0.0113  202 ASP A CA  
3111 C  C   . ASP A 200 ? 0.1437 0.0884 0.1193 -0.0059 -0.0051 0.0098  202 ASP A C   
3112 O  O   . ASP A 200 ? 0.1811 0.1279 0.1594 -0.0031 -0.0053 0.0086  202 ASP A O   
3113 C  CB  . ASP A 200 ? 0.1976 0.1360 0.1616 -0.0112 -0.0046 0.0140  202 ASP A CB  
3114 C  CG  . ASP A 200 ? 0.2467 0.1794 0.2025 -0.0126 -0.0059 0.0159  202 ASP A CG  
3115 O  OD1 . ASP A 200 ? 0.2532 0.1817 0.2072 -0.0093 -0.0085 0.0146  202 ASP A OD1 
3116 O  OD2 . ASP A 200 ? 0.2894 0.2232 0.2410 -0.0174 -0.0041 0.0187  202 ASP A OD2 
3121 N  N   . LEU A 201 ? 0.1262 0.0733 0.1046 -0.0079 -0.0041 0.0100  203 LEU A N   
3122 C  CA  . LEU A 201 ? 0.1262 0.0783 0.1105 -0.0071 -0.0031 0.0089  203 LEU A CA  
3123 C  C   . LEU A 201 ? 0.1314 0.0841 0.1179 -0.0048 -0.0041 0.0072  203 LEU A C   
3124 O  O   . LEU A 201 ? 0.1314 0.0878 0.1218 -0.0046 -0.0036 0.0068  203 LEU A O   
3125 C  CB  . LEU A 201 ? 0.1316 0.0859 0.1170 -0.0106 -0.0019 0.0100  203 LEU A CB  
3126 C  CG  . LEU A 201 ? 0.1640 0.1190 0.1469 -0.0137 -0.0004 0.0120  203 LEU A CG  
3127 C  CD1 . LEU A 201 ? 0.1756 0.1350 0.1600 -0.0182 0.0008  0.0132  203 LEU A CD1 
3128 C  CD2 . LEU A 201 ? 0.1883 0.1471 0.1740 -0.0102 0.0001  0.0105  203 LEU A CD2 
3140 N  N   . THR A 202 ? 0.1379 0.0866 0.1212 -0.0030 -0.0060 0.0063  204 THR A N   
3141 C  CA  . THR A 202 ? 0.1589 0.1069 0.1426 -0.0004 -0.0074 0.0044  204 THR A CA  
3142 C  C   . THR A 202 ? 0.1573 0.1037 0.1396 0.0034  -0.0094 0.0031  204 THR A C   
3143 O  O   . THR A 202 ? 0.2009 0.1459 0.1823 0.0066  -0.0114 0.0009  204 THR A O   
3144 C  CB  . THR A 202 ? 0.1521 0.0958 0.1326 -0.0008 -0.0088 0.0036  204 THR A CB  
3145 O  OG1 . THR A 202 ? 0.1683 0.1059 0.1433 -0.0010 -0.0106 0.0041  204 THR A OG1 
3146 C  CG2 . THR A 202 ? 0.1496 0.0955 0.1320 -0.0044 -0.0073 0.0046  204 THR A CG2 
3154 N  N   . THR A 203 ? 0.1566 0.1036 0.1387 0.0035  -0.0093 0.0038  205 THR A N   
3155 C  CA  . THR A 203 ? 0.1789 0.1246 0.1595 0.0071  -0.0116 0.0026  205 THR A CA  
3156 C  C   . THR A 203 ? 0.2180 0.1677 0.2023 0.0073  -0.0115 0.0028  205 THR A C   
3157 O  O   . THR A 203 ? 0.2412 0.1903 0.2244 0.0096  -0.0136 0.0021  205 THR A O   
3158 C  CB  . THR A 203 ? 0.2208 0.1609 0.1955 0.0071  -0.0131 0.0033  205 THR A CB  
3159 O  OG1 . THR A 203 ? 0.2050 0.1450 0.1786 0.0037  -0.0111 0.0055  205 THR A OG1 
3160 C  CG2 . THR A 203 ? 0.2710 0.2051 0.2409 0.0078  -0.0152 0.0026  205 THR A CG2 
3168 N  N   . LYS A 204 ? 0.1707 0.1241 0.1590 0.0049  -0.0100 0.0036  206 LYS A N   
3169 C  CA  . LYS A 204 ? 0.1673 0.1230 0.1583 0.0043  -0.0109 0.0040  206 LYS A CA  
3170 C  C   . LYS A 204 ? 0.1638 0.1264 0.1600 0.0036  -0.0117 0.0036  206 LYS A C   
3171 O  O   . LYS A 204 ? 0.1845 0.1508 0.1834 0.0024  -0.0130 0.0039  206 LYS A O   
3172 C  CB  . LYS A 204 ? 0.1972 0.1544 0.1891 0.0019  -0.0087 0.0049  206 LYS A CB  
3173 C  CG  . LYS A 204 ? 0.2339 0.1889 0.2223 0.0018  -0.0074 0.0053  206 LYS A CG  
3174 C  CD  . LYS A 204 ? 0.3409 0.2926 0.3253 0.0035  -0.0089 0.0050  206 LYS A CD  
3175 C  CE  . LYS A 204 ? 0.3740 0.3219 0.3530 0.0027  -0.0080 0.0062  206 LYS A CE  
3176 N  NZ  . LYS A 204 ? 0.3822 0.3304 0.3613 0.0023  -0.0071 0.0062  206 LYS A NZ  
3190 N  N   . ALA A 205 ? 0.1404 0.1069 0.1381 0.0036  -0.0107 0.0030  207 ALA A N   
3191 C  CA  . ALA A 205 ? 0.1482 0.1246 0.1506 0.0016  -0.0103 0.0032  207 ALA A CA  
3192 C  C   . ALA A 205 ? 0.1490 0.1339 0.1539 0.0041  -0.0115 0.0013  207 ALA A C   
3193 O  O   . ALA A 205 ? 0.1675 0.1493 0.1700 0.0086  -0.0129 -0.0008 207 ALA A O   
3194 C  CB  . ALA A 205 ? 0.1408 0.1192 0.1431 0.0008  -0.0086 0.0031  207 ALA A CB  
3200 N  N   . THR A 206 ? 0.1178 0.1139 0.1273 0.0011  -0.0112 0.0019  208 THR A N   
3201 C  CA  . THR A 206 ? 0.1477 0.1565 0.1610 0.0030  -0.0120 -0.0001 208 THR A CA  
3202 C  C   . THR A 206 ? 0.1509 0.1635 0.1631 0.0092  -0.0115 -0.0040 208 THR A C   
3203 O  O   . THR A 206 ? 0.1966 0.2136 0.2096 0.0147  -0.0133 -0.0071 208 THR A O   
3204 C  CB  . THR A 206 ? 0.1312 0.1531 0.1494 -0.0033 -0.0114 0.0023  208 THR A CB  
3205 O  OG1 . THR A 206 ? 0.1291 0.1439 0.1466 -0.0090 -0.0128 0.0058  208 THR A OG1 
3206 C  CG2 . THR A 206 ? 0.1917 0.2300 0.2151 -0.0023 -0.0123 0.0003  208 THR A CG2 
3214 N  N   . LEU A 207 ? 0.1492 0.1597 0.1594 0.0090  -0.0098 -0.0041 209 LEU A N   
3215 C  CA  . LEU A 207 ? 0.1680 0.1804 0.1759 0.0148  -0.0098 -0.0081 209 LEU A CA  
3216 C  C   . LEU A 207 ? 0.1569 0.1570 0.1598 0.0137  -0.0091 -0.0072 209 LEU A C   
3217 O  O   . LEU A 207 ? 0.1412 0.1404 0.1448 0.0083  -0.0074 -0.0041 209 LEU A O   
3218 C  CB  . LEU A 207 ? 0.1848 0.2158 0.1968 0.0147  -0.0079 -0.0098 209 LEU A CB  
3219 C  CG  . LEU A 207 ? 0.2131 0.2479 0.2226 0.0211  -0.0079 -0.0146 209 LEU A CG  
3220 C  CD1 . LEU A 207 ? 0.2819 0.3140 0.2893 0.0301  -0.0111 -0.0196 209 LEU A CD1 
3221 C  CD2 . LEU A 207 ? 0.2134 0.2694 0.2272 0.0193  -0.0052 -0.0154 209 LEU A CD2 
3233 N  N   . VAL A 208 ? 0.1547 0.1452 0.1523 0.0187  -0.0110 -0.0100 210 VAL A N   
3234 C  CA  . VAL A 208 ? 0.1585 0.1374 0.1512 0.0170  -0.0109 -0.0092 210 VAL A CA  
3235 C  C   . VAL A 208 ? 0.1887 0.1682 0.1780 0.0222  -0.0122 -0.0137 210 VAL A C   
3236 O  O   . VAL A 208 ? 0.2357 0.2149 0.2228 0.0291  -0.0149 -0.0178 210 VAL A O   
3237 C  CB  . VAL A 208 ? 0.1610 0.1244 0.1487 0.0162  -0.0127 -0.0073 210 VAL A CB  
3238 C  CG1 . VAL A 208 ? 0.1901 0.1443 0.1738 0.0130  -0.0125 -0.0061 210 VAL A CG1 
3239 C  CG2 . VAL A 208 ? 0.2138 0.1774 0.2043 0.0124  -0.0116 -0.0038 210 VAL A CG2 
3249 N  N   . LEU A 209 ? 0.1709 0.1527 0.1599 0.0196  -0.0106 -0.0134 211 LEU A N   
3250 C  CA  . LEU A 209 ? 0.2166 0.2005 0.2021 0.0243  -0.0116 -0.0181 211 LEU A CA  
3251 C  C   . LEU A 209 ? 0.2158 0.1870 0.1959 0.0220  -0.0128 -0.0175 211 LEU A C   
3252 O  O   . LEU A 209 ? 0.1983 0.1655 0.1796 0.0157  -0.0114 -0.0133 211 LEU A O   
3253 C  CB  . LEU A 209 ? 0.1991 0.2016 0.1891 0.0232  -0.0084 -0.0186 211 LEU A CB  
3254 C  CG  . LEU A 209 ? 0.2411 0.2601 0.2375 0.0232  -0.0067 -0.0183 211 LEU A CG  
3255 C  CD1 . LEU A 209 ? 0.1728 0.2088 0.1724 0.0196  -0.0036 -0.0173 211 LEU A CD1 
3256 C  CD2 . LEU A 209 ? 0.2401 0.2632 0.2359 0.0322  -0.0091 -0.0240 211 LEU A CD2 
3268 N  N   . ASN A 210 ? 0.2306 0.1961 0.2047 0.0273  -0.0158 -0.0223 212 ASN A N   
3269 C  CA  . ASN A 210 ? 0.2600 0.2140 0.2286 0.0247  -0.0175 -0.0222 212 ASN A CA  
3270 C  C   . ASN A 210 ? 0.2216 0.1858 0.1922 0.0218  -0.0148 -0.0220 212 ASN A C   
3271 O  O   . ASN A 210 ? 0.2305 0.1882 0.1993 0.0172  -0.0152 -0.0201 212 ASN A O   
3272 C  CB  . ASN A 210 ? 0.3120 0.2538 0.2722 0.0317  -0.0229 -0.0277 212 ASN A CB  
3273 C  CG  . ASN A 210 ? 0.3485 0.2816 0.3069 0.0315  -0.0257 -0.0249 212 ASN A CG  
3274 O  OD1 . ASN A 210 ? 0.3653 0.2935 0.3249 0.0254  -0.0246 -0.0198 212 ASN A OD1 
3275 N  ND2 . ASN A 210 ? 0.3976 0.3303 0.3528 0.0382  -0.0293 -0.0284 212 ASN A ND2 
3282 N  N   . SER A 211 ? 0.2199 0.2012 0.1945 0.0239  -0.0120 -0.0235 213 SER A N   
3283 C  CA  . SER A 211 ? 0.2034 0.1948 0.1786 0.0211  -0.0096 -0.0231 213 SER A CA  
3284 C  C   . SER A 211 ? 0.1730 0.1836 0.1541 0.0198  -0.0058 -0.0217 213 SER A C   
3285 O  O   . SER A 211 ? 0.1851 0.2037 0.1689 0.0239  -0.0056 -0.0238 213 SER A O   
3286 C  CB  . SER A 211 ? 0.2321 0.2224 0.2006 0.0273  -0.0119 -0.0295 213 SER A CB  
3287 O  OG  . SER A 211 ? 0.2476 0.2504 0.2163 0.0255  -0.0093 -0.0296 213 SER A OG  
3293 N  N   . LEU A 212 ? 0.1816 0.2000 0.1642 0.0140  -0.0033 -0.0181 214 LEU A N   
3294 C  CA  . LEU A 212 ? 0.1916 0.2289 0.1782 0.0115  -0.0001 -0.0164 214 LEU A CA  
3295 C  C   . LEU A 212 ? 0.2402 0.2925 0.2253 0.0183  0.0007  -0.0226 214 LEU A C   
3296 O  O   . LEU A 212 ? 0.2137 0.2835 0.2032 0.0176  0.0031  -0.0222 214 LEU A O   
3297 C  CB  . LEU A 212 ? 0.1960 0.2373 0.1823 0.0040  0.0015  -0.0113 214 LEU A CB  
3298 C  CG  . LEU A 212 ? 0.1477 0.1793 0.1367 -0.0025 0.0009  -0.0051 214 LEU A CG  
3299 C  CD1 . LEU A 212 ? 0.2050 0.2368 0.1916 -0.0081 0.0010  -0.0013 214 LEU A CD1 
3300 C  CD2 . LEU A 212 ? 0.1760 0.2128 0.1701 -0.0054 0.0016  -0.0020 214 LEU A CD2 
3312 N  N   . GLN A 213 ? 0.2121 0.2583 0.1912 0.0248  -0.0015 -0.0284 215 GLN A N   
3313 C  CA  . GLN A 213 ? 0.2611 0.3204 0.2379 0.0334  -0.0014 -0.0358 215 GLN A CA  
3314 C  C   . GLN A 213 ? 0.2827 0.3489 0.2634 0.0400  -0.0022 -0.0394 215 GLN A C   
3315 O  O   . GLN A 213 ? 0.3413 0.4255 0.3229 0.0463  -0.0011 -0.0447 215 GLN A O   
3316 C  CB  . GLN A 213 ? 0.2753 0.3203 0.2436 0.0397  -0.0054 -0.0416 215 GLN A CB  
3317 C  CG  . GLN A 213 ? 0.2992 0.3431 0.2634 0.0349  -0.0046 -0.0399 215 GLN A CG  
3318 C  CD  . GLN A 213 ? 0.3952 0.4218 0.3508 0.0394  -0.0094 -0.0449 215 GLN A CD  
3319 O  OE1 . GLN A 213 ? 0.5192 0.5267 0.4722 0.0411  -0.0137 -0.0457 215 GLN A OE1 
3320 N  NE2 . GLN A 213 ? 0.4145 0.4472 0.3649 0.0403  -0.0090 -0.0477 215 GLN A NE2 
3329 N  N   . ASP A 214 ? 0.2517 0.3042 0.2344 0.0391  -0.0043 -0.0369 216 ASP A N   
3330 C  CA  . ASP A 214 ? 0.3265 0.3823 0.3120 0.0455  -0.0060 -0.0401 216 ASP A CA  
3331 C  C   . ASP A 214 ? 0.2652 0.3370 0.2595 0.0399  -0.0029 -0.0355 216 ASP A C   
3332 O  O   . ASP A 214 ? 0.2987 0.3756 0.2964 0.0445  -0.0042 -0.0377 216 ASP A O   
3333 C  CB  . ASP A 214 ? 0.3043 0.3358 0.2860 0.0473  -0.0106 -0.0396 216 ASP A CB  
3334 C  CG  . ASP A 214 ? 0.3620 0.3751 0.3344 0.0516  -0.0149 -0.0435 216 ASP A CG  
3335 O  OD1 . ASP A 214 ? 0.4113 0.4307 0.3805 0.0564  -0.0155 -0.0482 216 ASP A OD1 
3336 O  OD2 . ASP A 214 ? 0.3967 0.3894 0.3653 0.0488  -0.0179 -0.0407 216 ASP A OD2 
3341 N  N   . PHE A 215 ? 0.2094 0.2876 0.2066 0.0299  0.0005  -0.0290 217 PHE A N   
3342 C  CA  . PHE A 215 ? 0.2029 0.2940 0.2072 0.0234  0.0027  -0.0243 217 PHE A CA  
3343 C  C   . PHE A 215 ? 0.2229 0.3413 0.2313 0.0262  0.0051  -0.0279 217 PHE A C   
3344 O  O   . PHE A 215 ? 0.2125 0.3434 0.2185 0.0274  0.0072  -0.0303 217 PHE A O   
3345 C  CB  . PHE A 215 ? 0.1848 0.2732 0.1894 0.0123  0.0045  -0.0166 217 PHE A CB  
3346 C  CG  . PHE A 215 ? 0.1636 0.2631 0.1741 0.0044  0.0057  -0.0113 217 PHE A CG  
3347 C  CD1 . PHE A 215 ? 0.1652 0.2582 0.1794 0.0040  0.0038  -0.0099 217 PHE A CD1 
3348 C  CD2 . PHE A 215 ? 0.2143 0.3304 0.2258 -0.0030 0.0084  -0.0076 217 PHE A CD2 
3349 C  CE1 . PHE A 215 ? 0.1722 0.2737 0.1909 -0.0034 0.0041  -0.0052 217 PHE A CE1 
3350 C  CE2 . PHE A 215 ? 0.1723 0.2968 0.1881 -0.0112 0.0086  -0.0024 217 PHE A CE2 
3351 C  CZ  . PHE A 215 ? 0.1844 0.3015 0.2041 -0.0113 0.0063  -0.0014 217 PHE A CZ  
3361 N  N   . GLN A 216 ? 0.2118 0.3402 0.2263 0.0274  0.0046  -0.0283 218 GLN A N   
3362 C  CA  . GLN A 216 ? 0.2352 0.3905 0.2545 0.0292  0.0064  -0.0313 218 GLN A CA  
3363 C  C   . GLN A 216 ? 0.1876 0.3534 0.2122 0.0171  0.0083  -0.0238 218 GLN A C   
3364 O  O   . GLN A 216 ? 0.1929 0.3555 0.2222 0.0151  0.0067  -0.0216 218 GLN A O   
3365 C  CB  . GLN A 216 ? 0.2533 0.4065 0.2730 0.0392  0.0024  -0.0372 218 GLN A CB  
3366 C  CG  . GLN A 216 ? 0.2841 0.4198 0.2965 0.0500  -0.0015 -0.0435 218 GLN A CG  
3367 C  CD  . GLN A 216 ? 0.3450 0.4762 0.3564 0.0586  -0.0064 -0.0481 218 GLN A CD  
3368 O  OE1 . GLN A 216 ? 0.3571 0.4764 0.3696 0.0591  -0.0086 -0.0467 218 GLN A OE1 
3369 N  NE2 . GLN A 216 ? 0.4022 0.5436 0.4112 0.0652  -0.0085 -0.0536 218 GLN A NE2 
3378 N  N   . PRO A 217 ? 0.2021 0.3770 0.2249 0.0082  0.0107  -0.0191 219 PRO A N   
3379 C  CA  . PRO A 217 ? 0.1983 0.3760 0.2232 -0.0043 0.0110  -0.0110 219 PRO A CA  
3380 C  C   . PRO A 217 ? 0.2034 0.3917 0.2328 -0.0053 0.0099  -0.0112 219 PRO A C   
3381 O  O   . PRO A 217 ? 0.1936 0.3769 0.2249 -0.0135 0.0088  -0.0055 219 PRO A O   
3382 C  CB  . PRO A 217 ? 0.2360 0.4229 0.2563 -0.0106 0.0127  -0.0081 219 PRO A CB  
3383 C  CG  . PRO A 217 ? 0.2514 0.4330 0.2674 -0.0039 0.0137  -0.0123 219 PRO A CG  
3384 C  CD  . PRO A 217 ? 0.1773 0.3570 0.1946 0.0093  0.0122  -0.0208 219 PRO A CD  
3392 N  N   . GLU A 218 ? 0.2012 0.4028 0.2315 0.0031  0.0097  -0.0178 220 GLU A N   
3393 C  CA  . GLU A 218 ? 0.2510 0.4653 0.2852 0.0027  0.0089  -0.0186 220 GLU A CA  
3394 C  C   . GLU A 218 ? 0.2360 0.4382 0.2744 0.0047  0.0064  -0.0184 220 GLU A C   
3395 O  O   . GLU A 218 ? 0.2111 0.4197 0.2532 0.0006  0.0056  -0.0164 220 GLU A O   
3396 C  CB  . GLU A 218 ? 0.2578 0.4888 0.2914 0.0126  0.0086  -0.0265 220 GLU A CB  
3397 C  CG  . GLU A 218 ? 0.3017 0.5222 0.3333 0.0267  0.0059  -0.0346 220 GLU A CG  
3398 C  CD  . GLU A 218 ? 0.2948 0.5090 0.3209 0.0315  0.0061  -0.0376 220 GLU A CD  
3399 O  OE1 . GLU A 218 ? 0.2579 0.4715 0.2822 0.0238  0.0086  -0.0328 220 GLU A OE1 
3400 O  OE2 . GLU A 218 ? 0.3350 0.5435 0.3576 0.0430  0.0031  -0.0446 220 GLU A OE2 
3407 N  N   . LEU A 219 ? 0.2147 0.3996 0.2526 0.0106  0.0048  -0.0203 221 LEU A N   
3408 C  CA  . LEU A 219 ? 0.1922 0.3653 0.2336 0.0124  0.0017  -0.0199 221 LEU A CA  
3409 C  C   . LEU A 219 ? 0.2141 0.3830 0.2580 0.0002  0.0013  -0.0121 221 LEU A C   
3410 O  O   . LEU A 219 ? 0.2479 0.4129 0.2951 -0.0006 -0.0013 -0.0112 221 LEU A O   
3411 C  CB  . LEU A 219 ? 0.2508 0.4050 0.2897 0.0200  -0.0003 -0.0225 221 LEU A CB  
3412 C  CG  . LEU A 219 ? 0.3183 0.4569 0.3572 0.0250  -0.0045 -0.0237 221 LEU A CG  
3413 C  CD1 . LEU A 219 ? 0.3292 0.4780 0.3700 0.0321  -0.0064 -0.0287 221 LEU A CD1 
3414 C  CD2 . LEU A 219 ? 0.3277 0.4405 0.3579 0.0311  -0.0063 -0.0256 221 LEU A CD2 
3426 N  N   . PHE A 220 ? 0.2148 0.3823 0.2558 -0.0092 0.0032  -0.0065 222 PHE A N   
3427 C  CA  . PHE A 220 ? 0.1854 0.3447 0.2259 -0.0207 0.0018  0.0010  222 PHE A CA  
3428 C  C   . PHE A 220 ? 0.2282 0.4004 0.2669 -0.0291 0.0029  0.0048  222 PHE A C   
3429 O  O   . PHE A 220 ? 0.2339 0.3978 0.2691 -0.0389 0.0016  0.0114  222 PHE A O   
3430 C  CB  . PHE A 220 ? 0.1821 0.3240 0.2188 -0.0249 0.0014  0.0051  222 PHE A CB  
3431 C  CG  . PHE A 220 ? 0.1954 0.3182 0.2312 -0.0182 -0.0007 0.0027  222 PHE A CG  
3432 C  CD1 . PHE A 220 ? 0.1970 0.3128 0.2292 -0.0088 0.0002  -0.0023 222 PHE A CD1 
3433 C  CD2 . PHE A 220 ? 0.1731 0.2808 0.2086 -0.0207 -0.0039 0.0052  222 PHE A CD2 
3434 C  CE1 . PHE A 220 ? 0.1762 0.2701 0.2046 -0.0034 -0.0019 -0.0038 222 PHE A CE1 
3435 C  CE2 . PHE A 220 ? 0.1735 0.2605 0.2053 -0.0143 -0.0056 0.0032  222 PHE A CE2 
3436 C  CZ  . PHE A 220 ? 0.1685 0.2495 0.1969 -0.0061 -0.0045 -0.0010 222 PHE A CZ  
3446 N  N   . GLY A 221 ? 0.2200 0.4118 0.2604 -0.0250 0.0046  0.0006  223 GLY A N   
3447 C  CA  . GLY A 221 ? 0.2555 0.4626 0.2948 -0.0327 0.0053  0.0038  223 GLY A CA  
3448 C  C   . GLY A 221 ? 0.2726 0.4832 0.3059 -0.0386 0.0069  0.0073  223 GLY A C   
3449 O  O   . GLY A 221 ? 0.2855 0.5036 0.3163 -0.0477 0.0065  0.0121  223 GLY A O   
3453 N  N   . LEU A 222 ? 0.2230 0.4279 0.2535 -0.0338 0.0083  0.0050  224 LEU A N   
3454 C  CA  . LEU A 222 ? 0.2762 0.4846 0.3010 -0.0384 0.0095  0.0077  224 LEU A CA  
3455 C  C   . LEU A 222 ? 0.2659 0.4951 0.2907 -0.0315 0.0118  0.0014  224 LEU A C   
3456 O  O   . LEU A 222 ? 0.2425 0.4781 0.2706 -0.0212 0.0121  -0.0057 224 LEU A O   
3457 C  CB  . LEU A 222 ? 0.2637 0.4528 0.2851 -0.0379 0.0092  0.0093  224 LEU A CB  
3458 C  CG  . LEU A 222 ? 0.1938 0.3604 0.2148 -0.0426 0.0064  0.0143  224 LEU A CG  
3459 C  CD1 . LEU A 222 ? 0.2337 0.3842 0.2527 -0.0394 0.0066  0.0138  224 LEU A CD1 
3460 C  CD2 . LEU A 222 ? 0.2704 0.4310 0.2869 -0.0535 0.0038  0.0216  224 LEU A CD2 
3472 N  N   . PRO A 223 ? 0.2707 0.5101 0.2913 -0.0367 0.0127  0.0037  225 PRO A N   
3473 C  CA  . PRO A 223 ? 0.2870 0.5462 0.3071 -0.0301 0.0145  -0.0024 225 PRO A CA  
3474 C  C   . PRO A 223 ? 0.3054 0.5578 0.3255 -0.0176 0.0149  -0.0098 225 PRO A C   
3475 O  O   . PRO A 223 ? 0.2829 0.5171 0.3008 -0.0174 0.0148  -0.0082 225 PRO A O   
3476 C  CB  . PRO A 223 ? 0.3246 0.5877 0.3394 -0.0388 0.0149  0.0028  225 PRO A CB  
3477 C  CG  . PRO A 223 ? 0.3146 0.5677 0.3275 -0.0509 0.0128  0.0115  225 PRO A CG  
3478 C  CD  . PRO A 223 ? 0.3126 0.5446 0.3279 -0.0486 0.0114  0.0120  225 PRO A CD  
3486 N  N   . SER A 224 ? 0.2729 0.5387 0.2949 -0.0071 0.0149  -0.0178 226 SER A N   
3487 C  CA  . SER A 224 ? 0.2867 0.5454 0.3070 0.0053  0.0142  -0.0253 226 SER A CA  
3488 C  C   . SER A 224 ? 0.2912 0.5519 0.3069 0.0044  0.0154  -0.0251 226 SER A C   
3489 O  O   . SER A 224 ? 0.3015 0.5746 0.3157 -0.0042 0.0167  -0.0207 226 SER A O   
3490 C  CB  . SER A 224 ? 0.3289 0.6010 0.3509 0.0171  0.0126  -0.0341 226 SER A CB  
3491 O  OG  . SER A 224 ? 0.4238 0.6929 0.4498 0.0198  0.0110  -0.0354 226 SER A OG  
3497 N  N   . TYR A 225 ? 0.3361 0.5841 0.3491 0.0135  0.0145  -0.0302 227 TYR A N   
3498 C  CA  . TYR A 225 ? 0.3346 0.5834 0.3430 0.0150  0.0153  -0.0317 227 TYR A CA  
3499 C  C   . TYR A 225 ? 0.4137 0.6856 0.4224 0.0206  0.0152  -0.0373 227 TYR A C   
3500 O  O   . TYR A 225 ? 0.4678 0.7464 0.4784 0.0299  0.0131  -0.0439 227 TYR A O   
3501 C  CB  . TYR A 225 ? 0.3947 0.6229 0.3995 0.0241  0.0137  -0.0364 227 TYR A CB  
3502 C  CG  . TYR A 225 ? 0.3442 0.5511 0.3472 0.0184  0.0144  -0.0310 227 TYR A CG  
3503 C  CD1 . TYR A 225 ? 0.3244 0.5290 0.3248 0.0078  0.0163  -0.0239 227 TYR A CD1 
3504 C  CD2 . TYR A 225 ? 0.3415 0.5304 0.3447 0.0239  0.0126  -0.0333 227 TYR A CD2 
3505 C  CE1 . TYR A 225 ? 0.3305 0.5163 0.3286 0.0031  0.0164  -0.0193 227 TYR A CE1 
3506 C  CE2 . TYR A 225 ? 0.3047 0.4761 0.3059 0.0189  0.0133  -0.0288 227 TYR A CE2 
3507 C  CZ  . TYR A 225 ? 0.3315 0.5019 0.3303 0.0086  0.0153  -0.0219 227 TYR A CZ  
3508 O  OH  . TYR A 225 ? 0.2797 0.4329 0.2759 0.0037  0.0155  -0.0173 227 TYR A OH  
3518 N  N   . GLU A 226 ? 0.5029 0.7868 0.5092 0.0151  0.0171  -0.0349 228 GLU A N   
3519 C  CA  . GLU A 226 ? 0.5932 0.9012 0.5995 0.0198  0.0173  -0.0400 228 GLU A CA  
3520 C  C   . GLU A 226 ? 0.6716 0.9741 0.6743 0.0325  0.0156  -0.0482 228 GLU A C   
3521 O  O   . GLU A 226 ? 0.7116 0.9943 0.7103 0.0334  0.0155  -0.0476 228 GLU A O   
3522 C  CB  . GLU A 226 ? 0.6134 0.9366 0.6182 0.0081  0.0198  -0.0337 228 GLU A CB  
3525 MG MG  . MG  B .   ? 0.1055 0.0807 0.1074 -0.0152 -0.0098 0.0129  301 MG  A MG  
3526 O  O01 . FJF C .   ? 0.2296 0.2396 0.2512 -0.0218 -0.0087 0.0078  302 FJF A O01 
3527 C  C02 . FJF C .   ? 0.2480 0.2570 0.2703 -0.0168 -0.0099 0.0073  302 FJF A C02 
3528 N  N03 . FJF C .   ? 0.2349 0.2340 0.2530 -0.0151 -0.0108 0.0080  302 FJF A N03 
3529 C  C04 . FJF C .   ? 0.2513 0.2474 0.2690 -0.0109 -0.0128 0.0081  302 FJF A C04 
3530 C  C05 . FJF C .   ? 0.2798 0.2811 0.3010 -0.0063 -0.0147 0.0066  302 FJF A C05 
3531 C  C06 . FJF C .   ? 0.2634 0.2766 0.2896 -0.0063 -0.0135 0.0049  302 FJF A C06 
3532 O  O07 . FJF C .   ? 0.3374 0.3573 0.3670 -0.0015 -0.0152 0.0028  302 FJF A O07 
3533 N  N08 . FJF C .   ? 0.2817 0.2995 0.3088 -0.0122 -0.0109 0.0056  302 FJF A N08 
3534 C  C09 . FJF C .   ? 0.2836 0.2789 0.3030 -0.0017 -0.0181 0.0065  302 FJF A C09 
3535 O  O10 . FJF C .   ? 0.3272 0.3130 0.3421 -0.0031 -0.0180 0.0083  302 FJF A O10 
3536 C  C11 . FJF C .   ? 0.3056 0.2853 0.3169 -0.0043 -0.0212 0.0106  302 FJF A C11 
3537 C  C12 . FJF C .   ? 0.2919 0.2699 0.3005 -0.0090 -0.0185 0.0123  302 FJF A C12 
3538 O  O13 . FJF C .   ? 0.2395 0.2193 0.2492 -0.0100 -0.0145 0.0112  302 FJF A O13 
3539 C  C14 . FJF C .   ? 0.3257 0.3101 0.3390 -0.0027 -0.0242 0.0100  302 FJF A C14 
3540 O  O15 . FJF C .   ? 0.3866 0.3643 0.3965 -0.0005 -0.0296 0.0114  302 FJF A O15 
3541 C  C16 . FJF C .   ? 0.3014 0.2955 0.3205 0.0007  -0.0230 0.0068  302 FJF A C16 
3542 O  O17 . FJF C .   ? 0.3410 0.3330 0.3601 0.0069  -0.0266 0.0050  302 FJF A O17 
3543 O  O   . HOH D .   ? 0.3440 0.5594 0.3937 0.0068  0.0226  -0.0202 401 HOH A O   
3544 O  O   . HOH D .   ? 0.5611 0.5498 0.5656 0.0180  -0.0256 -0.0051 402 HOH A O   
3545 O  O   . HOH D .   ? 0.3463 0.2438 0.3097 0.0083  -0.0648 -0.0023 403 HOH A O   
3546 O  O   . HOH D .   ? 0.4830 0.4226 0.4253 -0.0410 -0.0559 0.0454  404 HOH A O   
3547 O  O   . HOH D .   ? 0.4843 0.3730 0.4437 0.0079  -0.0721 0.0004  405 HOH A O   
3548 O  O   . HOH D .   ? 0.6160 0.6309 0.6351 -0.0512 -0.0386 0.0218  406 HOH A O   
3549 O  O   . HOH D .   ? 0.4350 0.5270 0.3981 -0.0862 -0.0127 0.0506  407 HOH A O   
3550 O  O   . HOH D .   ? 0.4891 0.7441 0.5016 0.0430  0.0082  -0.0502 408 HOH A O   
3551 O  O   . HOH D .   ? 0.6593 0.5211 0.6201 0.0000  0.0000  -0.0257 409 HOH A O   
3552 O  O   . HOH D .   ? 0.4813 0.5593 0.5165 -0.0545 -0.0247 0.0219  410 HOH A O   
3553 O  O   . HOH D .   ? 0.4828 0.5165 0.4387 -0.1140 -0.0468 0.0693  411 HOH A O   
3554 O  O   . HOH D .   ? 0.4402 0.6295 0.5358 0.0195  -0.0260 -0.0225 412 HOH A O   
3555 O  O   . HOH D .   ? 0.4205 0.5262 0.4588 -0.0554 -0.0180 0.0219  413 HOH A O   
3556 O  O   . HOH D .   ? 0.4216 0.3839 0.3662 -0.0471 -0.0439 0.0456  414 HOH A O   
3557 O  O   . HOH D .   ? 0.4302 0.5806 0.5143 -0.0385 -0.0334 -0.0039 415 HOH A O   
3558 O  O   . HOH D .   ? 0.5491 0.5067 0.5441 0.0480  -0.0460 -0.0207 416 HOH A O   
3559 O  O   . HOH D .   ? 0.3152 0.2684 0.3048 0.0032  -0.0142 0.0025  417 HOH A O   
3560 O  O   . HOH D .   ? 0.5296 0.7678 0.5275 -0.0902 0.0037  0.0374  418 HOH A O   
3561 O  O   . HOH D .   ? 0.5318 0.5311 0.4789 -0.0746 -0.0345 0.0541  419 HOH A O   
3562 O  O   . HOH D .   ? 0.2470 0.2865 0.2677 -0.0461 -0.0193 0.0237  420 HOH A O   
3563 O  O   . HOH D .   ? 0.5354 0.5555 0.4816 -0.0008 -0.0089 -0.0190 421 HOH A O   
3564 O  O   . HOH D .   ? 0.4577 0.5824 0.5232 -0.0709 -0.0297 0.0049  422 HOH A O   
3565 O  O   . HOH D .   ? 0.4896 0.4797 0.4379 -0.0223 -0.0288 -0.0057 423 HOH A O   
3566 O  O   . HOH D .   ? 0.4845 0.4623 0.4474 -0.0221 -0.0255 -0.0062 424 HOH A O   
3567 O  O   . HOH D .   ? 0.5417 0.6084 0.5693 -0.0661 -0.0297 0.0287  425 HOH A O   
3568 O  O   . HOH D .   ? 0.1318 0.1046 0.1352 -0.0124 -0.0100 0.0125  426 HOH A O   
3569 O  O   . HOH D .   ? 0.4862 0.5696 0.5168 0.0792  -0.0293 -0.0469 427 HOH A O   
3570 O  O   . HOH D .   ? 0.5039 0.7686 0.5849 -0.0772 0.0072  0.0078  428 HOH A O   
3571 O  O   . HOH D .   ? 0.1184 0.0943 0.1227 -0.0145 -0.0086 0.0107  429 HOH A O   
3572 O  O   . HOH D .   ? 0.2387 0.5053 0.3454 -0.0029 -0.0066 -0.0226 430 HOH A O   
3573 O  O   . HOH D .   ? 0.5323 0.6422 0.5959 -0.0554 -0.0395 -0.0007 431 HOH A O   
3574 O  O   . HOH D .   ? 0.5597 0.4480 0.4995 -0.0512 -0.0834 0.0388  432 HOH A O   
3575 O  O   . HOH D .   ? 0.5276 0.5438 0.5434 0.0851  -0.0622 -0.0415 433 HOH A O   
3576 O  O   . HOH D .   ? 0.5262 0.5350 0.5420 0.0058  -0.0553 0.0092  434 HOH A O   
3577 O  O   . HOH D .   ? 0.5157 0.6396 0.4997 0.0413  0.0054  -0.0438 435 HOH A O   
3578 O  O   . HOH D .   ? 0.4747 0.4093 0.4564 0.0299  -0.0414 -0.0139 436 HOH A O   
3579 O  O   . HOH D .   ? 0.4550 0.5392 0.4641 0.0394  -0.0044 -0.0320 437 HOH A O   
3580 O  O   . HOH D .   ? 0.5988 0.5084 0.5684 0.0458  -0.0713 -0.0205 438 HOH A O   
3581 O  O   . HOH D .   ? 0.4322 0.3717 0.3985 -0.0380 -0.0108 0.0170  439 HOH A O   
3582 O  O   . HOH D .   ? 0.4267 0.6270 0.4793 0.0477  0.0069  -0.0403 440 HOH A O   
3583 O  O   . HOH D .   ? 0.4700 0.4531 0.4429 -0.0272 -0.0289 -0.0009 441 HOH A O   
3584 O  O   . HOH D .   ? 0.3878 0.4946 0.4072 0.0238  0.0002  -0.0228 442 HOH A O   
3585 O  O   . HOH D .   ? 0.3470 0.3347 0.3505 0.0021  -0.0009 0.0023  443 HOH A O   
3586 O  O   . HOH D .   ? 0.4161 0.5345 0.4504 0.0644  -0.0078 -0.0421 444 HOH A O   
3587 O  O   . HOH D .   ? 0.3728 0.4893 0.3679 0.0179  0.0089  -0.0248 445 HOH A O   
3588 O  O   . HOH D .   ? 0.3541 0.3366 0.3652 -0.0238 -0.0261 0.0135  446 HOH A O   
3589 O  O   . HOH D .   ? 0.4894 0.4812 0.4705 -0.0120 -0.0615 0.0197  447 HOH A O   
3590 O  O   . HOH D .   ? 0.3149 0.3148 0.2733 -0.0290 -0.0525 0.0070  448 HOH A O   
3591 O  O   . HOH D .   ? 0.4765 0.3811 0.4437 0.0192  -0.0608 -0.0082 449 HOH A O   
3592 O  O   . HOH D .   ? 0.3828 0.3423 0.3850 -0.0176 -0.0308 0.0104  450 HOH A O   
3593 O  O   . HOH D .   ? 0.2580 0.2171 0.2617 0.0154  -0.0459 0.0079  451 HOH A O   
3594 O  O   . HOH D .   ? 0.4654 0.4462 0.4706 -0.0442 -0.0393 0.0228  452 HOH A O   
3595 O  O   . HOH D .   ? 0.3873 0.4336 0.4108 0.0178  -0.0157 -0.0108 453 HOH A O   
3596 O  O   . HOH D .   ? 0.1780 0.1389 0.1729 -0.0028 -0.0041 0.0064  454 HOH A O   
3597 O  O   . HOH D .   ? 0.3381 0.2440 0.2935 -0.0284 -0.0663 0.0308  455 HOH A O   
3598 O  O   . HOH D .   ? 0.4828 0.6945 0.5520 0.0511  -0.0029 -0.0426 456 HOH A O   
3599 O  O   . HOH D .   ? 0.2402 0.3794 0.2947 0.0705  -0.0218 -0.0451 457 HOH A O   
3600 O  O   . HOH D .   ? 0.3911 0.4629 0.3827 -0.0989 -0.0313 0.0543  458 HOH A O   
3601 O  O   . HOH D .   ? 0.2652 0.2083 0.2357 0.0038  -0.0150 -0.0110 459 HOH A O   
3602 O  O   . HOH D .   ? 0.2453 0.2166 0.2342 -0.0201 -0.0127 0.0031  460 HOH A O   
3603 O  O   . HOH D .   ? 0.1886 0.1907 0.1657 0.0058  -0.0051 -0.0140 461 HOH A O   
3604 O  O   . HOH D .   ? 0.4045 0.3154 0.3759 0.0075  -0.0543 -0.0018 462 HOH A O   
3605 O  O   . HOH D .   ? 0.5338 0.4033 0.4664 -0.0364 -0.0897 0.0345  463 HOH A O   
3606 O  O   . HOH D .   ? 0.5244 0.5758 0.4561 -0.0379 -0.0078 0.0200  464 HOH A O   
3607 O  O   . HOH D .   ? 0.5051 0.4218 0.4500 -0.0567 -0.0676 0.0452  465 HOH A O   
3608 O  O   . HOH D .   ? 0.2174 0.1822 0.2110 -0.0167 -0.0077 0.0054  466 HOH A O   
3609 O  O   . HOH D .   ? 0.1945 0.1642 0.1908 -0.0177 -0.0201 0.0197  467 HOH A O   
3610 O  O   . HOH D .   ? 0.3544 0.4953 0.3487 -0.0914 -0.0105 0.0468  468 HOH A O   
3611 O  O   . HOH D .   ? 0.4878 0.7416 0.4837 -0.0176 0.0200  -0.0109 469 HOH A O   
3612 O  O   . HOH D .   ? 0.2536 0.1811 0.2202 0.0072  -0.0172 -0.0001 470 HOH A O   
3613 O  O   . HOH D .   ? 0.1563 0.1330 0.1432 -0.0062 -0.0063 -0.0015 471 HOH A O   
3614 O  O   . HOH D .   ? 0.4116 0.6851 0.4462 -0.0171 0.0122  -0.0119 472 HOH A O   
3615 O  O   . HOH D .   ? 0.2643 0.2185 0.2333 -0.0251 0.0016  0.0184  473 HOH A O   
3616 O  O   . HOH D .   ? 0.3188 0.5642 0.4083 0.0620  -0.0165 -0.0506 474 HOH A O   
3617 O  O   . HOH D .   ? 0.5287 0.4773 0.4581 -0.0444 -0.0564 0.0493  475 HOH A O   
3618 O  O   . HOH D .   ? 0.2083 0.1962 0.2206 0.0012  -0.0368 0.0109  476 HOH A O   
3619 O  O   . HOH D .   ? 0.3087 0.2363 0.2750 0.0074  -0.0183 -0.0088 477 HOH A O   
3620 O  O   . HOH D .   ? 0.5905 0.7807 0.6659 0.0883  -0.0370 -0.0579 478 HOH A O   
3621 O  O   . HOH D .   ? 0.4102 0.3444 0.3817 -0.0267 -0.0194 0.0017  479 HOH A O   
3622 O  O   . HOH D .   ? 0.2430 0.1784 0.2303 -0.0007 -0.0383 0.0081  480 HOH A O   
3623 O  O   . HOH D .   ? 0.3642 0.4758 0.3339 -0.0900 -0.0113 0.0505  481 HOH A O   
3624 O  O   . HOH D .   ? 0.6227 0.5686 0.5538 -0.0955 -0.0699 0.0654  482 HOH A O   
3625 O  O   . HOH D .   ? 0.2304 0.1881 0.2222 -0.0019 -0.0041 0.0068  483 HOH A O   
3626 O  O   . HOH D .   ? 0.5322 0.8136 0.6058 -0.0222 0.0207  -0.0138 484 HOH A O   
3627 O  O   . HOH D .   ? 0.2422 0.3000 0.2006 -0.0040 0.0019  -0.0119 485 HOH A O   
3628 O  O   . HOH D .   ? 0.4528 0.5695 0.4969 0.0883  -0.0356 -0.0536 486 HOH A O   
3629 O  O   . HOH D .   ? 0.2688 0.3058 0.3078 0.0121  -0.0328 -0.0016 487 HOH A O   
3630 O  O   . HOH D .   ? 0.4802 0.5955 0.5516 0.0340  -0.0615 -0.0146 488 HOH A O   
3631 O  O   . HOH D .   ? 0.5283 0.7185 0.5650 -0.0593 0.0233  0.0122  489 HOH A O   
3632 O  O   . HOH D .   ? 0.4188 0.4756 0.4543 -0.0334 -0.0444 0.0017  490 HOH A O   
3633 O  O   . HOH D .   ? 0.3928 0.3728 0.3985 0.0011  -0.0171 0.0031  491 HOH A O   
3634 O  O   . HOH D .   ? 0.4685 0.4645 0.4016 -0.0678 -0.0339 0.0537  492 HOH A O   
3635 O  O   . HOH D .   ? 0.4039 0.5320 0.4629 -0.0755 -0.0166 0.0106  493 HOH A O   
3636 O  O   . HOH D .   ? 0.3185 0.3189 0.3334 -0.0072 -0.0179 0.0053  494 HOH A O   
3637 O  O   . HOH D .   ? 0.4590 0.3110 0.3883 -0.0253 -0.0992 0.0248  495 HOH A O   
3638 O  O   . HOH D .   ? 0.3388 0.5558 0.3534 0.0304  0.0097  -0.0384 496 HOH A O   
3639 O  O   . HOH D .   ? 0.4118 0.3903 0.3844 0.0457  -0.0199 -0.0341 497 HOH A O   
3640 O  O   . HOH D .   ? 0.4526 0.3478 0.4054 -0.0187 -0.0730 0.0274  498 HOH A O   
3641 O  O   . HOH D .   ? 0.1518 0.1111 0.1439 -0.0136 -0.0062 0.0054  499 HOH A O   
3642 O  O   . HOH D .   ? 0.3124 0.3070 0.2643 -0.0314 -0.0314 0.0231  500 HOH A O   
3643 O  O   . HOH D .   ? 0.2901 0.2402 0.2711 -0.0026 -0.0036 0.0084  501 HOH A O   
3644 O  O   . HOH D .   ? 0.5348 0.7204 0.5455 0.0608  -0.0024 -0.0553 502 HOH A O   
3645 O  O   . HOH D .   ? 0.3107 0.3620 0.3426 -0.0110 -0.0191 0.0030  503 HOH A O   
3646 O  O   . HOH D .   ? 0.4021 0.4676 0.4100 -0.0691 0.0078  0.0237  504 HOH A O   
3647 O  O   . HOH D .   ? 0.3872 0.4220 0.3722 -0.0987 -0.0425 0.0559  505 HOH A O   
3648 O  O   . HOH D .   ? 0.3791 0.4705 0.4106 0.0376  0.0008  -0.0245 506 HOH A O   
3649 O  O   . HOH D .   ? 0.3676 0.2988 0.3498 -0.0042 -0.0407 0.0027  507 HOH A O   
3650 O  O   . HOH D .   ? 0.4673 0.3908 0.4454 -0.0150 -0.0500 0.0108  508 HOH A O   
3651 O  O   . HOH D .   ? 0.5569 0.6725 0.6214 0.0744  -0.0538 -0.0377 509 HOH A O   
3652 O  O   . HOH D .   ? 0.4085 0.3815 0.3904 -0.0552 -0.0083 0.0200  510 HOH A O   
3653 O  O   . HOH D .   ? 0.1658 0.1394 0.1690 -0.0142 -0.0139 0.0144  511 HOH A O   
3654 O  O   . HOH D .   ? 0.3555 0.3129 0.3495 0.0037  -0.0164 0.0037  512 HOH A O   
3655 O  O   . HOH D .   ? 0.3979 0.5460 0.4607 0.0914  -0.0439 -0.0551 513 HOH A O   
3656 O  O   . HOH D .   ? 0.2463 0.2114 0.2446 0.0040  -0.0072 0.0030  514 HOH A O   
3657 O  O   . HOH D .   ? 0.5716 0.5737 0.5357 -0.0254 -0.0586 0.0120  515 HOH A O   
3658 O  O   . HOH D .   ? 0.4923 0.4226 0.4278 -0.0250 -0.0038 0.0247  516 HOH A O   
3659 O  O   . HOH D .   ? 0.3227 0.5217 0.3050 -0.0123 0.0192  -0.0108 517 HOH A O   
3660 O  O   . HOH D .   ? 0.1151 0.0899 0.1210 -0.0078 -0.0040 0.0080  518 HOH A O   
3661 O  O   . HOH D .   ? 0.2898 0.2893 0.3025 0.0391  -0.0216 -0.0170 519 HOH A O   
3662 O  O   . HOH D .   ? 0.4109 0.3067 0.3769 0.0197  -0.0735 -0.0002 520 HOH A O   
3663 O  O   . HOH D .   ? 0.3510 0.3956 0.2659 -0.0428 -0.0155 0.0258  521 HOH A O   
3664 O  O   . HOH D .   ? 0.3240 0.2380 0.2622 -0.0099 -0.0139 0.0169  522 HOH A O   
3665 O  O   . HOH D .   ? 0.5088 0.4595 0.4768 -0.0054 -0.0669 0.0279  523 HOH A O   
3666 O  O   . HOH D .   ? 0.2704 0.3620 0.2304 0.0048  0.0075  -0.0201 524 HOH A O   
3667 O  O   . HOH D .   ? 0.1714 0.1677 0.1562 -0.0044 -0.0041 -0.0038 525 HOH A O   
3668 O  O   . HOH D .   ? 0.3848 0.4356 0.4262 0.0624  -0.0571 -0.0240 526 HOH A O   
3669 O  O   . HOH D .   ? 0.6567 0.6629 0.5900 -0.1098 -0.0502 0.0714  527 HOH A O   
3670 O  O   . HOH D .   ? 0.2921 0.2486 0.2914 0.0259  -0.0288 -0.0074 528 HOH A O   
3671 O  O   . HOH D .   ? 0.1559 0.1130 0.1485 0.0005  -0.0073 0.0047  529 HOH A O   
3672 O  O   . HOH D .   ? 0.5013 0.5676 0.4569 -0.1076 -0.0313 0.0647  530 HOH A O   
3673 O  O   . HOH D .   ? 0.5611 0.5679 0.5714 0.0205  -0.0194 -0.0085 531 HOH A O   
3674 O  O   . HOH D .   ? 0.2607 0.2808 0.1797 -0.0490 -0.0250 0.0373  532 HOH A O   
3675 O  O   . HOH D .   ? 0.4638 0.3922 0.4294 -0.0113 -0.0198 -0.0071 533 HOH A O   
3676 O  O   . HOH D .   ? 0.3247 0.2677 0.3132 0.0105  -0.0266 -0.0026 534 HOH A O   
3677 O  O   . HOH D .   ? 0.5248 0.5705 0.4667 -0.0989 -0.0301 0.0633  535 HOH A O   
3678 O  O   . HOH D .   ? 0.3416 0.3204 0.3343 -0.0419 -0.0280 0.0013  536 HOH A O   
3679 O  O   . HOH D .   ? 0.4875 0.3973 0.4345 -0.0431 -0.0673 0.0400  537 HOH A O   
3680 O  O   . HOH D .   ? 0.4176 0.5750 0.5000 -0.0455 -0.0230 -0.0010 538 HOH A O   
3681 O  O   . HOH D .   ? 0.2095 0.1678 0.1913 -0.0262 -0.0014 0.0147  539 HOH A O   
3682 O  O   . HOH D .   ? 0.3534 0.3187 0.3410 -0.0153 -0.0097 0.0019  540 HOH A O   
3683 O  O   . HOH D .   ? 0.2918 0.2745 0.2675 -0.0235 -0.0219 0.0012  541 HOH A O   
3684 O  O   . HOH D .   ? 0.4553 0.4184 0.4460 0.0180  -0.0165 -0.0043 542 HOH A O   
3685 O  O   . HOH D .   ? 0.3597 0.3589 0.2984 -0.0280 -0.0380 0.0056  543 HOH A O   
3686 O  O   . HOH D .   ? 0.2628 0.2973 0.3003 0.0114  -0.0246 -0.0023 544 HOH A O   
3687 O  O   . HOH D .   ? 0.2507 0.2819 0.2751 0.0455  -0.0200 -0.0221 545 HOH A O   
3688 O  O   . HOH D .   ? 0.3037 0.2993 0.2938 -0.0287 0.0083  0.0158  546 HOH A O   
3689 O  O   . HOH D .   ? 0.4114 0.3443 0.3738 -0.0429 -0.0158 0.0167  547 HOH A O   
3690 O  O   . HOH D .   ? 0.5051 0.5841 0.5157 0.0496  -0.0099 -0.0366 548 HOH A O   
3691 O  O   . HOH D .   ? 0.3995 0.3324 0.3661 0.0229  -0.0216 -0.0141 549 HOH A O   
3692 O  O   . HOH D .   ? 0.4730 0.5057 0.4952 -0.0629 -0.0218 0.0096  550 HOH A O   
3693 O  O   . HOH D .   ? 0.5063 0.7038 0.5312 0.0574  -0.0045 -0.0522 551 HOH A O   
3694 O  O   . HOH D .   ? 0.2579 0.2372 0.2573 -0.0062 0.0010  0.0069  552 HOH A O   
3695 O  O   . HOH D .   ? 0.3147 0.2993 0.3089 0.0306  -0.0176 -0.0150 553 HOH A O   
3696 O  O   . HOH D .   ? 0.3265 0.2824 0.3199 0.0110  -0.0581 0.0146  554 HOH A O   
3697 O  O   . HOH D .   ? 0.5076 0.8110 0.5372 -0.0061 0.0144  -0.0218 555 HOH A O   
3698 O  O   . HOH D .   ? 0.5354 0.8504 0.5595 -0.0174 0.0164  -0.0158 556 HOH A O   
3699 O  O   . HOH D .   ? 0.6735 0.5664 0.5989 -0.0854 -0.0951 0.0581  557 HOH A O   
3700 O  O   . HOH D .   ? 0.5323 0.4540 0.5104 0.0231  -0.0727 0.0076  558 HOH A O   
3701 O  O   . HOH D .   ? 0.4490 0.3812 0.4287 0.0159  -0.0700 0.0140  559 HOH A O   
3702 O  O   . HOH D .   ? 0.2357 0.2048 0.2410 0.0104  -0.0475 0.0115  560 HOH A O   
3703 O  O   . HOH D .   ? 0.4649 0.4829 0.4719 0.0919  -0.0570 -0.0506 561 HOH A O   
3704 O  O   . HOH D .   ? 0.5054 0.7303 0.5842 -0.0907 -0.0054 0.0127  562 HOH A O   
3705 O  O   . HOH D .   ? 0.4448 0.3813 0.4173 0.0161  -0.0183 -0.0042 563 HOH A O   
3706 O  O   . HOH D .   ? 0.5890 0.6528 0.6278 -0.0494 -0.0359 0.0160  564 HOH A O   
3707 O  O   . HOH D .   ? 0.6514 0.5437 0.6075 -0.0228 -0.0729 0.0194  565 HOH A O   
3708 O  O   . HOH D .   ? 0.4003 0.4147 0.3843 -0.0658 0.0041  0.0273  566 HOH A O   
3709 O  O   . HOH D .   ? 0.5538 0.5013 0.5462 0.0446  -0.0519 -0.0169 567 HOH A O   
3710 O  O   . HOH D .   ? 0.5268 0.7391 0.5830 0.0273  0.0143  -0.0305 568 HOH A O   
3711 O  O   . HOH D .   ? 0.5003 0.4802 0.4980 -0.0447 -0.0199 0.0062  569 HOH A O   
3712 O  O   . HOH D .   ? 0.3180 0.3737 0.2685 0.0201  -0.0014 -0.0339 570 HOH A O   
3713 O  O   . HOH D .   ? 0.5429 0.6284 0.5995 0.0441  -0.0682 -0.0137 571 HOH A O   
3714 O  O   . HOH D .   ? 0.2809 0.3016 0.2235 -0.0158 -0.0124 -0.0050 572 HOH A O   
3715 O  O   . HOH D .   ? 0.5365 0.4880 0.4930 -0.0277 0.0026  0.0220  573 HOH A O   
3716 O  O   . HOH D .   ? 0.4070 0.5864 0.4654 0.0608  -0.0072 -0.0447 574 HOH A O   
3717 O  O   . HOH D .   ? 0.5155 0.5173 0.4600 -0.0220 -0.0234 -0.0009 575 HOH A O   
3718 O  O   . HOH D .   ? 0.3220 0.2434 0.2834 -0.0020 -0.0209 -0.0091 576 HOH A O   
3719 O  O   . HOH D .   ? 0.4822 0.4173 0.4360 0.0176  -0.0229 -0.0258 577 HOH A O   
3720 O  O   . HOH D .   ? 0.0637 0.0286 0.0648 -0.0106 -0.0203 0.0156  578 HOH A O   
3721 O  O   . HOH D .   ? 0.2980 0.3157 0.3146 -0.0391 -0.0309 0.0043  579 HOH A O   
3722 O  O   . HOH D .   ? 0.4078 0.3751 0.4008 -0.0333 -0.0141 0.0059  580 HOH A O   
3723 O  O   . HOH D .   ? 0.5270 0.4074 0.4799 0.0097  -0.0775 -0.0034 581 HOH A O   
3724 O  O   . HOH D .   ? 0.3828 0.3173 0.3234 -0.0669 -0.0615 0.0524  582 HOH A O   
3725 O  O   . HOH D .   ? 0.4544 0.4650 0.4034 0.0066  -0.0100 -0.0247 583 HOH A O   
3726 O  O   . HOH D .   ? 0.3885 0.4909 0.4035 -0.0790 0.0098  0.0251  584 HOH A O   
3727 O  O   . HOH D .   ? 0.5416 0.7070 0.5278 -0.1047 -0.0109 0.0529  585 HOH A O   
3728 O  O   . HOH D .   ? 0.2889 0.2589 0.2973 0.0381  -0.0516 -0.0070 586 HOH A O   
3729 O  O   . HOH D .   ? 0.5688 0.4596 0.5268 -0.0132 -0.0720 0.0121  587 HOH A O   
3730 O  O   . HOH D .   ? 0.5527 0.6406 0.5948 -0.0801 -0.0212 0.0127  588 HOH A O   
3731 O  O   . HOH D .   ? 0.4601 0.4513 0.4643 -0.0426 -0.0078 0.0119  589 HOH A O   
3732 O  O   . HOH D .   ? 0.4208 0.3632 0.3966 -0.0360 -0.0184 0.0064  590 HOH A O   
3733 O  O   . HOH D .   ? 0.5102 0.6395 0.5072 0.0526  0.0001  -0.0481 591 HOH A O   
3734 O  O   . HOH D .   ? 0.5205 0.5684 0.4525 -0.0217 -0.0073 0.0012  592 HOH A O   
3735 O  O   . HOH D .   ? 0.4662 0.6099 0.5500 0.0353  -0.0495 -0.0207 593 HOH A O   
3736 O  O   . HOH D .   ? 0.5121 0.6221 0.4548 -0.0574 0.0035  0.0307  594 HOH A O   
3737 O  O   . HOH D .   ? 0.4880 0.6508 0.5166 -0.0562 0.0234  0.0137  595 HOH A O   
3738 O  O   . HOH D .   ? 0.4961 0.4523 0.4825 -0.0248 -0.0135 0.0031  596 HOH A O   
3739 O  O   . HOH D .   ? 0.6839 0.5582 0.6304 -0.0194 -0.0846 0.0161  597 HOH A O   
3740 O  O   . HOH D .   ? 0.3542 0.3100 0.3306 -0.0351 -0.0040 0.0172  598 HOH A O   
3741 O  O   . HOH D .   ? 0.4922 0.4756 0.4769 -0.0410 -0.0379 -0.0028 599 HOH A O   
3742 O  O   . HOH D .   ? 0.6631 0.5466 0.6157 -0.0187 -0.0785 0.0146  600 HOH A O   
3743 O  O   . HOH D .   ? 0.4073 0.4178 0.4278 -0.0377 -0.0295 0.0177  601 HOH A O   
3744 O  O   . HOH D .   ? 0.4078 0.4917 0.3459 -0.0370 0.0022  0.0162  602 HOH A O   
3745 O  O   . HOH D .   ? 0.5776 0.5214 0.5474 0.0346  -0.0246 -0.0187 603 HOH A O   
3746 O  O   . HOH D .   ? 0.3963 0.6275 0.3816 -0.0289 0.0199  -0.0015 604 HOH A O   
3747 O  O   . HOH D .   ? 0.5625 0.5853 0.4996 -0.1047 -0.0410 0.0680  605 HOH A O   
3748 O  O   . HOH D .   ? 0.5619 0.4483 0.5212 0.0314  -0.0811 -0.0102 606 HOH A O   
3749 O  O   . HOH D .   ? 0.5578 0.4926 0.5434 -0.0122 -0.0428 0.0068  607 HOH A O   
3750 O  O   . HOH D .   ? 0.5053 0.4634 0.4689 -0.0082 -0.0684 0.0291  608 HOH A O   
3751 O  O   . HOH D .   ? 0.3847 0.3289 0.3729 0.0203  -0.0284 -0.0078 609 HOH A O   
3752 O  O   . HOH D .   ? 0.4640 0.4403 0.4589 -0.0445 -0.0118 0.0113  610 HOH A O   
3753 O  O   . HOH D .   ? 0.4131 0.5980 0.5093 0.0312  -0.0352 -0.0258 611 HOH A O   
3754 O  O   . HOH D .   ? 0.4751 0.4760 0.4921 -0.0203 -0.0232 0.0108  612 HOH A O   
3755 O  O   . HOH D .   ? 0.5317 0.5097 0.5415 0.0233  -0.0561 0.0053  613 HOH A O   
3756 O  O   . HOH D .   ? 0.3708 0.3766 0.3868 0.0608  -0.0417 -0.0277 614 HOH A O   
3757 O  O   . HOH D .   ? 0.4453 0.4785 0.4341 0.0000  0.0000  0.0391  615 HOH A O   
3758 O  O   . HOH D .   ? 0.6785 0.7254 0.6872 0.1047  -0.0545 -0.0622 616 HOH A O   
3759 O  O   . HOH D .   ? 0.5910 0.5902 0.5971 0.0830  -0.0606 -0.0418 617 HOH A O   
3760 O  O   . HOH D .   ? 0.4856 0.6199 0.5060 0.0000  0.0000  0.0438  618 HOH A O   
3761 O  O   . HOH D .   ? 0.6293 0.5659 0.5677 -0.0494 -0.0571 0.0490  619 HOH A O   
3762 O  O   . HOH D .   ? 0.5851 0.4831 0.5524 0.0318  -0.0803 -0.0037 620 HOH A O   
3763 O  O   . HOH D .   ? 0.3645 0.3585 0.3639 -0.0440 -0.0327 0.0013  621 HOH A O   
3764 O  O   . HOH D .   ? 0.5664 0.4937 0.5132 -0.0410 -0.0593 0.0432  622 HOH A O   
3765 O  O   . HOH D .   ? 0.6475 0.5447 0.5918 -0.0309 -0.0739 0.0366  623 HOH A O   
3766 O  O   . HOH D .   ? 0.2900 0.2624 0.2592 0.0078  -0.0117 -0.0174 624 HOH A O   
3767 O  O   . HOH D .   ? 0.3552 0.3251 0.3605 0.0475  -0.0488 -0.0163 625 HOH A O   
3768 O  O   . HOH D .   ? 0.4322 0.5855 0.5065 -0.0681 -0.0209 0.0055  626 HOH A O   
3769 O  O   . HOH D .   ? 0.4321 0.3829 0.4241 0.0272  -0.0286 -0.0106 627 HOH A O   
3770 O  O   . HOH D .   ? 0.4690 0.3548 0.4025 -0.0479 -0.0824 0.0423  628 HOH A O   
3771 O  O   . HOH D .   ? 0.3009 0.2655 0.2954 -0.0019 -0.0026 0.0062  629 HOH A O   
3772 O  O   . HOH D .   ? 0.5355 0.5862 0.5580 0.0730  -0.0316 -0.0406 630 HOH A O   
3773 O  O   . HOH D .   ? 0.5721 0.5461 0.5145 -0.0594 -0.0399 0.0501  631 HOH A O   
3774 O  O   . HOH D .   ? 0.5074 0.6342 0.4693 -0.1081 -0.0162 0.0598  632 HOH A O   
3775 O  O   . HOH D .   ? 0.5036 0.4293 0.4822 0.0030  -0.0424 -0.0008 633 HOH A O   
3776 O  O   . HOH D .   ? 0.4921 0.4128 0.4671 0.0139  -0.0461 -0.0066 634 HOH A O   
3777 O  O   . HOH D .   ? 0.4586 0.4629 0.4715 0.0193  -0.0666 0.0072  635 HOH A O   
3778 O  O   . HOH D .   ? 0.6019 0.7112 0.6559 -0.0835 -0.0282 0.0097  636 HOH A O   
3779 O  O   . HOH D .   ? 0.2555 0.2237 0.2336 -0.0322 0.0032  0.0189  637 HOH A O   
3780 O  O   . HOH D .   ? 0.5580 0.5022 0.5508 0.0231  -0.0599 0.0056  638 HOH A O   
3781 O  O   . HOH D .   ? 0.4354 0.6079 0.4404 0.0491  0.0034  -0.0480 639 HOH A O   
3782 O  O   . HOH D .   ? 0.2330 0.1940 0.2095 -0.0016 -0.0111 -0.0084 640 HOH A O   
3783 O  O   . HOH D .   ? 0.4811 0.5827 0.4273 -0.0453 0.0052  0.0221  641 HOH A O   
3784 O  O   . HOH D .   ? 0.4003 0.3448 0.3951 0.0225  -0.0545 0.0037  642 HOH A O   
3785 O  O   . HOH D .   ? 0.5134 0.5352 0.5046 -0.0311 0.0140  0.0158  643 HOH A O   
3786 O  O   . HOH D .   ? 0.2845 0.3467 0.3109 0.0489  -0.0104 -0.0278 644 HOH A O   
3787 O  O   . HOH D .   ? 0.4816 0.6187 0.5002 -0.0890 -0.0169 0.0414  645 HOH A O   
3788 O  O   . HOH D .   ? 0.2998 0.2095 0.2519 0.0030  -0.0267 -0.0124 646 HOH A O   
3789 O  O   . HOH D .   ? 0.4160 0.3688 0.3923 -0.0100 -0.0132 -0.0051 647 HOH A O   
3790 O  O   . HOH D .   ? 0.5098 0.7194 0.5822 0.0953  -0.0324 -0.0656 648 HOH A O   
3791 O  O   . HOH D .   ? 0.4747 0.5436 0.4875 0.0534  -0.0152 -0.0360 649 HOH A O   
3792 O  O   . HOH D .   ? 0.4638 0.4273 0.4492 -0.0447 -0.0268 0.0020  650 HOH A O   
3793 O  O   . HOH D .   ? 0.4616 0.5343 0.4844 0.0677  -0.0168 -0.0404 651 HOH A O   
3794 O  O   . HOH D .   ? 0.5304 0.7502 0.5183 0.0029  0.0191  -0.0229 652 HOH A O   
3795 O  O   . HOH D .   ? 0.5703 0.7777 0.5494 0.0246  0.0163  -0.0385 653 HOH A O   
3796 O  O   . HOH D .   ? 0.5045 0.4566 0.4950 0.0019  -0.0192 0.0024  654 HOH A O   
3797 O  O   . HOH D .   ? 0.6016 0.6026 0.5806 0.0582  -0.0220 -0.0405 655 HOH A O   
3798 O  O   . HOH D .   ? 0.5114 0.7159 0.5584 0.0660  0.0015  -0.0515 656 HOH A O   
3799 O  O   . HOH D .   ? 0.6239 0.6423 0.6290 0.0836  -0.0460 -0.0471 657 HOH A O   
3800 O  O   . HOH D .   ? 0.5450 0.4521 0.4758 -0.0685 -0.0768 0.0530  658 HOH A O   
3801 O  O   . HOH D .   ? 0.4612 0.4262 0.4613 -0.0006 -0.0216 0.0039  659 HOH A O   
3802 O  O   . HOH D .   ? 0.4986 0.6885 0.4685 -0.0053 0.0193  -0.0164 660 HOH A O   
3803 O  O   . HOH D .   ? 0.6177 0.4854 0.5538 -0.0227 -0.0898 0.0292  661 HOH A O   
3804 O  O   . HOH D .   ? 0.4964 0.5195 0.5160 0.0601  -0.0313 -0.0297 662 HOH A O   
3805 O  O   . HOH D .   ? 0.4993 0.5360 0.4957 0.0584  -0.0177 -0.0395 663 HOH A O   
3806 O  O   . HOH D .   ? 0.3711 0.4097 0.3979 -0.0413 -0.0368 0.0029  664 HOH A O   
3807 O  O   . HOH D .   ? 0.3667 0.3324 0.3413 -0.0178 0.0045  0.0148  665 HOH A O   
3808 O  O   . HOH D .   ? 0.5347 0.4889 0.5333 0.0436  -0.0567 -0.0118 666 HOH A O   
3809 O  O   . HOH D .   ? 0.4091 0.5155 0.4154 -0.1002 -0.0265 0.0504  667 HOH A O   
3810 O  O   . HOH D .   ? 0.5278 0.4895 0.5208 0.0319  -0.0220 -0.0140 668 HOH A O   
3811 O  O   . HOH D .   ? 0.6227 0.5489 0.6054 0.0354  -0.0733 -0.0016 669 HOH A O   
3812 O  O   . HOH D .   ? 0.5548 0.6664 0.6186 -0.0587 -0.0464 -0.0025 670 HOH A O   
3813 O  O   . HOH D .   ? 0.5162 0.5699 0.5363 0.0395  -0.0194 -0.0234 671 HOH A O   
3814 O  O   . HOH D .   ? 0.5432 0.5426 0.5488 0.0533  -0.0247 -0.0269 672 HOH A O   
3815 O  O   . HOH D .   ? 0.4472 0.4294 0.4601 0.0437  -0.0581 -0.0084 673 HOH A O   
3816 O  O   . HOH D .   ? 0.5462 0.4948 0.4999 0.0147  -0.0206 -0.0269 674 HOH A O   
3817 O  O   . HOH D .   ? 0.4705 0.4304 0.4710 -0.0074 -0.0268 0.0058  675 HOH A O   
3818 O  O   . HOH D .   ? 0.4150 0.4416 0.4277 0.0458  -0.0131 -0.0245 676 HOH A O   
3819 O  O   . HOH D .   ? 0.2851 0.2154 0.2526 0.0170  -0.0203 -0.0080 677 HOH A O   
3820 O  O   . HOH D .   ? 0.5845 0.5934 0.5158 -0.0216 -0.0248 -0.0032 678 HOH A O   
3821 O  O   . HOH D .   ? 0.5419 0.5433 0.5568 0.0764  -0.0680 -0.0315 679 HOH A O   
3822 O  O   . HOH D .   ? 0.6026 0.5328 0.5684 0.0206  -0.0231 -0.0054 680 HOH A O   
3823 O  O   . HOH D .   ? 0.6036 0.7581 0.6492 0.1043  -0.0360 -0.0680 681 HOH A O   
3824 O  O   . HOH D .   ? 0.5550 0.5047 0.5117 -0.0025 -0.0788 0.0298  682 HOH A O   
3825 O  O   . HOH D .   ? 0.5429 0.4948 0.5384 0.0269  -0.0635 0.0049  683 HOH A O   
3826 O  O   . HOH D .   ? 0.6885 0.5453 0.6073 -0.0476 -0.0993 0.0421  684 HOH A O   
3827 O  O   . HOH D .   ? 0.5558 0.6131 0.5541 -0.1010 -0.0401 0.0527  685 HOH A O   
3828 O  O   . HOH D .   ? 0.4884 0.4725 0.4784 -0.0149 0.0059  0.0109  686 HOH A O   
3829 O  O   . HOH D .   ? 0.4160 0.3479 0.3810 0.0283  -0.0258 -0.0127 687 HOH A O   
3830 O  O   . HOH D .   ? 0.5747 0.5840 0.5980 0.0597  -0.0607 -0.0197 688 HOH A O   
3831 O  O   . HOH D .   ? 0.5838 0.5557 0.5818 0.0763  -0.0684 -0.0349 689 HOH A O   
3832 O  O   . HOH D .   ? 0.5627 0.5145 0.5221 0.0016  -0.0186 -0.0189 690 HOH A O   
3833 O  O   . HOH D .   ? 0.5789 0.5133 0.5114 -0.0604 -0.0599 0.0539  691 HOH A O   
3834 O  O   . HOH D .   ? 0.5256 0.4480 0.4454 -0.0211 -0.0059 0.0263  692 HOH A O   
3835 O  O   . HOH D .   ? 0.6628 0.5121 0.5840 -0.0326 -0.1016 0.0347  693 HOH A O   
3836 O  O   . HOH D .   ? 0.5434 0.7303 0.5117 0.0215  0.0161  -0.0364 694 HOH A O   
3837 O  O   . HOH D .   ? 0.6650 0.5500 0.6218 0.0476  -0.0892 -0.0195 695 HOH A O   
3838 O  O   . HOH D .   ? 0.4407 0.4724 0.4606 -0.0483 -0.0399 0.0009  696 HOH A O   
3839 O  O   . HOH D .   ? 0.7453 0.7270 0.7427 0.0377  -0.0871 0.0055  697 HOH A O   
3840 O  O   . HOH D .   ? 0.7420 0.7512 0.7570 0.0523  -0.0883 -0.0052 698 HOH A O   
3841 O  O   . HOH D .   ? 0.4244 0.4310 0.4309 -0.0527 -0.0362 0.0012  699 HOH A O   
3842 O  O   . HOH D .   ? 0.5843 0.5218 0.5140 -0.0701 -0.0609 0.0577  700 HOH A O   
# 
